Datasets:

habdine

/

Prot2Text-Data

like 2

Q5LC87

NHAA_BACFN

Sodium/proton antiporter NhaA

Bacteroides

MTVLRSMKDFSSMNITASILLFVTAIAAAVIANSPAASVYQEFLSHELHFRIGGFNLLSHAGHNLTMIEFINDGLMTIFFLMVGLEIKRELLVGELSSFRKAALPFIAACGGMVVPVVIYSMVCAPGTEGGQGLAIPMATDIAFSLGVLSLLGKRVPLSLKIFLTAFAVVDDIGGILVIAIFYSSHVAYEYLLWAALLYVLLYFIGKKGATNKIFFLVVGVVIWYLFLQSGIHSTISGVILAFVIPAKPQLNVGTYIERIRRIISTFPEMGANNIVLTNQQIAKLKEVESASDRVISPLQSLEDNLHGAVNYLVLPLFAFVNAGVMFSGEGEVIGGVTLAVALGLLAGKFLGIYSFTWLAVKSGLTPMPLGMNWKNISGVALLGGIGFTVSLFIANLSFGSAHPVLLNQAKLGVLSGTVMAGILGYLVLHWVLPKRR

Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.

Q5LC87

A1UJ38

TIG_MYCSK

PPIase

unclassified Mycobacterium

MKSTVEKLSPTRVRINVEVPFTELEPDFDRAFKELAKQVRLPGFRPGKAPRKLLEARVGREAMLDQVVGEAVPGRYTEAVTSSDVQPLGQPEIEITKKEYGEDLVFTAEVDVRPEITLPDLSALEITVDPIEITDEEVDTELQSLRARFGTLTGVDRPAKDGDFVSIDLSATVDGKDVPEATTEGLSHEVGSGQLIEGLDDAIVGLSEGESKEFTTTLAAGEHAGKEAIVTVTVKSIKERELPEPDDEFAQLASEFDTIDELKESLTEQVRRVKRVQQAEQIRDKALELLLEQTEVPLPEKIVQAQIDDTVHNAIHGLDHDEDRFAEQLAEQGSSREEFDANTRTEAEKAVKTQLLMDALADQLEVQVGQGDLTERLVLMSRQYGLEPQQLLQILQQNNQLPAMFADVRRGLTIAAVVHGATVKDTDGNDIDTTEFFGPSGGAQAEAEGADEADADSDADSDTEADSDTEADEADEAK

Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.

A1UJ38

B2IA21

UBIE_XYLF2

Demethylmenaquinone methyltransferase

Xylella

MSESSEKTSTTHFGFRQVAAKDKKTLVAEVFTSVSRRYDLMNDLMSLGIHRAWKRYFVATAQVKSGDRVLDLAGGTGDIAMLLKNRVGAEGSIVLGDINASMLSVGRDRLIDRGVVARLDYVQCNAEALPFQDKCFDLVTMSFGLRNVTDKDAALREMFRVLKVGGQARVLEFSAVTAEWFKPIYDFHSFQVLPRLGRLFARDAASYRYLAESIRKHPPQEELQAMMGSAGFERCGYRNLTGGIVAIHSGYKY

Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).

B2IA21

A4Y5X9

FABA_SHEPC

Trans-2-decenoyl-[acyl-carrier-protein] isomerase

Shewanella

MNKANSFNKEELIACGHGKLFGPNSPRLPVDNMLMIDRIVTINDNGGEFGKGEIVAELDINPELWFFDCHFISDPVMPGCLGLDAMWQLVGFYLGWEGAEGKGRALGVGEVKFTGQVLPGAKKVTYKLNIKRTIHRKLVMGIADAILEVDGRQIYSATDLKVGVFSDTSTF

Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length.

A4Y5X9

A1QZS8

RS8_BORT9

30S ribosomal protein S8

Borrelia

MAVTHSVGDMLTKIRNASRVKHESVDLKMSKINKSILDILKEEGYIKNYNIFDKKGISFIKAILNYDNKRNPAINRIDAISTPGRKVYSSYKNMPRIKNGYGILIVSSSKGVITGKQAKDNKVGGELICSVW

One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.

A1QZS8

Q32DS5

MENH_SHIDS

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase

Shigella

MILHAQTKHGKPGLPWLVFLHGFSGDCHEWQEVGEVFADYSRLYVDLPGHGGSAAISVDGFDDVTDLLRKTLVSYNILDFWLVGYSLGGRVAMMAACQGLAGLCGVIVEGGHPGLQNAEQRAERQRSDRQWAQRFRTEPLTAVFADWYQQPVFASLNDDQRRELVALRSNNNGATLAAMLEATSLAVQPDLRANLSARTFAFYYLCGERDSKFRALAAELAADCHVIPRAGHNAHRENPAGVIASLAQILRF

Catalyzes a proton abstraction reaction that results in 2,5-elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC).

Q32DS5

A3CZA5

MOAC_SHEB5

Molybdenum cofactor biosynthesis protein C

Shewanella

MSNVFTHINADGNAHMVDVTEKAVTEREARAEAFIEMASTTLEMIMSGSHHKGDVFATARIAGIQAAKKTSDLIPLCHPLMLTKVEVDLEAQPEHNRVRITSLCKLSGKTGVEMEALTAASVAALTIYDMCKAVQKDMVISQVRLLEKRGGKSGHFKV

Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).

A3CZA5

Q8TQS4

THII_METAC

tRNA 4-thiouridine synthase

Methanosarcina

MPDIFTDNTDKQDSDPSRQGFEGQPNVVIVRYGELALKSTGVRNWYEKILMKNIAAMLDSRNIPYSLLRREWGRIFIETTDPRAAEAAADVFGVVSTSPALVTKPDLESAARTCAFLGTGLIREGESFAIRARRSGNHPFSSADVGRNCGDAVWDSLEKEGKHPRVNLTSPDKEIFVEMRQNLAYVYLETVKGVGGLPLGTQGSMVVLMSGGLDSPVAAWLMMKRGVMITPVYCNNSPYAEDAARERAFDCIRQLQTWAPGHQFATYEIPHGPNLRAFIGTCDRKNTCLLCKRMMYREAYEVMKKVGASGIITGSSLGQVASQTAANMHAEIYQLAIPIYHPLIAFDKSEIVDIARRIGTYDISTRPAGICTAVPERPEVKANYDLIVLEEKKLGIETMVGDALKAVKILKL

Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.

Q8TQS4

P14159

HXD4_SHEEP

Homeobox protein Hox-8.1

Ovis

VNSNYTGGEPKRSRTAYTRQQVLELEKEFLFNRYLTRRRRIQHTLT

Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.

P14159

A5GQ34

IF3_SYNR3

Translation initiation factor IF-3

unclassified Synechococcus

MAPRPRFDRRAPVRELPNINDRINYPKLRVVDADGTQLGVISRDEALDVARERELDLVLVSEKADPPVCRIMDYGKFKFEQEKKAKEAKKKSHQTEVKEVKMRYKIDAHDYQVRIGQAVRFLKAGDKVKCTVIFRGREIQHTALAEKLLMRMAKDLEESAEVQQPPKREGRNMIMFLGPRKTPLQKDKPEQATKAERTLPIAKPPGKTAAPAAAN

IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins.

A5GQ34

D3ZTL1

PO4F3_RAT

POU domain, class 4, transcription factor 3

Rattus

MMAMNAKQPFGMHPVLQEPKFSSLHSGSEAMRRVCLPAPQLQGNIFGSFDESLLARAEALAAVDIVSHGKNHPFKPDATYHTMSSVPCTSTSPTVPISHPAALTSHPHHPVHQGLEGDLLEHISPTLSVSGLGAPEHSVMPAQIHPHHLGAMGHLHQAMGMSHPHAVAPHSAMPACLSDVESDPRELEAFAERFKQRRIKLGVTQADVGAALANLKIPGVGSLSQSTICRFESLTLSHNNMIALKPVLQAWLEEAEAAYREKNSKPELFNGSERKRKRTSIAAPEKRSLEAYFAIQPRPSSEKIAAIAEKLDLKKNVVRVWFCNQRQKQKRMKYSAVH

Acts as a transcriptional activator. Acts by binding to sequences related to the consensus octamer motif 5'-ATGCAAAT-3' in the regulatory regions of its target genes. Involved in the auditory system development, required for terminal differentiation of hair cells in the inner ear.

D3ZTL1

O42099

MK08B_CYPCA

c-Jun N-terminal kinase B

Cyprinus

MNKNKREKEFYSVDVGDSTFTVLKRYQNLRPIGSGAQGIVCSAYDHNLERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIQMELDHERLSYLLYQMLCGTKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAATGLLMTPYVVTRYYRAPEVILGMGYQANVDVWSVGCIMAEMVRGSVLFPGSDHIDQWNKVIEQLGTPSQEFMMKLNQSVRTYVENRPRYTGYSFEKLFPDVLFPADSEHNKLKASQARDLLSKMLVIDASKRISVDEALQHPYINVWYDPAEVEAPPPLIIDKQLDEREHTVEEWKELIFKEVLDWEERMKNGVIRGQPSPIGAAVINGSPQPSSSSSINDVSSMSTEPTVASDTDSSLEASAGPLSCCR

Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating a number of transcription factors, primarily components of AP-1 such as c-Jun and ATF2 and thus regulates AP-1 transcriptional activity. May play a role in the regulation of the circadian clock.

O42099

Q2GXT0

YTM1_CHAGB

Ribosome biogenesis protein YTM1

Chaetomium

MDEPMVDASGAQVKVTFTTTEADLQLPESKRQLLVPADIRRYGLSRVLNSESMLDTGSIPFDFLVNGSFLRTSLEDYLTNNGLSLESNLTLQYVRSLIPPVYEASFEHDDWVSAVDVLSASSPSGRWSGDNFQRGQDRILSASFDGLLRIWNASGQVIATSPSGSHGGHTASIKAAKFLTNSQLASAGMDRTVRVWKYTESDHFSGDLKPTLELYGHTGSIDSLEVDGASKRILTASADGSIGFWSTSKASAPEADSSLLPNAHTSKRRKVTTSVTAAQRGPLSLMPIHSAPASAAVFDPRDRTVAYSASQDHTLRTIDLTTSTVVTTHSTSHPLLSLCALPRGNSASPLLAAGTAARHITLVDPRASAATTSVMTLRGHANKPVGLCASPRNEYALVSGAHDGTCRVWDLRSVRPATQEEGGLGSVSEAVYVIEREGAKGGKKTVAGEGCKVFGVVWDAELGIVSGAEDKRVQINAGRDVVAE

Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome.

Q2GXT0

B0YDW9

FAEB1_ASPFC

Ferulic acid esterase B-1

Aspergillus subgen. Fumigati

MMWWFLLIGLASAAATASSASSASFESRCQHFHKEIHLQNVHVLSTTYVPIGSNIPMVYNPPICGGTASSSISTIQFCQVALNVTTSDKSQFFMEAWLPSNYTGRFLSTGNGGLNGCVSYADMVYATQYGFATIGTNNGHFGDTGQYFLNNPEVIEDFAYRALHTGTVVGKALTKLFYPQGYKNSYYLGCSTGGRQGWKSIQRFPDDFDGVVAGAPAINFVNLCSWGSRFLKITGPPGSETFVTSAQWSAVHNEILRQCDALDGAVDGIIEDTDLCQPVFETLLCNSTAVDKTSCLTGVQANTVNEVFSAMYGLDGKWLYPRMQPGSELAASFIYYSGNGFKYSDDWYKYVVYNDSNWDHSTWTLADAAAAAAQDPFQISSFDGNISGFQKAGGKVLHYHGLEDAIITSDSSKAYYKHVADTMGLSPSELDHFYRLFPISGMGHCSPGTGAASIGQGSSTYAGDDPQDNVLMAIVQWVEKGIAPEYVRGSKMSRDGTIDYRRKHCKYPKRNRYVGPGKYTDENAWKCV

Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans as well as the feruloyl-galactose and feruloyl-arabinose ester bonds in pectin.

B0YDW9

A8GPE4

RS3_RICAH

30S ribosomal protein S3

spotted fever group

MGQKVCAHGFRVGPTLIKGWDSVLYAEKHYKTLFIQDLKIRDLINKGFNQAQVSRVLIERPSNKSIIISINAKKPNIIIGRNGSEIDKLKKAIEKMTFLKEVYINIHEVRKFNIDAAIVAQTIALQLEKRVSFRKAMKTAIQASLKQGGQGIRVSCSGRLGGAEIARTEWYIEGRMPLHTLRADIDYSTAEAITTYGVIGVKVWIYKGEYTENKRYN

Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.

A8GPE4

Q9SV68

QORH_ARATH

Chloroplast envelope quinone oxidoreductase homolog

Arabidopsis

MAGKLMHALQYNSYGGGAAGLEHVQVPVPTPKSNEVCLKLEATSLNPVDWKIQKGMIRPFLPRKFPCIPATDVAGEVVEVGSGVKNFKAGDKVVAVLSHLGGGGLAEFAVATEKLTVKRPQEVGAAEAAALPVAGLTALQALTNPAGLKLDGTGKKANILVTAASGGVGHYAVQLAKLANAHVTATCGARNIEFVKSLGADEVLDYKTPEGAALKSPSGKKYDAVVHCANGIPFSVFEPNLSENGKVIDITPGPNAMWTYAVKKITMSKKQLVPLLLIPKAENLEFMVNLVKEGKVKTVIDSKHPLSKAEDAWAKSIDGHATGKIIVEP

NADPH-dependent alpha,beta-unsaturated oxoene reductase reducing the double bond of medium-chain (C9) to long-chain (C18) reactive electrophile species deriving from poly-unsaturated fatty acid peroxides. The best substrates are 13-lipoxygenase-derived gamma-ketols, but is unable to reduce the double bond of short-chain alkenals and alkenones such as acrolein, crotonaldehyde, 3-buten-2-one, 4-hexen-3-one and trans-2-hexenal, or quinones such as duroquinone, decylubiquinone, coenzyme Q0, menadione, menaquinone and phylloquinone. Can use trans-2-nonenal, trans-3-decen-2-one, 4-hydroxynonenal, 12-oxo-10(E) dodecanoate (traumatin), 4-oxononenal, trans-1,3 diphenyl-2-propenone, trans-1,4-diphenyl-2-butene-1,4-dione, 9-oxo-12,13-epoxy-(10E)-octadecenoic acid (trans-EKODE-1b), 9-hydroxy-12-oxo-10(E)-octadecenoic acid, 9-Hydroxy-12-oxo-10(E),15(Z)-octadecadienoic acid and 9,13-dihydroxy-10-oxo-11-octadecenoic acid as substrates, but has no activity with 13(R,S)-hydroperoxy-9(Z),11(E)-octadecadienoic acid (13-HPOD), 9(S),12(S),13(S)-trihydroxy-10(E)-octadecenoic acid, 13-hydroxy-12-oxo-9(Z)-octadecenoic acid, 9-oxo-10(E),12(Z)-octadecadienoic acid (9-KODE), 13-oxo-9(Z),11(E)-octadecadienoic acid (13-KODE) and 12-oxo-10,15(Z)-phytodienoic acid (12-OPDA).

Q9SV68

C0HL10

B1OKC_NIDOK

Brevinin-1OKc

Nidirana

FFGSIIGALAKGLPSLISLIKK

Antimicrobial peptide. Active against Gram-negative bacterium E.coli (MIC=6 uM) and against Gram-positive bacterium S.aureus (MIC=12.5 uM).

C0HL10

O54423

UREF_ACTPL

Urease accessory protein UreF

Actinobacillus

MGQLGALLHLVDPTLPIGGFNHSNGLETFVQQGKVNSRASLEEYVQTQLMQNWIYNDGAYLSLAFDAMANHDLDRLLALDQELAASKIARESREGSYKLGVRLLKIFIRYENHPLLSEFQQAVSEKRCQGYFPIVFAMVAQAMNLDKAETLYAFYYNAAVGVVTNGVKLVPLSQMDGQDILFALRTPLAQAVENSLNPDLDWLGAATLASDIRSMQHEQLYTRLYMS

Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.

O54423

Q0VDE8

ADIG_HUMAN

Adipogenin

Homo

MKYPLMPLVNDLTFSFLVFWFCLPVGLLLLLIIWLRFLLSQDSEENDSSVCLDWEPWSKGPAEFCWKGTLHGQEKERPCW

Plays a role in stimulating adipocyte differentiation and development.

Q0VDE8

Q8R7X9

RS13_CALS4

30S ribosomal protein S13

Caldanaerobacter

MARIAGVDLPRDKRVEIALTYIYGIGRSRSKEILAKAGVNPDTRVRDLTEDEVSKLREIIEKEYKVEGDLRKEVAMNIKRLIDIGCYRGIRHKLGLPVRGQRTRTNARTRKGPRKTVAKKKK

Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.

Q8R7X9

Q6B8K4

PSBE_GRATL

PSII reaction center subunit V

Agarophyton tenuistipitatum

MSGGSTGERPFSDIITSIRYWVIHSITIPSLFVAGWLFVSTGLAYDVFGTPRPNEYFTQDRQQVPLVNDRFSAKQELEDLTKGI

This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.

Q6B8K4

Q5R1W2

ADH1B_PANTR

Alcohol dehydrogenase subunit beta

Pan

MSTAGKVIKCKAAVLWEVKKPFSIEDVEVAPPKAYEVRIKMVAVGICRTDDHVVSGNLVTPLPAILGHEAAGIVESVGEGVTTVKPGDKVIPLFTPQCGKCRVCKNPESNYCLKNDLGNPRGTLQDGTRRFTCRGKPIHHFLGTSTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTGYGSAVNVAKVTPGSTCAVFGLGGVGLSAVMGCKAAGAARIIAVDINKDKFAKAKELGATECINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPASQNLSINPMLLLTGRTWKGAVYGGFKSKEGIPKLVADFMAKKFSLDALITHVLPFEKINEGFDLLHSGKSIRTVLTF

Catalyzes the NAD-dependent oxidation of all-trans-retinol and its derivatives such as all-trans-4-hydroxyretinol and may participate in retinoid metabolism. In vitro can also catalyzes the NADH-dependent reduction of all-trans-retinal and its derivatives such as all-trans-4-oxoretinal. Catalyzes in the oxidative direction with higher efficiency. Has the same affinity for all-trans-4-hydroxyretinol and all-trans-4-oxoretinal.

Q5R1W2

P38812

GEP4_YEAST

PGP phosphatase GEP4

Saccharomyces

MNISGTLNTLRLLYNPSLCKPSLVVPTFNDLPIPIHDSIKAVVLDKDNCIAFPHDDKIWPDYLQHWETLRSKYSNKALLIVSNTAGSNSDKDYSQAKLLEDKTGIPVLRHSTKKPGCHNEILDYFYRNKTITNPKEVAVVGDRLFTDILMANLMGSYGVWIRDGVKVSANPLSKFEKKLYNFLGF

Phosphatidylglycerophosphatase involved in the biosynthesis of cardiolipin (CL), a unique dimeric phosphoglycerolipid predominantly present in mitochondrial membranes and which has important functions for cellular energy metabolism, mitochondrial dynamics and the initiation of apoptotic pathways. Required for the stability of respiratory chain supercomplexes and for growth at elevated temperature, in presence of ethidium bromide or in absence of prohibitins.

P38812

Q9Y5I4

PCDC2_HUMAN

Protocadherin alpha-C2

Homo

MEQAGTRPAATEHPRLRRPMPWLLLLPLLLLLLLLLPGPAASQLRYSVPEEQAPGALVGNVARALGLELRRLGPGCLRINHLGAPSPRYLELDLTSGALFVNERIDREALCEQRPRCLLSLEVLAHNPVAVSAVEVEILDINDNSPRFPRPNYQLQVSESVAPGARFHIESAQDPDVGANSVQTYELSPSEHFELDLKPLQENSKVLELVLRKGLDREQAALHHLVLTAVDGGIPARSGTAQISVRVLDTNDNSPAFDQSTYRVQLREDSPPGTLVVKLNASDPDEGSNGELRYSLSSYTSDRERQLFSIDASTGEVRVIGGLDYEEASSYQIYVQATDRGPVPMAGHCKVLVDIVDVNDNAPEVVLTDLYSPVPENATPNTIVAVLSVNDQDSGPNRKVSLGLEATLPFRLNGFGNSYTLVVSGPLDRERVAVYNITVTATDGGIPQLTSLRTLKVEISDINDNPPSFLEDSYSIYIQENNLPGVLLCTVQATDPDEKENAEVTYSLLEREIQGLPVTSYVSINSASGSLYAVNSFDYEKFREFFVTVEAQDKGSPPLSSTVTANVYVVDMNDHAPHILYPTSTNSSAAFEMVPRTAPAGYLVTKVIAMDSDSGQNAWLFYHLAQTSDLDLFKVELHTGEIRTTRKMGDESGSTFNLTVVVRDNGEPSLSASVAITVAVVDRVSKILPDTQRHVKSPRTYSEITLYLIIALSTVSFIFLLTIIILSIIKCYRYTAYGTACCGGFCGVRERSPAELYKQANNNIDARIPHGLKVQPHFIEVRGNGSLTKTYCYKACLTAGSGSDTFMFYNTGAQTGPGPSGAQAAVTDSRNLTGQSGQNAGNLIILKNEAVSQNEPRQPNPDWRYSASLRAGMHSSVHLEEAGILRAGPGGPDQQWPTVSSATPEPEAGEVSPPVGAGVNSNSWTFKYGPGNPKQSGPGELPDKFIIPGSPAIISIRQEPTNSQIDKSDFITFGKKEETKKKKKKKKGNKTQEKKEKGNSTTDNSDQ

Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.

Q9Y5I4

A4F727

THIE_SACEN

Thiamine-phosphate pyrophosphorylase

Saccharopolyspora

MPGLDGFGIRARLEEALLYLCTDARTERGDLAEFADAALDGGVDIIQLRDKSAGGAPLEARHELAALEVLAEACVRHGALLAVNDRADVAMAADADVLHLGQDDLPVELARRIVGDQVVVGRSTHDVVQADSAATEQGVDYFCTGPVWTTPTKPGREAAGLELVRHTAEHRGHGRPWFAIGGIGMDNIDEVVQAGARRVVVVRAITEAEDPRAAAAALRTKLG

Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).

A4F727

Q7T2Q4

PA2A2_BUNFL

Phosphatidylcholine 2-acylhydrolase

Bungarus

MNPAHLLVLSAVCVSLLGAAIVPPQPLNLIQFSSLIQCANGGSRATWHYADYGCYCGKGGGGTPVDELDRCCQTHDNCYGEAEKLTKCSPYYKTYKYDCSEGKLTCNDAPGSCERSVCDCDRVAAICFAGAPYNDKNFMINTETNCQ

PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.

Q7T2Q4

A6TRL1

RIMP_ALKMQ

Ribosome maturation factor RimP

Alkaliphilus

MNKIESITEDLITPIVEAEQFELVDIEFKKEGPHKYLRVYIDKPGGITLDDCQKVSEGLSKKLDEADPIVENYFLEVSSPGLDRPLKREVDFLKFKGEMIELKLYEAIDGQKTIEGELVGLIDDKIVIKISETEEVEMPREKVAITKLAIKF

Required for maturation of 30S ribosomal subunits.

A6TRL1

Q4IBL8

DML1_GIBZE

Protein DML1

Fusarium

MREIVTLQLDQESYFTYSSDEKSLIDHNVHWRAGLGADGSETFLPRTVIYDLKGGFGSLRKINALYEAESESAPEALWSGQSVVHKQTPITPSEYQQSLDAGSEPAQLTTSNVRYWSDFSRVYFHPKSLNQLYDFELNSTTMPFERFSMGTELFSMLDREHDLADRDFRPFAEECDRMQGIQVFTTIDDAWGGFTSSYLESLRDDFPKTTIWTWGLQSPLLDISRAKRQLRLVNTAHSIEQLCTQSTTVVPLALPEEDMTTSVSMDRRSPWHTSALMAAAIETATLPSRLTQGSSEQAGSLDVLAESLNVNGNQPLASMRMSLAPAKDSPEDSRINVDFFQVGRVWSRQHVARLDTHKHVFGEILSYRDLDPLGHDNENGHLAPGERPIIGNSIVRKYDSALRFPLLDAYPQIYPQLAGNSDASLQTTLSTNSSIVQRIRTLRTESARLVPVNEREDLGNGLADLADAYQEGWFSGSDEDDDDL

Involved in the partitioning of the mitochondrial organelle and mitochondrial DNA (mtDNA) inheritance.

Q4IBL8

G3XDT7

LYSC_DRONO

1,4-beta-N-acetylmuramidase C

Dromaius

MKFFLILGFCLLPLIAQGKVFQRCELAAAMKKHGLSNYRGYSLGHWVCAAKYESNFNTAAINRNRDGSSDYGILQINSRWWCNDGRTSGAKNLCKISCSALLSSDITASVNCAKRVVSDKNGMNAWVAWRNHCKGRDVSQWIRGCRV

Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.

G3XDT7

Q9RKY0

RBPA_STRCO

RNA polymerase-binding protein RbpA

Streptomyces albidoflavus group

MSERALRGTRLVVTSYETDRGIDLAPRQAVEYACEKGHRFEMPFSVEAEIPPEWECKVCGAQALLVDGDGPEEKKAKPARTHWDMLMERRTREELEEVLEERLAVLRSGAMNIAVHPRDSRKSA

Binds to RNA polymerase (RNAP), stimulating transcription from principal, but not alternative sigma factor promoters. Stimulates transcription from several principal sigma factor HrdB (SigA)-dependent promoters but not from a SigR-dependent promoter. Stimulation occurs in the presence of the transcription initiation inhibitor rifampicin (Rif).

Q9RKY0

Q2NEH8

GCH3_METST

GTP cyclohydrolase III

Methanosphaera

MIQVTLIQIDNYGPWTVTPGPRAEPDLQTLQSRLYGDLEREFGAHGAIVFFNRFDNLIAISNGMDYDDHLLIQQSIRNRYPITISMGVGTADTAYEAQKIATKMIQNGGGAQSANRCEVLNIDSLADDDNSLVQIAHIDINDITNTLTDIETAFDTSIKVYEVLLALMDELAKIGGMCFFIGGDNYMAPTNGISKDQLREALKVVDKKTGVTLKAGIGVAKQAGRAADLADIGLEDIRAELVDDSVLLFNDLDEY

Catalyzes the formation of 2-amino-5-formylamino-6-ribofuranosylamino-4(3H)-pyrimidinone ribonucleotide monophosphate and inorganic phosphate from GTP. Also has an independent pyrophosphate phosphohydrolase activity.

Q2NEH8

Q6HC18

GLGA_BACHK

Starch [bacterial glycogen] synthase

Bacillus cereus group

MNILFAVSECVPFVKSGGLADVAGALPKELKKLGVEVRIILPNYSLIPQKLRDGCTLHKVINVPLGWRNQYCGILKGEQDGITYYLIDNEYYFKRDSLYGHYDDGERFSYFSKAVLECIPHLDFEVDVLHSHDWHTAMVNFLLREKYQDNPSYEHIKTVYTIHNLQFQGVFSPEVMYDLLELGDEYFHSEQLEFYGNVNFMKGGIIASDQITAVSPTYKEEIQYEFFGEKLDGLLRKYNDKLSGIVNGIDTSVYNPETDSYITAQYDADSLYEKNENKRALQRYFGLPEKEDTPIISMVTRLTKQKGLDLVRTVFREIMEEDVQCIILGSGDSEYEQFFEWMAYEYPEKVKVYIGFNEELAHQVYAGSDLFLMPSLFEPCGLGQLIALAYGTIPIVRETGGLNDTVQSYDEETGEGNGFSFTNFNAHDMLHTVLRAIEFYHDKPVWDQLVKQAMTEDYSWEKSALAYKKLYKSLME

Synthesizes alpha-1,4-glucan chains using ADP-glucose.

Q6HC18

A9ISF8

RL7_BART1

50S ribosomal protein L7/L12

Bartonella

MADLAKIVEDLSNLTLLEAAELSKLLEEKWGVSAAAPVAVAAVAGAAAPAAEEKTEFDVILVEGGAQKINVIKEVRALTGLGLKEAKDLVEGAPKPIKEGASKEEAEKIKSQLEAAGAKVELK

Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.

A9ISF8

Q7M803

ACPS_WOLSU

4'-phosphopantetheinyl transferase AcpS

Wolinella

MIGIDLVSIERIEAFIAKHGQRGLERFLLPEEILLANKPETIAGFWAAKEACSKALGTGIGAEVGFHDIRLFKNPKGAPLLELSPRVKDRFEIDSCALSITHDKGFAIAVVAMEKRRA

Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.

Q7M803

C0HK11

CZS15_CRUCA

Cruzioseptin-15

Cruziohyla

GFLDIVKGVGLVALGAVSKS

Has antimicrobial activity.

C0HK11

C7J6G6

AB46G_ORYSJ

Pleiotropic drug resistance protein 21

Oryza sativa

MDDDVDAGEIYAVDRQREEGSASAAAFSRSPSTGRVDDDDDDLLTYGRSARRMAALPAPAMPEGTELRRPVGGDVVGDDDYLRFLYKFKELFDRVGIKLPTIEVRYKNLNVEAESYVGSRGLPTILNTYANILKGLANTLHMTTRSKQKISVLHNASGIIKPHRMTLLLGSPGSGKTSLLLALAGTLPSTVKVSGMITYNGHTMDKFIPQRSAAYVSQHDLHMAELTVRETINFSAKCQGVGHHYDLFLELLRREEEENITPDPETDIYLKAATTGEEKAEIVTNHILKILRLDICADTIVGDNMLRGISGGQKRCLDAHTAPNVDSAAEMLVTLGRALFMDEISNGLDSSTTFQIVNTIQQTIHVLGGTAVIALLQPAPETYELFDDIILLSDGQVVYSGPRDHVLEFFKSLGFKCLERIGVADFLQEVTSRKDQKQYWIHGDDTYRYIPVTVIAEAFQCFHVGQAIRSELAIPFDNSKSHIAALKTSKHGVNLKKILKANIDREILLLKRKSFLYIFNALQLTLVAIIAMSVFIHTNMHHDSIENGRMYMGVQFFGTLAIMFKGLAEMGAALANLPVFFKQRDLLFYPAWTYSLPSWIIKTPISFLNTIIWVSITYYVIGFDPNIERCFRQFLVLFVMSEAICGLFRFIAALTRHPVVASTVSEFCILIVMVSSGFILSRDEVKKWLIWEYWTSPLMYALNALAVNEFLSPSWNEALPGFREPLGRLVLESRGVFPEAKWYWIGLGALLGYVLLFNILYTICLSILTLLKRNVREMSQETLQIKLENLTGYDQEPSSGGRVTNDKRYTEGGNNDEATSSNANHNSSPARKGSILPFVPVYMTFEDIRYSIDMPKALKVQGMAGSRLELLKDLSGSFRPGVLTALMGISGAGKTTLLDVLAGRKTSGHIHGNITVSGYPKKQETFSRVSGYCEQNDIHSPNLTVYESLMFSAWLRLPAEIDSMARKRFIDEFMELVELFPLKDALVGLLGLSGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNIVDMGRTVVCTIHQPSIDIFESFDELFLMKRGGEAIYVGPLGQHSCELIKYFESIEGVRKIKHGYNPSTWMLEVTCTLQEQITGVNFTQVYKNSELYRRNKNLIKELSTPHDGSSDLLFPTKYSQTFVIQCLACLWKQRLSYWRNPPYIAVNFFFTVVIALLFGTMFWGVGRKRQSQQALLSAMGSMYSTCFTLGVQNSSSVQPVVNIERTVFYRERASHMYSPLPYALGQVVVELPYIFLQTLIYGVIVYSMMGYEWTCTKFFWYMFFMYFTLSYFTFYGMMAAGLTPNYTMSSIVSTTFYAIWHLFSGFLIPKTRIPIWWRWYYWICPVAWTINGLVTSQFGDVDDKFDNGVRVSDFVESYFGYNLDLLWVAAMAVVSFAILFAILFGFSLKLFNFQKR

May be a general defense protein.

C7J6G6

B4S010

RL9_ALTMD

50S ribosomal protein L9

Alteromonas

MNIILLDKIANLGGLGDQVTVKSGYARNFLFPQGKAVPATKDNVEKFEARRAELEAKIAEQLAAANARAEKVAELAEVTIAAPAGDEGKLFGSVGTRDIADAITAAGVEVQKAEVKLPTGTLRETGEYDIDLQLHSDVITSIKVIIIAEA

Binds to the 23S rRNA.

B4S010

P83041

DID5_CERCE

Disintegrin CC5B

Cerastes

MNSAHPCCDPVTCKPKRGEHCISGPCCRNCKFLSPGTICKKARGDDMNDYCTGISSDCPRNRYKS

Binds and inhibits integrins alpha-IIb/beta-3 (ITGA2B/ITGB3), alpha-V/beta-3 (ITGAV/ITGB3) and alpha-5/beta-1 (ITGA5/ITGB1).

P83041

Q5VVX9

UBE2U_HUMAN

Ubiquitin-protein ligase U

Homo

MHGRAYLLLHRDFCDLKENNYKGITAKPVSEDMMEWEVEIEGLQNSVWQGLVFQLTIHFTSEYNYAPPVVKFITIPFHPNVDPHTGQPCIDFLDNPEKWNTNYTLSSILLALQVMLSNPVLENPVNLEAARILVKDESLYRTILRLFNRPLQMKDDSQELPKDPRKCIRPIKTTSFSDYYQTWSRIATSKATEYYRTPLLKVPNFIGQYYKWKKMDLQHQKEWNLKYSVIKCWLARKRMPHEVTHSMEEIKLCPTLIPTTDEIFLESPTAINSITDIYETEEEGWKSDTSLYENDTDEPREEEVEDLISWTNTLNTNTSED

Catalyzes the covalent attachment of ubiquitin to other proteins.

Q5VVX9

O65862

CAMT1_POPTR

Trans-caffeoyl-CoA 3-O-methyltransferase 1

Populus

MATNGEEQQSQAGRHQEVGHKSLLQSDALYQYILETSVYPREPECMKELREVTAKHPWNIMTTSADEGQFLNMLLKLVNAKNTMEIGVYTGYSLLATALAIPEDGKILAMDINRENYELGLPVIQKAGVAHKIDFKEGPALPVLDQMIEDGKCHGSFDFIFVDADKDNYINYHKRLIELVKVGGLIGYDNTLWNGSVVAPPDAPMRKYVRYYRDFVLELNKALAADPRIEICMLPVGDGITLCRRIQ

Methylates caffeoyl-CoA to feruloyl-CoA and 5-hydroxyferuloyl-CoA to sinapoyl-CoA. Plays a role in the synthesis of feruloylated polysaccharides. Involved in the reinforcement of the plant cell wall. Also involved in the responding to wounding or pathogen challenge by the increased formation of cell wall-bound ferulic acid polymers.

O65862

X5JB51

SECAB_ARATH

Exocyst complex component SEC10b

Arabidopsis

MTERIRARGPRSSSVNSVPLILDIEDFKGDFSFDALFGNLVNDLLPSFLDEEADSGDGHGNIAGVDGLTNGHLRGQSAPLSSAPFFPEVDGLLSLFKDACKELVDLRKQVDGRLNTLKKEVSTQDSKHRKTLTEIEKGVDGLFESFARLDGRISSVGQTAAKIGDHLQSADAQRETASQTIDLIKYLMEFNGSPGDLMELSALFSDDSRVAEAASIAQKLRSFAEEDIGRQGASTAAGNATPGRGLEVAVANLQDYCNELENRLLSRFDAASQRRDLSTMSECAKILSQFNRGTSAMQHYVATRPMFIDVEVMNSDIRLVLGDHGSQPSPSNVARGLSALFKEITDTVRKEAATITAVFPTPNEVMAILVQRVLEQRVTGILDKILAKPSLMSPPPVQEGGLLLYLRMLAVAYERTQELAKDLRAVGCGDLDVEDLTESLFSSHKDEYPEHERASLKQLYQAKMEELRAESQQVSESSGTIGRSKGASISSSLQQISVTFVTEFVRWNEEAITRCTLFSSQPATLAANVKAIFTCLLDQVSVYITEGLERARDSLSEAAALRERFVLGTSVSRRVAAAAASAAEAAAAAGESSFKSFMVAVQRCGSSVAIVQQYFANSISRLLLPVDGAHAASCEEMSTALSKAEAAAYKGLQQCIETVMAEVDRLLSSEQKSTDYRSPDDGIASDHRPTNACIRVVAYLSRVLESAFTALEGLNKQAFLTELGNRLEKLLLTHWQKFTFNPSGGLRLKRDLNEYVGFVKSFGAPSVDEKFELLGIIANVFIVAPDSLPTLFEGSPSIRKDAQRFIQLREDYKSAKLATKLSSLWPSLS

Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane during regulated or polarized secretion. Involved in polarized cell growth and organ morphogenesis. During cytokinesis, involved in cell plate initiation, cell plate maturation and formation of new primary cell wall.

X5JB51

B8EE60

CYSD_SHEB2

Sulfate adenylate transferase

Shewanella

MAGRELSHLQQLEAESIQIIREVAAEFDNPVMLYSIGKDSSVMLHLARKAFYPGKIPFPLLHVDTGWKFKEMIAFRDAQAKKFGFELLTHINPEGLAQGINPFDHGSAKHTDIMKTQGLKQALNQYGFDAAFGGARRDEEKSRAKERVYSFRDRHHRWDPKNQRPELWRTYNGAVNKGESIRVFPLSNWTELDIWQYIYQENIELVPLYFAAKRQVVERGGQLIMADDERMKLAEGEQFKEELVRFRTLGCYPLTAAMHSEADSLEKIIEEMLLTRSSERQGRLIDSDQSASMEQKKRQGYF

With CysN forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.

B8EE60

A6L1V8

LEUC_PHOV8

Isopropylmalate isomerase

Phocaeicola

MANTLFDKIWDAHVVQKVEEGPTQLYIDRLYCHEVTSPQAFAGLRARGVKVFRPDHVYCMPDHNTPTHDQDKPIEDPVSKTQVDTLAKNAKDFGLAHFGMMDKRNGIIHVVGPERGLTLPGMTIVCGDSHTSTHGAMGAVAFGIGTSEVEMVLASQCILQSRPKTMRITIDGELGKGVTAKDMALYMMSKMTTSGATGFFVEYAGSAVRNLSMEGRLTLCNLSIEMGARGGMVAPDEVTFEYIKGREHAPKGVDWDKAVSHWKTLKSDDDAVFDKEIRFDAADIQPMITYGTNPGMGMGITEHIPVDDKSASFKKSLDYMGFQPGESLLGKKIDYVFLGACTNGRIEDFRAFTSLVRGKKKADHVTAWLVPGSWMVDAQIREEGLDKILEEAGFAIRQPGCSACLAMNDDKIPAGKYSVSTSNRNFEGRQGPGARTLLASPLVAAAAAVTGVITDPRELI

Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.

A6L1V8

Q8R3Q2

PP6R2_MOUSE

SAPS domain family member 2

Mus

MFWKFDLNTTSHVDKLLDKEHVTLQELMDEDDILQECKAQNQKLLDFLCRQQCMEELVNLITQDPPQDMEEKVRFKYPNTACELLTCDVPQISDRLGEDESLLNLLYDFLDQEPPLNPLLASFFSKTIGNLIARKTEQVIMFLKKKEKFISQLLKHIGTSALMDLLLRLVSCVEPVGLRQEVLHWLNEEKIIQRLVALIHPHQDEDRQSNASQALCDIIRLGRDQGSQLQETVEPDPLLITLESQDCVEQLLKNMFDGDQTESCLVSGMQVLLALLEPRRVGTEGLVDSFSQGLERSHSVSSSILRGIEPWLKNFHQLLLNPPKKKAILTTIGVLEEPLGNARLHGARLMAALLHTNTPGINQELCRLNTMDLLLDLFFKYTWNNFLHLQVELCIAAILSHAAREEQAEASGSDGKVEPLQGSGDGNGKLETTPSITSPPENTMVTHLFQKCCLVQRILEAWEANDHTQAAGGMRRGNMGHLTRIANAVVQNLEQGPVQAHISEVIRGLPADCRGRWESFVEETLMETNRRNTVDLAFSEYQIQQMTANFVDQFGFNDEEFADQDDNINAPFDRIAEINFNIEADEDSPSAALFEACCSDRIQPFDDDEEEDIWEDDETRCAARVMARARFGAPHVSDNYSKNALEHGGQDRKTGSAVARNVPGLAAPSSPTQKEGPRSESDSAGTTWTAVFDEPVNPLSATPGAARDVGSSAWAAGPSVVEEKGWAKFTDFQPFCCSETGPRCSSPVDMDHSNAEGGQSPGPEKTFGPTSPCAWNVCVTRKAPLVASDSSSSGGSDSEDDEKAAGAVEAVCTGHTGKVSPPPRTAEAAVGRAECPDSTVLAPACPAPSEVTISPAVATIAPSKAGSPTATIVVSSSVAAAVPPGPIVAVTTAAPAIVATLGTMTKDRKADALPEGAALNGPV

Regulatory subunit of protein phosphatase 6 (PP6). May function as a scaffolding PP6 subunit. Involved in the PP6-mediated dephosphorylation of NFKBIE opposing its degradation in response to TNF-alpha.

Q8R3Q2

Q2YXP5

TRUB_STAAB

tRNA-uridine isomerase

Staphylococcus

MYNGILPVYKERGLTSHDVVFKLRKILKTKKIGHTGTLDPEVAGVLPVCIGNATRVSDYVMDMGKAYEANVSIGRSTTTEDQTGDTLEMKGVHSADFNNDDIDRLLENFKGVIEQIPPMYSSVKVNGKKLYEYARNNETVERPKRKVNIKDIGRISELDFKENECHFKIRVICGKGTYIRTLATDIGVKLGFPAHMSKLTRIESGGFVLKDSLTLEQIKELHEQDSLQNKLFPLEYGLKGLPSIKIKDSHIKKRILNGQKFNKNEFDNKIKDQIVFIDDDSEKVLAIYMVHPTKESEIKPKKVFN

Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.

Q2YXP5

Q2NHD9

IF2B_METST

eIF-2-beta

Methanosphaera

MAKENAEFKEYEKLLDQAYEQLPDKIFEAKRFKVPKGYSVIQGNRTIIKNFGDVSRTLNRDPQHVLKYLLRELGTSGNVEGNRAILQGKFTHYVINDRVKEYVDNFVMCHECNRPDTVIIREDRIDMLKCSACGARAPLKSL

eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.

Q2NHD9

Q46GA1

RS3_METBF

30S ribosomal protein S3

Methanosarcina

MAIERKFVNDGFVKASMDEYFAEQLNRAGYGGMELNRTPMGTQIVIYSEKPGMVIGKAGKVIRKLTRDVAARYNLENPQIDAQEVKKPELNAQMMASRLAASIERGWYFRKAGHNTLRAVMNAGALGCEVVISGKLTGARSRVEKFVDGYIKHSGNPVDEVVDEGFAVAIKKLGTLGCKVRIIQPGVVLPDSYTTTEPSEPVTEPVEKPAEKPAAKPAEKPVEAPKKESAAKPKTPAVAPEKPVETAEVAEPEEAEEEPQAEVAEDLEEAEVIQVEGSEELRRQVNGVWQHKHEGYDYWHPMARVHKEAKE

Binds the lower part of the 30S subunit head.

Q46GA1

Q8FS54

RL6_COREF

50S ribosomal protein L6

Corynebacterium

MSRIGKNPIAIPSGVEVKIDGRLVDVKGPKGNLNVTLPEPITASIENNEILVTRPDDHRNSRSMHGLSRSLVNNLVVGVTEGYTIKMEIFGVGYRVALKGKNLEFSLGYSHPVLIEAPEGITFAVDGTTKLSISGIDKQKVGQVAAVIRRLRKDDPYKGKGIRYEGEQIRRKVGKTGK

This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.

Q8FS54

Q9KGE8

SECE_HALH5

Protein translocase subunit SecE

Halalkalibacterium (ex Joshi et al. 2022)

MAGGVKGIGKFFGDVVAEMKRVSWPTRKELTRYTLVVLGTVAFITVFFAVVDYGISALVRGLIE

Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.

Q9KGE8

Q4G3C6

PSBZ_EMIHU

Photosystem II reaction center protein Z

Emiliania

MVGILPLFVVLLIIVSFAMVVAVPVILATPGEWEKSQGIVWSGAGLWSALVILTGVFNAVPA

Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.

Q4G3C6

Q9SLK2

ALIS3_ARATH

ALA-interacting subunit 3

Arabidopsis

MSSNTASSSAGAAGSGDSSAARKNSKRPKYSKFTQQELPACKPILTPGWVISTFLIVSVIFIPLGVISLFASQDVVEIVDRYDTECIPAPARTNKVAYIQGDGDKVCNRDLKVTKRMKQPIYVYYQLENFYQNHRRYVKSRSDSQLRSTKYENQISACKPEDDVGGQPIVPCGLIAWSLFNDTYALSRNNVSLAVNKKGIAWKSDKEHKFGNKVFPKNFQKGNITGGATLDPRIPLSEQEDLIVWMRTAALPTFRKLYGKIESDLEMGDTIHVKLNNNYNTYSFNGKKKLVLSTTSWLGGKNDFLGIAYLTVGGICFILALAFTIMYLVKPRRLGDPSYLSWNRNPGGR

Required for the lipid transport activity of the ALA/ALIS P4-ATPase complex.

Q9SLK2

B2VK80

RL18_ERWT9

50S ribosomal protein L18

Erwinia

MDKKSARIRRATRARRKLKELGATRLVVHRTPRHIYAQVIAPNGSEVLVAASTVEKAIGEQLKYTGNKDAAAAVGKAVAERAIEKGITGVSFDRSGFQYHGRVQALADAAREAGLQF

This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.

B2VK80

A9WFA3

CH602_CHLAA

Chaperonin-60 2

Chloroflexus

MAKQLIFDQQARTALKHGIDTLALAVKTTLGPRGRNVALDKKWGAPTVTHDGVSVAKEIELKDPFANLGVQLLKQAAVKTNDVAGDGTTTATVLAQAIINEGLKLVAAGANPMLLKRGLDKGGQALVARIKEQAITLKTRDEIRNVATISAQDAEVGELLATVMDKIGRDGVVTVEEGKSTHLEHELVEGMQFDRGYISPYFITDSARMEAVLDEPYILITDKKISAIKDLLPILEAVLSSGKKDLLVIAEDVDGEALATLVVNKLRGTLNALAVKAPGFGDRRKAMLQDIAILTGGTVISEEIGRKLESATLQDLGRARRVKADKDNTVIVEGHGDKQAIQARIAQLKQQIETTTSDYDREKLQERVAKLSGGVAVIKVGAPTEPAMKERKARVEDALNATRAAVEEGIVPGGGVALLNAIPALDNVTTQFEEERMALNVLRRALEEPLRQLATNAGEDGSVVVENVRNEQRKHNNNHYGYDVMTGTYVDLMQAGIIDPAKVVRSALENAISVAGMVLTTEALIVDAPEPKKKNGTPPMPDDDF

Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.

A9WFA3

P06149

DLD_ECOLI

Respiratory D-lactate dehydrogenase

Escherichia

MSSMTTTDNKAFLNELARLVGSSHLLTDPAKTARYRKGFRSGQGDALAVVFPGSLLELWRVLKACVTADKIILMQAANTGLTEGSTPNGNDYDRDVVIISTLRLDKLHVLGKGEQVLAYPGTTLYSLEKALKPLGREPHSVIGSSCIGASVIGGICNNSGGSLVQRGPAYTEMSLFARINEDGKLTLVNHLGIDLGETPEQILSKLDDDRIKDDDVRHDGRHAHDYDYVHRVRDIEADTPARYNADPDRLFESSGCAGKLAVFAVRLDTFEAEKNQQVFYIGTNQPEVLTEIRRHILANFENLPVAGEYMHRDIYDIAEKYGKDTFLMIDKLGTDKMPFFFNLKGRTDAMLEKVKFFRPHFTDRAMQKFGHLFPSHLPPRMKNWRDKYEHHLLLKMAGDGVGEAKSWLVDYFKQAEGDFFVCTPEEGSKAFLHRFAAAGAAIRYQAVHSDEVEDILALDIALRRNDTEWYEHLPPEIDSQLVHKLYYGHFMCYVFHQDYIVKKGVDVHALKEQMLELLQQRGAQYPAEHNVGHLYKAPETLQKFYRENDPTNSMNPGIGKTSKRKNWQEVE

Catalyzes the oxidation of D-lactate to pyruvate. Electrons derived from D-lactate oxidation are transferred to the ubiquinone/cytochrome electron transfer chain, where they may be used to provide energy for the active transport of a variety of amino acids and sugars across the membrane.

P06149

Q07IE7

ILVD_RHOP5

Dihydroxy-acid dehydratase

Rhodopseudomonas

MPAYRSRTSTHGRNMAGARSLWRATGMKNEDFGKPIIAVVNSFTQFVPGHVHLKDLGQLVAREIEKAGGIAKEFNTIAIDDGIAMGHDGMLYSLPSRELIADSVEYMVNGHCADAMVCISNCDKITPGMLMASLRLNIPSVFVSGGPMEAGKVVLSTGARKVDLIDAMVSAADDSMSDADVAVMEENACPTCGSCSGMFTANSMNCLTEALGLSLPGNGSVLATHADRQRLFVEAGHLIVDITRRYYEQNDDSVLPRNVASFAAFENAMSLDIAMGGSTNTVLHLLAAAQEGEVNFTMTDIDRLSRRVPCLCKVAPSVATVHMEDVHRAGGIMSILGQLDAAGLLNGDTKTVHATSLRAAIDRWDISRTNSDSVRQFYLAAPGGVPSQTAFSQSQRWDSLDTDRENGVIRSKAHAFSQDGGLAVLFGNIALDGCIVKTAGVDDSILKFSGPAVVYESQDDAVNGILTGKVKEGDVVVIRYEGPRGGPGMQEMLYPTSYLKSKGLGKACALITDGRFSGGTSGLSIGHCSPEAAEGGTIGLVETGDMIDIDIPNRGINLRVSDAVLAERRKAMEAKGKDAWKPVAPRKRKISSALKAYALFASSAAKGAVRVLKD

Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.

Q07IE7

A1JIM8

TDCC_YERE8

H(+)/threonine-serine symporter

Yersinia

MHIDNAITTTIETKTWRKSDTTWTLGLFGTAIGAGVLFFPIRAGFGGLIPILIMLVLAYPIAFLCHRALARLCLSGSNCSGNITETVEEHFGKTGGVVITFLYFFAICPLLWIYGVTITNTFMTFWENQLQLAPLNRGVVALALLLLMAVVIYFGKDLMVKVMSFLVFPFIACLVLISLSLIPYWNASVIEQVDLSQISLLGHDGILVTVWLGISIMVFSFNFSPIVSSFVVSKREEYEPEFGREYTEKKCSQIISRASILMVAVVMFFAFSCLFTLSPQNMAEAKAQNIPVLSYLANHFSSMAGSRSTFSITLEYAASLIALVAIFKSFFGHYLGTLEGLNGLVIKFGYKGDKTKISSGKLNLISMFFIMGSTWLVAYINPNILDLIEAMGAPIIASLLCLLPMYAIHKLPSLARFRGRPENYFVTIVGLLTIFNIVYKLL

Involved in the import of threonine and serine into the cell, with the concomitant import of a proton (symport system).

A1JIM8

A3N1M8

IF1_ACTP2

Translation initiation factor IF-1

Actinobacillus

MAKEDCIEMQGTILETLPNTMFRVELENGHVVTAHISGKMRKNYIRILTGDKVTVEMTPYDLSKARIIFRAR

One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.

A3N1M8

P37738

FATD_VIBA7

Ferric-anguibactin transport system permease protein FatD

Vibrio

MTFRMILAFFTLCATSLFFGANQIEWSLLPTFNEKAWLPIIASRLPRLVALILTGSGLAMCGVILQHIVRNRFVEPGTTGSLDAAKLGILVSIVMLPSSDKLERMFFAVLFCFAAGLVYIAIIRKVKFSNTALVPVIGLMFGSVLSALAEFYAYQNNILQSMSGWLMGDFSKVVQEHYEIIFLILPITLLTYLYAHRFTVMGMGEDIASNLGISYAMTAALGLILVSITVAVTVVTVGAIHFVGLVIPNLVALKYGDHLKNTLPIVALGGASLLIFCDVISRVVLFPFEVPVGLTASAVGGVMFLAFLLKGAKA

Involved in the uptake of iron in complex with the siderophore anguibactin. Responsible for the translocation of ferric-anguibactin across the cytoplasmic membrane.

P37738

O74368

MMM1_SCHPO

Maintenance of mitochondrial morphology protein 1

Schizosaccharomyces

MIHLPQGSFTQGLIVGQLLTLAIIYVFLRFFLFCSPIPKSVANSPKQTGNETPDETPSTPLSNNKKRYKKPLTILEPHILNLLYDVNEHEPESLDWFNVLIAQALIQFRYDACSNDVALRKLETVLNKGAQDKSMVDHIYVRDLSLGDGFPVFSHCRVLPHQHNSSQLRAEMLVSLTDNINCTVDTKLLLNFPKPAFATLPLSITVRICKFVGKIMIYFSPSNGAGQPAYMNLSFDPNFVISLQVSSLVGARSKLQDIPKITQLIESRIRQWFTNRCVSPQFQQIAIPNLWPTSAKEGHARSHAPQEESSNED

Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The mdm12-mmm1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The mdm10-mdm12-mmm1 subcomplex further acts in the TOM40-specific pathway after the action of the mdm12-mmm1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.

O74368

P29987

PYG2_NOSS1

L-RC 28.5

Nostoc

MSIPLLEYKPSSQNQRVPGYEVPNEDTPRIYRIEDAAYDSELKELIWATYRQVFSEHVILKFFRQGNLESQLKNRAISVRDFVRGLAKSEAFKTLVIKSNSNYRLVELALKRLLGRAPYNKDEEIAWSIKIATNGWDGFVDALLDSEEYQSNFGENIVPYQRRRYKDRPFNLVTPRYGNYWRDKLESERYIEGDIKNFLELAKSIEIKTVTFTPVSTANIKIPDTTRNTTPTGIPISVNPSANFPVR

Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer.

P29987

Q1GUG9

GREA_SPHAL

Transcript cleavage factor GreA

Sphingopyxis

MASVEKVPMLAEGYEKLTAQLAALKAERPLIVDAIEEARAHGDLSENAEYHAAKERQGQVEATIGDLEDKLSRAQVIDPTTLSGDRIVFGATVTLTDEDDKPVKYQIVGQAEADAKAGKISYNSPLGRALIGRRVDDEIEVTVPSGDKYYLVTKIEFI

Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides.

Q1GUG9

B4K4M0

HH_DROMO

Protein hedgehog N-product

Drosophila

MDNNQAVSALWSCASATCLSLDAKRHSLEPSSPDGQASLDVNNKSAPVDAHARKLRHIAHTPRGSCFMALLLLLLLALNFRHAHSCGPGRGLGRRRERNLYPLVLKQTVPNLSEYHNGASGPLEGVIHRDSPKFKNLVLNYNKDILFRDEEGTGADRVMSKRCREKLNMLAYSVMNEWPGVRLLVTESWDEDHQHGQESLHYEGRAVTIATSDRDQSKYGMLARLAVEAGFDWVSYVSRRHIYCSVKSDSSPSISHVHGCFTPESTALLESGAEKALSELAIGDRVLSMDTKGQPVYSEVILFMDRNLEQVQNFVQLHTDGGAVLTVTPAHLIAVWQAERQTLEFVFADRVEELSQVLVHDATGELRPQRVLRVDSVQSRGVVAPLTREGTIVVNSVAASCYAVISSQSLAHWGLAPMRLWSTLQSWMPAKGQLRSAQDKPTPKDATAQQQNGIHWYANALYKVKDYVLPQSWRHD

The dually lipidated hedgehog protein N-product is a morphogen which is essential for a variety of patterning events during development. Establishes the anterior-posterior axis of the embryonic segments and patterns the larval imaginal disks. Binds to the patched (ptc) receptor, which functions in association with smoothened (smo), to activate the transcription of target genes wingless (wg), decapentaplegic (dpp) and ptc. In the absence of hh, ptc represses the constitutive signaling activity of smo through fused (fu). Essential component of a signaling pathway which regulates the Duox-dependent gut immune response to bacterial uracil; required to activate Cad99C-dependent endosome formation, norpA-dependent Ca2+ mobilization and p38 MAPK, which are essential steps in the Duox-dependent production of reactive oxygen species (ROS) in response to intestinal bacterial infection. During photoreceptor differentiation, it up-regulates transcription of Ubr3, which in turn promotes the hh-signaling pathway by mediating the ubiquitination and degradation of cos.

B4K4M0

Q60AI1

POTA_METCA

Spermidine/putrescine import ATP-binding protein PotA

Methylococcus

MRPSRRPRFRNILENRTIAAMTRSTIASFRAVSKHYGSHCALRDFNLELREGELLTLLGPSGCGKTTVLRLLAGLEIPDSGEIFLDGRTLAGVPPEARNVNTVFQSYALFPHLSVAENVAFGLRMKKLGSAEIRARTAEALRMVRLDGLGGHRPLQLSGGQQQRVALARALVNRPRVLLLDECLSALDYQLRREMQLELKGLQRQTGITFVFVTHDREEALSMSDRIAVMRTGRIEQLGPPRDIYERPANLFVAQFAGESNVLEATVTAITAPDSLIVELAGTPLTVRTDRRFRVGARLVLVLRPEDLHVHDDAAAEGGLAGHVLERTYRGVTLDTVIALDAGPRIKTSEFFREDTPALDHPPGQRVRVSWTPGWEIVLPHDPET

Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.

Q60AI1

Q43594

TBB1_ORYSJ

Beta-1-tubulin

Oryza sativa

MREILHIQGGQCGNQIGSKFWEVVCDEHGIDPTGRYVGTSDLQLERVNVYYNEASCGRFVPRAVLMDLEPGTMDSVRTGPYGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGKMSTKEVDEQMINVQNKNSSYFVEWIPNNVKSSVCDIPPRGLSMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEEGDYEDEEEQVPEDE

Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.

Q43594

Q5MIM5

RK31_PALPL

50S ribosomal protein L31, chloroplastic

Palmaria

MPQIDIHPEWYNDSKVYCDGKHIMTIGSTKPELHVDIWSGNHPFFTGSQRIIDTEGRVERFMRKYNVQKTADT

Binds the 23S rRNA.

Q5MIM5

Q8K4I6

CBY1_RAT

PKD2 interactor, Golgi and endoplasmic reticulum-associated 1

Rattus

MPLFGSIFSPKKTPPRKSASLSNLHSLDRSTRELELGLDYGTPTMNLAGQSLKFENGQWVADSVISGGVDRRETQRLRKRNQQLEEENNLLRLKVDILLDMLSETTAESHLKDKELDELKITNRRRK

Inhibits the Wnt/Wingless pathway by binding to CTNNB1/beta-catenin and inhibiting beta-catenin-mediated transcriptional activation through competition with TCF/LEF transcription factors. Has also been shown to play a role in regulating the intracellular trafficking of polycystin-2/PKD2 and possibly of other intracellular proteins. Promotes adipocyte and cardiomyocyte differentiation.

Q8K4I6

Q32CN1

SYA_SHIDS

Alanyl-tRNA synthetase

Shigella

MSKSTAEIRQAFLDFFHSKGHQVVASSSLVPHNDPTLLFTNAGMNQFKDVFLGLDKRNYSRATTSQRCVRAGGKHNDLENVGYTARHHTFFEMLGNFSFGDYFKHDAIQFAWELLTSEKWFALPKERLWVTVYESDDEAYEIWEKEVGIPRERIIRIGDNKGAPYASDNFWQMGDTGPCGPCTEIFYDHGDHIWGGPPGSPEEDGDRYIEIWNIVFMQFNRQADGTMEPLPKPSVDTGMGLERIAAVLQHVNSNYDIDLFRTLIQAVAKVTGATDLSNKSLRVIADHIRSCAFLIADGVMPSNENRGYVLRRIIRRAVRHGNMLGAKETFFYKLVGPLIDVMGSAGEDLKRQQAQVEQVLKTEEEQFARTLERGLALLDEELAKLSGDTLDGETAFRLYDTYGFPVDLTADVCRERNIKVDEAGFEAAMEEQRRRAREASGFGADYNAMIRVDSASEFKGYDHLELNGKVTALFVDGKAVDAINAGQDAVVVLDQTPFYAESGGQVGDKGELKGANFSFVVEDTQKYGQAIGHIGKLAAGSLKVGDAVQADVDEARRARIRLNHSATHLMHAALRQVLGTHVSQKGSLVNDKVLRFDFSHNEAMKPEEIRAVEDLVNAQIRRNLPIETNIMDLEAAKAKGAMALFGEKYDERVRVLSMGDFSTELCGGTHASRTGDIGLFRIISESGTAAGVRRIEAVTGEGAIATVHADSDRLSEVAHLLKGDSNNLADKVRSVLERTRQLEKELQQLKEQAAAQESANLSSKAIDVNGVKLLVSELSGVEPKMLRTMVDDLKNQLGSTIIVLATVAEGKVSLIAGVSKDVTDRVKAGELIGMVAQQVGGKGGGRPDMAQAGGTDAAALPAALASVKGWVSAKLQ

Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.

Q32CN1

Q7UWC8

ISPG_RHOBA

1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase

Rhodopirellula

MLSFMKIRRNPTRPVTIGSITIGDGHPIAVQSMTATKTQNIDATVEQAEALHARGAGVVRIAVDSDKDAEALAEIRKQTQANLAVDLQENFRLAEKVAPHVDKIRYNPGHLYHHARELTWQEKVRYLIDTAGSNNCAVRIGVNCGSVDPAKKEKYDHDDSITPMLESALEHCELVDSLGFHNFVVSLKDSDPSKVVQVNTLFAEKRPDVALHLGVTEAGMPPDGIIKTRIAFEQLIGKGIGDTVRVSLTLPNPRKPEEIDAGKQIVEDIHAGRVRSVVKFDDSKLNIISCPSCSRVENEAFIDLAAKVKEMTTFAQEYSITIAVMGCRVNGPGETDDADLGLWCGPAKVNLKRGPEALGAFGYDEILPKLKQELDDLIAAKQ

Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.

Q7UWC8

Q9N4D9

NTM1_CAEEL

X-Pro-Lys N-terminal protein methyltransferase 1

Caenorhabditis

MSSSSSSRIHNGEDVYEKAEEYWSRASQDVNGMLGGFEALHAPDISASKRFIEGLKKKNLFGYFDYALDCGAGIGRVTKHLLMPFFSKVDMEDVVEELITKSDQYIGKHPRIGDKFVEGLQTFAPPERRYDLIWIQWVSGHLVDEDLVDFFKRCAKGLKPGGCIVLKDNVTNHEKRLFDDDDHSWTRTEPELLKAFADSQLDMVSKALQTGFPKEIYPVKMYALKPQHTGFTNN

Alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif.

Q9N4D9

Q5T753

LCE1E_HUMAN

Late envelope protein 5

Homo

MSCQQSQQQCQPPPKCTPKCPPKCPTPKCPPKCPPKCPPVSSCCSVSSGGCCGSSSGGSCGSSSGGCCSSGGGGCCLSHHRHHRSHRHRPQSSDCCSQPSGGSSCCGGGSGQHSGGCC

Precursors of the cornified envelope of the stratum corneum.

Q5T753

A9QCA0

CCSA_TRACE

Cytochrome c biogenesis protein CcsA

Trachelium

MKFSTLEHILIHLSFSICSIVITIRLINLVVTTILKPYDFSEKGIITTFLCLTGFLVTRWIYSGHFPLSNLYESLIFLSWSFSLIHIVAYLKKNKNLSRITASSTIFTQGFATSGLLTEINKSGILVPALQSEWLIMHVSMMILSYAALLCGSLLSAALLVITCRKKFNELLRLIESLSFDKIQYRNQRIHLFGKTYFFSVKNYYKIQLVQQLDYWSYRVISLGFIFLTMGILSGAVWANEAWGSYWSWDPKETWAFITWIIFAIYLHTRTNKNFWGANSAIVAVIGFLIIWICYFGVNLLGIGLHSYGSFKGMAS

Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment.

A9QCA0

Q6G1Z7

EFP_BARHE

Elongation factor P

Bartonella

MKINGNEIRPGNVIEHQGSLWVAVKCNAVKPGKGGAFNQVEMKNLIDGTKLNERFRAAETVERVRLEQKDFTFLYQQGDALIFMDSQSYEQLELQKDFVGERAAFLQDGMTVTVELYQEKPIGISLPDQVSVTIVEADPALKGQTVTASYKPAILENGIRILVPPFINAGERIIVDTNELIYVRRANEKDK

Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.

Q6G1Z7

P22005

PENK_MOUSE

Met-enkephalin-Arg-Phe

Mus

MARFLRLCTWLLALGSCLLATVQAECSQDCAKCSYRLVRPGDINFLACTLECEGQLPSFKIWETCKDLLQVSRPEFPWDNIDMYKDSSKQDESHLLAKKYGGFMKRYGGFMKKMDELYPMEPEEEANGGEILAKRYGGFMKKDADEGDTLANSSDLLKELLGTGDNRAKDSHQQESTNNDEDMSKRYGGFMRSLKRSPQLEDEAKELQKRYGGFMRRVGRPEWWMDYQKRYGGFLKRFAESLPSDEEGENYSKEVPEIEKRYGGFMRF

Increases glutamate release in the striatum.

P22005

B0R2R5

NIKR_HALS3

Putative nickel-responsive regulator

Halobacterium

MSVVSVSMPEELLERLDDFADDHGYTGRSEVVREASRNLLGEFEDKKLEGRELMGVVTVVFDYETTTVEEKMMHLRHEHEGLVASNFHSHVGGHHCMELFVLEGSLESISTFVGKIRATKDTLTIDYSVLPVDEFGGLADVS

Transcriptional regulator.

B0R2R5

Q8DA38

PNCB_VIBVU

Nicotinate phosphoribosyltransferase

Vibrio

MCAPLFQPAIIQSVLDLDVYKINMMQAAYRFYPQTQVRYELIVRSDDNLSDLVEEVREEINRLAELRFDAAQLAYLAEKAPYLTAEFLSYLETFRFHPQQQVSVGIFRTAQGDCQLRVTINGIWHETILYETLVMSIISELRNRRYWAQIPQSQLHKVLEDKLDFLDSELKRRNITNFRFSEMGTRRRFSFAAQKTMLDVLRARVPELLLGTSNYHLAQEFNLTPIGTVAHEWTMAHQALVAIQHSQRVALDKWLEAFNGSLGIALTDTIGIDAFLSDFDLDKATAYAGVRHDSGSPFVWGDKIIAHYESLGIDPTTKTLIFTDGLDFARALDICEYFAGRAQISFGIGTFLANDMGNWTNDKGTRYQPISMVVKMAECNGSPVAKISDEPEKAMCEDIFFLMNLKQRFGLEVDLDKAIETLKQMKRQQKKRIQSVA

Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP.

Q8DA38

P47292

TSAD_MYCGE

tRNA threonylcarbamoyladenosine biosynthesis protein TsaD

Mycoplasma

MEQPLCVLGIETTCDDTGLSIVIDQKIKSNIVISSANLHVKTGGVVPEIAARCHEQNLFKAIRDLNFEIRDLSHIAYACNPGLAGCLHVGATFARSLSFLLDKPLLPINHLYAHIFSCLIDQDLNKLQLPALGLVISGGHTAIYLVKSFYELELIAETSDDAIGEVYDKIGRAMGFDYPAGSKIDSLFNKELVKPHYFFKPSTKWTKFSYSGLKSQCLNKIKQISANKTRIDWSELASNFQATIIDHYIDHVKNAIKKFAPKMLLVGGGVSANSYLSNRISTLNLPFLIADSKYTSDNGAMIGFYASLLINGDKN

Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.

P47292

P19972

TOXK_MILFA

Salt-mediated killer toxin 1 beta chain

Millerozyma

MRKETLIGLAFITANVIAWSLRWRMQKSTTIAAIAGCSGAATFGGLAGGIVGCIAAGILAILQGFEVNWHNGGGGDRSNPVKRSSDSFSIVNHNGEKVDSYAHLVPGKVGKVIIDNIELSAIRYANNHTSLGYHFTSDGSGPAARGEATTIWGVGADEAIDKGTPSKNDLQNMSADLAKNGFKGHQGVACSTVKDGNKDVYMIKFSLAGGSNDPGGSPCSDD

This toxin kills sensitive strains of yeast.

P19972

Q4FPA9

SYI_PELUB

Isoleucyl-tRNA synthetase

Candidatus Pelagibacter

MSKENINLPKTAFSMKANLQNKEPEILEYWKKIDLYKELRKSNKGKEKFILHDGPPYANGNIHMGTALNKILKDIIVKFHQMDGKDSVYVPGWDCHGLPIEWKIEEQYKKNKKNKNEVPITEFRKECREFAEKWIEVHKTQFKRLGVVGDWENHYATMSFEAEAQIVRELGKFLKEGSLYRGFKPVLWSTVEKTALADAEVEYQDHKSDTIYTAFPVKKTNIKELENTDVIIWTTTPWTIPANKALAYNEALDYLIIELGDEGDFKNKKIVVAEALLESVIKDCEIKSYKEIKKFKGKDFKDTICSHPFLELGYDYDIPMLEARFVTTEQGTGIVHCAPSHGPDDFNLCLKYGIKAIETVDGDGKYTKNLPLFEGTHIFKANPIVIEKLKEQKKLLSNGELVHSYPHSWRSKAPLVHRATPQWFISMESHGLRKKALKALDDTKFYPDKGRERIKAMIETRPDWCVSRQRVWGVPLPIFVHKTTKEILVDDNVNENIASIYEKEGSDCWFSDSPQRFLGDKYKAEDYEKISDIVEVWFDSGCTHAFVLEKREDLQWPASMYLEGSDQHRGWFHSSLLESCGTRGRAPYESILSHGFVVDGKGLKMSKSVGNVIAPEDILKKYGADILRIWVASSNYAEDLRIDYSILEQHADSYRKIRNTFRYLLGNLNDDFQKIDLESLDIKQLPELERYMLHRVYELNNNFKNYFKSYDFHNLYKELLNFCTVDLSSFYFDIRKDALYCDSKNSDRRKSSIVVLNIILESLVKWFAPILSFTTEEIFTLINKEQKSIHLEQFMKYPESFQDEELHKKWIELKKIRDICNISIEAKRASKEIGSSLEASLIINLNKSLFEISKNVDFSEICITSSALVHQSNTDEIIIKTIKAEGNKCPVCWKINKVKCERHSD

Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).

Q4FPA9

P34619

SOR1_CAEEL

Sop-2-related protein 1

Caenorhabditis

MTINIKYSSKFSSSKTSSSEELKPKTYIPAYYQPPVSMPKYYVNWLRIKLSLNKLKNIRAIYLFDQCQNFNQYQESSRKFSAGQVSSLTPWYSNFSNYSTVILRMKDTSLPPLENPSNGGTYLFNLITVFPSIALSFNYSWRGDTGPSISIFSFSLSVLFFSLFPQHKNICARAWCRPFRRSLSFSLRFIMSSEPASSSTEKVPEEPHPHSIKHKFQGPQFVIPRALSDYVLNVNNQTPESYEKALNAKYGRDDYITLCLHVTSLCTEYGPLDDGPEYVLLCDSRARVDKLIEDLVKLLEIDTDYVQLELHGGKRLHLQKPDAVLRDIAYKQSNEGSDKFFLEMKLVPSESMKAKIMKQEEEEEKARKHGQYQQYQEYHQQHQAMNDGQSSSSVPSTSSPSCSSEANRKEMETVREPAGPSELMRAINAPVAPAPVVIKIETPVALPEEDETLMDDDEMPSLTVEAPSEEASFEAEQPSPQVPQASIEGPSQQQQIPGTSQQKRQVARGSRTNMISYHDLPPGTGNAPPMACPQVTLKLEKNVPFEAKIRAVAGYTRKPISEVQKMRPSDLESIFHSICIASVQRIKRRNELVQQLQEINAQSCKSPTMTMNKKFTLAKAYQRVQNEIEKIDREQILPQQYMNMPPMPPQGQQRLPPPAYPPGILPPQQNRQQGVPPQFQRSPQFMIGPDGQRYAHPYMQLPNSNQRARILNTSSVQPSEEVRNRLVKIEAMAMNMAQLNPPRPPPPQPPHRALQGELQFLRPGAPDPCNFRPDSKQTYNNTYVTVASPATLTNSIIPWHFPPYEKSGRLNVSNTIKAINEYRLLCNSRQADPASFLEFYFLGDPMPHFNKILSIADYNMYLSRRRCDEADVKIHRMSHSDQLQLYLLELQSDESNVEKWKTFYRIMQWDLPLNNEFPRILLPSSLDIGRPVVDRKKKSIDQVMNHIHRMHSQRPPSMGNSSTSSEASSTSPTNAATATSSPASNRPTTSTAQPPTLNPT

Acts synergistically with sop-2 to maintain the transcriptionally repressive state of homeotic genes throughout development. Not required to initiate repression, but to maintain it during later stages of development. Also required to repress expression of other genes. Binds RNA in a sequence-independent manner.

P34619

Q479B1

DADA_DECAR

D-amino acid dehydrogenase

Dechloromonas

MRVLVLGAGVVGTTSAWYLARAGHQVTVVDRQPVAGNETSFANGGQISVSHAEPWANPHVLPRVLKWLGREDAPLLWRWRADPAQLAWGLRFLGECFPGRVRRNIAAIVSMALYSRGRLQALREELGLQYDHLERGILHIYTDRDEFSAALDAARVMRQFGLDRDTVDVDKCLEIEPALSGARHLLVGGDYTRSDESGDANKFTCALAEHAKAAGVDFRYGLTVERIATSGSEIVGVLVQHSEGGPERLTADAYVVALGSYSPLLLRPIGVGLPVYPAKGYSATLTLAEASLAPTVSLTDDERKLVFSRLGNRLRIAGTAEFNGYNLELNPVRCQALIDRTRQLFPRLEIVGEPTLWCGLRPATPSNVPYIGQTRYRNLWLNTGHGTLGWTMACGSAASLAEMISGRRPEPEFPFLRC

Oxidative deamination of D-amino acids.

Q479B1

C0HJJ7

TX1A_GRAIH

GiTx1

Grammostola

SCQKWMWTCDQKRPCCEDMVCKLWCKIIK

Inhibits mammalian and insect voltage-gated sodium and potassium voltage-gated channels. Inhibits the mammalian sodium channels rNav1.2/SCN2A, rNav1.3/SCN3A, rNav1.4/SCN4A, hNav1.5/SCN5A, mNav1.6/SCN8A (IC(50)=156.39 nM), hNav1.8/SCN10A, the arachnid sodium channel VdNav (IC(50)=124.05 nM), as well as the potassium channels Kv11.1/KCNH2/ERG1 (IC(50)=3.7 uM) and rKv4.3/KCND3. In vivo, is lethal on insects (tested on flies M.domestica). When tested on mice, it shows very low toxicity, causing reversible paralyzes at the first hour after intracerebroventricular injection.

C0HJJ7

A4JCW1

ASTB_BURVG

N-succinylarginine dihydrolase

Burkholderia cepacia complex

MNAQEANFDGLVGPTHNYAGLSFGNVASLNNEKSAANPKAAAKQGLRKMKQLADLGFAQGVLPPQERPSLRLLRELGFSGKDADVIAKAAKQAPELLAAASSASAMWTANAATVSPSADTADGRVHFTPANLCSKLHRAIEHEATRRTLSTLFADPARFVVHDALTGTPALGDEGAANHTRFCAAYGKPGVEFFVYGRAEYRRGPEPKRFPARQTFEASRAVAQRHGLDETATVYAQQDPDVIDAGVFHNDVISVGNRDTLFTHERAFVNKQAVYDTLTAALDARGARLNVIEVPDAAVSVNDAVTSYLFNSQLLSRADGSQVLVVPQECRENANVAAYLDRLAAANGPIGDVLVFDLRESMKNGGGPACLRLRVVLTDAERAAVTSNVWMNDTLFASLDAWIDTHYRDRIAPEDLADPALLDESRTALDELTQILRVGSLYDFQR

Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO(2).

A4JCW1

Q0T6V4

END8_SHIF8

Endonuclease VIII

Shigella

MPEGPEIRRAADNLEAAIKGKPLTDVWFAFPQLKTYQSQLIGQHVTHVETRGKALLTHFPNGLTLYSHNQLYGVWRVVDTGEEPQTTRVLRVKLQTADKTILLYSASDIEMLRPEQLTTHPFLQRVGPDVLDPNLTPEVVKERLLSPRFRNRQFAGLLLDQAFLAGLGNYLRVEILWQVGLTGNHKAKDLNAAQLDALAHALLEIPRFSYATRGQVDENKHHGALFRFKVFHRDGELCERCGGIIEKTTLSSRPFYWCPGCQH

Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, 5,6-dihydrouracil and 5,6-dihydrothymine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.

Q0T6V4

P65259

LDH_STRP1

L-lactate dehydrogenase

Streptococcus

MTATKQHKKVILVGDGAVGSSYAFALVTQNIAQELGIIDIFKEKTQGDAEDLSHALAFTSPKKIYAADYSDCHDADLVVLTAGAPQKPGETRLDLVEKNLRINKEVVTQIVASGFKGIFLVAANPVDVLTYSTWKFSGFPKERVIGSGTSLDSARFRQALAAKIGVDARSVHAYIMGEHGDSEFAVWSHANVAGVGLYDWLQANRDIDEQGLVDLFISVRDAAYSIINKKGATFYGIAVALARITKAILDDENAVLPLSVFQEGQYEGVEDCYIGQPAIVGAYGIVRPVNIPLNDAELQKMQASANQLKAIIDEAFAKEEFASAAKN

Catalyzes the conversion of lactate to pyruvate.

P65259

Q8ZAP9

THIG_YERPE

Thiazole synthase

Yersinia

MLKIADTTFTSRLFTGTGKFSSPELMLEALRASGSQLITMAMKRVDLQSGNDAILAPLRQLGVRLLPNTSGAKTAEEAIFAARLAREALNTHWVKLEVHPDVRYLLPDPIETLKAAEVLVKEGFVVLPYCGADPVLCKRLEEVGCAAVMPLGSPIGSNLGLRTRDFLQIIIEQSKVPVVVDAGIGAPSHALEALELGADAVLVNTAIAVAHSPVQMAHAFRLAVESGERARLAGLGASPFNPSQPDTLQLRATATSPLTGFLSQLEEQDHV

Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.

Q8ZAP9

Q741V3

GLMU_MYCPA

Glucosamine-1-phosphate N-acetyltransferase

Mycobacterium avium complex (MAC)

MSSPGDTAVLVLAAGPGTRMRSDTPKVLHPLGGRSMLSHLLHAIAKVAPQHLAVVLGHDHERIAPLIADWADDLGRPIDVALQERPRGTGDAVRCGLSALPDDYAGVLVVTSGDTPLLDADTVADLIAGHTATRAAVTVLTTTLSDPSGYGRILRTQDNEVTAIVEHADATESQREIREVNAGVYAFDTAALRSALNRLSADNAQQELYLTDVIAILRGDGLPIRARHVDDSALVAGVNNRVQLAQLGAELNRRIVAAHQLAGVTVVDPATTWIDVDVTIGRDTVIHPGTQLLGRTQIGGHCVVGPDTTLTDVSVGDGASVVRTHGTGSSVGAGATVGPFAYLRPGTVLGDDGKLGAFVETKNATIGTGTKVPHLTYVGDADIGEHSNIGASSVFVNYDGESKRRTTVGSHVRTGSDTMFVAPVTVGDGAYTGAGTVVREDVPPGALAVSAGPQRNIEGWVRRKRPGSAAARAAEAAEKAAGGRPAGEAE

Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.

Q741V3

Q92445

DCOR_PARBR

Ornithine decarboxylase

Paracoccidioides

GVSFHVGSGAEDPKSFVKAVEDSRFVFDQAAEVGFDLKVLDVGGGFSEDTFERFAATLSDALDEYFPPHIRIIAEPGRI

Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis.

Q92445

A6GXP5

AROC_FLAPJ

5-enolpyruvylshikimate-3-phosphate phospholyase

Flavobacterium

MSGNSYGKIFKITTFGESHGEALGGIIDGCPPNIILDLDAIQIEMQRRKPGQSSIVTQRKEADEVQFLSGIFEGKTTGTPIGFIIKNTNQKSDDYSHIKDSYRPSHADYVYEKKYRIRDYRGGGRSSARETASRVVAGAIAKQVIPEIKINAFVSSVGDISLDKPYQDLNFSLTETNAVRCPDLASAEKMENYIKEIKKQGDTVGGTITCVIQNVPIGLGEPVFDKLHAELGKAMLSINAVKGFEYGSGFCGAKMKGSNHNDPYNQDGTTRTNLSGGIQGGISNGMDIYFRIAFKPVATLIQKQEVLTNTNEIIEQQGKGRHDPCVVPRAVPIVEAMAAIVMADFFLLNKIYNNH

Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.

A6GXP5

Q9SR62

RLPH2_ARATH

Protein RHIZOBIALE-LIKE PHOSPHATASE 2

Arabidopsis

MAQKPRTVICVGDIHGYISKLNNLWLNLQSAIDPSDFSSALVIFLGDYCDRGPETRKVIDFLISLPEKHPDQTHVFLAGNHDFAFSGFLGLLPRPSDGSDLKDTWKEYSKSEETEGWYTGEGFEDMHLQGRRWAGKIKATFNSVKGMAYKGSIYDAGSTFESYGVPHGSSDLMKAVPESHKKFLTNMVWVHEEDDVCIETEEGLKHCKLIAVHAGLEKGNNVEEQLKLLRAKDTSISKIQHLSGRKNVWDIPQELDDKHTVVVSGHHGKLHIDGMRLIIDEGGGFPDKPVAAIVLPSKKIIRDTDNLSS

Protein phosphatase that dephosphorylates specifically tyrosine-phosphorylated peptides; especially active on dual-phosphorylated substrates containing a phosphothreonine-X-phosphotyrosine motif.

Q9SR62

B1LWT3

RL16_METRJ

50S ribosomal protein L16

Methylobacterium

MLQPKKTRFRKQFKGRIHGAAKGGFELNFGQFGLKAVEPERVTARQIEAARRAITREMKRQGRVWIRVFPDVPVSSKPTEVRMGSGKGAPDYWAARVHPGRIMFEVDGVAENIAKEALRLGAAKLPIRTRVVQRIAD

Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.

B1LWT3

A8DQI9

NU4M_AVAUN

NADH dehydrogenase subunit 4

Avahi

MLKIIIPTIMLFPVTWYSNNSMIWINTTSHSLMISLMGLFLLNHPSNNSNNFSLNFFSDPLSSPLLMLTMWLLPLMIMASQYHLAKEPWFRKKSYLSMLITLQTFLIMTFMATELILFYILFEATLIPTLIIITRWGNQTERLNAGMYFLFYTLTGSLPLLVALIYLQNSMGSLNLLTINLWLKELPNSWSTNLLWMACIMAFMVKMPLYGLHLWLPKAHVEAPIAGSMVLAAVLLKLGGYGMMRITMILDPTTKSMAYPFLMLCLWGMIMTSSICLRQTDLKSLIAYSSVSHMALVIVAILVQTPLGFMGATALMIAHGLTSSMLFCLANSNYERIHSRTMLMARGLQTLLPLTATWWLLASLNNLALPPSINLIGELLVTITSFSWSNITVILIGLNMLITALYSLYMLITTQRGKLTYYLHNLNPSLTRENTLMSMHILPLLFLTLNPKIILGPTF

Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.

A8DQI9

A7MK12

MTND_CROS8

Acireductone dioxygenase (Ni(2+)-requiring)

Cronobacter

MSALTIFADNGASEPLWQSTDADAIREQLNAQGVRFERWQADRELGDNPTPETVLTAYQHAIDLLVAEKGYQSWDVISMRADNPQKEALRDKFLNEHTHGEDEVRFFVEGAGLFCLHIGDKVYQVLCEKNDLISVPAGTPHWFDMGSEPHFTAIRIFDNPEGWIANFTGSPIAEAYPRLA

Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.

A7MK12

Q9CGX1

RF2_LACLA

Peptide chain release factor 2

Lactococcus

MELSEIRNLLEGYAEKINGFRESLDLERLEEEIALLENDMAQPEFWNDQAAAQKVIDESNALKAKYDNYQAMNNMLEEAQTMLEMLQEEADEEMQAELEEMTIALGQKIESYELEIMLNQPYDHMNAVLEIHPGSGGTESQDWGSMLMRMYTRWGEAHGFKVEILDYQDGDVAGLKSVALRFVGRNAYGFLRGEKGVHRLVRISPFDSANRRHTSFTSVDVMPELDDSIEVDVRDADVKMDTFRSGGAGGQNVNKVSTGVRLTHIPTGIVVQSTMDRTQYGNRDKAMAMLKSKLYQLEMDKKQAEVDELRGDQSEISWGSQIRSYVFMPYQLVKDTRTGYETGQISNVMDGELDGFINAYLRWNL

Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.

Q9CGX1

Q8JFF3

MKRN1_SERQU

RING-type E3 ubiquitin transferase makorin-1

Seriola

MAEAAAASTAASGVIGGWTKHVTCRYFMHGLCKEGDNCRYSHDLTNSKPAAMICKFFQKGNCVFGDRCRFEHCKPAKNEELPAPQMLPLPSASLAGPSDPEPSGPTPVPGAQDWVNAAEFVPGQPYCGRAEQAKVESSVPLIEEFDSYPAPDNKQLRKQLCPYAAVGECRYGINCAYLHGDVCYMCGLQVLHPTDNNQRSEHTKACIEAHEKDMEISFAIQRSKDMMCGVCMEVVFEKANPSERRFGILSNCSHCYCLKCIRKWRSAKQFESKIIKSCPECRITSNFVIPSEYWVEDKDDKQKLIQKYKDGMGSKPCRYFDEGRGTCPFGSNCFYKHAFPDGRLEEAQPQRRQTGSNSRNRNSRRTPLWDIYDERESTDSFDNEDEEMVTFELSEMLLMLLAAGTDDEEVIIRPPSCATSSGRLDPTVTRYRKAC

E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins.

Q8JFF3

Q5FS12

MNMG_GLUOX

Glucose-inhibited division protein A

Gluconobacter

MSDFDVIVIGGGHAGCEAAAASARFGARTLLLTHRLETIGAMSCNPAIGGIGKGHLVREIDALDGLMGKAADRAGIHFKLLNRSKGPAVHGPRAQADRSLYRAAIQDLLAATPNLTILEGAAGDLIEENGRITGVICEDGREFRCGAVVLTTGTFLRGVIHVGHTQTEAGRIGEAPAKRLGERLYALGLQMGRLKTGTPPRLARDSIDWDNLPADPGDAEPEAFSPMTTAIINPQVVCRISHTTAETHRIINENLHRSAMYGGAIAGRGPRYCPSIEDKVVRFAERTSHQVFLEPEALPGNPGGDLVYPNGISTSLPADVQAAMIATMPGLENARIVTAGYAVEYDYVDPRELLPSLQLRRLPGLYLAGQINGTTGYEEAGAQGLLAGLNAARATAGNEPLTLDRSDAYLGVMIDDLTLHGISEPYRMFTSRAEYRLTLRADNADLRLTPKGIAAGCVLPEREAAFTAQKAELDAAMARAAETTFLPQTLRDVGFEVSLDGRRRTVLDVLASNGDHTKLDTLAPWFAELPLRVRRHVETEARYDGYLHRQDREIRQLASESAIALPADLDYTAIGGLSSEMRERFSQARPTSFAAAQRVRGVTPAALVALLAHVRTLS

NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.

Q5FS12

Q3MB44

RBSA_TRIV2

Ribose import ATP-binding protein RbsA

Trichormus

MTTNIKTDFSPPATATPVLEMQGIAKRFHGVPALQGVNLTIYPGEVHALMGENGAGKSTLMKILAGAYIADEGEIRINGKGVKITDPGTARQAGINLIYQELNVAPNLTVTENIFMGSELTRGQFLDRKAMELEAQQVLASLGASFAPTDIVGTLAIAEQQQVEIARALKDNSRILVMDEPTAALSDRETERLFEVIRKLRNDGIAIIYISHRMEEIYALADRISVLRDGQYIGSLTREEISPQRLVQMMVGRSMQDFYEHQRQSNPGPVVLEVRNISDGRKVQPASFQLRAGEILGLAGLVGAGRTEVSRLIFGADRKVSGEVFLNGKKLEIHSPSDAIAVGIGYVPEDRKDQGLFLEMSSRKNIGLNRLKQDANLGIVNWGSVNKIATDAVENFHIRLANLEIRAVDLSGGNQQKLLLARWLAINPRVLMLDEPTRGVDIGAKSEIYRIISDLSAQGVAILMVSSELPEIVGLSDRVLVMREGQLVGELDNSIGKEITQENIMHYATGASEVTAS

Part of the ABC transporter complex RbsABC involved in ribose import. Responsible for energy coupling to the transport system.

Q3MB44

P02454

CO1A1_RAT

Alpha-1 type I collagen

Rattus

MFSFVDLRLLLLLGATALLTHGQEDIPEVSCIHNGLRVPNGETWKPDVCLICICHNGTAVCDGVLCKEDLDCPNPQKREGECCPFCPEEYVSPDAEVIGVEGPKGDPGPQGPRGPVGPPGQDGIPGQPGLPGPPGPPGPPGPPGLGGNFASQMSYGYDEKSAGVSVPGPMGPSGPRGLPGPPGAPGPQGFQGPPGEPGEPGASGPMGPRGPPGPPGKNGDDGEAGKPGRPGERGPPGPQGARGLPGTAGLPGMKGHRGFSGLDGAKGDTGPAGPKGEPGSPGENGAPGQMGPRGLPGERGRPGPPGSAGARGNDGAVGAAGPPGPTGPTGPPGFPGAAGAKGEAGPQGARGSEGPQGVRGEPGPPGPAGAAGPAGNPGADGQPGAKGANGAPGIAGAPGFPGARGPSGPQGPSGAPGPKGNSGEPGAPGNKGDTGAKGEPGPAGVQGPPGPAGEEGKRGARGEPGPSGLPGPPGERGGPGSRGFPGADGVAGPKGPAGERGSPGPAGPKGSPGEAGRPGEAGLPGAKGLTGSPGSPGPDGKTGPPGPAGQDGRPGPAGPPGARGQAGVMGFPGPKGTAGEPGKAGERGVPGPPGAVGPAGKDGEAGAQGAPGPAGPAGERGEQGPAGSPGFQGLPGPAGPPGEAGKPGEQGVPGDLGAPGPSGARGERGFPGERGVQGPPGPAGPRGNNGAPGNDGAKGDTGAPGAPGSQGAPGLQGMPGERGAAGLPGPKGDRGDAGPKGADGSPGKDGVRGLTGPIGPPGPAGAPGDKGETGPSGPAGPTGARGAPGDRGEPGPPGPAGFAGPPGADGQPGAKGEPGDTGVKGDAGPPGPAGPAGPPGPIGNVGAPGPKGSRGAAGPPGATGFPGAAGRVGPPGPSGNAGPPGPPGPVGKEGGKGPRGETGPAGRPGEVGPPGPPGPAGEKGSPGADGPAGSPGTPGPQGIAGQRGVVGLPGQRGERGFPGLPGPSGEPGKQGPSGASGERGPPGPMGPPGLAGPPGESGREGSPGAEGSPGRDGAPGAKGDRGETGPAGPPGAPGAPGAPGPVGPAGKNGDRGETGPAGPAGPIGPAGARGPAGPQGPRGDKGETGEQGDRGIKGHRGFSGLQGPPGSPGSPGEQGPSGASGPAGPRGPPGSAGSPGKDGLNGLPGPIGPPGPRGRTGDSGPAGPPGPPGPPGPPGPPSGGYDFSFLPQPPQEKSQDGGRYYRADDANVVRDRDLEVDTTLKSLSQQIENIRSPEGSRKNPARTCRDLKMCHSDWKSGEYWIDPNQGCNLDAIKVYCNMETGQTCVFPTQPSVPQKNWYISPNPKEKKHVWFGESMTDGFQFEYGSEGSDPADVAIQLTFLRLMSTEASQNITYHCKNSVAYMDQQTGNLKKSLLLQGSNEIELRGEGNSRFTYSTLVDGCTSHTGTWGKTVIEYKTTKTSRLPIIDVAPLDIGAPDQEFGMDIGPACFV

Type I collagen is a member of group I collagen (fibrillar forming collagen).

P02454

C5DDM1

RSSA_LACTC

40S ribosomal protein S0

Lachancea

MSLPATFDLTPEDAQLLLAANVHLGSKNVQVHQEPYVFKTRPDGVNVVNVGKTWEKIVLAARIIAAIPNPEDVVAISSRTYGQRAVLKFSAHTGATAIAGRFTPGSFTNYITRSFKEPRLVIVTDPRSDAQAIKESSYVNIPVIALTDLDSPSEYVDVAIPCNNKGKHSIGLIWYLLAREVLRLRGSLVDRTQPWSIMPDLYFYRDPEEVDQQVAEEATAAADEDVKEEVAEEQTEAADWAEGNTEEVASW

Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits.

C5DDM1

Q8WYL5

SSH1_HUMAN

SSH-like protein 1

Homo

MALVTLQRSPTPSAASSSASNSELEAGSEEDRKLNLSLSESFFMVKGAALFLQQGSSPQGQRSLQHPHKHAGDLPQHLQVMINLLRCEDRIKLAVRLESAWADRVRYMVVVYSSGRQDTEENILLGVDFSSKESKSCTIGMVLRLWSDTKIHLDGDGGFSVSTAGRMHIFKPVSVQAMWSALQVLHKACEVARRHNYFPGGVALIWATYYESCISSEQSCINEWNAMQDLESTRPDSPALFVDKPTEGERTERLIKAKLRSIMMSQDLENVTSKEIRNELEKQMNCNLKELKEFIDNEMLLILGQMDKPSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNHSKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYEGILDASKQRHNKLWRQQTDSSLQQPVDDPAGPGDFLPETPDGTPESQLPFLDDAAQPGLGPPLPCCFRRLSDPLLPSPEDETGSLVHLEDPEREALLEEAAPPAEVHRPARQPQQGSGLCEKDVKKKLEFGSPKGRSGSLLQVEETEREEGLGAGRWGQLPTQLDQNLLNSENLNNNSKRSCPNGMEDDAIFGILNKVKPSYKSCADCMYPTASGAPEASRERCEDPNAPAICTQPAFLPHITSSPVAHLASRSRVPEKPASGPTEPPPFLPPAGSRRADTSGPGAGAALEPPASLLEPSRETPKVLPKSLLLKNSHCDKNPPSTEVVIKEESSPKKDMKPAKDLRLLFSNESEKPTTNSYLMQHQESIIQLQKAGLVRKHTKELERLKSVPADPAPPSRDGPASRLEASIPEESQDPAALHELGPLVMPSQAGSDEKSEAAPASLEGGSLKSPPPFFYRLDHTSSFSKDFLKTICYTPTSSSMSSNLTRSSSSDSIHSVRGKPGLVKQRTQEIETRLRLAGLTVSSPLKRSHSLAKLGSLTFSTEDLSSEADPSTVADSQDTTLSESSFLHEPQGTPRDPAATSKPSGKPAPENLKSPSWMSKS

Protein phosphatase which regulates actin filament dynamics. Dephosphorylates and activates the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly. Inhibitory phosphorylation of cofilin is mediated by LIMK1, which may also be dephosphorylated and inactivated by this protein.

Q8WYL5

A6S043

EIF3C_BOTFB

Translation initiation factor eIF3, p93 subunit homolog

Botrytis

MSRFFRGDSSSDSSSDEEEDLYSDDEEVQEQPEEESSEDDSEEDDDDDDDSDSSSDDGAGKKTGANAFLKDDSDSDSESSGDEGVKVVKSAKNKRFEELEATAKAIENGEKINDWGSISAEFDKLNRQVAKLLQSGTIPKVYIKAIADLEDFMNETLAKQKVTPKKMNATNSRGLNAVKQKIKKASKEHQKDIDSFRADKDAYMESEDEEVVAPKQKKPRSSAAQDVAADDDDEGWGTVGKGGRTLQFTPESILKHLRTILESRGKKNTDRNEQIKIMEKLYEVAATPYQRIRVLLTIISTRFDMTTGTQTFMSQEQWKAAEKEFGTLLSVLETSREYVVVETAEPWEDDEKLPTVAEGGKFAIPGSVVSYVERLDDELTRSLQHIDPHTAEYIERLSDESDLYNNIVRTMLYQEEISKDASLNEPQRSLNRVVMRRLEHVYFKPSAVIKILDENCWKAVPAELNSTITPRGSVEDAKTLVNVLCNYLYINTEGEGLTKARAMLCQIYFEALHDNYYKARDMMLMSHLQETINSFDVHSQILFNRTLVQVGLCAFRAGLVYEAQTTLQEICGSGRQKELLAQGVMIQRYNQVTPDQERLEKQRQLPFHMHINLELLECVYLTCSMLLEIPLFAQTGSSPDIKKRVISKTYRRMLEYHERQIFTGPPENTRDHVMQASKALAQGEWKRATEFIHSIKIWELMSKPEEIKAMLSAQIQEEGLRTYLFTYAPYYDTLSVSRLSSMFDLSDRKVAAIVSKMISHEELAAALDQVSSSIIFRKGVELSRLQSLALSLSDKASGLIESNERTLETRTQGTANAFERQGGRGGRGGNRGGRGGGRGGRGGISNAPRQAGGTQFTGGALGAAVGSRA

Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.

A6S043