lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Down-regulates hemolysin expression, in complex with H-NS, and can also stimulate transposition events in vivo. Modifies the set of genes regulated by H-NS; Hha and Cnu (YdgT) increase the number of genes DNA bound by H-NS/StpA and may also modulate the oligomerization of the H-NS/StpA-complex. Binds DNA and influences DNA topology in response to environmental stimuli. Decreases biofilm formation (By similarity).
Sequence:
MSEKPLTKTDYLMRLRRCQTIDTLERVIEKNKYELSDNELAVFYSAADHRLAELTMNKLYDKIPSSVWKFIR
The following text describes a protein:
Function:
Probable transcription factor (By similarity). Promotes slightly the tolerance to cadmium (Cd) and to oxidizing chemicals (e.g. diamide).
Subcellular Localization:
Nucleus.
Sequence:
MEVMVGSSFGIGMAAYVRDHRGVSAQDKAVQTALFLADESGRGGSQIGIGLRMSNNNNKSPEESSDSSSSIGESSENEEEEEEDDAVSCQRGTLDSFSSSLEDSLPIKRGLSNHYVGKSKSFGNLMEAASKAKDLEKVENPFNKRRRLVIANKLRRRGRSMSASNFYSWQNPNSMPLLALQEPNEEDHHIHNDDYEDDDGDGDDHRKIMMMMKNKKELMAQTRSCFCLSSLQEEDDGDGDDDEDE
The following text describes a protein:
Function:
May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity.
Subcellular Localization:
Cell membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein.
Sequence:
MAKPLLSASSTSVMAREIPSEFGLDMDMRDPNSINEHTKVLFDDVFAEPEGTHSADGVWRWSFKCYNGSKSCCYKTLTYICALPIACCWGCEFACLSFCQIWAMVPCIKTCNITLASVKQVWSSLVRTCLDPCNESCALCLSNIRITQQSA
The following text describes a protein:
Function:
Activation of anaerobic ribonucleoside-triphosphate reductase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine.
Subcellular Localization:
Cytoplasm.
Sequence:
MNYHQYYPVDIVNGPGTRCTLFVSGCVHECPGCYNKSTWRVNSGQPFTKAMEDQIINDLNDTRIKRQGISLSGGDPLHPQNVPDILKLVQRIRAECPGKDIWVWTGYKLDELNAAQMQVVDLINVLVDGKFVQDLKDPSLIWRGSSNQVVHHLR
The following text describes a protein:
Function:
Chemokine, which displays chemotactic activity for T lymphocytes, preferentially Th2 cells, but not monocytes or granulocytes. Therefore plays an important role in a wide range of inflammatory and immunological processes. Acts by binding to CCR4 at T-cell surface. Mediates GM-CSF/CSF2-driven pain and inflammation. In the brain, required to maintain the typical, highly branched morphology of hippocampal microglia under homeostatic conditions. May be important for the appropriate adaptation of microglial morphology and synaptic plasticity to acute lipopolysaccharide (LPS)-induced neuroinflammation. Plays a role in wound healing, mainly by inducing fibroblast migration into the wound.
Subcellular Localization:
Secreted.
Sequence:
MASQAAVLLALSLLLLWTSPALGGANDAEDCCLSVTQRPIPGNIVRAFHYLLIKDGCRLPAVVFTTLKGRQLCAPPDQPWVDRIIRRLQKNSAKASPALPSPAFSLRAPAQDPNP
The following text describes a protein:
Function:
Necessary for normal cell division and for the maintenance of normal septation.
Sequence:
MKVTKADIVISAVKPEQYPDSDLPEIALAGRSNVGKSSFINKILNRKKLVRISSKPGKTQTLNFFLINEMMHFVDVPGYGYAKVSKSERAAWGKMIETYFTTREQLDAAVLVVDLRHQPTSDDVMMYDFLKHYEIPTIIIATKADKIPKGKWQKHLKVVKETLAVEIGDEIVLFSSETGLGKEEAWKAIHKFTKTKNA
The following text describes a protein:
Function:
Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase.
Subcellular Localization:
Plastid, chloroplast thylakoid membrane; Peripheral membrane protein.
Sequence:
MAMTSAATGFILTANVPAAIGGGSSKSTTIVSFLPMRSFGSRLVVRAAEDTPPATASSDSSSTTAAAAPAKVPAAKAKPPPIGPKRGSKVKILRKESYWYKNVGSVVAVDQDPKTRYPVVVRFAKVNYANISTNNYALDEVEEVK
The following text describes a protein:
Function:
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Subcellular Localization:
Cytoplasm.
Sequence:
MNELIEKAKVLQEALPYIREFHGKVFVIKYGGSAMHDEELRESFARDVVLLKYVGINPVIVHGGGPQISKTLEKFGIKPKFVGGMRKTDEETMHVVEMVLSGDINKDIVALINRYSGEKIYAVGLSGRDGRLLKAKKLDKERYFSELGLPVPEEDIGFVGEIVDVNEELIFTLLSHNFIPVIAPVGVGEEGEAYNVNADLAASEIAGEIKAEKLIYLTDTKGVLDEKGELISSLSKDKAEELIKKGVIREGMIPKVRSALRALEKGVKKVHIIDGRVKHSILLEVFTKEGVGTEITLE
The following text describes a protein:
Function:
May function as a cell-type specific modulator for G protein-mediated cell signaling.
Sequence:
MFIKSQPGASPSATYVGQTTAGSPDQEGFFNLLSHVQGDRMEEQRCSLQAGPSQTSESQSGPPPEMDSLMDMLASTQGRRMDDQRVTVSALPGFQPVGPKDGVQKRAGTLSPQPLLTPQDPSALSFRRNSSPQPQTQAP
The following text describes a protein:
Function:
Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Sequence:
MAPSQEQSKEQIQSQTSKDQQPTKSDKSKVQKEEELSEEDQHLKDELELLVERLNEPNQDRALYNKYLDALKTFIKESTTSMTAVPKPLKFLRPHYPSLTELYTNWSNQFSAKDVIVIKLADILSVLATTYSDEGNRDSLKYRLLASDDTISDWGHEYMRHLALEIGESFQENLGVDEELVNKLVKLALQIVPFFLKHNAEADAVDLLLEIECIDKLPQFVDENTFARVCLYVTSCVPYLAPPDDVSFLNTAYSIYLSHNQLTQALTLAIKLDDNELIKQVFDSTTDESLHKQLGFILSQQNSNFKYPGENPEVQECISNVKLAEYFQYLVKELNLLDPKVPEDVYKSHLENSKFGLGTSGSIDSAKQNLAASFVNGFLNLGFGNDKLVQTEEDNKSWIYRTKGSGMASTTASLGSIHQWNINEGLQVLDKYTYSEDSEVKAGALLGTGVVSANVHDEVDAAFALLQEYVHEPNKLYQTAAINGLGIAFAGSANEDVLNLLLPLVSDLDISLEISCLAALALGHIFVGTCHGDVTSTILQTLLERDYTQLTNKFIKFMSLGLGLLYMGRTEQAEDVLETIDAIEHPISKTLKVLVNICAFAGTGNVLQIQALLQMCTAKPKDQLEEEKKLEQSEEEQQQQQQNKDTKSNGEGGEEEEDVEMEDAESKNETSENTTASATSTTSSSKEKGDSSSSAAAAAAGDEKAQEGGDDKEDEEEIDEEEELYQGIAVLGLACIAMGEDIGQDMSLRHFGHLMHYGNSLIRRAVPLAMGLVSTSNPQMKVFETLSRYSHDPDLEVAQNSIYSMGLVGAGTNNARLAQLLRQLASYYIKSPDTLFMVRIAQGILHLGKGTLTLTPYNSERTILSKVSLASLLTIAIALLDPRSFILNDSTTETTHQLLYYLTPAVKPRMLVTVDEELKPIKVNVRVGQAVDVVGQAGKPKTITGWVTQSTPVLLNYGERAELENTDEWISLSSSLEGVVILKKNPEYMEIDS
The following text describes a protein:
Function:
Probable RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase that regulates RNA polymerase II transcription. May have functional redundancy with RTR1.
Miscellaneous:
MISCELLANEOUS: Present with 1050 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MQIITTTFIQKVILGSHQLHEQLSIVEARMIESAIVSMLTESFCENEQTLKYLARLLSPMSYMDVINARRGKKICGYPLCYKSAAENSSDGFFIHSMYCNNYHSKCSLYLMRQLSQTPLHERRGVHLTSYINLEFDDMYSVSLLEELVGSEVPIDTVKSLITSFKDLEFDDTYKNEPLPLDVYFGQLTTDEETCIE
The following text describes a protein:
Function:
Antitoxin component of a type II toxin-antitoxin (TA) system.
Sequence:
MIRQKRIFRLGDHRRLASTCNSYSRWPFDAKSCSPQGYTRYLYSAPVQQVETMTLETTYTQARANFAQLCDEVIANRTAVIITRRGGANVALIAADELASLVETAHLLRSPRNAQRLLEALQEADAGSVKPQTVEQLQRELGFGEET
The following text describes a protein:
Function:
One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Subcellular Localization:
Cell junction, gap junction. Cell membrane; Multi-pass membrane protein.
Sequence:
VMSWKYLDDVLLRLSKNSTLLGKYWIATVLLLRLVVLTVFGESVWSDEQREFTCNTKQPGCENVCFNTFAPVSNVRMWGLQILAVSVPGALYFVYVMHVVSVSNENDKVKTSDLSTAANERVRTANKRWKVLTNHVIPSELHKTRGQCIWRLYLLQIFSRMLIECVFIMLQYTVYFYRWTVPQVFRCQVWPCPHTVDCFISRPQEKTVFFRYMYVISAFSILLSIGELLYIGW
The following text describes a protein:
Function:
Involved in sequestration of excess metal in the cytoplasm into vacuoles to maintain metal homeostasis.
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein.
Sequence:
MGFRFFRLNPISNPYLSRISSITHKNSIFTHQNPSKITSLTTQLQQFNDPSYVTINPPNFQTFKRWHFGHSHHHHQGPHQDSSKKSEDIFRLGLAADIGLTAGKAVTGYLSGSTAIIADAAHSLSDVVLSSVALLSFKAARVPRDKEHPYGHGKFETLGALGISGMLIVTAGGIAWHAADILLAWFTAAPEVASHSLMHEHGNHSGQSGHDHKIDMQHPILALNMVILSIAVKEGLFRITKRAGEKEGSGLMKANAWHHRADAISSFVALIGVGGSIVGVKILDPLAGLLVSGMILKAGLETGYQSVLELVDAAIPQQQLDPHRKTILQVEGVKGCHRLRGRRAGSFLHLDVHIEVDPFTSVSAAHHIGENVRHRIHESHPEVVEVFIHIDPSISQISPELDVKDDLNDSEENYDISLKDEEFDNIISDIFSSHFPKKVKLEHITPHLLQNKIMLDVEVSMPPDIMIRDAMMMAEEVEKEILKTVSDVIQVHVQLRLSSANHTIPS
The following text describes a protein:
Function:
Unusual broad substrate spectrum amino acid:sodium cotransporter that promotes absorption of the D isomers of essential amino acids. Neutral amino acids are the preferred substrates, especially methionine and phenylalanine.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MQNGGGAFLIPYLIMLLLVGRPLYYLEMVMGQFASRGCIKVFDVAPLMRGVGVGQTLALLLILGYYAAVLSVSVRYFVASFGSPLAWARCEPDWSGCVDSEFKGRVQNASLRPSAEYYFNRTVLHNFWTVEDGIGVPDWKLAVCLLFCWMCITGILIKGIRSSGKASYFLAIFPYVILLVLLVRTCTLEGADQGILYLMKPQWEKLIDVQVWYAAVTQCFFSLTISLGSVIVFASYNSFTNNIYRDAMIISWLDTFTSIVSGIVVFGIVGNIAHITGNRVEDMQLQGPQLTFITYPDAIAKFDAAQNVFAVLFFLMFFLLGLGSNTGIVTTIVTAVRDRFPELPNWKVVISIAIYGFCCGLVYITPGGLHVLDVVDKYGVTLTTLTLVMLEIVTFCWMYGVEQIGHDIQLMLSRRTGVFWRVCWSFVTFGIIAVIWVFSFIQYTPLPVPLGMTVFGWCLYAFVISQVAIWAVYALCERKEEKLLDRIKAACQPTSDWGPEDSTVRSQYQAERSKRSEENRAQSVGVGKCVLRKMCNTFVQK
The following text describes a protein:
Function:
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with NCS6 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation.
Subcellular Localization:
Cytoplasm.
Sequence:
MSAESTCRRCDGPTAIKTRQANFCQPCFITFIQQKQRKAMEGCKVLFARPGCVLPPAINILVPISFGQSSLALLDMAHAQLEEQAKTYENAAGFTLNAVFIDCSEADPLEKEPNQIISELEKRFAHAKFTCIPLSKAFEGASSVTLKHNRDYTSFVSGISEEPTSVQQLLSCIGTKSAREDIISVLQRHLIIEEAKKQNESLPTTVAWGHNATRLAELTLSLTIKGRGNRIHAQVLEHKNPKDSISGLPEIHPLNDVLSYEIPFYNSFRNVSDLAVDTVSKPSQVTKNLSIDQLMHQYFENIQTNFPSIASTVVRTAAKLDDPNAAKQGLTPCLICASPVDPNQSLAWLTNITVNEPAAPETEEEEELSKKAHMEKSQEKTGDADRHLPVPNLCYGCIITIRDTDSFTFPKRASKQDILDEFTL
The following text describes a protein:
Function:
Converts sphingomyelin to ceramide.
Subcellular Localization:
Secreted.
Sequence:
MQTSILLILLFNVLFVFCRNHQHTEIPQIISHGVQTLQTTQTLPHSLTSAVKNLTKIPDPKLANDIFCQSCELVFNQIIEYRRGGANKDSMISYFQKLCRLFTDWGPVACDGYINIEIDTVLYIIDNKKDLTGFRICAIAFQQKTCKDPNLKKWSVAIPPQPQPGNPPKIHHNHATPLKLLHLTDFHYDPLYQAGSNAACDLPLCCQQSNGPPVKPPNAAGFWGDYRVCDTPWYSITNLTAHLTQNHATFDLVYYTGDIISHRSWATTKDHNVEAVQKIFKLFKDTFNATPVYPILGNHEPHPTDFYSPDGVSPKISTQWVFDLMAAEWARWLPNDTSATIKAGGYYTVLVKPKFRIVALNSNVCFISNLWLLYDDNDPYDQLKWLVQVLTEAEKNGEKVHILSHIPPGEILCLQRWSNQFHKIVNRFAPIIVGQFNGHTHLDELRLFRDTNNTRKIVNVAYNAGSFTTFVGYNPNYRTYEIDQNDYSVLDYDHYTFNLTKANQDRNKTPDWFKLYSFKEAYGLKNTSYASLADMLDRMAKNHTMMQQYFRA
The following text describes a protein:
Function:
Controls stomatal patterning.
Subcellular Localization:
Secreted.
Sequence:
MEWKRYRKLNLSLSHKSHFLYCFSLFFFSVCALFSITSTATTCQQDIRCSLTGQADSICFQEIAEKRKHEDKMGSLDIQGLPLTLARRFLSGPGSSPPRCTSKCGNCTPCKPVHVPVPPGTPVTAEYYPEAWRCKCGNKLYMP
The following text describes a protein:
Function:
Induces RNA cleavage activity in the RNA polymerase. In its presence, the cleavage activity of the RNA polymerase truncates the RNA back to position +15 in a stepwise manner by releasing mainly dinucleotides from the 3'-end of the nascent RNA. The truncated RNAs are able to continue elongation. Involved in transcriptional proofreading and fidelity. Misincorporation of nucleotides during elongation of transcription leads to arrested elongation complexes which are rescued by TFS-promoted removal of a dinucleotide from the 3'-end. TFS is able to induce a cleavage resynthesis cycle in stalled elongation complexes (resulting from the next missing nucleotide or a reduced incorporation rate of a wrong nucleotide) preventing misincorporation and enabling proofreading in a post-incorporation manner. Pausing of elongation complexes is the main determinant of TFS-induced RNA cleavage.
Sequence:
MVKFCPKCNNLMLPKDGKLKCAVCGYEEETTAEGSKEYEYKEHLENKKEKITVIESEGLETLPTTRIECPKCGHNEAYWWLQQTRCADEPETRFYKCKKCGHTWREYD
The following text describes a protein:
Function:
Involved in DNA repair and RecF pathway recombination.
Sequence:
MSGNSPGALKKIRGIVLESKTIQEGDALIRLLPEAGSVENFRIRGIRKSKTRPIASVEPGSLSDVDYYHSKNKETHNVKEISLINRFDRAKSGYLGTVLVSYLVELASSFTPDGAEHPGEFRLLFGALEELEENGISILILPFFKLRLLVSGGFLSKELICHSCGAELKEMTFVTLQTTPLELICGNCLYGDRNDLGCVQWIQTFLMLRFRDLKEREISVENILDLDRICNQMLEPILRKKLKSAPTLYEALGENLGKFS
The following text describes a protein:
Function:
Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde.
Miscellaneous:
MISCELLANEOUS: The active site is at the interface between 2 subunits. The proton acceptor Cys is on one subunit, and the charge relay system is on the other subunit (By similarity).
Sequence:
MFKISKEFSFDMAHLLDGHDGKCQNLHGHTYKLQVEISGDLYKSGAKKAMVIDFSDLKSIVKKVILDPMDHAFIYDQTNERESQIATLLQKLNSKTFGVPFRTTAEEIARFIFNRLKHDEQLSISSIRLWETPTSFCEYQE
The following text describes a protein:
Function:
Growth factor involved in osteogenesis and adipogenesis. Plays an inhibitory role in the process of osteoblast differentiation via SMAD2/3 pathway. Plays an inhibitory role in the process of adipogenesis.
Miscellaneous:
MISCELLANEOUS: 3T3-L1 cells endogenously secrete biologically active Gdf10 as a unique complex that contains both the pro-region and the mature region.
Subcellular Localization:
Secreted.
Sequence:
MAPGPARISLGSQLLPMVPLLLLLRGAGCGHRGPSWSSLPSAAAGLQGDRDSQQSPGDAAAALGPGAQDMVAIHMLRLYEKYNRRGAPPGGGNTVRSFRARLEMIDQKPVYFFNLTSMQDSEMILTAAFHFYSEPPRWPRAREVFCKPRAKNASCRLLTPGLPARLHLIFRSLSQNTATQGLLRGAMALTPPPRGLWQAKDISSIIKAARRDGELLLSAQLDTGEKDPGVPRPSSHMPYILVYANDLAISEPNSVAVSLQRYDPFPAGDFEPGAAPNSSADPRVRRAAQVSKPLQDNELPGLDERPAPALHAQNFHKHEFWSSPFRALKPRTGRKDRKKKDQDTFTAASSQVLDFDEKTMQKARRRQWDEPRVCSRRYLKVDFADIGWNEWIISPKSFDAYYCAGACEFPMPKIVRPSNHATIQSIVRAVGIVPGIPEPCCVPDKMNSLGVLFLDENRNAVLKVYPNMSVETCACR
The following text describes a protein:
Function:
Involved in the biosynthesis of carotenoids. Catalyzes the condensation of two molecules of geranylgeranyl diphosphate (GGPP) to give prephytoene diphosphate (PPPP) and the subsequent rearrangement of the cyclopropylcarbinyl intermediate to yield phytoene (By similarity).
Sequence:
MTEIEQAYRITESITRTAARNFYYGIRLLPREKRAALSAVYALGRRIDDVADGELAPETKITELDAIRKSLDNIDDSSDPVLVALADAARRFPVPIAMFAELIDGARMEIDWTGCRDFDELIVYCRRGAGTIGKLCLSIFGPVSTATSRYAEQLGIALQQTNILRDVREDFLNGRIYLPRDELDRLGVRLRLDDTGALDDPDGRLAALLRFSADRAADWYSLGLRLIPHLDRRSAACCAAMSGIYRRQLALIRASPAVVYDRRISLSGLKKAQVAAAALASSVTCGPAHGPLPADLGSHPSH
The following text describes a protein:
Function:
SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. SNAP29 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane. Also plays a role in ciliogenesis by regulating membrane fusions.
Subcellular Localization:
Cell projection, cilium membrane; Peripheral membrane protein. Cytoplasmic vesicle, autophagosome membrane; Peripheral membrane protein.
Sequence:
MAYGGGTFDKTNPFADDDDDLNGEDGDDGGWDLMRDELATRQGNISRSTQRCLGAIAESERVGVATAEELLHQREQLERTEKNLDKINKDLDVSQRHITSIKSMWGGVINFFKKKPEEPPPVAAEQETKVQAAPKLRQAMEVSQNQPRPAGEHPALQLRDESRYARGSSQSFQKWNAEFEDGLDDMSTGLGTLKSLALGLNEEITEQNAMLDRLGDKTDKSEFRIHGTNKEMRNMLK
The following text describes a protein:
Function:
Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular Localization:
Cell membrane; Lipid-anchor; Cytoplasmic side.
Sequence:
MSSSSNVVAMRKVVQQLRLEAGLHRVKVSQAAADLKQFCLQNAQNDPLLTGVSSSTNPFRPQKVCSFL
The following text describes a protein:
Function:
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MKYLLVLLIFLLDRITKELAERGYFSRLNIDFFLNFYLTHNYGVAFGIDIARKIILIFNFLALIVLVLLYRKFGFIGLAFILGGLLGNLYDRVFYGYVIDFIHLRNFFVFNLADLFISLGGVLVFFKLIK
The following text describes a protein:
Function:
Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MPWHQEQCSGLWRSEDMIRVNIILQREVLHDTMYEVGMLGCVQFLDMNEGVTAFARPFTEELRRCEELQRKLHFIEESMCKDADLLERYPEDVHMSATVEEMRSSLLRGQMHMIDDRIESTVNELTAMLTSLEGFQHEMNQNQEMALLYYKYRLLVETPCDMAASNSSYAHHGAAVSSEAFSRLASLFGFIDSKLSEELYRLCYRITRGNAIVEISNEPAMFVDVQTGERNVAKTSFMVLCASPTMITRLKKLMIGLGADVYTLDEVQSRGIELTTSTTAHHVEDTIEGVERRKRDVLTLWYEEHRLYKTYLKVEKVVLTAMNTCAMSGSTCTASAWVPLRHEQSLRRALQDAVASANGSVESIVTLHAEQKHPPTFFETNRFTESFQGIVDSYGMARYKEVNPGVFTIITFPYLFGIMYGDIGHGFLLLFIALFFISKEKAWRTAQLNEIVAMAFGGRYLLLLMSLFAIYMGVLYNDFFGFSLNLFSSGYTWAPISEQKGTTYPTTPNGLPSVKPPRVYAMGLDAAWAETDNKLEFYNSVKMKHAVIVGVAQMFAGLFLSLNNSIYEKNWYKIAFLFVPEFVFLLCTFGYMSILIMVKWCRTWENTNKAPSILEIMTNFFLQPGSVPNPLFGGQAGLQVFLLLAAFAMVPFMLLGMPYIEMRDYKRWQRRRQVWGSRRRHGRALRTSVVTIENSDYTDAFLNEPSASLQHRQTSDSGDESAHRNLMSDDDETANIFGDDNMHPFGVPAASSEEGSTATVIERENEKFEHFDVSELIIHYVIHTIEYVLSSVSNTASYLRLWALSLAHSQLSEVFFSFTVAKTLDIDNSSGFVIAIGVLLWIGTTLGVLVGMEALSAFLHALRLHWVEFQNKFYAGDGRAFDPLDLTNLNTAN
The following text describes a protein:
Function:
Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the first dolichyl beta-D-mannosyl phosphate derived mannose in an alpha-1,3 linkage to Man(5)GlcNAc(2)-PP-dolichol to produce Man(6)GlcNAc(2)-PP-dolichol.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MSSVSSMAWLRRVCLDDYGYNFALPALTIVSAVLSEAVIRRVSFTEIDFQTYLGQAALYLDGERDYSNLDPPGGSGPCVYPAAHIYLYSFFHWLTHAGGNILPAQHVFAATLTANNLLVAMLYRQAGMPPLAVLPLILSKRIYSIFLLRMFNDPIAVLFVYLALFAATNSRWKLSALLFSFGLGIKMNVLLFLPGFAAAAFVYTGIRGAISYIAVVIVVQALLSAPFTLHDPHAYLTRAFDFSRSFLHVWTVNWRFVPEDTFLSQHFACGLLSLHIVLLTLFGLFRWTGIASHGPKWILQNLSARSHKLVQSEKTALMCCAFTSNTIGILCSRSLHYQFYSWYFHQVPLLLWLSQLPNIVKLILPVVLEWCWNVFPSTDTSSLLLLACHVVLVLGCFTMPGLVTAKRPLSSIAQDDDGAEVEALLLTDDLRLSKPSEPDSKTASTSNDPADVREEALLRLAQARKAKAAKEAKLRDAFRRRIATRRRVLALLGKLLLLLRPILVLASIVLILVLPHPQSPVSKGTYVDENALQPGQARVYWDYFDVTYADMLSEKVSFLKDASSAERADFVFRELQSYGLEVNRQHYKYDSIPLHHGSALSGINVYARSATPRIDGREAIILTASWRSRWQGADDPFPPAENLDETVSIDQRGRINVRGVASILALARYLTTQAHLSKDLIFVISDGHLEGIHAWSSAYFGSKSEGLQVDPVSAGGSQVWNAISIDYPSDSFSSLEVQYEGFDGQLPNMDVVNTIVRIADTVTGGMPLTFGLRSAPLHLKEPVQRLAQKWGIRLRSDVEYELGNYENGVRAALRQVGFGVTGRASGPHGFFQRHHVDAITLYAVPATGPYGFFHMGRLVESFVRSMSNLLERLHHSQFFYLLLNPRRFVPIGTAILVPLLLSISLTISGLALWFAEEKVSKQEREAIFSGLDPSAGDDGDMQPETPTMSWYRNQIVQNHFTAVEGEDAADRKTNEYGVALRESMRPIATTLACVGLTVLAGVGVLLRNDLLFAEMSGGLTKRGKQLGAARVVIMLLPIAGAVLLRSRCGIKRAHRIGSLLIAFAYLQAGMLVAVLSVLNFALAAFLALLTYSALRIASGRPSSSPLTEAVPAHSWVNFIRGLAVMVFSPVFWAALLLQFLRRETLQHEVSALVLHWKLYNAATVPILCVAYLPIVLQAQLGAFLRV
The following text describes a protein:
Function:
Involved in mitochondrial fission. Acts as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity).
Subcellular Localization:
Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MSDVTHFSKVVAATASTLVSGDLSQSHVMRDISRPAFQKRIFSFSKRPSELVRITSSSKDVLLPDEMLVDIPSNENQFSLFQGFQATLPEHSVGSQLLLGDGSKVGEKSAREQLVEGKKSLSHKLDLLEVRKALAANEITEIDARVAHLQSMRQIVFDRVASLEQQEFQLESEVLRIDAELEQMEEEKEEVIQRHDYETRTPEELEDDVVDLKSVSEKLQSASQKTLPRRNLSRRKTQPTLQQYYEPGNKIRQIKAHSDSVTCLDFDIPFGTMVSAGMDLGLKVWDLSRGDLVTDLKGHNASVTCLQVDNNVLATGSADATIRVWNLDQVVSNPDAQDEGDDAYTIHVLDSHVGEISAIHFSDHTLVSGSADKTIRQWDLNTGRCVQTLDVIWANSAQNALYSNDRLRTGFDANAPFIGAVQCRDAALATGTADGIVRLWDLRSGQVQRTLQGHTAAVTCLQFDDVHLATGSRDRSVRIWDLRMGNIFDAFAYDSPITSLDFDNRRIASTNGENTVKIYDRAAEKHWSLGRGEGDPEAPESTVVKTKEGYLVEGGGDGVVGVWAC
The following text describes a protein:
Function:
The two proteins produced are among the major shell proteins of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. Required for structural integrity of BMCs and to mitigate propionaldehyde toxicity. The N-terminal 13 residues are important for correct assembly of the BMC shell. The isolated BMC shell component protein ratio for J:A:B':B:K:T:U is approximately 15:10:7:6:1:1:2. The N-terminus of the long form (PduB) is required for correct formation of BMCs, deletions in the first 37 residues have substantially reduced levels of the major lumen enzymes. May play a major role in binding the enzyme contents to the shell; The 1,2-PD-specific bacterial microcompartment (BMC) concentrates low levels of 1,2-PD catabolic enzymes, concentrates volatile reaction intermediates thus enhancing pathway flux and keeps the level of toxic, mutagenic propionaldehyde low.
Miscellaneous:
MISCELLANEOUS: Bacterial microcompartments (BMC) 100-200 nm in cross section are formed during aerobic growth on minimal 1,2-PD-B12 or anaerobic growth on 1,2-PD-tetrathionate medium, but not during aerobic growth on glucose, anerobic growth on glucose or pyruvate-tetrathionate. BMCs can constitute up to 10% of total cell protein.
Subcellular Localization:
Bacterial microcompartment.
Domain:
A probable alpha helix (residues 6-18) probably binds to cargo enzymes, attaching them to the shell; Has 2 BMC domains which can evolve independently of each other.
Sequence:
MSSNELVEQIMAQVIARVATPEQQAIPGQPQPIRETAMAEKSCSLTEFVGTAIGDTLGLVIANVDTALLDAMKLEKRYRSIGILGARTGAGPHIMAADEAVKATNTEVVSIELPRDTKGGAGHGSLIILGGNDVSDVKRGIEVALKELDRTFGDVYGNEAGHIELQYTARASYALEKAFGAPIGRACGIIVGAPASVGVLMADTALKSANVEVVAYSSPAHGTSFSNEAILVISGDSGAVRQAVTSAREIGKTVLATLGSEPKNDRPSYI
The following text describes a protein:
Function:
Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation.
Subcellular Localization:
Periplasm. Note=Is capable of associating with the outer membrane.
Domain:
The PPIase activity resides only in the second parvulin domain. The N-terminal region and the C-terminal tail are necessary and sufficient for the chaperone activity of SurA. The PPIase activity is dispensable for SurA to function as a chaperone. The N-terminal region and the C-terminal tail are also required for porin recognition.
Sequence:
MGAALLCSFAHAEVVPLDRVVAIVDNDVIMQSQLDQRLREVHQTLLKRGAPLPPEHVLTQQVLERLIIENIQQQIGDRSGIRISDEELNQAMGTIAQRNGMSLEQFQTALTRDGLSYADAREQVRREMVISRVRQRRVAERIQVSEQEVKNFLASDMGKIQLSEEYRLANILIPVPEAASSDVIQAAARQAQELYQQLKQGADFGQLAISRSAGDNALEGGEIGWRKAAQLPQPFDSMIGSLAVGDVTEPVRTPGGFIILKLEEKRGGSKMVRDEVHVRHILLKPSEIRSEAETEKLAQKLYERIQSGEDFGELAKSFSEDPGSALNGGDLNWIDPEALVPEFRQVMNDTPQGELSKPFRSQFGWHILQVLGRRATDSSEKFREQQAVSVLRNRKYDEELQAWLRQIRDEAYVEIKQ
The following text describes a protein:
Function:
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in chloroplasts and mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Subcellular Localization:
Mitochondrion. Plastid, chloroplast.
Sequence:
MAVGSCESIVLLYSQPRIPRSALQIRCSSSLASKQASSSSKIPSALQDFEAVIGVETHVQLGTATKAFCGCLSQYGAQPNSNVCPVCMGLPGALPVLNERVVDFAVKLGLALNCDLSLRSKFDRKQYFYADLPKGYQISQFDIPIARHGSIEVDLPVEYGGGHRKFGITRVHIEEDAGKLVHAGGGGRLSGSPYSLVTFFFSSCCFSLLVFVDLNRAGVPLLEIVSEPDMRTGIEAAEYAAEVARVVKCLGIGSGSMAEGSLRCDVNVSVRPRGQAAFGTKVEIKNMNSCAAMHRAIDFEILRQVALHKEGLESKIVQETRLWEEGSQRTVTMRAKEGLADYRYFPEPDLLELVLKQEQVDSINEALPELPNETRRRYEALGLSMQDVLVLADDKSVSEYFDSTLEQGADMKMAANWIMGDITAYLKTEKLSISDVKISPSVLAELVSLIKDGTISGKIGKEISDEAEIASLVDKVLLENPKQLEAFKKGKTKLQGFFEGQVMRSTNGRVNPILMKKVVAQKLGLS