lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Promotes the formation of magnetite in Fe(2+)-rich conditions, when magnetite is not readily formed. Binds Fe(3+) and Fe(2+) (Probable). May play a role in nucleation of magnetite crystal formation (Probable). May help control production of crystals with a specific morphology (Probable). Greatly improves the formation of magnetosome-like magnetite crystals in vitro. Isolated short protein, probably residues 75-133, binds up to 18 Fe(3+) per monomer and self-assembles into micelles about 21-26 nm in diameter; the C-terminal 21 residues also self-assemble.
Miscellaneous:
MISCELLANEOUS: This bacteria makes up to 20 cubo-octahedral magnetosomes of about 45 nm in diameter which contain membrane-bound crystals of magnetite (Fe(3)O(4)).
Subcellular Localization:
Magnetosome membrane; Single-pass membrane protein. Note=Tightly associated with magnetite crystals. Tagged protein forms straight lines with a punctate pattern extending along most of the cell associated with its inner curvature, in the correct position to be associated with magnetosomes. Under aerobic conditions, when magnetites cannot form, or in the absence of iron, the protein is dispersed in the cell, probably in the inner membrane; as magnetosomes form tagged Mms6 localizes in a line that corresponds to the position of magnetite crystals. Short protein seems to localize specifically to magnetosomes which have magnetite crystals (Probable).
Domain:
Fe(3+) binding by the shorter form (residues 75-133) is inhibited by Ca(2+) and Mg(2+). The C-terminal 21 residues (magnetite-interacting component, MIC, residues 112-133) self assemble into multimers up to octamers; this fragment binds Fe(3+) which alters its structure. Another paper showed binding of MIC to Fe(2+) via Asp-123, Glu-124, Glu-125, and Glu-127 with a minor contribution from Glu-118. The isolated lumenal MIC binds Fe(2+) and Ni(2+), Ni(2+)-binding may not be physiological; in this paper binding to Fe(3+) was poor. Although it binds iron the protein fragment has no effect on magnetite crystal formation in an iron co-precipitation experiment, however mutating some of its residues decreases crystal size. Correct subcellular location to the magnetosomes requires the N-terminal 75 residues.
Sequence:
MGEMEREGAAAKAGAAKTGAAKTGTVAKTGIAAKTGVATAVAAPAAPANVAAAQGAGTKVALGAGKAAAGAKVVGGTIWTGKGLGLGLGLGLGAWGPIILGVVGAGAVYAYMKSRDIESAQSDEEVELRDALA
The following text describes a protein:
Function:
Probable serine protease that plays a role in hearing. Acts as a permissive factor for cochlear hair cell survival and activation at the onset of hearing and is required for saccular hair cell survival. Activates ENaC (in vitro).
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Sequence:
MQAVGPKPLPTLLCGGRTENRMAWILSFLIRSCPCEPGKVCVYAKLVILLPTISSVVPSTFLGLGNYEIEVEVEPEVRGPEIVTMGENDPPAAEAPFSFRSLFGLDDLKISPVAPDANAVAAQILSLLPLKFFPIIVIGIIALILALAIGLGIHFDCSGKYRCRSSFKCVELTARCDGVSDCRDGEDEYRCVRVSGRNAVLQVFTAASWKTMCSDDWKGHYANVACAQLGFPSYVSSDNLRVSSLEGQFREEFVSINHLLPDDKVTALHHSVYVREGCASGHVVTLQCTACGHRRGYSSRIVGGNMSSLSQWPWQASLQFQGYHLCGGSVITPMWIVTAAHCVYDLYLPKSWTIQVGLVSLLDNPAPSHLVEKIVYHSKYKPKRLGNDIALMKLTGPLTFNEMIQPVCLPNSEENFPDGKVCWTSGWGATEDGGDASPVLNHAAVPLISNKICNHRDVYGGIISPSMLCAGYLKGGVDSCQGDSGGPLVCQERRLWKLVGATSFGIGCAEANKPGVYTRVTSFLDWIHEQMERDLKT
The following text describes a protein:
Function:
Regulates mitochondrial small subunit maturation by controlling 15S rRNA 5'-end processing. Localizes to the 5' precursor of the 15S rRNA in a position that is subsequently occupied by mS47 in the mature yeast mtSSU. Uses structure and sequence-specific RNA recognition, binding to a single-stranded region of the precursor and specifically recognizing bases -6 to -1. The exchange of Ccm1 for mS47 is coupled to the irreversible removal of precursor rRNA that is accompanied by conformational changes of the mitoribosomal proteins uS5m and mS26. These conformational changes signal completion of 5'-end rRNA processing through protection of the mature 5'-end of the 15S rRNA and stabilization of mS47. The removal of the 5' precursor together with the dissociation of Ccm1 may be catalyzed by the 5'-3' exoribonuclease Pet127. Involved in the specific removal of group I introns in mitochondrial encoded transcripts.
Sequence:
MLKSLTSRPTVMYGMAAFKLNRSPYRYLTFGSKLQTRHSSHVFPESMKVTTVQKELDVQVTTDDIDILYKALKTPIASQAKSGPAASVSHKLSPEYLQSLHLSLKDVEAEKLSKKTNQFKSLERALKNKTNTPTLSQLTQLIHINAIAKRPKQALESFNHIEKVGLTPDVVAYNHLLDSYSRAGDLNGAVAVFSRMQTAGIFPDLVSFSTLINACVAKRDLNGAFKLYHEMKSKNIQPNQIIYTTLINGCAKTKDFARAWKTFNFMRTEISLPDAVAFNLMIHICSKTEDAERAIDLFKEMSERGLEISQYTLTSLIQACSSRHDYYNESFVLLEQMAASGFVPSIRTYNVILSGAARFGDILRGRLIWNDIVERMREQPLSSNPDVIQLNRISPDEYIYASMLRLYTKAIKIETQKALLLDPSTNTAAPPTLASDPTQQAKDFNLETSFDNSQATAETSISLLESTDTSPAALLDEAQSIWQIFLKQHHLHNTENTKRVQSAYLKLLCTDPSHNAFARAYDFWNTLDSVSKKSIANYYCLITLAMRQSDTIDQGTVLWNSLLEWDAEMEKSLDVQSGEKMTRTEKELLRLQHGRSREIMFKMHLTMANGYALAGKIESAVKVLYDTVLFRYPYYLPAVHFRDISPIVKIAEQNADNAQWDLMNHILGLCPPITDPLSQVQHMLKLKAVPSGSWWGWNILGVDEHAMAMLRRKQQKERSKVVQRTEAYRNRSTHHRNTKVVLANVPELVKSHTDKNSTTRG
The following text describes a protein:
Function:
Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2-alpha/SUI2) on 'Ser-52' in response to low amino acid, carbon, or purine availability. Required for adapatation to nutrient starvation by acting as a key component of the integrated stress response (ISR), by which cells alter their translational and transcriptional output in response to starvation. Converts phosphorylated eIF-2-alpha/SUI2 either to a competitive inhibitor of translation initiation factor eIF-2B, leading to a global protein synthesis repression, and thus to a reduced overall utilization of amino acids, or to a translational initiation activation of specific mRNAs, such as the transcriptional activator GCN4, and hence allowing GCN4-mediated reprogramming of transcription to alleviate nutrient depletion. Binds uncharged tRNAs (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MDAAKRLELCKEIQENEIEALKAIFMDDFEELKVRNAWNVTNGHVYCIHLCSRSANSKSIAKLDLCIELGRSYPYVKPVIKLQNGENVLNSQIRFLLDKLDTKAKDLLGEEMIFELASIVQDYLNDWQSDLSSQFASLEEERAVQLKHDRERAEVDLQLRLKREKDALFEEEQTLQNKIQDELQRRSYETPQSSSKKKTNSKETTSLETLPTSIYFDCSISVRDCHDSLVTFNRVLPLYTISHSNLSTLTLVKPESKEISLQDCVFLLRTVRISTPYWSTEDGKREIQELEYELESLKVIRHDLLASIYEYQLERETRGYGWRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHRTFAKLMDFGFTRTLRDMNASHPFNINSQSITNILPEGLYPPEVSESSFAAASRKTDIWCFGLLVLQMLCGAHVLNKFSSLKLIMTHVIPLLPGSYQDLVRRCLMRDSRKRPSAIDLLSSHVIRLGTAVLPPVEQGTFSKSARPSYGGQQDGIIDLLYRKSVSRYETDFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSRILREVMTLSRLHHEHVVRYYTAWVETEANDTVTEIISSDSESLSQSLNMAVDFRQSSSLPADKLSSLDIHFEDDYNSSADEEDPEASDISFQYSNTSDKEGSSDKDSSIEEASSVKTQENGLNATLYIQMEYCEKLSLQDIIRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDNNDKWKNRQSADEDLTTGVGTALYVAPELLSRRNGVRYDAKVDMYSLGIILFEMCMTFSTSMERIRIIDTIRSPSISFPSTFPFSRASHEFKVIHCLLQHDPTKRPSSQELLESEAIPPKVGEEFIQEGLRLLSNPNTPYYLKLLKVLFGQVPDRHKDFTYDFNLSEESGVLSKVSDRGWDSLLACLVRDHVVKVFRRHGAKERESHILFPKSSQYDKDQASVSLLDKNGTLLQLPYDTVLPYARNVARNAVEEEKTYLISDVFREAKGGGRPKAIKEISFDITTNSDNLDWYDAETIKALDEVLTEIPSLTESCILINHADILSSILDYLQVSKDKRRMATHILGQINQRLTLSQVRNQLRIESLVPSTTLDDLSLFDFRENYEEGASKLRKIFGKEMPQKMRTALNYMERVVKLLRALKISHQLYFMPLCVYNFEFYDGGLMFQAINLAEKSELICAGGRYDKLVRFFDPPLMRTARKKHVVGICFALEKLVFSMLRYIRFHNSKQSSKHSPSPTLKSVGPWAPRRVDVLVTSIGKDSILEKCSLLQELWALNIQADIVLRGASSLEEIVTHYRSEGINWVLVVRQKNTQMEHSVKARNILKNEDDEIRFDEVGMWLLGEINERKRNESMLQSKRILDSAQQDVAKFVDTSQSNLDVQLISLKDVNDRKYKWKHKQNAMNKVYDLVQSAIRESSEDAIALAVDCDSEAMEKLRSTTTLDEESWKRLIESCPASQREYMQRLQKKLVTLAEQDKKRVWICSFRTNEIYLYGLK
The following text describes a protein:
Function:
Hydrolase that can remove 'Lys-48'-linked conjugated ubiquitin from proteins; Probable hydrolase that can remove 'Lys-48'-linked conjugated ubiquitin from proteins.
Sequence:
MATGIAAASDNKMDLFKLVAALENTTPNNLFASAARPKTSQEEFKSTKPTKKQAEEEEGPKAGDDITMETAEGIKDVLYGRRSFTIDEEWKKAPFIRTPVDGPFPYGLLTPKDKARGLIIAIQAQFIQKVFSGGDDGIQSAHDPAKVAGRLKLVYEWKQRKVFIETLATILWRAGEGKKAIVALVYPAYAALLYSQQKRLEHFIKTVKVIECVSYKQVTKLLEKKLGMFEDQDGGGPLMFLLSLILSRRILKLKDDLQGELLFTETDQCNLSLINLILMGQATPYLFNGKQEYGLDAKPLDVPQYGIGQRAEVGILVVDRLDGKEAKNAKKITIGSMLKTPLFPIWVLRLKGRYSLFFCCNLNLNRDWRSEAKFNLYYYTGQREQKDEVRLTIDSRLRLMEEKKKKDDKNVPLLEECIQSRWPGAHVDWNGVSPFF
The following text describes a protein:
Function:
Involved in the synthesis of fatty acids. Elongates C10 fatty acids to C14.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MFPYVTDYSGFAIRKWMIDNVDVAGFLCLLYLGLVWKGPGVVKSLREKNLINATLLQGVFIMWNLFLSTFSVIGMIVVVPAAIAHISNKGLVPALCERDVNMIYDSPVGFWVGVFALSKIPELFDTVLLVLQGKQPPFLHWYHHTTVLIFSWQSYCEGSSTIFVFVAMNLTVHAVMYFYFAMCASGFKAIMRTIAPVITIMQILQMIVGSAVTMYSAYVLYNPQPDGPQTCDVTKASARMGVVMYLSYLYLFAALFVESYLKPKKRTEKSK
The following text describes a protein:
Function:
May play a role in the regulation of cytokinesis.
Subcellular Localization:
Cytoplasm.
Sequence:
MAHPSEVAQLGLLAKSVNNESAEFTGLSDALEKLGPIVRNSSLDHNYRKELSEDRAIWKEICDCLNGAHLDRVEEKEPRHLRMRAVRGMILLGRNLSVENQRLPQELALHSRVVELLAQVQCQYDEMEIALHKAAYELLYNLTRASATFDQQSLGNVCRALRYPLGAHGSRDLALPVSLYFLNMVRDDEFLFAFLKHPDADKIVYQFMLQGVIKNHTELFDVIDNKTHDLENLSSLGAIQMSIWSCLVTHASFSPYLERLESHNWEAFDTILRFAQLVVTSSEKWDKEQLTAITVWAFRIFESTASSVEEYTRRGIDDEAEASRLHQKLLVVLDILSVFSKYESIRKFIMFYNGVEVLINTLRYLQNHCMRINFTKAKSNMAATFKAYNSNYERVEDEGKIKSIINIETSSIKSTNFPECKSLIIEILGFLTYKNREVQDKCRELHGLELVLSNCVIDDNDPFIKERSIMCIRFLLEDNAENQSFVAQLEAKKAVNDDVLAEAGYEVKVGADGKIGLTKNPRAAVEDKMDLNLT
The following text describes a protein:
Function:
Part of the ABC transporter complex VatCDB involved in the import of iron(3+)-complexed aerobactin, a citrate-hydroxamate siderophore produced by other bacteria. Binds the iron(3+)-aerobactin complex and transfers it to the membrane-bound permease. Functions in the import of iron(3+)-complexed vulnibactin, a catecholate siderophore synthesized by V.vulnificus, in the absence of FatB.
Subcellular Localization:
Periplasm.
Sequence:
MLSAALAFNSYALDITHEMGTTSFETTPKKVVALDWVLTETVLSLGIELEGAANISGYQQWVAEPHLNADAIDVGSRREPNLELLSNIKPDVILISKHLAAAYEPLSKIAPVLVYSVYSEDKQPLESAKRITRSLGKLFDKEQQAEQVIAQTDQRLAANGAKITSAGKAEKPLLFARFINDKTLRIHSEGSLAQDTINAMGLKNDWQEPTNLWGFTTTGTEKLAEHQKANVMIFGPLSQEERQQLTQSPLWQAMEFSRTDSVYELPAIWTFGGLLAAQRLSDHITGRLTQPQ
The following text describes a protein:
Function:
Binds mRNA and regulates the stability of target mRNA.
Subcellular Localization:
Cytoplasm. Cytoplasm, P-body. Cytoplasmic granule. Note=Detected at cytoplasmic stress granules and P-bodies. Detected at exosome granules where mRNA is degraded.
Sequence:
MSSEPPPPPLQPPTHQTSVGLLDTPRTRDRSPSPLRGNVVPSPLPTRRTRTFSATVRASQGPVYKGVCKCFCRSKGHGFITPADGGPDIFLHISDVEGEYVPVEGDEVTYKMCSIPPKNEKLQAVEVVITHLAPGTKHETWSGHVISN
The following text describes a protein:
Function:
ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2).
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MPGPSPGLHRALLGLWAVLGLGLLGLSAVAQEPFWADLQPRVALVERGGSLWLNCSTNCPRPERGGLETSLRRNGTQRGLRWLARQLVDIREPETQPVCFFRCARRTLQARGLIRTFQRPDRVELVPLPAWQPVGENFTLSCRVPGAGPRGSLTLTLLRGAQELIRRSFAGEPPRARGAVLTATVLARREDHGANFSCRAELDLRPHGLGLFENSSATRELRTFALPPDPPLLAAPRLLEVGSGRLVSCAMDGLFPASEAGVYLALGDQRLSPDITLEGDAFMATATATASAEQEGARQLVCNVTLGGESRETRENVTVYSFPEPLLTLSEPNAPEGKTVTVTCAAGARALVTLDGIPAAVPGQPAQLQLNATENDDRRSFLCDATLEVNGETLSKNESTELRVLYAPRLDDSDCPRSWTWPEGPEQTLRCEARGNPAPSVHCARPDGGAVLALGLLGPITRALAGTYRCTATNVQGQAVKDVTLTVEYAPALDSVGCPERITWLEGTEASLSCVAHGVPPPNVSCVRSGEAGVVEGLLHVVREHAGTYRCEATNARGSAAKNVAVTVEYGPSFEELSCPSNWTWVEGSGQLFSCEVDGKPEPSVVCVGSGGTSEGVLLPLAPPDPGARAPPIPRELAPGTYICNATNQHGSTVKMVSVSAESPPQMDESTCPSHQTWLEGAEAAALACSARGRPSPQVRCSREGTPRTQRLHVSREDAGVYRCLATNTHGTDARIVTVGVEYRPVVAELAASPPGGVRPGGNFTLTCRAEAWPPAQISWRAPPGALNIGLSSNNSTLSVAGAVGSHGGEYECAATNAHGRHTRRITVRVAGPWLWVAVGGAAGGAALLAAGAGLAFYVQSTACKKGEYNVQEAESSGEAVCLNGAGAGAGADTGAEGGTEAADTAEAPAGGEVFAIQLTSA
The following text describes a protein:
Function:
Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing. Activates coagulation factor XI (F11); activation is promoted by the contact with negatively charged surfaces. Triggers the production of pro-inflammatory cytokines, such as MCP-1/CCL2 and IL8/CXCL8, in endothelial cells.
Sequence:
MTSGVLFLHSGLILTQQGCDSTYSAPFAFPLQPGLYRMAHSKTTMLQGLLLFGLLHLTLSHDGVFLEKGQALSLLKRPRRANKGFLEEMIKGNLERECLEETCNYEEAFEALESTVDTDAFWAKYQVCQGTKMPRTTLDACLEGNCAVNLGQNYRGTINYTKSGIECQVWTSKYPHIPKFNASIYPDLTENYCRNPDNNSEGPWCYTRDPTVEREECPIPVCGQERTTVEFTPRVKPSTTGQPCESEKGMLYTGTLSVTVSGARCLPWASEKAKALLQDKTINPEVKLLENYCRNPDADDEGVWCVIDEPPYFEYCDLHYCDSSLEDENEQVEEIAGRTIFQEFKTFFDEKTFGEGEADCGTRPLFEKKQITDQSEKELMDSYMGGRVVHGNDAEVGSAPWQVMLYKKSPQELLCGASLISNSWILTAAHCLLYPPWDKNLTTNDILVRIGKHFRAKYERNKEKIVLLDKVIIHPKYNWKENMDRDIALLHLKRPVIFSDYIHPVCLPTKELVQRLMLAGFKGRVTGWGNLKETWATTPENLPTVLQQLNLPIVDQNTCKASTRVKVTDNMFCAGYSPEDSKRGDACEGDSGGPFVMKNPDDNRWYQVGIVSWGEGCDRDGKYGFYTHVFRLKKWMRKTIEKQG
The following text describes a protein:
Function:
TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation.
Subcellular Localization:
Nucleus.
Sequence:
MSNEKVYNINLTKGTKKWNIAKFSNKIELSSFSKPVKMYKFNPLTQLLNHDINNATNNNTNGTTGTTNGTNGTTSTTTTTTTTTTTTTTTNNATPNPNAAQPFHRKKRYEAKPVNPKTIPWKLEDSNGNHSYQGNVEGNQSSSNYFLFMFQSDGSIKAVPCNDWYNFRPKKEFVSLTTEEAEDFMKKKNQEWDFLTAKLKKNDPNANLEKIEEEEQPLKKKVNEDPNRYTEADVKNDKKLQNRKEKKENEYNEDGDAPDFENRFEDDEDDTYMEGDGLTAEDENQIEDEDNDKDLSAAGIEMKKMIKKQQKDLEDDKDDSADENEEKNDDEDDDEEEIDPDEDEDFPKGLPNVKKEDDGSSKDSKDSKKKSKKQKDGSPKGKEKKSKKNKADSSNDTRDSKKLKKEPSSPQPPQPQPNSPPQPTSPTQPAEPPFTEEYIRRYLEKIKKIKSMDLINIFKTPLKDPNNKKIFVTMVQNVARVVEENGVKYLIPK
The following text describes a protein:
Function:
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.
Sequence:
MSERLQPGDPAPAFTLPDADGNEVSLSDHQGRKVIVYFYPAALTPGCTKQACDFTDNLELLTGAGYDVIGISPDKPEKLAKFREAESLKVTLLADPDKKVLDAYGAFGEKKNYGKTYMGVIRSTIVVDEQGKVERALYNVRATGHVAKIIKDLGI
The following text describes a protein:
Function:
Non-catalytic component of the proteasome.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MAATMVKEAGSEPSQLLGPESASERTLYPYVTGTSVVALKYKDGILMAADMGASYGSTLRYKSVERMKSIGKHSLLGASGEISDFQEILRYLDELILYDNMWDDGNSLGPKEVHNYLTRVMYNRRNKFNPLWNSLVLGGVKNGQKYLGMVSMIGVNFEDNHVATGFGNHFARPILRDEWHENLSFEDGVKLLEKCMRVLLYRDRSAVNKLQIAKITEEGVTISQPYALKTFWGFSAFQNPTVGAEGSW
The following text describes a protein:
Function:
Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MEEPVMTNTRRLSTIAILSAISFVLMYFDFPLLPAASFLKIEFSILPVLVGLVVMDLPAALGVLLLRSLLKLLLNSQGVNTYIGLPMNIVALGVFVIVFALIWKKERTTLRFLLGSLAGTVGLTLAMLVLNYVYAVPLYAKFANFDIGKILGLSNYLMTMVLPFNLIEGVIFSVSFWLLYVLLKPTLKHYER
The following text describes a protein:
Function:
[Isoform 2]: Negatively regulates the plasma membrane cation channel TRPM8 activity. Involved in the recruitment of TRPM8 to the cell surface. Promotes prostate cancer cell migration stimulation in a TRPM8-dependent manner.
Subcellular Localization:
[Isoform 2]: Cell membrane. Note=Colocalizes with TRPM8 on the plasma membrane.
Sequence:
MATIAAAAFEALMDGVTCWDVPRGPIPSELLLIGEAAFPVMVNDKGQVLIAASSYGRGRLVVVSHEGYLSHTGLAPFLLNAVSWLCPCPGAPVGVHPSLAPLVNILQDAGLEAQVKPEPGEPLGVYCINAYNDTLTATLIQFVKHGGGLLIGGQAWYWASQHGPDKVLSRFPGNKVTSVAGVYFTDTYGDRDRFKVSKKVPKIPLHVRYGEDVRQDQQQLLEGISELDIRTGGVPSQLLVHGALAFPLGLDASLNCFLAAAHYGRGRVVLAAHECLLCAPKMGPFLLNAVRWLARGQTGKVGVNTNLKDLCPLLSEHGLQCSLEPHLNSDLCVYCCKAYSDKEAKQLQEFVAEGGGLLIGGQAWWWASQNPGHCPLAGFPGNIILNCFGLSILPQTLKAGCFPVPTPEMRSYHFRKALSQFQAILNHENGNLEKSCLAKLRVDGAAFLQIPAEGVPAYISLHRLLRKMLRGSGLPAVSRENPVASDSYEAAVLSLATGLAHSGTDCSQLAQGLGTWTCSSSLYPSKHPITVEINGINPGNNDCWVSTGLYLLEGQNAEVSLSEAAASAGLRVQIGCHTDDLTKARKLSRAPVVTHQCWMDRTERSVSCLWGGLLYVIVPKGSQLGPVPVTIRGAVPAPYYKLGKTSLEEWKRQMQENLAPWGELATDNIILTVPTTNLQALKDPEPVLRLWDEMMQAVARLAAEPFPFRRPERIVADVQISAGWMHSGYPIMCHLESVKEIINEMDMRSRGVWGPIHELGHNQQRHGWEFPPHTTEATCNLWSVYVHETVLGIPRAQAHEALSPPERERRIKAHLGKGAPLCDWNVWTALETYLQLQEAFGWEPFTQLFAEYQTLSHLPKDNTGRMNLWVKKFSEKVKKNLVPFFEAWGWPIQKEVADSLASLPEWQENPMQVYLRARK
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 organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate.
Sequence:
MTDKFNYEELGLKVGLEIHRQLDTKKLFSPVPSELSDEVDFTFERRLRPTMSELGEIDPAALEEFKKGRKYIYEGNYRLTDLVYMDEEPPRGPDREALEVALQIGYLLNAKPVDEVHFMRKIVIDGSNVSGFQRTAIVAVNGKVDTPWGSVGIPTVCLEEDACRIVERKEKEVIYRIDRLGIPLVEISTTPDIHHPEQAKVVAKYIGDALRATRKVKRGLGTIRQDLNVSIRGGARVEIKGVQELDMIPLIIEREVERQLNLLRIRDELKRRGVKPEDIKEEFYDVTEIFQNTGSKIIARAIKSGGKVLAVKLPKFRGLIGKEIQPGRRLGTEMADRAKKYVRGIFHIDELPNYGITELEVNAVIEKLGLGEEDAFVLVAAEEETAKNALREVIKRAREAIEGVPEETRRALPDGNTQYMRPLPGKARMYPETDIPSIFLPPEEKERIRANLPELPQERVERYVKEYKIDRSLAETLVNDERDELFEELVEKGVKPSLAASILVVVLKGLKKEVPVENITDGHIMEAFQLYLEGKIAKEAFEEIFKELALHPEKTAKQVAEEKGLTLLSEEEVEKIIDEVIQQNIEVIKAKGMGAMGMIMGRAMAKLRGRADGKLVSSLVRKKIQEIAG
The following text describes a protein:
Function:
Involved in the central benzoyl-CoA catabolism. Catalyzes the oxidation of 6-hydroxycyclohex-1-ene-1-carbonyl-CoA to 6-oxocyclohex-1-ene-1-carbonyl-CoA. It is specific to NAD and is also able to oxidize 2-hydroxycyclohexane-1-carbonyl-CoA.
Sequence:
MAAKSSVSSWRSEMSSNPHRWMMTSPGAPMVRAEFEIGELSADQVVVAVAGCGVCHTDLGYYYDSVRTNHALPLALGHEISGRVVQAGANAAQWLGRAVIVPAVMPCGTCELCTSGHGTICRDQVMPGNDIQGGFASHVVVPARGLCPVDEARLAAAGLQLADVSVVADAVTTPYQAVLQAGVEPGDVAVVIGVGGVGGYAVQIANAFGASVVAIDVDPAKLEMMSKHGAALTLNAREISGRDLKKAIEAHAKANGLRLTRWKIFECSGTGAGQTSAYGLLTHGATLAVVGFTMDKVEVRLSNLMAFHARALGNWGCLPEYYPAALDLVLDKKIDLASFIERHPLDQIGEVFAAAHAHKLTRRAILTP
The following text describes a protein:
Function:
Involved in endocytosis positive regulation. Acts in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Confers salt tolerance.
Subcellular Localization:
Endosome membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm.
Domain:
The EH domain (1-93) is critical for vesicular localization.
Sequence:
MEIESVAAGSCSKENQMIYKEWFEFSDSDGDGRITGNDAIKFFTMSNLPRPELKQIWAIADSKRQGYLGFKEFIVAMQLVSLAQTGHEISHEVLISDVDFKNINPPTMEGLGVLMAKKKHSSKSSDPNMNGSPAADTSLTAHWFSSKSSKKISLSSVTSIVDGLKRLYIQKLKPLEVAYRFNDFVSPLLTNSDFDAKPMVMLLGQYSTGKTTFIKHLLKSTYPGAHIGPEPTTDRFVVVMSGPDERSIPGNTVAVQADMPFSGLTTFGTAFLSKFECSQMPHPLLEHVTFVDTPGVLSGEKQRTQRAYDFTGVTSWFASKCDLILLLFDPHKLDVSDEFKRVISSLRGHDDKIRVVLNKADQVDTQQLMRVYGALMWSLGKVLNTPEVSRVYIGSFSDKPINEAATGPIGRELFEKEQDDLLADLKDIPKKACDRRINEFVKRARAAKIHAYIISHLKKEMPAIMGKAKAQQKLIDNLEDEFGKVQREHHLPKGDFPNVDHFREVLSGYNIDKFEKLKPKMLQTVDDMLGYDIPELLKNFKNPYD
The following text describes a protein:
Function:
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
Subcellular Localization:
Cytoplasm.
Sequence:
MKHAENEYLNLCRHVMEHGTKKEDRTGTGTVSVFGYQMRFDLSKGFPLLTTKRVPFRLVASELLWFMKGDTNIRYLLQHNNNIWNEWAFKSWVESDEYTGPDMTDFGLRSQQDEEFKVQYDEQMELFKKNVLEDDEFSNKYGYLGDVYGKQWRAWKTTAGETLDQLKDVIEMIKKTPDSRRLIVSAWNPEDVPSMALPPCHTLFQFYVADGKLSCQLYQRSGDIFLGIPFNIASYSLLTHLIAHECGLEVGEFVHTIGDAHIYTNHFEQVEKQLAREPRPFPKLTLNPDVKSVFDFEMEDLTIEGYDPHPAIKAPVAV
The following text describes a protein:
Function:
Required for correct meiotic chromosome segregation.
Subcellular Localization:
Cytoplasm.
Sequence:
MCYLSRMSSQQMQLTISGFENRIKILEDLMNEFDSNLYIRLKRECDFKLPKEYDVSIHALTILMKRHLSNMEPIDCYQDLDTGTLQTMLIFCCTLRMIEHYEKSLSNINFFSLSNDLKRLEEYNTSCSVLLSLYQRQLKKISTTIESYYLADTLRHNQNILNLCERIYNIQKLLNKREKASVLRH
The following text describes a protein:
Function:
Involved in regulation of actin and microtubule organization. Part of a WAVE complex that activates the Arp2/3 complex.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MPIERHIIKNAYGLSDPKLYGVLVSNHSELLLDGVSMAGYVGVLRLLGDLAQFSSELFHDLQEQVISTFSRGHKLLLRVEKIELDLPQIEKSFISQTNHKIIKCSPGTEWHPKISLDRNIVSNIDMPRFVLDSFDVCRFPPQLSKLDQFDEAGDGACLKRFYDPTFFQSHFSLLLTSEFLSQQQNKTYKIKISGLHSRKHQSLEISNAKAKDNSILQDMTFEKPNCILALKRMKLKKRNLQYQRNNIRRSYIECVLADLDLDGIYFQLDESPQTDLIDSIILVPDIHDEIDADSEFDISDSDQKFYTDFKNGHEETDRIIRELDDYYKETYKDSFYYHKSEFCRSFDGSSDSGTDKISFESVVNIDFSSDVSYISDDDDDDIVKNTEPVNDYFEKKTEERSESCFSLMRFQKELSDDENKEQSFNSLSCNSFENCYSTDDNIGMKQSSIDMKSGNLNSEEGDGDSESLRLGLSLHNTIYSGLKETGYPQLEPDALSDTGVSEVSHGTDAFSDATEDDTTCLDLSTYQAGSVVRMKLHKQNSISSENKDIYKKCPNSVNVSNEDIHSFDCESEDSDIKSPQRDGKDSHVISDKFNQDLIDTSNFGVSDESRRMENEKTQNVTCNSFGEKEEIAHSFEDDVNCGFSNNQQVLPNNNPIFSLNSSDRSFNTEETKSLLVTTSETQILSISHDTSEIVKTKPVNLLPSRPVRIPGGVALPGMAELHKNTMQKVLQPQLSKPAVTPDDESLPIMNELNNTFKKVSHINPIVEKTMDIMLEQIKNKSFTLKPVAAQRPKMKGPMTNHNLAAIIEKARTIRQVTVGSDDDDGENWED
The following text describes a protein:
Function:
Has phosphatidylinositol transfer activity (By similarity).
Sequence:
MESTASTSDSASAITTGLSEVDINQQSPPIILKEGEIFDPLKNLNEKQLEAFKEIKSNFSDLTDPTDIAFCTDMCFLRYLRARNYIVSKSEKMLRDTLEWRKKFRPQDIQLGGDIREIGSAGCVYVNKRDKKGRPIIFAVPRNDTLKNVPSELKFKNLVYWLEQGFSRMDEPKGIEQFCFIVDYKDFGSGNMDMKTNLEAMHFLLDHCPERMGQSLFLDPPALFWFAWKIISPFLNEVTLSKVRFINSKKVDGKRTFAELLEYVDIENLEQNLGGNLDYNYNIDEYLKENPDPIVDTPPITFSTETDSKKQKKEKKKEEKEKKKEEKEKKKEEKEEKKKEKEEKKKLKKEASFTKQQENADEVD
The following text describes a protein:
Function:
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.
Sequence:
MKNILTEENMNKLKEELEYRMTKKRAEIAKEKLEAAAHGDRSENAEYKEACANYRENDNRIQYLLTMISTASVIDEKNQNKSVLGVNSKCKIKFIEDEFETNVSLVTTMDADPEKMLISVESDLGKALMGKKVGDVAEVDAPGEKYTVEVLEII
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase.
Subcellular Localization:
Endomembrane system. Endoplasmic reticulum membrane; Single-pass type IV membrane protein.
Domain:
The RING-type zinc finger domain is responsible for E3 ligase activity.
Sequence:
MDFEHEEFFNQEWKADGNSVTETEKENIDNCFDCHICLDFAHEPVVTLCGHLFCWSCIYKWLFVQRASLAPDEHPQCPVCKHDISHTKMVPLYGRGQTLSSRRGRNRKATLEDISIPPRPPASEIQSLLETRTSPQSDQQEQENDDTSQVQNLDTLVTPVIPRYMFGNYEDLHLMVANKSLNKISFFFFLCFVMCLILF
The following text describes a protein:
Function:
Plays a role in chemotaxis signal transduction system in order to colonize the host stomach. May act as a phosphate sink to control the flow of phosphate to CheAY.
Sequence:
MAEKTANDLKLSEIELVDFRIYGMQEGVPYEGIYGINVAKVQEIIPMPTLFEYPTNLDYIIGVFDLRSIIIPLIDLAKWIGIIPDKSKENEKIVIITEFNNVKMGFLVHSARRIRRISWKDVEPASFSASNSINKENITGTTRIENDKTLLILDLESILDDLKLNEDAKNAKDTHKERFEGEVLFLDDSKTARKTLKNHLSKLGFSITEAVDGEDGLNKLEMLFKKYGDDLRKHLKFIISDVEMPKMDGYHFLFKLQKDPRFAYIPVIFNSSICDNYSAERAKEMGAVAYLVKFDAEKFTEEISKILDKNA
The following text describes a protein:
Function:
Transmembrane tyrosine-protein kinase (Probable). Required for the formation of facial lymphatic structures and brain lymphatic endothelial cells. Also required for embryonic ventral and dorsal migration of parachordal lymphoblasts along the arterial intersegmental vessel. Plays a role in the embryonic formation of the dorsal longitudinal anastomotic vessel.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
QLLQFAADVATGMHYLSDKQFIHRDLAARNVLVGDNLVAKIADFGLSRGEEVYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRMEQPRNCDDEVYELMRQCWRDRPYERPPFSQISVQLNRMQEARKAYVNMALFENFTYAGIDATAEEA
The following text describes a protein:
Function:
May have antimicrobial activity.
Subcellular Localization:
Secreted.
Sequence:
MISTSSILILVFLLACFMATSAQWGYGGYGRGYGGYGGYGRGMYGGYGRGMYGGYGRGMYGGWGK