lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Essential for normal culmination. May function as a transcriptional regulator.
Subcellular Localization:
Nucleus, nucleoplasm.
Sequence:
MNQSQNFHNIDLGHYGAQGSNQSFNNNNNGNNGMMMNQQQMQQHVVPHLHHLQQQQQQPQQQQLRNVPDYSNSPNGTTNGSTMSPNCINTNNNNNNNNNNNNNSNNNNNNNNNASNNLTSNKSSSTNTPQIGQLQASPANLTNSPSAISSPITISNNSSLNSPSTTSSPNLLLNGTSNKRIMISQQTCLVEEKFSKNGVQKNVHVVVKNNPFLLTLSLLDSSLNFHQLTPEVQLVYDSESLKEVDSATVKPLEYKTRANEEGDQLTIELRIKVLSSQLEDMLFRAKVKIVDPRTRKETHGLSVITHPIRVVSKPDQVKKKAKKRKRAPTDSLMDTLNRIEHQQKEQQRLLKKLCYHDKENNIIQLIQQQQQQQQLLNNVTNNINNNNNINNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNTTSTTTTTTTTTSSCNNNNNNNNENNEHIVKIENTECNNNNNNIINNTENDENINKPILNSKDEFQSAFKEFIGAFKQLQCLDPDGADGAFKINTCANDAQTMCEILEMVKVELKKDENFKDKCGGSSGGACGENNPDNPCSCKVCPYKQKVDHINQSYETYFNMFNPSNSNSVVPQQSQQLQQQQIQQQQQSQQQVQQQQQQQMQQQPQQQQQQPQQQQQNQQQGQQPQQQQQQGQLDYTTYIDPQLQMQQQLQMQQAAQQQYMQQTMDQQQQQQYYMQQYHLQQQQQQQQAQRYLMQQQYMQQQAQQQQQQHQQVAIQQQQQQNQQQNQQQNQQQQNQSPQNQQSLDFQNANNFIDFNSGLGFMNFPNINFGDMGFSAV
The following text describes a protein:
Function:
Cell surface protein which plays a role in the plasticity of cholinergic synapses at neuromuscular junctions and in the polarity of the mechanosensory neuron ALM, possibly by antagonizing Wnt signaling.
Subcellular Localization:
Cell projection, axon. Synapse. Cell membrane; Lipid-anchor, GPI-anchor. Note=Membrane association is important for synaptic function.
Sequence:
MGRLLAKMLFPLAMCLFVSAVSASDSPSSNEANPIVISSEAMDYDTNTITVREGKKLMVSCVFESDEQIHKSDLLWKQANGNNIDGESNPSLFSVILNEKGSKHRKTSLHFSSVHTRDTGLYTCTGRTAGGENFEKTIKLVVLPAIEWNDKDTVKGALLGEPITIDCGVKGPSGKEPMIQMTNGNGEPLDEEIWTIAGNEATIDSLKKEHAELTVSCITIEMHQETSKEEFPVVDRKDVNIEVYTLPEFETEESVQYTVIDNHVRDAIIYCNVTHSFPPVRHYTFYHGDEEIKMSDKFNIFVNVGVSQGAHLKIHNVNENDLGTYKCEANNIKAKSYHTIHLREANAPAEPKVTLIEDKRHSIIWKVESIDRDPDLPMTAVEIRHLRAGTAEASGVSDEDISDAYWKSHSIFMQRNIKDDGIYEINGLRHGHEYVWRFRQINEAGFGDSVVLRAKTLDDHDLEMMDSASDSKFPLALATLFFVCLFI
The following text describes a protein:
Function:
Putative gamma-glutamylcyclotransferase.
Sequence:
MGAEEAEKKTIIFTYGTLKRGFSNHVLLQDMIAAGDASFLGVYQTADRLPLVCGPYRVPFLLNFPGSGERVWGELYAVSARGLVRMDELEGITRAHYERLPIKVQQQAQAQPEVTTAEAYYAHRNYAEALWKRNGEKGYSCYSEKEAKGYVKRKDRPQHLTFLEQIGLFISSSADQKDNPNSCYCNKHLPAASVPINLVNH
The following text describes a protein:
Function:
Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of replication as well as for processivity of DNA replication.
Subcellular Localization:
Cytoplasm.
Sequence:
MKVTVTTLELKDKITIASKALAKKSVKPILAGFLFEVKDGNFYICATDLETGVKATVNAAEISGEARFVVPGDVIQKMVKVLPDEITELSLEGDALVISSGSTVFRITTMPADEFPEITPAESGITFEVDTSLLEEMVEKVIFAAAKDEFMRNLNGVFWELHKNLLRLVASDGFRLALAEEQIENEEEASFLLSLKSMKEVQNVLDNTTEPTITVRYDGRRVSLSTNDVETVMRVVDAEFPDYKRVIPETFKTKVVVSRKELRESLKRVMVIASKGSESVKFEIEENVMRLVSKSPDYGEVVDEVEVQKEGEDLVIAFNPKFIEDVLKHIETEEIEMNFVDSTSPCQINPLDISGYLYIVMPIRLA
The following text describes a protein:
Function:
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the extracellular potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSASLLQFVVLLGVMAALVVPVGNWLYGVATGQKDTALERLTYRVIGINPRERMDWKRYGLAIVVSNLVMLLLAYLLIRLQGALPWNPAGLAAQSPDLAWNTVVSFMTNTNWQAYSGEQSLSYFSQMAVITTFMFTSAATGFAAALAFMRGLAGRDGTNLGNFWVDVTRLIYRVLLPVCFGLALVFVWQGMPQTLGAYANATTLEGAAQRIALGPVASLESIKHVGTNGGGFFSMNAAHPFENPTPLTNALHILSMLLLPSALTYVFGRMLGNLKQGWVIFGGMLVMFVGFLGTVYSFEQAGNPILSKLGAEQAITATQAGGNMEGKEVRFGIAQTSLFATTTTAATTGSVDSMHDSYTGMGGFVPMLQMMLNNVFGGKGVGFINFVQYLVLGVFIAGLMVGRTPEFLGKKIEAKEVKLTMLAVLAHPLSILGFTALACVLPGALNSLNNPGPHGFSEILYAYTSGTANNGSAFAGLSANTFFYNLTIGLSMLMGRYLTLLPMLAVAGMLAAKRRVPAGSGTLPTDTALFGALTVFVILIVGALTFLPALTLGPVADHLQMLRGVVLK
The following text describes a protein:
Function:
Ribosome-binding protein that promotes ribosome hibernation, a process during which ribosomes are stabilized in an inactive state and preserved from proteasomal degradation. Acts via its association with EEF2/eEF2 factor, sequestering EEF2/eEF2 at the A-site of the ribosome and promoting ribosome stabilization and storage in an inactive state. May also play a role in the regulation of mRNA stability: binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers cyclic nucleotide regulation of message decay. Seems to play a role in PML-nuclear bodies formation (By similarity).
Sequence:
MPGHLQEGFGCVVTNRFDQLFDDESDPFEVLKAAENKKKEAGGGGVGGPGAKSAAQAAAQTNSNAAGKQLRKESQKDRKNPLPPNVGVVDKKEETQPPVALKKEGIRRVGRRPDQQLQGEGKIIDRRPERRPPRERRFEKPLEEKGEGGEFSVDRPIIDRPIRGRGGLGRGRGGRGRGMGRGDGFDSRGKREFDRHSGSDRSSFSHYSGLKHEDKRGGSGSHNWGTVKDELTESPKYIQKQISYNCSDLDQSNVTEETPEGEEHPVADTENKENEVEEVKEEGPKEMTLDEWKAIQNKDRAKVEFNIRKPNEGADGQWKKGFVLHKSKSEEAHAEDSVMDHHFRKPANDITSQLEINFGDLGRPGRGGRGGRGGRGRGGRPNRGSRTDKSSASAPDVDDPEAFPALA
The following text describes a protein:
Function:
This is a non catalytic metalloprotease-like protein. May play a role in sperm-egg fusion (By similarity).
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MKTPISSILKSNGLGIFLYRSFITSTAVSYTYDRQDVRHSQSLSSLKNCNYNGYVAGFPNSIVSLTVCSGLRGMIQFENVSYGIEPVETLSGFIHVIYENTNQQAKIPDLGENQTYSWSDELDYQFRSNMKKSGFAVLRPRYIKTDIVVDKKLFDYMGSDTRVVLQKVIQIIGFINTMFSKLKLTVLINSVEIWSKENRIDFPEAPENLLVQFLHWKHKYRPQHISYLLAFVEHPASTGALYPGNLCKPIYGAAIALYPKGLSLESYSVIVLQLLSIGIGLTYDNADSCHCTGDVCLMTPKAIYSGGVKDFSTCSLDDFKYLSTQDLECLQDLPMERQKKKPSRPRRICGNGILEMNEQCDCGTLKNCTHKKCCDPMSCRLKSKAVCGSGECCGQDCKVKPVNVLCRKSKNECDFEEYCNGNDAYCVPDTFARNGQYCDSGQAFCYSGLCMTSNNQCMNLLGKYVRGASFACYEEFNSRNDRFGNCIRKFCSFENSLCGKLVCTWPFKRLLMKDNMSAAYGQIRDDLCISLYKGGRPLKTTLSTYSDMSERDETFVKDGTICGPDMFCLETQCKETRFLVDFQQCNTSRDCNDHGVCNNFNHCHCDKGYNPPYCESVKGQFGSIDDGHKYYIDEGKSAKQQNRGIHPKQQLQLILYITLPLIMIISAVFIKQSKLSRLCGRERSEGTSCITEDSVSNTKMTTNEGSTLH
The following text describes a protein:
Function:
Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex that plays a role in different processes including cell migration, cell proliferation or cytoskeletal reorganization. Mediates RHOA ubiquitination and degradation in a ERK2-dependent manner. Induces RAC1 and RAC3 degradation by the proteasome system and thereby regulates TGFB1-induced E-cadherin down-regulation and cell migration. Also mediates ubiquitination and degradation of IL-33-induced receptor IL1RL1 and subsequently blocks IL-33-mediated apoptosis. Within the nucleus, binds to DNA containing unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides. Recruits CDK-mediator to chromatin and targets CDK8 to promoters of silent developmental genes leading to induction of these genes during cell differentiation. In addition, plays a critical role in the recruitment of RNF20 to histone H2B leading to H2B mono-ubiquitination.
Domain:
The CXXC zinc finger mediates binding to DNA containing unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides.
Sequence:
MSSSSRGPGAGARRRRTRCRRCRACVRTECGDCHFCRDMKKFGGPGRMKQSCLLRQCTAPVLPHTAVCLLCGEAGKEDTVEGEDEKFSLSLMECTICNEIVHPGCLKMGKAEGVINSEIPNCWECPRCTQEGRTSKDAGEGPGRRRADNGEEGANLGGGWKLTEEPPPPPPLPRRKGPLPAGPTPDDVPGPPKRKEREGGNEPPTPRKKVKGGRERHLKKVGGDACLLRGADPGSPGLLPPRVLNPSQAFSSCHPGLPPENWEKPKPPIASAEGPAVPSPSPQREKLERFKRMCQLLERVPDTSSSSSDSDSDSDSSGTSLSEDEAPGEARNGRRPARGSSGEKENRGGRRAIRPGTGGPLLSWPLGPAPPPRPPQLERHVVRPPPRSPEPDTLPLAAGSDHPLPRAAWLRVFQHLGPRELCVCMRVCRTWSRWCYDKRLWPRMDLSRRKSLTPPMLSGVVRRQPRALDLSWTGVSKKQLMWLLNRLQGLQELVLSGCSWLSVSALGSAPLPALRLLDLRWIEDVKDSQLRELLLPPPDTKPGQTESRGRLQGVAELRLAGLELTDASLRLLLRHAPQLSALDLSHCAHVGDPSVHLLTAPTSPLRETLVHLNLAGCHRLTDHCLPLFRRCPRLRRLDLRSCRQLSPEACARLAAAGPPGPFRCPEEKLLLKDS
The following text describes a protein:
Function:
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Domain:
Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.
Sequence:
MQFDIDRYFPDTSQESGDSGRASFEEKRPLYLAASKHFLTHYREEIKSVHRGGAAGTTVVKHITAMTDTLIRKLFRSITRDVAQPGRGREHLTLMAIGGYGRGELNPHSDIDLMFLYGGKDAARVEDIAQKLLYFLWDMRLDVGYSVRTLQDCVEMASSDLTVRTALLDSRVLAGSRVFFREFEKVMLTQILAKKSDSFIRDKVAELRKRREKYGSSVYLLEPNVKESEGGLRDLHTALWVMKIKYKVKDPKELVVKGILSEEELASYHEALSYLWRVRNELHFLAGRKNDQLTFEAQTELASFFGYEDSARTLAVEEFMRDYYLHANRVEHLASSLIARCMRKEEGAFKILGYFIRRPIGEGFYILKGELVIPDESVIEKEPARLMKIFEYAQKHGVEISVAVKSLIRKNLHLVNDKFRRSREVNQSFFAILRSDKGVPETLRLMHHLEFLNHFIPEFGHIYCKVQHDLYHIYTVDIHSLFAVEEIVKLLRGEHEKELPLLTSLARQVDKRELLLLAVLFHDIGKGEGGGHAEKGAAMMPTIARRMGLSKEDSERLEFLVRQHLLFAHIAQRRDLHDEKMIVQFARQMEKSENLKMLYLLTYADIRAVGTDVWTEWKARLLQELYEKAFNVLERGDFRLEAHSERVKKVKRKVVELLGDEYPAAAVREELRAMTIRHLLSNPAAVIAEHVKILHALEPGGVLTHVTHVQEGGYSTYSICTWDIPGLFSMITGVMAANGINILGAQIHTSSNGKVLDILQVNSPQGFMIIEESRWSRVDEDLRQVLTGKIRVASLVAKRQRPTLLTERPKPRFPSRVDIDNEVSSDYTVIDIYTHDKVGLLYRITSTLTDLGLYIGIAKISTKVDQVADVFYVKDIFGHKITSVERLEEIREKLRVAVEQPE
The following text describes a protein:
Function:
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate.
Subcellular Localization:
Cytoplasm.
Sequence:
MTETFDCADPEQRSRGIVSAVGAIKAGQLVVMPTDTVYGIGADAFDSSAVAALLSAKGRGRDMPVGVLVGSWHTIEGLVYSMPDGARELIRAFWPGALSLVVVQAPSLQWDLGDAHGTVMLRMPLHPVAIELLREVGPMAVSSANISGHPPPVDAEQARSQLGDHVAVYLDAGPSEQQAGSTIVDLTGATPRVLRPGPVSTERIAEVLGVDAASLFG
The following text describes a protein:
Function:
Binds CRF and inactivates it. May prevent inappropriate pituitary-adrenal stimulation in pregnancy.
Subcellular Localization:
Secreted.
Sequence:
MTPLAVVLTLFSCSVLVIRGHPGFEIQPEVNARRLLNSVHLQKQLTRGPLAQARSKRTSDHIITDCIFMTSEEGDFYHKSSIADGTACGAYIFSDPDQTIEVHFNYLDVPCENGGLVSFVDGWELNGEFFPSPSDHPLPLNSRFTEFCGKRKVKQTFKSSQNVALIQYRMPAKGTSFGFSVRFIKNPTPCNVLFQSTEDIYTLRNYGKRSNCSLSTLFPAAVRVASLNVGIVPSLGRGIELETGTIHKVRSQCQKRGLDDYLQIGGSRGLDNANLLLADSVCGLDSKPGKHVEVIACGTTTVRLVSSGAFDNSATVAIRGLTEDDINGYMSVFCQEEALE
The following text describes a protein:
Function:
May be involved in sister chromatid cohesion during mitosis.
Miscellaneous:
MISCELLANEOUS: [Isoform 2]: Derived from PCR data. Produced by intron retention; MISCELLANEOUS: [Isoform 3]: Derived from PCR data. Produced by intron retention.
Subcellular Localization:
Nucleus.
Sequence:
MFYSHTLLARKGPLGTVWCAAHVHQRLKKSQYTSINIPDTVDNIMFPEVPLALRTSSHLLVGVVRIYSKKVDYLYNDWNLLNTWVAKAFVSTQVNLPEDARQAPPESVTLPQALNLDEFDLEDDTLDMEFDNHTRSEEDITLTDQIPTGIDPYVAVTFDEDIISESIPMDVDQSTEPVSRHTGEIDVETAHETGPDNEPRDSNIAFDTGTYSPRNVTEEFTEVQDPRQSNLTEERIPNSERNDATSPGTVPEIERMRDAAHDLSPTSHPSFAAQQQDVRVERTESLDETLNEKEPTIPSIDEEMLNSGRHSAFELRSGSPGSAAGSEEERADFVHPSPQLVLQPSPPPQPQRRARKRKNFDGVTVLTNKNISERLKDPSDTLRKRKKMPSSKLKFWRMNNQSRKDQNFNEPLFTGFSDDLRNVFEKDYVASKPHLAVSDETLPEPASVSPTREAEVEINPVSPIPDSTNPDSTVQLSPAQQTEDVLDSAGPRPAHAESVATEAQSPRTFDNDDMGIEHLRDGGFPVYMPSPPPRSSPFRTDDFTTQSGNWETESYRTEPSTSTVPEDLPGQRNLGLSPVSERTDEELYFLEVGGNSPVGTPASQDSAALTGRARALAQYLKQRSSSSPTTSSHPSGDLSLSEILAGKTRKLAARMFFETLVLKSRGLIDMQQDRPYGDIALKLMPALFSKVQT
The following text describes a protein:
Function:
Involved in DNA recombination.
Sequence:
MVMWSYCIARTGGRMESLLILLLIANLAGLFLIWQRQDRQEKHLSKSLEDQADHLSDQLDYRFDQARQASQLDQKDLEVAVSDRLQEVRIELHQGLTQVRQEMTDNLLQTRDKTDQRLQALQESNEQRLEQMRQTVEEKLEKTLQTRLQASFEIVSKQLESVNRGLGEMQTVARDVGALNKVLSGTKTRGILGELQLGQIIEDIMTPAQYEREYATVENSSERVEYAIKLPGQGDQEYVYLPIDSKFPLADYYRLEEAYETGDKDEIERCRKSLLASVKRFAKDIKSKYIAPPRTTNFGILFVPTEGLYSEIVRNPVFFDDLRREEQIIVAGPSTLSALLNSLSVGFKTLNIQKSADHISKTLASVKTEFGKFGGILVKAQKHLQHASGNIDELLNRRTIAIERTLRHIELSEGEPALDLLHFQENEEEYED
The following text describes a protein:
Function:
Regulates myosin phosphatase activity. Augments Ca(2+) sensitivity of the contractile apparatus.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MSSLDARNNSAMMKRAEQLKRWEESDTNRAAPTPRHEHGRRIKFSSGCVFLAACLSGDKDEVVQLLDQGADINTANVDGLTALHQACIDDNLDMVEFLVERGADINRQDNEGWTPLHATASCGFVSIARYLVENGADVAAVNSDGDLALDLAIDVQHMAMIDYMEKMVQELNINVDEARKAEELAMLNDAKKWLRSDAAEVDRPHPKTGATALHVAAAKGYTKVLGLLLAGRGNVDRQDNDGWTPLHAASHWGQRETAEMLVESLADMDIRNYAGQSCIDVADRKIVKFLEELRANKRNKRRPSSQISRISDAMENHVEKTPTKLVRVEVRTDATKDAENVKPNQQIHAVEHPVEEEAPWRRKLPRTPSDSPTNNQVPDRELGTNSSETANDVILRRTQSFENDQKFYQKYNELRARIKANSCPILPANANANAAAANKSNNNNNLSSNNYHNNNNNNNKSDLLLGYAAGTTTTTSTPTTTTTTTSSTFNNTHSNTNNTSTTQQQPAAAAAASAANQLYSVQRSASLKDNSMYYRKPTVTIATSTAATAINSPSTTVQTPPIRRSFVPPVRDEESETQRKAHAKRVRETRRSTQGVTLDEIKSAEELVKKKNMGMANNNNNNNISTTTTNTISNSGFKLEDITSGGTYPPNNSTIIPSAPAVMAAANLSTTTGVQRRISSGPIALNASNQSLNSVGRPVSAPSEGTNNSAYVTPSARKFETNATSTGATTAATTTSNSTSNSVSATSANHTTATAPNATSNHDDKDNDKENDNRTQTVIQRRRKPKRRSTGVVHIDMDELDPERQNESSNNDNEEKEKESGSERTSRSRLGSTASTATTSESKSSSSNDKTENGDGIDYKALWEAEKLENDKLRQMLKQKDDEAVQTRATLERFANAQLDAYKSDNHRLKEENAALIRVISKLSK
The following text describes a protein:
Function:
Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein such as NqrB and NqrC, two subunits of the NQR complex.
Subcellular Localization:
Cell inner membrane; Lipid-anchor; Periplasmic side.
Sequence:
MGKFFASYLLILAPFFLQSCSAPSRTTLEGVRMTIPYRIVFGEALSPDAFQQAQKEIDRVFDHIDQTFNNWNPLSEISRINRTTKQTPIPLSPALFAFLCEIDHFHAFSDGRFDPTLGALKSLWLLHLKSHTIPSQELQHLYKHSSGWHLISLDKTQQTLRKLSPLVQLDLCGTVKGFAVDLLGTACAQFCQNYYVEWGGEIKTKGKHPSGRSWAVASSATPEILHLHDHAIATSGSQYQRWHVDNKTYTHILDPLTGTPLEDSSHPILAVSVINESCAFADAMATALTTFSSKQEALDWANKKHLCAYITDKNVS
The following text describes a protein:
Function:
Involved in the synthesis of hordatines (antifungal hydroxycinnamoylagmatine derivatives). Specific for agmatine as the acyl acceptor, inactive towards tyramine and putrescine. Has activity with the acyl donors 4-coumaroyl-CoA, cinnamoyl-CoA, caffeoyl-CoA, feruloyl-CoA, and to a lesser extent sinapoyl-CoA.
Sequence:
MKVTVLSSRAVKPDYGACGAPPGSTADVVPLTVLDKANFDAYISVIYAFRPPAPPNAVLEAGLARALVDYREWAGRLGVDAASGDRAILLCDAGARFVEATADVALDSVMPMKPTPEVLSLHPSGDDGPEELMLIQVTRFACGSIVVGFTAQHLVSDGRATSNFFLAWSQATRGLAVDPVPVHDRASFFKPRDPPRVEFEHRGVEFKPYEKVEENDDERHAGDGDVVVVNKVHLSLEFISKLKSRASVGAHRPHSTLRCLVAHLWRCVTKARGLDGRVSTSVAIAVDGRARMSPQVPDGYTGNVVLWARPTATAQELVTRPLQHAVELINREVARINGGYFESFIDFASSEAVQKERLVTTADAAEMALSPNIEVDSWLRIPFYDLDFGGGQPFFFMPSYLPVEGLLILLPSFAGDGSVDAYVPLFSRDMDAFKNCCYNLE
The following text describes a protein:
Function:
Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Subcellular Localization:
Cytoplasm.
Sequence:
MQATSEELFINLCSTDHMDFVFKGVSYKKQLEAARKATGSLCAMHVYHVKEPVEYIRAVQEFAFMGGSLGCAEGEKLSRACEYCVEHCMPLVIEAASGGVRMQEGVVALMQMANTTSCIESVKQAGIPVIVVIKDPCYGGTSGSFATLGDLTFGIKGSRFGFAGQNVIKNTIFNGSNEAFDRSVPAGFQTTDRAAATGAIDQLFDSLESAYASIHGILEVLIQRKGMQSVEAAAKTALLRLTGVPHGAEVDTEDAFLVQDAFVYRDARNVTRPQPCDYLKNFVDMAASLRVDKCITVAFGVFADTLPVIAIATSREDVLDPEAGLGSPTGYRFAARAIYLANRLSIPVITLVDTAGALPSPEAEEQCQSRAISECLLAFQAVHVPIISIITGEGGSGGALALAGGNYVGILSKAFYNVISPEGAASILQPSVYRNNTAEMRANFISDAELLAHVQRCYPIDLRNAGVVNDIIVGPEYSETRDACKDTSNRIAVFVARMLIKCSQIKNLKKHRNIRYRNLSVFDELTTERAQQWVAQLKGLKIVSSKLERATELTETQQEHLEQLKRVTLYLTDVAHLKGSKLFDVLNNSKTSLPPVKEPCNITVPNTIINRLSFRISDHPITCKSILKSQGPEAVCKYIIESGRLFYTDTTFRDAHQSLLATRLRTRELIEGAILLQNTSIPSIDKTPLFSVECWGGATFDTSLRFLDENPYDRLKLFTEAMPHTLTQMLFRGANAVGYTAYERSFIEQFIIKTADAGLDVFRVFDAFNSLQQMEVAVDTILSRCQKSICEICICFTGDFLDTTKRENIYTLDYYSNLCSEIVARWPNFHILCIKDMAGLLRPAHAAPLVARIKEAIGPTKPIHFHTHDTSGAGISTCLAMAKAGCHIIDLASSSLAGSTSQPSLQTFLQVHSTEERLYQANHEHVECIPRFFKLGDCCGDIIEALSVYDSYWRMLRKEYRELDTNFTAPSPDVYKHEMPGGQLTNLYQQCCEMGLEYRWNEAVDIYARCNAELGFLIKVTPSSKVVGDLALFLLAKNLEPEVLRDKQKSQTIDWPDSLVNLLKGKLGLPHHGFPLHVVKHVLKLSEADARAHLQSLEQSYRSASTELEASQQTHRYTQENNTAVEGASFTAEDAEILCSTMYPKPYTQFRERIEKYSDLLWLMPSSVYCKGLTVGESCWFLFETGIVGSITLSRVQNTDLQKTERKFEFIMELFEAGDLVEPSTMSRITFKDPSRLMLKQILSHKHTCKYKYSIPNQTCCPMADVNDETHVAASIPGVVEKLLVMVGQEVKKGDALLRIGSAKLDLVLTAHRNGRINEIMCHQNMPVMPGSLLLVVS
The following text describes a protein:
Function:
Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. RRP4 as peripheral part of the Exo-9 complex is thought to stabilize the hexameric ring of RNase PH-domain subunits.
Miscellaneous:
MISCELLANEOUS: Present with 4840 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus, nucleolus.
Sequence:
MSEVITITKRNGAFQNSSNLSYNNTGISDDENDEEDIYMHDVNSASKSESDSQIVTPGELVTDDPIWMRGHGTYFLDNMTYSSVAGTVSRVNRLLSVIPLKGRYAPETGDHVVGRIAEVGNKRWKVDIGGKQHAVLMLGSVNLPGGILRRKSESDELQMRSFLKEGDLLNAEVQSLFQDGSASLHTRSLKYGKLRNGMFCQVPSSLIVRAKNHTHNLPGNITVVLGVNGYIWLRKTSQMDLARDTPSANNSSSIKSTGPTGAVSLNPSITRLEEESSWQIYSDENDPSISNNIRQAICRYANVIKALAFCEIGITQQRIVSAYEASMVYSNVGELIEKNVMESIGSDILTAEKMRGNGN
The following text describes a protein:
Function:
Hydrolyzes galactooligomers with a degree of polymerization higher than 3. Hydrolyzes radish root arabinogalactan-protein. Does not hydrolyze dextran, arabinan, starch, laminarin, beta-1,4- and beta-1,3-galactans, larch wood arabinogalactan or acid-insoluble polygalacturonic acid.
Sequence:
MRSIVLPSLALALFSQRARADTTLTIDPTSNWGTWEGWGVSLAWWAKAFGNRDDLASVFFSRNNQAVNGQTLPGLGFNIVRYNAGACSNNSYDGSTMVVSPNIKPSRQMDGFWLDWASSDPSSSSWNWNVDANQRAMLQKAKANGANIFELFSNSPMWWMCNNHNPSGSGSSDNLQSWNYQNHAVYLADIAQHAQQSWRIQFQSVEAFNEPSSSWWTAEGTQEGCHFDVSTMATVIGYLNTELSSRGLSSFVASSDENTYDLAISTWQGFNSSTRNIVKRINVHGYQDGGGRRDTLYSLASQAGKRLWNSEYGDSDASGKSMYQNLLLDFTWLHPTAWVYWQAIDGAGWGLIVGDNDNLTLSSASTKYFVLAQLTRHIRQGMQILTTPDVNTAVAYDAGSQKLVIVTANWGSAQTITFDLTRARTAGSNGATVPRWSTQTGGGDQYRSYTDTKINNGKFSASFSSGQVQTFEVSGVVLQ
The following text describes a protein:
Function:
Rho GTPase-activating protein which may be involved in clathrin-mediated endocytosis. GTPase activators for the Rho-type GTPases act by converting them to an inactive GDP-bound state. Has activity toward CDC42 and RAC1.
Subcellular Localization:
Cytoplasm. Membrane; Peripheral membrane protein.
Sequence:
MAADVEGDVYVLVEHPFEYTGKDGRRVAIRPNERYRLLRRSTEHWWHVRSEPGGRPFYLPAQYVRELPALGHPATPPHAPLPGPTASEPLAYDYRFVSASAPAGPDGTPAEPRDRAGSLCSLARGRNVTQRRSLAPGLPACLYTRPTAPVRPAQSLDDLARTAVPPAGLLGSRGSFKACSVAGSWVCPRPLARSDSENVYEAIQDVRGQPREQHPKQADDPPEPVYVNLERQPRATSPRATAAPLPSPVWETHTDAGTGRPYYYNPDTGVTTWESPFEAAEGAASPATSPASVGSHESLETEWGQYWDEESRRVFFYNPLTGETAWEDESEDQPEDELEMQPGLSPGSPRDQRPPTPEADYPESLTSYPEEDYSPVGSFSEPGPTSPLVIPPGWSCHVSPDGQTLYTNNFTQEQWVRLEDQLGKPYFYNTDDASVQWELPQVPVPAPRSIRKSSQDSETPAQASPPEEKIKTLDKAGVLHRTKTVDKGKRLRKKHWSASWTVLEGGVLTFFKDSKTSAAGGLRQPSKLSTPEYTVELKGASLTWAPKDKSSKKNVLELRSRDGSEYLIQHDSEAIISTWHKAIAQGIQELSADLPPEEESESSAVFGSSERLGSCREDEARPGAGVPGGLESDVSKVRYKLRKFLLRRPTLQSLREKGYIKDQVFGCALAVLCERERSSVPRFVQQCIRAVEARGLEIDGLYRISGNLATIQKLRYKVDHDERLDLDDGRWEDVHVITGALKLFFRELPEPLFPFCYFRQFITAIKLQDQAQRSRCVRDLVRSLPAPNHDTLRLLIQHLCRVIEHGEQNRMSVQSVAIVFGPTLLRPETEETSMPMTMVFQNQVVELILQQCADIFPPH
The following text describes a protein:
Function:
Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia.
Subcellular Localization:
Cell junction, tight junction. Cell membrane; Multi-pass membrane protein.
Sequence:
MAISSCQIVGYLVGILTWLGALLVVTLPDWKHSYVSERSFSGVLVVRGLWTTCTVKESGSVECINISEPVFALPTLIKGCRTLSVLGTVLAFCAVAITPLGMRCTRIGGDAKTKLRIARCCAVLFGLAAILIGIAVSWYAEDVAKDFHNPLSLRKLPPVSDLKYVYGNALYIGWATMATGAISSTFL
The following text describes a protein:
Function:
Component of the outer dynein arm-docking complex (ODA-DC) that mediates outer dynein arms (ODA) binding onto the doublet microtubule. Involved in mediating assembly of both ODAs and their axonemal docking complex onto ciliary microtubules.
Subcellular Localization:
Cytoplasm, cytoskeleton, cilium basal body. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, cytoskeleton, cilium axoneme.
Sequence:
MTSPLCWAAASNAMPSQDQISTPSKVKATQVQLKPYRSRGKGLVPVWHSLHSKAGPLHASEGKSAVNMQVAELQRKIQLLEGDRKAFYESTQWNIKKNQETINQLREETRVLQLQLTALLQGDEKVVQAVIREWKSEKPYLKNRTGQQALEHLDYRLNEKVKQLNALRHQLGLRQKWLEELQLQHSLRELEIAEAQDSNTEVAKTMRNLENRLEKARMKAEEAEHITSVYLQLKAYLQEESLHLGNRLDFMEAEVVRTKHELEELHLVNQEALNARDIAKNQLQYLEETVFRERKKRERYLTECKKRAEEKKLQNERMERKTQREHVLLQSDDTLQDSMYSKEEELKRRWSMYQMEVLFGKVKDATGVAETHAVVRRFLAQGDTFTQLEMLKSENEQTLLRLKQEKQRLQQELEDLKYSGEALLVSEQKRQAELQGRLKMEEQRRADAQNQLDRTMRALQITKEGLEHLAGKLNHIVVAGPTYEEGSPGASLDTKGSATPQPQETGRSVGKMDPKVDDYLPNLLGLVEEKLLKLHSQLENHNVPEMLRHIVDLEFYATLEGKLPSYNTRIALPVAGHKDKFFDEEESEEDDSDVVTRAALKMRSQKLIESRSKRRGRSRRS
The following text describes a protein:
Function:
May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane.
Sequence:
MSSTELETPIQSVPKEEPPSYNTIAPYAPPDSYPPPTSNPLMAITPVMGLPPGMENLLQINQLSIREKFKVSQGWARNFDVLNSAGQGLFQAEQRLHCCVAIFDVIVRDTHGNSMMELHEGCHCCSREMEVYTPARSLLGSVTLHWNSFVTHLSIMDSSKQVLLLILGPSLQANVFGNVSFEVKSSDEQHVVGMIRHTNEEVTVSFPLDMEVTLKSVLLGSAFYMDCLIYQRRSELLSTRNSD
The following text describes a protein:
Function:
Involved in transformation (genetic competence for DNA uptake). DNA uptake is energy dependent, this protein may provide the driving force for DNA uptake (Probable). Does not have helicase activity, translocates on single-stranded (ss)DNA in a 5'-3' direction in an ATP-dependent manner, but does not unwind double-stranded (ds)DNA (tested with 5'- and 3'-overhang dsDNA). ATP hydrolysis causes the release of ssDNA from ComFA. A ssDNA-stimulated ATPase; dsDNA does not stimulate ATPase. ATP hydrolysis causes the release of ssDNA from ComFA. ComFC has no effect on ATPase activity. Binds ssDNA but only very poorly to dsDNA in the absence of ATP. Binding to ssDNA does not require free DNA ends.
Subcellular Localization:
Cytoplasm. Note=Localizes mostly to the cell poles during the development of competence.
Domain:
Oligomerizes via its C-terminus (residues 73-432).
Sequence:
MKVNLDYLGRLFTENELTEEERQLAEKLPAMRKEKGKLFCQRCNSTILEEWYLPIGAYYCRECLLMKRVRSDQTLYYFPQEDFPKQDVLKWRGQLTPFQEKVSEGLLQAVDKQKPTLVHAVTGAGKTEMIYQVVAKVINAGGAVCLASPRIDVCLELYKRLQQDFSCGIALLHGESEPYFRTPLVVATTHQLLKFYQAFDLLIVDEVDAFPYVDNPMLYHAVKNSVKENGLRIFLTATSTNELDKKVRLGELKRLNLPRRFHGNPLIIPKPIWLSDFNRYLDKNRLSPKLKSYIEKQRKTAYPLLIFASEIKKGEQLAEILQEQFPNEKIGFVSSVTEDRLEQVQAFRDGELTILISTTILERGVTFPCVDVFVVEANHRLFTKSSLIQIGGRVGRSMDRPTGDLLFFHDGLNASIKKAIKEIQMMNKEAGL