lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalyzes the oxidation of hydrogen sulfide, with the help of a quinone.
Subcellular Localization:
Mitochondrion.
Sequence:
MLTLNSTIKSVTGSFQSASMLARFASTHHKVLVVGGGSAGISVAHQIYNKFSKYRFANDQGKDTSLKPGEIGIVDGAKYHYYQPGWTLTGAGLSSVAKTRRELASLVPADKFKLHPEFVKSLHPRENKIVTQSGQEISYDYLVMAAGIYTDFGRIKGLTEALDDPNTPVVTIYSEKYADAVYPWIEKTKSGNAIFTQPSGVLKCAGAPQKIMWMAEDYWRRHKVRSNIDVSFYTGMPTLFSVKRYSDALLRQNEQLHRNVKINYKDELVEVKGSERKAVFKNLNDGSLFERPFDLLHAVPSMRSHEFIAKSDLADKSGFVAVDQSTTQSTKFPNVFAIGDCSGLPTSKTYAAITAQAPVMVHNLWSFVNGKNLTASYNGYTSCPLLTGYGKLILAEFLYKQEPKESFGRFSRFLDQTVPRRMFYHLKKDFFPFVYWNFAVRNGKWYGSRGLIPPHFPVN
The following text describes a protein:
Function:
Putative transcription factor that may potentiate the function of warA.
Subcellular Localization:
Nucleus.
Sequence:
MNIGSLLHSSMLGKQFQSNQSQQEVVSNNIAECNENNNNNNNNNNNNNNSNNNNNNNNNNNNNNNNNNNNNNDNNNNSNNNKININESSQSITETVRSPYSSPSSSISSPSRSPSPNSPASSSPIHSPIPNTNFKQSGEYQSIPSPQNIHGLNKKVKVDMLESPNSSNSSPSFSSNMSPSSSNSPRHRSNSTSNNKSLLQYQFNQSNQSPSFSPLRNNKNNNNINNNNNNNNNNNNNNNNNNNQSPSMNGSPSSNLSKSNSGIPPLQLQAPSNTSSPQLLSPNHNQQRISPNRYLNGGNNNHNNNNNNNNNNNNNNNNNNNNNNNNHNNHNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNINNNNINNNNHNYNHNQNHNHNHNYNNNNQNNQNNNNDDNFSPSHSPNLSPSNYNSSPTHYGNNNNDTPKRSHASYKNNNNNNNNNNNSNSSFDEYQPQQKVSRSNSPNNDKEKKRRTRLKKEQADILKTFFDNDDYPTKDDKETLANRLGMSYCAVTTWFSNKRQEKKRRGDVAPVQTGGRRVPIDDEDDYENRNGDNSPSRNQGGAIELLKNSSSGLTPILESLNVKQQNNINFFKNNNMDNNNKNVPHLSLSNNNNNNNNNNNNNNNNNNNNNNNNRNRNNNNIYNNNNNNNNNNSNNRGKNFSDSGSSDSDSELNRHNNNNNNNSNNYNNGNSNSNNNRNNNNNYNYNNYINNNNYNNNNNRQHCDDEEEDEQYFNNNNNNNNNNNNNRISDSSDDQYFSDDTNNNNDNYNNGNNNYNNNNNNNNFNNNYMNNYNNNYNNNNYNNNNSYNNSNGNNNFNNNNNNNNQNNNNNNNNNQYNNNNKNYLNNIPSSKKHQLQGNYERRNSLPNSQIQNNFNGDNNNNNNNKNNNNNNQNNNGNGNNNNNNNNDNNIYKRRHSMDDDCQQN
The following text describes a protein:
Function:
Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Subcellular Localization:
Cytoplasm.
Sequence:
MLDPRSVPFAAQIHPQARPARRLTWDSREAGPDTAFVALPGEKMHGNRFVERALAAGAPFVLTDLDVPRAVRVDDARGALFAWARSERAKNPLVVGITGSAGKTTAKSYAAAALDAHFMPVFNTMPAIACFLVQYGASQKPLVVEMGIDHIGEMAELMDLVRPDVGVVTTIGPAHLEQFGMVETIAHEKGQILTARRALVGSQAAAFFPKAQFPHVDSYGFGDVTFRGEGLELSPQAARFRFGGMGVILPLASRVQAEAAVLGMVLAREAGIALADAAVRMSAVEVPGGRYRLHPGRFTVIDDAYNASPVAVRAALDALHALKPEGEVGRRISVLGRMLELGPTERELHAEVGSYAREQADLTYGVGEFAQELGERAFATVPELLADLLNEVRDGDIVLVKASRGISLTPEQRAVTGVGLDVVVEALLDQRDR
The following text describes a protein:
Function:
Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding.
Subcellular Localization:
Cytoplasm.
Sequence:
MSQEQAEQLMQQMQMLETYFADLSQRENTFLGVFREATAAIESIKSLSKNPESDTLVPIGLGTYVPTKISSDSKIILNIGAGVAVEKDFPSAINYLEERIKEIEIAIQDTAAKKQDAAQRLEQGKAQVNQLMQAMQQSGQPPKSG
The following text describes a protein:
Function:
Cleavable component of the cohesin complex, involved in chromosome cohesion during cell cycle. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At metaphase-anaphase transition, this protein is cleaved by cut1 and dissociates from chromatin, allowing sister chromatids to segregate. Also involved in the DNA double-strand-break (DSB) repair system.
Subcellular Localization:
Nucleus. Chromosome, centromere. Note=Associates with chromatin. Cohesin complex mainly associates with broad centromere region. Also associates with mating-type heterochromatic region.
Sequence:
MFYSEAILSKKGPLAKVWLAAHWEKKLSKVQTLHTSIEQSVHAIVTEETAPMALRLSGQLMLGVVRIYSRKARYLLEDCTEALMRLKMSFQPGQVDMIEPATALQSLKGKDAVTQSANLTLPETITEFDLLVPDSTFDFQWSQLLRTPSRSSNTLELHSLPISSSPSFPSSQLSIEAGRNAQVESGFSLGESFAHVGNDMQFHLPISNSGAATPRSVHSDNQSQISIEVGRDAPAAAATDLSGIIGPQMTKSPASSVTHFSTPSMLPIGGTSLDDELLAPVDDLNLDLGLDDLLGDEQGANAPAIEADEQAETSSIHLPSDIMEDDSSRPAAAGVEEGQVVESATAPQQEKINPQKTVRRQRAIIDPVTELSSKQMKKQLADTSSITSPLCLNTSSIVFNATVNFTRNGKFNTSIFSSNLNPKVNELLQADFKQAILRKRKNESPEEVEPAKHQRTDTSTENQETAEVLDPEEIAAAELANITEAAIATLPQETVVQPEGEAPELGSPMGFPVTALESADDSLFDAPPVMLDEADLLGSERLDSSVSEALPSSQTAKDSLRNKWDPYTEGEKVSFQTLSAGCNREEAVQLFFDVLVLATKDVISVKQDVAIQNEITLTAKRGMLLSSL
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 (By similarity). Involved in apoptotic DNA degradation. In vitro, does not bind or digest single-stranded RNA. In vitro, binds to double-stranded DNA without detectable DNase activity.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MAGRLREMRCELSFLKNADGSACFSQGATCIWASCSGPGDVHASKASDEAMTLDISYRANCGDNKFNVLNNIIHSTLSNAINLELFPHTTISVTVHGIQDDGSMGAVAINGACFALLDNGMPFETVFCGVLIVRVKDELIIDPTAKQEAASTGRVLFSVCKGSDGHPEVCAMDAIGHWDFIQLEAAWSLAQPSASAIFDFYKTVMKRKLSVDEQ
The following text describes a protein:
Function:
Has a dual role in the cell cycle. In mitosis, it is involved in maintenance of cdc2 kinase activity. It is subsequently required for regulation of septum formation. Could be involved in maintenance of cdc2 kinase activity by preventing, directly or indirectly, the degradation of cyclin or the dephosphorylation of 'Thr-167' of cdc2.
Subcellular Localization:
Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body.
Sequence:
MPSIDCKRLQKLAPKSPENQSKCISRLRYMVMLDQVESDEGGNSSTRPYVWAVLLNAPPRNADEYIRYVRQGPSPMAQKIQNDVSRTLVVESQFHSRVSQSSLSRLLNAYVWKRGALYVQGMNVLASPFLYACKSENQAFQFFDRLLQNECPLYVLPNIDGVHRGAKLLDKCLEVLDHRLYTYLLSKGLTAKIYALPSILTLSACTAPLSEALTIWDFLFAYGIHLNILCVIAQMFIFREQLIDHPSPMTLLRTFPPLNAKNIMKITILLISKLPPELYNLLARHAWDSEAGVLIDRLT
The following text describes a protein:
Function:
Ligand-specific transporter trafficking between intracellular organelles (TGN) and the plasma membrane. Plays a role in autocrine regulation of cell growth mediated by growth regulators containing cell surface retention sequence binding (CRS). May act as a hyaluronan (HA) transporter, either mediating its uptake for catabolism within lymphatic endothelial cells themselves, or its transport into the lumen of afferent lymphatic vessels for subsequent re-uptake and degradation in lymph nodes. Binds to pericelluar hyaluronan matrices deposited on the surface of leukocytes and facilitates cell adhesion and migration through lymphatic endothelium.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MCVCFLILLLSSIYKTLIRVVGSVKIALELGVQMTPSILGVYLYSVGQYSFNVTEARSACESLGVTIATKSQVSKARQNGLETCRYGWVDEQIAVIPRIKSLDKCGKNSTGLVVWRAEHSSKFDVFCFNSSGYWSNLKLPELCSTDPLINVTSVTTQTSVTTGLTARETRSLTAQLPSMTSVSLKGPRSSTPPETQSPFLTTTLSSTLRSTTVSSDPLSQGLVQSPFTGLRSSLPLALFVIAGILLLTAAAGAVWYCRRHKNVHPFSNKEPPKENIETEVWKQNNRDEQHQENQLETDLDKSRKNSQDLRLEVEPEAKAQ
The following text describes a protein:
Function:
Involved in ciliogenesis.
Subcellular Localization:
Cytoplasm, cytoskeleton, cilium basal body. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole.
Sequence:
MRNNPHPAGLIHPSAVSLQECDVDSDSSEERRNVCSSVSLEIHGLQREQDVYFSNQEYYRRLEELKSTHLRNMAELEKMYISQAKARHDEEAGGIWRGVNLDGRSSSRSPNISFPCSGPTRKLQRINSQEELDFHESSSGSDHSDFCGEDSGGELGWAPGPAGAFGRNILRSPNQNTTQTQIRTRAKAPGPKPQGGVSHPTGARGRSKVTVPKPFQMMLREEEKKKHQVRTRSEIELENTLLRQELEELRECQKKFRATPAPAHIHLPLYEVISRRQKNIRENIRGSAAVFPKPFHFLEREKRKREARMEAELGTFSHREERRAFSARAMPSSVYGSTADTRKSSSRQQPQSFCTLERDVTDGQSDQSSDLEDDCRPQRPSSSKAVKKHIELSIEMVGDREWSPYKIPMRSVCAPQQLQGSSFKDRSQHTSL
The following text describes a protein:
Function:
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MEESINPIISIGPVIFNLTMLAMTLLIVGVIFVFIYWASRNMTLKPKGKQNVLEYVYDFVIGFTEPNIGSRYMKDYSLFFLCLFLFMVIANNLGLMTKLQTIDGTNWWSSPTANLQYDLTLSFLVILLTHIESVRRRGFKKSIKSFMSPVFVIPMNILEEFTNFLSLALRIFGNIFAGEVMTSLLLLLSHQAIYWYPVAFGANLAWTAFSVFISCIQAYVFTLLTSVYLGNKINIEEE
The following text describes a protein:
Function:
Large subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the other to pyrimidine nucleotides. The large subunit (synthetase) binds the substrates ammonia (free or transferred from glutamine from the small subunit), hydrogencarbonate and ATP and carries out an ATP-coupled ligase reaction, activating hydrogencarbonate by forming carboxy phosphate which reacts with ammonia to form carbamoyl phosphate.
Domain:
The large subunit is composed of 2 ATP-grasp domains that are involved in binding the 2 ATP molecules needed for carbamoyl phosphate synthesis. The N-terminal ATP-grasp domain (referred to as the carboxyphosphate synthetic component) catalyzes the ATP-dependent phosphorylation of hydrogencarbonate to carboxyphosphate and the subsequent nucleophilic attack by ammonia to form a carbamate intermediate. The C-terminal ATP-grasp domain (referred to as the carbamoyl phosphate synthetic component) then catalyzes the phosphorylation of carbamate with the second ATP to form the end product carbamoyl phosphate. The reactive and unstable enzyme intermediates are sequentially channeled from one active site to the next through the interior of the protein over a distance of at least 96 A.
Sequence:
MPKRTDIQSVLVIGSGPIVIGQAAEFDYSGTQACRVLKAEGLRVVLVNSNPATIMTDPEIADATYVEPITPEFVEKIIAKERPDALLPTLGGQTALNTAISLHGNGVLEKYGVELIGANVEAINKGEDRDLFKEVVEEVRKKIGHGESARSYICHSMDDVLKGVDALGGYPVVVRPSFTMGGAGSGFAHDEDELRRIAGQGLTLSPTTEVLLEESILGWKEYELELMRDKNDNVVVVCSIENFDPMGVHTGDSITVAPAMTLTDREYQTLRDVGIAIIREVGVDTGGCNIQFAVNPEDGRVIVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGYTLDEIPNDITQETPASFEPTLDYVVVKAPRFAFEKFPSADSTLTTTMKSVGEAMAIGRNFTEAFQKALRSLEKKGSQFTFVGEPGDKDELLREAVRPTDGRINAVMQAIRAGATPEEVFDATKIDPWFVDQLFLIKEIADEIAESRELTADLLTEAKRHGFSDQQIAEISGLGEDVVRQVRHALGVRPVYKTVDTCAAEFAARTPYFYSSYDEESEVAPREKPAVIILGSGPNRIGQGIEFDYSCVHASFALSDAGYETVMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIVHAEQQAGPVAGVIVQLGGQTPLGLSQALKDNGVPVVGTSPEAIHAAEDRGAFGRVLAEAGLPAPKHGTATTFGEAKAIADEIGYPVLVRPSYVLGGRGMEIVYDETRLEAYIAESTEISPSRPVLVDRFLDDAIEIDVDALYDGEELYLGGVMEHIEEAGIHSGDSACALPPITLGGFDIKRLRASTEGIAKGVGVRGLINIQFALAGDILYVLEANPRASRTVPFTSKATAVPLAKAAARISLGATIAELRAEGLLPALGDGGTLPLDAPISVKEAVMPWSRFRDIHGRGVDTVLGPEMRSTGEVMGIDSVFGTAYAKSQAGAYGPLPTKGRAFISVANRDKRSMIFPARELVAHGFELMATSGTAEVLKRNGINATVVRKQSEGTGPNGEKTIVQLIHDGEVDLIVNTPYGTSGRLDGYDIRTAAVARSVPCLTTVQALAAAVQGIDALNHGDVGVRSLQEHAAFLIAARD
The following text describes a protein:
Function:
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. MDM34 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10.
Subcellular Localization:
Mitochondrion outer membrane; Multi-pass membrane protein. Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids.
Domain:
Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin; The SMP-LTD domain is a barrel-like domain that can bind various types of glycerophospholipids in its interior and mediate their transfer between two adjacent bilayers.
Sequence:
MSFIFNRETFEDNSFNEVLREKLMRALNLHDRTVGSSSGAMTTGTGAVECSGAAAAGQRPPRSKGGFSKVDILKSGIIVKKVEFPTIPKLEILDLDVSIQSKSLIKGICKVSCRDAMVQITTEIESNLLLLHVNSSPKFTTPKLISNDSFTVPITMTFDKLHLEAITNIFVKNTGVGISFNDVNLDFRLQCSIKLLQSSIEKRLKASMEEVFKDVLPSVIFNMSQRWFTHGETVVPTVDKSMVSSDTPVQPRMILDESDLSDLSPANMLRLSTLVSSRQTLCLNPTAVDTISTIPGCLERQNLHRFNLRFPSLYNYYSNKEQQGAHNNEKNRVEHLKLWGRSSSNPIPTRASFKVENTLPKEVLDSNSYDVRVITAIQTKMYERASNDVVLRRRKIKMRSRKPSKANKDAVSPAQNDSGTSSCSNVASELPHASLQANPQSDEIDPAPEGGPNAEDAYKEELEDSGLRAPQDFPALENVTPVLAQLPNQQRSRLGSPLSAGRPTPLLSPLDDSHWLLQKRDPQDLRTTLYSPIRNGRFYVMPQPQLDTKEASAFLLENGKRFGFVGLLNNHNLKWGNDPPPPYREVSITQ
The following text describes a protein:
Function:
May be involved in photosynthetic membrane biogenesis.
Sequence:
MTSKRTVSDSKRAFFAAYPRPVNSIYRRVIDELLVEVHLLITNQDFRHDPLFATGLLTAYQALMEGYTPVEQRDAILRALCTALELSYEQLHTDAAQWRAIAAELPAQEVLEVMAGKREAGDGRLKAMGDTLAGIANAERFKYSRLFSLGLANILEQAGRAAAMSEKDRLERLQQICTYLKLDYNRVKRDLDFFHSVLERIKRSKEVVDELSQTERRKREERAVSQPG
The following text describes a protein:
Function:
Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MGFNLTFHLSYKFRLLLLLTLCLTVVGWATSNYFVGAIQEFPKAKEFMANFHKTLILGKGKTLTSEASTKKAELNNCPSVSPYLRGQSKLIFKPDLTLEEVQAENPKVSRGRYCPEECKALQRVAILVPHRNREKHLMYLLEHLHPFLQRQQLDYGIYVIHQAGGKKFNRAKLLNVGYLEALKEENWDCFIFHDVDLVPENDFNLYKCEEHPKHLVVGRNSTGYRLRYSGYFGGVTALSREQFFKVNGFSNNYWGWGGEDDDLRLRVELHRMKISRPLPEVGKYTMVFHTRDKGNEVNAERMKLLHQVSRVWRTDGLSSCSYKLVSVEHNPLYINITVDFWSGA
The following text describes a protein:
Function:
Transcription factor capable of interacting with purine rich repeats (GA repeats). Must associate with GABP-alpha to bind DNA.
Subcellular Localization:
Nucleus.
Sequence:
MSLVDLGKRLLEAARKGQDDEVRTLMANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVMLQEAMQNQVNTNHERANPVANPVTVTAPFIFTSGEVINLASFVSSANTKATSAHLEEMEEGNSLDSSTQQVVGSGGQRVITIVTDGVPLGNIQTSLPAGGIGQPFIVTMQDGQQVLTVPAGQVAEETIIEDEEEEEEKLPLVKRPRMAEMTNRVEEMKEGSERELLQQQLQEANRRAQEYRHQLLKKEQEAEQYRLRLEAMAQQQTNGVEVDVTVVEEVAEVDAVVVTEGDEVERATQVMKSGRTTEPHTNVSIETISS
The following text describes a protein:
Function:
Early endosomal protein that functions to recruit SMAD2/SMAD3 to intracellular membranes and to the TGF-beta receptor. Plays a significant role in TGF-mediated signaling by regulating the subcellular location of SMAD2 and SMAD3 and modulating the transcriptional activity of the SMAD3/SMAD4 complex. Possibly associated with TGF-beta receptor internalization.
Miscellaneous:
MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Subcellular Localization:
Cytoplasm. Early endosome membrane.
Domain:
The SMAD binding domain (SBD) interacts with the MH2 domains of SMAD2 or SMAD3; The FYVE-type zinc finger is necessary and sufficient for its localization into early endosomes and mediates the association with PI3P.
Sequence:
MENYFQAEAYNLDKVLDEFEQNEDETVSSTLLDTKWNKILDPPSHRLSFNPTLASVNESAVSNESQPQLKVFSLAHSAPLTTEEEDHCANGQDCNLNPEIATMWIDENAVAEDQLIKRNYSWDDQCSAVEVGEKKCGNLACLPDEKNVLVVAVMHNCDKRTLQNDLQDCNNYNSQSLMDAFSCSLDNENRQTDQFSFSINESTEKDMNSEKQMDPLNRPKTEGRSVNHLCPTSSDSLASVCSPSQLKDDGSIGRDPSMSAITSLTVDSVISSQGTDGCPAVKKQENYIPDEDLTGKISSPRTDLGSPNSFSHMSEGILMKKEPAEESTTEESLRSGLPLLLKPDMPNGSGRNNDCERCSDCLVPNEVRADENEGYEHEETLGTTEFLNMTEHFSESQDMTNWKLTKLNEMNDSQVNEEKEKFLQISQPEDTNGDSGGQCVGLADAGLDLKGTCISESEECDFSTVIDTPAANYLSNGCDSYGMQDPGVSFVPKTLPSKEDSVTEEKEIEESKSECYSNIYEQRGNEATEGSGLLLNSTGDLMKKNYLHNFCSQVPSVLGQSSPKVVASLPSISVPFGGARPKQPSNLKLQIPKPLSDHLQNDFPANSGNNTKNKNDILGKAKLGENSATNVCSPSLGNISNVDTNGEHLESYEAEISTRPCLALAPDSPDNDLRAGQFGISARKPFTTLGEVAPVWVPDSQAPNCMKCEARFTFTKRRHHCRACGKVFCASCCSLKCKLLYMDRKEARVCVICHSVLMNAQAWENMMSASSQSPNPNNPAEYCSTIPPLQQAQASGALSSPPPTVMVPVGVLKHPGAEVAQPREQRRVWFADGILPNGEVADAAKLTMNGTSSAGTLAVSHDPVKPVTTSPLPAETDICLFSGSITQVGSPVGSAMNLIPEDGLPPILISTGVKGDYAVEEKPSQISVMQQLEDGGPDPLVFVLNANLLSMVKIVNYVNRKCWCFTTKGMHAVGQSEIVILLQCLPDEKCLPKDIFNHFVQLYRDALAGNVVSNLGHSFFSQSFLGSKEHGGFLYVTSTYQSLQDLVLPTPPYLFGILIQKWETPWAKVFPIRLMLRLGAEYRLYPCPLFSVRFRKPLFGETGHTIMNLLADFRNYQYTLPVVQGLVVDMEVRKTSIKIPSNRYNEMMKAMNKSNEHVLAGGACFNEKADSHLVCVQNDDGNYQTQAISIHNQPRKVTGASFFVFSGALKSSSGYLAKSSIVEDGVMVQITAENMDSLRQALREMKDFTITCGKADAEEPQEHIHIQWVDDDKNVSKGVVSPIDGKSMETITNVKIFHGSEYKANGKVIRWTEVFFLENDDQHNCLSDPADHSRLTEHVAKAFCLALCPHLKLLKEDGMTKLGLRVTLDSDQVGYQAGSNGQPLPSQYMNDLDSALVPVIHGGACQLSEGPVVMELIFYILENIV
The following text describes a protein:
Function:
Ribosome biogenesis factor. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome. Involved in nucleolar processing of pre-18S ribosomal RNA. Required for optimal pre-ribosomal RNA transcription by RNA polymerase I.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MVEQERVRVVRCGGSELNFRRAVFSADSKYGATRRCRPGRGWSLPGAAGKNCQARRDSLGGGSWLGKGCMRAPPGTRDGAGVCVLCEEGDTPQARGTAPWGARPLPRLSPAGRLRGPGGRAHVSRIGWALGRLEDGPGVDVYATAVALPRGPSFFRTESYIFCVSGDFVKVYSTATEECVHILQGHRNLVTGIQLNPNNHLQLYSCSFDGTIKLWDYVDGILIKTFIVGHKLHALFTVARAEDSVFVTINKEKPDIFQLVSVKLPKSSSQEIESKELSFVLDYINQSPKYIAFGNEGEYVAAVRDFYLSVYFFKKKTTSRFTLSSSRNKKHAKNNFTCVACHPKEDCIATGHKDGKIRLWRNFDDDKKYTYTCLHWHHDMVMDLAFSVTGTSLLSGGRESVLVEWRDAAEKNKEFLPRLGATIEHISVSPAGDLFCTSHSDNKIIVIHRNLEASAVIQGLVKDSNIFTGLMIDPRTKALVLNGKPGHLQFYSLQSDKQLYNLDIVQQEYINDYGLIQIELTKAAFGCYGNWLATVEQRQEKETELELQMKLWMYNKKTQGFVLNTKVNMPHEDHITALCFCNAEKSENPTLVTASKDGHFKVWILTDDSDIYKKAVGWTCDFVGSYHKYQATNCCFSEDGSLLAVSFEEIVTIWDSETWELKCTFCQRAGKIRHLCFGRLTCSKYLLGATENGILCCWNLLSCALEWSAKLNVRVMEPDLNSENIAAISHSSMGSDLFVFKPSEPRPLYIQKNISREEVQWGVFVPRDVPESFTSEAYQWLNRSQFYFLTKSQSLLTLSTKSPEEKLTPTSKQLLAEESLPTTPFYFILGKHRQQQDEKLNAALENELVQLPLTENIPAISELLHTPAHVLPSASFLCSMFVNSLLLSKESKSAEEIPDDVDMEEEKERDDSDEENDFTEKVQDTDNTDLGEDIIHQLSKSEEKELRKFRKVDYSWITAL
The following text describes a protein:
Function:
Functions as a component of the nuclear pore complex (NPC). Involved in poly(A)+ RNA transport.
Subcellular Localization:
Nucleus, nuclear pore complex.
Sequence:
MLHLSAAPPAPPPEVTATARPCLCSVGRRGDGGKMAAAGALERSFVELSGAERERPRHFREFTVCSIGTANAVAGAVKYSESAGGFYYVESGKLFSVTRNRFIHWKTSGDTLELMEESLDINLLNNAIRLKFQNCSVLPGGVYVSETQNRVIILMLTNQTVHRLLLPHPSRMYRSELVVDSQMQSIFTDIGKVDFTDPCNYQLIPAVPGISPNSTASTAWLSSDGEALFALPCASGGIFVLKLPPYDIPGMVSVVELKQSSVMQRLLTGWMPTAIRGDQSPSDRPLSLAVHCVEHDAFIFALCQDHKLRMWSYKEQMCLMVADMLEYVPVKKDLRLTAGTGHKLRLAYSPTMGLYLGIYMHAPKRGQFCIFQLVSTESNRYSLDHISSLFTSQETLIDFALTSTDIWALWHDAENQTVVKYINFEHNVAGQWNPVFMQPLPEEEIVIRDDQDPREMYLQSLFTPGQFTNEALCKALQIFCRGTERNLDLSWSELKKEVTLAVENELQGSVTEYEFSQEEFRNLQQEFWCKFYACCLQYQEALSHPLALHLNPHTNMVCLLKKGYLSFLIPSSLVDHLYLLPYENLLTEDETTISDDVDIARDVICLIKCLRLIEESVTVDMSVIMEMSCYNLQSPEKAAEQILEDMITIDVENVMEDICSKLQEIRNPIHAIGLLIREMDYETEVEMEKGFNPAQPLNIRMNLTQLYGSNTAGYIVCRGVHKIASTRFLICRDLLILQQLLMRLGDAVIWGTGQLFQAQQDLLHRTAPLLLSYYLIKWGSECLATDVPLDTLESNLQHLSVLELTDSGALMANRFVSSPQTIVELFFQEVARKHIISHLFSQPKAPLSQTGLNWPEMITAITSYLLQLLWPSNPGCLFLECLMGNCQYVQLQDYIQLLHPWCQVNVGSCRFMLGRCYLVTGEGQKALECFCQAASEVGKEEFLDRLIRSEDGEIVSTPRLQYYDKVLRLLDVIGLPELVIQLATSAITEAGDDWKSQATLRTCIFKHHLDLGHNSQAYEALTQIPDSSRQLDCLRQLVVVLCERSQLQDLVEFPYVNLHNEVVGIIESRARAVDLMTHNYYELLYAFHIYRHNYRKAGTVMFEYGMRLGREVRTLRGLEKQGNCYLAALNCLRLIRPEYAWIVQPVSGAVYDRPGASPKRNHDGECTAAPTNRQIEILELEDLEKECSLARIRLTLAQHDPSAVAVAGSSSAEEMVTLLVQAGLFDTAISLCQTFKLPLTPVFEGLAFKCIKLQFGGEAAQAEAWAWLAANQLSSVITTKESSATDEAWRLLSTYLERYKVQNNLYHHCVINKLLSHGVPLPNWLINSYKKVDAAELLRLYLNYDLLEEAVDLVSEYVDAVLGKGHQYFGIEFPLSATAPMVWLPYSSIDQLLQALGENSANSHNIALSQKILDKLEDYQQKVDKATRDLLYRRTL
The following text describes a protein:
Function:
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Miscellaneous:
MISCELLANEOUS: Present with 922 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSLEAIVFDRSEPENVSVKVLDQLLLPYTTKYVPIHTIDDGYSVIKSMQVRGAPAIAIVGSLSVLTEVQLIKHNPTSDVATLYSLVNWESTKTVLNKRLDFLLSSRPTAVNLSNSLVEIKNILKSSSDLKAFDGSLYNYVCELIDEDLANNMKMGDNGAKYLIDVLQKDGFKDEFAVLTICNTGSLATSGYGTALGVIRSLWKDSLAKTDKADSGLDNEKCPRMGHVFPLETRPYNQGSRLTAYELVYDKIPSTLITDSSIAYRIRTSPIPIKAAFVGADRIVRNGDTANKIGTLQLAVICKQFGIKFFVVAPKTTIDNVTETGDDIIVEERNPEEFKVVTGTVINPENGSLILNESGEPITGKVGIAPLEINVWNPAFDITPHELIDGIITEEGVFTKNSSGEFQLESLF
The following text describes a protein:
Function:
GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state.
Sequence:
MHDLPPDSGARRGGRGLADHSFPAGARAPGQPPSRGAAYRRACPRDGERGGGGRPRQQVSPPRSPQREPRGGQLRTPRMRPSCSRSLESLRVGAKPPPFQRWPSDSWIRCGAHRDWDEPPPRGGRMDGWSGDRARAAAPTGLQPPGCKDHGCSSGSPFRDPAGSSVIRSGKGDRQEGPSFLRPPAVTVKKLQKWMYKGRLLSLGMKGRARGTAPKVTGTQAASPNVGALKVRENRVLSVPPDQRITLTDLFENAYGSSMKGRELEELKDNIEFRGHKPLNSITVSKKRNWLYQSTLRPLNLEEENKKCQDRSHLSISPVSLPKHQLSQSFLKSSKEYCTYVVCNATNSSLSKNCALDFNEENDADDEGEIWYNPIPEDDDLGISSALSFGEADSAVLKLPAVNLSMLSGSDLMKAERHTEDSLCSSEHAGDIQTTRSNGMNPIHPAHSTEFVQQYKQKLGHKTQEGIMVEDSPMLKSPFAGSGILAATNSTELGIMEPSSPNPSPVKKGSSINWSLPDKIKSPRTVRKLSMKMKKLPEFSRKLSVKGTLNYINSPDNTPSLSKYNCREVHHTDILPSGNTTTAAKRNVISRYHLDTSVSSQQSYQKKNSMSSKYSCKGGYLSDGDSPELTTKASKHGSENKFGKGKEIISNSCSKNEIDIDAFRHYSFSDQPKCSQYISGLMSVHFYGAEDLKPPRIDSKDVFCAIQVDSVNKARTALLTCRTTFLDMDHTFNIEIENAQHLKLVVFSWEPTPRKNRVCCHGTVVLPTLFRVTKTHQLAVKLEPRGLIYVKVTLMEQWENSLHGLDINQEPIIFGVDIQKVVEKENIGLMVPLLIQKCIMEIEKRGCQVVGLYRLCGSAAVKKELREAFERDSKAVGLCENQYPDINVITGVLKDYLRELPSPLITKQLYEAVLDAMAKSPLKMSSNGCENDPGDSKYTVDLLDCLPEIEKATLKMLLDHLKLVASYHEVNKMTCQNLAVCFGPVLLSQRQEPSTHNNRVFTDSEELASALDFKKHIEVLHYLLQLWPVQRLTVKKSTDNLFPEQKSSLNYLRQKKERPHMLNLSGTDSSGVLRPRQNRLDSPLSNRYAGDWSSCGENYFLNTKENLNDVDYDDVPSEDRKIGENYSKMDGPEVMIEQPIPMSKECTFQTYLTMQTVESTVDRKNNLKDLQESIDTLIGNLERELNKNKLNMSF
The following text describes a protein:
Function:
Regulator of liver fat metabolism influencing triglyceride secretion and hepatic lipid droplet content. May function as sterol isomerase.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein.
Sequence:
MDIPPLAGKIAALSLSALPVSYALNHVSALSHPLWVALMSALILGLLFVAVYSLSHGEVSYDPLYAVFAVFAFTSVVDLIIALQEDSYVVGFMEFYTKEGEPYLRTAHGVFICYWDGTVHYLLYLAMAGAICRRKRYRNFGLYWLGSFAMSILVFLTGNILGKYSSEIRPAFFLTIPYLLVPCWAGMKVFSQPRALTRCTANMVQEEQRKGLLQRPADLALVIYLILAGFFTLFRGLVVLDCPTDACFVYIYQYEPYLRDPVAYPKVQMLMYMFYVLPFCGLAAYALTFPGCSWLPDWALVFAGGIGQAQFSHMGASMHLRTPFTYRVPEDTWGCFFVCNLLYALGPHLLAYRCLQWPAFFHQPPPSDPLALHKKQH
The following text describes a protein:
Function:
May function in recognizing stalled ribosomes, interact with stem-loop structures in stalled mRNA molecules, and effect endonucleolytic cleavage of the mRNA. May play a role in the release non-functional ribosomes and degradation of damaged mRNAs. Has endoribonuclease activity.
Subcellular Localization:
Cytoplasm.
Domain:
The N-terminal domain has the RNA-binding Sm fold. It harbors the endoribonuclease activity.
Sequence:
MQLKDRHTVEGGRERITLVPESLDDLWHLAYVLEPGDFVAGDTHRRIQRNDDQMRDTGGEREHMFVTIDVGDVEFHKFSNRLRVSGTIEDCSREDQLGLHHTLNVAEREELEVEKHWQPDQLNRLNEAVEATDQPDVAIATVEEGEAHIHVVQQYGVDEQGSFTATTGKGEQNDRGRDELFGTLADALARMQADAIILAGPGFTKQDALDHITEEYPDLQETITMVDTSAVGGRGVHEVLKRGAVEDVQEETRIAEESELIDELTTQMATDGKAAYGIDEVQKAVEFGAVEDLLILDERLRLERAGEGDWVDVDVNDLVRTVEQQGGSVTVFSHEFAPGEQLRNLGGIGAVLRYRLD
The following text describes a protein:
Function:
Degradation of inorganic polyphosphates (polyP). Releases orthophosphate processively from the ends of the polyP chain. Also has polyphosphate:ADP phosphotransferase activity, catalyzing the production of ATP from ADP and polyP.
Subcellular Localization:
Cell membrane; Peripheral membrane protein.
Domain:
The catalytic activity is found in the N-terminal region formed by subdomains I and II. The peptide that connects subdomains II and III is also essential for activity. The C-terminal domain may be important for the recognition and/or interaction with long polyP chains.
Sequence:
MDLQSMPQKPAEAFPLIAALDLGSNSFHLCLAKANIHGEVRILERLGEKVQLAAGLDEERNLSEEATQRGLDCLRRFAQFISGMPQGSVRVVATNALREARNRSDFIRRAEEVLGHPVEVISGREEARLIYLGVANSMPDSGGRRLVSDIGGGSTEFIIGQGFESELRESLQMGCVSYTQRYFRDGKITPARYAQAYTAARLELMGIENSLRRLGWQQAVGASGTIRAVALAIKAGGHGNGEISPDGLAWLKRKVLKLGDVEKLDLEGIKPDRRTIFPAGLAILEAIFDALELEQMVHSEGALREGVLYDLVGRHQHEDVRERTISSLMQRYHVDPEQASRVEAKALKVLAEVGDAWELNGELHRDLLSWGARVHEIGLDIAHYHYHKHGAYLIEHSDLAGFSRQDQQMLSLLVRGHRRNIPADKLAEFAEEGDKLVRLCIVLRFAILFHHIRGTQEMPSVRLKAEPKSLSVTFPEGWLEANPLTQADFAQEAEWLKRVGYSLNVR