lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
May regulate CAX1 cation transporter.
Subcellular Localization:
Nucleus.
Sequence:
MPATAGRVRMPANNRVHSSAALQTHGIWQSAIGYDPYAPTSKEEPKTTQQKTEDPENSYASFQGLLALARITGSNNDEARGSCKKCGRVGHLTFQCRNFLSTKEDKEKDPGAIEAAVLSGLEKIRRGVGKGEVEEVSSEEEEESESSDSDVDSEMERIIAERFGKKKGGSSVKKTSSVRKKKKRVSDESDSDSDSGDRKRRRRSMKKRSSHKRRSLSESEDEEEGRSKRRKERRGRKRDEDDSDESEDEDDRRVKRKSRKEKRRRRSRRNHSDDSDSESSEDDRRQKRRNKVAASSDSEANVSGDDVSRVGRGSSKRSEKKSRKRHHRKERE
The following text describes a protein:
Function:
Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. When present individually lacticin 3147 A2 exhibits weak activity towards L.lactis strain AM2 and L.lactis strain HP, and no activity towards L.lactis strain IFPL359, but when combined with lacticin 3147 A1 it displays strong activity towards all three strains.
Subcellular Localization:
Secreted.
Sequence:
MKEKNMKKNDTIELQLGKYLEDDMIELAEGDESHGGTTPATPAISILSAYISTNTCPTTKCTRAC
The following text describes a protein:
Function:
Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. May be involved in the fusion of the spermatozoa with the oocyte during fertilization. Also acts as a costimulatory factor for T-cells which induces the differentiation of CD4+ into T-regulatory 1 cells. T-regulatory 1 cells suppress immune responses by secreting interleukin-10, and therefore are thought to prevent autoimmunity.
Subcellular Localization:
Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane; Single-pass type I membrane protein.
Sequence:
MESPGRRECPFPSWRFPGLLLAAMVLLLSSFSDACEEPPTFEAMELIGKPKPYYEIGERVDYKCKKGYFYIPPLATHTICDRNHTWLPVSDDACYRETCPYIRDPLNGQAIPANGTYEFGYQMHFICNEGYYLIGEEILYCELKGSVAVWSGKPPICEKVLCTPPPKIKNGKHTFSEVEVFEYLDAVTYSCDPAPGPDPFSLIGESTIYCGDNSVWSRAAPECKVVKCRFPVVENGKQISGFGKKFYYKATVMFECDKGFYLDGSDTIVCDSNSTWVPPVPKCLKVLPPSSTKPPALSHSVSTSSTTKSPASSASGPRPTYKPPVSNYPGYPKPEEGILDSLDVWVIAVIVIAIVVGVAVICVVPYRYLQRRKKKGSYLTDETHREVKFTSL
The following text describes a protein:
Function:
Part of the elfADCG-ycbUVF fimbrial operon, which promotes adhesion of bacteria to different abiotic surfaces.
Miscellaneous:
MISCELLANEOUS: The operon is cryptic under classical laboratory conditions, but is functional when constitutively expressed.
Sequence:
MLKRIIWILFLLGLTWGCELFAHDGTVNISGSFRRNTCVLAQDSKQINVQLGDVSLTRFSHGNYGPEKSFIINLQDCGTDVSTVDVTFSGTPDGVQSEMLSIESGTDAASGLAIAILDDAKILIPLNQASKDYSLHSGKVPLTFYAQLRPVNSDVQSGKVNASATFVLHYD
The following text describes a protein:
Function:
Cell surface glycoprotein involved in various biological processes including angiogenesis, immune response modulation, and tissue remodeling and repair. Participates in pericyte proliferation through positive modulation of the PDGF receptor signaling pathway. Acts as a scaffold for factor X, triggering allosteric changes and the spatial re-alignment of factor X with the TF-factor VIIa complex, thereby enhancing coagulation activation. Modulates the insulin signaling pathway by interacting with insulin receptor/INSR and by diminishing its capacity to be autophosphorylated in response to insulin. Also regulates LPS-induced inflammatory responses in macrophages by favoring production of proinflammatory cytokines.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MLLRLLLAWVAAVPALGQVPWTPEPRAACGPSSCYALFPRRRTFLEAWRACRELGGNLATPRTPEEAQRVDSLVGVGPANGLLWIGLQRQARQCQPQRPLRGFIWTTGDQDTAFTNWAQPATEGPCPAQRCAALEASGEHRWLEGSCTLAVDGYLCQFGFEGACPALPLEVGQAGPAVYTTPFNLVSSEFEWLPFGSVAAVQCQAGRGASLLCVKQPSGGVGWSQTGPLCPGTGCGPDNGGCEHECVEEVDGAVSCRCSEGFRLAADGHSCEDPCAQAPCEQQCEPGGPQGYSCHCRLGFRPAEDDPHRCVDTDECQIAGVCQQMCVNYVGGFECYCSEGHELEADGISCSPAGAMGAQASQDLRDELLDDGEEGEDEEEPWEDFDGTWTEEQGILWLAPTHPPDFGLPYRPNFPQDGEPQRLHLEPTWPPPLSAPRGPYHSSVVSATRPMVISATRPTLPSAHKTSVISATRPPLSPVHPPAMAPATPPAVFSEHQIPKIKANYPDLPFGHKPGITSATHPARSPPYQPPIISTNYPQVFPPHQAPMSPDTHTITYLPPVPPHLDPGDTTSKAHQHPLLPDAPGIRTQAPQLSVSALQPPLPTNSRSSVHETPVPAANQPPAFPSSPLPPQRPTNQTSSISPTHSYSRAPLVPREGVPSPKSVPQLPSVPSTAAPTALAESGLAGQSQRDDRWLLVALLVPTCVFLVVLLALGIVYCTRCGSHAPNKRITDCYRWVTHAGNKSSTEPMPPRGSLTGVQTCRTSV
The following text describes a protein:
Function:
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Subcellular Localization:
Cytoplasm.
Sequence:
MGIDEAGRGPVIGPMVVAAVILKRREAKRLKEMGVTDSKLLSAERREELFPMIIESAESYLIKVIEPKRIDEAVSKNMLNLLEAEVMSELIRELRPARVIVDSPMRNCRKFSDVLREFLGDSSVKIIAENKADSKYIQVASASIIAKVERDRRIRELSELTGVEIGSGYPGDPKTREAIRMILKGAEFPRDQVRWKWATINRLLEEIRGNDLTEFLD
The following text describes a protein:
Function:
Glucosidase involved in the degradation of cellulosic biomass. Active on lichenan (By similarity).
Subcellular Localization:
Cell membrane; Single-pass type II membrane protein.
Sequence:
MPTHSRSRDRYGGRDSDREARYDYDYARRRYATDDDDDYDDDELEHDLTERRYRRDGYRPPRESRARGYYERDAEGAADEELLGNERDPGPRASRSYGDDYDARRREHSRAREAPRRSERHRDRDREGRSRRRAYEDDGRHRTRDGRRDRGRESDGEARRSRRREAGRETAARKHRSSDSTNSASHLLSADALAKLGAQYEKEERRKREIAKDAAKAERKRQKKLAVVGEETRALRDPPGESHRDRTKARVASGAYLEEGRSPEMRVRHRGGGGPAMEARWRKEGSWGGTMDDSGGGRPFWKRKRWIGLGALIIILVIVIPVAVVVSKKHDNKSDPADSQGTSPGKSNLDGLSHDSIPAYAQGTYLDPWTWYDTTDFNVTFTNETVGGLSIMGLNSTWDDSARPNDNVPPLNEPFPYGSQPIRGVNLGGWLSIEPFIVPSLFDSYSSVSGIIDEWTLSKRLGSSAASTLEKHYATFITEQDFADIRDAGLDHVRIQYSYWAVATYDDDPYVAKISWRYLLRAIEYCRKYGLRVNLDPHGIPGSQNGWNHSGREGVIGWLNGTDGELNRNRSLAVHDSVSKFFAQDRYKNIVTIYGLVNEPLMLSLSIEDVLDWTTEATKLVQKNGITAYVALHDGFLNLSKWKSMLKNRPDKMLLDTHQYTIFNTGQIGLNHTAKVNLICNDWYNMIKEINSTSTGWGPTICGEWSQADTDCAKYLNNVGRGTRWEGTFSLTDSTQYCPTADTGPPCSCANANADVSKYSADYKKFLQTYAEAQMSAFETGQGWFYWTWRTESAAQWSYRTAWKNGFMPAKAYAPSFRCGDAVPDFGDLPEYY
The following text describes a protein:
Function:
Negatively regulates early sporulation-specific genes (By similarity). TOR signaling pathway component that contributes to morphogenesis as a regulator of this key morphogenetic pathway. Required for growth and hyphal formation at pH 9, for full virulence in a mouse model of systemic infection and for biofilm formation. Involved in chlamydospore formation, distinctive morphological feature of the fungal pathogen C.albicans that can be induced to form in oxygen-limited environments and has been reported in clinical specimens.
Subcellular Localization:
Cytoplasm.
Sequence:
MSTLIPTASACYSLQLPPTEKDDRLNLNVRTGSASTLYNSLIFVHGGLTIGLELLNYTIPELNEIFYNRINISASKYKTVEKYLSGELFYLSLIERNWSRVVLEELEIRPKPRLLHQICAFNNCLYLFGGLALSQENDEDPTLVPCNDLWEFDLVLKKWTLLDDGSNYELDDAVPSPRFNHKLTVISSLSFANRKDHFGLFIAGGKDKQSNEIYDNSIFDLVEKRYVGSQPFRLVATTGDDTKDKETGLNEFVSNPEHFLNVDQTRNAILSITDDADTPNRKQNKNPSNHHESIVVYGPTRQTGDCQNSLVSFKVGKREIKGGKVLRLHKNSRVAKLKQSIIPYNLRYPTAGLFGQNVVLTGFLPDEYEISIFVYNRPTGKWSRLNIFCSHEYGSHRFWGGFAWQSHHKVILIGNSMTSRTTSSVRFFSIMLTVSLPITNILVSSELSKGRSNNRTSSFVSHGEQRHHRNKSQNDSLLKAELSLESTTEDSTDSSSDKTAESVLDAPVPLANSRRQSFSSLGSDKSPTAVSFSDYVHYAAPKTTYTTIRSVFPPEAITLGRNAFNRIGDLIADIELVSCNGDRIPVSSAVLMERWGQHFISLLAKGYINAVDKFETDQALGLDENQRLRSKSSNSESSSSDIPKLKLSLSESLLSSSSGEHDKKEKMGLSSAHKPQKDVPQFRLPFQDSSESVNREEGSDCSKDRKTGGSSVSTAIDPHHVMPRKNSTSSFQSNSSSLLTSHLQDIPPQLPLPDEQIPAVPAAPVSYRSASRKNSQDHSSPRSSLIHTLTVLRNIPVSKSPRESPFSSPRPSMSGPSGGSADLFSSPFPSLKANYGKPPSNLRKKSYDMNDGTIESSLDSFSSGKSSMAKVSSVPGENPDSDESSIGFQEFNKNPISMFDNALLNFDNIDSENFRMEPSLIPRKLYIPFMTLTVKAFCEYLYTGQIGNKWLLAPTLMDNLLISKFYRVPLLYDLISEILFGVIGKKEAYIIGEARKLKARYFKLLRGANIPIDSNYEFPMDEYDGFLDTVDDGYLDITLLKKASKIHADSVAMSLKKKSVTSNNSRNASIRKEGSTTAESVLEEGEKQEEIVSKDDEDESRTGSTSEEDEVDKEYGLVYLEAKDKSLPTIGPRSKSIFDRQGLAAIEKLEEEQNDHQVHSIVEGEDHENLITLDELVASDAPSDYAIDLIFETATLVTDMKMLLRTSNLKAMTAKFRKCKADIEKEMADIEYQLTQMPSGSRNLAMKSANQLKESQLQSKSSPIIPTVSTVTPSPLPSISGVPSPRLPQQQLPEAQLPKLTKSTSSLSRIASHTSFKALRSMTDVTPMEKSTSDKSFRGKLQQTMLSRTPTNRNEDQDSSSASSIKSSSKKRGIFGLLTGLKR
The following text describes a protein:
Function:
Acts as a molecular chaperone for mitochondrial complex I assembly. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Is involved in the initial steps of cilia formation, including removal of CP110 from the mother centrioles, docking of membrane vesicles to the mother centrioles, and establishment of the transition zone.
Subcellular Localization:
Mitochondrion.
Sequence:
MGWSQRLFGVIRRALSKEVKEQVGTDRFGNKYYYIPEYKNWRGQTIREKRIVEAANKSEIDYEVGDIPTEWEAWIRKTRQTPPTMEEIMKNEKCREEIQMKSQDFYEKEKLLQEESNKELPPPVQTQIKGHASAPYFGKDEPSESPTSTGKTFQPGSWMPHGDKGHSQ
The following text describes a protein:
Function:
Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose.
Subcellular Localization:
Cell membrane; Single-pass type II membrane protein.
Sequence:
MSFYELRRGKYAKLDAPGDDDVDTPTRFSSESTGTLEDLEEHDPLAFDSRLKRKKSAGDLKVRKASFKDAEIAKQGSFARRKTLGRCCCWFLTFVAAVVLLLATGGIWAWKVSVPEDGLSPPWYPAPKGGADKLWEESYKKAAAMVKEMTLPEKVNLTTGTGWSMDMCVGQVGGVPRLKFPSLCLQDGPLGLRFADNITAFPAGITVGATWSKELMYLRGKAHGKEARLKGVHVLLGPAMGPLGRMPAGGRNWEGFGSDPVLQGIAAAQTIKGIQEEGVIATAKHYVGNEQEHFRQAWEWGLPNAISSNMDDRTLHEIYAWPFADSIKAGVGSVMCSYNQVNASYACQNSKLLNGVLKDELGFQGFVQSDWLAQRAGVASALAGLDMTMPGDGLRWAKGNSLWGPELTKSVLNGSVPVDRLDDMVTRIVASWYQVGQDKWGEDSGPNFSSWTNDRIGKLHEGSPSDKSMGVVNKYINAQGEGEDAHSHIVRRVAAEGTVLLKNEGRVLPLDRKGWKKGKRQTKFRVGIFGEDARLPRDGINHCPDQSCNEGTLASGWGSGAVNYSYLVEPMSAIREAFDKDSVYVTDWVENKLPSQKEILQEQDLCIVFANADAGEGYLHYEGIRGDRNDLYLQKGGDKLIQDVAKDCGEGMGDVVVVIHAVGPVIMENFADIMNVRAIVLANLPGTESGNAIVDILFGDVNPSGRLPYTIAKKEEDYGPGSKIKYLPSVSDGLAPQQNFSEGLYIDYRHFDKQDIAPRYEFGYGLSYTQFELLSLSIDAKGKKTPLPAARPAGIVPPSYSTEVPAPESALFPEGFHRVEKYIYPWIESTKGIKKSDVVASQLQSPLSDAGGGPGGNPDLYTAILAVSASVSNIGSVDGSTVVQLYVSLPQGYKDHETGEPVDFPVRVLRGFEKVALKHGDQNRVTFEVTRRDLSYWDVKRQNWVMPSTGEIKIAVGFSSRNLPLEGTW
The following text describes a protein:
Function:
Under low copper conditions, represses the expression of lpqS, Rv2963, mymT, socA, socB, mmcO and its own expression. In the presence of copper, RicR dissociates from DNA, leading to the expression of the target genes. Members of the RicR regulon are important for copper resistance during infections and full virulence in a mouse model of infection.
Miscellaneous:
MISCELLANEOUS: Constitutive repression of the RicR regulon by a 'copper-blind' RicR results in extreme copper sensitivity in vitro and attenuation of virulence in mice.
Subcellular Localization:
Cytoplasm.
Sequence:
MTAAHGYTQQKDNYAKRLRRVEGQVRGIARMIEEDKYCIDVLTQISAVTSALRSVALNLLDEHLSHCVTRAVAEGGPGADGKLAEASAAIARLVRS
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MAIPKSSLSPVLWEQDSFLQVKVKEEEASDSQSQESSPSFTAHPEAARLRFRHFRYEEASSPHQALAQLRELCCQWLRPESSSKEQMLELLVLEQFLGALPPEIQAWVGAQCPKSGKEAAVLVEDMTQLLDRRGWEPGMDREEASCKQSNTDELEPPEMATETIMGSVSPESTLAQTCKPENSSESQPELLGALWVKSTAQEVDLKKALEPRMDAPNDQPDHESDASGNDCSMLPKFPSEDKTSSEEKCGPLLDNETVPLDTCSEKKSSKDSECMRTLQNTSAQETHQKNHSQKTPYTCIECGKVFSRSTHLVQHQVVHTGAKPHACKECGKAFSRVAHLTQHQRIHTGEKPYKCEECGKTFSRSTHLTQHQRVHTGERPYECDTCGKAFSQSTHLTQHQRIHTGEKPYRCEVCGKAFSDCSALVRHLRVHSGEKPYRCKDCPKAFAQSSSLIEHQRTHTGEKPYKCSDCGKAFSRSSALMMHLKLHITVSRSTP
The following text describes a protein:
Function:
AMP deaminase plays a critical role in energy metabolism. Catalyzes the deamination of AMP to IMP and plays an important role in the purine nucleotide cycle.
Sequence:
MPSFMRVAISGEETSGVPFADLHEASDALIKALLIRAKYMKASHQSFPTITKRFLRRVCDEEHDYLAEDDSIVHQKKESILDHPIDAPSGHGAPFECTMEPPANYHLQVRNGVFQEEEEGEDENDGSLFAPPFTLAEFIADQNLLFALVADGPIKSFCYRRLNYLTSKHDLHVLLNEIREAATQKQVSHRDFYNVRKVDTHVHASSCMSQKHLLRFIKKKMKNEMGVAVCKLADGTSMTLQQARFDCLNLTAFDLSVDMLDVHCDRNTFHRFDKFNAKYNPVGESRLREIFIKTDNYMEGRYFAEILKEVMSDLEESKYQNAEYRLSIYGRSRDEWDKLAAWAVKYNMYSDNVRWLVQVPRLFDVYKVNGQVENFEELITNIFEPLFEVTNDPSSHPDLHRFLQYVTGIDSVDDESKPERVMFDKDAALPNEWTKHDNPSYAYYLYYMFANLVVLNNFRKARGFSTFVLRPHCGEAGPVHHLVTGFMVGQNISHGLLLRKAPVLQYLYYLSQIGIAMSPLSNNSLFLNYQRNPLIEFLGRGLLVSLSTDDPLQFHFTKEPLIEEYSIAAQVWKLSSVEMCELARNSVIMSGFPHEIKKFWLGPNYTKEGVAGNDMSRTNVPDIRVAFRHETFLEELSTLFHTLKDLDCMDAAFN
The following text describes a protein:
Function:
Two-heme-containing cytochrome. Catalyzes ascorbate-dependent trans-membrane electron transfer by utilizing a concerted H(+)/e(-) transfer mechanism.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MKGGAAPASNKAAMDARTLVAHVLAVAAIVLVLLWCIHFRGGLALRSQDKPLIFNVHPVLMVLGPIVLAGEAILSYRSLPLARDARKKVHLALHAAGLAGGVLGVYAVFKFHVESGIPNLYSLHSWVGIATVTLYGLQWTAGFLTYFFPGASPTTRRRTLPWHAVFGLLIFVLAVGTAQLGFLEKLTFMQGQPLRLPKYGAEALLINFTAVVVLLLGVAVVLATVNIDGTREGELPQRQRRERSCMDGQPGGKGGASAVAAPSRCMDERVEEEPRRRGRRGKRW
The following text describes a protein:
Function:
Also able to convert testosterone (T) into 5-alpha-dihydrotestosterone (DHT); Plays a key role in early steps of protein N-linked glycosylation by being involved in the conversion of polyprenol into dolichol. Acts as a polyprenal reductase that mediates the reduction of polyprenal into dolichal in a NADP-dependent mechanism. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-glycosylation.
Subcellular Localization:
Endoplasmic reticulum membrane.
Sequence:
MASSGRAELWALNRLRLLWLTPAAAFLLTLLLQLLPLGLLLGRAFFQDLIRFGKTSVGGPPRPAACLLWNGFLLWCLTPSLFLAASFPSWLYGLLRILRAAQFQGGKLALSAFLVLVFPWLRISVFSNGTTHIVQYCFGLAYYVLVGLSVLSQVPMDSRNAYVIGKKLLIQVRWFHILGMMIFIWPSAHQYKCHVILGNLRVNKAGVVIHCNHRIPFGDWFELVTYVFFNPALPAFLSHKFYKSKFVSYPKHRKAFLSFLF
The following text describes a protein:
Function:
Involved in the assembly of cytochrome c oxidase.
Subcellular Localization:
Mitochondrion intermembrane space. Note=Imported into the mitochondria via the mitochondrial MIA40-ERV1 machinery.
Domain:
The twin Cx9C motifs are involved in the recognition by the mitochondrial MIA40-ERV1 disulfide relay system and the subsequent transfer of disulfide bonds by dithiol/disulfide exchange reactions to the newly imported protein.
Sequence:
MVASCKDQKKAVAICLQRSPCVMIERHNPQECLDNPELNKDLPELCIAQMKAFLDCKRGIVDMTKRFTGNAPLSTGKYDQQYENLCKGKFDPREEMEKLKLLNSQQKD
The following text describes a protein:
Function:
Involved in the synthesis of glucuronoxylan hemicellulose in secondary cell walls.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MRPGGTQCDPWVKSDFLTSGKLTEATHCSKPISVFRILMQCTFCIAATILGFRLSCEADLVSVLRVEEAYGQFSRIYLEEFHVANGILLKGQNTTDAPEGNSSRLYVGRHPILKRPWPHPNQMEMAQAYNMIARVQLEQHRLYEIKSWKPIIAITPTYLRTFQSLHLAGLMCTLSLVRGPVTWIVIEAGGISAETVELLKLARVHKLVHLGASAHLPRSLQDRRILDSHLRVEGLRYVREQNLEGVVVFADVGNVYSMQFFNEIQKISWVGSVPVGILGHAGFEDPALSRHRDSLTESGVRVPSRRVVASPQAMLAFRNGVVQVQGPACDSFGNITGWHAIGSLSLDDELMKTNSAEETNLVWAGFVLNARAVWVSDPDRPKWIQEWIKWACAEEGVYIDWRSLLRDEAKVETLGPCRSDKEVFVWWARIEAHSDSKYPSRWDLDSPPEVVVPAKKTPWPDKVLSPSSQLPPVGKRRDGNRSDGRDGRTRQSQRRPHSVKGKTLGNQRETIATKNT
The following text describes a protein:
Function:
Putative antitoxin component of a type II toxin-antitoxin (TA) system. Its cognate toxin would be HigB2.
Sequence:
MAMTLRDMDAVRPVNREAVDRHKARMRDEVRAFRLRELRAAQSLTQVQVAALAHIRQSRVSSIENGDIGSAQVNTLRKYVSALGGELDITVRLGDETFTLA
The following text describes a protein:
Function:
MFS-type transporter; part of the gene cluster that mediates the biosynthesis of fumigermin that inhibits germination of spores of the inducing S.rapamycinicus, and thus helps the fungus to defend resources in the shared habitat against a bacterial competitor. May be involved in the secretion of fumigermin (Probable).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MTVAISNPAAPPVSARAYLSVIGGTCALLCTVGFVVAFGVFQGYYTEHLLRGMSEFDIPWIGSASIFLLYVSAPICGVLVDRFGPKVLLIAGSIGVLVAIFMISLCSQYYQIFLAQAVLLGISMGFVTWPPFAVVSRNLPHHRGLALGVITGGSSVGGIVWSIMIEELLTKRNLGFPWTVRVLGFTMLPLLAFACISITEPPKQSQPQPRPALEATVEGGSASPTPKPEYASLPLLRSTVFISICVGFGLAFLGLFNPFFYISSYAAGHGASAQTSSYMISIMNAATLFGRVIPGIVADRVGHYNVMIFVLLASGITSFCWTEVRSLTGLVIWSIAYGFSSGAILSLQGACAGKIATPQNQGKAIGFLQGSLAVTVLVGSPIGGQLLGHYGYLSLSMFTGATLVMGAVVMGYARLCLNRSPMEAHQFRFLLAPN
The following text describes a protein:
Function:
Component of the DASH complex that connects microtubules with kinetochores and couples microtubule depolymerisation to chromosome movement; it is involved in retrieving kinetochores to the spindle poles before their re-orientation on the spindle in early mitosis and allows microtubule depolymerization to pull chromosomes apart and resist detachment during anaphase (By similarity). Kinetochores, consisting of a centromere-associated inner segment and a microtubule-contacting outer segment, play a crucial role in chromosome segregation by mediating the physical connection between centromeric DNA and microtubules (By similarity). Kinetochores also serve as an input point for the spindle assembly checkpoint, which delays anaphase until all chromosomes have bioriented on the mitotic spindle (By similarity).
Subcellular Localization:
Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle. Nucleus.
Sequence:
MSRPGPSAPRQLTLTEELEKLEQQITLTLQEIDSNFAKAHRIVTTSILPLVEQYGEHSRAVWEATKFWKQFFEASANVSLSGYEELVDGGETSPAEETAHDQEEEQTTAIHDHTQEPSQYTPRPQTSAGGHDTTTLSSVDDQSSVLYDRSRAAQQQPAQLQHHDDSSVLTDRDGDLAGSTPHAPPRGIKIEQQQQPQPAGDEMDIDMDEEDSELIFQQHTTRLLGETSRYYDDDHGFEQGEEEEDEEEEEEEEEEEEGGGGGEVGDDSVLGARSRSKNPVLHRMQNKTYRIMATPHKGISAVKPNTTSNRGVSPVRWKIQPTTPKIKQEDTEKKRPLWEDSPSSSPEPAPPQLRSAAFMSPMRLAYGGPKTSEKLQAAAKAIAAPRTPGVSVQTPAVGRKTKDVFGGVGMQSATKAIVDAKAAAKEKRKSILEEITWESDEDLGVSPPKTIQFAVPASRLMQTPAREASRRIVDDLLLTAGGGDLIEGSSEYSPSVVKMNQDIMDESF
The following text describes a protein:
Function:
Has both L-asparaginase and beta-aspartyl peptidase activity. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine.
Sequence:
MPRPVLLIHGGAGDISDSRIAGKFAGIKQALRSAWGLLSPDNGSGGGSALDAVEAAVRSMELDENFNAGYGSCLNTSGQVELEASLMEGRDLRAGCITLLRDVMHPITVARRLMEKQRHTFLGGAAAQELALATGSERLQPGALVTEGARLTLKEFEDQVAQGKDPFFARTELTDDKPVPKTDPSGETVGAVAMDASGQIVVGTSTGGITGKWPGRIGDTPILGSGTYADNCRGGVSTTGHGETLMRYNLAQRILSAMEYQGLSAQAAADKECREMTKRLGGTGGAIVVGHSGDLGISFTSRRMAWGYVQDGTIFYGIEGQVVHQEPFTLST
The following text describes a protein:
Function:
Involved in resistance to carboplatin and cisplatin. Is probably involved in a pathway contributing to genomic integrity.
Miscellaneous:
MISCELLANEOUS: Present with 450 molecules/cell in log phase SD medium.
Sequence:
MSSDGMNRDVSNSKPNVRFAAPQRLSVAHPAISSPLHMPMSKSSRKPLVRTKIRLDPGHSALDWHSLTSNPANYYTKFVSLQLIQDLLDDPVFQKDNFKFSPSQLKNQLLVQKIPLYKIMPPLRINRKIVKKHCKGEDELWCVINGKVYDISSYLKFHPGGTDILIKHRNSDDLITYFNKYHQWVNYEKLLQVCFIGVVCE
The following text describes a protein:
Function:
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (Probable). Required for the efficient operation of ferredoxin-dependent plastoquinone reduction. Forms the electron donor-binding subcomplex in association with the NDHT and NDHU subunits.
Subcellular Localization:
Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side.
Sequence:
MATSSITIPTIRTPIHRSKFLGQTHQFSTVNRSVFPPPKQQSKLYQVKAMGKFNLWEVMGGRGLCNGEKGIEKELQRNIEDEQETSKAENNETERESDDSNLSFKVPEDGFEKEMMGLTGGFPGGEKGLKTFIEKNPPPPPPPPPAKQGSDASAVATDKKPKAPKLPLLMPGMIAIVKNQNSPYHMYCGIVQRITDGKAGVLFEGGNWDRLITFRLEELERREKGPPGKNPKSCILEPLIEQMQKEEAAP
The following text describes a protein:
Function:
Functions as a component of the nuclear pore complex (NPC); Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Required for the assembly of peripheral proteins into the NPC. May anchor NUP62 to the NPC. Involved in nephrogenesis.
Subcellular Localization:
Chromosome, centromere, kinetochore. Nucleus, nuclear pore complex. Nucleus membrane.
Sequence:
MDPNLSDSLGYSLSQLSTPVPERSRSRFSNRSFLQRTQDSISPSSRRVSPWPPSRRNGSRVAVADTLIYSATDCGTGLLRRSVNASANPGATDVTLFTAAALGSEHPAVSATAGIYAEFMEAYHSYASEHDILDLLDKYEALCEKYLAKLKKVAERMLSRTGDAVWQETQSCLTLLTEERNTWQLTKVLLRDQLESVELLDDEEQMTVDGVGGKETSDRQIVDALYAKDALIRRAQLVVDWLERCAALDHESEDRVEYFADVGGCAWENTLYRLQSQGDGCVPNCVSQLDPDAPSRLQQPLHDEDREDECRLFRNVFCHLRKGQLQRAQELAMENGHHWLAAALEGWKAHHDPNYGGLLNGASSLQPAEGNPYRDLWKEAAWDAVSGPNCSVYERAVYAALCGNLKGLVPVCHKWKDLLWAHMRLLVDVGIEQELRTATEQSRSLEPLPPGYPNQRRTLQEVFRDLQATLGFARQGELGLEYVVQRCVILNDVRGMAEEMKEWLANEERRVNVPMQTVRFAAHMVLLARRVGGSQAPSREACDAVVRCYVSQLVSEGRAELVATYAATLPTADQVSSYVRLLKDMPEDDPEQRELCLTLAREAGLNVPLITRTLVEQVRLADDDFAAPEEASARLRSPDVTPEDLRKVASLDWLLFDPSTRGEALKQANALMRGFVCLGKVAAAREAFRRLPSDSVDVVSAQWPRTTEGRSAAADDENAVREFFCFQALLQAHQSFQDWFEQFHRHKPAPPEEVAPGARFSEKVAHEHRVRSHQLELQQWRGTVSTLAREVEKDVYNVLLFVDGGWMMDQREQADDARRRQMEALRRLCIPQLTFLLHEALLESGLAADCPRLLDVVASEKQGLYREFGHEELQTLLRRSKGVSLPLLDEGLDALGYPLE
The following text describes a protein:
Function:
Probably involved in membrane trafficking.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle, secretory vesicle membrane; Multi-pass membrane protein.
Sequence:
MPSLPSTGIEMTASTGSHMGNDTKHRENAPHNIASFHFQSSGSVPPATNSGLLQLPHESATAPIDITLDSSANQVDLGTVQVEKYYPSISPAADVCLRYQCHEYSLICFLDAQELGRREEATARVGIVIEEKNWPPFFPIIHHDIANEIRIHLQKLQYAAFTAFLGLFVCLLWNTIALTIAWIREGDVKIWFLSIIYFISGVPGAYILWYRPLCRAFRTEGVVQFAGFFLFYKLHIIFCVFAAVSPRVVFDGKSLTGILPTLDLMSDDVLVGIFYFVGFGLFCLESVLSILVIGMAFLI
The following text describes a protein:
Function:
Beta-1,4-glucuronyltransferase involved in O-mannosylation of alpha-dystroglycan (DAG1). Transfers a glucuronic acid (GlcA) residue onto a xylose (Xyl) acceptor to produce the glucuronyl-beta-1,4-xylose-beta disaccharide primer, which is further elongated by LARGE1, during synthesis of phosphorylated O-mannosyl glycan. Phosphorylated O-mannosyl glycan is a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity. Required for axon guidance; via its function in O-mannosylation of alpha-dystroglycan (DAG1).
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein. Note=Localizes near the trans-Golgi apparatus.
Sequence:
MQMSYAIRCAFYQLLLAALMLVAMLQLLYLSLLSGLHGQEEQDQYFEFFPPSPRSVDQVKAQLRTALASGGVLDASGDYRVYRGLLKTTMDPNDVILATHASVDNLLHLSGLLERWEGPLSVSVFAATKEEAQLATVLTYALSSHCPDMRARVAMHLVCPSRYEAAVPDPREPGEFALLRSCQEVFDKLARVAQPGVNYALGTNVSYPNNLLRNLAREGANYALVIDVDMVPSEGLWRSLREMLDQSKQWAGTALVVPAFEIRRARRMPMNKNELLQLYQVGEVRPFYYGLCTPCQAPTNYSRWVNLPEETLLRPAYVVPWQDPWEPFYVAGGKVPTFDERFRQYGFNRISQACELHVAGFDFEVLNEGFLVHKGFKEVLKFHPQKEAENQHNKILYRQFKQELKAKYPDSPRHC
The following text describes a protein:
Function:
Possesses E3 ubiqutin-protein ligase activity in vitro. Acts as negative regulator of salinity stress tolerance mediated by the ubiquitin-proteasome degradation pathway.
Miscellaneous:
MISCELLANEOUS: Plants over-expressing SIRP1 exhibit enhanced sensitivity to seed germination and root growth inhibition by salt stress.
Subcellular Localization:
Cytoplasm.
Domain:
The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme.
Sequence:
MAEAAITRYWCHECEQAIEEAMVDEIKCPSCGGGFVEEMTDEEIERLTNRQPEPGFSQWNPIEHPGETMDSDDEDNDLGREFEGFIRRHRRASTLRRVLDSIHDDLADDQERDSSILINAFNQALALQGSVLDPDEGQGDQGGSTNDDGLLEEYVLGAGLSLLLQHLAESDPSRNGTPPAKKEAVEALPTVKIEEVVSCSVCLDDLEVGSQAKQMPCEHKFHSSCILPWLELHSSCPVCRFELPSEETKDLNEPSNIGRVEDSHEEVRADGPGNVSESSNRPWAIVPWLNELFSTREAQNAGGVSTDQQSPHTSGTNPNAGHS
The following text describes a protein:
Function:
Anaerobic nitric oxide reductase; uses NADH to detoxify nitric oxide (NO), protecting several 4Fe-4S NO-sensitive enzymes. Has at least 2 reductase partners, only one of which (NorW, flavorubredoxin reductase) has been identified. NO probably binds to the di-iron center; electrons enter from the NorW at rubredoxin and are transferred sequentially to the FMN center and the di-iron center. Also able to function as an aerobic oxygen reductase.
Subcellular Localization:
Cytoplasm.
Sequence:
MSILVKNNIHWVGQRDWEVRDFHGTEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRSEIDLADIDYIIINHAEEDHAGALTELMAQIPDTPIYCTANAIDSINGHHHHPEWNFKVVKTGDTLDIGNGKQLIFVETPMLHWPDSMMTYMTGDAVLFSNDAFGQHYCDERLFNDEVDQTELFEQCQRYYANILTPFSRLVTPKITEILGFNLPVDMIATSHGVVWRDNPTQIVELYLKWATDYQEDRITIFYDTMSNNTRMMADAIAQGINEVDPNVAVKIFNVARSDKNEILTNVFRSKGVLVGTSTMNNVMMPKIAGLVEEMTGLRFRNKRASAFGSHGWSGGAVDRLSTRLQDAGFEMSLSLKAKWRPDLDALELCRQHGRDIARQWALAPLPETTQQIAPVEETITCTAADLGPKMQCSVCQWIYDPALGEPLQDVAPGTPWNDVPDNFLCPECSLGKDVFDVLATEAK