lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid. DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan. The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde. EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline. EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine. Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A. Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus.
Sequence:
MLIERGLLSIMASKCSGTWSTYKTYTTANGCPFMKPEGPPADGRTLALNDHHLVESLAHFNREKIPERAVHAKGAAAYGEFEVTADISDICNIDMLLGVGKKTPCVTRFSTTGLERGSAEGMRDLKGMATKFYTKEGNWDWVCLNFPFFFIRDPLKFPSLMHAQRRDPRTNLLNPNMYWDWVTSNHESLHMVLLQFSDFGTMFNWRSLSGYMGHAYKWVMPNGSFKYVHIFLSSDRGPNFSQGEQAKDNSDLDPDHATRDLYEAIERGDYPTWTANVQVVDPAEAPDLGFNILDVTKHWNLGTYPKDLPKIPSRPFGKLTLNRIPDNFFAEVEQLAFSPSNMVPGVLPSEDPILQARMFAYPDAQRYRLGPNHHKIPVNQCPMTFNPTLRDGTGTFDANYGSLPGYVSESQGVNFARPQEHDPKFNAWLSQLSSRPWMQTNENDYKFPRDFYNALPEFRSQEFQDKMVENIIASVAQTRREIREKVYHTFHLVDPELSARVKRGVEKMDASFKQVSLSRL
The following text describes a protein:
Function:
An anti-sigma factor for extracytoplasmic function (ECF) sigma factor SigK. ECF sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut extracytoplasmically (site-1 protease, S1P), then within the membrane itself (site-2 protease, S2P, Rip1), while cytoplasmic proteases finish degrading the regulatory protein, liberating the sigma factor.
Subcellular Localization:
Cell membrane; Single-pass membrane protein.
Domain:
The cytosolic domain interacts with sigma factor SigK.
Sequence:
MTEHTDFELLELATPYALNAVSDDERADIDRRVAAAPSPVAAAFNDEVRAVRETMAVVSAATTAEPPAHLRTAILDATKPEVRRQSRWRTAAFASAAAIAVGLGAFGLGVLTRPSPPPTVAEQVLTAPDVRTVSRPLGAGTATVVFSRDRNTGLLVMNNVAPPSRGTVYQMWLLGGAKGPRSAGTMGTAAVTPSTTATLTDLGASTALAFTVEPGTGSPQPTGTILAELPLG
The following text describes a protein:
Function:
Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Sequence:
MVGQGSGAGSFPSLGALGLHWTRLLSRGILGVVVSSYQFFAGTQVAQTHRTTISQTPKRASGHVANKAGGRGPGRCSAAVCDTRSPRVASAPRDPGMVRAGAVGSHLPTSGLDIFGDLRKMNKRQLYYQVLNFAMIVSSALMIWKGLIVLTGSESPIVVVLSGSMEPAFHRGDLLFLTNFREDPIRAGEIVVFKVEGRDIPIVHRVIKVHEKDNGDIKFLTKGDNNEVDDRGCTKKGKTGSKRRTWWEEPEGFYRMLAWSP
The following text describes a protein:
Function:
Acts as a second functional copy of EDS1. Can mediate HRT-mediated resistance to turnip crinkle virus.
Miscellaneous:
MISCELLANEOUS: Ecotypes cv. Landsberg erecta and cv. Di-17 express a probably non-functional truncated protein comprising of only the first 162 amino acids. This protein is not expressed in cv. Wassilewskija.
Subcellular Localization:
Nucleus. Cytoplasm. Note=Found in both the nucleus and diffuse in the cytosol when associated with PAD4 and only in the nucleus when associated with SAG101.
Sequence:
MAFEALTGVNGDLVTISWMASKGANQTEHYLKEEVGGTVFFAFRASFSSEDLFATENTSPFGEIKMKRNQFPCMRSIGNDVDTTVNEAFLKSLEVLIGPRTSFHASVQSAVDRKQQVVFTGHSFGGATAILATVWYLETYFIRDAYAAPEPRCVTFGAPLVGDYIFKHALGRENWSRFFVNFVTRFDIVPRIMLARKTTIEQTLSYVLGKLDSTRAPIHESDQVITEFYTRVMRDTYTVASKAVCQLIGNGEAFLETLSSFYELSPYRPVGTFVFSTQKRLVVVNNSDAILQMLFYTCQSNDEQELSVIPFLSIRDHHGYEELVQSIGIKLLNHLDLHNPLLDGENSIGSALDDLGMSTRARQCIHAALEAEKQRVENQKKIETKRDQIVERLTWIVEVYKPKCQAHKNGYYDSFKDSNEENDFKANVKRVELAGIFDEVLGLVKKGQLPDGFEGSRGWINLATQYRRLIEPLDISNYHGQLKNEDTGPYMLHGRPSRYKYAQRGYEHDILKPTGMIAKDVFWSKVNGLNLGLQQDIQEILKNSGSECGSCFWAEVEELKGKPYEEVQVRFKTLEGLLEGWIKDGEVDEKEIFLEGSTFRKWWNTLPDSHKIHAPLYPRERMMDETRAT
The following text describes a protein:
Function:
Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified. Prefers the monoglycosylated Muc5AC-3 as substrate. Might have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Domain:
There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding; The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.
Sequence:
MRVSTIRSGRICRLALCLLVLLPLLYLLANWSDHHKRVQEAYHTRFGGPKFAHQRLEGRPREVPKLVDGLGNFEPKDVKPRSGPGENGEAHSLSPDKKHMSDASEMEYGMNIACSDEISMHRSVRDTRLEECRHWDYPFDLPRTSVIIVFHNEGFSVLMRTVHSVIDRSPTHMLHEIILVDDFSDKENLRSQLDEYVLQFKGLVKVIRNKEREGLIRTRSRGAMEATGEVIVFLDAHCEVNTNWLPPLLAPIYRDRTVMTVPIIDGIDHKNFEYRPVYGTDNHFRGIFEWGMLYKENEVPRREQRRRAHNSEPYRSPTHAGGLFAINREYFLELGAYDPGLLVWGGENFELSFKIWQCGGSIEWVPCSRVGHVYRGFMPYNFGKLASKKKGPLITINYKRVIETWFDDTHKEYFYTREPLARYLDMGDISEQLALKKRLNCKSFQWFMDHIAYDVYDKFPGLPANLHWGELRSVASDGCLDSMGHQPPAIMGLTYCHGGGNNQLVRLNAAGQLGVGERCVEADRQGIKLAVCRLGTVDGPWQYNEHTKHLMHRVHKKCMALHPATQQLSLGHCDVNDSYQQWWFKEIRPRW
The following text describes a protein:
Function:
Required for synthesis of steroid hormones, for olfactory sensory behavior and completion of the second larval molt (a steroid mediated developmental transition) and pupariation.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein.
Sequence:
MGINCLNIFRRGLHTSSARLQVIQSTTPTKRICIVGAGPAGFYAAQLILKQLDNCVVDVVEKLPVPFGLVRFGVAPDHPEVKNVINTFTKTAEHPRLRYFGNISLGTDVSLRELRDRYHAVLLTYGADQDRQLELENEQLDNVISARKFVAWYNGLPGAENLAPDLSGRDVTIVGQGNVAVDVARMLLSPLDALKTTDTTEYALEALSCSQVERVHLVGRRGPLQAAFTIKELREMLKLPNVDTRWRTEDFSGIDMQLDKLQRPRKRLTELMLKSLKEQGRISGSKQFLPIFLRAPKAIAPGEMEFSVTELQQEAAVPTSSTERLPSHLILRSIGYKSSCVDTGINFDTRRGRVHNINGRILKDDATGEVDPGLYVAGWLGTGPTGVIVTTMNGAFAVAKTICDDINTNALDTSSVKPGYDADGKRVVTWDGWQRINDFESAAGKAKGKPREKIVSIEEMLRVAGV
The following text describes a protein:
Function:
VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MHTIFPAALLAGYVVAFVAADATNTLAHDSTLWCHDIQYLEAILAAIDKEMNNRQKQLQVDAELIAKWKLAEAAAEQWHERRKYTALSVVIATLASKNSEAATEYLSAAAEAKKAINRRLEALQLVARTTSALKQTVTGAPQAASANAACQGSTEYASEAEFTCAPPEAGELKTAEVQTKLHTATHIKLTSFKALNELVAAPKITITATAGTTPFASPGQTPGTCQTSGGQNIAAGTNHVQYAVSSATVLKTQTPAAQPIDSDSERPEEPTAKKATVTAWLDIKFVTAALKNLKTAYNQKQIDLSQATHSTLAGLAGFKTVIANLFVGAEPPANNQETEYNNKIADIIKQTYGPEPGDFKRKFVTELANQDVKYTKAGNEQEKKLGALSKGADLSIALSFIINKRHESQLQKAAKAVSTVPKQNCTGKTKEKCKDACEWKGTDDKGECKPKDEEGQTNAAGTQGAETEGKDDKNNTNTTGSNSFVIHKAPLLLAVFVSIIYFLKISAQF
The following text describes a protein:
Function:
Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MRCLKSLLAFFTAFPIGGAELSFKCVWALPYVAAPIIAAIPTTLLYLGASPAIAYIALLAATGLHHLDGLADVGDALLVRDREAARRVLEDPRRGTGGIFAVTAVVVTTAAHLHSPLQLLLGEVFSKSTALLFAGFSKSFKPGLGEAFTEAAKRQWPAALPALAVLAYLAPVTTAVSLATSALLYQLAYRHLGGANGDVYGYLLEVSRSAFVIWSAYVPVPTAF
The following text describes a protein:
Function:
Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.
Subcellular Localization:
Nucleus.
Sequence:
MDYVSVLPQDIDLSSSHQYLRIPHPRTGEAQLYLPYTTAAGQDVVLEAAKLNGSQRRTWFIGDSGIDAGAMLVHYPIDPLFIVIPLILALVPNGPPPPFQPLHDLLSAASTSTSFALPLPFTSGTKGKSPNRSEGVNEDIERLLTLKNVKRAFKACCEKKVISTAPPSPDPSSSPQPPTQSFYRPSQDLIIQHLKRKAGFFAGPEEFEKFDHLVRGLGRDGLLEKDIDEELLSSARLRAACDHLAQWLPGPVLSKLVKSYDFAALEEHLASRSAAAFAASQITTSNNKKEAKGIKRKAPPASRGVESLKKVNTNKMAKLTSFFKPKEKK
The following text describes a protein:
Function:
Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis.
Subcellular Localization:
Cytoplasm. Mitochondrion inner membrane. Mitochondrion matrix.
Sequence:
MFRIADFTVRWRKMMNKFTCETASISLLHVSSVKSHLLSTMKGSNVASTLDESYENAISSLNSLQSNSSVLQDSILRKHSEDNKHINDTLKYLLRIGVSMDHLNQLPVIHVSGTKGKGSTCAMIESILRSNGYRTGFFSSPHLVSVKERVRLNGMPLSSDKFRLYFWKIYKQLLAYREHSRDMPSYFCFLTILALDVFLRESVDVCVIEVGIGGRYDCTNVLPKTGTVGITSLGLEHTKLLGNTLEEIAWQKAGIIKRGSDVFSVVQPSECMEIIREECRKLKANLFVVPSELKAYQWAKKPELVNESCDILDILELNTSLAIQIATNWMNKNISEISQENITSIVTKQTVEGIDRCFWPGRLQRILYDTKKTLYLDGAHTLESIHLCARWYNMKSHSQYKRLLIFNTTGDRDSAKLLSTLSSMIKFDAAFFTPSVPRDTVTCVDAMNHNFPFELQLQRCRQNYEYWSQTIQHKEGFLHESIESVFKQIDEDFVFKGETCDILITGSIHLIGAAFVALNLERFMCTSTTQ
The following text describes a protein:
Function:
Has bactericidal activity. Active against E.coli ML35 and S.aureus 502A.
Subcellular Localization:
Secreted.
Sequence:
MRLHHLLLALLFLVLSAGSGISGPLSCRRNGGVCIPIRCPGPMRQIGTCFGRPVKCCRSW
The following text describes a protein:
Function:
Hydrolyzes carboxymethylcellulose (CMC). Also hydrolyzes lichenan and barley beta-1,4-D-glucan. CMC is hydrolyzed majorily to cellobiose (G2), cellotriose (G3) and cellotetraose (G4). Cellohexaose (G6) is hydrolyzed to G4 and G2 with traces of G3. Cellopentaose (G5) is completely hydrolyzed to G2 and G3, and G4 is partially hydrolyzed to G2. Does not hydrolyze G2 or G3. Does not hydrolyze crystalline cellulose, soluble starch, xylan, mannan or laminarin.
Subcellular Localization:
Secreted.
Sequence:
MKVFVVLAAIVAIANGLTSGSGVTTRYWDCCKPSCSWGGKASVTKPVRTCKANGNTTIDSNTQSGCNGGSSYVCNDQQPFTQGNVGYGFAAASISGQPESQTCCACYEMTFTNTAISGQKMIVQVTNTGSDLNGNHFDLMIPGGGVGIFNGCQSQWGAPSNGWGQRYGGISSQSECNQLPTSLRAGCNWRFGWFKNADNPSMKFTQVRCPTILTQKSQCVRTPGP
The following text describes a protein:
Function:
Protease that deconjugates SUMO1, SUMO2 and SUMO3 from targeted proteins. Processes preferentially poly-SUMO2 and poly-SUMO3 chains, but does not efficiently process SUMO1, SUMO2 and SUMO3 precursors. Deconjugates SUMO1 from RXRA, leading to transcriptional activation. Involved in chromosome alignment and spindle assembly, by regulating the kinetochore CENPH-CENPI-CENPK complex. Desumoylates PML and CENPI, protecting them from degradation by the ubiquitin ligase RNF4, which targets polysumoylated proteins for proteasomal degradation. Also desumoylates RPA1, thus preventing recruitment of RAD51 to the DNA damage foci to initiate DNA repair through homologous recombination.
Subcellular Localization:
Nucleus.
Sequence:
MAAGKSGGSAGALFLKALDRSESKRDGGFKNNWSFDHEEESEGDADKDGANLLSVEDEDSEISKGKKLNRRSEIVATSSGDFILKTYVRRSKTDGFKTLKGNPIGLNMLSNNKKLSESTAGTALCSGTVVHGRRFHHAHSQTPGIRTAAQRKEYPPYVHKAENSPVMLSHGQGGDHIMKKTEESESYVESEIKRKVQQKRHCSTYQLSPLSPASKKCLTHLEVSEQREYCPKCGKEKENQTKCQSCGIVFHNDLQRNCRQAVTLNEPTGPLLRTSIHQNSGGQKSQNTGLTAKKFYGNSVDKIPIDILVTCDDSRHNYIQTNGKVILPGGKIPKLTNPKERKISVSDLNDPIILSSDDDDDDDDRTKRRESTSPKPADSACSSPVPSTGKVEAALNADACRAEQEPRSSPAEPELNTIVIPRKARMKDQLGNSISTPLKRRKVNSHAAFIHPMSLSCQNFESVILNCRSIRVGTLFRLLVEPVIFSLESITIHLDGPESDPVDIILNTSDLTKCEWCNVRKLPVVFLQAIPAVYQKLSMQLQMSKEDKVWNDCKGINRITSLEEQYIILIFQTGLDHQAEVVFESIITDIGIRNNVPNFFAKILFDEANSRLVACTRSYEESIKGNCAQKENKVKTVSFESKIQLRSKQELQFFDDDEEAGESHTIFIGPVEKLIVYPPPPAKGGISVTNEDLHCLSEGEFLNDVIIDFYLKYLVLEKLKKEDADRIHIFSSFFYKRLNQRERRNPETTNLSIQQKRHGRVKTWTRHVDIFEKDFIFVPLNEAAHWFLAVVCFPGLEKPKYEPNPHYHENAVMQKTPSAEDSCVSSASEMGACSQNSAAKPVIKKMLNRKHCLAVTDSSAAQEESEPCYRRNAYSVKCSMKKKNHAINENEEPSNGESTCQDICDRTQSENGLRDECFSSVHHPDALSKIRLNYGDQSADGGKLLEDELIDFSEDQDDPDDSSDDGLLADENYSSEIGQWHLKPTVCKQPCILLMDSLRGPSRSNVVKILREYLEVEWEVKKGSKRSFSKDVMKGSNPKVPQQNNFSDCGVYVLQYVESFFENPVLNFELPMNLMNWFPPPRMKTKREEIRNIILKLQESQSKDKKLLKDSLAETSLGDGAEQYASASGGSE
The following text describes a protein:
Function:
Possible function in spermatogenesis. Enhances the degradation of MDM2 and increases the amount of p53 probably by modulating the nucleocytoplasmic transport.
Subcellular Localization:
Nucleus matrix.
Sequence:
MGALSSRVLRPAGRTEQPEPTPGAGGAARRSDAGEDAGHSFCYCPGGRKRKRSSGTFCYCHPDSETDDDEDEGDEQQRLLNTPRRKKLKSTSKYIYQTLFLNGENSDIKICALGEEWSLHKIYLCQSGYFSSMFSGSWKESSMNIIELEIPDQNIDIEALQVAFGSLYRDDVLIKPSRVVAILAAACMLQLDGLIQQCGETMKETISVRTVCGYYTSAGTYGLDSVKKKCLEWLLNNLMTHQSVELFKELSINVMKQLIGSSNLFVMQVEMDVYTALKKWMFLQLVPSWNGSLKQLLTETDVWFSKWKKDFEGTTFLETEQGKPFAPVFRHLRLQYIISDLASARIIEQDSLVPSEWLAAVYKQQWLAMLRAEQDSEVGPQEINKEELEGNSMRCGRKLAKDGEYCWRWTGFNFGFDLLVTYTNRYIIFKRNTLNQPCSGSVSLQPRRSIAFRLRLASFDSSGKLICSRATGYQILTLEKDQEQVVMNLDSRLLIFPLYICCNFLYISPEKRTESNRHPENPGH
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase that specifically catalyzes 'Lys-29'- and 'Lys-48'-linked polyubiquitin chains (By similarity). Accepts ubiquitin from the E2 ubiquitin-conjugating enzyme UBE2D1 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (By similarity). Associates with the proteasome and promotes elongation of ubiquitin chains on substrates bound to the 26S proteasome (By similarity). Also catalyzes 'Lys-29'- and 'Lys-48'-linked ubiquitination of 26S proteasome subunit ADRM1/RPN13 in response to proteotoxic stress, impairing the ability of the proteasome to bind and degrade ubiquitin-conjugated proteins (By similarity). Acts as a negative regulator of autophagy by mediating 'Lys-29'- and 'Lys-48'-linked ubiquitination of PIK3C3/VPS34, promoting its degradation (By similarity). Can assemble unanchored poly-ubiquitin chains in either 'Lys-29'- or 'Lys-48'-linked polyubiquitin chains; with some preference for 'Lys-48' linkages (By similarity). Acts as a negative regulator of type I interferon by mediating 'Lys-48'-linked ubiquitination of IRF3 and IRF7, leading to their degradation by the proteasome. Catalyzes ubiquitination and degradation of CAND2 (By similarity).
Sequence:
MFSFEGDFKTRPKVSLGGASRKEEKASLLHRTQEERRKREEERRRLKNAVIIQSFIRGYRDRKQQYFIQRSAFDQCTDSAQPGGTFCLADGPNLTLLVRQLLFFYKQSEDSKRLIWLYQNLIKHSSLFVKQLDGSERLTCLFQIKRLMSLCCRLLQNCSDDSLNVALPMRMLEVFTSENTYLPVLQDSSYVVSVIEQILHYMVHSGYYRSLYLLINSKLPSSIEYSDLSRVPIAKILLENVLKPLHFTYSSCPEASRHQVFSAFTEEFLGAPFTDQIFHFVIPAFADAQTVFPYEPFLNALLLLESQSSKRCSGVPWLFYFVLTVGENYLGALSEDGLLVYLRVLQTFLSQLPASPTGTGCPDSTSDSEDDNEETDQPNSPEDGRVSAPYITEECLRKLDTKQQTNTLLNLVWRDSASEEVFTRMASICHTLMVQHRMMVPKVRLLYSLAFNARFLRHLWFLISSMTTQMITGSMVPLLQLISRGSPMSFEDSSRIIPLFYLFSSLFSHSLISIHDNEFFGDPIEVVGQRQSSMMPFTLEELILLSRCLRDACLGIIKLAYPETKPEVREEYVTAFQSIGVTTNSEMQQCIQMEQKRWVQLFKVITNLVKMLKSRDTRRNFCPPNHWLSEQEDIKADKVTQLYVPASRHVWRFRRMGRIGPLQSTLEVGLESLPLSVSEERQLAILTELPFVVPFEERVKIFQRLIYADKQEVQGDGPFLDGINVTIRRNYIYEDAYDKLSPENEPDLKKRIRVHLLNAHGLDEAGIDGGGIFREFLNELLKSGFNPNQGFFKTTNEGLLYPNPAAQMLVGDSFARHYYFLGRMLGKALYENMLVELPFAGFFLSKLLGTSADVDIHHLASLDPEVYRNLLFLKSYEEDVEELGLNFTVVNNDLGEAQVVELKFGGKDIPVTGANRIAYIHLVADYRLNKQIRPHCLAFRQGLANVVSLEWLRMFDQQEIQVLISGAQVPVSLEDLKSFTNYSGGYSADHPVIKIFWRVVEGFTDEEKRKLLKFVTSCSRPPLLGFKELYPAFCIHNGGSDLERLPTASTCMNLLKLPEFYDEALLRSKLLYAIECAAGFELS
The following text describes a protein:
Function:
Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Sequence:
MAQPLREVLVWLNNKIKEINPESAWLEAELLVAFVLNKDRAFIYTIDFLTDEEVEKLKKLLDLRKKGIPLNYIIEKKQFYDIELFVERGVLIPRSETEILIEVAKDTILKEGYKKIVEIGVGSGNISITLAKEFKDIKIYACDISPEAIKVARFNAKKHKVSDKIEFFFGFLLYPMVHRNVDFELIISNPPYIASWEFPFLQKEVKKEPWKALYGGWDGCEFYRKLFTLLKKRGKNFTAILEISPYIYHKVLNILKNFFDSVIIESFRDYLGHERVIKVIWH
The following text describes a protein:
Function:
Required for mitochondrial morphology. May control phospholipid metabolism in the mitochondrial intermembrane space (By similarity).
Subcellular Localization:
Cytoplasm. Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. Mitochondrion intermembrane space.
Sequence:
MKIFESCHLFQYPFEQVSAAHWQKYPNEHATHVIAVDTLDRKVLDNGVLYTERLITCHQALPRWILKLIDGAQDCYIRETSYVDLKARTLTLLTSNLTFSDRLRVDETVTYSPHPELEATVFQQEARIEALACMKRLSNLIEQWSVDGFGKKASRGKEGFESVLEKINMSVFQTRPFGSSEATA
The following text describes a protein:
Function:
Promotes cell proliferation.
Subcellular Localization:
Cytoplasm.
Sequence:
MEEVREGHALGGGMEADGPASPQELPPSPRSPSPPPSPPPLPSPPSLPSPAAPEAPELPEPAQPSEAHARQLLLEEWGPLSGGLELPQRLTWKLLLLRRPLYRNLLRSPNPEGINIYEPAPPTGPTQRPLETLGNFRGWYIRTEKLQQNQSWTVKQQCVDLLAEGLWEELLDDEQPAITVMDWFEDSRLDVCVYELHVWLLAADRRTVIAQHHVAPRTSGRGPPGRWVQVSHVFRHYGPGVRFIHFLHKAKNRMEPGGLRRTRVTDSSVSVQLRE
The following text describes a protein:
Function:
Essential component of stress-response pathways entailing repair of RNA breaks with 2',3'-cyclic phosphate and 5'-OH ends. Tri-functional enzyme that repairs RNA breaks with 2',3'-cyclic-PO(4) and 5'-OH ends. The ligation activity requires three sequential enzymatic activities: opening of the 2'3'-cyclic phosphodiester bond of the 5' half-tRNA leaving a 2'-phosphomonoester (CPDase activity), phosphorylation of the 5' terminus of the 3' half-tRNA in the presence of ATP (kinase activity) and ligation of the two tRNA halves in an ATP-dependent reaction (ligase activity). Deficient in transferring AMP to pRNA(OH) to form AppRNA(OH) but proficient at sealing pre-adenylylated AppRNA(OH). CPDase and kinase reactions are almost insensitive to RNA length, whereas the ligase activity decreases with shorter RNA size. Can also splice DNA ended by a single 3'-terminal ribonucleoside 2',3'-cyclic-PO(4). Binds to mRNA, mature and immature. Exhibits tRNA ligase activity in vitro. Required for the splicing of precursor tRNA molecules containing introns. Can circularize an intron cleaved from a pre-tRNA by splicing endonuclease in vitro. Seems not involved in unfolded protein response (UPR) in the endoplasmic reticulum. Involved in auxin signaling and polar transport during organ morphogenesis.
Subcellular Localization:
Nucleus. Cytoplasm. Note=Associated on polysomes.
Domain:
Has three domains each corresponding to an enzymatic activity, namely in N- to C-terminal order: ligase, kinase and cyclic phosphodiesterase (CPDase).
Sequence:
MDAPFESGDSSATVVAEAVNNQFGGLSLKESNTNAPVLPSQTTSNHRVQNLVWKPKSYGTVSGSSSATEVGKTSAVSQIGSSGDTKVGLNLSKIFGGNLLEKFSVDKSTYCHAQIRATFYPKFENEKTDQEIRTRMIEMVSKGLATLEVSLKHSGSLFMYAGHKGGAYAKNSFGNIYTAVGVFVLSRMFREAWGTKAPKKEAEFNDFLEKNRMCISMELVTAVLGDHGQRPLDDYVVVTAVTELGNGKPQFYSTSEIISFCRKWRLPTNHVWLFSTRKSVTSFFAAFDALCEEGIATSVCRALDEVADISVPASKDHVKVQGEILEGLVARIVSSQSSRDMENVLRDHPPPPCDGANLDLGLSLREICAAHRSNEKQQMRALLRSVGPSFCPSDVEWFGDESHPKSADKSVITKFLQSQPADYSTSKLQEMVRLMKEKRLPAAFKCYHNFHRAEDISPDNLFYKLVVHVHSDSGFRRYHKEMRHMPSLWPLYRGFFVDINLFKSNKGRDLMALKSIDNASENDGRGEKDGLADDDANLMIKMKFLTYKLRTFLIRNGLSILFKDGAAAYKTYYLRQMKIWGTSDGKQKELCKMLDEWAAYIRRKCGNDQLSSSTYLSEAEPFLEQYAKRSPKNHILIGSAGNLVRTEDFLAIVDGDLDEEGDLVKKQGVTPATPEPAVKEAVQKDEGLIVFFPGIPGSAKSALCKELLNAPGGFGDDRPVHTLMGDLVKGKYWPKVADERRKKPQSIMLADKNAPNEDVWRQIEDMCRRTRASAVPIVADSEGTDTNPYSLDALAVFMFRVLQRVNHPGKLDKESSNAGYVLLMFYHLYEGKNRNEFESELIERFGSLIKMPLLKSDRTPLPDPVKSVLEEGIDLFNLHSRRHGRLESTKGTYAAEWTKWEKQLRDTLVANSEYLSSIQVPFESMVHQVREELKTIAKGDYKPPSSEKRKHGSIVFAAINLPATQVHSLLEKLAAANPTMRSFLEGKKKSIQEKLERSHVTLAHKRSHGVATVASYSQHLNREVPVELTELIYNDKMAALTAHVGSVDGETVVSKNEWPHVTLWTAEGVTAKEANTLPQLYLEGKASRLVIDPPVSISGPLEFF
The following text describes a protein:
Function:
Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes. NF-Y can function as both an activator and a repressor, depending on its interacting cofactors (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MSTEGGFGGAGSSDAQQSLQSFWPRVMEEIRNLTVKDFRVQELPLARIKKIMKLDEDVKMISAEAPVLFAKAAQIFITELTLRAWIHTEDNKRRTLQRNDIAMAITKFDQFDFLIDIVPRDELKPPKRQEEVRQSVTPAEPVQYYFTLAQQPTAVQVQGQQQGQQTTSSTTTIQPGQIIIAQPQQGQTTPVTMQVGEGQQVQIVQAQPQGQAQQAQSGTGQTMQVMQQIITNTGEIQQIPVQLNAGQLQYIRLAQPVSGTQVVQGQIQTLATNAQQITQTEVQQGQQQFSQFTDGQQLYQIQQVTMPAGQDLAQPMFIQSANQPSDGQAPQVTGD
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 (By similarity).
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MIRYQIRNEYGLSDPELYAPGEKDDPEALLEGVAMAGLVGVLRQLGDLAEFAAEIFHDLHEDVMATASRGHGLMLRLRQLEAEFPAVEKAIISQSDHSNYPHDDGVEWHTNLQIDQNMITQGDMPRFILDSYEECRGPPRLFTLDKFDVAGAGASLKRYSDPSFFKTEHSSDMIETDAVIEKKPRKIKKKALRWRKGETLESLLIANSESHTTSKDRSSRKVPPRTTKLKYRYPRESDHKNISRICREHLQEIISSQQKIFSNYSSRYYHPKFRLTESSETASSFGEIDNFSARAQSSAKLELTKVVPINEFDTKGIAPTHINGSDCLEALEADDRQLQATQHEPDKVEDVCKRSLVEQNAMLSNSDRMQSVQEENLLSAMVPADQNDDRCRPDDTGSDQENFVDALNNMESEGEAHAEMKIKKDPGAKMELDELNFHRDEGENERHTEFSELGHVIDSSPWLNDSYNGGEPNHAISSNTNFSGVDCTNDEEPSNDVDLMEMDVSSSSSVFSDDNDVFRTNGNMNGFQQYQEASLSNDHHAVIAHSSDKQSSQKSSGLDGSSIESNDFIEKPFHSLEDDKNFAPDGTSVILGRPNDVSQCEEEIEVGNADDSLLQPTISNQEVHRSNNQLEGVAMHASISSGKVASFPDMDPGMCTKDLELDNVLVPKETVANTPPTGLGTDHIHEHVDELDSGVAPINSSIQSDSTYESDDDDMAEDLNSLPEDDLYKHDVEDLYKHVLEDDGIIALGKGPCSTRANMHQEDPMEVSDVRGDFSNGQELPVLTETASPQGELVGGGELPLLTETASPQGGEEDLADEVVVISSRDLNDEKKPSLAEVPLACGDASLLDSSASCLEHDESTETGEIAKSDEVLVNVEVAEESITGRFTDDMTPFQEDLPDGAKYSEDAEFLANPRVDNSRHDVQLQSSSPCREELETVKAPCENLCALDESREHIFEKSVLQINNLPQHIETKNTGEACSDIDDIQHLSALHCPKNPVCQEELPDETNLSADVQYHCDVEKGGAVILNSKMVEEQPENIDLVREPRAQDSFGTNPFMDPGYKANHALADPCPSYQPCFSEEEQDFISELLIPHGNMGIEDLNPVPVADSLWEPATPPDEVPLPSEVMTEEDFRSFCHEYHEMDLTATPESIDDKPASDSNVVSSSLVTSESEFLYCVSAVRTGVDQEESRDAPDDTLMHFSAKADPDDKAANSDLKSDEPFIDEKIHELGVPSVPMELEVEQHALHEVDSHGDSQLLDNDMIDETCSSPSGNSIAVKDKQETCANLVSRAFINERTDELEVPVSNSVLLEPSEEVHDSDEYNYQDVPWSSTDEGRDEVDAHPLSKRIQTQGSEALVLGELDSRAVPSCSVNEMADHVDAPPLSTVLEAEQEPEDCISGEHNSQVTKSSLVDEKIGELDDASPLSNTLLAEMEREVCVPGKSASQIASCSPTPSNEKIDELNAPPLSSSGLIELESEDSVSGDLDSQIIPCSSPNDKTNEPDGATSTHVLPVELEQEVCSFPELDSLVAPCSLNDDKVCELDEPPCKQLESENGSYCLPQVDCQIEPCYSESVVLSEASTMSSANAMPSTEETYRLSSPVPPPNEPFSNVSYEDPQKPPPLPPLLWRLGKPRLGIASTKGHMLEPERGKGPVLHTSDAGMDNMPGCLSGMTESIEPVSSQEIKERHLDPILDNNERGVEFRRLATPPTANDVAVTEHVQLFSDACENIKHQERVSSSETEAEEHQNGTGITDVMDSHPPKPLFLVPSISQQGLQGSVFPSDTSDNGEHSSYTSRAVSEDEKTVDDHNAACAMDLHITSSSASSHVSENGCNQQSHGESLPVTSVDKVHTSDASCEDNKLKNHFITSEVCSDATNLSASGLLTEEENIHNVEDQYEGPLPSEESSGCLDYPHDDHNSEKEDIHQPDGYAASPGNNNHFDSSHEGGYLHAEQPPVMGWTVRPQMLHPNYGISMEENQFEPKVEDHLLIKKPVSIRNIPRNPLVDAVAAHDRSTMRKVSELVAPTDKSKPNERNLLLEQIRNKTFNLKPVSSAKQPTIRTPPRASTRNLKVAAIIEKANAIRQAVGSDDEDGDNWSESSDT