lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Polygalacturonase required for degrading the pollen mother cell wall during microspore development.
Subcellular Localization:
Secreted, cell wall.
Sequence:
MELRKSQVAMPVFLAIMSLMVSQVVFAEKDSGSMSPHDRALAEMQALKASLVRRNLPALVSPPPTPPQAVPGPRVYQVISYGADPTGKLDSTDAILKAMEEAFDGPNHGVLMQGINDLGGARIDLQGGSYLISRPLRFPSAGAGNLLISGGTLRASNDFPVDRYLIELKDESSKLQYIFEYITLRDLLIDCNYRGGAIAVINSLRTSIDNCYITRFGDTNGILVKSGHETYIRNSFLGQHITAGGDRGERSFSGTAINLMGNDNAVTDTVIFSARIGVMVSGQANLLSGVHCYNKATGFGGTGIYLRLPGLTQNRIVNSYLDYTGIVAEDPVQLQISGTFFLGDAFILLKSIAGYIRGVSIVDNMFSGSGHGVQIVQLDQRNTAFDDVGQVVVDRNSVNGMVEKSTVARGSVDGNGTSWTVDFNPVLLFPDLINHVQYTLVASEAGVFPLHALRNVSDNRVVVETNAPVTGTVYVTVNQGV
The following text describes a protein:
Function:
Serine peptidase whose precise substrate specificity remains unclear. Does not cleave peptides after a arginine or lysine residue. Regulates trans-Golgi network morphology and sorting by regulating the membrane binding of the AP-1 complex. May play a role in the regulation of synaptic vesicle exocytosis.
Sequence:
MSDTQSLQQQLEREINFRMSHEPFPRPIRIDPYYYYTTIGQRGQLMHMRKPVDTPFAEGQVVLDTAQFTDLTKSNCLPGRLLICENHRRFGVMAEHPQLETCDLYIFDLEPPSPAAPTNTTTKSTLEGFFGVANEEKLHLVAKVPNIVNAEFNADATAVLYTQHDERFRPYVLRQRNLPALDAPAHSIVGRVVEDALLLTENDDRNFVDIGKTKDNKFFTINVNNKRASKVSLLPTRSGASFDELAEVTPPGPCHYFVEHAHGQLYIITDWQAPNYCVMTTQGPAEPWLPFVEHNPRIKIDDAEIFSSCLVLYESTEASPQISIVSLQDGSRRTKTLPEPFHLGNLEPTINAVFASKNLNFNTSDPLHQRIDWQLNLATCELNQLEQHDTQDVAGFVASQYEVTRLWAPTSDNLSVPITIVGRRDQPLSQPAPTLALVYGAYGHNLERRYNPTWVSLLQRGFRLAYCHVRGGGELGTAWHEGGMGLHKRNTFLDLEACLSYLVNEGITTTEQLALRGASAGGLAAAHIVVRRPDMIRACVLSVPFVDVLTTMLDSTLPLTRHEYDEWGNPELDREAFANIRGYCPYHNIADGHFPSCYIVGCLHDSRVKYWQPAKFAAKVRCFVHVPVI
The following text describes a protein:
Function:
General activator of RNA polymerase III transcription.
Subcellular Localization:
Nucleus.
Sequence:
MSSQILTSPTKKSMSRFAPKFTARREKVSDQKEVVHEEKNQPLTGNEVETSAQLSRDTANADISSPVVQTVVHKEATENPTASSYRKDDSVKQNEKLLHSNPTFKISKPTVLEQPLNAIEHLSPETDLSSSAEQQFMKELDLFFDENIPLSQLSAVSDGKADSPATKKSRRSYRESSLKRKSQLILENVGTDEKIINISETKMSALCDDPGIGRKSQRFIELEKMLFEEKRAKRIKKQGASTASSSREASLDSTIKQPLSASLLESSEPKEKEEIVGSLEEEGTDESASLEDSLSHPTKSILDQLADKMEVDGLNNNSNYSATPRTRVVNGQIVLDETSLEVDRHERDFVPAEEREYVEENSLSRRVTSATWGNRQKPEKWNAMDTEKFYKALSQWGTDFALIANMFPTRNRRQIKLKFKQEERRNPARVNQALKIKKPIDMEEYSKVSGKVFRPVEEMEKELQKIRENFEEERRRAIEVAEQRQLIVNHELEQEKNAPSPTDDKSYVFEDGVEVVGQVV
The following text describes a protein:
Function:
Transcription factor. Regulates WOX8 and WOX9 expression and basal cell division patterns during early embryogenesis. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element. Required to repolarize the zygote from a transient symmetric state.
Subcellular Localization:
Nucleus.
Sequence:
MAGFDENVAVMGEWVPRSPSPGTLFSSAIGEEKSSKRVLERELSLNHGQVIGLEEDTSSNHNKDSSQSNVFRGGLSERIAARAGFNAPRLNTENIRTNTDFSIDSNLRSPCLTISSPGLSPATLLESPVFLSNPLAQPSPTTGKFPFLPGVNGNALSSEKAKDEFFDDIGASFSFHPVSRSSSSFFQGTTEMMSVDYGNYNNRSSSHQSAEEVKPGSENIESSNLYGIETDNQNGQNKTSDVTTNTSLETVDHQEEEEEQRRGDSMAGGAPAEDGYNWRKYGQKLVKGSEYPRSYYKCTNPNCQVKKKVERSREGHITEIIYKGAHNHLKPPPNRRSGMQVDGTEQVEQQQQQRDSAATWVSCNNTQQQGGSNENNVEEGSTRFEYGNQSGSIQAQTGGQYESGDPVVVVDASSTFSNDEDEDDRGTHGSVSLGYDGGGGGGGGEGDESESKRRKLEAFAAEMSGSTRAIREPRVVVQTTSDVDILDDGYRWRKYGQKVVKGNPNPRSYYKCTAPGCTVRKHVERASHDLKSVITTYEGKHNHDVPAARNSSHGGGGDSGNGNSGGSAAVSHHYHNGHHSEPPRGRFDRQVTTNNQSPFSRPFSFQPHLGPPSGFSFGLGQTGLVNLSMPGLAYGQGKMPGLPHPYMTQPVGMSEAMMQRGMEPKVEPVSDSGQSVYNQIMSRLPQI
The following text describes a protein:
Function:
Involved in the pathway that organizes the shaping and sizing of the prospore membrane (PSM) during sporulation. Required for the proper formation of the spindle pole body (SPB) outer plaque. May connect the outer plaque to the central plaque embedded in the nuclear envelope.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Note=Localizes to the meiotic outer plaque of the SPB, at the end of the meiotic spindles.
Domain:
The length of the coiled coil are required to adjust the space between outer plaque and the central plaque.
Sequence:
MTDFDLMNFPFHERLDSPVSENGEIKDGEPIPQNWLNENHVGKSILPLFVNPEDVINCNFSNARDSYEENKSPSMDQMNYARNTSYQESPGLQERPKNEKDKSPIGTDVHKKDVPNFIHSTPRENSSKHFTRANEQASAQPTDEHTSPDISIEDCNGAKIFLQNSLSKEDFRMLENVILGYQKKVIELGRDNLRQEERANSLQKELEAATKSNDKTLDNKKKIEEQTVLIENLTKDLSLNKEMLEKANDTIQTKHTALLSLTDSLRKAELFEIPIGILFFDLYDSEENSSKLDHILQEKYPNIKGFLCASQQEELSRISQRFKNAKAEAEDLRNELENKKIEIQTMREKNNTLIGTNKTLSKQNKILCDKFDKLTIDEKEILKGCNEEIKIKLERLNERLGSWEKSKEKYETSLKDKEKMLADAEKKTNTLSKELDNLRSRFGNLEGNTSERITIKNILQSRPDISAEECNFLMVEQIDSANLTTLQNTVKEIVLAVGIPYPKLRRKIPLLAIKLKYENIMLSNFAQRLHRQVYSQEMNLKKFTDQAYYDFMSTRRMDSIDHHLERCLDHLYDHILEKMVK
The following text describes a protein:
Function:
Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
Sequence:
MGTGSREENASKQKDEPSIVVIKETNALVIHALDDAASRLGLHIGQPLANARAMCPDLRVFDADVVADAKTLSDIADWCDRFTPLVALDPPHGLFLDITGCAHLFGGEAALLQTLIRALGRQGFAVSAAIAGTSVCARTLTRQVTGTIVADGGEAEAISRLPVSALGAGEAITTGLRRAGLKTIGDVASRGAHEITARFGARFSTLLAHALGQGDAPINPRKPLPDYIVEKRFAEPIATDTMIAMTLSRLADTLIASMEKQGKGARRLEAAFFRTDGVVRAIMVETGRPVTRSAVIDRLFRERLDALADPLDPGFGFDMVRLSASRTEIVVQEQRDLDAHVHDNDELAALIDRIAARIGGKRVVVHLPQDTHVPECAVLAAPAQHHLAAAMQAEWPARAEGEPPLRPLRLFDKPEPVTVPFATVPDGPPHQFTWRRAKHAVVRVEGPERIAMEWWRQDGKQLTRDYFRIEDAEGLRFWIFRDGLYEGEVFDADGKPAPPNWYVHGLFA
The following text describes a protein:
Function:
Binds to and modulates brain Na,K-ATPase subunits ATP1B1 and ATP1B3 and may thereby participate in the regulation of electrical excitability and synaptic transmission. May not display kinase activity.
Subcellular Localization:
Cell membrane; Peripheral membrane protein. Cytoplasm.
Sequence:
MAIFEQQTVKKVVLDDTEPLSCVIENWRNVNGHTEFVIKVQRGPFSDKTWRVYKRYNDFYKLHAYLQTSGISLQLPPKKLIGNMDPEFITERQQGLQKYLNSVLMNPILVSSLPARSFVDPANYCQPFGELALQHVSLALRGEVGWEVVGPLEEMGWRLRKHYYHIKCKSQPKDDLIGGWTDYGPDKHLDDKDMHALFKSLNQIQHPFIHSIELCLCTDTGGLVVRTNHKNGSLRDLLCGAKPRQSFLKKYGNPKGHKPLEVSQVALYGRQILEALKFLMDKGLPYGHLHTGNVIIENDRVKLLDIENGVLGVPSFYRPYFMQHRKINTLQAIDVYCFGHTLYEMTFGAPLHESVADNIPSCPSLLKSVLESILSSEACKSGLPTIESLLNHRFFSSVAITLLPDDKAHLKIPNSTKEHLKLAVAQMEERLKEEQKMVRSQKRLVKVQEMMSSEEEKKKQRHKLKQEQRQLAREQMRQKSKSEKDDVDRPDSVNSSTATSIGTATPPSMTGSSVPSPPPPPPPPAPPSMSNGNGAPPLPELTKDRSALLGAICSFNKTSLRKTKVN
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MAPPSAPLLLRAVGEAGPTRKRGRRPRALKFVDVAVYFSSEEWGCLQPAQRTLYRDVMRETYGLLGALGCAGPKPALISWLERNTDDWEPAALDPQEYRRWVTFQRKTRSKQKTEEKDVFPPKEAPRKGKRGRKPSKPRLIPRQTSGGPICPDCGCTFPDHLALESHKCAQNLKKPYPCPDCGRRFSYPSLLVSHRRAHSGECPYVCDQCGKRFSQRKNLSQHQVIHTGEKPYHCPDCGRCFRRSRSLANHRTTHTGEKPHQCPSCGRRFAYPSLLAIHQRTHTGEKPYTCLECSRRFRQRTALVIHQRIHTGEKPYPCPDCERRFSSSSRLVSHRRVHSGERPYACENCEARFSQRSTLLQHQLLHTGEKPYPCPDCGRAFRRSGSLAIHRSTHTEEKLHACDDCGRRFAYPSLLASHRRVHSGERPYACDLCSKRFAQWSHLSQHQLLHTGEKPFPCLECGRCFRQRWSLAVHKCCPNTPNGSPRPLIGGPSQRSSAL
The following text describes a protein:
Function:
Lipid transfer protein involved in autophagosome assembly. Tethers the edge of the isolation membrane (IM) to the endoplasmic reticulum (ER) and mediates direct lipid transfer from ER to IM for IM expansion. Binds to the ER exit site (ERES), which is the membrane source for autophagosome formation, and extracts phospholipids from the membrane source and transfers them to ATG9 (ATG9A or ATG9B) to the IM for membrane expansion. Lipid transfer activity is enhanced by WIPI1 and WDR45/WIPI4, which promote ATG2A-association with phosphatidylinositol 3-monophosphate (PI3P)-containing membranes. Also regulates lipid droplets morphology and distribution within the cell.
Subcellular Localization:
Preautophagosomal structure membrane; Peripheral membrane protein. Lipid droplet. Endoplasmic reticulum membrane; Peripheral membrane protein. Note=Localizes to endoplasmic reticulum-autophagosome contact sites.
Domain:
The chorein N-terminal domain mediates lipid transfer activity.
Sequence:
MSRWLWPWSNCVKERVCRYLLHHYLGHFFQEHLSLDQLSLDLYKGSVALRDIHLEIWSVNEVLESMESPLELVEGFVGSIEVAVPWAALLTDHCTVRVSGLQLTLQPRRGPAPGAADSQSWASCMTTSLQLAQECLRDGLPEPSEPPQPLEGLEMFAQTIETVLRRIKVTFLDTVVRVEHSPGDGERGVAVEVRVQRLEYCDEAVRDPSQAPPVDVHQPPAFLHKLLQLAGVRLHYEELPAQEEPPEPPLQIGSCSGYMELMVKLKQNEAFPGPKLEVAGQLGSLHLLLTPRQLQQLQELLSAVSLTDHEGLADKLNKSRPLGAEDLWLIEQDLNQQLQAGAVAEPLSPDPLTNPLLNLDNTDLFFSMAGLTSSVASALSELSLSDVDLASSVRSDMASRRLSAQAHPAGKMAPNPLLDTMRPDSLLKMTLGGVTLTLLQTSAPSSGPPDLATHFFTEFDATKDGPFGSRDFHHLRPRFQRACPCSHVRLTGTAVQLSWELRTGSRGRRTTSMEVHFGQLEVLECLWPRGTSEPEYTEILTFPGTLGSQASARPCAHLRHTQILRRVPKSRPRRSVACHCHSELALDLANFQADVELGALDRLAALLRLATVPAEPPAGLLTEPLPAMEQQTVFRLSAPRATLRLRFPIADLRPEPDPWAGQAVRAEQLRLELSEPQFRSELSSGPGPPVPTHLELTCSDLHGIYEDGGKPPVPCLRVSKALDPKSTGRKYFLPQVVVTVNPQSSSTQWEVAPEKGEELELSVESPCELREPEPSPFSSKRTMYETEEMVIPGDPEEMRTFQSRTLALSRCSLEVILPSVHIFLPSKEVYESIYNRINNDLLMWEPADLLPTPDPAAQPSGFPGPSGFWHDSFKMCKSAFKLANCFDLTPDSDSDDEDAHFFSVGASGGPQAAAPEAPSLHLQSTFSTLVTVLKGRITALCETKDEGGKRLEAVHGELVLDMEHGTLFSVSQYCGQPGLGYFCLEAEKATLYHRAAVDDYPLPSHLDLPSFAPPAQLAPTIYPSEEGVTERGASGRKGQGRGPHMLSTAVRIHLDPHKNVKEFLVTLRLHKATLRHYMALPEQSWHSQLLEFLDVLDDPVLGYLPPTVITILHTHLFSCSVDYRPLYLPVRVLITAETFTLSSNIIMDTSTFLLRFILDDSALYLSDKCEVETLDLRRDYVCVLDVDLLELVIKTWKGSTEGKLSQPLFELRCSNNVVHVHSCADSCALLVNLLQYVMSTGDLHPPPRPPSPTEIAGQKLSESPASLPSCPPVETALINQRDLADALLDTERSLRELAQPSGGHLPQASPISVYLFPGERSGAPPPSPPVGGPAGSLGSCSEEKEDEREEEGDGDTLDSDEFCILDAPGLGIPPRDGEPVVTQLHPGPIVVRDGYFSRPIGSTDLLRAPAHFPVPSTRVVLREVSLVWHLYGGRDFGPHPGHRARTGLSGPRSSPSRCSGPNRPQNSWRTQGGSGRQHHVLMEIQLSKVSFQHEVYPAEPATGPAAPSQELEERPLSRQVFIVQELEVRDRLASSQINKFLYLHTSERMPRRAHSNMLTIKALHVAPTTNLGGPECCLRVSLMPLRLNVDQDALFFLKDFFTSLVAGINPVVPGETSAEARPETRAQPSSPLEGQAEGVETTGSQEAPGGGHSPSPPDQQPIYFREFRFTSEVPIWLDYHGKHVTMDQVGTFAGLLIGLAQLNCSELKLKRLCCRHGLLGVDKVLGYALNEWLQDIRKNQLPGLLGGVGPMHSVVQLFQGFRDLLWLPIEQYRKDGRLMRGLQRGAASFGSSTASAALELSNRLVQAIQATAETVYDILSPAAPVSRSLQDKRSARRLRRGQQPADLREGVAKAYDTVREGILDTAQTICDVASRGHEQKGLTGAVGGVIRQLPPTVVKPLILATEATSSLLGGMRNQIVPDAHKDHALKWRSDSAQD
The following text describes a protein:
Function:
Required for translation of the mitochondrial OLI1 transcript coding for the mitochondrial ATP synthase subunit 9.
Miscellaneous:
MISCELLANEOUS: Present with 2680 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion.
Sequence:
MWINRLVKHPSYSVLRFYTKRLCTVSVKSLREFGVLPNSTICHSVYPRRTYVMGRAVINDILIKKSYSTHTVCAIDRSKDENNGSAYDKFEAKGIPIDVHTLKRIISSSGMDESEFSKSISYLFAKTVDPEPKDVLSLEDLSFLLSKLYTQRFQIRRICRDINAKYSEFWFKLFSLYAEKVDAKRNQVNLRNTKLDACEIFDANLMIKNFIELGQLGKAQKILSFILDRNPDILLSPKNADISTIVHFLQLRCGALAPYWKIPDNSEQKQGFLRKMVRLGAKNTSIRLSSTYKAMDHQTLLKIADLALQEKKLLNSEDLLSTLIQSFGHLGQTQILERCIEHIWQISPQEFPSHVVIKHRGCYPSSKILVSILVSFYFNDHDLHRGLSILDSFIKHYPDVKLDALFWRRLFQLSHFAWTPANDKKATSVVRCWHLMKQWYASKRLRPSVDYETLRQLYDIMKKTGNFPLGIDVLRSFKPGIERTRAENAGKVNNIIIKYQKCIIKELVNRGRFSAVREFIDSYGFDRKMTKDLNIFCANRMFLRSKKMKNKIENKKEREKVRLDSFDDDEDDGMIIGSLW
The following text describes a protein:
Function:
May play a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Required for formation of the cleavage furrow during cytokinesis.
Subcellular Localization:
Nucleus matrix. Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Membrane. Note=Cellular localization varies throughout development and may be related to phosphorylation levels. Shows diffuse cortical cytoplasm localization in oocytes, with membrane-association increasing after fertilization, particularly in the vegetal hemisphere (By similarity).
Sequence:
MASGVMVSDDVIKVFNDMKVRHQLSPEEAKKRKKAVVFCLSEDKKMIILEPGKEILQGDVGCNVDDPYKAFVKMLPRNDCRYALYDALYETKETKKEDLVFVFWAPEEASLKSKMIYASSKDAIKKRFPGIKHEWQTNTFEDINDPCNLAEKLGGSTVISLEGKTLKS
The following text describes a protein:
Function:
Catalyzes the hydrolysis of ATP coupled with the transport of calcium.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MVYPAHAHTPEEVAKYFNSDLEKGLTDEQVLINREKYGVNSVPPPKRKSIFSMILEQFQDPMVIILLISVVLGFIFAYFEEDPEERTTAFIEPWVIIFILVVNATIAVYQDLNAQKSVEALKEFTPSLANVIRNGELREIPAVEVVCGDLVDVSEGRAISADIRLCKFKSSMVAINESNLTGEPVPVQKSLEVVKEDAVVNDRINVAYKGTPLERGGFIGIAYAVGKDTQMGYIEETTQQEEEVITPLQRNLDNFSKYISVGILFICVITWFANISKFDEVGNGNRIKGGLMFFKIAISLAVAAIPEGLPAVVTMTLSLGVNRMAKSNAIVTKLPAVETLGCTSVICSDKTGTLTTNKMVVQVFATVIDGKSSVYQVQGKDYDPDGALAIQGQKVSNLYEHKAAQMSAMVGTLANDGAIIYSKEKGFGRKGEPTDAAIKVFAEKVGLPTKEAEEARLKKGAVERMEDVSKYWYKEYPKVRTHEFTRARKSMSCIVGKNTLVMKGAFEVILAKCDRYIEDMTGEVKPLTEAVRKEIDSCRQEWAGKKAYRCIGLAYKECTDDWNNWNIIDQQELIKYESGCIWAGSVGILDPERPDVAQSIKDCYNANIRVIMCTGDNPETATAIARNIHMLGEHEDPTGKVFTGAAWEKMNDAEKREAAKNAVVLARVEPKHKRELVGILQEQNNVVAMTGDGVNDAPALSKADIGIAMGTGTTVAQGAAQMILSDDSFSTIVKAVREGRAIYNNTTSFIRYLLTCNIGEVVCCFVSSLIGGPNLLRSTQLLFVNLVTDGLPATALGVNPAEPNVMDLPPRPKDENIITPMNLCRYIVGGVYLGLATIAAAYYHYILDPLGPHLTYYEITHYHGNPHIKEILEDETAGTMAMTVLVIIEMFSALTAVSEHLSFFQLPPHRNPKLILSICGSVLVHLLVIELPITQKIFSVVHLNCTQWAIIVLLAFPVVIIEEIFKFYIRKTQKHIHIVRE
The following text describes a protein:
Function:
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Sequence:
MKNIGILLLFISVVLSTTNEIANVDIDITTAYPGIKMDITVTSEQPLHSYAFYLPKSYEISSLVFLNKETEKELTFTTHNETEYTQFIVEFEDTPKISLTMAYIQINNYLPVPKFISQFDSQEFDYTLLLCPLTQSKTKSCQVLLHHYDKLKVISDIKHSTIKNTTAFGPFDDLSPMEVIETTVHSNSLPHIKVNKMIHSVDLPTISSFVKVEDWFEDFTNEGAQLSSGFSRFDFQQNIGNYPNAIGFFEINLNTRASSIQYKDTSGNISTSSLLLNDDNLVLIALPRYPLLTGWKTEFMIGYSLPNKVVISKGKAIITLPSIKTAMAKEVIVRVYLPDNAKYLKVEGKNIENIEVKDCDAFLSFAGRKEVLITMKNINIMDEVQLTLYYEESVSGSINTFIVFGCYVLLFFLGFFLFIKYSA
The following text describes a protein:
Function:
A translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Usually binds in the 5'-UTR at or near the Shine-Dalgarno sequence preventing ribosome-binding, thus repressing translation. Its main target seems to be the major flagellin gene, while its function is anatagonized by FliW.
Subcellular Localization:
Cytoplasm.
Sequence:
MLVLTRKIGQSIRIGDNIVIKIVNVDGSQVKIGIEAPKGMAIFREELYEKLKESNIEALNTAKELKLDELLLKAENSMNKVGASQNKEQKDDNS
The following text describes a protein:
Function:
Oxidase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the saturated C-C bonds of the alkyl side chain (Probable). PynA subsequently forms the amide bond between the acyl chain and L-serine. Although pynA has a terminal reductase domain, it appears to require the thioesterase pynI for the release of the straight-chain intermediate from pynA via the formation of a tetramic acid pyranonigrin J. The methyltransferase pynC then coverts pyranonigrin J to pyranonigrin I via N-methylation. The FAD-dependent monooxygenase pynG catalyzes an epoxidation-mediated cyclization to form the dihydro-gamma-pyrone moiety, followed by pynD-catalyzed oxidation of the alcohol to the ketone and enolization to yield the characteristic tetramic acid-fused gamma-pyrone core of pyranonigrin H. Pyranonigrin H is substrate of pynH for dehydration-mediated exo-methylene formation from the serine side chain to produce pyranonigrin E, before the oxidase pynE reduces the exo-methylene of pyranonigrin E into a pendant methyl to form pyranonigrin G. The FAD-linked oxidoreductase pynB performs the reverse reaction and converts pyranonigrin G back to pyranonigrin E.
Sequence:
MSKPTIAFLGATGGCINACLAHTLQTGYHAVALARTPSKLTALLRTQNIDQETLDSRLRIVTGDATDPEAVKSTLLLQPGFPTDPTTSASSPTPTLVSHIISGIGATGNFRGWCFEFDQPHICEEATRALLTALRNIYATYPEFMLPANVKSRPLLTVLSGMGVDPSQKQMDVPFLLRRVYHGLLHVPHADKWVMEEMLAKREAREFFRGVITVRPGSLLTGDHMLGSGYGYEKVRVGTEREEPSVGWTIPRADVGEWVFREVVVMGGGRWVDEKVTLTCW
The following text describes a protein:
Function:
Promotes matrix assembly and cell adhesiveness (By similarity). Can stimulate endothelial cell proliferation, migration, as well as angiogenesis.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix, basement membrane.
Sequence:
MLLPQLCWLPLLAGLLPPVPAQKFSALTFLRVDQDKDKDCSLDCAGSPQKPLCASDGRTFLSRCEFQRAKCKDPQLEIAYRGNCKDVSRCVAERKYTQEQARKEFQQVFIPECNDDGTYSQVQCHSYTGYCWCVTPNGRPISGTAVAHKTPRCPGSVNEKLPQREGTGKTDDAAAPALETQPQGDEEDIASRYPTLWTEQVKSRQNKTNKNSVSSCDQEHQSALEEAKQPKNDNVVIPECAHGGLYKPVQCHPSTGYCWCVLVDTGRPIPGTSTRYEQPKCDNTARAHPAKARDLYKGRQLQGCPGAKKHEFLTSVLDALSTDMVHAASDPSSSSGRLSEPDPSHTLEERVVHWYFKLLDKNSSGDIGKKEIKPFKRFLRKKSKPKKCVKKFVEYCDVNNDKSISVQELMGCLGVAKEDGKADTKKRHTPRGHAESTSNRQPRKQG
The following text describes a protein:
Function:
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER).
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein. Membrane; Single-pass type I membrane protein.
Sequence:
MKVNHLFGLLPTLLQGLISLESRVSADKILIVIEDGVERSNYQLLWSSLNARNHQLSFRAAKDATPALAEFGEPAFDHLILFSPTAKSFPADLSPQALVQFLEDGGNILLAGSTNLSEYWRDFGREFDVDFDDRASSVIDNFHHLDQDPLTTYTSIETNPLIEDQIVIPPSLRSNNLPVLFRGIGHAVGKNPLLMSVLRASPLAYSAEAKSKESDPNPFIIGDEIGLVSAFQTKKQSRILFVGSLDFFSDQFMTTELTLPDGKKTSTGNRKVVDHLTKWVMQESGVLRIVSVTHSKVGGEPEPPRYRVNEQIEYKVDVQMLQNGRWGPCPLKDLQLEFTMLDPHLRVTLTPTKSPKGTHTTYSTVFRAPDRHGVFTFKLDYRRRTGYTHLEKGIQVSVTPLEHDQYERFIFGAYPYYLGTLSVLASFLLFSFVWLTHFPGTTAHKKTK
The following text describes a protein:
Function:
This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of the final effector complex. The ATPase activity of MutL is stimulated by DNA.
Sequence:
MPIQVLPPQLANQIAAGEVVERPASVVKELVENSLDAGATRIDIDIERGGAKLIRIRDNGCGIKKDELALALARHATSKIASLDDLEAIISLGFRGEALASISSVSRLTLTSRTAEQQEAWQAYAEGRDMNVTVKPAAHPVGTTLEVLDLFYNTPARRKFLRTEKTEFNHIDEIIRRIALARFDVTINLSHNGKIVRQYRAVPEGGQKERRLGAICGTAFLEQALAIEWQHGDLTLRGWVADPNHTTPALAEIQYCYVNGRMMRDRLINHAIRQACEDKLGADQQPAFVLYLEIDPHQVDVNVHPAKHEVRFHQSRLVHDFIYQGVLSVLQQQLETPLPLDDEPQPAPRSIPENRVAAGRNHFAEPAAREPVAPRYTPAPASGSRPAAPWPNAQPGYQKQQGEVYRQLLQTPAPMQKLKAPEPQEPALAANSQSFGRVLTIVHSDCALLERDGNISLLSLPVAERWLRQAQLTPGEAPVCAQPLLIPLRLKVSAEEKSALEKAQSALAELGIDFQSDAQHVTIRAVPLPLRQQNLQILIPELIGYLAKQSVFEPGNIAQWIARNLMSEHAQWSMAQAITLLADVERLCPQLVKTPPGGLLQSVDLHPAIKALKDE
The following text describes a protein:
Function:
Plays a role in autophagy. Functions at the preautophagosomal structure (PAS) in order to form normal autophagosomes under starvation conditions. Also plays a role in mitophagy and regulation of filamentous growth.
Subcellular Localization:
Preautophagosomal structure.
Sequence:
MTSPTQSGNTKFTVLIRLPFPRGGFVDPPPVDWNAAKDQALWDILSRPSKGNDIDWKALAESFDVTLEFLLQQAAWLYDRQLSQVRAQMRKVPTAHSNAASPAQGSIYASTALGQPAKTGQSNSSRAPSRLASQPKEAPPVRAPIPRRNSSGNTVQQIKAQTSHPGTPTLGTKEPRRESHGRQPSTNRREQAPVSLADQRSPTLEEEDLTSSLSESNSDDESDTIAGRKGLGFKRFGRFSTHRPDLRDDDDDDDESPAFLPLSRGHETTSHGTSGHDLSTTLRMEQEGVSAVQRRVTGPPPSLRKSVTTESSESSVSSGVPVGRPLNQRGNQINHPSPRRTADVNHMSPRRSTTSGRDISDGTPSMGSSFSDLDGDTSVTQSMLEEALLSNMQHGGMASRMSTISQALRSRYLP
The following text describes a protein:
Function:
Catalyzes the reduction of 3'-oxosphinganine (3-ketodihydrosphingosine/KDS) to sphinganine (dihydrosphingosine/DHS), the second step of de novo sphingolipid biosynthesis.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MPTPLALLLSAILIIGTYFAMPFWPFRKSNYDPRGKHCYITGGSSGLGKALAERLVKQGAHVTIVGRDSKKAEGVVEELKAIAAPGQIIQCIAADLTSPIASTNAIHAACKPHADQAPDYVYLCAGFSRPKLFVETTKQELKDGLDGVYWVSAYTAHEACQMMSKQRRTGKIIFVASFLSYVSFAGYSSYSPAKYALRGLSDALRSEMLLHNIDIHIFLPCGISGPGFDAENRTKPAVTKKIEEGDTPITPEVCAAALESGLKKGYYQITDNLVTEPIRLRSNGGVPTNNFLLDTLWLIVSSVGVPIWRMTADSAVRSFRAKVEKELEAKGYYVS
The following text describes a protein:
Function:
DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
Sequence:
MELIEILLKKLNKNAVVTEIAKDKDPFKVLISTIISARTKDEVTEEVSKKLFKEIKDVDDLLNIDEEKLADLIYPAGFYKNKAKNLKKLAKILKENYNGKVPDSLEELLKLPGVGRKTANLVITLAFNKDGICVDTHVHRICNRWEIVDTETPEETEFELRKKLPKKYWKVINNLLVVFGREICSSKSKCDKCFKEIKEKCPYYEKIKHFENILKKFNFRKVSKNKIPNEKGTYILKIRLKEGKKIKFGKTERFFKKGYYFYIGSAFGNSMNLKNRIERHLKDDKKMHWHIDYLLKYGKIEEIYITNERVECEVANEFIKKFDFVENFGCSDCKCKSHLFYLKP
The following text describes a protein:
Function:
Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Sequence:
MLQRFSKQYQFSQIGRMKQRKRSHIKYFSKPIIEGQYGVVPARAVPSHIQRPSYISETKPVYGIYEGAPVVHGQDMIQKLRKAAQIAAKTAYVASKSVKQGMTTDDLDKIVHEFIISQNAYPSPIGFMGFPKSVCTSVNEVCCHGIPNLRPLDGGDSLNIDVTIFYDGVHGDTSVMAQVPEMNPEITKLIDTTQKALYEAIKICKPGQKFSKIGDIVEEVAGDEGFTVCELFTGHGIGELMHMPPTIIHNFNDYPGVMVPGNVFTIEPILLMRHDQYLMWKDNFTVVSPDNPSGIVNLQTVAQWEHMVLITENGYEVLTKREDETGI
The following text describes a protein:
Function:
In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Sequence:
MSFDNNYHGGQGYAKGGLGCSYGCGLSGYGYACYCPWCYERSWFSGCF
The following text describes a protein:
Function:
Probably involved in ribonucleotide reductase function.
Sequence:
MLRLVYDSLTGNVRHFAETLAAELHVSPMRVQDPAPTDAYLLLTYTFGSGEVPASTRRLLTTHGHLLRGVVASGSYHWGHNFARAADVIAAEYRVPVVAKLNKGGTAADRAAVRRWLLHYAESAPPFPTSCTGEPTPWNAG
The following text describes a protein:
Function:
Transport of phosphate groups from the cytosol to the mitochondrial matrix. Mediates salt stress tolerance through an ATP-dependent pathway and via modulation of the gibberellin metabolism.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MALSDLSRDSLLPSFLYSSPAARSFTAPRFPSSPSPYQAPAAAPAAGIVGAGGAGGGRPFSIRAPNEKIVMYSPAFYAACTAGGIASCGLTHMAVTPLDLVKCNMQIDPAKYKSITSGFGVLLKEQGARGFFRGWVPTLLGYSAQGACKFGFYEFFKKTYSDMAGPENAVKYKTLIYLAGSASAEVIADIALCPFEAVKVRVQTQPGFARGLSDGLPKFIKAEGAAGLYKGIVPLWGRQIPYTMMKFASFETIVELIYKHAVPVPKAECSKSSQLGISFAGGYIAGVFCAIVSHPADNLVSFLNNAKGATVGDAVKKIGMLGLFTRGLPLRIVMIGTLTGAQWGIYDAFKVMVGLPTTGGAPPVAPVEESA