lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
May be involved in female gametophyte development.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Domain:
The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme.
Sequence:
MNKILPEMKSTQNLISSSPPPPLIPLKSNTSLSNLNSKITPNILLIIIILSIIFFISGLLHILVKFLLTPSRESREDYFDNVTALQGQLQQLFNLHDSGVDQSLIDTLPVFHYKSIVGLKISPFDCPVCLCEFETEDKLRLLPKCSHAFHVECIDTWLLSHSTCPLCRSNLLSGFSSHHNLSSSYLLVLESEQSSRDMVPVLESNSQLGYDVNNDSESTRIRSGRKSCDPDGDMDGLDEKVVPLEVKLGKFRNIDHVGEGSDQKKNSISGNSKNVDGRRCLSMGSYEYIMDQEATLKVHVSTKKLSGKDRVPSHRTVMSECGFDPTVKGIEKSVVERESFSLSKIWLRGKKEKQKGTSARDSDCSFVSSSSLRFPNHRIPPEESLKSENSESLETKTPSFARRTMHWLAGRQNKIVQPSTSNV
The following text describes a protein:
Function:
Involved in rRNA-processing and ribosome biogenesis.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MRQKRAKNYRKLMHTYQLLFGFREPYQVLVDADFLKDLSQQKIDIQAALARTVQGAIKPMITQCCIRQLYSKSDELKQEIRIAKSFERRRCGHIDEALSPSECIQSVVNINGRNKHRYVVATQDPELRQALRSVPGVPLIYMKRSVVILEPASRATLLEKHNKESVQMGMSKEEKLLLSGKKRSANELAIDDQDTKESTDLAGTEDSAPKANKKRKGPKGPNPLSIKKRSSKNHTTDEPTLPVNIIGDVGERKKHRRKRK
The following text describes a protein:
Function:
Putative transcription factor required for axon growth and guidance in the central and peripheral nervous systems. Repels CNS axons away from the midline by promoting the expression of the midline repellent sli and its receptor robo.
Sequence:
MDNQVCLRWNNFQSSLTTTLEILWDEESFCDVTLFCGGQEIRAHKVVLSACSMIFKSLLKNNTCQHPIIILHDISLNILEAILQFIYKGEVNIEQDQLNNLLRAATLLQIRGLAGIAENEVDLENQLLSKPMKTGLSQNFPSSDFSPVKRKKPKVSSSPKENDDEPLLVTSKEEPLSEEETCGSAIYTDEVYERPDSLVLLDRKEEDECSHGVIDVDPLVTKPTNIPLAVNSSDEMISNSSQAVACNNTQFPPYPCPFCCRAYATWGFRRRHIKAIHTTSPKLPCKWCSTVMASRGDWENHVIDEHHLSRSEAEQGLKVLEEAHMVLQTTNIADDVLKETADRSFRSKDKK
The following text describes a protein:
Function:
Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules.
Subcellular Localization:
Cytoplasm.
Sequence:
MKYNIQQLYDANFPQRLNDFLNYLRTIKGKSENTIESYKLDLIMFFRFLKLYKGMVPGETEFNDIEIKDISDEDIKNISLTDLFAFVSFVENYRNNGSYAKARKVATLKSFFRFLQGKVKIIKENPALELESPKISKRNPVYLTLDESKRLLSSIDGKFKERDLCIVTMFLNCGLRLSELCGINISNIKNDILTVVGKGNKERTVYLNKACIKTLNDYLNVRKEMGEKIVDKDALFLSKNYTRINKRSVEMLVKKYVKKAGLDGEKYSPHKLRHTAATLMYKHGGVDIRSLQMILGHENISTTQIYTHVDSDRLREAVKSNPLSDE
The following text describes a protein:
Function:
Ribonuclease that cleaves double-stranded RNA (dsRNA). Required for 3'-external transcribed spacer (ETS) cleavage of the pre-rRNA precursors. May promote the production of 21 nucleotide small interfering RNA (siRNA) during post-transcriptional gene silencing (PTGS).
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MDHSISPEYNFPAITRCSLSNSLPHRPPSPLPSSADIHRFYNSLSPSAPSVPVSSEMESMEAVEKILNYKFSNKSLLKEAITHTSCTDFPSYERLEFIGDSAIGLAISNYLYLTYPSLEPHDLSLLRAANVSTEKLARVSLNHGLYSFLRRNAPSLDEKVKEFSEAVGKEDDLSVSYGGLVKAPKVLADLFESLAGAVYVDVNFDLQRLWVIFRGLLEPIVTLDDLQKQPQPVSMLFKLCHKHKKRIDIKNWKDGNVSIAVIYLDDELLASGRAENKDIARLIAAKEALRKLSEVFPVEMVIDEDSVEIQLTHAKTKLNEICLKKKWPKPIYSVEEDRSSVQGKRFVCSAKIKITEEKTLYMKGDEQSKIKKAESSSAYHMIRALRKSHYL
The following text describes a protein:
Function:
Involved in chromosome cohesion during cell cycle and in DNA repair. Involved in the repair of double strand breaks during mitosis and meiosis. Required for chromosome segregation during mitosis. Central component of cohesin complex. 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 (By similarity). At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate (By similarity). Required for the localization of lab-1 to meiotic and mitotic chromosomes.
Subcellular Localization:
Nucleus. Chromosome. Note=Has diffuse nuclear appearance at interphase during mitosis in somatic and germline tissues.
Sequence:
MKIKEVRITGFRSYKDNTNVSGFSPRSNVVVGRNGSGKSNFFHAIQFVLSDEYAHLKEEQRLGLLHESTGPKVAHARVEITFDNSEKRLMAFENSEVKIVRQVGKKKDQYYIDNKMVPRAEVVNLMESAGFSRSNPYYIVKQGKINELATSPDAYKLKLLREVAGTRVYDERKEESLKILKETKMKTEKIQGLLKYIDERLQTLENEKEDLKEYQKLDKTKRSVEYTMYDNTNKEAIKEKTKLDEQKVELNQKDNNVKSQLNDVIAEMAKLKTDKKKLESLGRGLREDKETLQAEETKMVEEKMTLKLEIDSLNEENTRERQGRQNAEHSLQGVGDEIFKNEEELDTIKPEYAKLLEEESRLKTDIRIDESRAKEILAKQGQRSQFSSVDDRDKFLRNEIRRISGLIADNKEREETIQKELADVEREDEKLNNEIQSISRTIDENRYEMDTFAAKSTSLKQEYDAAYVAQQTAAREEKAIRDKIGNTEQDISAANDQLRRIVARPVYNGITGVRKVIEEFKHDNRNGQHDDVINGYYGTVIELAEVPDMFRTAVEVIAQNRLFYHVVETDRIATKILRKFNEMQLPGEINFFPMNRVSAPRQRDLSNNSNARPMSDVIDYEVQYDKVFKSITANVIIVRTLDQAARDLRNEGFDVVSVDGDQMSKKGVMTGGFIDKKRSKLELHTQKDRFTKELAELQKSLAEAEKMVRERTQEAEKIRNRMQQHENQIGDFHRKHRELTEAKNAISQQFYMVTSTKEPKKDQLLGIKNHLRELLAQKENFEQEIGSNMSSQLTSDEEQTVKKLRKKVDEMTKQLATVSRRRMDLMHRKNAIENLLTKKLYKTKESLTARVDDISDNERRHKLENANAQLTSLLTRMESTRKQLATAISELQDYETKEKALQINIDNVLEQQRDLEKQQADFQLQYDKITAKEDEVKQKREDSLKKLILSRYSIKTRKNQFSYEISDSEEVGAKREPIEHRKLKISTFCLEYRAKLEKVHSNMRLLGALPTDTFSKWQNVKPRELEKKLLECVNELKKYENVNKKALDQYMTASSQKEELTKRMAEQKKSEDSIEELLKVLENRKYEAIDLTFKQVKKNFEQVFKQLVPHGRGKMQMRAREQRDDEEGINSVELYEGISVLVSFVSDDGDSETREMTQLSGGQKSLVALAIIFSIQKCDPAPFYLFDEIDAALDAQHRKSVADMIQSLSDQAQFVTTTFRPELLATAEKFYGVRFRNKVSHIDSVTREQAYDFVEDDTTHG
The following text describes a protein:
Function:
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Subcellular Localization:
Mitochondrion.
Sequence:
MLRISRDTKIVARVTHVTKSRTYATSTAPKLVVGLEIHTQLLTKRKLFSSTTVPSLSTTPNTKVSYFDAALPGTQPRLNPQALLLALKAAIALRCDVKELTAFDRKHYFYPDQPAGYQITQHRKPLAINGKLKLNWWDLYSQNEWPALLAKEANTDSADTRDLASRSIDVPILQIQLEQDTGKSTYHGSETLVDLNRTNMPLIEIVTAPVIHTASHAAAFVKKLQTLLKRIGVSTGEFESGAMRVDVNVSIGEDGERCEIKNLPNTSSIEAAIEAEYNRQVELVGKGGTVEKSTMGFDGKKTFILRSKENAVDYRYMPDPELPLIRLSKGTLLKVRDSLPELPDKVFSRLTDDPYYVTTKDALTLIHVAGLSDYYFEVFERVSEETEDAKALKQPVNWVVNELLGRVRKADEARAAESAESGEPDLGAHDYNSIYPPAKLAELILAVHNHQLTLPSARLLFQHFLANPEDLKNMTIEQAITEFELGESGDVVDACRQVINEHESVVKSVKDGSKPGSIKFLIGMVMKATQGRINPAVIERQLKTEMRHM
The following text describes a protein:
Function:
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with NCS6/CTU1 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position.
Subcellular Localization:
Cytoplasm.
Sequence:
MACGAGNCQSGCFRDDDDSVVTEKKKLTNRTLSSGSDIDLPNHHNLCLKCKVNETLASSGTVSVDGDIGRFCFDCFRGNLFGKFKLAVTSNAMISPTDNVLVAFSGGPSSRVALQFVHEMQHKAQKNFDASRDRSLPVFGVGVAFVDESAVSRIPSDEFDKAIQDMKSIVSNLAPPDKAFHVVPIESVYSSNGRDRLEELLNAVKDVTGKEDLLQHLRMLSLQKNAYENGYTKLLLGSCTSRIACHVISATVKGQGYSLPADIQYVDARWEIPVVLPLRDCLAQELNMLCRLDGLKTMEVLNSPHSGINGLVASFVTLLQEENPSRECTIVRTAGKLTPFHFNQIPESDDSNVHLASRRRQKKFNLKPNESVPPESYCPICNSPLSKSDHINLSSLGSDQTNADIFGATCCPSCQFQILPKEPVSMEHFYSLLPQQFVVQAKDRSFSMQRQLREQIQDFLLSDSEDGT
The following text describes a protein:
Function:
Catalyzes the conversion of L-ornithine to N(5)-hydroxyornithine, the first step in the biosynthesis of all hydroxamate-containing siderophores, such as the secreted triacetylfusarinine C (TAFC) involved in iron uptake and the intracellular iron storage compound desferriferricrocin (DFFC).
Sequence:
MEPLQRKSELDFQSYRKMPLAQQRTQRLKPTSPEELHDLICVGFGPASLAIAIALHDALDPCLNKCAPTSGWQPKVAFLERQKQFAWHSGMLVPGSRMQISFIKDLATLRDPRSSFTFLNYLHQKDRLIHFTNLSTFLPARMEFEDYMRWCANQFSDVVTYGEEVIEVLPGKSSPDSPVVDYFTVLSRNVETGEISSRSARKVVLALGGTAKLPAELPQDPRIMHSSKYCTALPNLLKDNNEPYNIAVLGSGQSAAEIFHDLQKRYPNSRTSLIMRDTAMRPSDDSPFVNEVFNPERTDKFYNLSAAERERSLKADKATNYSVVRLELIEEIYHDMYLQRVKNPDETQWQHRILPSRKITRVEHYGPNKRMRVHVRAVKDGKDSLIGDGKEVLEVDALMVATGYNRNAHEQLLSKVQYLRPATQDRWTPSRDYRVDLDRSKVSAGAGIWLQGSNEQTHGLSDSLLSVLATRGGEMVESIFGEQLESAAVPDTRFRAML
The following text describes a protein:
Function:
Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase.
Subcellular Localization:
Nucleus.
Sequence:
MSSLDNQLSAFKNKIKSAPTIKKPSFVAKRKEEEEGVGGQQKKRKVVPPVNPFNENVGRHAATQLMHAVEYIKKQVGVVPIENIRSYLSLQSADFLVPLLKKMDQMSYNAVQRGFEYMPKFNIRTKAQLMAFLKSQPTAKGLSVRDLKDGWADCLDSIEELEQSGDLIVLRTKKENSPRMMWANMGGPIGMVDGEFRSMWSQIKVPDESELPSKLEEAGLKPTSVDPATIKSNKANGNGSKKQKKPRRSKITNTHLDGVLKDYGR
The following text describes a protein:
Function:
Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MACNRADYLERTIKSILKHQNAVASKYPLFVSQDGSNAQVKEKALSYDQLTYMQHLDSKPLQTERPGELIAYYKIARHYKWALDKLFYEHKFSRVIILEDDMEIAPDFFDYFEAAAALMEKDKTIMAVSSWNDNGQKQFVHDPEILYRSDFFLDLDG
The following text describes a protein:
Function:
The main replicative DNA helicase, it participates in initiation and elongation during chromosome replication. Travels ahead of the DNA replisome, separating dsDNA into templates for DNA synthesis. A processive ATP-dependent 5'-3' DNA helicase it has DNA-dependent ATPase activity.
Sequence:
MKNFDTKAQFSISDTPLPYNFVAEKIVLSCLLINYEAIEITIKTVRVETFYFINHQEIYKAILEMYRKKIPINVLSVNDFLKETGCLYKIGGTKVLLELLNQIPNLVYLEEYIQLIQDKFLRRSLINLGYQAINSAYITNIPLEKILNDFEKKSFKLTTELIDDKRLTTAELFSTVFLELKQKALKPELPGLASGFYDLDSLTQGFQKADLIILAGRPSMGKTAFVLNITENILKNYKLPVIFFSLEMSKEQLIYRLLSNETGISQTRLKLGNLYKEDWHKLKNSIQDYSRLPFFIDDQAEITTQDIRAKIKKILFEQNKIGLIVIDYLQLLLTSKIKSENRVQELSQITRSLKSIAKEFQTPIIALSQLSRNVENRINKRPVLSDLRESGSIEQDADLVLMLYRENYYNLTIEKNEKITSAELIIAKHRNGPLGTAQLSFQVDPTKFFNTFPSSE
The following text describes a protein:
Function:
Serine/threonine-protein kinase involved in energy homeostasis and protein translation. Phosphorylates EEF1A1, GYS1, PDX1 and RPS6. Probably plays a role under changing environmental conditions (oxygen, glucose, nutrition), rather than under standard conditions. Acts as a sensor involved in energy homeostasis: regulates glycogen synthase synthesis by mediating phosphorylation of GYS1, leading to GYS1 inactivation. May be involved in glucose-stimulated insulin production in pancreas and regulation of glucagon secretion by glucose in alpha cells; however such data require additional evidences. May play a role in regulation of protein translation by phosphorylating EEF1A1, leading to increase translation efficiency. May also participate in respiratory regulation.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSTMARFPPNPRIRDKGQTFCGVDDYPSSPEDEFDLNKSYPCTQKPICRSFFKLQRRHYPSSLTGRGLDVFALMATRNHQLSSLLPGSLPHPSTASETEESLFSLLISGGFDLPEYPSSLNPNKAVLTISSQTGEILSANEQAAKLFESPSVDLIGKKISSLLKRTNQVLEEALEENDVRVDGTIGTVSGKVVDAVTSSGEVPVSLCTYREPQSEDRLLVMTEAVERVSAYFSFSQDGRILTCDSAFAHLHGYLNPEGLKGAAIQNLIPSLQIPLYSHTLPKMLRAQRVFGKSRDGTSVPLCVKLQSTVLCGKPPNQSDEHNSTRDGHELSNDECNQWEPHQDKRNVPNPEKQSREKSSGEKVDDIRTSLSPLLEYCGTVWMFVPRSSLLLLHPDGSIFSIHNHLALSLFGYSNEELLGKSVSFLMPGFYTWMSDLDKKDGPLSESRIELPKSPTSSRISDPSSLVAGDLAMVQQAVQGQTSSGRGRIFTGNCTNLEKHTSALSALSSPAVTSTRVVMANDTIELLREAARVAPCSSLPNSAETTQALLGTFTWVEPLEDGSCCSASTEVSVPRREGQQRSHTPVIVSVGTPTQHGQAASSVSDTCPVAEEEKPSCSSQLQDSSFDVISLESRSASGLCEKFNRHGEFKPDHAEESVPEHTLDSASSFLDINGDVVSTAFADLNLSSSIELLSSGGCTDDNQLSVASLDTAELLQTPSLCVIESDQESESVCVPHVAAEARNDMSEELQTAATTTDKGKSQECCANVSQQSMTDVPATSTPKKQKMDGQVLSSHRTIVDAQVEGSGYHRDGTRVDVQLDVHKTVLSDGSFMFCVWIKKAGQQGTAMQANHSLTNQSGASFGERIGEGSALRSTTDLENSRACDGQFEEEYQPAKAVGKGAFGFVWKAVRRCDGQEVIVKFISKARIVSDSWVDDPMLGKVSQEIAILTRVQHHNIVKVVEVFENGSYFQMVMEKHGDGLDLFEFIDMQPRLDEPLASYIFRQLVAAVFYLRTKNIIHRDIKDENIIIDKCFHIRLIDFGSAAILVPGKLFYNFCGTLEYCSPEVLQGHPYEGPELEMWSLGVLLFTLLFSENPFCDVEEILDAKLKLPFSVSSELHVVLRGLLHSNPKKRMTLDQLLLQPWISQPISLAEYSWSEVAPANESYCPPQPQKLSSPATVIKQGLFLDQGEETLSHDEEEDEEERLSMVALETELQKYLCED
The following text describes a protein:
Function:
Shows phosphodiesterase activity. Shows significant activity toward bis-p-nitrophenyl phosphate (bis-pNPP), an artificial substrate commonly used to detect phosphodiesterase activity. Also hydrolyzes, with lower efficiency, two other artificial phosphodiesterase substrates, thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). Shows phosphomonoesterase activity toward p-nitrophenyl phosphate (pNPP), with much lower catalytic efficiency. No activity was detected against a wide variety of naturally occurring phosphomonoesters and phosphodiesters, including various 2',3'- and 3',5'-cyclic nucleotides, suggesting that YfcE is highly specific for its physiological substrate, which is not yet known.
Sequence:
MMKLMFASDIHGSLPATERVLELFAQSGAQWLVILGDVLNHGPRNALPEGYAPAKVAERLNEVAHKVIAVRGNCDSEVDQMLLHFPITAPWQQVLLEKQRLFLTHGHLFGPENLPALNQNDVLVYGHTHLPVAEQRGEIFHFNPGSVSIPKGGNPASYGMLDNDVLSVIALNDQSIIAQVAINP
The following text describes a protein:
Function:
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
Subcellular Localization:
Cell membrane; Peripheral membrane protein.
Sequence:
MDKKTVKVIEKYSMPFVQLVLEKGEEDRIFSDLTQIKQVVEKTGLPSFLKQVAVDESDKEKTIAFFQDSVSPLLQNFIQVLAYNHRANLFYDVLVDCLNRLEKETNRFEVTITSAHPLTDEQKTRLLPLIEKKMSLKVRSVKEQIDESLIGGFVIFANHKTIDVSIKQQLKVVKENLK
The following text describes a protein:
Function:
Receptor kinase that detects X.oryzae pv. oryzae protein Ax21 to promote innate immunity. Following X.oryzae pv. oryzae protein Ax21 detection, undergoes cleavage, releasing the processed protein kinase Xa21 chain; The processed protein kinase Xa21 chain released by protein cleavage after X.oryzae pv. oryzae protein Ax21 detection translocates into the nucleus where it can bind and regulate WRKY62, a transcription factor. Confers resistance to the bacterial pathogen X.oryzae pv. oryzae (Xoo).
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MTSLLFPGFVRFLCLFLGFSCSLPSLGICDETPSDRQALLCFKSQLSGPAGFLASWSNVSVEFCDWYGVTCSATSPRRVIALDLESQGISGTIAPCIAKLTWLTRLQLSNNNFRGGVPSELGLLSRLASLNLSMNTLEGNIPPELSTCSQLKILGLWNNSLRGEIPHNLSQCKRLQEINLGNNKLQGSIPPAFGVLPALRVLVLAKNTLTGTIPPSLGSSRHLTYVDLATNALGGVIPQSLANSSSLQVLRLMSNSLTGKLPKALLNTLSLGAICLEKNNFVGTIPSVTVTPSPIKHLSLRYNNLSGRIPSSLGNLSSLVHLYLTNNYLVGSIPESIGYIPTLEILTLSMNNLSGPVPPSIFNMSSLKSLAIAKNSLVGRLPFDIGYTLPNIQDLILSDNNYDGPIPASLLKAYHLQRLDLKNNRFTGSIPFFGSLPNLVLLNLARNKLEADDWGFVSSLSNCSRLNMLALDGNNLNGKLPSSIGNLSNSLDYLWLSSNKISGPIPPEIGNLKSLIGLYMGDNLLTGNIPSTIGKLYKLVDLSFAQNKLSGQIPDTVANLVQLSTLELDHNSFSGRIPASISQCTQLTILNLAHNSLDGRIPSKILTISTLSKELDLSNNYLSGRMPDEVGSLLHLKKINMSNNRLTGNIPSTLGQCVDLEYLEMQNNFFAGRIPQTFSNLVSIKHMDISGNNLSGKVPEFLKSLKSLQGLNLSFNHFDGAVPTGGVFDNIGAVSLQGNDHLCTIIPMRGMSLCMALSDSKRKQKPVVLVLVILLPIVVATAILFSCMATIYRRKRMQANPRLQHDNEHVKKLEKISFEKISYEDLLRATDRFSSENLIGSGSFGRVYKGSLQFQADQVAIKIFDLDINGADRSFIAECEALRNVRHRNLVKIITSCSSVDHTGADFKALVFPYMPNGNLEMCLHLKYSEDGEKNILSLSQRTNIALDVAVALDYLHNQCAPPVIHCDLKPSNILLGLDMAAYVIDFGLARFLFSPENAHQDSSASLSRLKGSIGYIPPEYGMSEEISTKGDVYSFGVLLLQLITGCSPTDEKFNDGISLHEFVDRAFTKNIHEVVDSTMLQDSSNATNMMKNCVIPLLRIGLSCSMTSPKERPGMGQVSTEILRIKHVASDTCMSDEANNWQDSSKQQKFM
The following text describes a protein:
Function:
Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of a single 3-deoxy-D-manno-octulosonate (Kdo) residue from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. Is strictly monofunctional, i.e. is capable of adding only a single Kdo residue to the acceptor lipid.
Subcellular Localization:
Cell inner membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MQFEVLKRFFPKESLKNCKGALWVHTASIGEFNTFLPILKELKREHRILLTYFSPRAREYLKTKSDFYDCLHPLPLDNPFSVKRFEELSKPKALIVVEREFWPSLIIFTKVPKILVNAYAKGSLIEKILSKKFDLIIMRTQEDVEKFKTFGAKRVFSCGNLKFICQKGKGIKLKGEFIVAGSIHTGEVEIILKAFKEIKKTYSSLKLILVPRHIENAKIFEKKARDFGFKTSFFENLEGDVILVDRFGILKELYPVGKIAIVGGTFVNIGGHNLLEPTCWGIPVIYGPYTHKVNDLKEFLEKEGAGFEVKNETELVTKLTELLSVKKEIKVEEKSREIKGCYLEKLREFLRGL
The following text describes a protein:
Function:
H(+)-myo-inositol cotransporter. Can also transport related stereoisomers.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSRKSSDNEYNLRSLSNLMGERRKKVNDDGERSLIKAPSSSSINSQGSTAAATGDLERAARKQFQQDVTPGFVYVLAIFSALGGFLFGYDTGVVSGAMLLLKKEMNLSALWQELLVSSTVGSAAVSALAGGALNGVFGRRVCILLASFIFSAGGIVLSVSPTKEILLVGRVVVGLGIGIASMTVPVYIAEAAPPQLRGQLVTINTLFITGGQFIASVIDGAFSYLPKDGWRYMLGLSVVPAVLQFLGFLFLPESPRWLIQKGKTQKARRVLSQIRGNQNIDEEYESIKSSIDEEEKEAGGGGLVIWRMLTYAPARRALIVGCGLQMFQQLSGINTVMYYSATILQMSGVKDDKMAIWLSAVTAFTNFIFTLFGVWLVEKVGRRKLTLGSLTGTSLSLLVLAIGFLLSAQHSPPVILHPTDPSTPNSTCSQYGFCDSCMLDPGCGFCYQENSSSIFASSCVPVNKASTEEAEWGRCSNATVMKEGIFWAYNYCPTPYSWTALLGLILYLMCFAPGMGPMPWTVNSEIYPLWARSTGNACSAGVNWTFNVLVSLTFLHVAQYLTYYGAFFLYSGLATVGFLFVFGCLPETKGRRLEEIESLFENQLCTCGASDSDEVSQDYGSVIHREENTGPENEIAYICL
The following text describes a protein:
Function:
Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins. Is involved in resistance to the arginine analog canavanine (CAN).
Sequence:
MGKKVKKKPKTGQKEKRGPSVSQETVSKTPDDAVTAVKDRGICSHIDRGINLDKLSAKLRYSESFKCEDCRGNSDDARARKGKGKQSGGGKGARSESKAVWICLECGHFSCGGVGLPTTPQSHAIRHAKQQHHWLVVHCENHQLIWCFSCDKLINSDKSSEDSNHKRVLSEVVKRLKKKPGEEPSVKNVEDIWFGGGSNNETNATNSECSAISVACERVGYSVRGLSNLGNTCFFNSTMQNLLSINSLRDYFFRTETESIGPLTSALRKLFIETNTGSNFKTVINPRALFGILCTKAPQFKGSLQQDSHELLRCLLDNLSGEELSSRKKKQTESLVGPTFVDTIFGGQLSSTVTCLECGHASTNYEPFLDLSLPVPTKRPPIAKRNQPVVRSKKSKLPTKKSSRNLAKIRRDATILPPQECVSDQTIAQPVAEEFDTDIALDMGLTADDLSAIQKPNNEQAVEIEGEPLISPLDSFAWLDYLDENPVDVASETDETSAVENAVSLVNGVSVAEQENAFPHSEGNNVNSQSNEGIPPEVSVSMEIVVFDGEAARCSDSSSQVCSKDSNTAQINNSEVNSLSNELVLDEQDSLDFVGFGDLFSEPEVPVSEASDITKNGVVVNNSSESDPDQVDSNADAPVSVESCLALFMKPELLSKDEHAWQCEKCSKALREERRRLMRKSRNGSGDSNTGIEISTESEVNAIDIQSENGCVAGNNECEADKERESEGSEQDDEADSENLKVKRDATKSTLINKAPSILTIHLKRFIQDARGRLNKLNGHVNFGEIVDLKPYMDPRCSERERYTYRLVGVVEHQGTMRGGHYVAYVRGIKDNNGDCVWYHTSDSFVGEVSFEDVLRSEGYILFYEEI
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates ribosomal protein L23 (rpl23a and rpl23b).
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MEKLLHEALQNGCKLHKSVEFIQSRDDNACFGSYIAVAQNDIAPDQLLISCPFEYAITYNKAKEELKKLNPNFESCNPHITLCTFLALESLKGIQSKWYGYIEYLPKTFNTPLYFNENDNAFLISTNAYSAAQERLHIWKHEYQEALSLHPSPTERFTFDLYIWSATVFSSRCFSSNLIYKDSESTPILLPLIDSLNHKPKQPILWNSDFQDEKSVQLISQELVAKGNQLFNNYGPKGNEELLMGYGFCLPDNPFDTVTLKVAIHPDLPHKDQKAAILENDCQFQLSNLVFFLPKSPDKEIFQKILQCLAVVTASSLELRKLTAHLLTGDLASYVPSLRGQIKSLEVLLMYIDSRADLLLKSNPQVSPTSERQVWAKIYRDSQINILQDSITYVKNYMEESLQKTYKPLPNLLQYLILNSISIFLLQHPLFAPLSHAIESLYGSTDAEALVATDEQDILMILICVYCLSISEKLPFSISMLVEGYPAVANPEGVEVFEILDEMFFQQFTNVFGESKHFNKENVSWALQLVNDESLDFSGFTFIIAHN
The following text describes a protein:
Function:
Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia.
Subcellular Localization:
Cell junction, tight junction. Cell membrane; Multi-pass membrane protein.
Sequence:
MALTVLLGVICLAGTIAITALPTWKVTAFIGANLIVMEELQEGLWMNCIRHANFRMQCKAYDSVLILPGDLQAGRGLMCLSIILIIFAIILMSCGLKQSSLCQDNMKKKNSILAAGGSLYLVSFLTTLIPVCWASHSIITDFYNPTLGDSQKRELGSALYIGWATSVLLLITGVILLTRCSKRKTPEEQYYAEEERNFQDKNSISFTKTPSSIHKNQVYV
The following text describes a protein:
Function:
RNA cytidine acetyltransferase with specificity toward both 18S rRNA and tRNAs. Catalyzes the formation of N(4)-acetylcytidine (ac4C) in 18S rRNA. Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis. Catalyzes the formation of ac4C in serine and leucine tRNAs. Requires the tRNA-binding adapter protein TAN1 for full tRNA acetyltransferase activity but not for 18S rRNA acetylation.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MVGQRKAVDQRIPALIRNGIQEKKRSFIVVVGDRTKDVIVHLHYIMSSMDMKQNKSVMWAYKNKLLGFTSHRKKRETKIKKDIKRGIREANTEDPFELFVSLHNIRYVYYKETEKILGNTFGMCILQDFEAITPNLLARTIETVEGGGLVVLLLKGMNSLKQLYTLSMDIHSRYRTEAHDDVTARFNERFILSLGKCESCLVIDDELNVLPISGGKNVKALPPPDLDQPKSESQIELDNMKEALQDTQPVGSLVTLAKTVDQAKALLTFVDAIAEKTLRNTVTLTAGRGRGKSAALGVAVAAAVAHGYSNIFITSPSPENLKTLFEFIFKGFDALNYMDHVDYSIIQSTNPDFNKAIVRVNIHRQHRQTIQYIRPQDAHVLGQAELLVIDEAAAIPLPLVKKLMGPYLVFMASTINGYEGTGRSLSLKLIKQLREQSRGTTNGTEDVEIADRSSGKAAAKGADNSFSGGRSLREITLSEPIRYAKGDAVEKWLNQLLCLDATLPRSRLNTLQGCPDPSQCQLLNVNRDTLFSFHDVSEKFLQQMIALYVASHYKNTPDDLQLMSDAPAHQLFVLVPPIEENSRHLPEPLCVIQVALEGKISKQSVMNSLSRGQRAAGDLIPWLVSQQFQDDDFAGLSGARVVRIATNPDYIKMGYGSKALELLTDFYEGKFANLSEDMNDYVEETITRVTDEELTSASLLDDNIKVRDIRKMPPLFSKLSEKRPDNLDYIGVSYGLTQPLHRFWKRASFVPLYLRQTPNELTGEHTCVMVRTLENSENRDWESAFSRDFHRRFLSLLSYQFREFPSVLALSIDESANAGSKSDPEAAPKPLSKAELDKLMSPFDLKRLESYANNMLDYHVILDLIPTLANLYFTGRLKSDIKLTGIQSSILLAVGLQRKDLTAIESELSLPSSQLLAMFIKIMRKMSAHFGDLVSGAIEAEMPGRESIGVSREDANGALDDEVVDDRFVPLEQGLEEELEEGGDEAMKALKEKQRELIDALPLDQYEIEAGAPGWAEAEKQVKNAAKSGKKDIVVGVKSAKTKRKAGESAAEIYEQEMGDKTHKKAKKGSKKGH
The following text describes a protein:
Function:
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
Subcellular Localization:
Cytoplasm.
Domain:
Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain.
Sequence:
MRYSKLFIPTMREIPSGINAISHILMLKAGYVRQLAAGLFIFLPLGWRVLNKINMILKEEMERIGAQEISMPILHPAEIWQETGRWYTIKEEMFRLKDRTGRDMCLGMTHEEIMTWIASKEIKSYRQLPQIWYQIQTKLRDEARPRGGVLRTREFIMKDSYSFDIDWEGLDKSYNLHAEAYHRIFTKCGLKYYQVESDPGIMGDMESHEFMAPTPAGEDEIVLCDSCGYSANIEVAKSELPTLPSLNFEYKEIYTPEKKSVKEVSDFLGLSEKYFIKTLIVISEKNGPVLVMLRGDQELNEKKLARIIGEFSFATSEQALEILGVELGFVGPVGHKIKKIADFSIQKEISYISGANKKNYHLQGIIPGIHFDAQWADIRRVKEEDRCPKCGNSLKIEKAIEVGNIFKLGTKYTEPLHAYFLDKDGKEKPIIMGSYGIGPARVAAAAIEQNHDSDGIIWPKSISPFDIEIIPLNMDDEKTVSIAEELYEKVTEIYNSFADRHMEVLIDDRDERPGVKFKDADLIGIPIQIVIGKKGLKENKVEIKKRRTKETKKVSVNKAVVEIVNSYYETY
The following text describes a protein:
Function:
TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. May be involved in the recycling of the translocation apparatus after completion of the translocation process or may function as a membrane-bound chaperone facilitating folding of translocated proteins.
Miscellaneous:
MISCELLANEOUS: Seems to bind calcium.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Domain:
Shows a remarkable charge distribution with the N-terminus being highly negatively charged, and the cytoplasmic C-terminus positively charged.
Sequence:
MRLLPRLLLLLLLVFPATVLFRGGPRGLLAVAQDLTEDEETVEDSIIEDEDDEAEVEEDEPTDLVEDKEEEDVSGEPEASPSADTTILFVKGEDFPANNIVKFLVGFTNKGTEDFIVESLDASFRYPQDYQFYIQNFTALPLNTVVPPQRQATFEYSFIPAEPMGGRPFGLVINLNYKDLNGNVFQDAVFNQTVTVIEREDGLDGETIFMYMFLAGLGLLVIVGLHQLLESRKRKRPIQKVEMGTSSQNDVDMSWIPQETLNQINKASPRRLPRKRAQKRSVGSDE