lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Component of the coat protein complex II (COPII), that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII is composed of at least five proteins: the SEC23/24 complex, the SEC13/31 complex, and the protein SAR1. Acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex.
Subcellular Localization:
Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein.
Sequence:
MVGLCKIESNDDQTRPRQRRGRGGTGSQSRCSSSPIQDSASPHSSYHTSPSPLPAPAPPCPAAAPAPYPLGPPGPPGVMSVAELVQPIRERDQRMDQPYDVLGPRQGTSDFHRLSYRQVASVVSSVCEFKWNSDDTLFIYHHFVHKVMDNYGKQIHEWKKKWEINKVPKSMNDTIWKELCAHWDKEETKETSSTNFTNRRSDRNGNGVFKHNLGAQSIATLGYRMKKGRLVGLGRRSRSAASFSAPPPFVDPEVLTAQLKDKDDRISVLETQMAAQQAGYEAHKRLNEQMMEMIKMMYPNEVFPNVQDPTSSLRGPKRHTSVRRLLRSSSNRLTASGKDRHTYSSKSSSTFRPSPPFGQPPPQPYPQSAPSYGVQQQQPPPRPSPMPRPGPPPPALTRPGGPPQLSQPGGIPFGRPSGPPSSQPPFGSRPPGAFPGPPGGVAAPPPSGPRPVGFGSPPPMGPGMSMPGGPVTNGPPPMMTPGGPGPIPNGPPMMGPGGFPRGSQFPGGSMMGPPPPYGQPPNAHSLPGGSPLTSPPAHSIPPPTTFPGAPYAMPGGFPYGLPAQQHPSAPGTPGSMYGMGPVPNQSMTTVSGPSKVDLNQIPRPGSISGPIMYETRQENQANPPPPTTVDYIARDTGNCSPRYMRCTIHQIPCTVDLLSTSGMQLALIIQPLALSHPSEEPIQVVDFGESGPVRCSRCKGYINPFMKFVDQGRKFICNLCGYTDETPRDYQCNLGPDGKRRDADERPELCRGTVDFVATKEYMVRDPMPAVYFFLIDVSMNAIQTGATAAACSAIQQVLSDLPEGPRTFVGIATFDSTIHFYNLKRALQQPLMLIVPDVQDVYTPLETDVIVQLSECRQHLEILLESIPTMFQESKSPESAFGAAIKAAFLAMKSTGGKLMVFQSVLPSVGIGALSSREADGRANASADEKEAHKLLQPADKTLRTMAIEFAEYQVCVDLFITSQAYVDMASISDIPRTTGGQVYCYYPFSALSDPPKLYNDLRWNITRPQGFEAVMRVRCSQGIQVQEYSGSFCKRIPTDIDLPAIDCDKAVMVTLKHDDKLQDGAECGFQCALLYTTITGERRIRVINLSLPCTSMLSNLFRSADLDSQFACMLKQAANEIPTKALSLVKEQAISSCITALSSYRKFCATVTSAGQLILPEALKLLPLYTLALTKGVGLRSDGRIDDRSFWINHVSSLSTPLAIPLIYPRMIAVHDLDTKDNEETVVPSPIPLTSEDLRDDGVYFLENGDDGLIYVGESVNSDILMKLFNVPSAADIPSQYVLEKYDNQLSKKFNDVVNEIRRQRSSYLRLKLCKRGDPTGMLFLSYMVEDRTAGGPSYMDFLVQVHRQIQGKLN
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase.
Subcellular Localization:
Endomembrane system. Endoplasmic reticulum membrane; Single-pass type IV membrane protein.
Domain:
The RING-type zinc finger domain is responsible for E3 ligase activity.
Sequence:
MERNSEDQRMELDLNLEPPPGFDLGLGLGLDLHDWPGSSNPDLFLQSLYQSRGSSILSNIIRSSVETSEPVIDLDEPEPLAEPLVSSEAQEPPRSLQYSNRWRRILGQRASPLVDLVQTEEIDNGLGFDNGLGFGMERVAESTMLPKGGGVNLVAEALAEEEDEKKEQSSSHFDCNICLDLAEEPVVTSCGHLFCWPCLYQWLHVHSNTKECPVCKGEVTEMNLTPIYGRGSEKTRKSESTKKGETEEETELNIPPRPHACRIESLRQRLRRPDWRIGDFYRLRRRHTSIGEPAFIGGAIQEEHNHVLDVVDNGVEPFGGIHSHNEHILTRFRIAQRLQRTHLERDRLVRPVNSRNSGDLGQNPRARARGMDGNNGVDGGSGGGHRWGGIGLLSLQRLQRTENAMAMRASLNSLEGVIHRIGSNDRIGSNDASSQPGFNLNNTQSTSLNNQGPQGNGGFEDRTSVSSTAAVIELGSSVIEPGLEPESIGSSDPPRRRRIGASHSIDADGGTSRAPKRRRLN
The following text describes a protein:
Function:
Involved in vitamin D transport and storage, scavenging of extracellular G-actin, enhancement of the chemotactic activity of C5 alpha for neutrophils in inflammation and macrophage activation.
Subcellular Localization:
Secreted.
Sequence:
MMNASLILIYALIVPALLADKGTYTKEKVCQDLQVIGIEKFKEMVTVLYSQKFPNGTFEEVNCVADEMTTLAEKCCKDDASPDCYDKGATEISEKSCRKDSPFPKHPGIEQCCTLQGHERKLCLASLRYSADELPSLLEPTNEEICAEYTKDEKQYAVRYAYEFARRHRNIPAGFVLNATQHHVRMAARCCRPAVKNSCFFQERIQMRSSNIFLRFLSHVCNNQMNLKSYRYGLSAYYGSLLGLSFEEASVLSSRTHSGLEKCCLRPQPECIIEEISSVHNVLCDESKPTAMSEDLRKCCNKPALESLPCVDGLKRQSHQSPDVANPDSSQLCDGAQPHGIDRYLFLIGVKHATISLPVLATIFDRIRDTVTACCSSADASACLTEKESTLKKTTAFLSKLDDTCSQYSKLDLPAFTTLMQKEGGETRKQAWVSWASSCCSKLSPAQLCQKLTEEVIKYDDDSAA
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase. Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MGGKHKPAQRIKNNARPSSSGRSAELLASSSQVPQFAAVKEIRFVPPTLSLLKTEEFDSSVSPAFQIVFKKMNKKDCTTKLKALQEFCDLIASSEAEAVKTILAFWATLYSILATDTDHRVREAVHNAHHQIILKDKKMIAPFLKQLIGPWFTSQYDNYPPAATAASKAFNAAFPQNKVQDCVVFCQKEILTYIYDNLTSKIESNPKHGTNEDAEAKFERIIISSLQGYCLYLNTLTQEQIEKSEDLNKQIISNSRFLKLATHKTAQIRATWFKAVAILYQKAPFLLEEEHKNFVPVVFNNLDESEPPVVGSVWDAALLIMDLGQEWWKLINIEKSYLSKLKKVLREGGQGNATVIYPNLLSLLHKLPPSVRVDQFYDSFFENLRCGLKRKSVISSRSESTAVVAALVECLQYVILVNQENCDLCVKLIKSHLLPLIEWSLRAEQVCYRTVFHQIALLVQYWNRNKNLANYSEYLALFWSNVVTLVESVSKFEEENEDLVDRQIVFLQHLKTIAKPKEQLKVKFEEEARSESHLEGATQIDASYNENLTLLVYTLLKTYVVQIEENKSKVLIPNVYAVVRLFESREFLVGLSRSLYQSDNLVTVYDKLFEWLKSDELSCETLVDLAFILLNYVNDDEKNVILESFLQLSDRQLFGWCVKNAFSHPYNQDSSVQSWIKRSEVGRFLVSVADCNLKIDCPPDLKVLFKLAFAENEDGELLIDKNTLNQIIEKVRAPLLEPRSFEVAIDSCVHLASYITGTIYTENTLLKFGEDLLLALFQFSCNDHTDLEFLTDDTEWEVNTAWQDVVMIFAKNLPKNELQNLNGKFADLVEENFLGKFPTDVNTNCLIQTIVSFIKAVLNGQPFMASEVLRLFFERSFVPTWKNKIEDLCLQAEYLTGSLSRPENYKKETSQVSQEEILKYFVWSFIKISVLSSPLEEDEEENAPKDIIYVTDDQKQLIMDVLYDLTMCQSFLTNYKITKHYKNLSQYYDFIKEKTTQTLEKIQIGDEMTELFISQLNSNSGLWSKVIYLYNQEIFDKPPQETFKTYHNQTTSDLSQLHLVQLYGPHLDFDHVATSSVLNDVVILRSLAHCDEIDVQIAEIFEKIKKLRNRDIPKFLFENKERTCAESEVVIEVIRLFTRLIKVKFENLSRQHWDFGVISLASWASNCCKFRSGYDSGKNQAFMVAISEFYIALNEKINELKRNNVKSGFVDEWEELFLPNVHLDLVQLWLYLAEQFASKTCLLDYHPFLQEFGKVTDHFVYKLIFSKENTLPSWSKILKRCAVLLTNSTSILQLWGYKMLLILVPGLIEIDLQSDSSSTPNTKGFTIGQFKEILLQTHSIVDGVLAGFKLGEDSCQVTPFTDSYTYVFAYLLLWGVLLSMCEKSTPELRYQYADWFRNDDYFKSLLNNLFKLMPTEILHYSEGKTKAFSKLFSQNPGLGFKEPCTSEQLEHIVCWIYSFCLAQLPALVRQWWSQTETKVTQIVEKVTAFYVSPQLCNQELLDITQHENKFKNMTVKIVPSVREVIAVYTVDEAQMELVVTLPQNYPLGDPDVRCSRQIGGPLHKQWLMQLKKYLVHQNGRIWDGLSLWNSSLDKKFDGVEECYICFAVLHPGTYQLPKLTCQTCKKKFHSACLYKWFSTSNKSSCPICRNLF
The following text describes a protein:
Function:
Protease involved in the C-terminal processing of the chloroplastic D1 protein of photosystem II. This proteolytic processing is necessary to allow the light-driven assembly of the tetranuclear manganese cluster, which is responsible for photosynthetic water oxidation.
Subcellular Localization:
Plastid, chloroplast thylakoid lumen.
Sequence:
MEFLSSCASSSSSSSPHFAFFNLHHQNSLTSRATVKLQLLQWNSSAVGIGRSTSLSTDGRERIWSCNCGPRRALSLPQLRSSHSHMSSGFDLISLNCQYVFKWRRYPVNFRRIRSSMEKFRQRFSVQVARVMVCVMLVVSVSSTFGDTSSWALTEENLLFLEAWRTIDRAYIDKTFNGQSWFRYRENALRNEPMNTREETYTAIKKMLATLDDPFTRFLEPEKFKSLQSGTQGALTGVGLSIGYRTIADGPGGLVVISAAPGGPAERAGISSGDVILAIDDTTTESMGIYDAAERLQGSEGSSVQLTIQSGPSVKHLDLVREKVALNPVKSRICELPGSGNDSSKIGYIKLTSFTQKASGAVKEAIDSLRSNSVNAFVLDLRDNSGGLFPEGVEIAKIWLDKGVIVYICDSRGVRDIYDSDGSNTIAASEPLAVLVNKGTASASEILAGALKDNKRAMLFGEPTYGKGKIQSVFKLSDGSGLAVTVARYETPAHIDIDKVGVIPDGPLPASFPKDGDGFCSCFEDPASVCNINRVQLFSR
The following text describes a protein:
Function:
Plays a role in the inhibition of bacterial toxin-antitoxin system by blocking the action of host Lon protease.
Sequence:
MITVDKWFRINRADTGLCNYWPELSAGTVFKVRELVKECEDDIEPDTGIIEIELSDGKIINIYDKPITYWCLWNTESVENGEIEEVVERTNQVVQKPKADFQGERISYALAKLAAQENNDGYEGNLMQAAAEYIEWLETQISFSDRMIQQYKRLHQMFYNT
The following text describes a protein:
Function:
Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor.
Subcellular Localization:
Cytoplasm.
Sequence:
MMQELKILNEKRAEIYWWLSSLFFKELSEQDIARYHSAEVRTFLSGLADEQSLNREVKHLVEALNRLQNRQDAQLELAADFCDLFLKSDRDSALPYASVYTDKGLLNGKPAQQMRELLGAHGVKVEQNLNEPEDHLAIQLDFLAHLAISANQIEHSAQLSSALQAQSDFISQHLLTWLPAFAERCTQFDAFGLYSAAARLALAFIQQDKHCLDELFQETH
The following text describes a protein:
Function:
Peptidoglycan polymerase that is essential for cell division.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MPTLLERLQAPLRERTGETSPNAWVPEARLLVVLILCWLALGLLVLFSASLPVGELQYDDGLRFFTRQALTAAVGLLLMFWLCRTRIDRLFAVALPVFGVLLAMVFLVKIPGIGVELNGARRWLQLGPFSLQPSELIKPCVILLAAPLIANWRRLPNFTRLLGLVAAGLTVGGVLLQPDLGTAALIGVTLWLMGFAGGLPLGGLFAVLAAGGAVAAWKVSTTAYQMGRVTAFLDPWEVARGEGYQLVQSLLAVGSGGLQGTGFGLSAQKSAFLPYPYSDFIFAVFCEEFGLVGAAAFVLFLLLFLVVGLRVAVRCAEPTRRLIAAGATLLLVTQAFFHIAVVTGAVPPKGMPLPLMSYGGSGLIASLLCCALLIRAACEMNLAPAVRFVRRRPAAPPPRPVAPAARPASEPVRREPSPLPAYLLDTAVRSR
The following text describes a protein:
Function:
Component of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with other viral proteins.
Subcellular Localization:
Virion membrane; Multi-pass membrane protein. Host Golgi apparatus membrane; Multi-pass membrane protein. Note=Largely embedded in the lipid bilayer.
Sequence:
MKILLILACVIACACGERYCAMKSDTDLSCRNSTASDCESCFNGGDLIWHLANWNFSWSIILIVFITVLQYGRPQFSWFVYGIKMLIMWLLWPVVLALTIFNAYSEYQVSRYVMFGFSIAGAIVTFVLWIMYFVRSIQLYRRTKSWWSFNPETKAILCVSALGRSYVLPLEGVPTGVTLTLLSGNLYAEGFKIAGGMNIDNLPKYVMVALPSRTIVYTLVGKKLKASSATGWAYYVKSKAGDYSTEARTDNLSEQEKLLHMV
The following text describes a protein:
Function:
Catalyzes the reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and/or for immediate growth after restoration of oxygen; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Sequence:
MMKQELAPANLTDIARTVLKKRYLLKNEHGDVIETPETMFWRVAETIAAVDARYGASAEQVEERAERFYHLMTQGYFEPNSPTLMNAGRPLGQLSACFVLPIDDNLTSIYETLKHQALIHQSGGGTGFSFSRLRPRNDVVRSTMGVASGPVSFMDVYNHSTEAIKQGGTRRGANMGILRCDHPDILEFITCKLDTTKITNFNISVAITDAFMRAVERDEEYDLINPRTGLGQIASRDGLKHPLTGEVLVPAGQPMRLRARMVFDLIVQCAHATGEPGLFFIDRANEYNPVPHLGEYEATNPCGEQPLLAYDVCNLGSINLGKFVTDAGTIDWESLRDVVHESTRFLDNVIDANHYPLEQITQLSQRIRRIGLGVMGWADMLVRLGIPYNSAQAIDLARQVMRFIDEESKVASEQLARERGPFPEWEYSIWGPDATCARRPDGSRIRPQRLLRNCNVTTVAPTGTISIIAGCSSGIEPLFAIAFWRYQADTRMLDINQDFVAQAKREGWYSDELMERIADTGHIHHPEVPASVQRVWVTAHDIAPEWHVRMQAAFQEYTDSAISKTINFPHEATPDQVREAYELAFRLGCKGITVYRDGSRANQVLSTGSTGKSAEPAPASDQPVELKPRPVPAEGLPSHSFPVVTPLGKLRLFVTELDGKPFEVFAIIGRAGSDVTAFTEAIGRLISLALRCGVPVKLIAEQLRGIGGSRSAGFGPDRVRSVPDAIGKVLLDHYVKNGNGNGNGNGNGNGHDYEYGNGETDTSRTYTNGASEATATTPVSHPHSDHGHGTIEAAEICPECQNATMLNEEGCRKCHSCGYSEC
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.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MPLVRVEVRNEYALGAPELYREAKKEDPKEILEGVAVSGLVGVLRQLGDLAEFAAEVFHGLQEEVTITSSRSHKLMARVQRIEAALSPLEKALLAQRSHLHFAYTAGSNWHARIRSEQNHFVYSDVPQFIMESYENCRDPPCLQLLDRFDSGGPGSCLKRYSDPTFFKRSSVASGEASTDKISRDKKGRKIKKRRSFPKNGEVSRDTSAYNSGRMRFGHLNIGVHSPSQTASTYDATLRSDFGEQSNLHLRNGSGFTDGDSRTSYSVQPEEQDSRESISSLAKRRSDFLDYNFVDEQITNAYDDIEINLSEEQAGCIPSSVTWDEKREALDPTRRVSGNNGIKLEDDHNTHLESFSQDLDSEILCDDAVNFVTVDKMDLPSYDHAVESGDVHIDEIESETDHFMDALNTIESEFETEIDCTKKQEVEDYHKLDDKGVDDELIRHNIECQSSNSEPNVLSNPIESECEADIDCTERVVDAENELGRHNMECLSSNSESNVLSNSSLVNGSGAHNLVSTTPKPLDATTSSINGVAAKDEIKAISLAEKDLQSSQQAGDSSSPVSPQHLDSGNNVVSTSWTASANFRDSRPGMPVTDRATNSAESQKQLPETSNAASFTFWTNGGLLGLQPSKPPDFGVSKALPQDQMHKEDAAKQGQMENLKGITDHDDMDSSTCHDYQERGASFRKTSWKISPADLDIKHGKYGDLQYHNNANSTGSSVTTASGSFVPVNSTGSNKKLLTGGSGNYYPTVDHQNANAFEQKINRNGTFSGRSKDPFIGDSPVLSPSSSPPLKHMKISFQPIGGFETTKLKLKFPDVNTNSGNGSDIFPSFQLVPEASFTPQEVGSDSDADTFYRSSPSLSDDCHSNQSESNSDQWESSESPTSKDRDIYDSFRRVSLTESVSAVQEKGRTNRELQLPFTENGAQNSESCGSSDAQSLSTVNNSIRKELRNDTNLNDLVEPLFVPSPAPPPLPPVQWRGSSAPLDGSEDKPESSYYASFDRTHSSSTISQPKPAPLNEDQIDTANTQKLKQSSSWKSNKQREANQSTNVDENDFLRQIRTKSFNLRRTVTAKPTVPSGSSATVQVTAILQKANAIRQAVGSDGEEDGNWSDS
The following text describes a protein:
Function:
Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration. Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain.
Subcellular Localization:
Endomembrane system; Single-pass type I membrane protein. Cell junction, adherens junction. Cell projection, cilium, flagellum. Cytoplasmic vesicle, secretory vesicle, acrosome. Note=The majority of the protein is localized in a perinuclear compartment which may correspond to the trans-Golgi network or the late endosome. The pro-protein is the major detectable form on the cell surface, whereas the majority of the protein in the cell is processed (By similarity).
Domain:
The cytoplasmic domain is required for SH3GL2- and SNX9-binding; Disintegrin domain binds to integrin alphaV-beta3; The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Sequence:
MRLALLWALGLLGAGSPLPSWPLPNIGGTEEQQAESEKAPREPLEPQVLQDDLPISLKKVLQTSLPEPLRIKLELDGDSHILELLQNRELVPGRPTLVWYQPDGTRVVSEGHTLENCCYQGRVRGYAGSWVSICTCSGLRGLVVLTPERSYTLEQGPGDLQGPPIISRIQDLHLPGHTCALSWRESVHTQKPPEHPLGQRHIRRRRDVVTETKTVELVIVADHSEAQKYRDFQHLLNRTLEVALLLDTFFRPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLHWRRAHLLPRLPHDSAQLVTGTSFSGPTVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDLPGNSCPCPGPAPAKTCIMEASTDFLPGLNFSNCSRRALEKALLDGMGSCLFERLPSLPPMAAFCGNMFVEPGEQCDCGFLDDCVDPCCDSLTCQLRPGAQCASDGPCCQNCQLRPSGWQCRPTRGDCDLPEFCPGDSSQCPPDVSLGDGEPCAGGQAVCMHGRCASYAQQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRNPSGSYVSCTPRDAICGQLQCQTGRTQPLLGSIRDLLWETIDVNGTELNCSWVHLDLGSDVAQPLLTLPGTACGPGLVCIDHRCQRVDLLGAQECRSKCHGHGVCDSNRHCYCEEGWAPPDCTTQLKATSSLTTGLLLSLLVLLVLVMLGASYWYRARLHQRLCQLKGPTCQYRAAQSGPSERPGPPQRALLARGTKQASALSFPAPPSRPLPPDPVSKRLQAELADRPNPPTRPLPADPVVRSPKSQGPAKPPPPRKPLPADPQGRCPSGDLPGPGAGIPPLVVPSRPAPPPPTVSSLYL
The following text describes a protein:
Function:
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Subcellular Localization:
Cell inner membrane; Peripheral membrane protein.
Sequence:
MASLKEVKTRINSVKSTRKITSAMKMVASAKLHKAQGAIENMLPYERKLNKILTNFLSADLPVESPYIKAREVKRVAIVAFSSNTSLCGAFNANVIKMLLQTVGEFRTLGQDNILIFPVGKKVDEAVKRLGFEPQETSPTLSDKPSYQEASELAHRLMEMYVSGEIDRVELIYHHFKSMGVQILLRETYLPIDLTRVVDEEEKQKEEEVQGGEIANDYIIEPSAEELIANLIPTVLSQKLFTAAVDSNASEHAARTLAMQVATDNANELIQDLTKQYNKSRQQAITNELLDIVGGSMQ
The following text describes a protein:
Function:
6-hydroxytryprostatin B O-methyltransferase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities. The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA. Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B. The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively. The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B. Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties. In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).
Sequence:
MTQAVDIGTIQTLIRLEVPDQVPLTGSIPYDALVKKLKTPVDPELLQRLIRFTRLVGFLDEDAEGAVKHSPMSAIFVNDPDTAGQARFMADFGIRPCSFIYESIKLDPSGEAARQGPLALMAREPGAREGPTFFEVLEKDPVNRKRWHDGMAVHNDSMVRHVAGAYDWGTVQSLVDIGGSEGHVAAVIVNAFPHIQITVQDRPEIIEKARQRGDRHPNIIFEEHDFFTPQPRIADAYFLRLILHDWNDADCTRIVRQISSALRPGARLLIMDAVLPEPGEGSLQSERRLRRSDIGMYTLFSAKERSLAQMRRLVEDCDSRLRFEKLYTPPGSHASMLSWICE
The following text describes a protein:
Function:
Able to cleave the C-S bond of sulfoxide derivatives of Cys to produce allicin, thus giving rise to all sulfur compounds which are responsible for most of the properties of garlic, such as the specific smell and flavor as well as the health benefits like blood lipid or blood pressure lowering.
Subcellular Localization:
Vacuole.
Domain:
The 6 Cys residues of the EGF-like domain are arranged in a disulfide pattern different from the one found in the canonical EGFs. The function of this domain is unclear. It may be a binding site for other proteins or the docking site for a putative alliinase receptor.
Sequence:
MVESYKKIGSCNKMPCLVILTCIIMSNSLVNNNNMVQAKMTWTMKAAEEAEAVANINCSEHGRAFLDGIISEGSPKCECNTCYTGPDCSEKIQGCSADVASGDGLFLEEYWKQHKEASAVLVSPWHRMSYFFNPVSNFISFELEKTIKELHEVVGNAAAKDRYIVFGVGVTQLIHGLVISLSPNMTATPDAPESKVVAHAPFYPVFREQTKYFNKKGYVWAGNAANYVNVSNPEQYIEMVTSPNNPEGLLRHAVIKGCKSIYDMVYYWPHYTPIKYKADEDILLFTMSKFTGHSGSRFGWALIKDESVYNNLLNYMTKNTEGTPRETQLRSLKVLKEVVAMVKTQKGTMRDLNTFGFKKLRERWVNITALLDQSDRFSYQELPQSEYCNYFRRMRPPSPSYAWVKCEWEEDKDCYQTFQNGRINTQNGVGFEASSRYVRLSLIKTQDDFDQLMYYLKDMVKAKRKTPLIKQLFIDQTETASRRPFI
The following text describes a protein:
Function:
Tubulin-folding protein; involved in the first step of the tubulin folding pathway.
Sequence:
MENSEDISLNSSEKSIESSVVNLEDQQQSQQQTQQQTCQKTFVQEAPELTILIDKLIQLKHSNKDELISNTTRIIYIIDQYLEQPTLLDIHLNDIIQPLINFIKSNYINNSNNNNTTTTTTTIMTETEIVIKKLSIKNSFRIIYVLSKVRGFKTIVKLFQHEAIDLLPVLDQLEISYHQWVNINKQRDRLNEISVSYSSGINLKNYIKPEEESEQEVVDENNNNINNNHNIDDEYNENIISWEEVYVLALWVSLLVIIPFKFSSLDSASSGTASAAGDGGDGDGDGQLKSISSRILKLGKLALSDVSKIRDSFSELLSKLLNRPDMKFEQKQFIKWCTNSIQLISNNNNNNNQNNSSNNNILLIIGIYSTLATMFKKGNRLDFLPIDMNLYEKIMEANKYLSLSGSERITKKIFLKLLQRIAIIMLPPVSASWRYQKIIKPLLLKGELIKQINNNNNNNNNENNNEEGEEEEEEIPEEIDEILEEIMKSLKDKDTIIRWTSAKAIGRIVNLLPKDMGDQVIGLVIDQMFEKNEFIDADPSAWHGGCLALAELARRGLLLPERLDVVVPLVIRALFFDIIKGTYSIGSHVRDSACYLCWALARTYHNSILSPYLLPICRNLVVVSLYDREINCRKSASAAFQEMVGRHQGLVPNGIEIVTSADFFTVGNKNNSFTSLTTFIGKFQIDYYPIVIKHLATIKIYNWDLEIRQLASKSIHLLTNINPNDIVSNYLPLIIPNTQSDLVHVKHGASLAISEILISLFENNNINLLSDNLKMMILMTIKNTKNEKLFKGKGGVLIRIGMCKIIYSICLVEFSLDKNLSEIKKPTESTSTNGNEDRAAALKLKIAMLKAKTASQINKPIITPPSSKSTTNNNNNNNNNNLNDNEIAFNIILGYLNENLNHPNEEVQKEASKAFELLFSKYISSNEKISLLLELIDSHCKTLKFDINRSARRGSSLLLGSLPFNSANLSYDLLSKVVNELILSIFQDDPKFKDIETRVNSISSLYKIGIYILNLIFKNQENEQKEEEDFKKSKNYNLFIKIWNCLGLATNDYSIDKRGDIGSWVRELSCKVLFDFIKFIITNQNSSTTTTTASTTDLSIENLINEKMITEFICKLFQLSGEKLDKIRDVACKIIHELLWIENPSSINNIPHKEELKKIIVKDQDVHFNWFRTEESLPLICKVLKFNCYLYPLLFGLFSSLGGTSKYLINDSIQSIKQYFSSFDNDEKERFEKIISFSKAILEITNNTTQRMIQPTFRSIYNLLSTHIFDFLIINNLNEQSIFETILFNCYQIIESNQDDIYLLLNSIELFSYFFIQFENNNNEYIKDYSLKALLLLLSNLKYPKVRKLASDQLKKSTRLFINNNGDDETPSLIKSLIFNTKWDDSVDLIIEPLKSLLLLLNQKHLLELLSENPTKKPIPLAPPITSIEELKDKIQNPHKQSDDNNNNNNGELINNNTENNNNNNFDDNLPEDSQDLMEI
The following text describes a protein:
Function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs.
Subcellular Localization:
Nucleus.
Sequence:
MAARNLACDLINDQFGELVQRGSLLLSEIARFTGIDVAPLGDCLKQLIQHNCVQAFRASVEQEHDGLGAGGRPAPKPNTFYMLILDNVLHRMRFPKFMTLVRDDIGSEAQGLLGALLQHGRLTLDQLLKRAAECAQPGDVEVEMSVKKAFVELVEAHFIERCPLPEPTLPLAEEEQPNKRARMTAQTRERRVLDAAAQSDALRFRLPASLQLQSGDLVTLDDSLITGHKRKEMDTTLLDDKDVIWRVNYEEFIRRLRHQACVRLVSSKCDLGCGTVLACILDRSRKAERSVRQRLSSPLEMEAIVEAVRKTEEGRCMPLERIRCALLQMTADGFVVDRAGEASEHRALMPLGMFPDMRKILDVARQAEIEGIVLQRFGRKCCRIFRLLSTKGRLDHKQISDKSLVPSKEAWELLSKLVKEHFIELEAWHS
The following text describes a protein:
Function:
Autoreceptor for octopamine, which is a neurotransmitter, neurohormone, and neuromodulator in invertebrates. Also acts as a receptor for tyramine, but with much less potency. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MDPINGSHSGANATISDITNGAYNATDAGEWTSSVMFKLRTCVLLLIVIMAVLGNMLVIVSVMRHRKLRVITNYFVVSLAFADILVAMVVMPFNFSVQFNQGWVFGETICDLWNSSDVYFTSTSILHLCCISVDRYYAIVKPLKYPIKMTKKMAFVMLAATWLSPITISYVPIFMGWYTTTDFLESRRDDQCEFKVNKPYAVISSSISFWIPCTIMIFTYLAIFKEANRQEKALHARAGNAMLMHRHSREVSDKNGALHINATTPTKDRNLLKMKREHKAARTLGIIMGAFILCWLPFFLYYVSTSLCDSCNCPEVVTVIMFWTGYFNSALNPIIYAYFNRDFRNAFKNTLACAFCSFCKRSASDLDAMERLDRRGSAQLRVPIPSRRASDLASL
The following text describes a protein:
Function:
Probable serine protease inhibitor.
Domain:
The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable (By similarity).
Sequence:
MGISLRLAEQFSAEEDGGGGGGNLVFSPLSIYSALSVVTAGARGTTLTELLAALGAPSRDALAKNAAEIARALAGGTATGGPRVAHACGLWHERTRSLKLAFRDAAAASFNAATRAVDFLANPEEARKEINSWVAAATENLIDTILPPGSVSTDTGLVVTSAIYFNGTWQTPFRKQDTKKDKFHLLDGHGTVDADFMRTGEDQYIAAHDGFKVLKMPYAHDHAAPQPSPRYYSMYILLPDERDGLSSLEDRMAAAGGGGGGEGFLSEHMPVRRVEVGEFRIPRFKLSFSRSVVRALRGVGVNAVFDRAELPDMIEGEPLRVSDVLHKAVIEVNEEGTEAAAATAVLMEGAARYAPPPPPREDFVADHPFAFFVVEESSGAVLFAGHVVDPTKS
The following text describes a protein:
Function:
Has a dual role in the assembly of mitochondrial ATPase. Acts as a protease that removes N-terminal residues of mitochondrial ATPase CF(0) subunit 6 at the intermembrane space side. Also involved in the correct assembly of the membrane-embedded ATPase CF(0) particle, probably mediating association of subunit 6 with the subunit 9 ring (By similarity).
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. Note=Associates loosely with the inner membrane.
Sequence:
MSEDPQSWSKERKNCERVKRALMSQSPVIIFLKTALDRLNCNIEAKDISCQPCDAQSTGGYIPGKGIVLCENRLYTKKMAENTIAHEMIHMFDDHRFEVDWNNLRHQACSEIRASSMSGECRWTKELRFGNIKTFRKHHQECVKRRATISVQGNPNCKSKEQAEAIVEEVFNSCFNDFRPFEKIY
The following text describes a protein:
Function:
Peptidoglycan polymerase that is essential for cell division.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Note=Localizes to the division septum.
Domain:
Interacts with FtsZ via its C-terminal region, and with PbpB via two extracytoplasmic loops.
Sequence:
MLTRLLRRGTSDTDGSQTRGAEPVEGQRTGPEEASNPGSARPRTRFGAWLGRPMTSFHLIIAVAALLTTLGLIMVLSASAVRSYDDDGSAWVIFGKQVLWTLVGLIGGYVCLRMSVRFMRRIAFSGFAITIVMLVLVLVPGIGKEANGSRGWFVVAGFSMQPSELAKMAFAIWGAHLLAARRMERASLREMLIPLVPAAVVALALIVAQPDLGQTVSMGIILLGLLWYAGLPLRVFLSSLAAVVVSAAILAVSAGYRSDRVRSWLNPENDPQDSGYQARQAKFALAQGGIFGDGLGQGVAKWNYLPNAHNDFIFAIIGEELGLVGALGLLGLFGLFAYTGMRIASRSADPFLRLLTATTTLWVLGQAFINIGYVIGLLPVTGLQLPLISAGGTSTAATLSLIGIIANAARHEPEAVAALRAGRDDKVNRLLRLPLPEPYLPPRLEAFRDRKRANPQPAQTQPARKTPRTAPGQPARQMGLPPRPGSPRTADPPVRRSVHHGAGQRYAGQRRTRRVRALEGQRYG
The following text describes a protein:
Function:
Transcriptional repressor expressed under lysogenic conditions, which specifically binds the host DNA site 'RRGAAG'. The binding occurs cooperatively, probably as 2 copies of a dimer. Possibly prevents RNA polymerase access to the promoters for lytic cell cycle transcription (Probable).
Sequence:
MHRRVEWMTPTDDAILSLLGPPKQLELRSGDIARNTGYSRRRISDRCTVLVDRGLLFRDDEAGHPYYGLTDFGERYVAGELTVDNLEKA
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that methylates the delta-nitrogen atom of arginine residues to form N5-methylarginine (type IV) in target proteins. Monomethylates ribosomal protein L12.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MHRVMEEPSSSTAALCAAEQVTDLLAPSRVARNLELHLAAESGDLALIRSLLASSPSPVSSSSSETDEGGVDVWYEDPSSANWSALHFAAEQGHVEVVRLLLRNGAIWNAVDANGFTAAQVAWSMNHERCYREILEEGVRQTFLLNALRGAESGENEEEHEIGPSEAKRLKADGACDADRGSVVTSADGRHVTLKPVALDVANDTERYLCTPLRFVPDSLGQVRCLDADDNMVMAPWETDIMQLSASLLCSNQARNFSILNVGFGLGIIDTLIQTYKPARHVIIEAHPDAIAYAHQLGFDKLAGVEIFQGRWEDYLIHADPDSDDAIAKMTQLGSFDAVYFDTYSQDYADLKTFFDALPNIMNGPDSRFSFFHGLGATNRFFYEVYTRISELDLKEIGLTTQWTTMQPKVTEQEWQGVKRKYWDLADYYCPLARFDVLD