lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
One of the three PilY1 homologs of X.fastidiosa, which are involved in bacterial twitching motility as component of the filamentous type IV pili (T4P). The twitching motility of this protein is enhanced by calcium, which may provide the bacterium an adaptive advantage in environments with high calcium concentrations.
Subcellular Localization:
Fimbrium.
Sequence:
MLVMGRDHKLYYEAYNDASDLDGDGVLDVGYKPDKITYYGYYNSNVCYRANGTMFQAMSVANGSNGKKCTGAWSGDFLNYLTTSRMDALRKVLFGGYREVDTLTQTILRASYTPQDAHSWGKEYASVSHDGYDISDYAPLSAPGSGHYHLFAVTTLSDNGIPQLRVLADTTFRVWNWVSIERPVAGSDCFTPENKRVSCVSGGSRGISDYPLRVEVCSVADELRESNCKLYQNNTSYKPTGILHDYGENDRMYFGLLTGSYQKNITGGVLHSNVSNFSREINPLTGQFCLNGNCGGGGDVKGIVHTISSFRMLDFNYKDYTYGCGWIATRPVKEGECWMWGNPVAEMMYETLRYFGGATAPRPEYDINSSSQDIATLQLSHPGWKPPYTSVDKGGSGYSVCAQPTMTVFSDINPSYDDKLPGSHWSNFSGSGDPASMRNLDVSAEADRIWEAEGGGSKLFFIGESNNNSDNAPTPKVVSNLSTVRGLSPEEPSKGGTYYSAAVARYGANHKMGGSKFVRTYAVALASPLPKFEFPVGNARVSLVPFAKSVRGFGISATGNFQPTNQIIDFYVQRVANMAGSSGADYDATINGGRPYAEFRINYEDVEQGADHDMDAIALYTIYVNAKNQLVVTLKSEYSAGSIDQHMGYVISGTTRDGVYLEICDLADGHSNDGTRSSCAGQQPYKLNTPPNRLPGYCNATPMPGDCNGLPPVATRIFSVASQGANAVLLKDPLWYAAKYGHDQGVILNSSGGLANYFPVNNALYLRQQVAKAFSAIQSQAGSSGSIAVVGASVSSTSFAVIPSYSSTHDGKDWTGEMTAYRIDANGMIGDVLWLASAGVPSGTSAIAKRVIYTALSHVDDTNRASVVRRFVAEKLVDSSSGDVATDAAQVFGRLGYTPRGVIDDFGSSVTPNQLVNYLRGDKRMEGATLNTAPFRRRFGPLGDMINSIPVVATRRANYGWATASGLPQVQRDSYSAFINARQNSTAAEHIFVGANDGMLHAFDDKGTERFAYVPNGVLHHLGFLANPEYQHHYYVDGKSTLSDAYLDGSWRSVLVGGTGAGGRSMFALDVTSPSTFNESNVLWEMNSENDDDMGYTMGKPYIVPLQNGSWAAIFGNGYNSTNGRAVLFIVNLATGQLIRKIEARDGIDPDGSDPANMGYNGLGNLAVLDTDGDGLVDMVYGADLHGNLWKFNLSGKDPQRWGIAYKDGLGNPIPLFVARNPQGYRQPITGGLEVAVGPSAGYIIYFGSGRYFAANDNNSKDLSTLYGIWDSGSPVIAGRAALSAQIIQASDHPTSPDTRIVTRRPLSYLSKHGWYVDLVVQGQDPQGERSIATPLLQGGRVFFSTYVPGVSVNCASGGSNWLYVLDAASGGAALGQVNIPSRGSRSSIGNSDTGAVSTGGDAPIQSVAMTRTAPRQPVFCNPGEQGCPLVPETHAAPLDTRCSEVIIDPNDPTRSISLFRACGRQSWRQLR
The following text describes a protein:
Function:
Binds tRNA and catalyzes the iron and alpha-ketoglutarate dependent hydroxylation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its dioxygenase domain, giving rise to 5-(S)-methoxycarbonylhydroxymethyluridine.
Miscellaneous:
MISCELLANEOUS: [Isoform 2]: Arabidopsis ALKB8 isoform 2 has an extension of 83 amino acids in its N-terminus, but this extension shares no detectable sequence homology with other plant orthologs. The 159 nucleotide DNA sequence encoding the N-terminal part (53 amino acids) of the 83 amino acid extension is highly similar (94% sequence identity) to the Ac-type transposon Tag2.
Sequence:
MVQPRFVRPTQSSPSSISGEPNSSNLYVANCGPAVGLTHNAIAAVFAEFGEVNGVYAADDSGVRVIVSFADPFSAKAALEALSGRPCPDLKGRSLHIRYSVLQLPSETQVNDCVPVSLIDSELNIPGLFLLPDFVTVAEEQQLLAAVDARHWIGLAKRRVQHYGYEFCYGTRNVDTKKRLGELPSFVSPILERIYLFPNFDNGSASLNLDQLTVNEYPSGVGLSPHIDTHSAFEDCIFSLSLAGPCIMEFRRYSVSTWKASTTDAEKSGDSSCIKKALYLPPRSMLLLSGEARYAWNHYIPHHKIDKVKDKVIRRSSRRVSFTLRKVRNHPCSCKYPQYCDSQQQM
The following text describes a protein:
Function:
Plays a role in endocytosis and trafficking to the vacuole. Functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress.
Sequence:
MSIETISIGNELKDSYKSTSKWVNNGINWLQDISDFYQERSNLEKEYSTKLKELTKKYFDKKSKLSASLSVGDEPAITPGSLENASLVLWTDLLTQTEAIADEKSNLSREFQSKIADNLITLKNKCERVANLANSINDYLVEEKNKFEDEVNKAKKHYDSLCQTTETARDKNEKAPNDKHQKKLDEKQVIMNNGKNEYLIKINVANRLKDKYYYQDVPEILDYLQELNEDRVELMNKLLKNASIIERNSADKVKEKLHAIDQTIEQNNPKLDITMFIKHNAVDWKEPQDFYFIPCSFWHDDESLIIKEPELTELKKKLSIASNEYYKFEQSCIDVKQKLEESTNKRKRDNENITLKFDTGLQGSLSILHKFMKEDTNRVKNEVEIEVIQNFAGDKDLTYVAPVKEKKSRFGFLTGNHKKSQSGGGGGGGATQSDASSEVHSLNPVKTSTSLHSGIFDLRRNKSIASTVSGGVGNGAASIQARALYDYTAAGSDETTIVAGDQLSVIEEDDGSGWTMVNGPQGQGLVPTSYIEITSRGPPPSSQQPQQKKKGPSVAPRCGAKKVQYLEALYDYTADGDDEISITAGDRIVLVQDDTDGSGWTEGELNGQTGMFPTSYVKKI
The following text describes a protein:
Function:
RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular Localization:
Cytoplasm.
Sequence:
MPKDNKTNMTKGYAFIEFSTGAAADMAVILGNGFKLDKNHTLSAIKFDDVEMYANVPDKFIPPPEKTFQPKEHLKSWLADPRCRDQWVMIKEDEVTVYYNNKAEKPEKVESRMKWTDSYVAWSPQGIYLVTVHKQGIALWGGPSWNKLCRFEHPNVKMLEFSPNEKYVVTWSHEPFKTPENAFQHFIVWDVSTGRQLRTFGNEGTGINPNEPRSGPATTIKIDWPVFKWSFDSSYIARMTTGPQGGISVYELPEMGLLDKKSIKVENIQSFDWSPSSNRLGFWTPESGNIPARVTVIEMPSRKITRTKNLFGVIDCKLSWQNDGAYVLVQITRQKTKKQTVTSFEIFRMNEKEIPVDVVEHKQTEDVMSTFWEPHGNRFAVLSTEAQKTFINFYEVEPHTSTSANIGTKLLKSQEVKGINQISWSPKGRFCVLAGLRGMQGDLQFWDVDDLTILNTGDHYMCTDIEWDPTGRYLVTSISAWRVQSDNGFIMWNFAGQQITKQSVNQFKQFVWRPRPKTLLSATQQKTISKNLKEYSARFDRQDAMETNKVSQEVQEERIALWRAWMAYKAKCQEKYNQDRPTRISLYGGVDPDINSRQSENVEELEEWIEEIIDETEEIID
The following text describes a protein:
Function:
Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission (By similarity). Is possibly toxic to mice.
Subcellular Localization:
Secreted.
Domain:
Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Sequence:
MNYFILLFVATFLLLDVNCKKDGYPVDANNCKFECWKNEYCDELCKAKRAESGYCYKLKLSCWCEGLPDDEPTKTSDRCYGTGR
The following text describes a protein:
Function:
This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
Sequence:
MEIKEIKEIISFLKDTDVTELNIEREGFKIRIKRGYIYGPIEITKTVKPSEETVKPSHVVEIQEQEELLHTVTSPLVGTFYRASSPEAAPFVEVGTRVEKGQVLCIIEAMKIMNEIESDVSGIVKKILVENGQPVEYGEPLFLIEVA
The following text describes a protein:
Function:
Plays a role in acrosome compaction and sperm morphogenesis. Is implicated in sperm-oocyte interaction during fertilization (By similarity).
Subcellular Localization:
Cytoplasmic vesicle, secretory vesicle, acrosome. Cytoplasmic vesicle, secretory vesicle, acrosome membrane; Peripheral membrane protein. Secreted. Note=First localized in acrosome granule, later migrates to the inner and outer acrosomal membrane. Released after the acrosomal reaction.
Sequence:
MEAFALGPARRGRRRTRAAGSLLSRAAILLFISAFLVRVPSSVGHLVRLPRAFRLTKDSVKIVGSTSFPVKAYVMLHQKSPHVLCVTQQLRNAELIDPSFQWYGPKGKVVSVENRTAQITSTGSLVFQNFEESMSGIYTCFLEYKPTVEEIVKRLQLKYAIYAYREPHYYYQFTARYHAAPCNSIYNISFEKKLLQILSKLLLDLSCEISLLKSECHRVKMQRAGLQNELFFAFSVSSLDTEKGPKRCTDHNCEPYKRLFKAKNLIERFFNQQVEILGRRAEQLPQIYYIEGTLQMVWINRCFPGYGMNVQQHPKCPECCVICSPGSYNPRDGIHCLQCNSSLVYGAKTCL
The following text describes a protein:
Function:
Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs.
Miscellaneous:
MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice site.
Subcellular Localization:
Nucleus, nucleolus.
Domain:
The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half donut. The number as well as the specific sequence of the repeats determine the specificity for target mRNAs (By similarity).
Sequence:
MVSVGSKSLPSRRHRTIEEDSLMGERGKSSNNHSERNKGMRRKDHKGNRGFDVDSSKKNQSGGAPNVKPASKKHSEFEHQNQFVRKEIDPETSKYFSEIANLFDSNEVELEERSVICGNALEETRGREYEIATDYIISHVLQTLLEGCELDQLCSFIRNSASVFPAIAMDRSGSHVAESALKSLATHLENPDAYSVIEEALHSICKVIVDNPLDMMCNCYGSHVLRRLLCLCKGVSLDSPELYGAKSSKALAKRLNLKMSQLDDNNLEIPHQGFPGMLTYLLSGLLSCSREDMKYLQVDQYSSLVLQTALRLMLKQDEQLLEIIPLILRCNSTNKKVEGFHIETNVAKEILESMKDNSFSHLVEVILEVAPESLYNEMFNKVFKNSLFELSVDRCANFVIQALISHARDQEQMGIMWEELAPRFKDLLEQGKSGVVASLIAVSQRLQSHENKCCEALVGAVCSTNESRISILPRLLFLDYYFGCRDKSTWEWAPGAKMHVMGCLILQGIFKFSSDHIQPYITSLTSMKAEYITETAKDSSGARVIEAFLASDAATKQKRRLIIKLRGHFGELSLHTSGSFTVEKCFDACNLTLREAIASELLDVKVDLSKTKQGPYLLRKLDIDGYASRPDQWKSRQEAKQSTYNEFCSAFGSNKSNFPKNTFVSDASEDAAQEIEVKNTRKEIDHHPTSGFKRHREKHAKDKDEPFAGEKRSKQKKNKTSEATDKPKLAGSKRPFLSGEMTGKNRHSNKMRI
The following text describes a protein:
Function:
Catalyzes the reversible isomerization between hydroxypyruvate and 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde).
Sequence:
MGFADQRFNVNLSILFTELPLLERPAAAAAAGFTAVELWWPWIDSPTPEQSELDALKSAIEDAGVQLTGLNFYAGQLPGPDRGALSIPGEESERFRANIDVAADFARSLGCTALNALYGNRVEGVDPAEQDRLALENLVLAARAADRIGAVLLVEALNKPESPRYPLVSAPAAIAVVDRVNEATGLGNAKFLMDLYHLSMNGEDLPQVIDAYAAKTGHVQIADNPGRGAPGTGSLPLEDLLDRLAKAGYDGWVGLEYKPGDDPSAQSFSWLPAGARAAR
The following text describes a protein:
Function:
Implicated in the coupling of mother cell to forespore gene expression. Required for spore formation at 37 degrees Celsius, but not at 30 degrees Celsius. SpoIVFA plays a central role in both maintaining the SpoIVFA/BofA/SpoIVFB complex and anchoring it to the outer forespore membrane. SpoIVFA brings BofA into close proximity to SpoIVFB, allowing BofA to inhibit SpoIVFB. Increased accumulation of SpoIVFA seems to inhibit the activity of SpoIVFB and thus regulates the activation of sigma-K.
Subcellular Localization:
Forespore outer membrane.
Sequence:
MSHRADEIRKRLEKRRKQLSGSKRFSTQTVSEKQKPPSWVMVTDQEKHGTLPVYEDNMPTFNGKHPLVKTDSIILKCLLSACLVLVSAIAYKTNIGPVSQIKPAVAKTFETEFQFASASHWFETKFGNPLAFLAPEHKNKEQQIEVGKDLIAPASGKVQQDFQDNGEGIKVETSSDKIDSVKEGYVVEVSKDSQTGLTVKVQHADNTYSIYGELKDVDVALYDFVDKGKKLGSIKLDDHNKGVYYFAMKDGDKFIDPIQVISFE
The following text describes a protein:
Function:
Guanylate cyclase involved in the production of the second messenger cGMP (By similarity).
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Domain:
The protein kinase domain is predicted to be catalytically inactive.
Sequence:
MASSVGWQTSASAIEIAMDRIKSEHLIDNIGINFIYVFDDCNEAKAAGLSSKLLMDANVSAIVGPTCNAAGLAVVNLAGYYNTPVLTWGLTISSSFIDTSKYPTTVTIVPVAKSIAAAIHEVMIQFEWTEFVYVFVEDEKCGYFRDDLEQITSDSNYTSLSRTIQIYDQSYTNLVRQLEKLKTVSRIFTVCLPEAGDIKRRFMLAAYDLDMTTDEYVYLFAGPKSTAYQQTSSTGDVVGIWVDWSENPDGRDEEAKLAFMRTMVIVATPVQGEQYAAFKKEVIERMKLPPYNCVDECKEKEYQEAAEYADQLHDTIYLYALILNKTIEEQGIEQIANGSNIVTRGAGIEFEGMSGVVRMNGIGYRLPNMNLANLDSNATQRTVAYMDIDSTSVNWTFAIIDQALIWDAYNGKLPQTRPECGYSGKSCPVNFFVDYLYIVVIVAVIIVLCCAAAAIAAFLVIKARRDEELRLDDQWIVPHGMLQSIIKGRKESHHSSRSLQSNSTTTTGTTGISSRSVFFPETETQGYFVYMNEPVLARKYQLRVPIFKQDRSELRMLRSIEHDNVNRFIGLSIDGPVYMSFWRYCSRGSIKDVIAKSSINMDGFFIYCLIKDIASGLQYIHHSPIKQHGSLTSECCYINDRWQVKIGSYGLSFMQGVEKRTEDGLLHTAPEVLREGLTSGTQAGDVYSFSIVCSELVGHSSAWNLENRKEEADEIIFMVKRGGRTPFRPSLDDVDDDINPAMLHLIRDCWDEDPKQRPNIDMVNKLMKNMNSGRSGSANLMDHVFSVLEKHASSLEDEVQERMKELVEEKKKSDILLYRMLPQQVAERLKLGQSVEPEAFESVTIFFSDVVGFTVLANKSTPLQVVNLLNDLYTTFDAIIEKNDSYKVETIGDAYLVVSGLPRRNGTEHVANIANMSLELMDSLQAFKIPHLPQEKVQIRIGMHSGSCVAGVVGLTMPRYCLFGDTVNTASRMESNGKPGFIHLSSDCYDLLTSLYKEYNTESRGEVIIKGKGVMQTYWLLGMKEESA
The following text describes a protein:
Function:
Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling (By similarity).
Subcellular Localization:
Cytoplasm. Cytoplasm, cytoskeleton, cilium basal body. Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme.
Sequence:
MNPREEKVKIITEEFIENDEDADMGRQNKNSKVRRQPRKKQPPTAVPKEMVSEKSHLGNPQEPVQEEPKTRLLSMTVRRGPRSLPPIPSTSRTGFAEFSMRGRMREKLQAARSKAESALLQEIPTPRPRRLRSPSKKELETEFGTEPGKEVERTQQEVDSQSYSRVKFHDSARKIKPKPQVPPGFPSAEEAYNFFTFNFDPEPEGSEEKPKARHRAGTNQEEEEGEEEEPPAQGGGKEMDEEELLNGDDAEDFLLGLDHVADDFVAVRPADYESIHDRLQMEREMLFIPSRQTVPTYKKLPENVQPRFLEDEGLYTGVRPEVARTNQNIMENRLLMQDPERRWFGDDGRILALPNPIKPFPSRPPVLTQEQSIKAELETLYKKAVKYVHSSQHVIRSGDPPGNFQLDIDISGLIFTHHPCFSREHVLAAKLAQLYDQYLARHQRNKAKFLTDKLQALRNAVQTGLDPEKPHQSLDTIQKTINEYKSEIRQTRKFRDAEQEKDRTLLKTIIKVWKEMKSLREFQRFTNTPLKLVLRKEKADQKADEEAYEAEIQAEISELLEEHTEEYAQKMEEYRTSLQQWKAWRKVQRAKKKKRKQAAEEHPGDEIAEPYPEEDLVKPSPPEPTDRAVIEQEVRERAAQSRRRPWEPTLVPELSLAGSVTPNDQCPRAEVSRREDVKKRSVYLKVLFNNKEVSRTVSRPLGADFRVHFGQIFNLQIVNWPESLTLQVYETVGHSSPTLLAEVFLPIPETTVVTGRAPTEEVEFSSNQHVTLDHEGVGSGVPFSFEADGSNQLTLMTSGKVSHSVAWAIGENGIPLIPPLSQQNIGFRSALKKADAISSIGTSGLTDMKKLAKWAAESKLDPNDPNNAPLMQLISVATSGESYVPDFFRLEQLQQEFNFVSDQELNRSKRFRLLHLRSQEVPEFRNYKQVPVYDREIMEKVFQDYEKRLRDRNVIETKEHIDTHRAIVAKYLQQVRESVINRFLIAKQYFLLADMIVEEEVPNISILGLSLFKLAEQKRPLRPRRKGRKKVTAQNLSDGDIKLLVNIVRAYDIPVRKPAVSKFQQPSRSSRMFSEKHAASPSTYSPTHNADYPLGQVLVRPFVEVSFQRTVCHTTTAEGPNPSWNEELELPFRAPNGDYSTASLQSVKDVVFINIFDEVLHDVLEDDRERGSGIHTRIERHWLGCVKMPFSTIYFQARIDGTFKIDIPPVLLGYSKERNMILERGFDSVRSLSEGSYITLFITIEPQLVPGESIREKFESQEDEKLLQATEKFQAECALKFPNRQCLTTVIDISGKTVFITRYLKPLNPPQELLNVYPNNLQATAELVARYVSLIPFLPDTVSFGGICDLWSTSDQFLDLLAGDEEEHAVLLCNYFLSLGKKAWLLMGNAIPEGPTAYVLTWEQGRYLIWNPCSGHFYGQFDTFCPLKNVGCLIGPDNIWFNIQRYESPLRINFDVTRPKLWKSFFSRSLPYPGLSSVQPEELIYQRSDKAAAAELQDRIEKILKEKIMDWRPRHLTRWNRYCTSTLRHFLPLLEKSQGEDVEDDHRAELLKQLGDYRFSGFPLHMPYSEVKPLIDAVYSTGVHNIDVPNVEFALAVYIHPYPKNVLSVWIYVASLIRNR
The following text describes a protein:
Function:
Is the main repressor of the genes involved in the de novo synthesis of purine nucleotides, regulating purB, purC, purEK, purF, purHD, purL, purMN and guaBA expression. In addition, it participates in the regulation or coregulation of genes involved in de novo pyrimidine nucleotide biosynthesis, salvage and uptake (pyrC, pyrD, carAB and codBA), and of several genes encoding enzymes necessary for nucleotide and polyamine biosynthesis (prsA, glyA, gcvTHP, speA, glnB). Binds to a 16-bp palindromic sequence located within the promoter region of pur regulon genes. The consensus binding sequence is 5'-ACGCAAACGTTTTCNT-3'. PurR is allosterically activated to bind its cognate DNA by binding the purine corepressors, hypoxanthine or guanine, thereby effecting transcription repression.
Miscellaneous:
MISCELLANEOUS: The corepressors hypoxanthine and guanine bind cooperatively to single PurR sites in each subunit of the dimer, inducing a conformational change which increases the affinity of PurR for its DNA operator sites.
Domain:
Consists of two structural and functional domains: an N-terminal DNA-binding domain, approximately the first 60 residues, and a larger C-terminal domain, approximately 280 residues, which imparts the function of corepressor binding and oligomerization.
Sequence:
MATIKDVAKRANVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEEYRHIPMVVMDWGEAKADFTDAVIDNAFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESWIVQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGETAFNMLLDRIVNKREEPQSIEVHPRLIERRSVADGPFRDYRR
The following text describes a protein:
Function:
Probably involved in the biogenesis of the COX complex.
Subcellular Localization:
Membrane. Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MFNIHTTRLVKLKPIRLLQFNRSVKTLTMDWKPMKAVPGNLRTLEHQSKMPTIRRVLLGLMYAMPIISFALGCWQVHRLQWKTDLIAKCENNLAAPVIPELPPNLDPSVIADFEYRRFKCRGRFDYDQEMFLGPRLKDGELGYLVVTPFIRKNGGDPILIERGWISKDKVVPSSRSSGYLSHLARPQGEIEIEALFRVMPKKSFLQLEHEQGSRLFHVPDVPAMAKQSGSLPIYCQMIYDLHDHIDWRKDENGQQQKPSVISSLLFSKKKDSDAAFIATNANKDETLQFQEFEFVNEGVPIAAKPFIKFSNNHLQYLITWFGLSIGSTVLLLFSIYKSKQFATAEQLLAAKRKDMQKKA
The following text describes a protein:
Function:
A site-1 protease (S1P) that cleaves the peptide bond between 'Val-148' and 'Ser-149' in RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. When heat shock or other environmental stresses disrupt protein folding in the periplasm, DegS senses the accumulation of unassembled outer membrane porins (OMP) and then initiates RseA (anti sigma-E factor) degradation by cleaving its periplasmic domain, making it a substrate for subsequent cleavage by RseP. This cascade ultimately leads to the sigma-E-driven expression of a variety of factors dealing with folding stress in the periplasm and OMP assembly. Required for basal and stress-induced degradation of RseA (By similarity).
Miscellaneous:
MISCELLANEOUS: Regulated intramembrane proteolysis (RIP) occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. A membrane-spanning regulatory substrate protein is first cut extracytoplasmically (site-1 protease, S1P, this enzyme), then within the membrane itself (site-2 protease, S2P), while cytoplasmic proteases finish degrading the regulatory protein, liberating the effector protein (By similarity).
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein.
Domain:
The PDZ domain probably binds peptides ending with C-terminal Tyr-X-Phe sequences, which activates proteolysis. In the absence of OMP peptides the PDZ domain inhibits peptidase activity (By similarity).
Sequence:
MLKKLFHSALWGLAAAGVILFAVPRLNNSNIFTSDDIISFKNAVRIASPAVVNVYNRSFSSASINDNDQLQVNNLGSGVIMSKDGYILTNKHLIQNADQIVVALQNGNIFEASLVGSDDLTDLAVLKIRADNLSTIPQNSARQAHVGDVVLAIGNPYNLGQSVSQGIISAIGRNAVGDSVGRQNFIQTDASINRGNSGGALINSAGELVGISTLSIGKTANEIAEGLNFAIPIDIANDVLRKIMRDGRVIRGYFGVQSDISSSSEEGIVITDVSPNSPAAKSGIQVGDVILKLNNQEGISAREMMQIIANTKPNSKVLVTILRLGKILQIPVVIEEFPVN
The following text describes a protein:
Function:
Has antibacterial activity.
Subcellular Localization:
Secreted.
Sequence:
GLMDMVKGAAKNLFASALDTLKCKITGC
The following text describes a protein:
Function:
Acts as an osmosensitive calcium-permeable cation channel.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MNSTNSTNSTTTATSTNTSTQQVVTSLVSNGTIFGVFVIAFLILRIKLKRIYEPKSSFNLINEEKKPEPLPQGVWQWLKPLLKKSDNFVIQQAGLDGYFFLRYLFIIAIYCAVSMSYIFPILLSINASNGNHESGLNQLAYQNVKHRGRYFAHVFCGWIFFWGFLYIIYRELYFYTSMKQAVLASPRYAKKLSSRTVLFQTVPKQYLSEEEFSKLFDGVKRVWIARGSGSIEAMVKARDNMAIQLEGAETKYLKAALKKIKKLNKKSPQLSVSDNIAEYVPDKKRPHHKINKVAKFFFGKKVDTISYIKEELPKLNQKVKALQEDHENSSPFNSVFVEFESQYQAQVAAQITTYHAPLFMTPVYIGIEPSDVVWFNLRMFWWERLGREVSAVSAIVALVILWAFPVAFVGMISNITSLTNEVKWLKFIYKLPKQLLGLLTSLAPTVALAVLMSFLPKFIRGMAITQGAPSKQNVEYFTQQAYFAFQVIQVFLVTTLSSAATSTVTEIVKEPTKAMDLLASNLPKASNFFMSYVILQGLSISSGALLQIVPLILFYVLGAFLDGTVRKKWNRFCGLSSMQWGTAFPVYTNLAVITFSYSIISPLILLFAAVAFFLLYIAYLYNLTYVYQESPDARGIYYPRALFQTIVGIYIGQICLLGLFAVGKGWGPIVLQVIGICVTVLIHLHLSAAFDHLSKVIPVDTMKPLDGVSDTPSFKNIYKGIESTKVKKNTFGANIDMDGIKELPEFPIKKYHKRSESVTEQQVENSIFSENTFEYQFNPANEANADGHAINAENLIEDVPLLADGDTMKIPPAPWWKRFLKPHIYYSYKAVKSRLPEIYGLVDPDERVNDFDISHAYDYPAVSAQCPELWIPRDPFGFSKLLISDVSGVVEMNDENATIDENLKFTLRDVPPPYNDVKDEANGEANGEFDTASKENNPFADPKYKEEESRSAV
The following text describes a protein:
Function:
Involved in isoflavonoid biosynthesis. Converts liquiritigenin to 2-hydroxyisoflavanone which spontaneously dehydrates to daidzein.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein. Microsome membrane; Single-pass membrane protein.
Sequence:
MLLELALGLLVLALFLHLRPTPTAKSKALRHLPNPPSPKPRLPFIGHLHLLKDKLLHYALIDLSKKHGPLFSLYFGSMPTVVASTPELFKLFLQTHEATSFNTRFQTSAIRRLTYDSSVAMVPFGPYWKFVRKLIMNDLLNATTVNKLRPLRTQQIRKFLRVMAQGAEAQKPLDLTEELLKWTNSTISMMMLGEAEEIRDIAREVLKIFGEYSLTDFIWPLKHLKVGKYEKRIDDILNKFDPVVERVIKKRREIVRRRKNGEVVEGEVSGVFLDTLLEFAEDETMEIKITKDHIKGLVVDFFSAGTDSTAVATEWALAELINNPKVLEKAREEVYSVVGKDRLVDEVDTQNLPYIRAIVKETFRMHPPLPVVKRKCTEECEINGYVIPEGALILFNVWQVGRDPKYWDRPSEFRPERFLETGAEGEAGPLDLRGQHFQLLPFGSGRRMCPGVNLATSGMATLLASLIQCFDLQVLGPQGQILKGGDAKVSMEERAGLTVPRAHSLVCVPLARIGVASKLLS
The following text describes a protein:
Function:
Regulates CDK7, the catalytic subunit of the CDK-activating kinase (CAK) enzymatic complex. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Involved in cell cycle control and in RNA transcription by RNA polymerase II. Its expression and activity are constant throughout the cell cycle.
Sequence:
FTYPVSSQKRSWTFANEGQLMEFRVEQNSKYIESHEEEAQGRDLNEHFLTSAEERLLLKQYEIYLFDFCRRFEPTMPKCVVGTAFHYFKRFYLNNSPMDYHPKEILATCVFVACKVEEFNVSINQFVNNIKGDRNKATDIVLSNELLLIGQLNYYLTIHNPFRPIEGFLIDIKTRSNMQNPDRLRPHIDSFIDSTYYSDACLLHTPSQIALAAVLHAASREQENLDSYVTDLLFVSAREKLPGLIDAVRKIRIMVKQYQQPDREKVKAIEKKLDKCRNQANNPDSELYKERLRRLYTDEDDMPAEDASFHIADVSSDTSAMNISQ
The following text describes a protein:
Function:
Catalyzes the formation of the signaling molecule cAMP. May function as sensor that mediates responses to changes in cellular bicarbonate and CO(2) levels. Has a critical role in mammalian spermatogenesis by producing the cAMP which regulates cAMP-responsive nuclear factors indispensable for sperm maturation in the epididymis. Induces capacitation, the maturational process that sperm undergo prior to fertilization. Involved in ciliary beat regulation.
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, cilium. Cytoplasm, cytoskeleton. Cytoplasm, perinuclear region. Nucleus.
Sequence:
MNTPKEEFQDWPIVRIAAHLPDLIVYGHFSPERPFIDYFDGVLMFVDISGFTAMTEKFSSAMYMDRGAEQLVEILNYHISAIVEKVLIFGGDILKFAGDALLALWRVERKQLKNIITVVIKCSLEIHGLFETQEWEEGLDIRVKIGLAAGHISMLVFGDETHSHFLVIGQAVDDVRLAQNMAQMNDVILSPNCWQLCDRSMIEIESVPDQRAVKVNFLKPPPNFNFDEFFTKCMTFMHYYPSGEHKNLLRLACTLKPDPELEVSLQKYVMESILKQIDNKQLQGYLSELRPVTIVFVNLMFEDQDKAEEIGLAIQDAYMHITSVLKIFQGQINKVFMFDKGCSFLCVFGFPGEKVPDELTHALECAMGIFDFCSQVHKIQTVSIGIASGIVFCGIVGHTVRHEYTVIGQKVNLAARMMMYYPGIVTCDSVTYNGSNLPAYFFKELPKKVMKGVADSGPLYQYWGRTEKVMFGMACLICNRKEDYPLLGRNKEINYFMYTMKKFLISNSSQVLMYEGLPGYGKSQILMKIEYLAQGKNHRIIAISLNKISLHQTFYTIQMFMASVLGLDTCKHYKERQTNLRNKVMTLLDEKFYCLLNDIFHVQFPISREISRMSKLKKQKQLEILFMKILKLIVKEERIIFIIDEAQFVDSTSWRFMEKLIRTLPIFIIMSLCPFVNIPCAAASAVMKNRNTTYIVIGAVQPNDISNKICLDLNVSCISKELDSYLGEGSCGIPFYCEELLKNLEHHEVLVFQQTESEEKTNRTWNNLFKYSIKLTEKLNMVTLHSDKESEEVCHLTSGVRLKNLSPPTSLKEISLIQLDSMRLSHQMLVRCAAIIGLTFTTELLFEILPCWNMKMMIKTLATLVESNIFYCFRNGKELQKALKQNDPSFEVHYRSLSLKPSEGMDHGEEEQLRELENEVIECHRIRFCNPMMQKTAYELWLKDQRKAMHLKCARFLEEDAHRCDHCRGRDFIPYHHFTVNIRLNALDMDAIKKMAMSHGFKTEEKLILSKSEIPETSAFFPENCSPEEIREKILNFFDHVLTKMKTSDEDIIPLESCQCEEILEIVILPLAHHFLALGENNKALYYFLEIASAYLIFCDNYMAYMYLNEGQKLLKTLKKDKSWSQTFESATFYSLKGEVCFNMGQIVLAKKMLRKALKLLNQIFPYNLISLFLHIHIEKNRHFHYVNRQAQESPPPGKKRLAQLYRQTVCLSLLWRIYSYSYLFHCKYYAHLAVMMQMNTALETQNCFQIIKAYLDYSLYHHLAGYQGVWFKYEVMAMEHIFNLPLKGEGIEIVAYVAETLVFNKLIMGHLDLAIELGSRALQMWALLQNPNRHYQSLCRLSRCLLLNSRYPQLIQVLGRLWELSVTQEHIFSKAFFYFVCLDILLYSGFVYRTFEECLEFIHQYENNRILKFHSGLLLGLYSSVAIWYARLQEWDNFYKFSNRAKNLLPRRTMTLIYYDGISRYMEGQVLHLQKQIKEQSENAQASGEELLKNLENLVAQNTTGPVFCPRLYHLMAYVCILMGDGQKCGLFLNTALRLSETQGNILEKCWLNMNKESWYSTSELKEDQWLQTILSLPSWEKIVAGRLNIQDLQKNKFLMRANTMDNHF
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.
Sequence:
MYNLPVLPPELRPIVYRSGDKVVTSDINELYKRVIRRNNNLAYLLKRSELAPADLVMCQEKLVQEAVDTLLDSGSRGQPTRDGHNKVYKSLSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHQCGLPLEIAIKLFQLFVIRDLITKRATSNVRIAKRKIWEKEPIVWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPTLVEGRTICLHPLVCKGFNADFDGDQMAVHLPLSLEAQAEARLLMFSHMNLLSPAIGDPICVPTQDMLIGLYVLTIGNRRGICANRYNSCGNSPNKKVNYNNNNYYKYTKDKEPHFSSSYDALGAYRQKRIGLNSPLWLRWKLDQRVVGSREVPIEVQYESFGTYHEIYAHYLVVGNRKKEIRSIYIRTTLGHISFYREIEEAIQGFSRAYSYTI