lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenylation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and with PAB1.
Subcellular Localization:
Cytoplasm.
Domain:
The N-terminal zinc finger binds to poly(A) RNA; Contains a pseudokinase domain. The protein kinase domain is predicted to be catalytically inactive because some of the residues important for catalytic activity are substituted and it lacks the equivalent of the binding site for a peptide substrate. However, it has retained an ATP-binding site and ATP-binding is required for mRNA degradation, stimulating the activity of the PAN2 nuclease in vitro. The nucleotide-binding site is juxtaposed to the RNase active site of PAN2 in the complex and may actually bind nucleosides of a poly(A) RNA rather than ATP, feeding the poly(A)-tail to the active site of the deadenylase and thus increasing the efficiency with which this distributive enzyme degrades oligo(A) RNAs; The pseudokinase domain, the coiled-coil (CC), and C-terminal knob domain (CK) form a structural unit (PKC) that forms an extensive high-affinity interaction surface for PAN2.
Sequence:
MMMNKSKTDWAKDTPCKNITIYGYCKYENDGCIFNHGKPLSTSSNTGGAAAGSAEDSAASGGVTVGNTGKSTFNAKTATSFTPSVAIPDFNNIPSFTPERIVSSPAGDGATAFTPSFNPYGSDSFNPSANVSGPGSAVFAAASGNAGASATAAPRSQSVHVGTGGYLPLAGTAFPTVYPPSHSILQYHLYAPDPPPHLQVPLKANERTPETLFIPNNLREHLLKRNLSALQVFPSDGNLPDIVGDYFGLVPLEFHNRQTGKGRYLGHQNSLYKVFSNFDGKVYIIRRIHDVKTTDVGQISLPFRKWQKVSCPNVVKVKDAFTTLAFGDSSLCVVHDYYPQSNSLYETHVANYTVVPVTQKYLWSYLVQLSNALNEVHRHGLSMNNISLDKVIVTGDPGRIKVGDSAVHDILAFDEGRDIAKEQQADYSAVGALLMDLAQRMLGTRDQPLDSMDIDPLFKRVLAYLLSDEKKTIAEFTALFSHKMLDIISSSQTYSEYIEQHLSRELENGRLFRLMCKLNFIFGRMESSMDIHWSEAGDKFPIILFYDYVFHQVDENGKSVMDLTHVLRCLNKLDTGVSEKIILVTPDEMNCIIISYKELKDSIDSTFRSMTQ
The following text describes a protein:
Function:
FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation.
Subcellular Localization:
Bacterial flagellum basal body. Cell membrane; Peripheral membrane protein.
Sequence:
MSNESLSQNQVENLLKAMETADLDEEGTDAPTETKDSAESKDAENATVGSSAPVVGAAHPADSKPYSPGVPTGARVTAYDFKRPERVGKDQMRAMHSLHESIARNFGASISGLLRTMIEVKLLSVDQLTYSEFVFSLDNPSCFNVIKPLPLEGHWVLDIAPGLAYAIIDRMLGGDPVPGETIRRPLTEIETRLMCRVVELFLEQIVPAWENVIQLEPSIHTTESNPQLAQIVPPNEVAILVGFEVLLGKNRGMMNLCIPFNSIEKYNAKLSRNGWVGYGKTNPTPQSRRKIADSIDAAPVDVVVTLARSKIRTSDLLDLNVGDIITTEQAASSALELSVQDVHKFAAVAGAYKGKKAVQVQSTVEPKYCEPEVDPEEELENDSPATAEAEPVKDELENVLDAAQAKVPTTTQPNASPKASPTKPAPTR
The following text describes a protein:
Function:
Probable methyltransferase.
Sequence:
MSYEYFDNSDRFTLYDIQDIEYNPWIEVKTIANKGRCIYSKKFIPKGTIIFKDIPHSAIVDNQYKKNICNTCFKLFLESNRHNIITCPSCGEVNYCSEYCKQFSKIDTRHFELECKWIHEFSISYKYQLSEDDRNIVLLILKILARRIYEKKPLVFHNPPISSLPDNAASSALNETNSSNEEISFSNVENLPMIPNEVQDLIDHLDEYLANIKNSNEQEPKEQGKENELLKYSKIWKNDLKKLINTSLIIRNLVIDSIEEGHPNKIINSGFIDSEGDSEMTDFNEEPKDIKEIVERLTDFDLNILRLLCKIRSNYFGLWHTGYKSNLNKPIFEITETMKEEGNNETTKKDDEPTNQYMWCGSAVYLKLSLFNHGCFPNCTTLLEYNINHNDYSYYQGFESDNRLSISIITLRDVPQNSELLITYIPLNQKGHERYHNLKSNWMFPCDCLRCFHEKTNPELTEKIFNDSSCKNSKCSGGLLLPIEPNSNEGICRVCKTISAPLPQSFGPLI
The following text describes a protein:
Function:
Catalyzes the ATP-dependent ligation of histidine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (His-AMP). Plays a role in axon guidance.
Subcellular Localization:
Cytoplasm.
Sequence:
PSRAPSVPRRTFPYLGSHVRGLKEEKASAEQIEEEVTKLLKLKAQLGHDEGKQKFVLKTPKGTRDYSPLQMAVREKVFDVIIHCFKRHGAEVIDRPCNFDIAGQFDPMIPDAECLKMIKFRTICSSVDKLDKVSWEEVKNEMVGEKGLAPEVADHIGDYVQQHGGVSLVEQFLQHPKLSQSKQAVEGLGDLKLLFEYLTLFGIDDKISFDLNLAVLLQMPTQAGKEPLGVGSIAAGGRYHRLEGIFDPKGRKVPCVGLSIGVERIFPIVEQKLEVLVASAQKKLLEERLKLISELWDAGIKAELLYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLCSVTSRKEMDVQREDLVEEIRRRTNQPLSM
The following text describes a protein:
Function:
Contributes to the degradation of lignin at the level of the protocatechuate 4,5-cleavage pathway. Catalyzes the hydrolysis of 2-pyrone-4,6-dicarboxylate (PDC) to (4E)-oxalomesaconate (OMA). The keto form of OMA can tautomerize into the enol form, 4-carboxy-2-hydroxymuconate (CHM), under certain pH conditions. Also catalyzes the reverse reaction. Is essential for the growth of Sphingobium sp. SYK-6 on vanillate but is not responsible for the growth of this strain on syringate.
Miscellaneous:
MISCELLANEOUS: This is the first enzyme from the amidohydrolase superfamily that does not require a divalent metal ion for catalytic activity.
Sequence:
MTNDERILSWNETPSKPRYTPPPGAIDAHCHVFGPMAQFPFSPKAKYLPRDAGPDMLFALRDHLGFARNVIVQASCHGTDNAATLDAIARAQGKARGIAVVDPAIDEAELAALHEGGMRGIRFNFLKRLVDDAPKDKFLEVAGRLPAGWHVVIYFEADILEELRPFMDAIPVPIVIDHMGRPDVRQGPDGADMKAFRRLLDSREDIWFKATCPDRLDPAGPPWDDFARSVAPLVADYADRVIWGTDWPHPNMQDAIPDDGLVVDMIPRIAPTPELQHKMLVTNPMRLYWSEEM
The following text describes a protein:
Function:
Forms the apical lamina, a component of the extracellular matrix.
Subcellular Localization:
Apical cell membrane; Single-pass type I membrane protein. Secreted, extracellular space.
Sequence:
MDSYFCALLGLLLLCISGTIALNECDSSPCQNGAECRDGLEGYYTCLCAQGYHGTNCEIRMDQDCGTNLYDQVGSFQSSSYPSNYGSREECFYLIRSHGAHVINFTIEDFNTELNKDVLEYGYGDTVDINNVEGLYQGNIITPVEISVPGSSAWFFFSTDRNVQLKGFRISVSADGNDCLSAPCINGGTCIDGIRSYTCECAPGFTGFNCETDIDECESNPCRNSGLCVDGVNSYTCNCASGWTGPTCLINVDECASNPCQNGVCTDGINRYDCICNSGWAGTNCDIDIDECASNPCLNVGTCNDRVDGYICACASGWEGDICEINTDECASFPCQNEGNCIDLINGFFCACSPGWTGVNCEINVDECTSFPCRNGGQCVDLVNSYRCVCASGWTGVTCLIDIDECTSMPCQNGGICTNGVDGYICACAAGYEGDNCELDTNECRSNPCVNGGFCTDILDGYVCACQPGFTGTRCQSEINECASNPCVNGDCVDILNAYQCTCRAGWSGPRCDINIDECASNPCQNGGMCNDLVNRYTCDCVPGYTGVLCQIEINECASAPCINGLCSDVINAYTCTCQPGWAGTNCDININECASGPCRNGATCNDFVNFYTCDCAPGWTGTHCENDVDECASFPCLNGAICSNQENQFVCTCVLGWTGINCQIDIDECASDPCQNGALCSDLINRYECQCLPGWTGVNCNIEIDECSSGPCQNGAVCNDQLNSFTCVCAPGYTGTFCTEDINECSSNPCQNGGLCNDLLNRYTCVCIPGYTGVNCQIDIDECASRPCQNQGQCLDLIDAYVCSCVSGWAGIHCETNIDECASAPCRNGGSCEDMVNGYTCTCAPGWTGIHCSVDINECTSNPCLNGICSNANNKYFCTCNPGWTGVNCETDIDECASFPCGNGGICDDGINGYICTCGPGWTGTNCFVDIDECVSNPCLNGATCNNLQNRYTCSCAGGFTGNSCETNINECTSAPCLNGGVCLDGINQYTCDCDAGWNGINCEIEINECSSRPCQNGGTCVDGTNSFTCDCASGWTGTLCELDIDECGSGPCQNGGVCTQGIDYYVCTCQPGWNGYNCETDRQECNSDPCQNGGTCFDGVDGYSCQCVTGFTGTHCETDINECASNPCMNGATCLNEVNQYSCRCAPGYEGNNCQFDTNECASNPCLNGATCNDRVNLFTCTCQPGYTGVRCEQDIPECNSGPCQNGANCVDLVNDFTCVCVAGFTGLRCEFEIDECASSPCLNGGACNNGINQYTCDCRSGFEGTNCETDIDECASGPCLNGGICTDQIDLYTCECASGWTGINCQLDIDECASNPCLNGAQCVDNVDNFDCVCTSGWEGTFCELGTNECGSNPCANGGRCFDLFDSFTCQCVPGYTGVTCETDINECGSNPCQNGGICSQSVDYYSCVCPAGYMGVNCETDINECASNPCRNGGNCADLVNGYECTCQVGWLGTNCDIGADDCALSPCVNGAICLDGDNDFTCACLAGFEGDLCEIDVDECASNPCQTDAICLDGINRYTCTCAPGWTGYNCDEDINECASNPCINGGECNNMQNAFSCNCTAGWTGVTCETDVNECASTPCFNSGICTNGRNVYTCTCQPGWSGTNCETNIDECQSVPCQNGGQCIDFENRYQCTCMAGWIGINCEIGVNECFSNPCVNGICVDMEDGFECRCDLGYNGTLCENNIDECASDPCVNDGTCVDGLNSFTCVCVEGWTGRLCSTDVNECGSNPCLNGAVCLNEFARFSCVCLFGYTGIICETNIDECGSLPCMNGGLCFNDGNDGYTCECTPGYNGIHCENEILECASNPCLNGATCVEGLNSISCLCQPGYAGFLCGTNIDECESYPCENGGACRDGVNGFTCSCPTGYSGDRCEINLNECASNPCDNLGTCVNRVESHGYDCFCQPGFTGTHCEINIDECANQPCLNGGICNDLANGYRCTCPMGWAGDNCEQSVGCRVNYTLAVGTKLEIHSPNYPSNYGNMENCRWFIQGINGRQVTVEIKDYITENRYDEFRLGVGSNPNDEGSRRMTLSGPGPFSTRTMTLQANNIWTTFITDNEKTERGFSIEITDSAYVAITPCDAEPCINGGTCENVGNTRFTCSCTSLWTGQQCEEPAEMNKCAFHPCTNGAECTNIGLDYTCTCPVGFTGKNCSMEIDECASNPCQNGGTCQDLIGAYVCICANCFSGVNCDQAPVTDSCIKNVCENSGECSFYDGYFTCTCQDGYSGDYCEKDFDFCRNAPCLNGGTCTSLNGTFSCDCQDNYIGITCSIQVTLSCVHANPCQNGALCTYIDESYLCSCPSGITGEFCETNIDNCDPYPCANNGVCEDGIDFFSCYCPSGFSGDLCEIDIDECGSNPCQNGGTCLNGINKFFCQCPESLDQPVCASVVVNQAAQSGDTFLGAEINLNPWYILLIVALALIAIFFLLLFISSAACRKNKSALYDAELAKKERERGVPNSQLHDTLPIFDDERPLSRDNDYGFLPPNAVESNVREVNSYENPWPQSTDEMQKTHL
The following text describes a protein:
Function:
Assembly factor required for Rieske Fe-S protein RIP1 incorporation into the cytochrome b-c1 (CIII) complex. Functions as a chaperone, binding to this subunit within the mitochondrial matrix and stabilizing it prior to its translocation and insertion into the late CIII dimeric intermediate within the mitochondrial inner membrane. Modulates the mitochondrial matrix zinc pool.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MTKFPAALKPAARSAYREVLRAARITFQGDSTRHHALLTALRATFSSPTLTPPPSASSPPVIPISEESIGVDDVAKRITEWKELARFLKRNVVQGVRSDDGAWKLRVTEHTELGDNASVKNPPKLPTTPFPNRNRRKCSDAAPAS
The following text describes a protein:
Function:
As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage.
Subcellular Localization:
Nucleus.
Sequence:
MAKFTLTANSLEKVMSGLPCEKPVVQVLGHKKIVGAGQGPERFRLLLSDGVHTVSSVMLATQLNDKVTSGQIDINAVVRLDKYICNIIQAEKRVVVVLELTVLGVSSIVGGKIGNPQPYKQQAAGELTNSNVTAATAAADLRQQLPLQAQNNNSNNNSGFSGKSQFDNTSAKQQQQRTQSSTSSSVSQQINKNNSSMLDTPSKITSISSLNPYLNRWTIKARVTQKSSIKTWSNSKGEGKLFSMNLIDQSGEIRATLFKNEVDKFFDMIEVNKVYFIRKAQLKIANKQFSNLNNDFELTFTGETEVIPCADGEDCDDDGQQLPSISFNFVGIDKFEQMQPNVIVDVIAVVKDCGDLKVVTQRQSNKEIKKRDITLVDQSKVQVTLTLWGDYAESFKAEGNPVLAIKGVRLTDFGGRSLSQSNNSQILENPDFPECHSLRGWFDNVGCSAEYSEYKKEQTSSFGGPLLYKTMLESKNELHDGEAANYFMATATIPVFKKDNSLYKACPQPDCNKKVVDCGNSSYRCEKCSKEFGTFKWRLILQMNISDFTESQWVTAFNEVAETILNIKADELGALKDTDSTRFDQVFTNASFSTFTFKLRSKVEKYNDESRLKTACIQATPISYADENKRLILILEKYLQ
The following text describes a protein:
Function:
Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MRNVPQSYCFVTILFDSVNKLGTQIVNPYSVKQYVMQQQVKNFRHSVRSVFFLSEIFGLVNLKYRETYFRLSKTKTFCTLVTALVYCSLAIFVLCELLIEGTTSILINVPSLIIHVSTSAYVATVWINSVINRWKFIEFIRKVLEFDVKCVSNYTKQQSKIHLIVRSVFVTTYLMFDYCTVLRVQRFNNYQSLAHYLRVFFTVFNVVHCYLASELVLMLKNRFVTLNVQLTKLTKNCATKAQSVVLGRICTLHHHLSKLVTRFNEIFGLGLLLMFGVSFLLITQTIFIICVIVQSEQIAWLHLLYIFLVGIMYAADVFYICHVCCSTIHEVSKAGELIHKIETNDHEIIDKIEMFSLQILNERAGFSAAGFFPIDYSLVFSFLGGVTTYIIILLQLSSSVPV
The following text describes a protein:
Function:
Component of the survival motor neuron (SMN) complex that catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. One of 3 almost identical paralogs (Glos/Gem4a, Gem4b and Gem4c), resulting from a genomic triplication, that have some redundant function. Required for neuromuscular function and organismal viability.
Sequence:
MITAEKHPLDNCQLFVQLKKIFHDNNEQAKCLKDMIYWSGNDEHIEKICDQVTDLLEEHDLIIQPPDTMDPFAMNQLRGLLVYLVLNTAHDYFLCKSQWSANVMHLCNQLPPIPLFLTIAIAVNCCLMEPLEEFLACGPRWLTIQYFEAFNEALSVINSDCVETLPLLSAALRAAGRAIVNCNLPAENKQLLRQIACMEHRHILDSKQRLHTLPRPSTRKIYLAKAMDHLIEVLLYTLNDPLKREKPNCFAVYSQITEDISDSNSSDPMPDLRHFAQILLDVLRRIFQLVSVDTYMYWHEMKSKSALYNCQELICRQTAELLKVLQSDNMLGEHPVCKQMQSFADAAKTLEQRVAEMRMGELLVFLDSGMATDEELLAGLDNLFSRFIAFGNDECVETMANHLIMLTKKHAQIILSFLGQVVESEMVVEDEGISVTEVNQGDDEDETSSNDDYEELLSLVLRPLFMQLNVEDKMEVLLLRDEQNVTQGFNFKAPDHRERRIRFFNQLDYNKRFPITKFLVLCFENARQTWIDFSHLGVTHTRFSKLFWHIAQSCPKHAAFHISACADNILVNEQLLQKPYALQFTLYLYGHRQILNGLYTSARQLCVSLKDGRCPYGEDELRQAQNRFLDACAYGLAKFIEPMNLPSLQLILKLLKQISLGESNLITRGTAELNALEKEHPKLENGDDAPAVKVAKHYTYLNASLPEWRLKHWKLISHVMKTIDALRWDLATFEDFRVDNLELAVWYWQDGLSHLTFLGTECRQRILNQVNSLKHKGFWLIYLKEDTLKDTRSFLKLLTQSSAQEANDLFKKLLKKRADCAVMGDLSDAVVKVNSESAFMAFRFLFREYLIAFRSHAKHNKTITKRQHWDHLMAVVAKAPFSIRNEIMKLASKAFAVRFGINIQEQQAAKC
The following text describes a protein:
Function:
Involved in pre-mRNA splicing. This protein is associated with snRNP U2. It binds stem loop IV of U2 snRNA (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MNQNTLYVNNLNDKINKNDLRTALYMLFSTYGTVVDIVALKTPKMRGQAHVVFFDPSAAAIAMKALKNFIFFGKEMKIQYAHSKSKIIERIVAENDSRGPLKRLRDEADLE
The following text describes a protein:
Function:
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MTERTREVEKLEERPLIEHLRELAYRLRRILIALAITFMIYFMLGLELVRVYLPYPFFGLKYVLAEVPVLYPSLFDSISVQLTQLFIYNELPKGVKLIIINLFDPLFASFYISLYLAIFTTIPIIVREIWAFVAPGLYEHEKKLFKSIIFPAFLLFALGSAFAYFLLIPLMLRIILLYATALGSAVEPTLGLRSFVSTVMTLLIATGLSFELPLIMGGLTGVGVVKSITWLKNWRWGVLVSFIIAWIISPGTTGGIIETVIGITLSTLYFIGALISKFMEKGRKKESQKTLERI
The following text describes a protein:
Function:
Part of the ABC transporter complex LpqY-SugA-SugB-SugC, which is highly specific for uptake of trehalose. Involved in the recycling of extracellular trehalose released from trehalose-containing molecules synthesized by M.tuberculosis. Trehalose uptake is essential for virulence. Probably responsible for the translocation of the substrate across the membrane.
Miscellaneous:
MISCELLANEOUS: Was identified as a high-confidence drug target.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MGARRATYWAVLDTLVVGYALLPVLWIFSLSLKPTSTVKDGKLIPSTVTFDNYRGIFRGDLFSSALINSIGIGLITTVIAVVLGAMAAYAVARLEFPGKRLLIGAALLITMFPSISLVTPLFNIERAIGLFDTWPGLILPYITFALPLAIYTLSAFFREIPWDLEKAAKMDGATPGQAFRKVIVPLAAPGLVTAAILVFIFAWNDLLLALSLTATKAAITAPVAIANFTGSSQFEEPTGSIAAGAIVITIPIIVFVLIFQRRIVAGLTSGAVKG
The following text describes a protein:
Function:
Involved in retrograde transport from early and late endosomes to late Golgi by linking the vesicle through the t-SNARE TGL1 to the Golgi, leading to the membrane fusion between late Golgi and endosomal vesicles. May also be involved in the actin cytoskeleton organization.
Miscellaneous:
MISCELLANEOUS: Present with 3130 molecules/cell in log phase SD medium.
Subcellular Localization:
Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein. Endosome membrane; Peripheral membrane protein. Cytoplasm, cytoskeleton.
Sequence:
MDVLKEVLSLDQDKFDQLKETSRDKTNETDDPFENYLKDCKFKAPSNKDQSPFAKLKSLQETHSNNEAAINIIIPQLIDYLTEFTNRLSNYTQDLDFIKKKSNELQSLLEYNSTKLAHISPMVNDLMIPPELIDDIIKGKINESWQDNITFIADKEEIYNKYRSNNLDQDNKDAENSAMLAPKDFDKLCQLLDILKNVILERSKRLIISKIKTLRSHNPVPSQRIQNKLLKVQKIFPFIRDNNLSLALELRQAYCYTMKWYYREYFSRYIRSLTILQFQQIDSQFALGNGLSTTSVSGFNNSPSLFFSNYLTTSASNAFYNKLPVTDEKIDKYFQIKKRLNILTQEDNTVMVSQIAENNTTKNYIEIGFKNLNLAILDNCTVEYHFLKDFFAMNGDNFEEINGLLEQIFQPTFDEATTYTQQLIQYNYDIFGVLISIRVANQLQFESERRGIPSMFDSFLNGQLIQLWPRFQQLVDFQCESLRKAAITTNVAKYAGNSSTSNSSPLTSPHELTVQFGKFLSSFLTLAITHKQSIDERSEPLYNSIIRLRNDFETVMTKCSKKTKSPERFLATNYMYLYNNLQQLHLHLNINDSDAQNYNFDSAENVGTKVANDDDNDSSVPLIIRETENHFKTLVEAFTRN
The following text describes a protein:
Function:
Protein-lysine N-methyltransferase. Monomethylates PRMT5, modulating its transcriptional activity. May also act as a histone methyltransferase. Plays a critical role in cardiac development. Acts as a key epigenetic regulator of gene expression during cardiac development via its dual activities as a methyltransferase and negative regulator of HDAC1.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MARIESWQDVLDSTCDRIRQGNGFSAFAALESNEDRVKFCLRNEVARPRLQHWLTVLCSSKHRKFWEKASELRSEGNLCFNRKQYAKAAELYTQSVLSAPFPDTPDAEGHSEEMSLGFANRSAAFFHAGKYKQALCDVRYAFELGYPVHLRYKLYLRKGQCYLRLGKPREALENFDLANKSLRRAALEGRKLAQQCKEIDTFKALCSQDCAPTPTSEEEDPDDESQVPDVAYGAHGTVPSCSMAVDMLYSTEKGRFLVANRDLQPGDAIFVERPYASVLLPGHTKTNCQHCHKRLLNAVPCAQCNQVRYCSFACAKDSWNSYHRWECGNLNLLYSVGIAHLAVRVLLVTGLSGLADFCRHLAEGKVDVDKNGGYGSVHELVTHSEKMHVEDLLQYSLTAALLSMLLDHVLFFNVDEASWKMSELSFGSRNGSSYRLASTDAAALKTVVGGLLLRHIQQLVCNAHAITSLESKTSQEDDVVMTTEQVRIATAIYPSASLMNHSCDPNIFSSFRCGSTLVVRAIRRIQEGEEVLNCYGPHHRRMSFAERQQLLQEQYFFVCSCTACSSGEDAEQRLQALKCEYCEGPLKQPDDSGKATCLDCGTTQECLGSEQKAFRMHDLYVQGVQLAEKGNHVEALQRLNKCLKTREKVMYKHNLKLLEVKDMVAKCLCSLGDFRSASGVLKPAVDAVRVIYGENSIELAYELQKLSDVLVSALPQAVKEEASSEEISKLVKDADAVIDEAMTIFILHYGTRHRTTRDQQVKRRMLASAL
The following text describes a protein:
Function:
Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP3 is essential for sperm binding and zona matrix formation.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix. Zona pellucida. Cell membrane; Single-pass type I membrane protein.
Domain:
The ZP domain is involved in the polymerization of the ZP proteins to form the zona pellucida.
Sequence:
MKAFLAHSASLVLLISFLRGVAIAIRTLKEGPMIDADGREYKTASLTEDSSPRASDSVRVECTEVSMIVYIQADFYRTGRLVSPGDLFLGGAEHKQDSRCRAVVSGHNEYVIEAGLQDCGSKLTITDDDVIYSNKLVFSPVSNHHTITRMTDAIVPVSCHYKRTHTVSSSNTEQAPMTFSQSAKFSTKNSAFSLKLMADDWLTEMLSSKFHLGDFLRFEAKYTGPEPRQLFVESCVATLTPDATSVPRYYFIENHGCFTDSKAGSVASFLPRSRANLLQFQIDAFLFRNDLRNTIYITCNLKATLQMRTTLTDKACNYVHSSWKSVDENDSVCWCCDSICYQSLPRDDDLCDIVTLGPLRIISNK
The following text describes a protein:
Function:
Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin-T1) complex, also called positive transcription elongation factor B (P-TEFb), which facilitates the transition from abortive to productive elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNA Pol II). Required to activate the protein kinase activity of CDK9: acts by mediating formation of liquid-liquid phase separation (LLPS) that enhances binding of P-TEFb to the CTD of RNA Pol II.
Subcellular Localization:
Nucleus.
Sequence:
MEGASAKRWYFSREQLEKSPSRRAGLDPDKELSYRQQAANLLQDMGQRLNVSQLTINTAIVYMHRFYMVQSFTQFHRNTVAPAALFLAAKVEEQPHKLEHVIKVAHACLHSQETLPDTRSEAYLQQAQDLVILESIILQTLGFEITIDHPHTHVVKCTQLVRASKDLAQTSYFMATNSLHLTTFSLQYTPPVVACVCIHLACKWSNWEIPVSTDGKHWWEYVDVTVTLELLDELTHEFLQILEKTPNRLKRIRNWRACQAAKKSKADEPGKDNGLSEQTILSMISRSSSDVAVAGLMSMSAASAAPAPPAGPEDCASDPLQGERWAPGHSSIKLEAAQGHRPGEGPALLGTEPGLAPDGVAAFLAQKPGGKGTPAAKVSLKEYRAKHAEELAAQKRQLENMEANVKSQYAYAAQNLLVQQQREREAQQDDHPPPADRAVLKARPPQAGGGDKALPSRPDEIKMRIKVHASADKHGPADEGGGKSREHKEKHKSHASNHHHHHHHHHHHHHNHQAHKHLHGQPGAGSKRPPDPKHGGQPASSAHKGYGPPGSVTAPAASSSASSSGRKRPLPEELAVAYEVPAKTSKSAPLTFPFPQLPSVPQLAAHSVDAGGLPFAPAACKGRAAHVKADKGPAGANGHSAPQPIDYQDTVNMLHSLLSAQGMQPSQPPAFDFLHSYGEYLAPRAGGIPARAADKPRPPPLPSEPPPPLPPLPK
The following text describes a protein:
Function:
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are held in an inactive form by a cognate anti-sigma factor until released, although no anti-sigma factor is known for this protein (By similarity).
Domain:
The sigma-70 factor domain-2 mediates sequence-specific interaction with the -10 element in promoter DNA, and plays an important role in melting the double-stranded DNA and the formation of the transcription bubble. The sigma-70 factor domain-2 mediates interaction with the RNA polymerase subunits RpoB and RpoC (By similarity); The sigma-70 factor domain-4 contains a helix-turn-helix (H-T-H) motif that mediates interaction with the -35 element in promoter DNA. The domain also mediates interaction with the RNA polymerase subunit RpoA (By similarity).
Sequence:
MSQHDPVSAAWRAHRAYLVDLAFRMVGDIGVAEDMVQEAFSRLLRAPVGDIDDERGWLIVVTSRLCLDHIKSASTRRERPQDIAAWHDGDASVSSVDPADRVTLDDEVRLALLIMLERLGPAERVVFVLHEIFGLPYQQIATTIGSQASTCRQLAHRARRKINESRIAASVEPAQHRVVTRAFIEACSNGDLDTLLEVLDPGVAGEIDARKGVVVVGADRVGPTILRHWSHPATVLVAQPVCGQPAVLAFVNRALAGVLALSIEAGKITKIHVLVQPSTLDPLRAELGGG
The following text describes a protein:
Function:
Required for the methylation of the wobble bases at position 34 in tRNA. Appears to have a role in stress-response (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MEIEYENEYVHQVYDKIATHFSDTRYKPWPVVEKFLKSLPLGSVGVDIGCGNGKYQKVNPNVYMIGSDRCVKLVKIASNLGPMVISDGLHVPHPSNRFDFALSIAVIHHFSNENRRLQAVQEVLRPLVKGGKALFFVWALEQKNSRRGFSEDGPQDVYVPWILKRQYEYPNAKPEELKGHDPAENIAYQRYYHLFRKGELNELVETAGGSILEHGYDRDNWWVIAEKN
The following text describes a protein:
Function:
Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite.
Subcellular Localization:
Periplasm.
Sequence:
MSISRREFLKANAAVAAATAVGVTLPVKMVEAAESDNIKWDKAPCRFCGVGCSVLVGTKAGKVVATKGDPESPVNRGLNCIKGYFLSKIMYGKDRLTTPLLRMKDGKYHKEGEFTPVSWDVAFDTMAAKWKHSIATKGPTSVGMFGSGQWTIWEGYAASKLHKAGFLTNNIDPNARHCMASAVVGFMRTFGIDEPMGCYDDLEAADHFVLWGANMAEMHPILWARLSDRRLSSKDCRVHVLSTFENRSFDLADNPMVFHPQSDLVILNYIANYIIQNKAVNTDFVTKHTKFALGVDDIGYGLRPDHPLEKKAKNPGNGKSTPISFDEYAKFVSTYTLEYAAKMSGVEPEKLETLAKAYADPKAKVMSLWTMGINQHVRGVWANNMLYNIHLLTGKIATPGNSPFSLTGQPSACGTAREVGTFAHRLPADMVVDNDKHRAITEKMWQVPEGTIPPKPGYHAVLQSRMLKDGKLNCYWTMCTNNMQAGPNINEEMYPGFRNPENFIVVSDPYPTVTAMAADLILPTAMWVEKEGAYGNAERRTHMWHQQVKAPEGAKSDLWQLVEFSKRFKVAEVWPAELIAKKPEYADKTLYEVLFANGVINKFPTTDCKGDLNDESEHFSFYVQKGIFEEYAAFGRGHGHDLAEFDRYHETRGLRWPVVNDKETLRRFVEGSDPYVKAGEGYNFYGKPDGKAVIFALPYEPAAEEPNSEYDLWMSTGRVLEHWHTGSMTARVPELYRAYPDAQIFMHPEDAKARGLQRGDEVLVASPRGEIKTRVETKGRNKPPRGVVFMPFFDARQLVNKLILDATDPLSKETDFKKCPVKVMKA
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome.
Subcellular Localization:
Cytoplasm.
Domain:
The N-terminus is composed of the phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. The PTB domain, which is also called TKB (tyrosine kinase binding) domain, is composed of three different subdomains: a four-helix bundle (4H), a calcium-binding EF hand and a divergent SH2 domain.
Sequence:
MATRGSGTRVQSQPKIFPSLLSKLHGAISEACVSQRLSTDKKTLEKTWKLMDKVVKLCQQPKMNLKNSPPFILDILPDTYQRLRLIYSKNEDQMHLLHANEHFNVFINNLMRKCKQAIKLFKEGKEKMFDENSHYRRNLTKLSLVFSHMLSELKAIFPNGVFAGDQFRITKADAADFWKSNFGNSTLVPWKIFRQELNKVHPIISGLEAMALKTTIDLTCNDFISNFEFDVFTRLFQPWVTLLRNWQILAVTHPGYVAFLTYDEVKARLQRYILKAGSYVFRLSCTRLGQWAIGYVTAEGEILQTIPQNKSLCQALLDGHREGFYLYPDGQAYNPDLSSAVQSPTEDHITVTQEQYELYCEMGSTFQLCKICAENDKDIRIEPCGHLLCTPCLTSWQVDSEGQGCPFCRAEIKGTEQIVVDAFDPRKQHNRNVTNGRQQQQEEDDTEV
The following text describes a protein:
Function:
Involved in the regulation of the intracellular balance between NAD(H) and NADP(H), and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Subcellular Localization:
Cytoplasm.
Sequence:
MRAAVVYKTDGHVKRIEEALKRLEVEVELFNQPSEELENFDFIVSVGGDGTILRILQKLKRCPPIFGINTGRVGLLTHASPENFEVELKKAVEKFEVERFPRVSCSAMPDVLALNEIAVLSRKPAKMIDVALRVDGVEVDRIRCDGFIVATQIGSTGYAFSAGGPVVEPYLECFILIPIAPFRFGWKPYVVSMERKIEVIAEKAIVVADGQKSVDFDGEITIEKSEFPAVFFKNEKRFRNLFGKVRSIG
The following text describes a protein:
Function:
Component of the SMC5-SMC6 complex, that promotes sister chromatid alignment after DNA damage and facilitates double-stranded DNA breaks (DSBs) repair via homologous recombination between sister chromatids.
Subcellular Localization:
Nucleus.
Sequence:
MARGGDAGPSSQQVQQTQADRRKLREDYRKLKDRAAAQKDELLQPESHKLQEALLEADALHQQVRKPREQKADADLLAQLTEVTLQAAKQLRPDASLCTPTAFLGRLMTHFTGGMDMEEEEEVSPERFDWQNAGRMIGMPLLASAPGITCMLGPLDSQPKQRKQPQQRAKRKRPEEQTNPDEIVEQTQDGKEKETDANMTTMFEILRRNHGGIPFERLFLNKKSFSQTIENQFSLSFLIKDGRASTRKMDDGTILVEPRNAPSKEELGTGKAETSAFMAKFQYKDWLDLKEKCPGSDYMPTRKGANEPAQPPRNGTPVRKGQGKFRPRENSYSQQPVEEESEEEEEEALVVNRRRKKQRS