lhallee/plat_data huggingface dataset:
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. Second largest core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol III is composed of mobile elements and RPC2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft.
Subcellular Localization:
Nucleus.
Sequence:
MHGRDDMRYEGKKLTDPINTAEDKWRLLPAFLQTKGLVKQHLDSFNYFLETDIKLIVQANAKVDSDIDPHFFLRFLDIRIKPPQAEDIQKGVVYELTPQECRLRDITYAGTICVDIEYVRGKQVIVKRNIEIGRMPIMLKSSYCVLTNKSPDEIADLGECPLDPGGYFIIRGTEKVILIQEQLSRNRIIVETDRFGCICSNVTSSTLEKKSKTIVACGKTGKMVLKHNSLTAEVPVTVIMKAMGVESDREIAELICGDDLKYLALFSPSLEEGASLKISTQRQALEYIGAKVKVTFKTNRVGIRRDWVEEARDLLATTVLAHVPVEADDAGVLNFRPKAIYIALMIRRVLQAVKEGGIVDDRDFIGNKRLELAGQLMSLLFEDLFKSWISAIKRAVDIQLKRTNRTSQYDAAAAVSQTSRFITDGMFRAISSGNWSVKRFKMERAGVTQVLSRLSYVSALGMLTRISSQFEKTRKVAGPRSLQTSQWGMICLSGDTEQGEACGLIKNLALMTYITTDSNDVSLRKLAFVLGTEDINLVSGSDLYATSETFLVFLNGVIMGVHRNAEQFVSDLRRLRRAGRTSAFVSIYRTVSQRTINISSDGGRVCRPLIIVERGIPKVTEEDIRGIIHGILRFDDLIAQGKIEYLDTNEETDSDIAVKINSVLIDQPNTTHLEIAPFTILGAVAGLIPYPHHNQSPRNTYQCAMGKQAIGTIAYNQLTRIDTLLYLMVYPHHPMVRTRTIEMIGFDKLPAGQNATVAVMSYSGYDIEDALVLNKASVDRGYGRCQVMRKSSTMIKSYPNQTFDRLADPVLDPLTGQVQERYNILDNDGICGVGERVYPNQIVINKQTPTETSPRVSAPTNGGGSDDESSAPMLGRAVDPSSIPFKNTPMSFKYPGDAVIDQVLLTTNEEDQTLIKVLIRQTRRPELGDKFSSRHGQKGVCGIIVSQEDMPFSENGVVPDVIMNPHGFPSRMTVGKMIELLAGKAGLFAGQVQYGTAFGGSKVEDMSRILVENGYSYSGKDMLTSGITGEPLQAYIFFGPVYYQKLKHMVMDKMHARSRGPRATLTRQPTEGRSRDGGLRVGEMERDCLIGHGASSLLIERLLYSSDAYDVEVCSRCGIIGAWHGYCPFCKMRSGVVTVKMPYACKLLFQELMSMNVVPRVQVDDLK
The following text describes a protein:
Function:
Plays essential roles in regulation of cellular metabolism by catalyzing the synthesis of a second messenger, cAMP.
Sequence:
MLFTMQFTTRSTVASPEQQHQHQQRSISYSDIELGLERISSRDSNGSSNFTHRAYPPPLSQQYDDTSTNSFHSSQPDITASSSTLSSRLVSANYSRPRFEHAHTQPPTPDQDRSSSGSGSGSGSRSYFPANSHSDSLPGPSTHSISPSFDEDELRQIMSHIPANQATSSSDGDVGKAVQSANHQDISPFLFQSENAAPFSSSHSNRTSVNPSAASTASPSTSAATRTRPRGGTNASQYNTLDTSFGSIDRPGLSSSRSQYSLRPQTPPSASTSTSTLNGSKDTHASAVKKTRNPFGFLKKKSSAHSNASSNHPTRHDIGSVSSLSSRYGPNAAANVNPMRPPAWLDNHCTLANSNSPSSASLRSHYHQPPASSNPPPWQNPLVSRADSTPSAMSLEDEVEAEHHLKKDPRKRIKGVRHHLAKTTKPGEDADSARDPAFAAQSQSIEQEVELSLDMNFDQLDDFVDTNAARQRLQGSITESASPSEHRSPNGSEAGVYRSPSPSQTPIAERQTSVTSTVESPSHASEASLAPSGSLRTPSRTTASTSTSSASTVLSDRLPSQVNMLPRNSVPRLSLAEMQNYQSLRKLSNNLIDMSQTQNPSAMGASYRRGSIAAAQAPVDAPQLGVAPRTDSELSDRKDSVVSTHSMRSNHSGISPKTSYANLPSVIQERQKPATALPSAANWTSSITRDKTANGHADHAYQFPPATEYQSNLLLSVRKSSASSGQEPSSSWMAPDSWAVQPDKMRDYLRDDNVGEEEDDDDDQHQARAALATDGKRRGSSSGISSTHASSMFRTSSTDPFKKTASLAGSRRGTDDSVDPLTALPPLPGSKSVDEAAANKVDVLQQTNNLAQSALVQQQSQSQNHHQPSPNVRPTSRGGAGAHMFASAGASAAAAAAGKLGLHRPSKHRMNARPNTAGSVGATRPSTTTLGSTLSAEDDTSINGSIRRDGHPLKRSATANTNNATGTLPRNHFIRVYKTDGTFATLSCSLVSTANEVQTILARKSLTTESAAYRLFVRDKGSERPLGISDKPSQLQRRRLIQAGYTENDGLEDMGRDDLSYLLRFVFRPDSVPTFDSESIGHSEHTFQHLDLHSRNLEMVPIFLYKHADWIVSLDLSGNPMSDLPLDFVQLCSSLRTLRLSNLALKRIPQSVRHSETLTHLDVSNNRIVELAHVSLDLIPELMSLKVQNNRLFDLPSYFSSISTLRNLNISNNRFEEFPKVICDVPSLVDLDVSFNSITELPAEIANLINLERFILAGNELEKLPDSMSELVSLRTIDLRRNKVQDVSSLLGLPRLQNIQAESNNIKSFEATLGPQLTQVELGRNPLSKVRIAALTTCDLTSLDLSSTNMTRLEEGLFPQLPALVKLTLDGNQLVVLPDTLGDLKRLEMLSCSNNLLATLPESIGDLKALKELLVHNNNLKTLPQTLWLCESLAHINLSSNLLESFPAVPDIRTDASVGDAAAAAGTSAVIAARKGSTSSSLTHRSNTGGANGNINLSTPSEVFVAPLSLSLQKLRLGDNRLGDDVFSVLSELTSLEVLNLSFNEIFEIPDFSLQTLTKLRELYISGNQLSTIPSDDLVVLQELRILHLNCNKLTTLPTELGKLKKLANLDVGNNVLKYNIANWHYDWNWNMNPELRYLNLSGNTRLEIKTKLSDMGFTRKSNISDFSRLTSLRMLGLMDVTMPLHSNATPDESDNRRVRTSLSQVNGMAYGIADALGKHDNLSVIDLVIPTFRKDEGECIFGLFDGRGHGAHVGSRIAHHLAEWSGHRLSWEFQKHQNEMTAEPVSVPDALRRAFLRLQKDYADALINDGSRKLSEAHAEAAADVTRSSAPAIAAASNKHDWRAGASAILAYVVDHTLYIANAGDALAVMSRNGGTAHLISNKHEPFDRAEIERIRSAEGWVSLRGYVNDMLDVSRSFGYFHLFPIVNAAPAVTTVQLTDSDEFVIIANRTLWQYVSYQTAVDIARTQRNDPMIAAQKLRDFAISYGAEESIMVMVISVGDLFYRSDQRNGGGLNFASYKNSDAIQKAGRRFREELPGDRTLARLDREVAPPIGQVALVFTDIKNSTSLWETNNGMQTAMRLHNYLLRRQLRTIGGYEVKTEGDAFMVSFPSVSAALLWCFTVQQQLLQEDWPREILDSEDGKEVYDQSGELIHRGLSVRMGIHWGRPVCEADPITRRMDYFGPMVNRAARISGAADGGQILASKDVIKELQGLLGTFDESSTAGGAGGEGENLEKTEEELDEDAFRLLNPNVSRDVVLLRRMGFGLSQLGERRLKGLETPEMLWLVYPKQLAGRLEQAKTDDAPDAPTAQVYEPTVQLLDIEDVKQVGMLCLRLEYLSNSTVCPGIFAAKDEADRSQPSTPLDDNGRNPIDGHGTAVPLLSHQARRKGVEAMLTMHPELLIYSIRDDATDEELAGILDQLTTRIQNAVSSLMLNMLRDKTANGTKELGVDPGVLELLMGLLSQPPPRASTSALSLPSPRTSPRNRLLELVP
The following text describes a protein:
Function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MLGQSIRRFTTSVVRRSRYEEGPGKNIPFSVENKWRLLAMMTLFFGSGFAAPFFIVRH
The following text describes a protein:
Function:
Required for the activity of the bacterial periplasmic transport system of putrescine and spermidine.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Sequence:
MMSKKLNLQNAIVTLIVGWLVLFVLIPNLMIIGTSFLTRDEANLIKFAFTFENYTRLLDPLYGKVMLHSFYMAIVATLICLVIGYPFAYIVAKMPEKWRPFMLFLIIVPFWTNSLIRTYGLKIVLGTQGILNQALMSLGLIDAPLRIMFTETAVMIGLVYILLPFMILPLYSAIEKLDGTYIEAARDLGANKFQTLVRVILPLTMPGIIGGCLLVLLPALGMFYIADLLGGAKNLLIGNVIKSQVLNARDWPFGAATSIALTLAMAIMLYAYYRAGKLLNKKVELD
The following text describes a protein:
Function:
Participates in ABA-regulated gene expression during seed development and subsequent vegetative stage by acting as the major mediator of ABA repression of growth. Binds to the embryo specification element and the ABA-responsive element (ABRE) of the Dc3 gene promoter and to the ABRE of the Em1 and Em6 genes promoters. Can also trans-activate its own promoter, suggesting that it is autoregulated. Plays a role in sugar-mediated senescence.
Subcellular Localization:
Nucleus.
Sequence:
MVTRETKLTSEREVESSMAQARHNGGGGGENHPFTSLGRQSSIYSLTLDEFQHALCENGKNFGSMNMDEFLVSIWNAEENNNNQQQAAAAAGSHSVPANHNGFNNNNNNGGEGGVGVFSGGSRGNEDANNKRGIANESSLPRQGSLTLPAPLCRKTVDEVWSEIHRGGGSGNGGDSNGRSSSSNGQNNAQNGGETAARQPTFGEMTLEDFLVKAGVVREHPTNPKPNPNPNQNQNPSSVIPAAAQQQLYGVFQGTGDPSFPGQAMGVGDPSGYAKRTGGGGYQQAPPVQAGVCYGGGVGFGAGGQQMGMVGPLSPVSSDGLGHGQVDNIGGQYGVDMGGLRGRKRVVDGPVEKVVERRQRRMIKNRESAARSRARKQAYTVELEAELNQLKEENAQLKHALAELERKRKQQYFESLKSRAQPKLPKSNGRLRTLMRNPSCPL
The following text describes a protein:
Function:
Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (By similarity). The SRP complex interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the ER (By similarity). The SRP complex targets the ribosome-nascent chain complex to the SRP receptor (SR), which is anchored in the ER, where SR compaction and GTPase rearrangement drive cotranslational protein translocation into the ER (By similarity). Binds the signal recognition particle RNA (7SL RNA) in presence of srp68 (By similarity). Can bind 7SL RNA with low affinity (By similarity). The SRP complex possibly participates in the elongation arrest function (By similarity).
Subcellular Localization:
Cytoplasm. Endoplasmic reticulum membrane. Nucleus, nucleolus.
Sequence:
MSNHEEEIEELAQRIGKIEVGDTKSDIYQKVLNLIDIERYEHALKIIEKYLGETDAVYERAYCAFQLGKEDFSLEDKQFLQHLQAQKAYRLSDFSKALKIYEHLENDLPEQRADIRVNMLAAASQLPGLQLNNAVSLDDQDSVFNLATRYLTIGDWNQAIELLSSSLEKLENSDSNSEDHKSQINLCRLQLFFAYLQAGDNEKASKESLKISKDCLDETSQAIFVNNLISMSIDNPYISFRDLHGTNLEKALSSLLASQKKQFIRNLALLDMAVGKQRSVRKEKKRNPEESIYFSTILLREETKSLISPKKLPGYLENLFKSDSDNIVVALLLMQHKISNGNFRGALSIYQKLRTSLEASQSLSVLYSPGLVGLGDALHYKIQSTGFKSQLLHEAANYWRKQQSCEAKLLLCTRSLLAHLDERAPVSTIQDDMSVIDDLLQWKGPISELVSCKVAALCYLDKEIESGMDKYLVPTKDLITGIDVDDIEIRGVPVSAAIGPIKRSVEANSSNSSKKTRKRRKPTPKSFNPKATPDPQRWIPKRDRTNVKIKSKGKSMQGGVA
The following text describes a protein:
Function:
Sequence-specific transcriptional activator. Recognizes the DNA sequence 5'-C[CA]GGAAGT-3' (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MDGTIKEALSVVSDDQSLFDSAYGAAAHLPKADMTASGSPDYGQPHKINPLPPQQEWMNQPVRVNVKREYDHMNGSRESPVDCSVSKCGKLVGGGESNTMSYTSYVDEKNGPPPPNMTTNERRVIVPADPTLWTQEHVRQWLEWAIKEYGLMEIDTSFFQNMDGKELCKLNKEDFLRATSLYNTEVLLSHLTYLRESSLLPYNTTSHTDPSSRLNVKEDPSYDSVRRGGWGSNMNSGLNKSPPLAGAQTMSKNTEQRPQPDPYQILGPTSSRLANPGSGQIQLWQFLLELLSDSANASCITWEGTNGEFKMTDPDEVARRWGERKSKPNMNYDKLSRALRYYYDKNIMTKVHGKRYAYKFDFHGIAQALQPHPTESSMYKYPSDISYVPSYHTHQQKVNFVPPHPSSMPVTSSSFFGAASQYWTSPTGGIYPNPNVPRHPNTHVPSHLGSYY
The following text describes a protein:
Function:
Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs).
Subcellular Localization:
Nucleus.
Sequence:
MASSEVTMKGNCLNHNDGGATEPHSPSTAKDAEAALFRELWHACAGPLVTVPREKERVFYFPQGHIEQVEASTNQVADQHMPVYDLPPKILCRVINVQLKAEPDTDEVFAQVTLLPEPNQDENAVEKEPPPPPPPRFHVHSFCKTLTASDTSTHGGFSVLRRHADECLPPLDMSKQPPTQELVAKDLHANEWRFKHIFRGQPRRHLLQSGWSVFVSSKRLVAGDAFIFLRGENGELRVGVRRAMRQQGNVPSSVISSHSMHLGVLATAWHAILTGTIFTVYYKPRTSPAEFIVPYDQYMESLKNSYSIGMRFKMRFEGEEAPEQRFTGTVVGIEDSDPKRWRDSKWRCLKVRWDETSNTPRPERVSPWKIEPALAPPALNPLSMPRPKRPRSNAVPSSPDSSVLTREASSKVSIDPSPANGFPRVLQGQEFSTLRGNFTESNEFDTAEKSVVWPPTAVDDEKMDVSTSRKYGSESWMSMGRNEPTYSDLLSGFGTSGDPSHSSLKDQMSPAYSARKQSLDHEGKLHMPHPWPVMPSSLSLNILDSNAKGPTHGGDTSFQARGNLRFSAFGEYPALHGHKVEDSHGNLMPPPPAPQTQYQSPCSRELMSKHVSAKTCEAVKPKDGDCKLFGFSLISGPIVPEPSLSQRNVSEPAGQMHLTAHQQRTSENDEKSDHSKGSRPVDDLVVDDHDRPLQTSQSHTKDVQAKPLSGSARSCTKVHKKGIALGRSVDLTKYSGYDELVAELDQLFEFGGELLSTKKDWLIVYTDNEGDMMLVGDDPWQEFCAMVCKIYIYPKEEIQKMSPGTLSSKNEENQSVMASDGADAKVVKCQPHQKFNSENGLDA
The following text describes a protein:
Function:
Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Does not deaminate acetylated N-terminal glutamine. With the exception of proline, all tested second-position residues on substrate peptides do not greatly influence the activity. In contrast, a proline at position 2, virtually abolishes deamidation of N-terminal glutamine.
Sequence:
MEGAVPTAAAAHYQPASPPRDACVYNSCYCEENIWKLCEYIKNHDQYPLEECYAVFISNERKMIPIWKQQARPGDGPVIWDYHVVLLHVSSGGQSFIYDLDTVLPFPCPFDIYVEDAFKSDEDIHPQFRSFGFQLIISRGFFDRKFRVIRADSYLKNFASDRSHMKDSSGNWREPPPSYPCIETGDSKMNLNDFISMDPEVGWGAVYSLSEFVHRFGSQNY
The following text describes a protein:
Function:
Involved in the conversion of UDP-GalP into UDP-GalF through a 2-keto intermediate.
Sequence:
MNVILSVMLFSSPSCVNINSFDILIVGAGISGIVLANILANHNKRVLIVEKRDHIGGNCYDKVDSKTQLLFHQYGPHIFHTNNQTVINFISPFFELNNYHHRVGLKLKNNLDLTLPFDFQQIYKLMGKDGRKLVSFFKENFSLNTHLSLAELQLIDNPLAQKLYQFLISNVYKPYSVKMWGLPFAMINENVINRVKIVLSEQSSYFPDAIIQGLPKSGYTNSFLKMLANPLIDVQLNCKDNLLVYQDEKLFFNNNLIEKPVVYCGLIDKLFNFCFGHLQYRSLAFSWKRFNQKKYQTYPVVNMPLAKSITRSVEYKQLTNQGSFKPQTIVSFETPGSYAINDPRFNEPYYPINNTLNDTLFKKYWKKASKLKNLHLLGRLATYQYIDMDKAILLSIKKAQQLLS
The following text describes a protein:
Function:
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
Subcellular Localization:
Mitochondrion.
Sequence:
MAWRQILKRSANARVVASKSLKYAPSSITTSAESSCSCLQGLRYHDVSMKVSLIRCFHASPELLARRRDEDSFGLKTARRESNKGKFRKREIGKPPVEAAYVPPKPKKTVKSSQDKTVDIFEGMAVVELAKQSGASITTLQDILVNVGEKVDSEFEPLSIDVAELVVMELGFNVRRIHSSEGTEILPRPPVVTVMGHVDHGKTSLLDALRQTSLVAKEAGGITQHMGAFVVGMSTGASITFLDTPGHAAFSAMRKRGAAVTDIVVLVVAADDGVMPQTLEAIAHANAANVPIVVAINKCDKPAADPERVKNQLGAEGLELEDWGGKVQVVEVSAVKKTGLDDLEVALLLQAEMMNLKARVDGPAQAYVVEARLDKGRGPLTTAIVKAGTLVCGQHVVVGHEWGRIRAIRDMVGKSTDKARPAMPVEIEGLKGLPMAGDDIIVVDSEERARMLSSGRKKKFEKDRVRKINEERTENLEPSEDVPKRAEMPVIVKADVQGTVQAVTDALKTLNSPQLFVNVVHVGVGSVTQSDVDLAQACGACIVGFNVKSPPTSVSQAATQAGIKILMHSIIYHLLDDFGNLVVDKAPGTFETQVAGEAEVLNIFELKGRSKAKGDDVKIAGCRVIDGCFTRSSTMRLLRSGEVVFEGSCISLKREKQDVDTVAKGNECGLVIRDWHDFQVGDIIQCLEQVLVKPKFISSESGTVRIEC
The following text describes a protein:
Function:
Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity.
Sequence:
MPLTGLQRSMLNEFMQITGVSERTGTRLLKGTSWRLEPACDSFFQANNNAVPSAQAKEKETLTKLFESYRTFSDDVNMVGVDGTMKYFGDDLGVNLEGVEFLIPCEIIQVPSIGEMSKEGFVEGWKKLGLDTIPKQKSHISKAVASLATDSELFKRVYKHTFVCAREKGQKALSLELASVYWELLFNAPGRQWKTASTNWIALWLEFLGQNWKKSVNKDLWNQTYQFHAKTMEDESLSFWNEDGAWPSVIDEFVAWVKKNRGDPEAGETMETD
The following text describes a protein:
Function:
Core component of the complement C1 complex, a multiprotein complex that initiates the classical pathway of the complement system, a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system. The classical complement pathway is initiated by the C1Q subcomplex of the C1 complex, which specifically binds IgG or IgM immunoglobulins complexed with antigens, forming antigen-antibody complexes on the surface of pathogens: C1QA, together with C1QB and C1QC, specifically recognizes and binds the Fc regions of IgG or IgM via its C1q domain. Immunoglobulin-binding activates the proenzyme C1R, which cleaves C1S, initiating the proteolytic cascade of the complement system. The C1Q subcomplex is activated by a hexamer of IgG complexed with antigens, while it is activated by a pentameric IgM. The C1Q subcomplex also recognizes and binds phosphatidylserine exposed on the surface of cells undergoing programmed cell death, possibly promoting activation of the complement system.
Subcellular Localization:
Secreted. Cell surface. Note=Specifically binds IgG or IgM immunoglobulins complexed with antigens, forming antigen-antibody complexes on the surface of pathogens.
Domain:
The C1q domain is the ligand-recognition domain, which specifically recognizes and binds the Fc regions of IgG or IgM immunoglobulins; The collagen-like domain interacts with C1R and C1S proenzymes.
Sequence:
MMMKIPWGSIPVLMLLLLLGLIDISQAQLSCTGPPAIPGIPGIPGTPGPDGQPGTPGIKGEKGLPGLAGDHGEFGEKGDPGIPGNPGKVGPKGPMGPKGGPGAPGAPGPKGESGDYKATQKIAFSATRTINVPLRRDQTIRFDHVITNMNNNYEPRSGKFTCKVPGLYYFTYHASSRGNLCVNLMRGRERAQKVVTFCDYAYNTFQVTTGGMVLKLEQGENVFLQATDKNSLLGMEGANSIFSGFLLFPDMEA
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MFTAPGVAATRERPYSCSVCGKSFQYSAVLLRHERAHGGDKRFRCLECGERCARASDLRVHRWTHAGQTLYICSECGQSFSHSSLLDLHLGTHRRRSSTCPCRLCGRRFPHVSALLLHRVRQHPPEKPHRCPLCARSFRQSALPFHLARAHPPETTIATAPAPSTLYHCTQCPRAFHSSAGLRNHSRIHVVPSLSDPGAEAHRCGVCGKSFSKSSTLTRHLQRHSGEKPFKCPECGKGFLESATLVRHQRTHTGEKPYACNDCGRCFSESSTLLRHQRSHQGERPHICATCGKGFGQRYDLVVHQRSHTGERPFPCPECGRGFTDRSDLTKHLRTHTGEKPYHCELCGKRFTCISNLNVHLRNHAGHKPHKCPECGKSFSVASKLALHRKTHLGERTAECTECGKFFSHGRSLSQHQRSHRRARAAAMAATTTTTVVTEMTIGPSLTLTGPTEQEKSGLLVSTFQETC
The following text describes a protein:
Function:
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Endomembrane system; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MTLRDTLEPFFNKLPAVASPEKHVHFKDKLWWTLGVLVLYFALANVPLFGMSQDSIDLFESYRAFFAGASGSLVLLGIGPIVTASIVLQLLVGADIIKMDLSDPKDQAFFQGAQKFLVFVMIILEALPQLLGGYIQPDPGLAATLNVGLGVITLLLLVQIFIGGTLILFMDEVVSKWGIGSGVGLFIVAGISQQIVTGIFNWEFEEGLPVGLIPKWIYIAQNTGADYLFSGEGLMFLLVRGGILALLSTVAIFLLVVYVESTRIEIPLAHSAVRGARGRFPVKLIYASVLPMILVRALQANIQMVGIILASRGITFLGEFSGSKPLNGIMYYLAPIHSPYDWIPSLVRESFASYGATAPAIWQIGLHVLADAIMLIGGGIIFALFWIETTGMGAKPTAQKIFNSGMQIPGFRRNIGSIEKVMQRYIPKVTVIGGAFIGILTLVASLLGTLGSAGGTGLLLTVSIVYRLYEDIASEQMMEMHPMIRSFFGEQ
The following text describes a protein:
Function:
Part of the SNAPc complex required for the transcription of both RNA polymerase II and III small-nuclear RNA genes. Binds to the proximal sequence element (PSE), a non-TATA-box basal promoter element common to these 2 types of genes. Recruits TBP and BRF2 to the U6 snRNA TATA box.
Subcellular Localization:
Nucleus.
Sequence:
MDRVHEADRRSWIGEKMKVRDFKQQWTDTFGSCESDPEENGLRYKIVELMNVPESVVKALEEECGPKSLFQERLHSLSSVQVLDLEDIPDNVDLVTVRLQKQDLDKRASDAAYRSRSIRIFKMMGSTSKVNFSKSKPAGRISKGGSPNDQAPVPEVALVVQIFRPIKLPNKLRRVTISTFIKNKIQGEVVVLGSQSLTTLRNTISCVADINAPGDYSEDPDKPQCPKAIDLYKSGFFFIGNTFYNDMTDPSCRDYSQVIREWAKNPRRNVGPFEVKRMEDTCFNDLEIQLGYPYVYVHQGYCEHLIVFSDMRMLHSDDSQQMSDYPMILQNHAHSKRLLCWLCHKAPAK
The following text describes a protein:
Function:
Probable receptor for neuropeptide ligand nlp-8 that plays a role in octopamine signaling and specifically, the octopamine inhibition of aversion responses in olfactory sensory neurons. Plays a crucial role in daf-7 expression. Acts in concert with gpa-4 to activate TGF-beta-like daf-7 secretion in the ASI neuron, thereby promoting larval development and inhibition of dauer diapause. Suppresses immune response against pathogenic infection by inhibiting transcription regulators elt-2 and hlh-30 in ASJ neuron. Promotes pathogen avoidance behavior via intestinal gon-2, independent of aerotaxis.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSVAVGIPYVCFFIILSVVGIIGNVIVIYAIAGDRNMRKSVMNILLLNLAVADLANLIFTIPEWIPPVFFGSTDWLFPSFLCPVCRYLECVFLFASISTQMIVCIERYIAIVLPMQARQLCSRRNVLITVLVDWIFVACFASPYAVWHSVKTKDRNTNSLRFKLFQLSATCSNTVGKSTWWQGYKLTEFLAFYFVPCFIITVVYTKVAKCLWCKDPTLQCETRSCLDNKSSSRSSDALRTRRNVVKMLIACVAVYFVCYSPIQVIFLSKAVLNVTIHPPYDFILLMNALAMTCSASNPLLYTLFSQKFRRRLRDVLYCPSDVENETKTYYSINNTSIVGPRASFN
The following text describes a protein:
Function:
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Subcellular Localization:
Cytoplasm.
Sequence:
MKYKFRNVVLGGTFDTLHSGHVKLLATATLIGDRILIGLTSDSFASTYKQYKVRPFSVRLANLRNLMSLIAPEREVAYVEIHDPYGPAVFDPRLEAIVASIETAPRALQINDERAKRGLRPMEVFIISTVRDGYGHTLSSTYIRRVLERPESKQS
The following text describes a protein:
Function:
Specific and highly efficient GDP-D-glucose phosphorylase regulating the levels of GDP-D-glucose in cells.
Subcellular Localization:
Cytoplasm.
Sequence:
MKDPMEKTMGKIEMKISCLDNPILESSKRPRPVDKMPMRKIVMLGANARTQRSVSSIQLPAEFSPSASSAPYFNYSPSDFILDLRTHKESEENYQNGHTETDDGKKQLKDLLHERWENSKQFNAFNYSLNCMYRCMDGKYDLSMQLNIERGELRRKPMHFKNIKEPFNHLRFNFTKLHDNEILFYLKCDADPISNDPLDRHLVAVNASPLERDHSLIVPSVNKCNPQVLTLQAVRIAVDLMLLVDDDMFHILFNSLLGQASVNHLHLHAVYWPYDSDLINRKCEPLHDVPNVFVIRPPIWICPAIVFQLDCMENYEQFKTNIYKCVEHLTETNQAHNLFLARAQPIRTTGAEKEEDRRGERPQLVTCYVFPRMNMIGAKPPSNFNPAANELAGNLTSYTIRFFESATEQSVIRIIEEEASLDDDSFRSLCFDLSDVLIGRSVGTSRPHDLDILEGLTSPEIDELRDSFQSFMPRSPSIRHRSSTRTHSDEGPIV
The following text describes a protein:
Function:
Catalyzes the ATP or GTP-dependent addition of one L-glutamate molecule to tetrahydromethanopterin, producing tetrahydrosarcinapterin.
Sequence:
MKLGIITIERDAVVNDLIKSCEKYEVDYKVITPSNIVAGFNLDFKLKYYKSFLDELDCCFVRNLGWDSFFRFDVLKYLNHYIPVINPPDGIDRASNKFLTSVFLELNNLPQPKTVVTESINEAIVWIDKFEEAVLKPIFGCGGEGIVRVKKELPISTKLKILNEFKEKYNTFYIQEFIKPVRNEHRDIRAFVVDDEVVAAMYRIGGENWKNNVSQGGRVEKCEITEEIEKLALKAKNALGLFYAGVDLIESEDGLKVLEVNSTPSWIGLSKVSEVNIADKLLEKIIQYVKS
The following text describes a protein:
Function:
Irreversibly catalyzes the reduction of fumarate to succinate.
Sequence:
MNRRQIRLIFYLAVLSPIAAVVYHHLLPSIPDSFITDLVNRLFPSETSAMTSQASRPGVIIVGGGLAGLSAAYSALCAGAPSVRLLERAPKPGGNSIKASSGINGAPTRFQQAAWPNLGPDETFWDDTVRSAGARLSSQTTSQPAARAQRESLISVLTQRSADAINFLADLGVDLTVVAQLGGHSHPRTHRGAGKTPPGAAIITTLVAKLKEAGGDRFELMTDCEVTRLLTDPINAAVSSNGNGGSSVDHQSVTVTGVEYRSTNDSGNGGSGDDGTSLHQLTGPVIFATGGFGGDTHGLLARYRPDLDGMPSTNDPRPGTHDLLAAVGAKLVDMDSVQIHPTGFVDPANPLAPVKFLAAELLRGEGGILLHNSKRFVNELETREHVSNTIMALPGDGVEGASLRQWDIQLLLDPGAAEAAAGHMGFYLWKGLMKKLKVSELDATTKETLEEYASIVRREKEDPFRRKAFGHWKLGVNSDGIVDENAEVCVGRVTPIVHFTMGGAVFNEHAQVLSSELGEEQKPIQGLWAAGEITGGIHGDNRLGGSSLLECVVFGRIAGAEAADIAKRAYI
The following text describes a protein:
Function:
The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.
Sequence:
MSNVDLDSLPVQFKQAVEAIRAAVPAELASPKWGIICGSGLSGLASTLESAVHVPYTSIPGFAESTVQGHTSSLAFGYLSTTPSKRVAVVACLGRFHTYEGHSAATCVFPTRVMKLLGCRALVVTNAAGGLNDTFQVGTIMSIHDHLSLPTLTATNPLIGANISALGPRFPPLSNAYDLELRLALYRAAEKLSLLDSLASGTYAYVLGPSYESRADANFLKSVGADAVGMSTVPEVIAAAHTGLKTLAISLITNKVVLEPHFDFHSALKAEKQGGEKLELIVNRLIQSDQAAAANQEEVLQAGANRADDIRRLVAEVICSTPV