lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Has an unusual substrate specificity for synthetic organophosphate triesters and phosphorofluoridates. All of the phosphate triesters found to be substrates are synthetic compounds. The identity of any naturally occurring substrate for the enzyme is unknown. Has no detectable activity with phosphate monoesters or diesters and no activity as an esterase or protease. It catalyzes the hydrolysis of the insecticide paraoxon at a rate approaching the diffusion limit and thus appears to be optimally evolved for utilizing this synthetic substrate.
Subcellular Localization:
Cell membrane; Peripheral membrane protein.
Sequence:
MQTRRVVLKSAAAAGTLLGGLAGCASVAGSIGTGDRINTVRGPITISEAGFTLTHEHICGSSAGFLRAWPEFFGSRKALAEKAVRGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAADVHIVAATGLWFDPPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQELVLKAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDDTDDLSYLTALAARGYLIGLDHIPHSAIGLEDNASASALLGIRSWQTRALLIKALIDQGYMKQILVSNDWLFGFSSYVTNIMDVMDRVNPDGMAFIPLRVIPFLREKGVPQETLAGITVTNPARFLSPTLRAS
The following text describes a protein:
Function:
Represses the transcription of several genes encoded within the Vibrio 7th pandemic island-1 (VSP-1), including dncV, VC_0176, VC_0178 and VC_0180.
Sequence:
MRRSMKISAEMYKLLIERTLDGFSVIELRDEFIVIKDSLIDPDEAYKKVYRQILRFIKKGWLNGEGSGRQKRYFQTDTFKALHAEPKSENVDIEIVLNQDYSVLVSERNQYKGELEIVLGEIDEYQSLNIRFPELEPKLITLLDEAKERSACLLGKVNGLTNVLKVLSGQKIVHQKFKTKALLFERT
The following text describes a protein:
Function:
Probable adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase.
Subcellular Localization:
Cytoplasm.
Sequence:
MPRNVKKNPRDVTKLSGKPLAETIEPSPVLKTLQEGWVTSPDLIEGDLSFTLEVIQNMTVFLLANPNLNSSHLFRADILYDSLGVLSAPHAMEQSRDQGSGGRDQDTQKEDYVEPLPARSVPGFELKRTFVRRLIPRNRNLDRPLEQTCHFYEADELPPTSNSTNIAQSEQCESKAESPRQRFLVIYLPHVSSKEEMPWYHPLLRSLAFLYDFTPNAFPHSSEENKGTGIMSVHFLPYEEEPIQNRLERTLLALLSTHIRLARQTRLDEKPEGGNYNPHKDNVIPKHLVQDTYARLKLKYAADLCQNWVEDTEPTKHVFEDLSITAFLIELWRSMYGVVPADERSPDQKEQGKYDLKFPGFVDVACGNGVLVYVLLSEGYHGWGFDARRRKTWSIFPSSIQERLKEEIYIPKPFADVCTDSEMDFGVKTHTGMFPEHTFIISNHADELTVWTPLMAALSNPASPLPFISIPCCSHSLSGARYRYPPPKPNQKGSVDRPEDQEVEQNPQPAAGDLKALRAAKQKERTDTGAANSMYGSLTAKTVATAEEIGYEVEKTLLRIPSTRNMGVIGGRRRTTQEWTSRVHSAQASQAVGCSAPEAVRAAAQVLEWVAAVVQRECAREGGVEVAAKVWIERAKGLHKGQGKGNQPAH
The following text describes a protein:
Function:
Transcription activator that binds to the secondary wall NAC binding element (SNBE), 5'-(T/A)NN(C/T)(T/C/G)TNNNNNNNA(A/C)GN(A/C/T)(A/T)-3', and to the tracheary elements (TE) specific regulating cis-element (TERE), 5'-CTTNAAAGCNA-3', in the promoter of target genes (e.g. genes involved in secondary wall biosynthesis, cell wall modification such as xylan accumulation, and programmed cell death). Involved in xylem formation in roots and shoots, especially regulating metaxylem vessel differentiation by promoting immature xylem vessel-specific genes expression, especially genes regulating programmed cell death (PCD) and secondary wall formation in tracheary elements (TE). Can activate MYB25, MYB46, MYB58, MYB63, MYB83, MYB103, CESA4, LBD15, LBD30, ERF115, XCP1, XCP2, NAC010/SND3, KNAT7, ASL19 and ASL20 expression.
Subcellular Localization:
Nucleus.
Domain:
The NAC domain includes a DNA binding domain and a dimerization domain.
Sequence:
MESLAHIPPGYRFHPTDEELVDYYLKNKVAFPGMQVDVIKDVDLYKIEPWDIQELCGRGTGEEREWYFFSHKDKKYPTGTRTNRATGSGFWKATGRDKAIYSKQELVGMRKTLVFYKGRAPNGQKSDWIMHEYRLETDENGPPHEEGWVVCRAFKKKLTTMNYNNPRTMMGSSSGQESNWFTQQMDVGNGNYYHLPDLESPRMFQGSSSSSLSSLHQNDQDPYGVVLSTINATPTTIMQRDDGHVITNDDDHMIMMNTSTGDHHQSGLLVNDDHNDQVMDWQTLDKFVASQLIMSQEEEEVNKDPSDNSSNETFHHLSEEQAATMVSMNASSSSSPCSFYSWAQNTHT
The following text describes a protein:
Function:
Plasmanylethanolamine desaturase involved in plasmalogen biogenesis in the membrane, required for light-induced carotenogenesis. Plasmalogens are glycerophospholipids with a hydrocarbon chain linked by a vinyl ether bond at the glycerol sn-1 position, and are involved in antioxidative and signaling mechanisms, most precisely in sensing photooxidative stress through singlet oxygen. Participates in the light-dependent inactivation of the antisigma factor CarR. Mediates signaling by singlet oxygen, generated via photoexcited protoporphyrin IX.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Domain:
Histidine box-1 and -2 together with other histidine residues are essential for catalytic activity.
Sequence:
MKTQEIEKKVRQQDAQVLAQGYSPAIRAMEIAAIVSFVSLEVALVYRLWGTPYAGTWLLLSAVLLGYLAADFVSGFVHWMGDTWGSTEMPVLGKALIRPFREHHVDEKAITRHDFVETNGNNCLISLPVAIIALCLPMSGPGWVFCASFLGAMIFWVMATNQFHKWSHMDSPPALVGFLQRVHLILPPDHHRIHHTKPYNKYYCITVGWMNKPLTMVHFFPTAERLITWATGLLPRQDDIGAEAARALVVAAGGSEAPVVQAAKELLTQATVQEKPASTRP
The following text describes a protein:
Function:
Protein-tyrosine phosphatase that could participate in the transfer of hydrophobic ligands or in functions of the Golgi apparatus.
Subcellular Localization:
Cytoplasm.
Sequence:
MAENQLTAQEERAIDEFLAELKTREQPQLVSVPPNTALKFLMARKFDVSRAIDLFQAYRNTRLKEGIYNINPDEEPLRAELLSGKFTVLPGRDENGAALALFTARLHRPDVTTHKAVLQAIIYQLDKAIERVETQRNGLIFIYDMINSSYGNFDYELCVKILNLLKGAFPARLKCVFIVSSPLWFRAPFAVLRLFVREKLRERVRTVKAHELVNHIPKESLPEHLGGTSKYSHVSWIQSCVNSRQTQENADCMDHLFMIYTSDQNPVSDRLNSNCTQQNVTDNTRLIHNHYHENRTKNYSDVHRVSSCVHWNGSAGSGNYDCYDKNSSTNTNCRRPPPQSETPPDTPLYKQPADNPSIPPLPQKSRPLPPGMELSIHMPEDGGMMVLGLVQHVKRMKKRGIFQEYEEIRKDPPVGSFDISKKSHNQAKNRYSDVLCLDQSRVKLGLVGTDETTDYTNASFMDGYKRKNAYIATQGPLPKTFDDFWRMVWEQKVLIIVMTTRVIERGRIKCGQYWPLEAGRSEDTGHFIIRNIHIDLFQDFKLTHLEVYNKQTDESQSVAHYQYMSWPDFGVPKSASAMLDFRTQVKQHQAVAVQALGMAWTGHPAGPPVVVHCSAGIGRTGTFCTLDICLSRLEDIGTVDVLQTVKRMRTQRAFSIQTWDQYYFCYMAIIEYAQRKGIIAPVEWSDTDFETDSE
The following text describes a protein:
Function:
The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization; Transmembrane protein that plays important roles in connecting the extracellular matrix to the cytoskeleton. Acts as a cell adhesion receptor in both muscle and non-muscle tissues. Receptor for both DMD and UTRN and, through these interactions, scaffolds axin to the cytoskeleton. Also functions in cell adhesion-mediated signaling and implicated in cell polarity.
Subcellular Localization:
Cell membrane, sarcolemma. Cell membrane; Single-pass type I membrane protein. Cytoplasm, cytoskeleton. Nucleus, nucleoplasm. Postsynaptic cell membrane. Secreted, extracellular space.
Sequence:
MHIGLVSILMVSLVGTSCSNSQEKPIQRLYNVVAVVGRHFTYRVTPTDGSKNFKITEEGKKTLPHWLALDESTNTLEGVPSWRDKGTYHLELHGHETQHFKILVKDLNDIRSDLSLRNSNDTKVPDTKHIVCHSGLPVEAATIIFDLHAEKVDGKGRCALMKRVAEFADEAVESLHFSLGKGHNTALGLKDVQMLTAGPGNVQDARQPGLVISWQIGCGIDLAGTRVASLLKSSAETGAFHEALSAPVTGWHVATGFPKGPRHRARRQVILNLAPTPTPAQKKPYIPTKILQATPTPTATIAPPPSRVDASTVSIPTVRPTVTVPSNNAPVVISRLSRVTVYSGQLIRFLIPENTFSDREDGGTRRLNLKLLTLTGATIIPSSWILLNPASQEIYGLSITDLTTSHDFLVEAKDSGGLFTRQAIEFRVEQDLHQYNHEFTLEFSLSDNSAFMKNVELRLELLEKLSFYFGIAIQYVRAVSFNLGAAGINFKFHFANVPYEPCYGVLISSIIKKFGENGVNPALTTALQSRFRVTGGSYQRLGKCINSRPVVDQGVSSISAITGQALSYKVPSNAFRDAEDGPSDLTLNMLTSGLAKLPAMSWVLFNQQTNTIFGLPMEGMSGTYDYVLQATDRGGLKARDDFQINVQADNTLYNHEFTIVMDVDNVQFSSNVALRLQLLTLIAQYFQTTIDHVRVSAFGAGVTFSFRFDNIPYNECNKRLETMVNLFGKDTLNPSFTRALSPNYPVRSGSHKLLGPCNKPDSRPPVVGAPIPAIDVFSGQSIMRDIAPNTFKDGIDGDASNLKLDLLARGGIRLSPNSWIQLNGPALQIFGLATEDFGLHEFDLEATNSAGLKATAPFEVNIARDPVIYNHEFTLLLDYEKDTFLNVVSVRLELLRKLGKYFNVDVSKIRVKSYSATPDGVNFVFRIAGIPYEPCDSADLQQAITKFGKDSVSTAFINALKPEYPVKKASYETLGKCAANKIPTVKKGVTPTPIQAYGGQVITYPVPVDAFEDVEDGGTRNLTLQLLSADGKELPKSYWLIFNSDTQTIRGLPGSRQVGVHNFIMEAKDSKGGKVRNPFKIDVGEDTTPTSLLFTVYLDYDDDKFLNDVKVRLGLVDKIVDYFKINENEMQVDRYGSGVNFTFHLKTIPEKDCNHPSRTTAINKFGRRGKTSSAFKNALLPEYNVRQSFTEAIGECSAKGNTPPLLLTPVGTIAVQANHGFIYRIPYDTFFDREYGNTRNLDLRLRAGDRSRLPPGSWVTLEEAEQEIYIMPDEKLTGSHKFVLVAVDPADNKMKTHDVITIKVSEPVPPTTIFSLLLDTDEKAFQGNVKTRMGLLTKLAEYFKVTIPDIHIISYKPEDPGIRFTFGFSNVPTKPCDSPALAKLIELFGDSKVTDGLKDALKSGFTVKNGRVEQVGACKAPDINTAPKLFNAFDRLNVFGTQGLRFDIPGDSFFDKEDLYTKNLTLTLKLGEGDLGSLLPTSWILLNSTSQQIYALPMSDAIGLHKFVLEAADSGGLKAFDAFEVSVIKDEAGFNHQFTIFLNFDNATFMENVHVRLALVEKIAKFFGVNFTAIRVDNAGLGPFMTFHVAGIPLDDCNNPLLLKMQENFGPDGVSPALKAALAPYPVAGGDYTKTKPCGATAGIGASGVGDRGPGLWWTYALIPAIVLAVVILTIGLCVLLMMRARRKQRLSAEDRKTFIYKRKPVVFKEEYDVKEDLIKQPLVLPNEKPPLPPPAYPRTPNGSAVTTPNMGDERRAYQAPSFASGRQMSSSSSTGGFGGGGGGGGMGGGGGMAGGGGGMGGGGMAAGGGEFGGGEGMGGGGMAGGGGGMGGGGGGMGGGGEGMGAAGGGMGAGGEGGGAGGGGGGYSAQKSSSSFSYTSSSSSSAARKGAYSGYRLPPAYVPP
The following text describes a protein:
Function:
Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides.
Sequence:
MAMFKKVSVLTLLTTAVVGQDVITATGTNFSLNAEGMSYLFHVDHASGDLLADHFGGSISDFVPPAQPWNSGWNDQLSNKRREFPDIGRSDPRLPAIHIEHADGDTVSAFRYQSHNITEGKPSLPGLPATWGEAGNVTTLIVNLYDNVSDVSAALSYSVFPQYNAIARSFSITNHASSNGTAQGSGPITIQRAASFSTDFPNVDLEMIEPYGDWSDEFNVARRKVDYGRTSFGSQAGYASHVHNPFFALVSPSTTESAGEAWGFSLVWTGSFEATAEKYSNGFTRVLMGLNSLHASIKVQPGETFQSPEAVAVYSSEGVGGLSRSFHDLYRNHLSRHKATKETRPILLNSWEGLGFNINETSLVRLAEESEELGIQLFVNDDGWFGTEYPRNNDWTGLGDWTPNPRLFPSGFKHYVDSVNNLTVLNESSTRMQFGIWVEPEMVNPNSSLYLEHPDWVLHAGKHQRSLTRHQLVLNVGLPEVQDFIIDFMSKILDSANIQYVKWDNNRAMHEMARPSAGYDYILGLYRVIDNLTTKYPDVLWEGCASGGGRFDPGLLYYWPQHWTSDNTDASDRITIQMGTSLVYPPSSMGCHVSAVPNGATARNTSIEYRAHVAMWCGSFGLELNPEELTPVEAAGLPGIMAAAKRVNPIVINGDFYRLAWKDNSNWPAVQFVSADGNDAVLFAFQQSSVVKPAIPPLRLAGLDPKARYSNDWDNATYTGATYMNAGLNIPWKRTDYQSKMIWLTKQ
The following text describes a protein:
Function:
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MLKLLSSTAHTIHHSNPSPRVGSNPIKTPLFKALSQLTGWNRSSQELSRRAFCSNQSDAAADPKSDASNPEASDTKSSSAVVVSTTTTSLDDYQTVIALPLPKKPLFPGFYMPIYVKDRKLIEALQESMRRQTPYAGAFLLKDDEASADSSSSSTTCETENVLEKFKGKELLNRMHEVGTLAQISSIQGEQVILIGRRRLRITDMVSEDPLSVKVEHIKHIGDFNYQHLADFGAGISGANKHENQGVLEELDVHKRLELTLDLLKKEVEVNKIQASIAKTVEEKFSGERRQIVLKEQLKAIKKELGVETDGKSAFSEKFKERIEVNKDKIPKHVLKVIEENLTKLQLLEPTSSEFDVTLNYLDWLTVLPWGNISDENFDVLRAEKILNEDHYGLSDVKERILEFIAVGSLRGTSQGKIICLSGPPGVGKTSIGRSIARALDRKFFRFSVGGLSDVAEINGHRRTYIGAMPGKLVQCLKTVGTENPIILIDEIDKLGKGHSGDPASALLEVMDPEQNANFRDHYLDVTIDLSKVLFVCTANVIDTIPKPLLDRMEVISLAGYITDEKLHIARDFLVKNTCRDCGIKPEQVGVSDAALLSLIENYCREAGVRSLHKNIEKIYRKIALKLVRQRASTVVPAVSVDVTDTEDTKPLAKTDSETSTEGSTVLTDESATKTEQSGVVAEKVMIEESNLADYLGKPVFHTDKIYEKTPVGVVMGLAWTSMGGSTLYIETTFVEEVERKGRLRITGQLGSVMKESAQIAHTVARRIMLEKEPDNLFLANSKLHLHVPEGATPKDGPSAGCTMITSLLSLAMKKPVRKDLAMTGEVTLTGRILPIGGVKEKTIAARRCQVKMIIFPEANRKDFDELPENVKEGLDVHFVDEYEQIFELAFGYDH
The following text describes a protein:
Function:
This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand.
Subcellular Localization:
Nucleus.
Sequence:
MLEARLPEAVLLKKVLDAVRELITDANFECSEDGIRLQAMDNSHVALSAIELRTDCFEEFRCDRPMSIGVSLSSLGKILKSANNDDVLALKKSDDGDTLQMTFESPKSDRVGEFEMKLMDIDSEHLGIPDTQYDAVVKMSSGEFGRICRDLANIGESVKIEVSKEGVSFSAEGEIGAARMTLKQGSGTAVLADQDDDEDEDVKPAKKKRKQDATSSSSAGGQVPVKIEMQQAVNLTFSLKYLSNFAKAAPLADEVQLHMSNEVPLLCEFSFENGYVRFYLAPKLSEDDD
The following text describes a protein:
Function:
Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus membrane; Single-pass membrane protein.
Sequence:
MPPPPTSLYTLSLALALLLTLLVAGTLRLLAILPPRTRTQWRKRPVATRVLIVLGSGGHTHEMFYLLRDLDTSKYTHRTYVVSSGDAFSAQRAVEFERGLEEKEKEKEKEKRLGALRQQDAAIPSVSLNGKKVGKDEGRKCTGPEHYNVAVIPRARRIHQSLLSTPFSAMRTLLSSIPILLSSPPLLPNKPPSTPYESAAQDLPDLIITNGPATGVIVILGSLILRFFNFRSANSRGKCKTIYAESFARVKGLSLSGKLLSRVVDRFLVQWEELEGSGGGRGEFWGVLV
The following text describes a protein:
Function:
May be involved in the assembly of microtubule arrays during cell elongation.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Domain:
The ASD1 domain mediates F-actin binding.
Sequence:
MEALGTGRDRTSQASATESLDLRRLSTRADSAYSSFSTASGDPETRTPSPGTERLPYLDWDYVRVVWGSQSPTSKDAVLSTTQRPVQAVAGHSDPRSPEVQGSPGPLNRQDTPLLYALAAEAEATAHTAEPPSPPASRDAYRQRLQGAQRRVLRETSFQRKEFRMSLPGRLRPAVPTRLPTAHVRSASSSQELGEEEPARTAVPALAAAGRGRLSSQQRQCCFSEPGKLHRVGWSGGPTGEDLRKDYSTQELQRGMHAKSKGLLETQSLSSTELNSGPADLGNAHRPAGRSQSVSGEVMGPCKGSERTVATVQAVPQRADIRRPLLHTKLSRSLTQKEVTGVCPGEALQTKPAGCGRRISETSVSTPGPSLPEDDVFLREAKTPSPQDSQGLPTSTSYRQYENDLSKKAGQIAVSAERPLHETPGITGTEDCGQAVNGSVDLSRPTSIPETTNDDIPTFDTNGTTDPSAATEKKPLKPPPVDVLRPSDSETPGSPHHTSLTWGQFDSKTTWPSRHFEALVQELARLDPSLSRTLAAQPGPEPPQGLLDGLFPVEEIRSAMRPALEEMGEKAAGASEEGSCGHHLTQDLQTSQEASRSENSTPDPDQSSGQEFPEGNSTQAKKVELARLLQKMLQDLHAEQERLRGTAADWTQRNGALEAAVSQACTPRELERFRRFMTDLERVLGLLLLLGSRLVRVNLALARAGSNSDPDERASLLQRLQLLQRQQEEAKELKEHVARREQTLRQVLERELPAEHLRSYCVLLASKARILSQQRSLDDRIRFLKDQLDTIWSDLSHHPLSPRLTWAPAIRPLNKQPFLATLI
The following text describes a protein:
Function:
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes (By similarity). Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery (By similarity). Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional pre-initiation complex with RNA polymerase II and the general transcription factors (By similarity). Involved in development of gonad and seam cells. Plays a role in temporal regulation of seam cell division, probably acting as a part of the Mediator complex.
Subcellular Localization:
Nucleus.
Sequence:
MSGQGPPPSMTPQQQHMLMQQQQQQQMMRQQQMQQQQMQQQRQQQIQQQAQQPYQRARTPQMVPQGGSPGGAHLQMHPHLQPQGQMQPRSPLVGAQLQAPSSVPTAANPTTPQMMQQQMGMNQPMSLPPTHVSRPGSVAPPSSVPVNLQHTSGAPGLPGSQMEHQYPMHLQPQQQTLSRPGSQQSQHIQQPGSIQRPGSVLAPGSIPPGGPASQTGPQSIQVFGPGSVQPPGSTQAPSSVQPASTFNPGSIQAPASQQPPASVQPPPSAASGSTVAGAQSSKEPLKPNEEQIRMVQDPVDLVRNLVQKDLRNSLVEMNKRGAELVRQKQEGEVNEDGKAQYSRATNDFHAVCDEIDRTLTTVLETAKQLSKLDKVFFDRSSRDLDGEVMVNSVQNFVDNTEIVQRMFDDTIGSVTSSMESMRRRQKKWEDQHKNDDVEMME
The following text describes a protein:
Function:
RNA-binding protein required for assembly of the holoenzyme telomerase ribonucleoprotein (RNP) complex. Telomerase is an essential ribonucleoprotein enzyme that copies new telomeric repeats onto chromosome ends by repetitively synthesizing the short telomere-repeat sequence 5'-TTGGGG-3' using an RNA template component TER. TAP65/p65 specifically binds telomerase RNA template TER and is required for biogenesis and placement of the TER stem-terminus element: TAP65/p65 first protects the 3'-end of TER from degradation and acts as a chaperone to correctly fold TER for protein binding; it then bends TER stem-loop IV to position it for interaction of stem-loop IV with catalytic TERT RNA-binding domain.
Subcellular Localization:
Chromosome, telomere.
Domain:
The HTH La-type RNA-binding and RRM domains cooperatively bind to TER RNA UUU-3'OH sequence after it is transcribed by Polymerase III. UUU-3'OH-binding by the HTH La-type RNA-binding and RRM domains positions the xRRM domain to bind to the adjacent proximal stem-loop IV and central dinucleotide GA bulge.
Sequence:
MDEYLENTNLEELEQECFMEDYQHEDVVEQENHQVDANDIYENQQMNDESQLNQDVKISQQKEQAVEMIEEQQQNNQDKFKQFQDCMAHITELNFKRNYQNLTEQSSSNNVVAEELDIKESLKLQMEYYFCDTNLTHDSYLRGIISKSPKNCVDIKVFLKFNKIQQILKQIQDKQIVSTYGIENQSQKKNHKNYKNQNATFSKKDLIHLIRDSLKESKILKVKMDSLKVKRRFPFNLEQALKNSKQRTLYIDFLPPKCSKQTLVSIFGNFRIININLPLQKNSQLCQGFAFIEFFSEEEANQALITKNSSIPKELILLTEKKIGQGSIRIITYKKWQEEKQSFKELSKNQNEQKNKNMNQSRKASDEFVSIDVEIKQNCLIKIINIPQGTLKAEVVLAVRHLGYEFYCDYIDENSNQINSNKISLSTQQQNTAQCSNIQIENNLIQQDQHPQLNDLLKEGQAMIRFQNSDEQRLAIQKLLNHNNNKLQIEIRGQICDVISTIPEDEEKNYWNYIKFKKNEFRKFFFMKKQQKKQNITQNYNK
The following text describes a protein:
Function:
Plays a role in the regulation of phosphate uptake.
Subcellular Localization:
Cytoplasm.
Sequence:
MIRRKLTKQLEIIKDYLWDMKECVLKIIDDSLIALESKDKNLAKKIINEDEKIIDDYQYDIEDLCGRIIATEHPVATELREILAIIKIISSLERIADHATKIVKVVLLLESDLDDFDFLNLYFKPLREMADTAKEMLSDIFDAYFDGDFTKILKIVKYDNIIDKLFSKQKSIVIDAMKKNPENLDYLLNILFLNSFLERVGDHVATIGELLYFIRIGEKVNLT
The following text describes a protein:
Function:
Involved in the maturation of [NiFe] hydrogenases. Involved in the biosynthesis of the Fe(CN)(2)CO cofactor. HypC delivers iron-bound CO(2) to HypD where reduction to CO probably occurs. In complex with HypD, accepts the cyanide ligand generated by HypF and HypE, and also coordinates the carbon monoxide ligand. Involved in the maturation of the hydrogenase 3. Also participates in the maturation of hydrogenase 1.
Sequence:
MCIGVPGQIRTIDGNQAKVDVCGIQRDVDLTLVGSCDENGQPRVGQWVLVHVGFAMSVINEAEARDTLDALQNMFDVEPDVGALLYGEEK
The following text describes a protein:
Function:
RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Stimulates the 5'-3' DNA helicase activity of DnaB.
Domain:
Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.
Sequence:
MILKSSIDRLLQTIDIVEVISSYVNLRKSGSSYMACCPFHEERSASFSVNQIKGFYHCFGCGASGDSIKFVMAFEKLSFVEALEKLAHRFNIVLEYDKGVYYDHKEDYHLLEMVSSLYQEELFNAPFFLNYLQKRGLSLESIKAFKLGLCTNRIDYGIENKGLNKDKLIELGVLGKSDNDQKTYLRFLDRIMFPIYSPSAQVVGFGGRTLKEKAAKYINSPQSKLFDKSSLLYGYHLAKEHIYKQKQVIVTEGYLDVILLHQAGFKNAIATLGTALTPSHLPLLKKGDPEILLSYDGDKAGRNAAYKASLMLAKEQRRGGVILFENNLDPADMIANGQIETLKNWLSHPMAFIEFVLRRMADSYLLDDPLEKDKALKEMLGFLKNFSLLLQSEYKPLIATLLQAPLHVLGIRERVSFQPFYPKTEKPNRPQRFAHVSSAPSLEFLEKLVIRYLLEDRSLLDLAVGYIHSGVFLHKKQEFDALCQEKLDDPKLVALLLDANLPLKKGGFEKELRLLILRYFERQLKEIPKSSLPFSEKMICLKKARQAIMKLKQGELVAI
The following text describes a protein:
Function:
Probable member of a two-component regulatory system. It is not known what protein it phosphorylates and in which regulatory pathway it acts, as the narL and other nar genes do not exist in H.influenzae.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MYTKGSVSTRIAKYLFIILIVAGVISSLSLAIMSSNKYDAEAINISGSLRMQSYRLLYEMQEQPESVETNLRRYHISLHSSALLEVQNQFFTPNVLKHSYQNILQRWTNMEKYARQQDVKNYSKQLTDYVADVDYFVFELQRFSEQKWILGVSVLGFAMLLILLMVSYVIWYTNREVVKPLHLMTKASMQVQMRQFNHIPLDTRKQNELGTLARVFTQMSTELGQLYSRLEEAVNEKTQKLRQTNRTLSTLYQSAQLLNTNTINDKILNQVLNYIFISDHLNFVKVEVMGAEHWDITLGKQDANNELQIETLSVDNEELGVLSWQAGLPCPDPRIMQNLAQMLARALYFHKNLRQKEQLLLMEERSIIARELHDSLAQVLSFLQIQLTLLKHNLKKEDEQSKEKSLAIIANFEQALSGGYAQLRELLATFRLTIQEANLQLALKQVIDSLRSQTTMQMNVNCQLPSQSLNPQQLVHVLQIVREATTNAIKHSQGTVIEISARINAEGEYEILVEDDGVGIPNLEEPEGHYGLNIMAERCRQLNAQLHIHRREQGGTQVKITLPHTLY
The following text describes a protein:
Function:
Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. MlaD functions in substrate binding with strong affinity for phospholipids and modulates ATP hydrolytic activity of the complex.
Subcellular Localization:
Cell inner membrane; Single-pass type II membrane protein; Periplasmic side.
Domain:
Forms hexameric rings with a central hydrophobic pore via its periplasmic domain, which also binds phospholipids. Contains at least four binding sites.
Sequence:
MQTKKNEIWVGIFLLAALLAALFVCLKAANVTSIRTEPTYTLYATFDNIGGLKARSPVSIGGVVVGRVADITLDPKTYLPRVTLEIEQRYNHIPDTSSLSIRTSGLLGEQYLALNVGFEDPELGTAILKDGDTIQDTKSAMVLEDLIGQFLYGSKGDDNKNSGDAPAAAPGNNETTEPVGTTK
The following text describes a protein:
Function:
Vacuolar Fe(2+) uptake transporter.
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein.
Sequence:
MAFLGTSSNEMPIGHIEILIHSNDIEAKRSQDIAENNIDYSQRAQWLREAVFGAKNGLVLINLLMVGVEALNEDIIIMLLAGFAGLVVGACSMAIEEFVYTQLVRHGASAIGFSIGAVVSMLAAVFVWDYKIRLLVFAVPILALLVFGGVGIVLGKMLIGGWMTMAITFGFDKFIGYTRL
The following text describes a protein:
Function:
Possesses RNA-binding and ribonuclease activities in vitro.
Sequence:
MDGYEATRIVLSRIQSLDPENASKIMGLLLLQDHGEKEMIRLAFGPETLVHSVIVKAKKELGLMNCSRSPWSHQDELISPKNNRGSSLNPASLPFYANGGRSSRDLTNDFELMDDMNSRSTDFLGSVHARSGSCVLDGLGYGGDSDLGFGGVPCSYFARGFCKNGASCRFVHSDGGADLVGSPSRIELLRSNSVPPRLAHHFMTRSSLPSFSTKGVNLQQNDVQRAAAALMIGDELQKLGRWRPERIDLSAMACPASRQIYLTFPADSRFREEDVSNYFSTFGPVQDVRIPYQQKRMFGFVTFVYPETVKSILAKGNPHFVCDSRVLVKPYKEKGKVPDKYRTNQTTERELSPTGLDSSPRDVLGGRGFYNNTQDVLWRSKFEEEILELQSRRLMNLQLLDVKKHFQLNSPTNIHSPNPFSQSLISPRPLSVIKREYDGGEKGKGSSKEGSDDDTMNLPERLEDSLPDSPFASPAHHLLLFADSADNNGSDLWSPSSDNDDNSTPSTLSDSFNSFNYQMPRLPAIGMLPGRGGPTCRVGI
The following text describes a protein:
Function:
Pore-forming protein which might play a role in host defense. Exists as an antiparallel dimer in solution. Can also assemble into an octameric pore-like structure spanning the cell membrane. Oligomerization may be triggered by binding of the jacalin-type lectin domain to high-mannose cell-surface proteoglycans, and also requires a low pH environment. In vitro, shows high binding affinity for S.cerevisiae mannan and human HIV virus glycoprotein gp120.
Subcellular Localization:
Cell membrane.
Domain:
The jacalin-type lectin domain has strong affinity for high-mannose glycans with terminal non-reducing ends of Man(alpha-1,2)Man or Man(alpha-1,3)Man.
Sequence:
MTYPTNLEIIGGQGGSSFSFTGENNGASLEKIWVWVGGWQIKAVRAWLSDGRDETFGVPSGSHQEYVFTPGECFTSLSLWGNGAGTRLGAIKFKTNKGGEFFAHMTSWGLKTEYPMDVGSGYCLGIVGRGGSDIDCMGFMFLNAVQSTVLTNVNYPTINQLIPKVATEEIKSVSFENKTSVKQEQKVETSKKVIKTSSWSMTKSFSSTFSVEVSAGIPEIAEVSTGFSISFGVESTHSLEQTDEKNETLTTTVEVPPKKKVDVHITIGRASFDLPYTGTVKITCKNGSVLQYETKGQYKGVAYTDIKVNTVEKDL
The following text describes a protein:
Function:
Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z (By similarity). Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, and histone H2A to form H2AK4ac and H2AK7ac (By similarity). The NuA4 complex is involved in the DNA damage response and is required for chromosome segregation. The NuA4 complex plays a direct role in repair of DNA double-strand breaks (DSBs) through homologous recombination (By similarity). Recruitment to promoters depends on H3K4me. Also acetylates non-histone proteins (By similarity). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA) or (2E)-butenoyl-CoA (crotonyl-CoA), and is able to mediate protein 2-hydroxyisobutyrylation and crotonylation, respectively (By similarity).
Subcellular Localization:
Nucleus. Chromosome. Note=Following DNA damage, localizes to sites of DNA damage, such as double stand breaks (DSBs).
Domain:
The ESA1-RPD3 motif is common to ESA1 and RPD3 and is required for ESA1 histone acetyl-transferase (HAT) activity and RPD3 histone deacetylase (HDAC) activity.
Sequence:
MAVAEIKKEKGSSLSPEPSSPIQILSTEPDANTDIKQEKFTPKDILPGCKVHVSKDGEFRLAEILQEHIKKGRKVFYVHYQDFNKRLDEWIELDRIDFTRSLILPEIKADTKENKSKKKSKSKGQTKLSKNNTTANSTTGTPQPSDGQPIMGDDEMDLENLNVQGLKRPGEEFSREDEIKKLRTSGSMTQNHSEVARVRNLSTIILGEHIIEPWYFSPYPIELTEEDEIYICDFTLSYFGSKKQFERFRSKCSMKHPPGNEIYRDSKVSFWEIDGRKQRTWCRNLCLLSKLFLDHKTLYYDVDPFLFYIMTIKSDQGHHVVGYFSKEKESADGYNVACILTLPCYQKRGFGKLLIQFSYMLTKVERKVGSPEKPLSDLGLLSYRAYWTDTLVKLLVERNSPALFRKNNSQLEYDEAENGKDSSATPTPGPGSNASQSSILASAAASRSGLNSSPIFSNEITIEDISSITCMTTTDILHTLTTLQMLRYYKGQHIIVLTDQIMELYEKLVKKVKEKKKHELNPKLLHWTPPSFTANQLRFGW
The following text describes a protein:
Function:
Binds to the 50S ribosomal subunit and prevents its association with the 30S ribosomal subunit to form the 70S initiation complex.
Sequence:
MILKAKVLGSSNLGIYLRVAGRYLLTPKGVSRSLEGLADKLGLKIVEASVYESRMLGVLTVANSRALLLPSLSSERELRDLREKLDVEVHALPTTKLTALGNDIVANDYGAIVHPSFTDHELDIIAKLLGVKVMRGRVGGIPVVGSLVVANNRGCLISPSADDSELKGISDTLGVECLKGTINDGVIYVRVGLVACDSGALVGFPTTPIEIENLAEALKIEP