lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins (Probable). Can phosphorylate casein on threonine residues in vitro. Involved in the regulation of flowering time through gibberellin (GA) signaling, and independently of photoperiod. Phosphorylates the DELLA protein SLR1, stabilizing SLR1 protein and sustaining SLR1 activity as repressor of GA signaling. Required for normal development of male floral organs and grains, through modulation of GA signaling. Targeted and repressed by the homeobox protein HAZ1 during GA signaling. Can phosphorylate phosvitin and SLR1 in vitro. Is not required for clock function in either the presence or the absence of light signals. Involved in a genetic control pathway for photoperiodic flowering under long day (LD) conditions that includes HD1, GHD7, HD5 and HD2. Phosphorylates and activates GHD7, a major floral repressor under LD conditions. Phosphorylation of GHD7 enhances its function in the repression of EHD1, HD3A and HD3B/RFT1, and obviously delaying flowering.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MPELRGGVWRARLRSKKVYDVQDADPAASPVSPAPRGRTGRRGGAAAGRGNKTVAEGGGRKALKPRGKGCRAVDLCKDQPCKDLPEVIARKAVTGKAQEDLGLNKVADRAANLMMDGESGDKFAAAEDESTTTPVPERVQVGNSPEYITDRKLGKGGFGQVYVGRRVSGGGSRTGPDAQEVALKFEHRSSKGCNYGPPYEWQVYHTLNGCYGIPSVHYKGRLGDYYILVMDMLGPSLWDVWNSVGQAMSAHMVACIAVEAISILEKLHSKGFVHGDVKPENFLLGHPGSVDEKKLFLIDLGLASRWKEASSGQHVDYDQRPDVFRGTIRYASVHAHLGRTGSRRDDLESLAYTLIFLIRGRLPWQGYQGDNKSFLVCKKKMATSPELLCCFCPAPFKHFLEMVTNMKFDEEPNYPKLISLFDGLIEGPASRPIRIDGALKVGQKRGRMVVNLDDDEQPKKKVRLGSPATQWISVYNARRPMKQRYHYNVADSRLHQHIEKGNEDGLYISCVSSSANFWALIMDAGTGFCSQVYELSQVFLHKDWIMEQWEKNYYITAIAGATNGSSLVVMSKGTPYTQQSYKVSESFPYKWINKKWKEGFHVTSMATAGNRWGVVMSRNAGYSHQVVELDFLYPSEGIHRRWETGYRITSTAATPDQAAFILSIPKRKPMDETQETLRTSSFPSNHVKEKWSKNLYIASICYGRTVC
The following text describes a protein:
Function:
Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Binds to single-stranded DNA, transiently cleaves and then rejoins the end, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate. Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair or for DNA protection (Probable). Reconstituted holoenzyme binds dsDNA a bit better than ssDNA, this subunit preferentially binds dsDNA. In isolation this subunit has DNA-stimulated ATPase activity that is stimulated by topoisomerase-domain containing RgyA. This subunit inhibits the relaxation activity of the topoisomerase subunit while promoting positive supercoiling.
Miscellaneous:
MISCELLANEOUS: This enzyme is the only unique feature of hyperthermophilic bacteria/archaea known and seems to be essential for adaptation to life at high temperatures. It may play a role in stabilization of DNA at high temperatures.
Subcellular Localization:
Cytoplasm.
Domain:
Introduction of positive supercoils requires the cooperation of both the helicase-like and topoisomerase domains of the 2 subunits. The helicase-like domain probably does not directly unwind DNA, but more likely acts by driving ATP-dependent conformational changes within the whole enzyme. A beta hairpin in the 'latch' region of the N-terminal domain plays a regulatory role in the enzyme, repressing topoisomerase activity in the absence of ATP and preventing the enzyme from acting as an ATP-independent relaxing enzyme; it also helps to coordinate nucleotide hydrolysis by the ATPase domain with the supercoiling activity of the topoisomerase domain.
Sequence:
MKIYYNNVCPNCSGRISNERLIKGLPCENDYPYEEGTIEQVYEYLKENNKLKDWANIYNIEKAKKEFEEFFYKAVNNKPWSAQRAWFIRAYKGYSFSIIAPTGMGKTTFALVNALYWGKKGKKVYIIVPTRTLVKQLYEKINVFAERVGFDNIIVAYYGNNKQKKEAKELIKDGAFSILITSNQFLSRNFDLLKNNYFDIIFADDVDSIMKSSKNIDRILYLLGFSETTIEKAMQLIKLKISGKDLEKIRKMEEQLKELVRKEQRGILIAASATGSMRGLRVKLFRELLGFEVGAAKTTIRNIIDVYTEMRDYKKQTLELIKKLGNGGLVFVPTDYGIEKAEEIAQYLKENNIKAEAFYSGKSIELLDKYANKELDVLVGVAHYYGLIVRGIDLPHVVKYAIFVGIPRFRFSAKEKETKIGRILLLASTLSDYADEEFKKKLNTTYNMIKRVSTGALKMVEEAIEQNKELDGFLEELRKNIIYLRDKSFELINREDIIKKLEENPFIALERGDGINILIPDVKTYIQASGRTSRMYPGGITKGLSIILSDNEKLLRALEFKLKLLGIDLHPGSSS
The following text describes a protein:
Function:
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Subcellular Localization:
Cytoplasm.
Domain:
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Sequence:
MKQLFLIIGAPGSGKTTDAELIAKNNSETIAHFSTGDLLRAESAKKTERGLLIEKFTSQGELVPLEIVVETILSAIKSSGKGIILIDGYPRSVEQMQALDKELNAQNEVILKSVIEVEVSENTAKERVLGRSRGADDNEKVFHNRMRVFLDPLGEIQNFYKNKKVYKAIDGERSIEEIVGEMQEYILSFGN
The following text describes a protein:
Function:
DNA-binding protein involved in cell cycle control. May act as a transcription activator. Plays a role in pre-mRNA splicing as core component of precatalytic, catalytic and postcatalytic spliceosomal complexes. May also play a role in the response to DNA damage (DDR).
Subcellular Localization:
Nucleus. Cytoplasm. Note=May shuttle between cytoplasm and nucleus.
Sequence:
MRNVKGGVWKNTEDEILKVAIMKYGLNQWARISSLLTRKSPAQCKARWHEWLDPSIKKTEWSKEEEEKLLHLAKIFPSQWKTIAPLVGRTASQCLERYNRLLDEVQRQQDNENGGGSGGGGTTTTTTTTTGENDPRRLRMGDIDPTPETKPAKPDPIDMDEDEKETLSEAKARLSNTQGKKEKRKFREKQLEEARRLAFLQKKRELKAAGINYNPKKKGKEKSWDISKEIPFYLKPKAGFYDVPDEELRDEPNKDASFIGKRVDQIENPNYLQRQEKLNKLEDIKKSKKEIFNLPQLISETSKSNDVEHSIKRTKLQLPEPQLTDDDIQEISDYEKLNGSGSGGGSGGVGVGEFPLPAPRTASISSTAANNNTNNIRTPMKQDTIMSEAQNLLALSNAQTPLKGGAGPNVSQTPLPKSVNNSTPFRTPNPLANQTPTQHNKKQSLNDSNEFAIEDKFKRQQGKNQLLSNLKNLPSPTIEYKLELPSELPTIEDDTTLELDNSEIHIREQQQLKHKEQFKLRNRSTVLKRNLPRSRNLFPINKNNNNNNNNNINQDELRILKEINRIISHDNKTFPNDSITPSSTFDDDDDDDNHHHHHDDIDNNSINDNDEKYENYDYFTNTELEFADKLIRDEIEQIKQELKQPLPSSNEILEEIDQIRSQFIYLPKENQFIEKSNANQTQLIENLQFEYDKTLNKIKNSSMKSVNLEKKLNIYNGGYQNRSNTIIKNIDDMFDQLEQSEIEYQCFVALKNNESIQMEKRLKSIENQVYDQCEIESRLQQKYAQLLNEKNLLKKKLSIF
The following text describes a protein:
Function:
Binds RpoD and negatively regulates RpoD-mediated transcription activation by preventing the interaction between the primary sigma factor RpoD with the catalytic core of the RNA polymerase and with promoter DNA. May be involved in replacement of the RNA polymerase sigma subunit from RpoD to RpoS during the transition from exponential growth to the stationary phase.
Subcellular Localization:
Cytoplasm.
Sequence:
MLNQLDNLTERVRGSNKLVDRWLHVRKHLLVAYYNLVGIKPGKESYMRLNEKALDDFCQSLVDYLSAGHFSIYERILHKLEGNGQLARAAKIWPQLEANTQQIMDYYDSSLETAIDHDNYLEFQQVLSDIGEALEARFVLEDKLILLVLDAARVKHPA
The following text describes a protein:
Function:
This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction.
Subcellular Localization:
Nucleus.
Sequence:
MNRGGKSKKRPLPSTTLPPGKHRATGTPSPSPVVGTLEEEFVDEDVFVDEIDEESLILRDMEEREALSARSSTWARPPLSPAYLANSQSIIFQQLEIDYVIKEIHKELLPGSSGQAAVIRIFGVTREGHSVCCFVHGFEPYFYIACPPGMGPDDISRFHQSLEGRMRESNKNANVPKFVRHIEMVQKKSIMYYQQQKSQTFLKITVALPTMVASCRGILDRGIQIDGLGMKSFQTYESNIVFALRFMVDRDIVGGNWIEVPAGKYKKDARTLSYCQLEFHCLYSDLISHAPEGEYSKMAPFRVLSFDIECAGRKGHFPEAKHDPVIQIANLVTLQGEDQPFIRNVMTLNSCAPIVGVDVMSFETERKVLLAWKDFVRDVDPDIIIGYNICKFDLPYLIEHSMYYVDMFYCAEWYMNITNLYLENMLFSDSQRAAALGIEEFPLLGRVKNSRVRMRDSTFSSRQQGTRESKETTIEGRFQFDLFQAIHRDHKLSSYSLNSVSAHFLSEQKEDVHHSIITDLQNGNAETRRRLAVYCLKDAYLPQRLLDKLMCIYNYVEMARVTGVPISFLLARGQSIKVLSQLLRKAKQKNMVLPNAKQSGSEQGTFEGATVLEARTGFYEKPIATLDFASLYPSIMMAYNLCYCTLVTPEDVRKLNLPPEHINKTPSGETFVKQSLQKGILPEILEELITARKRAKADLKEAKDPLEKAVLDGRQLALKISANSVYGFTGATVGQLPCLEISSSVTSYGRQMIEQTKKFVEDKFTTLGGYEYNAEVIYGDTDSVMVQFGVPDVEAAMTLGKEAAEYISGTFIKPIKLEFEKVYFPYLLINKKRYAGLVWTNPQKFDKMDTKGIETVRRDNCLLVKNLVTESLNKILIDRDVQGAAEYVKNTIADLLMNRIDLSLLVITKGLTKTGDDYEVKSAHGELAERMRKRDAATAPNVGDRVPYVIITAAKGAKGYEKSEDPIYVLENNIPIDPKYYLENQISKPLLRIFDPVLKNASSELLHGDHMRSISITTPSNSGIMRFAKKQLSCVGCKVPISSFVPLVSSLSDCICGIFLSSFLLLTSTSTGTLCARCKGREAELYCKNVSQVSDLEELFGRLWTQCQECQGSLHQDVLCTSRDCPIFYRRMKAQKDMATAKQQLDRWSF
The following text describes a protein:
Function:
Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Also processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Probably processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
Subcellular Localization:
Cytoplasm.
Sequence:
MKMLEQLEKKLGYTFKDKSLLEKALTHVSYSKKEHYETLEFLGDALVNFFIVDLLVQYSPNKREGFLSPLKAYLISEEFFNLLAQKLELHKFIRIKRGKINETIIGDVFEALWAAVYIDSGRDANFTRELFYKLFKEDILSAIKEGRVKKDYKTILQEITQKRWKERPEYRLISVEGPHHKKKFIVEAKIKEYRTLGEGKSKKEAEQRAAEELIKLLEESE
The following text describes a protein:
Function:
Stimulates feeding and grooming behavior, metabolic rate and locomotor activity and increases blood pressure. May have orexigenic activity. May promote aldosterone secretion by the adrenal gland.
Subcellular Localization:
Secreted.
Sequence:
MRGFRPLLSLLLPLSACFPLLDRRGPTDIGDIGARMNWAQLAEGHPPNSVQNPQPQALLVVAREQQASHREHTGFRLGRQDGSSEAAGFLPADSEKASGPLGTLAEELSSYSRRKGGFSFRFGR
The following text describes a protein:
Function:
ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Subcellular Localization:
Nucleus, nucleolus.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MLSKSNQPSDALLDADFSFSQPPFSTLIDSRVLVALADQKFAHPTLVQAKAIPLLLEGKDVLARARTGSGKTAAYIVPAVQKILEAKADLSPASAEYQATRAIILVPTKELALQVSSFTKNVTKYCDGLVQCVDVAAGGASIQRVLLNDKPDIVISTPTKLLSLLQSKSLSLSQLSFLAIDEADLLLSYGFKDDLTRIMDPTSGWIPKLGVQGCLMSATLSDDVEGIKGLVLRNPAILTLSEPASASSLLSQHYTHTSERDKFLLIYVLLKLKLIRGKSIIFVNDVERGYRVKLFLEQFGVKCCVVNSELPLASRYHVVEEFNRGVYDVVVATDEGAGADAEEEEDVKQEESESEGEEDEDDDKEAEDKEKEAKEEAKPAPGPSKRRATSPPSKPNKRARRADPTSSLARGIDFTSASSVINFDLPLTSTSYMHRVGRTARAGQSGLALSFVVPRENWGKDKAVSIKSAEKDEKVFERIKERVKKESDSEIKEWDWKGRKGEIEGFRYRMEDALKAVTGKRVAEARREEVRRELLNSEKLKSHFAANPLDLSYLRHDAPLHPARQQTHLKHVPNYLMPKIAALPTGGDVTDHAGVGFSRRGRGGHRGRGGRGSKSGRGKKVDPLKFK
The following text describes a protein:
Function:
Component of the DSC E3 ubiquitin ligase complex which is required for the srbA transcriptional activator proteolytic cleavage to release the soluble transcription factor from the membrane in low oxygen or sterol conditions. Required for growth during hypoxia and triazole drug susceptibility, as well as for virulence in a murine model of invasive pulmonary aspergillosis (IPA).
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MTFPAFLSPDPTWDGDSTGGPLLLTVRFSASIPDFPLDIENPDITTAAGLKQLIRTHLPPNLSSHRLRLIYAGRGLEDATPLSVSLKLPPSPSRTPVVQEDATTVKGKGKAPIREQPRLYIHCSIGDIVLSDADLAAEAAIATTLQQEQADEDYTGRKKQQQPPPSTTSAPRGFDRLLSAGFTPSEVSALRSQFMAIQSVSRTPDTMPTGAELRELEDRWMDEGSSAMAAGVPGGGEGISFADDDGGFGAGSRGAMDDMLWGAVMGFFWPVGCAMWLRREEGVWSWRKGLAVFVGVVINVAFGAMRIMN
The following text describes a protein:
Function:
Plays a role in transport between endoplasmic reticulum and Golgi. In pancreatic beta cells, required to transport proinsulin from endoplasmic reticulum into the Golgi.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus, cis-Golgi network membrane; Multi-pass membrane protein. Cytoplasmic vesicle, COPII-coated vesicle. Note=Enriched at the endoplasmic reticulum exit sites (By similarity). Incorporated into COPII-coated vesicles (By similarity).
Sequence:
MSGFENLNTDFYQTSYSIDDQSQQSYDYGGSGGPYSKQYAGYDYSQQGRFVPPDMMQPQQPYTGQIYQPTQAYTPASPQPFYGNNFEDEPPLLEELGINFDHIWQKTLTVLHPLKVADGSIMNETDLAGPMVFCLAFGATLLLAGKIQFGYVYGISAIGCLGMFCLLNLMSMTGVSFGCVASVLGYCLLPMILLSSFAVIFSLQGMVGIILTAGIIGWCSFSASKIFISALAMEGQQLLVAYPCALLYGVFALISVF
The following text describes a protein:
Function:
Acts as a chaperone and as an inhibitor for separase sep-1. Plays an essential role in maintaining chromosome cohesion prior to meiotic and mitotic anaphase, in cytokinesis and in organizing the spindle and the centrosome. Ubiquitination-dependent degradation at the onset of anaphase is likely to activate sep-1 resulting in the proteolysis of the cohesin complex and the subsequent segregation of the chromosomes. Also required for cortical granule exocytosis.
Subcellular Localization:
Cytoplasm. Chromosome. Cytoplasm, cytoskeleton, spindle. Note=Localizes to cytoplasm in germ cells. After oocyte nuclear envelope breakdown, localizes to chromosomes and spindle microtubules until meiotic anaphase I where the chromosome localization disappears. Maintained at low levels in the cytoplasm during meiosis II and in subsequent mitotic divisions during early embryogenesis. Localizes to chromosomes during mitotic metaphase at the 4E embryonic stage.
Sequence:
MEDLNFEERGSTQIPASLQQHFSAKLGRQNELEKTPSRGGLGLVVNSSKTPGGKSLQSLASACKVPPSTKKNTIPIAFECYEDETDDQIADVATIKKTEKHPCSPIDTANRCETFDSLAADIEDDMLNLEDQDVVLSEDRPYGDVIDPAESEAEALAELGVEEWDSYPPIDPASRIGDDFNYVLRTEDFAEEGDVKLEETRHRTVIADIDEVKMSKAERNELFSMLADDLDSYDLLAEEANLPL
The following text describes a protein:
Function:
Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating.
Subcellular Localization:
Cytoplasm, cytoskeleton, cilium axoneme.
Sequence:
MASRSAGSLITHNNVTYIPPALMPGYRGHVPTASFTYGDTYGNTSARCFQDFRSTVLNSSRSPYCQGGQFPTSHSNDPALVIGHRSRGWDRFLHSPSWSRYNVDFKRSDELKQFHRAAEQHRDHYRDKSGTAHQVPHFIIPVKNPQTFPLPQQVL
The following text describes a protein:
Function:
Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC.
Sequence:
MGEKLTEYERRRLENIKRNDEMVAALKIHSRLNDLSAAAAASKRQRDESKSSKRSPVKKPRSESPVVLRRSLRSRGVPPDAATASGPNDDLTGRKLTFKNPQWNSRESTEVEGPLKMSGTYLGGDDGLNQKLIRTILQCSKKSVLSSDGDKGPRDSTVKLEKSEEFEKFIPGKRLTGSIDVNAFQLKPENIARVVPSRIMSLKFFPTVDMEMVVAGNKFGDVGFWNVNRKNEGGGGIYLYHPHSRPISGIVIDPFCISKMYTSCYDGFIRLMDVEKEIFDMVYYSDYTVYSMSQSPHDVKSLYFSEGRGGVNKWDVRAGKSCLKCDLHDERINTIDFNSENENIMATSSSDNTARIWDLRRINAVKPTPLKIVSHKRAVHSAYFSPTGKFLATTSLDDKVGLSSGANYEDTSMVYHYNRTGCWISTFRGIWGWDDSSIYIGNMKRGLDVISVEEAKTVTTLGSDLVSAITCRYEAHPYNVGMLAGATGGGQVYIWTQS
The following text describes a protein:
Function:
O-methyltransferase that mediates the formation of 3-methoxy-5-methyl-1-naphthoate from 3-hydroxy-5-methyl-1-naphthoate in the biosynthesis of the antitumor antibiotic azinomycin B.
Sequence:
MAAGSGSGTPPGTPPPTLLTDLATGLWKTQTLTAAIETGLFEALAAGDADAPETAQRLGIGKRPAEILLTACTALGLLEQRDGRYRNTAVAAHYLVPGLPDYFGGYVQMVARYTAPGWLRATEAVRTDAPTKPVPDPDRNMFEEGNRPESFWEGLFTFSTLTARQLAASVDLSGVRRIMDVGGGAGATLIELCRQHPHLSGTVVDLPHVCALAGERIAAAGMTGRIDTAAADFFADPLPSGHDAVLLSMILHDWDESQNRKILASCLDALPSGGTVLISELLVDDDKSGPVDAALMSMNMLVGTWGRNYTGAEYTDWLRDAGCSEVRTVRFASPGANGVVAGVKA
The following text describes a protein:
Function:
May catalyze the biosynthesis of dTMP using an unknown cosubstrate.
Subcellular Localization:
Cytoplasm.
Sequence:
MEDKFEIGRIIRAKNISDAWYRGLNIIWNHGQVITDERGSQIREFMDLMVVIENPYTDRIPEDTAWNEERLEEYAKQLISGENAQDFEYTYGQRLRNWNEEVDQIEYVIEKLQESPTSRRATAVTWIPPVDTKVNEVPCMILDDFKIRDGKVHLTTLFRSHDFGGAYPANLYGLSKLLEYVAGRVGVEPGMITTVSISAHVYDHDWDMVENIVKGIN
The following text describes a protein:
Function:
Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular Localization:
Cytoplasm.
Sequence:
MAPSRNGMILKPHFHKDWQQRVDTWFNQPARKIRRRKARQAKARRIAPRPASGPIRPIVRCPTVRYHTKVRAGRGFSLEELRVAGIHKKVARTIGISVDPRRRNKSTESLQANVQRLKEYRSKLILFPRKPSAPKKGDSSAEELKLATQLTGPVMPIRNVYKKEKARVITEEEKNFKAFASLRMARANARLFGIRAKRAKEAAEQDVEKKK
The following text describes a protein:
Function:
Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Major receptor that responds to all naturally occurring L-amino acids, except L-Gln and L-Asp. Also involved in repellent responses to trichloroethylene (TCE), chloroform and methylthiocyanate. Also mediates chemotaxis to histamine, but does not bind histamine. In addition, binds the quorum-sensing signal autoinducer 2 (AI-2), thus inducing chemotaxis toward AI-2 and biofilm formation.
Miscellaneous:
MISCELLANEOUS: PctA has a broad ligand range and responds to most of the proteinogenic amino acids, whereas PctB and PctC have a much narrower range and show strong ligand preference for L-glutamine and gamma-aminobutyrate, respectively. These receptors are paralogs: pctA gene duplication in the common ancestor of the genus Pseudomonas led to pctC, whereas pctB originated through another, independent pctA duplication.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Domain:
The ligand binding region binds directly to 17 L-amino acids.
Sequence:
MIKSLKFSHKILLAASLVVFAAFALFTLYNDYLQRNAIREDLESYLREMGDVTSSNIQNWLGGRLLLVEQTAQTLARDHSPETVSALLEQPALTSTFSFTYLGQQDGVFTMRPDSPMPAGYDPRSRPWYKDAVAAGGLTLTEPYVDAATQELIITAATPVKAAGNTLGVVGGDLSLKTLVQIINSLDFSGMGYAFLVSGDGKILVHPDKEQVMKTLSEVYPQNTPKIATGFSEAELHGHTRILAFTPIKGLPSVTWYLALSIDKDKAYAMLSKFRVSAIAAALISIVAILVLLGLLIRLLMQPLHLMGRAMQDIAQGEGDLTKRLAVTSRDEFGVLGDAFNQFVERIHRSIREVAGTAHKLHDVSQLVVNASNSSMANSDEQSNRTNSVAAAINELGAAAQEIARNAADASHHASDANHQAEDGKQVVEQTIRAMNELSEKISASCANIEALNSRTVNIGQILEVIKGISEQTNLLALNAAIEAARAGEAGRGFAVVADEVRNLAHRAQESAQQIQKMIEELQVGAREAVATMTESQRYSLESVEIANRAGESLSSVTRRIGEIDGMNQSVATATEEQTAVVDSLNMDITEINTLNQEGVENLQATLRACGELETQAGRLRQLVDSFKI
The following text describes a protein:
Function:
Binds directly to 16S ribosomal RNA.
Sequence:
MPNTSSASKRLRQNEKRRLLNRATRSNMRSTIRRVREAVENNDLETAKNEFKVAQKKLDRAAANNLIHKNAAARTKSRLNNLIKNAAQTA
The following text describes a protein:
Function:
Involved in the synthesis of glucuronoxylan hemicellulose in secondary cell walls.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MSSGSSLMIWSGWSSGFSSIAALGVSVHLVACIASLMLGMELSLILFSSSSDYHRANRGQPLLLESTIASHGAGGAPRMAMSAAGPPKTMASSSPSSCVHPGRHPIIVRPWPHPNPRELAAAQAIMDRVQLEQRRAFEEEELMNKKQEVIVVTTLGDCKVGQQRERRMQVLLRLGAMANTLACAASRASISWIVMECSNFTNDHQRDTTREVLSRSRATKFALLEPRMDDLASSMALSRRIQSLRSIFLASFIRENKMEGIIVFIDEHSTASLHLFDELQKVARVAAFPAGLARTSPPLHGVFTQRTTFGSAGKLVNGWELSSNSSNTSIVQSVPAHEWTGLAFNSKMLWSEERFSWARVWDEWIMLYPNSTVFGELYGLIRDIKIVEVLGSDEVALSSSKREFFSVEVHEQQDSHQAQSVPKFLLHSVEDSDAIGQGVRKHMNNNNNNINIHINFKNKCDRADLKDDIHKDDQREEKHKEQRDNQEKHNKREDKDEKKTFPYVENVVEL
The following text describes a protein:
Function:
Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).
Subcellular Localization:
Cytoplasm.
Domain:
IleRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated valine is translocated from the active site to the editing site, which sterically excludes the correctly activated isoleucine. The single editing site contains two valyl binding pockets, one specific for each substrate (Val-AMP or Val-tRNA(Ile)).
Sequence:
MKKVEPVNFRELDKKIKKFWEENDIYQKVKKKNERNKEFYFVDGPPYCSGAIHLGTAWNKIIKDTYLRFKRMQGYNVLDKAGWDMHGLPIEVKVENEFGIKNKKEIETKIGVKQFIEKCKEFALKHKEIMEKQFKNLGVWLDWENAYMPITKEYMEIGWWTLKVAHEKGLLTRDLRVVYWCPRCETALAEHEVRGEYKEVYDPSVYVKFRLANEENTYIVIWTTTPWTLVANLAVTVHPDYDYAYVEVEFDDKKEVWIIAEKLVEEVINKAKKFHNIKNYKIIKKVKGKELEGIKYIHPLLEENERQKEFAELENAHTVILGEHVTLEGGTGLVHTAPGHGEEDFEVGKKYNLPIYSPIDDEGKYVEGKWKGVFVKDADAEIIETLKNKGLLVYAGKIKHSYPHCWRCKTPLLFRATEQWFLEISKIKDNIIEHAKTVQWIPHWVETRYINGVKFVGDWNISRQRYWGIPIPVWVCEKCGKYIVVGSVEELEEKMINKDEVGEINDLHKPTVDKIKLRCECGGEMKRVPDVLDVWFDSGLAPYASIGVKELKKADFITEGHDQVTKWFYSQHALSAIVFNDIPYKKCLMHGFTLDEHGDKMSKSLGNVVNPDDVVEKYGADLLRFYLLSANKVWEDLRFVWSEMDDVLSLFNTLWNAYMFAVNYMVLDNFKPDEKYFEYLKDEDRWIVSRINSVAKIAIENLEVPYFHTYTWTLKDFILNDLSRWYIRLIRDRTWKEKDDADKLAAYQTLYYVLLKLATILAPVAPHTAEAIYQNLKTEDMEESIFMNKIEVDEEFIDEELERDMAIVRDVVDAIYRGRDRIKYTLRYPLKEITIAGGEEVKKAVERFEYIIKEQGNVKNIKFGEVEGSKYIIKPNYRELGKRYRSEVPKVVEALNKADAKELMERLKEGAVILDGYEIKPEYVEIRLEIPEHIAGVEFSKGTVFINTEITDDLIKEGLMREVIRRIQAMRKDMDLDIEEKIKIKVEGIDLDEFKEIIEREVRGQFVDEIKADYEKDWEIKTPNGEKYNVKIAIERINK
The following text describes a protein:
Function:
Catalyzes the last step of tRNA splicing, the transfer of the splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-ribose 1''-2'' cyclic phosphate.
Sequence:
MYKNMNSHELIEESNNSGTPATKSSSKPTKKIRPRNDLVHYSKALSKVLRHTAKANGLQIREDGYIEVDSILKLPQFRGMGMELLLSIVKGNDKKRFTMEEVEGVLYIRANQGHSIKAVQVPMARIDNASSIPKVVHGTKKELWPVISKQGLSRMKRNHIHCATGLYGDPGVISGIRKSCTLYIYIDSAKAMQDGVEFYRSENGVILTEGVNGLLSSKYFSRVETSDGEVLLDAKASPKNNRSDESDQSDPESIDPFCDNLQALSMHELELLEEKHSNFGYSEGIIKGKMQVAQSGFDDGFKHGSRLGFQMGKTIGTLKAKLYIFEENEQMEILKQELDRLQESAEFHIFVANHKEEILKCIREK
The following text describes a protein:
Function:
Cytoplasmic and mitochondrial threonylcarbamoyl-AMP synthase required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. Participates in t(6)A37 formation in cytoplasmic and mitochondrial tRNAs. May regulate the activity of some transporters.
Subcellular Localization:
Cell membrane; Peripheral membrane protein. Cytoplasm. Mitochondrion.
Sequence:
LLVFSSCTGHWLSFSPHMGLSEGLAGSAWSSRLLCPPSPALGAPGAQLLRLPGSGAIPTAAVVELDASAMVAVPTNTLYSLACSGRSEAKLLAVCLGLVADIYRYCHVRAPEGLLKDLLPVPMTLVMERSEQLNKDLNPFTPLVGIRIPDHAFMQDLARVFGGPLPLTSANLSSQASSLNVEEFQDLWPQLSLVIDGEPAGDGQSSEYHLGSAVVDVSVPGRFGIICPGCALESTTAILQQKYRLLPSYRSCL
The following text describes a protein:
Function:
Regulatory subunit of the condensin II complex, a complex that seems to play a role in prophase chromosome condensation and in chromosome segregation in mitosis and in meiosis.
Subcellular Localization:
Nucleus. Chromosome. Chromosome, centromere. Note=Localizes to the core of each sister chromatid in meiosis.
Sequence:
MTRNAPPGQESTDLAWLVTPAKDLVENFSIDVLKALAGYLEVIRQESEDTDNQVDAATTYRLFDFQRACRIIQGSCAVYGRKVDHVYELTISVVDLVENKGQDDGNTGSRRGAGRRKNFNLGSTNYDLADIDSLKQEALANFEKTVKEEKKSIDAVRMVENAEVIESQYERKSCLVAKPTQFMFKLNYGQLNRTDEQILNAKSRPDVIGKVKDFEIKKSKVKHDQQILYSHDCYRGNLDQFTLPGARWMPDNKELAANFGVADLEVELDLEQEHEKISAYGPFKDPLSGREVVPPPRWFIEQEAVRQNQEIQSRATSRAITIAAKTLRDSQGFGSQPTRLSQPFVERHRQSNHLNDFLSFVEGRVNKNRPSTHLTTGLVDMFVDNFGSVMQNDEPNTSRRPDENYAPMDFDDDFGGGGDDDDDDYIRNLSRRDEKRAPAPWDELDKNHIIWYTGDENLPVVSKPVKKITKFQPKPAEMLARKQRREEKINKSRRDEFMETHDYLQDYYYWRSAARINPIKDWKIESLRTAILAEKKRRIKEKTAKIREARIQNMQRKRTARVIPVEQFEPVTEDIPTSNRRTLGAEYDDVVDEDLAAEVELSMFGGGFDDDEEDVRPRGERPPMAPNNLEFDALQTDFDIPPAEYVPLRFEDIDDAELNSVINLPGNLLIDKALPLLKKFAENRTDREQMAYEMAKAYEDVDVAVSTLQEHVDKWHSRMEPILEEGETRKEYDVHAVGRAVIGQYDIEGGTKRLLDLVMDRPWYEISRYFLSCLFMCNVGNVMVSEDMELPLEERINSMKITLLKRDMHCEMFKEAGALDA