lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Exhibits NADPH-dependent reductase activity for a broad range of short-chain aldehydes. Shows highest catalytic efficiency toward butanal, propanal and the highly toxic aldehydes acrolein and malondialdehyde (MDA), which are produced mainly during lipid peroxidation. Mediates resistance to reactive oxygen species (ROS) elicitors, such as paraquat and potassium tellurite, probably by protecting the cell against the toxic effects of reactive aldehydes derived from membrane lipid peroxidation. Also acts, with lower efficiency, on acetaldehyde, glyceraldehyde, glycolaldehyde, methylglyoxal, glyoxal and hydroxyacetone. Could be involved in glyoxal metabolism, by catalyzing the reduction of glyoxal to glycolaldehyde, and further to 1,2-ethandiol. Catalyzes the reduction of isobutyraldehyde (2-methylpropanal) to isobutanol, and probably contributes to the production of isobutanol. Can probably catalyze the reduction of glutaraldehyde, a widely used biocide, to 1,5-pentanediol, which is non-toxic. Overexpression of YqhD protects the cells against glutaraldehyde toxicity. Can catalyze in vitro the NADPH-dependent reduction of furfural, a natural product of lignocellulosic decomposition, to the less toxic product, furfuryl alcohol. However, it is unlikely that furfural is a physiological substrate; In contrast, Sulzenbacher et al. detected significant activities only in the presence of alcohol and NADP(+). They reported in vitro NADP(+)-dependent alcohol dehydrogenase (ADH) activity towards various alcohols, with a preference for alcohols longer than C(3), but the affinity for the substrates is poor, suggesting that these compounds are not the physiological substrates. Perez et al. did not detect dehydrogenase activity with short and medium chain alcohols such as methanol, ethanol, propanol, butanol or isopropanol.
Domain:
Molecular dynamics simulations of the YqhD homodimer show that the oxidation state of the NADP/NADPH cofactor has a profound effect on enzyme structure and dynamics, which is consistent with differences in enzyme efficacy toward alcohols versus aldehydes. The NADP-bound YqhD fluctuates between open and closed conformations, while it was observed that NADPH-bound YqhD had slower opening/closing dynamics of the cofactor-binding cleft. The frequently sampled open conformation of the cofactor binding cleft with NADP leads to the more facile release of NADP while increased closed conformation sampling during NADPH binding enhances cofactor binding affinity and the aldehyde reductase activity of the enzyme.
Sequence:
MNNFNLHTPTRILFGKGAIAGLREQIPHDARVLITYGGGSVKKTGVLDQVLDALKGMDVLEFGGIEPNPAYETLMNAVKLVREQKVTFLLAVGGGSVLDGTKFIAAAANYPENIDPWHILQTGGKEIKSAIPMGCVLTLPATGSESNAGAVISRKTTGDKQAFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTKPVDAKIQDRFAEGILLTLIEDGPKALKEPENYDVRANVMWAATQALNGLIGAGVPQDWATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERVWNITEGSDDERIDAAIAATRNFFEQLGVPTHLSDYGLDGSSIPALLKKLEEHGMTQLGENHDITLDVSRRIYEAAR
The following text describes a protein:
Function:
Chorion membrane (egg shell) protein; plays a role in protecting the egg from the environment.
Subcellular Localization:
Secreted.
Sequence:
MQLGLWFGILAIAATPLVSANYGPAGGHGHGHGHGQYLSGPNAGLEEYVNVASGGNQQAANQIASQAEIQPTPEEARRLGRVQAQLQALNADPNYQKLKNSEDIAESLAETNLASNIRQGKIKVVSPQFVDQHLFRSLLVPSGHNNHQVIATQPLPPIIVHQPGAPPAHVNSGPPTVVRGNPVIYKIKPSVIYQQEVINKVPTPLSLNPVYVKVYKPGKKIEAPLAPVVAPVYSQPREYSQPQGYGSAGAASSAAGAASSADGNAYGNEAPLYNSPAPYGQPNY
The following text describes a protein:
Function:
Plays a role in meiotic chromosome cohesion and segregation. Necessary for sister chromatid co-orientation and sister chromatid cohension until meiosis II. May also be required for repair of programmed meiotic double stranded breaks. During spermatogenesis, likely involved in spermatocyte centriole cohesion, thus preventing their separation during the second meiotic division.
Subcellular Localization:
Chromosome. Nucleus. Cytoplasm, cytoskeleton, spindle pole. Note=Colocalizes with smc-1 along synapsed chromosomes during meiotic pachytene and diakinesis. Loaded onto chromosomes upon entry into meiosis. Localizes to chromosomes until meiotic anaphase II and to microtubules throughout meiotic divisions.
Sequence:
MVVSAEVIRKDAVFHVAWILGTGDSKKLSRREILDQNLPELCHSIIEMVPERHRGSATKTGLYLLSLLTYGTVLIHQVQVDFLKRDVEKLKELMKKKSFILLMAERFDRNQELQRKEDKFARLRSKPIMCVEELDRVDLAHLQAIGDELGINGNPGDFIMMDALPNMNQWIDNNSELNAIYGCVEPYLREKEITMHSTFVEGNGSNEHNKERRNDAVIADFSQLLFPEIPEITLGEKFPIDVDSRKRSAILQEEQEEALQLPKEASEIVQEEPTKFVSIALLPSETVEQPAPQEPIQEPIQPIIEEPAPQLELPQPELPPQLDAIDLVTIPASQQDMVVEYLQLINDLPDDENSRLPPLPKDLELFEDVILPPPAKKSKVEEEEDALERARRRPSSRPVTPINQTDLTDLHSTVRPEDPSFAIDSQIHDVLPQRKKSKRNLPIIHSDDLEIDEAVQKVLQADYSSLVRKKEDVIAKIPPKTDAVAVLMNLPEPVFSIGYRLPPEVRDMFKACYNQAVGSPVSDDEEDEDEEEEEEYKYAKVCLLSPNRIVEDTLLLEEQPRQPEEFPSTDNINPPRQLQENPVFENLEYEAPPHPIRTARTPTPIKDLKYSVISLFPTPEKRRETSIIAELNLDPIPVEEIDPLLTMRTEEELENVRRRQKSSLGVQFMRTDDLEEDTRRNRLFEDEERTRDAREDELFFYSSGSLLPNNRLNIHKELLNEAEARYPEWVNFNEFTADHDRKKAATAFEGLLLSLKNMKVEAKQEDPYFPILVRHISHEEM
The following text describes a protein:
Function:
Ligand for the receptor-type protein-tyrosine kinase KIT. Plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Cell projection, filopodium. Cell projection, lamellipodium. Cytoplasm, cytoskeleton. Secreted.
Sequence:
MKKTKTWIIICINLQLFLHCFGKPCGNPITDAVNDIPKLVGNIPNDYNMSVRYVPEKDGLPKHCWLYMMVVEMTHNLDKLSSKFENTSQNVLIIKNLSWIFQGIRQCIQLNDEMDFDSASSLYRVEVIKARDFFSYVTSTIEVFKEINDTEYSRLCILPQEYEFEYTTEDDFLILDSNHDLPYVPSTRKNSSRFDSSARSGFSTGTSIQYSTVLIALACLVIGFLLGVLCLWKFKHRQTQTQDNLSAVAVEPRAENESRHILQLAKIISV
The following text describes a protein:
Function:
Bifunctional diterpene synthase that directly generates the endocyclic double bond, as well as the hydroxyl group: produces an endocyclic double bond isomer of copalyl diphosphate (CPP), and carries out subsequent replacement of the diphosphate by a hydroxyl group to form (13E)-labda-7,13-dien-15-ol.
Miscellaneous:
MISCELLANEOUS: Selaginella moellendorffii contains two distinct types of functional terpene synthases (TPS) genes, the typical seed plants TPS genes (SmTPSs) and a microbial type TPS genes (SmMTPSLs).
Domain:
The Asp-Xaa-Asp-Asp (DXDD) and Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motifs are important for the catalytic activities, presumably through binding to Mg(2+).
Sequence:
MIEEMRKLLATLDDGEISPSAYDTAWVARIPSQSNATCPEFPETLEWIAHNQLPDGSWGDRNHFQIYDRVLSTVSCLVALKTWNLGHDNINKGERFLKQNIYKLTKDKGDLLCGFELIFMTMLEEAKQKGLDIPIDIPALKILQGYRQKKLQKIPLEMVHSIPTTILYSLEGLQDHINWEKILQFIGTDGSFLSSPSATACVYMHTKDPRCLEYLKGVVKKVKNSVPCQYAIDLFERLWIVDTLERLGIDRYFQPEIKNILDYVYKYWSDKKGIGWGRESYLKDIDDTSMGFRLLRLHGYKVTPDVFLNFMSSEDKFFCFPGESYHGASDIFNLYRASQVAFANDNILTKAKNYAHKYLSQLDKAYLDKWSAKKNFFQEVEFELSNQWNSCLPRAYSKSYIHNYGPNDIWIAKTIYRLPFVNNELFINLAKEDFNACQSIHQSEIQTLLRWWAALKFGDLPFFGDKVVTAHFSIASCMFEPEFSELRLFYTKYALLSSTLDDLADYYGSPAQTRCILEAIRSWDPSLVSHLSEEVQICFSGLYRTINEMVKSASKVQTGSSINIREHMQEQLAKLISAQLVDAEWMERKHIPSFETYLSNATVSVGMQDLLLSSIFFCGESISKHLMQEIKNSRCLQLTCLIARLCNDIGTYQFEREKGEVASSITCYMRENRGITESQAIEHLQGIIDESWKELTEEFLTPSQIPRSIKRLMFETARIFQFIYPKKDNFKDPSKAMASLIQNVLYKPAE
The following text describes a protein:
Function:
Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding.
Sequence:
MKQLNRTQNEQNLVHSAIAQIRKQYQNAESEEVPQDLLENKYYKEYEPLDKLELLADQHIKYCTKRLLNIGYSILYLDVGQPWCIYWPLNALSILQEDVSKYEEKILQYLQQCKIGGFGGGPYQFEHLAPTYSSLLTLFILGSPASLGLIDRKGLENFFWSIQDPREKGSYLMHINGEADMRAVYIVVIMVSINICKYISPKLLDGCAEYIASCQTYEGGIGAVRYSEAHGGYAYCGYAALVCMGKAHYIDQEKLLNWLVSRQMENEGGFNGRTNKVVDSCYSFWQGAIFNLLMLSGYVNEQLMDVQELKTYIQMCQNPAGGIFDKPSKNPDTYHTCYGLSGYSLSDSNFQNPIYNVPNKCIDFVQKFFQ
The following text describes a protein:
Function:
Involved in the export of cellular mRNA to the cytoplasm. Plays a role in the nuclear retention of unspliced mRNAs.
Subcellular Localization:
Nucleus. Note=Not localized at the nuclear rim.
Domain:
The RNA-binding domain is a non-canonical RNP-type domain.
Sequence:
MRGQNRRGYRNIEGRLSLSSHSSHSSPRQTHVTNLRPAEIKVVQDVVDGCYVATDDVLNLSNFSKNTEFVERDMLMCLTKTRVMSVVLQHIGYKYPRISGISFSNNRLCHLDHLSSLSSISKFLKFLDLSHNQISSGEELKKLGTIPVETVFFEGNPVCEKFVQCAEYANFIQKTFPKCSNLDGMEVEPKPDHNRIEQIIPFRNGYYGSDEVRTLVEEFIITYYKIYDGADGQQTRKQLLDAYDTNNSTFTHTVVCLWDPIKFVMYPDSESYRMYLRTSHNVLNQEYFAANRASRISHGAMDIVVALSRLPATIHLMDTFVVDVFLVSATLLGFTLHGTFRDGPSAIKPENTEEHDNYFTRTFMVAPRGEGKVAIVSDQLFISSMSKRRGDQYRMLVETATDIDQ
The following text describes a protein:
Function:
Antimicrobial peptide that renders both the outer and inner membrane of bacteria permeable to hydrophobic substances of low molecular mass.
Subcellular Localization:
Secreted.
Sequence:
MFTLKKSLLLLFFLGTINLSLCEEERNAEEERRDEPDERDVQVEKRLSPNLLKSLLGK
The following text describes a protein:
Function:
Regulatory subunit which plays a role in the allosteric regulation of the enzyme catalyzing the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers.
Subcellular Localization:
Mitochondrion.
Sequence:
FSQQTIPPSAKYGGILTVTMSPGDGDGPELMLTVXXXXXSACVPVDFEEVVVSSNADEEDIRTSLDLYANVIHCKLGDGLFLQCCKNIANPTATLLASCMMLDHLK
The following text describes a protein:
Function:
Transcription factor. Acts as a transcriptional activator by binding to promoter regions of target genes, such as Rec8, Mxd4 and Ddit4. Plays a role in natural killer (NK) cell maintenance and immunity. May play a role in the process of ciliogenesis in the neural tube and neural tube closure (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MAEEQQQPPPQQLDAPQQLPLSAPNPGVALPALVPGLPGTEANALQHKIKNSICKTVQSKVDCILQEVEKFTDLEKLYLYLQLPSGLSSAEKSDQNAMSSSRAQQMHAFSWIRNTLEEHPETSLPKQEVYDEYKSYCDNLGYHPLSAADFGKIMKNVFPNMKARRLGTRGKSKYCYSGLRKKAFVHMPTLPNLDFHKTGDGLEGVEPSGQLQNIDEEVISSACRLVCEWAQKVLSQPFDTVLELAHFLVKSHYIGTKSMAALTVMAAAPAGLKGIPQPSAFIPTAESNSFQPQVKTLPSPIDAKQQLQRKIQKKQQEQKLQSPLPGESSAKKPEGTTANGVANLPNGNPAILSPQPIGIVVAAVPSPIPVQRTRQLVTSPSPMNSPDGKVLPLNVQVVTQHMQSVKQTPKTPQNVPASPGGDRSARHRYPQILPKPANTSALTIRSPTTVLFTSSPIKTAVVPASHMSSLNVVKMTTISLTPSNSNAPLKHSASVSSATGTTEESRIVPQIKNGSVVSLQSPGSRASSTGGTSAVEVKMEPEGSSDEHPLQCQENSEETKAPLTTSSALWGQKSNTDGTVPKPSNEGVTEVKTTKVCDQRTKCKNRCNEILSGISAGNNQSTVTLSVATQNLPFTSTSSPSNGDSVNKDPKICTKSPRKRLSATLQESQVPPVKKPIVEQLSAVTIEGQKPGTVKKDQKVPHSGKTESSTAGAQIPNKVSISVSSQIIEDQPVNPALVTSEPVLEQQTTPSSSPDVKVKLEGSVFLLDRESKSDGSFNRNEWQQVTKDSDFIAASCEHQQDISVMTIAEHPDIHDLEKSVWELEGMPQDTYSQQLHSQIPESSLNEIQAQSSDQLPLQSELKEFESSVSQTNESYFPFDDELTQDSIVEELVLMEQQMSMNNSHSYGNCLGMSLQNQSVTPGAPMSSHASSTHFYHPIHSNGTPIHTPTPTPTPTPTPTPTPTPTSEMIAGSQSLSRESPCSRLAQTTPVDSALGSSRHTPIGTPHSNCSSSVPPSPVECRNPFAFTPISSSMAYHDASIVSSSPVKPMQRPMATHPDKTKLEWMNNGYGGVGNSSVSGHGILPSYQELVEDRFRKPHAFAVPGQSYQSQSRHHDTHFGRLTPVSPVQHQGATVNTNKQEGFAVPAPLDNKGTNSSAGSNFRCRSVSPAVHRQRNLSGSTLYPVSNIPRSNVTPFGSPVTPEVHVFTNVHTDACANNIAQRSQSVPLTVMMQTAFPNALQKQTNSKKITNVLLSKLDSDNDDSVRGLGINNVPSNYTARMNLTQILETSPVFPSANSQNMIDSSTSVYEFQTPSYLTKSNSTDQISFSPGDNQAQSEIGEQQLDFNSTVKDLLSGDNLQTSQQLVGQVASDLTNTASDFSSDIRLSSDLSGSINDLNTLDPNLLFDPGRQQGQDDEATLEELKNDPLFQQICSESMNSMTSSGFEWIESKDHPTVEMLG
The following text describes a protein:
Function:
An odorant receptor which affects chemotaxis to the volatile odorant diacetyl. Specifies AWA neuronal cell fate via the odr-7 pathway.
Subcellular Localization:
Cell projection, cilium membrane; Multi-pass membrane protein.
Sequence:
MLFAAIKFTIQLVSFIVSIIFNFTLIYLILTRSPKKMGTYKYLLIYFCCFSILYSILDIIVEPFIQSHGSCFFMMMNLGSWKSYPEVGFLFVTILCGCFAVSITTISIQFVFRYFALERKGRITYFRGHYLIVWFIVPLVSASIWITQLWVFQHPNSVTSAYLSETVFVNYGMNISDITYTGSLFYPPDEHGVPHLDLMQLFSYLGFCVTMGTTFSTVVVFGMKSYKLVCELPQLGESEYTYKLQSQLFRALVVQAFIPITFLFLPIGILFTAPLLHFDIEPASFLVTIFYSIYPAVDPLPIIFIVVDYRDGLVELVGHFLCKKNNQVNTSYTDQQVASIS
The following text describes a protein:
Function:
F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
Sequence:
MAEEWAYEEASDEEKLQIAQRFLLASPPGQIHEVLRDVAKLVPARVLPDAALRGALHAYNVKNFLPVDVPDADYKILICEEGEVDAAHYVDPIGNRVLGFDHIKQQIVAEDVAEIPEARVSEFEKERQEVQKTLQSYLQFEYMHGGTAGVYVVGTKIVVNLCTERINLRNFWGGRWKSRWEVDLTENPAKVKGSIQLHVHYFENGNLQLQSSKEVEEEVAIQRPNGLGDAILRVMKEAEDDLQTNLEDMYINMSEETFKEMRRVMPVTQTKMEWSLHAHRTAKDLGRK
The following text describes a protein:
Function:
Functions as a guanine exchange factor (GEF) for RAB26 and thus regulates autophagy of synaptic vesicles in axon terminal of motoneurons (By similarity). Involved in the control of neuronal cell differentiation. Plays a role in angiogenesis through regulation of endothelial cells chemotaxis. Also affects the migration, adhesion, and matrix/bone degradation in macrophages and osteoclasts.
Subcellular Localization:
Cytoplasm. Cytoplasm, perinuclear region. Cell membrane. Cell junction. Cell projection, lamellipodium. Note=Predominantly cytoplasmic, however when endothelial cells are stimulated with lysophosphatidic acid, PLEKHG5 is found in perinuclear regions and at the cell membrane. Localizes at cell-cell junctions in quiescent endothelial cells, and relocalizes to cytoplasmic vesicle and the leading edge of lamellipodia in migrating endothelial cells.
Sequence:
MHYDGHVRFDLPPQGSVLARNVSTRSCPPRTSPAVDLEEEEEESSVDGKGDRKSTGLKLSKKKARRRHTDDPSKECFTLKFDLNVDIETEIVPAMKKKSLGEVLLPVFERKGIALGKVDIYLDQSNTPLSLTFEAYRFGGHYLRVKAPAKPGDEGKVEQGMKDSKSLSLPILRPAGTGPPALERVDAQSRRESLDILAPGRRRKNMSEFLGEASIPGQEPPTPSSCSLPSGSSGSTNTGDSWKNRAASRFSGFFSSGPSTSAFGREVDKMEQLEGKLHTYSLFGLPRLPRGLRFDHDSWEEEYDEDEDEDNACLRLEDSWRELIDGHEKLTRRQCHQQEAVWELLHTEASYIRKLRVIINLFLCCLLNLQESGLLCEVEAERLFSNIPEIAQLHRRLWASVMAPVLEKARRTRALLQPGDFLKGFKMFGSLFKPYIRYCMEEEGCMEYMRGLLRDNDLFRAYITWAEKHPQCQRLKLSDMLAKPHQRLTKYPLLLKSVLRKTEEPRAKEAVVAMIGSVERFIHHVNACMRQRQERQRLAAVVSRIDAYEVVESSSDEVDKLLKEFLHLDLTAPIPGASPEETRQLLLEGSLRMKEGKDSKMDVYCFLFTDLLLVTKAVKKAERTRVIRPPLLVDKIVCRELRDPGSFLLIYLNEFHSAVGAYTFQASGQALCRGWVDTIYNAQNQLQQLRAQEPPGSQQPLQSLEEEEDEQEEEEEEEEEEEEGEDSGTSAASSPTIMRKSSGSPDSQHCASDGSTETLAMVVVEPGDTLSSPEFDSGPFSSQSDETSLSTTASSATPTSELLPLGPVDGRSCSMDSAYGTLSPTSLQDFVAPGPMAELVPRAPESPRVPSPPPSPRLRRRTPVQLLSCPPHLLKSKSEASLLQLLAGAGTHGTPSAPSRSLSELCLAVPAPGIRTQGSPQEAGPSWDCRGAPSPGSGPGLVGCLAGEPAGSHRKRCGDLPSGASPRVQPEPPPGVSAQHRKLTLAQLYRIRTTLLLNSTLTASEV
The following text describes a protein:
Function:
May act as a specific coactivator for the mammalian TEFs.
Subcellular Localization:
Chromosome. Nucleus.
Sequence:
MSGDHDDFGEQLRLQQLYGEAKRGGPQDGDPYTFVDPADGSAYEWDRDKKAWFPKITEDFLATYHANYGFPADGSSASDEKTETKADGDAKTSQKPVDKKTAQHTEPKPKGEKRKPEAGWFHVEEDRNTNVYVTGLPPDITKDEFVQVMSKCGIIMRDPQTEEYKIKLYKDKQGNLKGDGLCCYLKRESVDLALRLLDDDEIRGYKLHVEVAKFQLKGEYDASKKRKKCKDYRKKMSLQQKQLDWRPEKKAGASRMRHERVIIIRNMFHPKDFEEDPLVLNEIREDLRTECEKFGQVKKVLLFDRHPDGVASVSYKEADEADLCIQALNGRWFGGRQLSVEAWDGVTDYQVEETSREREERLKVWGSFLEDPNVNKEKSISDSNSASGSMELPEGKQPSKDNSIPKSGVPVKFPEMEGVKKDSIRLNKNKQQPIKTEWNSQCVLFTYFQGDINSVVDEHFSRALSNTKAPQDLSTKCRREDGILKNDNHMSSSQWNFSSQWTKPQQVSPVNSLAGCGLNLPAAAATAAMDHYPVPVMRNQPDHPGDLWHFQSMGNPSSSGPRYPLPFPELHMAQGPASEGKYGSLLSLLQQERCLGCSQESEMKQEPGSSCSTGTARLASVTQNPDGGKSPESASCDLANGSWYLNLQS
The following text describes a protein:
Function:
Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.
Subcellular Localization:
Secreted, extracellular space.
Sequence:
DSPGGASDTQKQHXVNSXXXKXY
The following text describes a protein:
Function:
Exhibits fusogenic activity. Mediates cell-cell fusion in mammalian cells (bilateral fusion).
Subcellular Localization:
Cell surface. Cell membrane; Multi-pass membrane protein.
Domain:
The extracellular N-terminus has 4 domains; the first 3 are structurally similar to fusogens from plants, C.elegans and viruses, while the fourth domain is unique to archaea. Domains I and II are discontinuous. The fusion loop in domain II is stabilized by a Ca(2+) ion so that it protrudes from the molecule.
Sequence:
MRAVSDFLKNKWVAVPAVALLILSLGFLAQNYITGSFVSGDQIEYTSNSEFFDGEVFVINYIGDRTTDKIHAEIPASELASAADGEVTKELTIDITSQETYARYSTTSTSLSRIYAFKAINSEVFTDTSSSEVESRKQSWAEQNCYDIDGDSEIEQGDDYTQRFWVDGAIADYYNAQVYCVRENGYYGNIAELSSPDKEFEAEVEVKADGETPQSTTLSNSDLGQGRCDNIGEYVRACWTGLNPTGEGVPEPYNVYAIHSNTFSPEWRVISAERYSSYNSYVENNLYSQIEAWKEGSLSQEEVVSTANDQAAQAAQRVSSGSFTDYQVEDSSYENGQIRLNPSYDIAWPEFTFYVDGADYISVEKPVGEPRIVNVEGDEFGEKQSGTVTAEVENTASYEGSFSARVSKCSDSFGYDSLQETKTVGPGETVSFDFRVSFTSDSFDQKTVSGSCEIVVSDTGDSSNSDTAVVDVEATQSNECTPNEEFVRTINSTHSRILECSSDGLTTTEVDVCGDGEEAAFRDSSWTCVSDGTLPGGGDGSGGSGGGGDTDDCVVFAVGDLEIEDPFCADGPLEMLSKMFHLVAGTAVAFFTGSLGYRAGRWVDGEYQIKGGFDPLKSRSVSRAKRGRFLIGLIAELVSFLLGFYVILLVPIWAQLMVILGYVLFKYYTPF
The following text describes a protein:
Function:
Required for 20S pre-rRNA processing.
Miscellaneous:
MISCELLANEOUS: Present with 13400 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSTQYIDETAFVQAEQGKTNLMFSDEKQQARFELGVSMVIYKWDALDVAVENSWGGPDSAEKRDWITGIVVDLFKNEKVVDAALIEETLLYAMIDEFETNVEDDSALPIAVEVINIYNDCFNLNYNKVEKLYLEWQEKQRTKKSKRVVHIEGDDDEDDEDVEDYDDEDEDEEMDEVVPDLVSSKPEPIVDEDGFELVQPKGRRKH
The following text describes a protein:
Function:
Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
Sequence:
MSILVTRPSPAGEELVSRLRTLGQVAWHFPLIEFSPGQQLPQLADQLAALGESDLLFALSQHAVAFAQSQLHQQDRKWPRLPDYFAIGRTTALALHTVSGQKILYPQDREISEVLLQLPELQNIAGKRALILRGNGGRELIGDTLTARGAEVTFCECYQRCAIHYDGAEEAMRWQAREVTMVVVTSGEMLQQLWSLIPQWYREHWLLHCRLLVVSERLAKLARELGWQDIKVADNADNDALLRALQ
The following text describes a protein:
Function:
Involved in EGFR signaling.
Sequence:
MADVSVDQSKLPGVKEVCRDFAVLEDHTLAHSLQEQEIEHHLASNIQRNRLVQHDLQVAKQLQEEDLKAQAQLQKRYKALEQHDCEIAQEIQEKLTIEAERRRIQEKKDEDIARLLQEKELQEEKKRKKHTPEFSGGSASGDNYYYEDGGMKSRGINEAVSAPARVSHRDQEWYDAEIARKLQEEELLATHMDIRAAQVAQDEEIARLLMAEEKKAYKKAKDREKSSLDKRKHDYDCKSKAKSAHSKSKEGDETQRAKIDRPSRPPPPAAMAPEDVDPTHFTNQHSNTRHFSKSESSHKGFHNKQ
The following text describes a protein:
Function:
Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Subcellular Localization:
Chromosome, telomere.
Sequence:
MSDSNNTPKEAAAGRPGLRFGTYTPRGVTPRGDTLSYAQNSPVFNPDDSGTDGTNGTNDTNGTNASNATILAVAPNDTTASDTDSDGVGPTANLDINPQRMPADTRRLDKIIPLLIQPESAVSERFPLLHRVIAGRLKTSLDLRGGRRVSRCSHKYGLGAATLNQTKKHRPDSHTFQTKVARSIGRSRGGRATANARIQGMCRKLRRKVRLSGCIGSGGFGTVFLAHKNTPHGQANFAIKINEHNTIAAMDDGSHVAEMMFFEEGGKVRYIPCEAMIMLLLTRSPRFPTLHSVYTEKDKVAIVMSACIDYDTLQLSNGMQETDQVWAIEGGHLRTRGKEPRLNELQAGKVSTQLLEAIAYLRDMNITYDDVSYRNYLVGENLETQLIDFGIMGFGLDDRDFLENSHTYVFWQEYLLSPEVAIELLKPQWRLHVRNTTRGIAQVKCRNDTRQTSLWNYAVEVFCLLHGYAPWEDPEWDDEIRTIGEFACRLINGRWQEPPELYDEGPRWDAAYARRKRMINEELAVREDLSQDCVDALRTMLQRDPKQRPRLSELISFPWFGQWAYHGDKLFRRPDIPREYFV
The following text describes a protein:
Function:
Fatty acid conjugase converting 18:2(9Z, 12Z) to calendic acid 18:3(8E, 10E, 12Z). Converts alpha-linolenic acid (18:3(9Z, 12Z, 15Z)) into 18:4(8E, 10E, 12Z, 15Z). Also has weak activity on the mono-unsaturates 16:1(9Z) and 18:1(9Z) producing two conjugated double bonds at delta(8) and delta(10) position (By similarity).
Subcellular Localization:
Microsome membrane; Multi-pass membrane protein.
Domain:
The histidine box domains may contain the active site and/or be involved in metal ion binding.
Sequence:
MGKAASAKKVLERVPISKPPFEYNDLKKAVPPHCFSRPLSRSLYFLFHDIIVTCILFYVASNYIHMLPRFLSCIVWPVYWISQGVFLGRLWMIGHECGHHSFSNYRWVDDTVGFLIHTATLTPYFSFKYSHRNHHAHTNSMEYDEVHIPKRKSEALYFEFLGNNPIGLMITMLCKLTFGYAAYIMFNYTGKKHKSGGLASHFYPQSPLFNDSERNHVLFSDIGICIVLYACYRIVTVTGAMPAFYVYGIPWVIMSAILFAATYLQHTHPSIPHYDTTEWNWLRGALSTIDRDLGFFNMNKTHYHVIHHLFPVIPEYHAQEATEAIKPILGQYYKYDGTPFLKALWREMKECIYVESDEGQKKQGIYWFKNKT
The following text describes a protein:
Function:
Catalyzes the double cyclization reaction which converts lycopene to beta-carotene and neurosporene to beta-zeacarotene.
Subcellular Localization:
Plastid.
Sequence:
MATTALLLRAHHACRPPPAPQPGRAAIVCRATASAGQALRSLAPPPRPELLSLDLPRYDPARSRPVDLAVVGGGPAGLAVAQRVAEAGLSVVSIDPSPSLVWPNNYGVWVDEFEAMGLSDCLDTVWPSASVFIDDHTSKSLHRPYARVARRKLKSTMMDRCIAHGVRFHQAKVAKVVHNEASSLLICDDGVAVPATVVLDATGFSRCLVQYDKPYNPGYQVAYGILAEVDEHPFDIDKMLFMDWRDSHLPEGSAIKERNSRVPTFLYAMPFSPTRIFLEETSLVARPGLSMDDIQERMAARLRHLGIRIRSVEEDERCVIPMGGPLPVLPQRVVGIGGTAGMVHPSTGYMVARTLATAPIVADSIVRFLDTGNGGIAGDALAAEVWKELWPTDRRRQREFFCFGMDVLLKLDLQGTRRFFNAFFDLEPHYWHGFLSSRLFLPELLMFGLSLFAHASNTSKLEIMAKGTVPLAKMVGNLIQDKDR
The following text describes a protein:
Function:
Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER.
Subcellular Localization:
Endoplasmic reticulum lumen. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Sequence:
MAAAVPRAAFLSPLLPLLLGFLLLSAPHGGSGLHTKGALPLDTVTFYKVIPKSKFVLVKFDTQYPYGEKQDEFKRLAENSASSDDLLVAEVGISDYGDKLNMELSEKYKLDKESYPVFYLFRDGDFENPVPYTGAVKVGAIQRWLKGQGVYLGMPGCLPVYDALAGEFIRASGVEARQALLKQGQDNLSSVKETQKKWAEQYLKIMGKILDQGEDFPASEMTRIARLIEKNKMSDGKKEELQKSLNILTAFQKKGAEKEEL
The following text describes a protein:
Function:
Catalyzes the isomerization of L-lysine to (3R)-3-methyl-D-ornithine via a radical-based mechanism, a step in the biosynthesis pathway of pyrrolysine (Probable). Also catalyzes the reverse reaction in vitro, converting (3R)-3-methyl-D-ornithine into L-lysine.
Sequence:
MIQKMALDEFDSLGDKVIEGYQLTDNDLRTLLSLESKEGLERLYSAARKVRDHYFGNRVFLNCFIYFSTYCKNQCSFCYYNCRNEINRYRLTMEEIKETCKTLKGAGFHMVDLTMGEDPYYYEDPNRFVELVQIVKEELGLPIMISPGLMDNATLLKAREKGANFLALYQETYDTELYRKLRVGQSFDGRVNARRFAKQQGYCVEDGILTGVGNDIESTILSLRGMSTNDPDMVRVMTFLPQEGTPLEGFRDKSNLSELKIISVLRLMFPKRLIPASLDLEGIDGMVLRLNAGANIVTSILPPDSQLEGVANYDRDLEERDRDIKSVVRRLEIMGMKPARQADFEAVLGC
The following text describes a protein:
Function:
RNA-binding protein involved in the regulation of flowering time. Acts as a repressor of the activity of SOC1, a transcriptional activator of flowering time. Binds to the 3'-UTR of SOC1 mRNA in the cytoplasm and participates in SOC1 mRNA decay, mediated by the distal region of the SOC1 3'-UTR.
Subcellular Localization:
Cytoplasm.
Sequence:
MAEETMENEERVKLFVGQVPKHMTEIQLLTLFREFSIVNEVNIIKEKTTRAPRGCCFLTCPTREDADKVINSFHNKKTLPGASSPLQVKYADGELERLEHKLFVGMLPKNVSETEVQSLFSEYGTIKDLQILRGSLQTSKGCLFLKYESKEQAVAAMEALNGRHIMEGANVPLIVKWADTEKERQARRLLKVQSHVSRLDPQNPSMFGALPMSYVPPYNGYGYHVPGTYGYMLPPIQTQHAFHNVISPNQGNGRALQGTALTESVPPRLAPRRNFPTALGNYGYHGLQYPMAFPRGMIPPRLPLTTVSPGISNNGTSIPSSLQTEGPAGANLFIYNIPREFEDQELAATFQPFGKVLSAKVFVDKATGISKCFGFISYDSQAAAQNAINTMNGCQLSGKKLKVQLKRDNGQQQQQQQSKNPLFNGLLNS
The following text describes a protein:
Function:
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Sequence:
MEKLNIYTFGKITLFLDVINKREDGYHNVKILLHNVDFWDFMQISLLPYPHFILESNLPIPSEENLVYKAYKKFIEITGEKVGAKVFLFKKIPTQAGLGGGSSNAAGTIWGLNLLTNLNLPLRDMAKIGETLGSDIPFFFYGGSAIAEGKGEIIKKITHQNFKFILIFPPYGISTKEIYSKIKKEDLNIHIDFENILLNFERGILLEPYNFFEYIVFKRYPELKKIKESISPITYVALTGTGSTMFVVIKNDSEIKEIIKKLEEYLEKGYKIKLVKSSPFGIKILKIKGVF