lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
May participate in a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MDPEKRGYKFQEFVAHDAEVRSLAIGKKSSRVFITGGSDRNVNLWAIGKQSPLLSLSGHTSSVEAVEFDTAEVLVLAGSSNGSIKLWDLEEAKVVRSLTGHRSSCTAVEFHPFGEFFASGSSDTDLKIWDIKKKGCLHTYKGHRGAIKSIRFTPDGRWIVTGGEDNIVKVWDLTAGKLLHDFKFHSGQIRCIDFHPQEFLLATGSADRTVKFWDLETFELIGSAGPEDTGVRSMVFHPDGKTLFCGLEESLKVFSWEPVRCHDAVDMRWNNLADLSIYEGKLLGCSYHERRVGVWVADISLIEPYALGVLPKAIFFAELVDSVDDNPVKPNGSTAKPIRAVATSHPKNMYKVQESGIAESRVRALHLTPGSTDKIKKDRSSSIPRRPDSSVKPSTPVRRMKPVDSPSTNLKTAERSFGQRDIQLLSRTGMTINSSTTKKAPPTESVAVKDIYTTSQAVSVPVVVPRDILEDKSAGSIHRGIGGRTAVPDDFYSPVHLRKRLPSGGTSDSVSSVKSMLAEPDVCSEGFSGLKFSFGLTPNDKKEESDGTNKGEIRQIAEKMDRIISFDHPVQSNDDKAAYESPCSTTGTARVKYVRGVAVPLGKTKSLVERFEKRESSSIDCSSPTGSCGDHTVKADSPPTSSAEASRTYERDLPTVDEMTTPIDLVRNHDEFINVVKSRLTKLEMMRHVFNLNGIKGAIAAVAKLPDIAVQADVVSTLKGKLGLFNLDIFSSLLPVLAGLLNSKTERHAIIALEMLLDLIKIFGPVIHSTLSASSPVGVDLQAEQRLQRCTRCFNHLQKIVQALQPLMMRSGQSAQLAQELNMSLQDLVVF
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).
Subcellular Localization:
Cytoplasm. Endoplasmic reticulum.
Sequence:
MANGADSGPEEALRRAFGDLNQALQADNPSKIVQCADQVLKLEADAVEAVQCKVVALAQLNQYDQAIKTLASSQHRSQFAYEEAYCLYASRQYAQALKLIDGALQSAEGAQRLRFLELRAQTLYRSEASAASADAYKQLLSEADDGRDEERRTNYLAALVEAEGSAGHSSTPEDVAQSMALLECQKAVALQMKGHTAEALDIYKRIVRERNNLGVVAVAANNIVSIHQGSDVFDSKKRIKAAANPDVLAKLNTKQRQNIELNQALLLLYSNTLDACYTSCAELHERYPKSRTILWIHVAALLRDKSVADKPAAVRVRFSALAEKYDQSTDLVLAEAQAQLEAGHRDAASKLLENNAQLASSPAILGYLIASARQHAPESVSGLLERAVKLWSARQEQGDAAEQVLVALLRALSAKHAQQHEDEAAVDCLRRAVQIDDENAGLLAEFVLALAKTDVEAAEQYAEKLPSADVAGDDEQLDVDALEEAAYLRVSKFRARREAPEARGPQASQADVEAANATTSAVRTKHKRKRRGPLPKNYDPNRQPDPERWLKKYERSSYAGRRRRRVKDNLAKGSQGAASISQAEAERLDASLRAPPPTEPVQNKKVAAAKKKGKKGGKRR
The following text describes a protein:
Function:
Involved in inducible protoporphyrin IX influx and heme efflux.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSTTDSGFVLYHYTPSKAAAIVFVVLFIIMTVIFAVQTLYAARKSSKALKNNPFESSDDKVDSLEDAEYKQLKITPTVFAFIPFFTGCIMEAVGYIGRALSSSNPERTTPYIIQSVLLLVAPALIAATIYMIFGRLLHVMRCQSLILISARFGTTFFVVGDVFSFFLQAAGGGLMSKAGSTKTGSGLITAGLFVQVIFFGFFIINEIRFTVNVKRRCLFYEDISRKWIFVNATLLLSSMLILLRSIVRIVEFIQGFNGYIISHEYFIYVFDAVPMLLVIIAFSVGSFFGNVFDVIKECQTLSN
The following text describes a protein:
Function:
Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. Exists in two complexes, either with EIF1 or with EIF4E (mutually exclusive). Together with EIF1, is required for leaky scanning, in particular for avoiding cap-proximal start codon. Together with EIF4E, antagonizes the scanning promoted by EIF1-EIF4G1 and locates the start codon (through a TISU element) without scanning. As a member of the eIF4F complex, required for endoplasmic reticulum stress-induced ATF4 mRNA translation.
Miscellaneous:
MISCELLANEOUS: [Isoform B]: Produced by alternative initiation at Met-41 of isoform A; MISCELLANEOUS: [Isoform C]: Produced by alternative initiation at Met-88 of isoform A; MISCELLANEOUS: [Isoform D]: Produced by alternative initiation at Met-165 of isoform A; MISCELLANEOUS: [Isoform E]: Produced by alternative initiation at Met-197 of isoform A; MISCELLANEOUS: [Isoform 7]: Produced by alternative splicing; MISCELLANEOUS: [Isoform 8]: Produced by alternative splicing; MISCELLANEOUS: [Isoform 9]: Produced by alternative splicing.
Subcellular Localization:
Cytoplasm. Nucleus. Cytoplasm, Stress granule.
Sequence:
MNKAPQSTGPPPAPSPGLPQPAFPPGQTAPVVFSTPQATQMNTPSQPRQHFYPSRAQPPSSAASRVQSAAPARPGPAAHVYPAGSQVMMIPSQISYPASQGAYYIPGQGRSTYVVPTQQYPVQPGAPGFYPGASPTEFGTYAGAYYPAQGVQQFPTGVAPTPVLMNQPPQIAPKRERKTIRIRDPNQGGKDITEEIMSGARTASTPTPPQTGGGLEPQANGETPQVAVIVRPDDRSQGAIIADRPGLPGPEHSPSESQPSSPSPTPSPSPVLEPGSEPNLAVLSIPGDTMTTIQMSVEESTPISRETGEPYRLSPEPTPLAEPILEVEVTLSKPVPESEFSSSPLQAPTPLASHTVEIHEPNGMVPSEDLEPEVESSPELAPPPACPSESPVPIAPTAQPEELLNGAPSPPAVDLSPVSEPEEQAKEVTASMAPPTIPSATPATAPSATSPAQEEEMEEEEEEEEGEAGEAGEAESEKGGEELLPPESTPIPANLSQNLEAAAATQVAVSVPKRRRKIKELNKKEAVGDLLDAFKEANPAVPEVENQPPAGSNPGPESEGSGVPPRPEEADETWDSKEDKIHNAENIQPGEQKYEYKSDQWKPLNLEEKKRYDREFLLGFQFIFASMQKPEGLPHISDVVLDKANKTPLRPLDPTRLQGINCGPDFTPSFANLGRTTLSTRGPPRGGPGGELPRGPAGLGPRRSQQGPRKEPRKIIATVLMTEDIKLNKAEKAWKPSSKRTAADKDRGEEDADGSKTQDLFRRVRSILNKLTPQMFQQLMKQVTQLAIDTEERLKGVIDLIFEKAISEPNFSVAYANMCRCLMALKVPTTEKPTVTVNFRKLLLNRCQKEFEKDKDDDEVFEKKQKEMDEAATAEERGRLKEELEEARDIARRRSLGNIKFIGELFKLKMLTEAIMHDCVVKLLKNHDEESLECLCRLLTTIGKDLDFEKAKPRMDQYFNQMEKIIKEKKTSSRIRFMLQDVLDLRGSNWVPRRGDQGPKTIDQIHKEAEMEEHREHIKVQQLMAKGSDKRRGGPPGPPISRGLPLVDDGGWNTVPISKGSRPIDTSRLTKITKPGSIDSNNQLFAPGGRLSWGKGSSGGSGAKPSDAASEAARPATSTLNRFSALQQAVPTESTDNRRVVQRSSLSRERGEKAGDRGDRLERSERGGDRGDRLDRARTPATKRSFSKEVEERSRERPSQPEGLRKAASLTEDRDRGRDAVKREAALPPVSPLKAALSEEELEKKSKAIIEEYLHLNDMKEAVQCVQELASPSLLFIFVRHGVESTLERSAIAREHMGQLLHQLLCAGHLSTAQYYQGLYEILELAEDMEIDIPHVWLYLAELVTPILQEGGVPMGELFREITKPLRPLGKAASLLLEILGLLCKSMGPKKVGTLWREAGLSWKEFLPEGQDIGAFVAEQKVEYTLGEESEAPGQRALPSEELNRQLEKLLKEGSSNQRVFDWIEANLSEQQIVSNTLVRALMTAVCYSAIIFETPLRVDVAVLKARAKLLQKYLCDEQKELQALYALQALVVTLEQPPNLLRMFFDALYDEDVVKEDAFYSWESSKDPAEQQGKGVALKSVTAFFKWLREAEEESDHN
The following text describes a protein:
Function:
Probable S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. May methylate the carboxyl group of leucine residues to form alpha-leucine ester residues (By similarity).
Sequence:
MNGVTNDKGHSDVTNTPESGISTPKKKNPKSDKPVKVKNPNNAASKAYTVDLKIQGTNNSSIVSKRSVERLYKEKHDLEFFRHFVKKPQRRSPIINRGYWTRMEAMGYCISAALAEKAPKHVIVNLGCGYDPYPFQHLHKHGLTENLIFVDVDYPDLMQIKVDTIRRSDELTKLVGEEKPAAEIKDKSVLMQTGNYIALSCDLRDLEKFEFIFRNLDLIVEGDNNPLILFTAEVSVTYMFQKDADNLLQWCASLPNSRFALLEQIIPAGTEHPFAKTMLAHFDSLQTTLWSVKKYPSIPAQYERFTCLGWKEVSGISLAQFWDSYVPDEKKEFVENVEAFDEWEEFLLFLNHYSIIYGGADIFQNSKSEYPEHEEFVLQCEKPTSEAHRIGAAACSFQNGVILNGGQAQNRESTSLLLSLDSTDEFIVDKNNMIARQYHSLSEIEPGVVLLAGGRSSPTKKFSDCHILKNGLWKPTFDLPEGRFRHCMQGTLLFGGSESKDQWLHFSPTAGWKALKCDFHYLTPYGATLIMKSPIEGILLGGMDAKGNLGKEVYSVTISEGETVVLSLIPMKSPLIYARYGAQGVYHGNRYLLVGGVSYDILFNEHNQVVELDIKKGNTIPVKLPFESYPLLVSHSVNIVRNCLVVAGGGAVCFSFGVFHSDPEVVGNRELKVIKEQRPSEEVKTEINSTVISVEEGTLESFPAAYVNATPTIFRNCDIGPSSELWKSHDYLKSNIGEDTKVSVHIADNKNLNFQSKNFSYQTLQFGELMKLISDIEADSESSKSAYLRSLSLDNPKSEATDLCKDFPGIARDFKLPKEMADFIGNKVFSTPLRISSSKTQIWLHYDVTANVLCQVTGSKRVRMYHPRDVVHLGFPAGESSSKIPNIFVHESCAQAYEVVMNPGDILFIPPMWLHAVEPQTESISVNCFWKDLDGNKYSKTKDIYGNKDLASYESGREGIKKIADKFAGLPADIKEFYLRRLAEELKQM
The following text describes a protein:
Function:
DNA-binding global transcriptional regulator which is involved in the adaptive response to starvation and acts by directly or indirectly controlling the expression of numerous genes in response to nutrient availability. During rapid exponential growth, CodY is highly active and represses genes whose products allow adaptation to nutrient depletion.
Subcellular Localization:
Cytoplasm.
Sequence:
MSSLLDKTRMLNRILQKSGTEPVDFEDICDLLSDVLACNVYIISRKGKILGSKFYSGFECDEVREVVLKENRFPDFYNNKLLNVNETLSNSPNHDKCVFDNLKDCSINNKLSTIVPINGNRERLGTLLLARFDKEFTDEDLVLAEYSATIIGLEILRSKQDQIEEEARKKAVVQLAIGTLSYSELEAVEHIFNELDGTEGLLVASKIADKVGITRSVIVNALRKFESAGVIESRSLGMKGTHIRILNDKLLEELKKIK
The following text describes a protein:
Function:
Methyltransferase; part of the gene cluster that mediates the biosynthesis of psilocybin, a psychotropic tryptamine-derived natural product. The first step in the pathway is the decarboxylation of L-tryptophan to tryptamine by the decarboxylase psiD. PsiD does not decarboxylate phenylalanine, tyrosine, or 5-hydroxy- L -tryptophan (5-HTP). 4-hydroxy-L-tryptophan is accepted as substrate by psiD as well. The cytochrome P450 monooxygenase psiH then converts tryptamine to 4-hydroxytryptamine. The kinase psiK catalyzes the 4-O-phosphorylation step by converting 4-hydroxytryptamine into norbaeocystin. The methyltransferase psiM then catalyzes iterative methyl transfer to the amino group of norbaeocystin to yield psilocybin via a monomethylated intermediate, baeocystin. 4-hydroxy-6-methyl-l-tryptophancan also be converted the decarboxylase PsiD, kinase PsiK, and methyltransferase PsiM into respectively 6-methyl-norbaeocystin, 6-methylbaeocystin, and 6-methylpsilocybin (By similarity).
Domain:
The conserved NPPF motif is required for catalysis and represent the basis of substrate specificity toward norbaeocystin; Residue Asn-247 is essential to allow enough space in the active site for multiple methylations while also participating in a network of hydrogen bonds that stabilizes secondary structure elements in the immediate vicinity of the active site for optimal methylation of norbaeocystin.
Sequence:
MHIRNPYRDGVDYQALAEAFPALKPHVTVNSDNTTSIDFAVPEAQRLYTAALLHRDFGLTITLPEDRLCPTVPNRLNYVLWVEDILKVTSDALGLPDNRQVKGIDIGTGASAIYPMLACSRFKTWSMVATEVDQKCIDTARLNVIANNLQERLAIIATSVDGPILVPLLQANSDFEYDFTMCNPPFYDGASDMQTSDAAKGFGFGVNAPHTGTVLEMATEGGESAFVAQMVRESLNLQTRCRWFTSNLGKLKSLYEIVGLLREHQISNYAINEYVQGATRRYAIAWSFIDVRLPDHLSRPSNPDLSSLF
The following text describes a protein:
Function:
Probable molecular chaperone assisting protein biosynthesis and transport in the endoplasmic reticulum. Required for the proper biosynthesis and transport of pulmonary surfactant-associated protein A/SP-A, pulmonary surfactant-associated protein D/SP-D and the lipid transporter ABCA3. By regulating both the proper expression and the degradation through the endoplasmic reticulum-associated protein degradation pathway of these proteins plays a crucial role in pulmonary surfactant homeostasis. Has an anti-fibrotic activity by negatively regulating the secretion of type I and type III collagens. This calcium-binding protein also transiently associates with immature PCSK6 and regulates its secretion.
Subcellular Localization:
Endoplasmic reticulum lumen.
Sequence:
MDLPFCACLLLLWQLPITTCHVHIHPNHYPDHYVDGEHDAEFDREILLGGKKEAEEYQKLSPEESKQRLMLLVKKIDVNGDGLLDRDELVDHMLESFNTYSVEEARDTFPTIDLDEDGKVSWEEYLQDTFGAEYSMEGDPAEDEMIQDDRRFFQQADEDQDGKLDEVEWLAFQHPEEYVRMHHFLVEEKLEESDWNEDGKIDFDEYLGDDEPDSSYSSEEEWRIVEREQFDEYDKDGDGVLEGEEVAAWVTPNHREAAEEEADHLLSMADTNKDEKLSAEEIMSDPDLFLQSDLTEQGELLHTIDHQEL
The following text describes a protein:
Function:
Probable non-functional open reading frame (ORF) of V region of the variable domain of immunoglobulin heavy chains. Non-functional ORF generally cannot participate in the synthesis of a productive immunoglobulin chain due to altered V-(D)-J or switch recombination and/or splicing site (at mRNA level) and/or conserved amino acid change (protein level). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular Localization:
Secreted. Cell membrane.
Sequence:
MLVCVLLYSFRLFGIQGEAQLTESGGDLVHLEGPLRLSCAASWFTFSIYEIHWVCQASGKGLEWVAVIWRGESHQYNADYVRGRLTTSRDNTKYMLYMQMISLRTQNMAAFNCAG
The following text describes a protein:
Function:
Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein; Cytoplasmic side.
Sequence:
MKKRNKGLVEQTTTEKNNFSRKTAWKVFWWVIILAVVIGVLAYIFSPRAATAVVESWKLNGGSNSTLTAKVSGFSNELTFKQINGSTYVTDTILQVSITFDGLNSPLTVTAHKTVNSNGNVIFNIANLSINQSNGQITVNSNGTMMNGGSSNNTKSIAGFETLGTFIAPDTRARDVLNGLFGLLPIIIFVVFFLLFWRSARGISAGGREEDNIFSIGKTQAKLAKSTVKFTNIAGLQEEKHELLEIVDYLKNPLKYAQMGARSPRGVILYGPPGTGKTLLAKAVAGEAGVPFFQSTGSGFEDMLVGVGAKRVRDLFNKAKKAAPCIIFIDEIDSVGSKRGRVELSSYSVVEQTLNQLLAEMDGFTSRTGVVVMAATNRLDVLDDALLRPGRFDRHIQINLPDIKEREGILKVHAENKNLSSKISLLDVAKRTPGFSGAQLENVINEATLLAVRDNRTTININDIDEAIDRVIAGPAKKSRVISDEDRKLVAYHEAGHALVGLHVHSNDEVQKITIIPRGQAGGYTLSTPKSGDLNLKRKSDLLAMIATAMGGRAAEEEIYGNLEITTGASSDFYKATNIARAMVTQLGMSKLGQVQYVPSQGTLPSNVKLYSEQTAKDIDNEINFIIEEQYKKAKTIIKSNRKELELLVEALLIAETILKSDIDFIHKNTKLPPEILLQKQEQQAKQKLNKSEVKPESETNS
The following text describes a protein:
Function:
The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MQPLFRCRQIQQVQHQSSRRFAINVAMFSLARCVALNASRQTRSLSLGCFPGTEMPFVPDVVFQDPRDSNLIPCFRVLDEEGEIVKGATDPQLSQDLCTQIYSQMIRLNTMDNIFYDAQRQGRISFYMTSYGEEAISFGSAAALRLGDMVFAQYREPGVLMWRGFSLQNFADQCFSNKDGHGKGCQMPVHYGSKNLNHQTISSPLATQLPQAAGAAYAFKLAKEDRISVCYFGEGAASEGDFHAALNFAATKDCPILFFCRNNGFAISTPTAEQFRGDGIASRGSGYGIPIMRVDGNDFLAVHEATRRAREFILKENRPVLVEAMSYRQGHHSTSDDSTQYRAVAEIKHWKETCDPIERTKRYLLKRGWLTEEQDRHMQDNERTNVLAALQQAETKEGPSLETMFEDVYDVKTPHLLEQEREMMEHVAKYPDHYTGEH
The following text describes a protein:
Function:
Essential for normal male fertility and for progressive motility of spermatozoa.
Subcellular Localization:
Cytoplasm, cytoskeleton, flagellum axoneme.
Sequence:
MESEGGGPLATSSCSGATFHVREPFVLPCRTKWCKDRMSSRPSTVRVFVRVKPTPNFAHEIIRFGEDNKTVDIHIKKDDRLGVVNNKRSDWSFKVDGLLHNASQDTVYDTVAKSVVSKALDGYNGTVMCYGQTGAGKTYTITGGTENYQLRGIIPRALQQVFKEIEGKSDQSITVRISYLEIYNETLYDLLSTVPDAPAPDTQMTIVDDAQGVIIKGLSLHLASNEEQALNLLFEGETNRMIGSHILNKNSSRSHCIFTIHVESHSRIISDAKYTISKINLVDLAGSERLGKTGSEEQVLKETTYINKSLSFLEQTIIALTDRSRDHIPFRQSKLTHALKDSLGGNCNTILVANIYGEVSQLSETLSTLRFASRMKCIPAESVVIEHYDPVRVARNLQKEIDHLRQELAVRDTLTNHARVSYEPFNESQIAEINAQVRRYLDGKVDEIDILNLRQIQEIFNQFKLILSQQEKAAEARLRQKYTLIDKTDFVTVTAAQKAGLLDADGLMVGEVDGHSFGIGVAPVSSKASSSLSARKPKSRKSKERSSPVSRKEGAGSPAPAKELEAFSPSKSNLLTASARELDLKETVIKEQPEVGSLDLQPAESTVKEERSLSSSPPPKPSAFEDFKAERGSELNRIFKENKAILADRKRKLKDVTQRINLIKKEMDDTSHTLNVAKVEREKQGEYINEEGQVIIDEQEFILIVRLKDLKKQYRADYEELQDLRAEVQYCQKLVDQCRQRLLTEFEAWYNESFVIPEDMQTLLKLGGSIRPGLIPANKLLELGEDEQERLERLQQELLMEVPGSLPFHNARSNVEKKYKYSRAAAQITPSKKKPSLITSTVKNKPPSMLSAA
The following text describes a protein:
Function:
Component of the mitochondrial inner membrane i-AAA protease supercomplex, which degrades misfolded mitochondrial proteins. Together with MGR1, functions in an adapter complex that targets substrates to the i-AAA protease for degradation. Required for growth of cells lacking the mitochondrial genome.
Miscellaneous:
MISCELLANEOUS: Present with 8970 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MLLQGMRLSQRLHKRHLFASKILTWTTNPAHIRHLHDIRPPASNFNTQESAPIPESPANSPTRPQMAPKPNLKKKNRSLMYSIIGVSIVGLYFWFKSNSRKQKLPLSAQKVWKEAIWQESDKMDFNYKEALRRYIEALDECDRSHVDLLSDDYTRIELKIAEMYEKLNMLEEAQNLYQELLSRFFEALNVPGKVDESERGEVLRKDLRILIKSLEINKDIESGKRKLLQHLLLAQEEILSKSPELKEFFENRKKKLSMVKDINRDPNDDFKTFVSEENIKFDEQGYMILDLEKNSSAWEPFKEEFFTARDLYTAYCLSSKDIAAALSCKITSVEWMVMADMPPGQILLSQANLGSLFYLQAEKLEADLNQLEQKKSKESNQELDMGTYIKAVRFVRKNRDLCLERAQKCYDSVIAFAKRNRKIRFHVKDQLDPSIAQSIALSTYGMGVLSLHEGVLAKAEKLFKDSITMAKETEFNELLAEAEKELEKTTVLKAAKKEGLN
The following text describes a protein:
Function:
Involved in heme d1 biosynthesis. Catalyzes the decarboxylation of siroheme into didecarboxysiroheme (By similarity).
Sequence:
MNPVEPLAAPQRQHLRYLLEQGLPLASRPYRVLAERIGAGEDEVLEQVRRWDEDGLFRRFGVILHHRALGYTANAMLVLDVADAEVDAVGRALAHETIVSLCYRRPRRLPMWPYNLFCMIHGRERGEVERQIEALLERHALRQTPHRWLFSLRAYKQCGGRYTAPPADLERRHG
The following text describes a protein:
Function:
Thought to be involved in DNA repair and/or mutagenesis. Its processivity is enhanced by the beta sliding clamp (dnaN) and clamp loader.
Sequence:
MAQAGFILTRHWRDTPQGTEVSFWLATDNGPLQVTLAPQESVAFIPADQVPRAQHILQGEQGFRLTPLALKDFHRQPVYGLYCRAHRQLMNYEKRLREGGVTVYEADVRPPERYLMERFITSPVWVEGDMHNGTIVNARLKPHPDYRPPLKWVSIDIETTRHGELYCIGLEGCGQRIVYMLGPENGDASSLDFELEYVASRPQLLEKLNAWFANYDPDVIIGWNVVQFDLRMLQKHAERYRLPLRLGRDNSELEWREHGFKNGVFFAQAKGRLIIDGIEALKSAFWNFSSFSLETVAQELLGEGKSIDNPWDRMDEIDRRFAEDKPALATYNLKDCELVTQIFHKTEIMPFLLERATVNGLPVDRHGGSVAAFGHLYFPRMHRAGYVAPNLGEVPPHASPGGYVMDSRPGLYDSVLVLDYKSLYPSIIRTFLIDPVGLVEGMAQPDPEHSTEGFLDAWFSREKHCLPEIVTNIWHGRDEAKRQGNKPLSQALKIIMNAFYGVLGTTACRFFDPRLASSITMRGHQIMRQTKALIEAQGYDVIYGDTDSTFVWLKGAHSEEEAAKIGRALVQHVNAWWAETLQKQRLTSALELEYETHFCRFLMPTIRGADTGSKKRYAGLIQEGDKQRMVFKGLETVRTDWTPLAQQFQQELYLRIFRNEPYQEYVRETIDKLMAGELDARLVYRKRLRRPLSEYQRNVPPHVRAARLADEENQKRGRPLQYQNRGTIKYVWTTNGPEPLDYQRSPLDYEHYLTRQLQPVAEGILPFIEDNFATLMTGQLGLF
The following text describes a protein:
Function:
Probable transcriptional factor. Binds to the promoter of the SQUAMOSA gene.
Subcellular Localization:
Nucleus.
Sequence:
MEYHWSSLINNSKSSSSSTTADCNTPTFNNGHHAWDSFNNAAGNFSRAAGAEQANWSYPLHYNNSVSYYSNPSAARQVVEAGAAAYQAVALREHEQEKMGGGGAAAANRCYQLDPHLTCLKLGKRQYFEDVMMAAAAPPPPAAAAKKGKPYYAVDGVQAAAVPRCQVEGCGVVLVDAKEYHRRHKVCEMHAKAPVVVVLGIQQRFCQQCSRFHRVAEFDETKRSCRRRLAGHNERRRKTSLNLDNQHHQFSHKLSLQGISRHDHDDGVINNNNIRGESCALSLLSSTNYYWTNFNTATSASRHLPETCSAALRDLIAENRASTSAFNKNHHLITNYPNNNNNHNQMDDYYNYKLNGSINNRPGSNPHGNGAGHVTLDLMEAQNSELGFMSTKERDEHQQECSELWKVPLGYR
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.
Sequence:
MSYNNSKEHNVKTTEKKARAAEVSAIRFIKAIRQKEIIIRRNKWRDDPRLTFENHKFKGYLGSGAWGDVLLAMNTETNKHYALKLLLNLTKISLRYIRNGHPHICNLEAFVQYKPGYGDEEYAMGLYFEYCDAGNLSILSKSFRTRGIKPPELFIWQVFYEMISGIAFLHNEHPDYNTKVENLGREAIFHDDLRSENVFLQWGSDKEDGYPHVKIGDFGTSFTEPLGGHISDPEFDPPTSQDEGWGPQPVKLKTEVWWVAAIVYELARTGVVLDNILKLSLQQSREQFRKIVPIDGHLSEGLDQVIRGTLTPELEKRPFSGEVYLNLKNAFEERVGLMYRKLRDWAGEMTLAHVFDEDMMKKVEEGGVEVELGLGLAGDINKNVI
The following text describes a protein:
Function:
Structural protein, a component of a tail fiber.
Subcellular Localization:
Virion.
Sequence:
MNKLVKRRFQAGLGSEIKRVYKEGQQINTLLLAQVIQVNYKYNTVDLLALQHKEVFQNSYANEGRFSARLPMEFGGRNIVGQPYGQVNPIAVGTVVLVGFINSDKDMPIVISVYNNNDVSKQLSRTQFSNSDPKDLELIGDMHQKFSLYPSLTYDSVDGEGGRVVTFSGKSFIAFDTKEVANSSTTDAGYGTKYEDLETSYYNNGDLIEPMKGRAPNVLFKHQGVLDDDGKPDLHDLLIHINPDGTYRTSMMNKEEDWRTLFEMTPDGRVKLRKQDSINIDGGIEISELGINNEGFVYLRNGDMDLEVRKDGIYSQGKLFTADVDLSDVYDKLNGLSIQIKETNGQLEIIANGVEEQNGKISELSTEITIVAGKVESKVTKTEVQDMIDSSFVDMSDAIKKAQEDADKANKVIADMSSDNRLTPSEKIDLLKEWDIIKNEYPSYLEQAETYEVDSKDYTAKYNSLELFVTPILADMESTSSVDGATLRKTFNSYYTARIALLNSISKKLKDGITEAMKKASQASLDATQAMADASQAKIDADNANKLISDIASDNKLTPSEKYQLKKEWDVIVKEYPTTIAQAEKYAVDTAEYTAKYKALELFVEPLFKDMDETSIVDGERLRATFSDYYASKIALLKEVTDSAKTELDAYGNKISVMETNITQTSEAITLLATRVQTVEDGVQSNKAQIEIQAEQISQKVTASEVKGIVDDSINNLTLGGTNLFVIKTQTAGLLNENDGTVGTAVDNSVVSDYIKVNQKTPYIATLYGNTGTNMIITDWYDKNRTFISGEAVADSGDFSKKYVSPENAVYARVSYKKANSVNIKFEAGTKATDYSPSWEDIKGDQTALEEYIKKVEEQAKKAQQDAENAKNDAENANNAIADMSNDNMLAPNEKKQILLQWEQIKTEYPINLDQATKFGVSSQQYTTAYNALDEYLKPILADMTTTSVVVGSTLRNTFNNYYDKRTTLLNRISDVAKNVADKAQETADTINDNLQNIGGYNYVGFSSGDNMLPRLMIKNVGYYTLGSSTTEFIDSMVAVKGDATTQPFDYTVGTSDKEIAGGGLADYRMKEVKEGQWLTASANVQVIDGGSARLAIYTLEGDNWVGSNSTPIQVSDGLKRVVAQRKVTGLTKGVLIRIESADTNVKEFRFGNVQLEVGIIPTPWKKSDIDIQEDINNVVQNIKTYTAWANDLQGLDFTREKVEGKTYMYVGTSMKDSDNYSDYTWRLTDEHIEGQINGKEGAWIYSPTAPTNPSQGLIWVDLSKVPNQPKRWVDSETGWVALTPEEVKDLPWGEDGTNLADWVAQAEQRISSDSIINTVLGSEDFTSVFDTKANTTDLDNLATYEDLDSIKEDYNRLIKEGINGIDFTPYVTNSELQQLKDSFNFSVQQAGGVNMLKNSLGFSGLDFWDGTVGKNLLPNSTWNLGFGRWGGASIASFEILPPEDDKPTSHILGSIGSRSSTKEIGNRPHPLKVNSGETYTISFDYKEEALAYDKDRPILVVRNYPDKDTDQWMEYSIEGWAVMANGSTTDLTVWRRFTKTFTIGTSGYLDILPKTIVESWTHRSFWRELKIEEGSQATTWVPNKEDGAFTGGIVETTQTEELANLGFGSGFVSSKRPSSSLTQSVELPEIGANLEYSLSFYMKVTTDNPVADFKCGIRVYEGDTLTYTLGIEDATQPIPLGFQQYKLVFTPTSTSTKIEMFVENGQEASVIISGIMYNIGNIPLKWQPYPSEIYNTNVKIDINGVTVKNNQTDGYTMITPQEFSGYSRIDGNIERIFTLNGQVTEVKMLKAEKRITMEPVSVFAMNTVTDTKRIRGWAFVPSFE
The following text describes a protein:
Function:
Catalyzes the dehydration of trans-3-hydroxy-L-proline (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Is likely involved in a degradation pathway that converts t3LHyp to L-proline. Can also catalyze the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp) in vitro. Displays no proline racemase activity.
Sequence:
MKVSKVYTTIDAHVAGEPLRIITGGVPEIKGDTQLERRAYCMEHLDHLREVLMYEPRGHHGMYGCIITPPASAHADFGVLFMHNEGWSTMCGHGIIAVITVGIETGMFEVTGEKQNFIIDSPAGEVIAYAKYNGSEVESVSFENVPSFVYKKDVPIIIDDYEFQVDIAFGGAFYAVVDSKEFGLKVDFKDLSAIQMWGGKIKHYIESKMEVKHPLEEGLKGIYGVIFSDEPKGEDATLRNVTIFADGQVDRSPCGTGTSARIATLFEKDALQKGEIFVHECITDGKFEGEVLSVTAVDTYEAVVPKVTGHAFITGFHQFVVDPRDDLKRGFLLG
The following text describes a protein:
Function:
TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation.
Subcellular Localization:
Nucleus.
Sequence:
MDYQHYRCTTLGQTFQDTLDELVQAEKITPEMASKALLRFDKTINEMLATKFDRKITFKADLTTYRYVDDVWTMVLENAVFEDRNDTFKVDIAKLVACEAPTLKKKKK
The following text describes a protein:
Function:
Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release.
Sequence:
MAQARISAKANEGRFCRSSSMADRSSRLLESLDQLELRVEALREAATAVEQEKEVLLEMIHSIQNSQDMRQISDGEREELNLTANRLMGRTLTVEVSVETIRSPQQQESLKHATRIIDEVVSKFLDDLGNARSHLMSLYSACSSEVPAGPVDQKFQSIVIGCALEDQKKIKRRLETLLRNIENADKAIKLLEHSKGAASKTLQQNAEARFN
The following text describes a protein:
Function:
The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
Subcellular Localization:
Mitochondrion.
Sequence:
MMLRAVIRRASTRGGSSASSGLGKSLQSSRVAASSQSFHSLSATQTLVPRGSHARSCFHHRSCPGCSECSRTVLASFQGTTLQRWVRPFSSDSGDVVEAVVPHMGESITDGTLANFLKKPGDRVEADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGNKVAIISKSADAVSHVAPSEKIPEKATPKPSPPTEEPKVESTKAAEKPKASPPPPPPSKQSAKEPQLPPKDRERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFFEKHGVKLGLMSGFIKAAVSALQAQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADQMNFADIEKTINSLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVQRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRIKDVVEDPQRLLLDI