lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Acts as a flagellar brake, regulating swimming and swarming in a bis-(3'-5') cyclic diguanylic acid (c-di-GMP)-dependent manner. Overexpression of this gene decreases swimming and swarming motility; those cells that are motile turn predominantly counterclockwise. The D-118 mutant is still able to bind FliM but no longer affects motility upon overexpression. Binds 1 c-di-GMP dimer per subunit.
Subcellular Localization:
Bacterial flagellum basal body. Note=Localization lost in FliM mutants E-155 or E-160.
Domain:
The N-terminal domain is involved in FliG binding, the C-terminal domain is involved in FliM binding.
Sequence:
MSGYNEQFLKKNPLAILGVLRDLNKNQVPLRISWAHGQFISKILAVDPEKLIVDYGSQEYENSAVLRAGQVAIIAETQGAKVEFTLPQLVTGEYQRLPAFITPLPSSLWFVQRREYFRIGAPLYPPYYGVTTLPDTRTLRFRLFDLSLGGMGALLESAIPDGLIEGARFSQVELNMGQWGIFHVDAQLISISERKVIDGKNETITTPRLSFRFLNVSPAVERELQRIIFSLEREARERANKVRE
The following text describes a protein:
Function:
Catalyzes the meta-cleavage of 3,4-dihydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione (3,4-DHSA) to produce 4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid (4,9-DSHA).
Miscellaneous:
MISCELLANEOUS: Cholesterol metabolism contributes to the survival of M.tuberculosis in the host by helping the bacterial multiplication during earlier stages of infection and to the dissemination of the pathogen in the host.
Sequence:
MSIRSLGYLRIEATDMAAWREYGLKVLGMVEGKGAPEGALYLRMDDFPARLVVVPGEHDRLLEAGWECANAEGLQEIRNRLDLEGTPYKEATAAELADRRVDEMIRFADPSGNCLEVFHGTALEHRRVVSPYGHRFVTGEQGMGHVVLSTRDDAEALHFYRDVLGFRLRDSMRLPPQMVGRPADGPPAWLRFFGCNPRHHSLAFLPMPTSSGIVHLMVEVEQADDVGLCLDRALRRKVPMSATLGRHVNDLMLSFYMKTPGGFDIEFGCEGRQVDDRDWIARESTAVSLWGHDFTVGARG
The following text describes a protein:
Function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively.
Subcellular Localization:
Nucleus.
Sequence:
MDPTNLFDTQFVVSQIDPDGKKFDRVSRIIATSPSLDMTLSIDIATDIWPVTEGQQLTFQLASTLKKETSSAKPDGVDGETQDAAAQAAERDAWRLDQPGNGGIADDFDYVMYGKIYRYDEKVADEVTVYGSFGGLMMALTGNFRHMSNITIGSNVYLLMR
The following text describes a protein:
Function:
This enzyme catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate.
Sequence:
MPSLSSISGPTYVNSQLLVQQTAYKLSDKIFSYSPETFDLDVAVKEWAEANEKNVHGETTTVVPLQTRAGAGAFALGYIFSKDFDLAKRHVPQTLLAPSLSLRHLRSSLDQLALLYGVSSPFVAHVAAADYSAEKGLGADYATALQIAEDLGLALVSSSSAYEVQHMSLLATLLASVLPTLHIYDGIRTARESLRVVDALGEAHIADIYAKISKEAAALNKRLDTAGKVVELLKAFNNELGTSYAPFEYHGHEAPETVLVVFGSAEAQLAKQVASALAAEGKKVGTIVVRVYRPFVEEAFLEVLPASVRQIAVLGQVADAAAVEDANVQSALYSDVLTAVSFTDKLSQAPEVVDVRYAVTDAHTPSSIASIFNKLTSKGEAEPVAFSLTAVEEAQQYVFWDVDNSSAAASASAVGKLLETEQSNNVYVHQTYDNLVQGGVVRTDIRVSQKSIEAPYPVESADVVFVGEEKLLKEIAIVKGVKAGGKLIVRLPNFKEDELEKRIPAAAQKEIQEKGIELYVLDSSSSPALEKEAGLLVDVAFLRVARADITKFDSLSADQTALTEAVNALDQSVRKVEVPAKWAEVENTVAPLVDSVKPNSFVAFQKEEEEETSSLENWQSAAKGFAFKEAYGTQNQLRPDLTVKTYTIKVKENRRLTPTDYDRNIFHIEFDLGDSGLTYNIGEALGIHADNDPEQVLQFIQAYGLNADDLVQVPSREDPAVLETRTVYQSLVQNVDILGKPPKRFFEALAQFATDEEEKKKLERLGSKEGADEFKRLTEEDTVTYVDVLDMFKSAHPDFNDLVRIVDPTKRREYSIASAQAVTPNSVTLMIVVVNWVDTKGRTRYGHATRYLSGLAPGSTITASVKPSVMKLPVKDTAPLIMAGLGTGLAPFRAFVQYRAMQKAQGKEIGSILLYLGSRHQREEYLYGEEWEAYLDAGVITLLGAAFSRDQPEKIYIQDRMRQTVTDIVKAYIKEEGSFYLCGPTWPVPDVTAVLEEAIAAEAQESSRKVDPRKEIERLKEDGRYVLEVY
The following text describes a protein:
Function:
NADP-dependent dehydrogenase with broad substrate specificity acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L-allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone. Also acts on D-threonine, L-serine, D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L-glycerate. Able to catalyze the reduction of the malonic semialdehyde to 3-hydroxypropionic acid. YdfG is apparently supplementing RutE, the presumed malonic semialdehyde reductase involved in pyrimidine degradation since both are able to detoxify malonic semialdehyde.
Sequence:
MSCALSDKVAVVTGASGGIGAAIALELAKAGANVAIGARRLEALQSVKQEIEEKISTSGSILVVQADVTNRLEMQNLVDTAEDAFGPVDILVNNAGVMHVQLMKNVNQESWDRMIDINCKGTLNGVAAVLPKMLARKSGHIVNISSDAGRKVFPGLGVYSASKMFVEGISQTLRLENVGSGLHVTSIQPGDVTTFLVDHANAVSGEDEEATEMFEAEPECEELQPEDVGRAVLYAVTQPADVAVNEVLDTRSLLTMSSNAPLSGTVAVVTGASGGIGAAIALELATAGAKVALGARRLEALETVKSRIEQQIGTTGGVLIVQTDVTNRQEVQSLVDKAEAAFGAVDILVNNAGVMPFELLKNVNQDSWERTIDINCKGTLNGVAAVLPKMLARKSGHIVNISSDAGRKVFPGLGVYSASKMFVEGISQALRLENVGSGLRVTSIQPGNVATDLVKHANAASGVDEEAMKLYGGPSECEVLKPQDIGRAVLYAVTQPPYVAVNEILVEPRDEPI
The following text describes a protein:
Function:
Non-catalytic subunit of the NatB N-terminal acetyltransferase, which catalyzes acetylation of the amino-terminal methionine residues of all proteins beginning with Met-Asp or Met-Glu and of some proteins beginning with Met-Asn or Met-Met.
Subcellular Localization:
Cytoplasm.
Sequence:
MRRSGSKESTIVYSALSLAQAGRGPEALALLEPLKSTPINSLELLDIIQAVYDDQKKGEESFVFWEKFLQTYGKQEKNLLAYFKASIRIKSLSHQRKAAVELQKNFPSRKHTLWVISSLYLLSKKSENEVEQRLLKALAEKTAKLIFEKPTGYIDSCEEFHLYLDVLLLVGDKDRALDALIHQDADRFVDADADLLLRKLELLASCARWDSLFTFSLSLFQTGNTDWKVCKALLDSASNDDSKLVPLKDCILKALSTSSTKRNLHLLWIEASARFFPEEHESALLGYIKKLYMKPIVFEDLRPYLLKLNVDAQHRLLDAFKLADLGESNESQKVDKLYAEVLLLKIHFLLFESFTAESVVDYVRRCFVAFEKGLSLSKGLLPTDFTHGYEALLLAVHSLIYMWEGNKDLKPAEKQALIFDAICLLEKGITYSQHNFHLKLPLIRLYLLLDGGFPAAAKVYDTMSIKQIQNDTLDHYLLTRATTYYPSSVTSHYINSSLKIYGSNEFETPEMISMAYEDGAYSQIEDMRNFRSRLDHSTWKSISLVERARIHYLTAFKPPKQYLPKCSSPKDNRDLKVFADYGSDKLPTVEESLRNSPKPDTLWIHLTVIGHSLVQDSIVNGDFEKAVLSAKEMEVLCENNDLSKQLTSEEIVHMKLLIQLGLLSVKVKNGDYENSSFETIENLIESFDYENSTPLSQLTKYTEIINDLITCLNSFLYHVSATKKKEFTRQYQLLKNISSNKLGSISGITKHKKKAARKYVSELLSNSWLSNLSETQVPYDPKFAKQVGEGMIDSYIQTTDAVSKLPKFVKF
The following text describes a protein:
Function:
Acyltransferase that catalyzes the sn-2-specific, acyl-CoA-dependent acylation of lysophosphatidic acid (LPA) to phosphatidic acid (PA) in lipid particles. Together with ALE1, plays a central role in PA biosynthesis. PA is the intermediate, from which all glycerophospholipids are synthesized. Can also acylate lysophosphoinositol (LPI) and lysophosphoserine (LPS). The fatty acyl substrates include 18:1-acyl-CoA, 14:0-acyl-CoA, 12:0-acyl-CoA and 10:0-acyl-CoA.
Subcellular Localization:
Lipid droplet.
Domain:
The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence:
MSVIGRFLYYLRSVLVVLALAGCGFYGVIASILCTLIGKQHLAQWITARCFYHVMKLMLGLDVKVVGEENLAKKPYIMIANHQSTLDIFMLGRIFPPGCTVTAKKSLKYVPFLGWFMALSGTYFLDRSKRQEAIDTLNKGLENVKKNKRALWVFPEGTRSYTSELTMLPFKKGAFHLAQQGKIPIVPVVVSNTSTLVSPKYGVFNRGCMIVRILKPISTENLTKDKIGEFAEKVRDQMVDTLKEIGYSPAINDTTLPPQAIEYAALQHDKKVNKKIKNEPVPSVSISNDVNTHNEGSSVKKMH
The following text describes a protein:
Function:
Plays a role in endocytosis and regulates internalization of plasma membrane proteins. Overexpression impairs internalization of SLC2A1/GLUT1 and TRPV4 and increases the levels of SLC2A1/GLUT1 and TRPV4 at the cell membrane. Inhibits the TRPV4 calcium channel activity.
Subcellular Localization:
Cell membrane. Cytoplasm. Endomembrane system; Peripheral membrane protein.
Sequence:
MPNYNMEAASNKGRDTSLENIRDAASTFWDIGNYKRTVKRVDDGVKLCDDMLAMIRDRMELERAYARSLKRWASDWRSSIQNGPEYGTMEESWKACFTEADEVANLHADVREKLLSKAYDSVKKWKKDHYHKSMMHYKETRDCDDNFSRIQKPWAKRFEKVVKAKKEYYSAAKAEDNNNKQLNTAESDNNMAADQVKKIRDKADKASKEASRAKDRYKERLEDLTTFNDSYQKSMTEEFDRWQAFEEDRLIFFKEMLVVIHNCVNIADNPNFSKIYNEMLQTIEKADSGRDLCGFAEQFGARMETRWPEFEEYTVTEKAAVKKSSSKFKKIQDSSENVSAPENTAKVEKINPSNEDHDTNDGYNRQISFDNEWDEPPSFNDGEGVPVRALYEYTRRESDELSFAAGDIIMKLSEEDGQGWIKGSLNGTVGLVPANYVEAV
The following text describes a protein:
Function:
May be involved in protein-linked oligosaccharide phosphorylation.
Subcellular Localization:
Cytoplasm. Nucleus. Cell tip.
Sequence:
MEFTDVFYNLENEKQFLAEIDELLTIPYEKNELEIGVSKFLSFINKYGEPYLITEFQLQRCMEKFLNSPLYQLDENAVLSIFYDCFFFLKEQQTLKFIIIVFQSEIQENEYCLRLLASTGFIPVLIKAMKQFKDRSENVAFTSFRYALFLVYYICRSRRLSPTDLVAIDEYFLVNLFKTSEEAWNDEDMDSFGMCVLTLLSINEQFMLVRLASKGSFEIANGIMDLLSSSKVDNGIYSEGLVFTLNREKDPRSRMLILKQLFLLFTTPATYEIFYTNDLNVLIDIFIREINNIPDELSDLRYAYLQVLIPLLENTQVRHPPHYKTKCIVDAVNNVLISHSKSSNMEDARTTDVAIRVLEVPWLQQEMKSLGTAQ
The following text describes a protein:
Function:
Dual specificity protein kinase that phosphorylates ANN1, ANN2 and CP29B at serine and threonine residues, and ANN1, ANN2 and ANN4 at tyrosine residues. May regulate the phosphorylation status of annexin proteins. Acts as a positive regulator in abscisic acid (ABA)-mediated regulation of postgermination growth and drought response. May regulate the expression of ABA-responsive genes such as RD22, RD29A, LTI65/RD29B and RAB18.
Sequence:
MDDIDSSDGAAAARAGEIGSIGVSTPWKPIQLVFKRYLPQNGSASKVHVAVKKPVVVRLTRDLVETYKICDPQFKYRGELNPKRYLTTPSVGVNNDGFDNVNYDLILAVNDDFCSSDSRQRYIVKDLLGHGTFGQVAKCWVPETNSFVAVKVIKNQLAYYQQALVEVSILTTLNKKYDPEDKNHIVRIYDYFLHQSHLCICFELLDMNLYELIKINQFRGLSLSIVKLFSKQILLGLALLKDAGIIHCDLKPENILLCASVKPTEIKIIDFGSACMEDKTVYSYIQSRYYRSPEVLLGYQYTTAIDMWSFGCIVAELFLGLPLFPGGSEFDILRRMIEILGKQPPDYVLKEAKNTNKFFKCVGSVHNLGNGGTYGGLKSAYMALTGEEFEAREKKKPEIGKEYFNHKNLEEIVKSYPYKINLPEDDVVKETQIRLALIDFLKGLMEFDPAKRWSPFQAAKHPFITGEPFTCPYNPPPETPRVHVTQNIKVDHHPGEGHWFAAGLSPHVSGRTRIPMHNSPHFQMMPYSHANSYGSIGSYGSYNDGTIQDNSYGSYGGTGNMFAYYSPVNHPGLYMQNQGGVSMLGTSPDARRRVMQYPHGNGPNGLGTSPSAGNFAPLPLGTSPSQFTPNTNNQFLAGSPGHHGPTSPVRNSCHGSPLGKMAAFSQINRRMSAGYSGGSQSQDSSLSQAQGHGMDNFYQNEGYSGQFSGSPSRRQLDSGVKNRKQTQGGTTLSTGYSTHNNANSSLRSNMYNPSSTAHHLENPDTALSVPDPGDWDPNYSDDLLLEEDSADESSLANAFSRGMQLGSTDASSYSRRFNSNASTSSSNPTTQRRYAPNQAFSQVETGSPPSNDPHARFGQHIPGSQYIPHVSQNSPSRLGQQPPQRYNHGRPNAGRTMDRNHMNAQLPPSNTNSGGQQRSPRSSSYTNGVPWGRRTNNHVPNVPSTSHGRVDYGSIA
The following text describes a protein:
Function:
N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN). Plays a scavenger role by digesting biologically active PGN into biologically inactive fragments. Has no direct bacteriolytic activity.
Subcellular Localization:
Secreted.
Sequence:
MVSKVALLLAVLVCSQYMAQGVYVVSKAEWGGRGAKWTVGLGNYLSYAIIHHTAGSYCETRAQCNAVLQSVQNYHMDSLGWPDIGYNFLIGGDGNVYEGRGWNNMGAHAAEWNPYSIGISFLGNYNWDTLEPNMISAAQQLLNDAVNRGQLSSGYILYGHRQVSATECPGTHIWNEIRGWSHWSG
The following text describes a protein:
Function:
GTPase-activating protein (GAP) for RhoA/Rho1 that plays an essential role in the stability of dorsal branches of mushroom body (MB) neurons. The MB neurons are the center for olfactory learning and memory. Acts by converting RhoA/Rho1 to an inactive GDP-bound state, leading to repress the RhoA/Rho1-Drok-MRLC signaling pathway thereby maintaining axon branch stability.
Sequence:
MRQFNISVIGLSGTEKDRGQVGVGKSCLCNRFMRPMADDYFIDHISVLSQSDFSGRIVNNDHFLYWGDVRKTTEEGVEYQFNIIEQTEFMDDSTFQAFKVGKMDPYSKRCTATKVFSAEKLMYICKNQLGIEKEYEQKVMPDGRLSIDGFVVVFDVSPVPNRSVEKQVEFVQNVIATILKNKKPLVLVTTKNDDAYELYVREAEKISQRKDYKSTVQLIETSAHESINIDLAFLLLAQMIDKVKNRVKIISYQESAKSRKELLDTRSEAVTRLIRNQITDYHVLWSQGSKMLSQYREWNEFLNIFGHEAGQKLFRRHMKKLRDDHLNKKLHQYLDKFALALEYLLPDIGALNISDDDAWECARNYLQNHIEFEQYFFECPQASWTELVDMDEAEDEARIPFDVLETSEAETVFRNYLNSVQQDKKKIGWKQQFKMLLEESGFVTPGKQLSEVRVLFMGRECFEALSEHDCQQIYDIHQDDIIEKSKQNFVELLLEHAQYFLQFKNVDNITQEDVRQITDVIQEDSRYKMLDRLDQERRLMLVQHLRFIHCPIRDHCPFFYNCVDSLIEEVLSDKSASNHKTPSGGGWKSSGSGSDRTLNLLIVGSEHLASDLLNDIRICTGSKGEYIYENQTYYLNYRIANGDMEAFKAIDVYSSGLICVYSNQQSFETLKDNLERTLLCNLELEDKFENLPIVLVYQPQDLKENEVEYLRNEGMRLSEMLHCDFIDHTQNHQKYVYDILNIVILSLKLTEMKSYEPYPSNHTDLRILCCIFCGDQYDIENIVQPLVEESTLVKANEHSIIVDVFIGDAKRRVEFILSSYHGTSQYRDELIHGYIYFYSTKRRSSLANLSILAAQNANIPLQIIAVTESGGVNAFFNSDICQFLITEGNAVADRFKGSFMTFSADQYVKFAFYNPFLKTAWDNKYEVENLHVEESITLDSGEGTLENSVNQMPRPPPRHESYMLSNTLGTDGSGSENYEMAPTRSLNSLNEERDISLDEIYDDNEKPKHLHQKWLEDKSDGRRNMNKNLIWNNFSGSTHAYTTGRRHIDSNLNKIRPKGPSQTLKVGEAPSRNCPAMSSSTFTLPTQQPGKLNMKNFQLVSDAVAKMNFTGSGSGSGSGSGSGSTGLGLGLGSGSGCMGDSFLEPVDKDGKRYDHAQLDGEDEDSEELAEYEQIYENEDCTESDSCASSTERRVRQQNAYYKASKKPVAAKKQKKKKVAIPVQTPRVPPFGSYVSPPEIPLHYQRMAVGGSGPEKPEPCVPEFMKSDKSPEYSMVPELAGAGIFGAENLPEYNMNQAKCLKDFEKLEKRRIKEETARQRKLQEKEKEQEKKLKRKLKQNAKGLVESAEAQFGKLMITSEQGEIPIFLNKCVEFIEKEGLDSEGIYRVPGSRAHVDMLFQRFEEDTNTEIDALDIPVNAVATALKDFFSKRLPPLFSKDIIKELEEIAGSRGVGNSKLNVEVKTDRSCRLIALKSLLQKLPPINFAILKYIFQHFVHVSDNSKLNSMDSKNLAICWWPTLIPIDFTDMGHFEQLRPYLEDIVQTMIDQFPYLFCGKDAFVMV
The following text describes a protein:
Function:
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular Localization:
Cytoplasm.
Sequence:
MSDDDWDADETIAPAAPAVTLPPKVPAKKWADEDAEDNDSDDDWDKSEDEKPQATKVAAVAPAKKKGTLKQKLAEKERLAKEAKEKGVDDDNDLMYTMTEQERRRLAREKEQEADLAVASDLMGAVDLGDEGDALKSVLSAHPSTKNDFSELSKNIYTSIIKKHESNPLYAHFVEQLAKDISAALTAVQTRKVSSALSVLGNTKQQEEREKASGKKKAASKPKLGAAKVLSKVDTEAYDDVLGDDDFM
The following text describes a protein:
Function:
Could play a role in neuronal development.
Subcellular Localization:
Nucleus.
Sequence:
MPNWGGGKKCGVCQKAVYFAEEVQCEGNSFHKSCFLCMVCKKNLDSTTVAVHGEEIYCKSCYGKKYGPKGYGYGQGAGTLSTDRGEALGIKYEEGQPHRPTNPNAARMAQKVGGADGCPRCGQAVYAAEKVIGAGKSWHKSCFRCAKCGKSLESTTLADKDGEIYCKGCYAKNFGPKGFGFG
The following text describes a protein:
Function:
Catalyzes the reduction of prostaglandin-ethanolamide H(2) (prostamide H(2)) to prostamide F(2alpha) with NADPH as proton donor. Also able to reduce prostaglandin H(2) to prostaglandin F(2alpha).
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MAKVDLAKVGKNVVKSADSGENVELQSLWQEQPVVLFFLRRFGCQVCRWMASEISKLEPDLRASGVSLVGVGPEEVGLQEFKEGGFFKGSIYVDDQKRCYKDLGFKRYTAISVVPAALGKKVRDISSKASAEGIQGNFSGDLLQSGGMLIVAKGGEKVLLHFIQDSPGDLVPLEDISKALGITASVKAGQKPVPSLTIVIKPMCDLMSDHHADASKVKGLVLVFAEERRLQDPCRKHWGRQTSHQLMSNFYHKNMEDNVFSSLKLLPIWFLFGE
The following text describes a protein:
Function:
Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). FHF complex promotes the distribution of AP-4 complex to the perinuclear area of the cell.
Sequence:
MKQVGATSGGSPQLANPRRVILGALASPTFHSMEKMSWLSKLAPRGPGHRAPRTTSLQTPVTADPETCLMVFKNHWSQVVRILERRAPQAAPGGSDDLSAVHNHMYQMLTLLVEDRVTPSAPTAPGPLLKITLHEDLLARVLAWQLQWDGPGDGVGAEERRAEQLKLFEMLVSEARQPLLHHQPVREALLTLLEACGPPTGPALDAGLVLLLSQLCVCVAREPALLELFLQPPPEPGAAPRLLLFSRLVPFVHREGTLGQQARDALLLLMALSAGSPTVGRYIADHSYFCPVLATGLSALYSSLPRKIEVRGDDWHCLRREDWLGVPALALFMSSLEFCNAVIQVAHPLVQKQLVDYIHNGFLVPVMGPALHKSSVEEMIASTAYLELFLRSVSEPALLRTFLRFLLLHRHDAHTILDTLVSRISSNSRLCMVSLSLFRTLLNLNCEDVVLQLVLRYLVPCNHVMLSQKRAVRDLDLYGRAADKFLSLIPRCCRHRAPSPPHLEQASWARGPGSPNLDSSSVVTVPRPSTPSRLALFLRQQSLGGTEPSSPAPRSPSLVPSPASSPGHRPGPVEEPGELEDNYLEYLREARRCVDHCVHACRSWSAPYDGEQPPADPSPVDPSSVPTGPRTKKRSLQPEEEDGEDGAEGEEEELGGGGHAGARILSLGEEEGSGLLTSLQVNGALGPWPEGAKKVRRGPRGGVGEQKGGIGGLVGLEGFGRELRELEVALSNGGAGPDSCHESPLPPEEEEAVYESFSCPPEPLGPLLSSPLRIPSQLPSQPFTGPFMAVLFAKLENMLQNSLYVNFLLTGLVAQLACYPQPLLRSFLLNTNMVFQPSVKSLLQVLGSVKNKIESFAASQEDFPALLSKAKKYLIARGKLDWAEGPGAGSTPRRPDTLVKARKPSLGELLLRHAHSPTRSRQTAQVVPQLGREGPGPALGLGVGLGPHSALGTSPLPLRSSPAERQGEALRIKNAVYCAVVFPEFLKELAAISQAHAVTSPFLLEAFEEGPRTPARPSPDP
The following text describes a protein:
Function:
Catalyzes the formation of 5-methyl-uridine at position 54 (m5U54) in all tRNA. May also have a role in tRNA stabilization or maturation.
Sequence:
MYEQFEFSFFFFENSDNKVKYKAHLISSIKRWSIITCMRCFWTVQKSIFKARFFACRNFVKKHNYKLISTMTGSTEMVPPTMKHTVDNKRLSSPLTDSGNRRTKKPKLRKYKAKKVETTSPMGVLEFEVNDLLKSQNLSREQVLNDVTSILNDKSSTDGPIVLQYHREVKNVKVLEITSNGNGLALIDNPVETEKKQVVIIPFGLPGDVVNIKVFKTHPYYVESDLLDVVEKSPMRRDDLIRDKYFGKSSGSQLEFLTYDDQLELKRKTIMNAYKFFAPRLVAEKLLPPFDTTVASPLQFGYRTKITPHFDMPKRKQKELSVRPPLGFGQKGRPQWRKDTLDIGGHGSILDIDECVLATEVLNKGLTNERRKFEQEFKNYKKGATILLRENTTILDPSKPTLEQLTEEASRDENGDISYVEVEDKKNNVRLAKTCVTNPRQIVTEYVDGYTFNFSAGEFFQNNNSILPIVTKYVRDNLQAPAKGDDNKTKFLVDAYCGSGLFSICSSKGVDKVIGVEISADSVSFAEKNAKANGVENCRFIVGKAEKLFESIDTPSENTSVILDPPRKGCDELFLKQLAAYNPAKIIYISCNVHSQARDVEYFLKETENGSAHQIESIRGFDFFPQTHHVESVCIMKRI
The following text describes a protein:
Function:
May be involved in the energy metabolism of the mature sperm.
Subcellular Localization:
Cytoplasm.
Sequence:
MCQVEFELACAAIKQLKGPVSDQEKLLVYSFYKQATQGDCNIPAPPATDVKAKAKWDAWNDKKGISKMDAMRIYVAKVEELKKNDTG
The following text describes a protein:
Function:
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatE shares overlapping functions with TatA.
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein.
Sequence:
MGEISITKLLVVAALVVLLFGTKKLRTLGGDLGAAIKGFKKAMNDDDAAAKKGADVDLQAEKLSHKE
The following text describes a protein:
Function:
Part of an ABC transporter complex involved in erythritol/L-threitol import. Binds erythritol and L-threitol. Functions in the transport for the degradation pathways of erythritol and L-threitol, that allow M.smegmatis to grow on these compounds as the sole carbon source.
Sequence:
MMSRESQPGLHRQLSRRNMLAAMGLAGAAAVSLPVLSACGVGGRTNAPNGASEVTGGFDWRKASGSTINILQTPHPYQQSYQPLLKEFTELTGINVNVDLVPEADYFTKLNTELAGGTGKHDAFMLGAYFIWQYGPPGWIEDLNPWLQNSSATNAEYDFEDIFEGLRTSTRWDFELGNPLGTGGQWAIPWGFENNVVAYNKAYFDQRGITKLPDNFDDFIQLAIDLTDRSENRYGIATRGSKSWATIHPGFMTQYVREGAVDYTFDGTDLVAEMDSDKAVEFTRKWIEMQHKAGPTSWTTYDYPNATGDLGDGTAMMVYDADSATYPKNKPGASAQAGNLGWYPGPAGPDGNYKTNLWTWTWAMNANSRNKLPAWLFIQWATGKESMNKAVEGGIYADPVRQSVFDTTFKRIAADQHGYLETFETVIGSSKIQFTPQKKFFDTTKDWAVALQDIYGGDDAASRLRSLAKTNTSKVNL
The following text describes a protein:
Function:
Weakly inhibits G protein signaling in nervous system, interacting preferentially with the G(O) subfamily member goa-1. In vitro, it acts as a GTPase activator of goa-1. Rgs-1 and rgs-2 redundantly adjust signaling when worms are fed to allow rapid induction of egg-laying behavior. Modulates chemotaxis responses by regulating negatively the sensitivity to quinine in ASH sensory neurons.
Sequence:
MRLLTCDCTFMGQKHSGSVSVEKKNQENDGPPTYEIVFGWSQSFENLMKHRAGQKYFAEFLKGEYSDENILFWQACEELKREKNAEKIEEKARIIYEDFISILSPKEVSLDSRVREIVNTNMGRPSASTFDEAQNQIYTLMQRDSYPRFLASNIYKTVMGTFGIKEEAV
The following text describes a protein:
Function:
Required for proper post-translational import and stabilization of peroxisomal membrane proteins (PMPs). Acts as a cytosolic import receptor for PMPs and delivers them to the docking factor PEX3 at the peroxisomal membrane for subsequent insertion into the membrane. Acts as a chaperone in stabilizing or maintaining PMPs in the lipid bilayer. Directs PEX17, a peripheral component of the peroxisomal matrix protein translocation machinery, to peroxisomes. Stabilizes VPS1, a protein required for peroxisomal fission, at the peroxisomal membrane. Also acts in conjunction with PEX3 in the formation of peroxisomes from preperoxisomal compartments at the endoplasmic reticulum during de novo peroxisome synthesis, probably via the import of additional PMPs.
Miscellaneous:
MISCELLANEOUS: Present with 5350 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Peroxisome membrane; Lipid-anchor; Cytoplasmic side. Endoplasmic reticulum membrane. Note=Predominantly cytoplasmic. Concentrates in a PEX3-dependent manner to defined foci on the endoplasmic reticulum membrane, which then bud off to form newly sythesized peroxisomes.
Sequence:
MNENEYDNFDDLDDLLDEDPTKLDEAEPDDVQAKGSVYNDSENKEKNAESKDSDGVQVANESEEDPELKEMMVDLQNEFANLMKNNGNENNVKTEDFNKLISALEEAAKVPHQQMEQGCSSLKSNSTDKGTVNGSNPGFKNIVSNTLDRLKENGNKVDTSLAEETKESQRSGQNNNIDDILSQLLDQMVASGGKESAENQFDLKDGEMDDAITKILDQMTSKEVLYEPMKEMRSEFGVWFQENGENEEHKEKIGTYKRQFNIVDEIVNIYELKDYDELKHKDRVTELLDELEQLGDSPIRSANSPLKHGNEEEELMKMLEIDGNDPNLGNLDKELTDGCKQQ
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MESLGLQTVTLSDGTTAYVQQAVKGEKLLEGQVIQLEDGTTAYIHQVMVQKEPLSFEDGQPVQLEDGSMAYIHRTPKEGYDPSALEAVQLEDGSTAYIHHPVAVPSDSAILAVQTEVGLEDLAAEDDEGFTADTVVALEQYASKVLHDSQAPHNGKGQQVGDRAFRCGYKGCGRLYTTAHHLKVHERAHTGDRPYRCDFPSCGKAFATGYGLKSHVRTHTGEKPYKCPEELCSKAFKTSGDLQKHVRTHTGERPFRCPFEGCGRSFTTSNIRKVHVRTHTGERPYTCPEPHCGRGFTSATNYKNHVRIHTAFCVLSQPYVSPHSPVTPATSVIPLCLLPLLFTTFNFTSPYPRTPSPSTCPFTSPSITSGLSGPTRLSPLCSAGHRPQLCLFRVPVSLRPHQLTPSPTPTPPPPSFPLASPSSHPPHSPVSPGEKPYVCTVPGCGKRFTEYSSLYKHHVVHTHCKPYTCSTCGKTYRQTSTLAMHKRSAHGELEATEESEQALYEQQQLDAACATEESPPPKRPRITYLSEVKEECCDVPAQVAMVTEEDGAPQVALITQDGAQQVSLSPEDLQALGSAITMVTQHSSTTLTIPSEDDDLATSGTHTVTMVSADGTQTQPVTIITSGAVVADDSSVASLHHQQVALLATANGTHIAVQLEEQQTLEEAISVATAAMQQGAVTLEATESGNGC
The following text describes a protein:
Function:
Catalyzes the S-methylmethionine (SMM) biosynthesis from adenosyl-L-homocysteine (AdoMet) and methionine. SMM biosynthesis (by MMT1) and degradation (by HMT-1, HMT-2 and HMT-3) constitute the SMM cycle in plants, which is probably required to achieve short term control of AdoMet level. Also able to catalyze the selenium-methylmethionine (SeMM) from AdoMet and selenium-methionine (SeMet). May play a role in phoem sulfur transport; such function is however not essential.
Subcellular Localization:
Cytoplasm.
Sequence:
MADLSSVDEFLNQCKQSGDAAYGALRSVLERLEDPNTRSKARIFLSDIYKRVGSSETSLQTYHFHIQDIYLDQYEGFQSRKKLTMMVIPSIFIPEDWSFTFYEGLNRHPDTIFKDKTVSELGCGNGWISIAIAAKWLPSKVYGLDINPRAVKISWINLYLNALDDNGEPVYDEEKKTLLDRVEFYESDLLGYCRDNKIQLERIVGCIPQILNPNPEAMSKLITENASEEFLHSLSNYCALQGFVEDQFGLGLIARAVEEGISVIKPAGIMIFNMGGRPGQGVCRRLFERRGVRVTQMWQTKILQAADTDISALVEIERSSPHRFEFFMGLSGDQPICARTAWAYGKAGGRISHALSVYSCQIRQPNLVKIIFDFLKNGFQEISNSLDLSFEDETVADEKIPFLAYLASVLKNSSYFPFEPPAGSKRFCSLIAGFMRTYHRIPINQDNIVVFPSRAVAIESAFRLFSPRLAIVDEHLTRQLPRSWLTSLAIEDTSMDKSDDQITVIESPHQSDLMIELIKKLKPQVVVTGMAPFEVITSSSFLHLLEVTKEIGCRLFLDISDHFELSSLPASNGVLKYLAENQLPSHAAIICGLVKNKVYSDLEVAFVITEVDAIAKALSKTVEVLEGHTAIISQYYYGCLFHELLAFQLADRHAPAERESEKAKSEEIIGFSSSAVSILKDAELSVTEIDETSLIHMDVDQSFLQIPQSVKAAIFESFVRQNISEAEVDINPSIKQFVWSNYGFPTKSSTGFVYADGSLALFNKLVICCAQEGGTLCLPAGTNGNYVAAAKFLKANVVNIPTESSDGFKLTEKTLTKALESVKKPWVCISGPTVSPTGLVYSNEEMDILLSTCAKFGAKVIIDTSFSGLEYSATSWDLKNALSKMDSSLSVSLLGCLSLNLLSGAIKLGFLVLDQSLIDAFHTLPGLSKPHSTVKYAAKKMLALKEEKASDFLDAVSETIKTLEGRSRRLKEVLQNSGWEVIQPSAGISMVAKPKAYLNKKVKLKAGDGQEIVELTDSNMRDVFLSHTGVCLNSGSWTGIPGYCRFSFALEDSEFDKAIESIAQFKSVLAN
The following text describes a protein:
Function:
Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics.
Subcellular Localization:
Cytoplasm.
Domain:
The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments (By similarity).
Sequence:
MGNAGSMDSQQTDFRAHNVPLKLPMPEPGELEERFAIVLNAMNLPPDKARLLRQYDNEKKWELICDQERFQVKNPPHTYIQKLKGYLDPAVTRKKFRRRVQESTQVLRELEISLRTNHIGWVREFLNEENKGLDVLVEYLSFAQYAVTFDFESVESTVESSVDKSKPWSRSIEDLHRGSNLPSPVGNSVSRSGRHSALRYNTLPSRRTLKNSRLVSKKDDVHVCIMCLRAIMNYQYGFNMVMSHPHAVNEIALSLNNKNPRTKALVLELLAAVCLVRGGHEIILSAFDNFKEVCGEKQRFEKLMEHFRNEDNNIDFMVASMQFINIVVHSVEDMNFRVHLQYEFTKLGLDEYLDKLKHTESDKLQVQIQAYLDNVFDVGALLEDAETKNAALERVEELEENISHLSEKLQDTENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLRKMVKEKEEAIQRQSTLEKKIHELEKQGTIKIQKKGDGDIAILPVVASGTLSMGSEVVAGNSVGPTMGAASSGPLPPPPPPLPPSSDTPETVQNGPVTPPMPPPPPPPPPPPPPPPPPPPPPLPGPAAETVPAPPLAPPLPSAPPLPGTSSPTVVFNSGLAAVKIKKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERILEDLNVDEFEEIFKTKAQGPAIDLSSSKQKIPQKGSNKVTLLEANRAKNLAITLRKAGKTADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERERKPLENLSDEDRFMMQFSKIERLMQKMTIMAFIGNFAESIQMLTPQLHAIIAASVSIKSSQKLKKILEIILALGNYMNSSKRGAVYGFKLQSLDLLLDTKSTDRKQTLLHYISNVVKEKYHQVSLFYNELHYVEKAAAVSLENVLLDVKELQRGMDLTKREYTMHDHNTLLKEFILNNEGKLKKLQDDAKIAQDAFDDVVKYFGENPKTTPPSVFFPVFVRFVKAYKQAEEENELRKKQEQALMEKLLEQEALMEQQDPKSPSHKSKRQQQELIAELRRRQVKDNRHVYEGKDGAIEDIITVLKTVPFTARTAKRGSRFFCEPVLTEEYHY