PharMolix/UniProtQA huggingface dataset:
Protein: TOP1_SALTY
Sequence: MGKALVIVESPAKAKTINKYLGNDYVVKSSVGHIRDLPTSGSAAKKSADSTSTKTAKKPKKDERGALVNRMGVDPWHNWDAHYEVLPGKEKVVSELKQLAEKADHIYLATDLDREGEAIAWHLREVIGGDDARYSRVVFNEITKNAIRQAFEQPGELNINRVNAQQARRFMDRVVGYMVSPLLWKKIARGLSAGRVQSVAVRLVVEREREIKAFVPEEFWEIDANTTTPSGEALPLQVTHQNDKPFRPVNREQTLAAVSLLEKARYSVLEREDKPTSSKPGAPFITSTLQQAASTRLGFGVKKTMMMAQRLYEAGYITYMRTDSTNLSQDAVNMVRGYIGDNFGKKYLPDNPNQYASKENSQEAHEAIRPSDVAVMAESLKDMEADAQKLYQLIWRQFVACQMTPAQYDSTTLTVGAGEFRLKARGRILRFDGWTKVMPALRKGDEDRTLPAVNKGDALTLLELTPAQHFTKPPARFSEASLVKELEKRGIGRPSTYASIISTIQDRGYVRVENRRFYAEKMGEIVTDRLEENFRELMNYDFTAQMEDSLDQVANHQAEWKAVLDNFFSDFTQQLDKAEKDPEEGGMRPNQMVLTSIDCPTCGRKMGIRTASTGVFLGCSGYALSPKERCKTTINLVPENEVLNVLEGDDAETNALRAKRRCQKCGTAMDSYLIDPKRKLHVCGNNPTCDGYEIEEGEFRIKGYDGPIVECEKCGSEMHLKMGRFGKYMACTNDECKNTRKILRNGEVAPPKEDPVPLPELPCEKSDAYFVLRDGAAGIFLAANTFPKSRETRAPLVEELYRFRDRLPEKLRYLADAPQQDPEGNKTVVRFSRKTKQQYVAAEKDGKATGWSAFFVDGKWVEGKK
What is the function of this protein?
Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex.  Introduces a single-strand break via transesterification at a target site in duplex DNA.  The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand.  The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils.  Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.
What are the official names of this protein?
DNA topoisomerase 1, DNA topoisomerase I, Omega-protein, Relaxing enzyme, Swivelase, Untwisting enzyme.
What is the protein family that this protein belongs to?
Belongs to the type IA topoisomerase family.
Protein: G1L8_ORYSI
Sequence: MEGGGGGADAQAQAQPVAQAPPAMQPMQQLSRYESQKRRDWNTFLQYLRNHRPPLTLARCSGAHVIEFLKYLDQFGKTKVHASGCAYYGQPSPPAPCPCPLRQAWGSLDALIGRLRAAYEESGHAPESNPFAARAVRIYLREVRDAQAKARGIPYEKKKRKRTQQQQPPPQPPLPPQHQPGAAAGEASSSSSAAAAAVAAEGSGSSAATAAATSQTGGGGGSTTTTTASAAAPTTATRV
What is the function of this protein?
Probable transcription regulator that acts as a developmental regulator by promoting cell growth in response to light.
What are the official names of this protein?
Protein G1-like8.
What is the protein family that this protein belongs to?
Belongs to the plant homeotic and developmental regulators ALOG protein family.
What are the subcellular locations of this protein?
Nucleus.
Protein: EPMA_YERPG
Sequence: MSDTASWQPSAPIANLLKRAAIMAEIRRFFADRGVLEVETPTMSQATVTDIHLVPFETRFVGPGAADGLTLYMMTSPEYHMKRLLAAGSGPIYQLGRSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQILDCNSAETLSYQQAFLRHLNIDPLSAEKAQLREVAAKLDLSNIADTEEDRDTLLQLLFTVGVEPYIGRDKPAFIYHFPASQASLAEISTEDHRVAERFEVYFKGIELANGFRELTDGDEQLQRFEQDNRNRAKRGLPQNPIDMNLIAALKQGLPDCSGVALGVDRLVMLALNAERLSDVIAFPVNIA
What is the function of this protein?
With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P).  Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.
What are the official names of this protein?
Elongation factor P--(R)-beta-lysine ligase, EF-P--(R)-beta-lysine ligase, EF-P post-translational modification enzyme A, EF-P-lysine lysyltransferase.
What is the protein family that this protein belongs to?
Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.
Protein: TMCAL_STRPB
Sequence: MTVTGIIAEFNPFHNGHKYLLETAEGLKIIAMSGNFMQRGEPALIDKWIRSEMALKNGADIVVELPFFVSVQSADYFAQGAIDILCQLGIQQLAFGTENVIDYQKLIKVYEKKSEQMTAYLSTLEDTLSYPQKTQKMWEIFAGVKFSGQTPNHILGLSYAKASAGKHIQLCPIKRQGAAYHSKDKNHLLASASAIRQHLNDWDFISHSVPNAGLLINNPHMSWDHYFSFLKYQILNHSDLTSIFQVNDELASRIKKAIKVSQNIDHLVDTVATKRYTKARVRRILTYILVNAKEPTLPKGIHILGFTSKGQAHLKKLKKSRPLITRIGAETWDEMTQKADSIYQLGHQDIPEQSFGRIPIIIKNERLN
What is the function of this protein?
Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates.  First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
What are the official names of this protein?
tRNA(Met) cytidine acetate ligase.
What is the protein family that this protein belongs to?
Belongs to the TmcAL family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: SYC_GLOVI
Sequence: MALQIYNTLTRRKEPFVPLEAGTVKMYVCGVTVYDYCHLGHGRTYVVWDTVRRYLISRGYAVTYVQNFTDVDDKILRRAQQEGTTMEAVAEKYIAAYFEDMDRLNVLRADSYPRATQTMPEIGALIDRLTSIGYAYPAAGDVYYSVRRFAEYGKLSGKRLAELEAGASERLQDEELARKKDPFDFALWKGAKPGEPAWDSPWGAGRPGWHIECSAMVRKSLGETIDIHAGGEDLQFPHHENEIAQSEAVTGKPLARYWMHNAFLNVVNSSGAEEKMSKSLGNFKTLRDLFEVFPPMALRLFLLKTSYRNPIAFSAEAFKGSEQNWRELEEVLQLAGWIAGQGRPATDDIESEPWVRRFNEAMDDDFNTAAALAEVIALGKQLAGRYHAAIHGTPLADPARFAREWRTFALLCDILGLKAAEPEARQSALPEAEIEAQIALRRQAREERNWAEADRIRKQLLDQGIVLIDHKEKPTTWRHADP
What are the official names of this protein?
Cysteine--tRNA ligase, Cysteinyl-tRNA synthetase, CysRS.
What is the protein family that this protein belongs to?
Belongs to the class-I aminoacyl-tRNA synthetase family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: DSBA_BUCAP
Sequence: MKKILIVLYSIFLSFTASSYEFNNKKEYEIEKRNISNVPKVMHFFSFFCPYCYELEKIYNIQSLIKNKIDKKIKIQTYHVNFLGGEFSKILTKIWIIAQKMKVEEKIMMPIFKEIQENNTISHTSNIKNIFLQKTGINKDQYNKFWNSFTIKMLIKKNDNDINKIKLNHVPTMIVNGKYVIDYYKLEKIFKTNFSKKYIKLIKFLLSKK
What is the function of this protein?
Involved in disulfide-bond formation.  Acts by transferring its disulfide bond to other proteins (By similarity).
What are the official names of this protein?
Thiol:disulfide interchange protein DsbA.
What is the protein family that this protein belongs to?
Belongs to the thioredoxin family. DsbA subfamily.
Protein: BETI_ECOSM
Sequence: MPKLGMQSIRRRQLIDATLEAINEVGMHDATIAQIARRAGVSTGIISHYFRDKNGLLEATMRDITSQLRDAVLNRLHALPQGSAEQRLQAIVGGNFDETQVSSAAMKAWLAFWASSMHQPMLYRLQQVSSRRLLSNLVSEFHRELPRQQAQEAGYGLAALIDGLWLRAALSGKPLDKPLAHSLTRHFITQHLPTD
What is the function of this protein?
Repressor involved in the biosynthesis of the osmoprotectant glycine betaine.  It represses transcription of the choline transporter BetT and the genes of BetAB involved in the synthesis of glycine betaine (By similarity).
What are the official names of this protein?
HTH-type transcriptional regulator BetI.
Protein: RECA_STAAB
Sequence: MDNDRQKALDTVIKNMEKSFGKGAVMKLGDNIGRRVSTTSTGSVTLDNALGVGGYPKGRIIEIYGPESSGKTTVALHAIAEVQSNGGVAAFIDAEHALDPEYAQALGVDIDNLYLSQPDHGEQGLEIAEAFVRSGAVDIVVVDSVAALTPKAEIEGEMGDTHVGLQARLMSQALRKLSGAISKSNTTAIFINQIREKVGVMFGNPETTPGGRALKFYSSVRLEVRRAEQLKQGQEIVGNRTKIKVVKNKVAPPFRVAEVDIMYGQGISKEGELIDLGVENDIVDKSGAWYSYNGERMGQGKENVKMYLKENPQIKEEIDRKLREKLGISDGDVEETEDAPKSLFDEE
What is the function of this protein?
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs.  It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
What are the official names of this protein?
Protein RecA, Recombinase A.
What is the protein family that this protein belongs to?
Belongs to the RecA family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: MHAA_STRAQ
Sequence: MADKWWGEQLLGRGDDGDLWAVSAAPVTRGELRAGVAGLRLRFRESGISEGSSVLLRMTPSFTYLQVLLALWSCGAQVVLVDFRLKPAEFEPLVERVRPQYLVVAAGAGGPVTGFRQESDFEVRRLAGGRPAEDGVVLVQFSSGSTGRPKVIGRPAGSVLAELDRHAGLPGTPGPGERVLLLNSVMHNMGLMTGVLHALAAGATLVVPPTFRPAEVLRLMARTEVSVMYGTPVHYDLLARTADRPERLSLRLAVSGGERVPEETRQRFLAAFGLPICQVYGVTEIGLIAGDLSGRCIPPEIGPPVPGVELEIDGEELLVRMDRSPYLYGEHTDRYRDGWLRTFDRVGRDPETGVLSILGRSDSLVVVGGLKVDLTEVEAALLDHPRVAEVVVTHQDAIEAFVGGDEDLTADELTAWCRERLSAVKIPKRFFVTRQLPRNSMGKLARDRALMHRHITSERSAQSRPAELKGAS
What is the function of this protein?
Involved in the biosynthesis of actinomycin (PubMed:1318300).  Activates 4-methyl-3-hydroxyanthranilic acid (4-MHA), the precursor of the chromophoric moiety of the actinomycin, as adenylate (PubMed:1318300, PubMed:10212227).  Can also use other benzene carboxylic acids, such as 4-methyl-3-hydroxybenzoic acid (4-MHB) or 3-hydroxyanthranilic acid (3-HA), but not pyridine, quinoline, or quinoxaline carboxylic acids (PubMed:1318300).
What are the official names of this protein?
3-hydroxy-4-methylanthranilate adenylyltransferase, 4-MHA-activating enzyme, 4-methyl-3-hydroxyanthranilic acid-AMP ligase, 4-MHA-AMP ligase, Actinomycin synthetase I, ACMS I.
What is the protein family that this protein belongs to?
Belongs to the ATP-dependent AMP-binding enzyme family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: ARNT_YERPB
Sequence: MKLLKDSGAALLALFFVLVYLLPVNSRLLWQPDETRYAEISREMLQRGDWVVPYFMDIRYFEKPVAGYWFNNISQWIFGDSNFAVRFGSIFSTALSAVLVYWLATLLWRNRSTSVLATLIYLSFLLVFGIGTYAVLDPMISLWLTAAMVSFYLTLKAENWQQKVGAYALLGVACGMGFMTKGFLALAVPVIAVLPIVIQQKRIKDLVVFGPIAIVCAVLLSLPWALAIAQREPDFWNYFFWVEHIQRFAEASAQHKSPIWYYLPILCIGVLPWLGLLPGALFKGWRERATKPELFFLLSWVVMPLLFFSVAKGKLPTYILPCMAPLSLLMAAYATDCANNIRMRALKINGVINLLFGVACALVIVVIGLGLVKDIVAYGPQENQKVWLGVLAFAGWGVTGFITLRNNARNWRWAAACPLLFILLVGYLIPQQVVDSKQPQNFIKNNFSELSSSRYVLTDSVGVAAGLAWELKRSDILMFSEKGELTYGLAYPDSQDNYISNDDFPTWLAQARKEGDVSLVVQLAKNEALPAHLPPADKVNLMNRLALLWYQKTP
What is the function of this protein?
Catalyzes the transfer of the L-Ara4N moiety of the glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A.  The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.
What are the official names of this protein?
Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase, 4-amino-4-deoxy-L-arabinose lipid A transferase, Lipid IV(A) 4-amino-4-deoxy-L-arabinosyltransferase, Undecaprenyl phosphate-alpha-L-Ara4N transferase.
What is the protein family that this protein belongs to?
Belongs to the glycosyltransferase 83 family.
What are the subcellular locations of this protein?
Cell inner membrane; Multi-pass membrane protein.
Protein: PUR5_SHIB3
Sequence: MTDKTSLSYKDAGVDIDAGNALVGRIKGVVKKTRRPEVMGGLGGFGALCALPQKYREPVLVSGTDGVGTKLRLAMDLKRHDTIGIDLVAMCVNDLVVQGAEPLFFLDYYATGKLDVDTASAVISGIAEGCLQSGCSLVGGETAEMPGMYHGEDYDVAGFCVGVVEKSEIIDGSKVSDGDVLIALGSSGPHSNGYSLVRKILEVSGCDPQTTELDGKPLADHLLAPTRIYVKSVLELIEKVDVHAIAHLTGGGFWENIPRVLPDNTQAVIDESSWQWPEVFNWLQTAGNVERHEMYRTFNCGVGMIIALPAPEVDKALALLNANGENAWKIGIIKASDSEQRVVIE
What are the official names of this protein?
Phosphoribosylformylglycinamidine cyclo-ligase, AIR synthase, AIRS, Phosphoribosyl-aminoimidazole synthetase.
What is the protein family that this protein belongs to?
Belongs to the AIR synthase family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: BIOD_XYLFM
Sequence: MSLSAFYVTGTDTGIGKTFVSCILLHMLRGRGQRAVGMKPVASGCTYSDTGWRNEDALALQAASDPTPAYDLINPYALPAAVAPEIAAIEARVTVALEPLSASFTQLRAQADVVVVEGVGGWATPLNATIDQATLVRALEIPVVLVVGLRLGCMNHARLSTAAIMADGLRCIGWIANTIDPHMARIEENLALLRQRLPIPYWGHLPHIPPGINPATLATRLHPQGD
What is the function of this protein?
Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
What are the official names of this protein?
ATP-dependent dethiobiotin synthetase BioD, DTB synthetase, DTBS, Dethiobiotin synthase.
What is the protein family that this protein belongs to?
Belongs to the dethiobiotin synthetase family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: ISPD_SALNS
Sequence: MAATLLDVCAVVPAAGFGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVVIAISPGDHRFAQLPLADHPQITVVDGGNERADSVLAGLQAVAEAQWVLVHDAARPCLHQDDLARLLAISENSRVGGILASPVRDTMKRGEPGKNAIAHTVERADLWHALTPQFFPRELLHDCLTRALNEGATITDEASALEYCGFHPALVEGRADNIKVTRPEDLALAEFYLTRTIHQEKA
What is the function of this protein?
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
What are the official names of this protein?
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, 4-diphosphocytidyl-2C-methyl-D-erythritol synthase, MEP cytidylyltransferase, MCT.
What is the protein family that this protein belongs to?
Belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily.
Protein: LIPG1_ARATH
Sequence: MIIMMNCFPCFTSQKSRNAPCTTNETNDDNVEHDEFRPPVVATTKRTEEREPAEQQPPVKTFNFRELATATKNFRQECLLGEGGFGRVYKGTLQSTGQLVAVKQLDKHGLHGNKEFLAEVLSLAKLEHPNLVKLIGYCADGDQRLLVFEYVSGGSLQDHLYEQKPGQKPMDWITRMKIAFGAAQGLDYLHDKVTPAVIYRDLKASNILLDAEFYPKLCDFGLHNLEPGTGDSLFLSSRVMDTYGYSAPEYTRGDDLTVKSDVYSFGVVLLELITGRRAIDTTKPNDEQNLVAWAQPIFKDPKRYPDMADPLLRKNFSERGLNQAVAITSMCLQEEPTARPLISDVMVALSFLSMSTEDGIPATVPMESFRDKSMSIALSRHGSCSVTPFCISRKDVGNKSSSSSDSEDEEEEKEQKAEKEEESTSKKRQEQEETATDSDDESDSNSEKDQEEEQSQLEKARESSSSSSDSGSERRSIDETNATAQSLKISYSNYSSEEEDNEKLSSKSSCKSNEESTFSRYDSGRDHDDSSRNTSMRINSLAHDDKEEDEEENHETRSYSDHDDSPRNTSMRINSLSHDDDEEEEEENHQTRLEHIHSSKSEDQSVYSDDDAGESGESSLHRIEAKEEEHISSDHD
What is the function of this protein?
Involved in pollen tube guidance into micropyle.  Participates in perception of the ovule-secreted peptide signal LURE1.
What are the official names of this protein?
Receptor-like kinase LIP1, Protein LOST IN POLLEN TUBE GUIDANCE 1, AtLIP1.
What is the protein family that this protein belongs to?
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
What are the subcellular locations of this protein?
Cell membrane; Lipid-anchor. Cytoplasm. Note=In pollen tubes, mainly located in the plasma membrane to the tip region.
Protein: GLPB_HAEDU
Sequence: MNFDVVIIGGGLAGLTCGIALQKQGKQCAIINNGQAAIDFSSGSMDLLSCLPSGQKVHVFCEAFSELSQQAPEHPYCLLGQHQVVAKVQQFEQFMQELGLVGSHKQNHLRVTPLGGLRHTWLSPKSVPVIAENEHFPYRQIAILGIEGYHDFQPQILVDNLKQNAAFSHCDFSIGYLNIPELDYLRQNAREFRSVNIAQLLEHKLAFEDLVQEIKQAAGNAQAVFLLACFGLDDQRFFDSLKQATALALFELPTLPPSLIGIRQYRTLRDQFEKLGGLLLNGDRAVRAEFDGDRVARIFTTLHQEESINAAHFVLASGSFFSNGLVAEFERVKEPIFDLDIIGNKAFINSERVSWTDKRFAAAQPYQSAGVAINHHCQVYKNGHLIPNLYAIGNVIGGFWGIEQGCASGVSVVTALTVAEWVGGTK
What is the function of this protein?
Conversion of glycerol 3-phosphate to dihydroxyacetone.  Uses fumarate or nitrate as electron acceptor.
What are the official names of this protein?
Anaerobic glycerol-3-phosphate dehydrogenase subunit B, Anaerobic G-3-P dehydrogenase subunit B, Anaerobic G3Pdhase B.
What is the protein family that this protein belongs to?
Belongs to the anaerobic G-3-P dehydrogenase subunit B family.
Protein: CD28_RAT
Sequence: MTLRLLFLALSFFSVQVTENKILVKQSPLLVVDNNEVSLSCRYSYNLLAKEFRASLYKGVNSDVEVCVGNGNFTYQPQFRPNVGFNCDGNFDNETVTFRLWNLDVNHTDIYFCKIEVMYPPPYLDNEKSNGTIIHIKEKHLCHAQTSPKLFWPLVVVAGVLLCYGLLVTVTLCIIWTNSRRNRLLQSDYMNMTPRRLGPTRKHYQPYAPARDFAAYRP
What is the function of this protein?
Involved in T-cell activation, the induction of cell proliferation and cytokine production and promotion of T-cell survival.  Enhances the production of IL4 and IL10 in T-cells in conjunction with TCR/CD3 ligation and CD40L costimulation.
What are the official names of this protein?
T-cell-specific surface glycoprotein CD28.
What are the subcellular locations of this protein?
Membrane; Single-pass type I membrane protein.
Protein: UAT1_USTMA
Sequence: MVVKRILPLPRPAGLAPPTEVPLDGQDLAMPKMVMHCIWFFLASSQPSLESTSLQELEQAFTLGMQLFLARFPAAGARTRHDKDTARWYLEYNDQGADLEVIQLDRPLQDDWKALDGKCDSVFAPRPVMIFDDDASIFSIKVTRLSCGSVAISTSTHHWLVDFVGYIDLMEELSHCVSIFLNDPNAQINIDEGATKFDWSRDLLAYSKQLEPESIPSATWFTERGSPPQMTRAPSSCHYASLLFTQESLEKLKRSLAEWALETAPTTATDRIVPSKDNWIATNDALHALLWAAITDARGLDLNATTQLHTPLDGRRLLSSLSSADSQSRGKYIGNVHPGHVFPLPSSVVSAKDRSGLFNLAWLIRTQYLNVTPGQMSAIIRHHNYTDAETFGPGRLPKCTSMFGNDVTISNVARIPVRQRLDFGEKLGKPYTLTVVGMVPVTLNGLTLDSADGTCFIIQAPAEWTSKEAVLQHQPRSGDNQAPGGMLVYVGMRSEEMDKLLQNSLLQEFALVL
What is the function of this protein?
Acyltransferase; part of the gene cluster that mediates the biosynthesis of the glycolipid biosurfactant ustilagic acid (UA) (PubMed:15932999, PubMed:17850255).  UA is a secreted cellobiose glycolipid that is toxic for many microorganisms and confers biocontrol activity to U. maydis (PubMed:15932999, PubMed:17850255).  UA consists of 15,16-dihydroxypalmitic or 2,15,16-trihydroxypalmitic acid, which is O-glycosidically linked to cellobiose at its terminal hydroxyl group (PubMed:17850255).  In addition, the cellobiose moiety is acetylated and acylated with a short-chain hydroxy fatty acid (PubMed:17850255).  UA biosynthesis starts with omega-hydroxylation of palmitic acid catalyzed by the cytochrome P450 monooxygenase cyp1 (PubMed:17850255).  Terminal hydroxylation of palmitic acid precedes subterminal hydroxylation catalyzed by the cytochrome P450 monooxygenase cyp2 (PubMed:17850255).  Sequential glucosylation of the hydroxy fatty acid is probably catalyzed by the glycosyltransferase ugt1 (Probable).  The cellobiose lipid is further decorated by acetylation of the proximal glucose residue and by acylation with a short-chain beta-hydroxy fatty acid at the distal glucose residue (Probable).  The acyltransferase uat1 may be a good candidate for catalyzing either acetylation or acylation of the cellobiose lipid (Probable).  The fatty acid synthase fas2 may be involved in synthesis of the carbon backbone of the short-chain beta-hydroxy fatty acid esterified to the cellobiose disaccharide (Probable).  The secreted UA consists of a mixture of both alpha-hydroxylated and non-hydroxylated glycolipids; therefore, alpha-hydroxylation of the long-chain fatty, catalyzed by the fatty acid hydroxylase ahd1, occurs late in UA biosynthesis and may be the last step before secretion (PubMed:17850255).
What are the official names of this protein?
Acyltransferase uat1, Ustilagic acid biosynthesis cluster protein uat1.
What is the protein family that this protein belongs to?
Belongs to the plant acyltransferase family.
Protein: MDM12_COCIM
Sequence: MSIDINWEAATSGPDGEALAERIRSFIHDKFQQIALPRFIRSVEVNSFDFGTIKPELQIKDLCDPFEDFYEEDEDNEIGDGEVSDIQDRSPKPRPSSAGNERSAADAWQAEHPAFLDDRLCGRIEPHDVPIPSKEDPLASRPIRSPMSFGDPLNPYFFPRAGTPGIPGGTSNLGYYYMPLGGISGTQTPLSSVPRGPFSPGLRDASVFGEPSNSQRPNPSGPARRQSEIDIDTGNSRPSTADTLDSLNIHGIPDPVLPRSSDDAHPNVLPRRDNSPAPRRVREKRPEDLQVLCRLRYNGNIRLSLTALVLLDYPMPNFVGLPLKLNITGLTFDGVAVVAYIRKRVHFCFLSPEDADTLFGADDTNEAGHLQSRDSLAGGINDTSYSSRRPHDSLLRDVRVESEIGRKEDGKQVLKNVGKVEKFVLEQVRRIFEEEFVYPSFWTFLV
What is the function of this protein?
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria.  Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria.  MDM12 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10.  The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all mitochondrial outer membrane beta-barrel proteins, and acts in a late step after the SAM complex.  The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex.  Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
What are the official names of this protein?
Mitochondrial distribution and morphology protein 12, Mitochondrial inheritance component MDM12.
What is the protein family that this protein belongs to?
Belongs to the MDM12 family.
What are the subcellular locations of this protein?
Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids.
Protein: CWO_DROME
Sequence: MEPYWNETNGHAAHPVKYESEAAVSSFPYCTESSLNFSTSATAYSEDDAEYATGRRNKTSRQDPLSHRIIEKRRRDRMNSCLADLSRLIPPQYQRKGRGRIEKTEIIEMAIRHLKHLQSECQQKESDYRSGYMDCMKEAAKFLYDVHMQDFCHRLLGRLQEHIDEMFKTDCYKSTRSCHMPDNVSASSGSPHQAYHPPLCHLRDMLATSASDVEHSQDHNDVKDLSFRNHLNQLQRSQQAAAAAAVAAAAVAVANGSSPASNAGVDSKVPLTNGGGTGGAPPAADNVPSNSTGSGSAAACAGGNSNSSGSNSSNAASSTICPPAGGSCPAKVTPLAAHQQPHQAPVITSTAPHHHHHHTDSSHHDFESSREPILHTDTSNMHSPPPRDLLLQQHPHLAHSHHTQDSLMSVRMRNYSESSHEIEHNNNYKYKNHIKERFVHELHDEETSSEHCPVAAHLQSDHSHLQALSEHSKDGTEPEIAPIMAKKRKLAEAAANGEIPLEVHTESSNAGASSANRLDKPSPSFNFSDIKDIKAELHNGNSNSSPLLAKLSAVAAAGGQLSTPSSTTAPLPPRHTFTVPIFALHGQGNYYVPLNVDYNALVPFLNGMDLLEKSYTSMPVVHPININVNFMPSSPSASLLAAAAAAAVAVGKQQQQQAVVAAGAGLPLSTNSAAAQAAAVAAAAVAKAKLEQAMNQSW
What is the function of this protein?
Plays a role in the regulation of circadian rhythms (PubMed:17555964, PubMed:17578907, PubMed:17578908, PubMed:27814361).  Transcriptional repressor which inhibits Clock-mediated transcriptional activation by binding to E boxes in the promoters of Clock target genes and repressing their transcription (PubMed:17555964, PubMed:17578907, PubMed:17578908, PubMed:27814361).  E box binding activity is time-dependent with higher binding activity seen in the early morning (zeitgeber time 2) than early evening (zeitgeber time 14) and is dependent on the presence of the circadian protein per (PubMed:27814361).  It is likely that per binds to Clock-cycle heterodimers, reducing their affinity for E box binding and allowing cwo to bind instead (PubMed:27814361).  Negatively regulates its own expression (PubMed:17578908, PubMed:18375860).
What are the official names of this protein?
Transcription factor cwo, Protein clockwork orange.
What are the subcellular locations of this protein?
Nucleus.
Protein: DNAA_RICB8
Sequence: MNTNQIILTNQNDNSVNVWSNVTQDLYNYYGEALYNSWFSKVNFIESSLNTVILCAPTNFIRDWIKSKYSVVILQLFQHYNNAIKTVEIITKELPASNQATLELPTKTFADIGSSELNSENIFSTFDIRFTFDNFVVGAPNELAYAAARAVAESSSAVSESNPLFLYGGVGLGKTHLMHAIGWYIKQNNPSRKVIYMSAEKFMYQFVKALRNKEVMSFKEKFRSVDVLMIDDIQFICGKDSTQEEFFHTFNTLIDNNRQMVISCDRSPSDLDDIEDRIKSRLGWGLVADVHSTTYELRLGILESKIEQMNVKVPKDAIDFLASKIVSNVRELEGALNKVIAHSNFTAKEITLENTQNILRDLLRSNERIITVEDIQKKVANRYNIKLSDMSSPRRMRTIARPRQIAMYLSKILTPKSLVDIGKKFGKKDHTTVMHAIKKVEELLESDLELREEINLMMKILQN
What is the function of this protein?
Plays an important role in the initiation and regulation of chromosomal replication.  Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'.  DnaA binds to ATP and to acidic phospholipids.
What are the official names of this protein?
Chromosomal replication initiator protein DnaA.
What is the protein family that this protein belongs to?
Belongs to the DnaA family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: ATPD_CYAP4
Sequence: MKQTTVGAEILEPYAEALMSLAQSNNLTGRFGEDVAFILDLLKTSPELQQVLANPFVKPESKKAILRQLVAPQVHDFVLKFLLLLVDRRRIFLLEPICKQFQALLRKLTNTVLAEVTSVVELTEPQRQAVIEKVKTMTGSQQVELETRLDPELIGGVIVKVGSQVLDSSIRGQLRRISNTLTSFT
What is the function of this protein?
This protein is part of the stalk that links CF(0) to CF(1).  It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
What are the official names of this protein?
ATP synthase subunit delta, ATP synthase F(1) sector subunit delta, F-type ATPase subunit delta, F-ATPase subunit delta.
What is the protein family that this protein belongs to?
Belongs to the ATPase delta chain family.
What are the subcellular locations of this protein?
Cellular thylakoid membrane; Peripheral membrane protein.
Protein: RPIA_SHEB9
Sequence: MTQDEMKKAAGWAALKYVERDSIVGVGTGSTVNHFIDALATMKADIEGAVSSSEASTQKMKALGIPVYDLNSVDRLSVYVDGADEINDRMDMIKGGGAALTREKIVAAVAEKFICIVDNTKQVDILGEFPLPVEVIPMARSYVARQLVKLGGDPVYREGVVTDNGNVILDVYNLKILNPKELESQINEIVGVVTNGLFAKRGADVLLVGTPDGVKTFTAE
What is the function of this protein?
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
What are the official names of this protein?
Ribose-5-phosphate isomerase A, Phosphoriboisomerase A, PRI.
What is the protein family that this protein belongs to?
Belongs to the ribose 5-phosphate isomerase family.