ID A8X6U0_CAEBR Unreviewed; 943 AA.
AC A8X6U0;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Protein CBR-UGT-63 {ECO:0000313|EMBL:CAP28351.2};
GN Name=ugt-63 {ECO:0000313|WormBase:CBG08680};
GN Synonyms=Cbr-ugt-63 {ECO:0000313|EMBL:CAP28351.2};
GN ORFNames=CBG08680 {ECO:0000313|WormBase:CBG08680}, CBG30582
GN {ECO:0000313|WormBase:CBG30582}, CBG_08680
GN {ECO:0000313|EMBL:CAP28351.2};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP28351.2, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP28351.2, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP28351.2,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor
CC beta-D-glucuronoside + H(+) + UDP; Xref=Rhea:RHEA:21032,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:132367, ChEBI:CHEBI:132368; EC=2.4.1.17;
CC Evidence={ECO:0000256|ARBA:ARBA00000301};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; HE601197; CAP28351.2; -; Genomic_DNA.
DR RefSeq; XP_002636378.1; XM_002636332.1.
DR AlphaFoldDB; A8X6U0; -.
DR STRING; 6238.A8X6U0; -.
DR GeneID; 8578373; -.
DR WormBase; CBG08680; CBP46238; WBGene00030430; Cbr-ugt-63.
DR WormBase; CBG30582; CBP42754; WBGene00270636; -.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_311514_0_0_1; -.
DR InParanoid; A8X6U0; -.
DR OrthoDB; 2879294at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR CDD; cd15489; PHD_SF; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR InterPro; IPR002213; UDP_glucos_trans.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR PANTHER; PTHR48043; EG:EG0003.4 PROTEIN-RELATED; 1.
DR PANTHER; PTHR48043:SF84; GLUCURONOSYLTRANSFERASE; 1.
DR Pfam; PF00201; UDPGT; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..943
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002732956"
FT REGION 664..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..733
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..780
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 943 AA; 108169 MW; 04F1EBFEF59F5DC2 CRC64;
MDIHMIIITF FINLLFLHIV ESARVLLTVM DQGRSHATSI NTFMHRLQKD NHTTALEFAW
FHPDIDFGMD ERFIDMKGFD NPFASPDFDK IAFEEDYSFI HQAVAYGFGS KTCDNILKHK
KERFNEILSE DWDLYLSDSL FAVCGYGMAE ISGKPHVMMH STDLESAQGS FKAFSRNYAT
FVPSNLPFTM LDFSVTKYFH RIWAAYDWFG SFIFTAFVGN FAQKWALRSI IPFPYFSFSE
YNRRSSYSFT DMPDSLFPPA SRTNDFFSFG AYCKPSSTPL PSDFLSFIDD PKSKGTILIA
FGTFIDWRRA PKHYYDTFST IVNQLTDYRV IWSMKGERPP GLRDHVKTSS WVPQNQILHH
NKTVLFLSHG GLKSTKEVIC SATPTIFVPM FGEQTRNSWL IKEKGFGRIM NKFNINVKEL
GTHVREVLEH PTYQDKANKF LTYYMDQPIP TLDEGAFRFS KLLKYGGRMP AFFYPRALDL
SHITVLNLDL AILVFFFDGT KRQNLEKLVG WLRLQFRNHI TASVETALQM VLRSELLFQL
NRYLGGLLRF RNGNGGRSMY VDCLVDTPDN EEARLEINEG VRREIPRIDR PIAENRGRMT
TEYYEDISPP TRQPVPEPVD SFDQKMARNL NSAVTYVGPA RRFGPSLVPR EESATDYFVA
DVPSTSSSFP DWPALSNPQP HCSRQPDPAA SNSSHTLPPR TQCAERVQTP LTESDVIQEY
DQFSEDDEPT LGDDLESLTP IRENIPPLQN VPMESQRAPR NADIRDNNAN DSEKTIPHNQ
SDSESYEIFS EFQSISALIL PKELMEGVYK SLAKNDVPEK SHDQQAEFIM GKLFPKRSPP
VNASMYRTGD NKVLGFQNSD THRIWLTPIE NQVIFLNGKL VACEPRKLGI CEICASYKFS
NHETLRCDSC KRVFHAKCFA VRAQRKGKCI CRARLCPEKN PYV
//