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Database: UniProt
Entry: A8X6U0_CAEBR
LinkDB: A8X6U0_CAEBR
Original site: A8X6U0_CAEBR 
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
//
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