ID A0A1I7SZ19_9PELO Unreviewed; 998 AA.
AC A0A1I7SZ19;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Glucuronosyltransferase {ECO:0000313|WBParaSite:Csp11.Scaffold37.g195.t1};
OS Caenorhabditis tropicalis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold37.g195.t1};
RN [1] {ECO:0000313|WBParaSite:Csp11.Scaffold37.g195.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000256|ARBA:ARBA00009995}.
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DR AlphaFoldDB; A0A1I7SZ19; -.
DR STRING; 1561998.A0A1I7SZ19; -.
DR WBParaSite; Csp11.Scaffold37.g195.t1; Csp11.Scaffold37.g195.t1; Csp11.Scaffold37.g195.
DR Proteomes; UP000095282; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd03784; GT1_Gtf-like; 2.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 4.
DR InterPro; IPR002213; UDP_glucos_trans.
DR InterPro; IPR035595; UDP_glycos_trans_CS.
DR PANTHER; PTHR48043; EG:EG0003.4 PROTEIN-RELATED; 1.
DR PANTHER; PTHR48043:SF103; UDP-GLUCURONOSYLTRANSFERASE; 1.
DR Pfam; PF00201; UDPGT; 2.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 2.
DR PROSITE; PS00375; UDPGT; 2.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..998
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009306875"
FT TRANSMEM 498..519
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 998 AA; 114752 MW; ACB87D6951B32FFA CRC64;
MLQSVFSLLL VLSFFGNVSS YNFLVISPVY GFSHMKYMAA VANHLARAGH NVTYFQPFVV
DDYHKHNLIE EDSIEIWNYY HDEIGMKHIP PQGCMKAAWD SSMYQSDVGA AFLLSKYLYP
AFEHMCRKMF EDTDLHSEMI GRRFDVVLSE AFDFCGLYLA SYLEMPSIIS TFTGNRLNAL
APVLGEPSFL HYLPAPTSQY GEEASIWDRA NDIWHKIFSS YGFAQLFDLQ YQQVQKLTNG
KVKHWKEIIH DVTYHFSNSN PYLDFVIPTI SKVIPIGGIT VDQNNWDMGN NHSVGLEDLL
NERKHNIFIS FGSMVRSVDM PAEYKDAMLK VFLDHPNITF LWKYEVPNDR ELLQKLPKNV
HLAKWFSQNA LLSDRRVDLF ITHGGLGSTM ELANAAKPAI VIPLFADQPG NAKMISRHRS
VEVYSKLDIP NWRKLSNLIR KMINSDVYQE HADRLADTLR FQPIAPAELM VKHAENAARF
GKMPNLVPYA KDMGFVEYYN LDLTLIIILP MFCLILIILN TFGNAYNFLV ISPVYGFSHM
KFLANVANQL ADAGHQVTYF QPFVIEAYQN HNLLKNNSIE VINYYHDEEG RKHIPPANDL
HDAWYSGKYQ SALASVFDMP QFLFSAWEHM CRKVFQDKEL HEILKSRNFD VVIAETFDFC
GLYLADYLDS KSIISVFTGS RLLSIMTPLG EPSWLHYLPA PSSSSFGPGS SIFDRLNDLY
HKYVFGSGYA ILFDWQYNQI SRLTGGKVRL WKKILQDVTY HFSNSNPYLD FSVPSIPKVI
PIGGFDMDES IHSELPVEYE EILKKRPITV FVSFGSMVKS KFMPDSYKES MLKLFSINYQ
NITFLWKYED PNDQFLVNRL PENVILKDWF PQRALLSDDR VKLFITHGGL GSAMELAYAA
KPAIMIPLIA EQPDNGKMLE RHGSVEVYSK YDIPNWEKLN NVLHRMLTEN SYQKSANRLA
HVLLNQPIKP RELMLKHAEM AAKFGKLPEL TPRVQEMV
//
