ID   A0A0M3KAB7_ANISI        Unreviewed;       501 AA.
AC   A0A0M3KAB7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=UDP-glucuronosyltransferase {ECO:0000256|RuleBase:RU362059};
DE            EC=2.4.1.17 {ECO:0000256|RuleBase:RU362059};
GN   ORFNames=ASIM_LOCUS17315 {ECO:0000313|EMBL:VDK60087.1};
OS   Anisakis simplex (Herring worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC   Anisakis simplex complex.
OX   NCBI_TaxID=6269 {ECO:0000313|Proteomes:UP000036680, ECO:0000313|WBParaSite:ASIM_0001791301-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ASIM_0001791301-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDK60087.1, ECO:0000313|Proteomes:UP000267096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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         ECO:0000256|RuleBase:RU362059};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167,
CC       ECO:0000256|RuleBase:RU362059}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167, ECO:0000256|RuleBase:RU362059}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00009995, ECO:0000256|RuleBase:RU003718}.
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DR   EMBL; UYRR01033984; VDK60087.1; -; Genomic_DNA.
DR   WBParaSite; ASIM_0001791301-mRNA-1; ASIM_0001791301-mRNA-1; ASIM_0001791301.
DR   Proteomes; UP000036680; Unplaced.
DR   Proteomes; UP000267096; Unassembled WGS sequence.
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; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
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:SF143; UDP-GLUCURONOSYLTRANSFERASE; 1.
DR   Pfam; PF00201; UDPGT; 2.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS00375; UDPGT; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU003718}; Membrane {ECO:0000256|RuleBase:RU362059};
KW   Reference proteome {ECO:0000313|Proteomes:UP000267096};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU362059};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003718};
KW   Transmembrane {ECO:0000256|RuleBase:RU362059};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362059}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|RuleBase:RU362059"
FT   CHAIN           19..501
FT                   /note="UDP-glucuronosyltransferase"
FT                   /evidence="ECO:0000256|RuleBase:RU362059"
FT                   /id="PRO_5035330302"
FT   TRANSMEM        458..482
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362059"
SQ   SEQUENCE   501 AA;  56989 MW;  621E8093EAC34B35 CRC64;
     MILITCTQFL LVLTLAQAAN ILIYSPSYTK SHLISNGRMA DTLAEAGHNV VIFVPIMEPI
     HFNATKYAKI IRMENVFAFE AKMDQMKQDI FTKTITLKDR MEWVDISAKF CEAILKRKDD
     LDQLRKYNFD VGFSEQLEYC GVGIIRYLGI KNHIWVSSMP LLVTTTYTLG VPSPISWLEX
     VYVHRARMVL QTEKFRALID PNFPDLQDVA ADSAICFVNT DEFLDIPRPI LHKVIYVGGI
     GVPLKPSPLP EKFEKLMQKG DKGVVLFSLG TIVPSSAIPM NIRVDIIRAF SEFSDFHFLM
     RVDENDNETD QVIKDMGVGN VELIGWMPQS DLLGHPRMKL FIMHGGLNGM IETAIRGVPL
     LVIPFFGDQF HNGAAAEHRG IGLALQRNDL NYAQMKKALT QLLIDEKYLK AARRLSEMIC
     NKPNKPEEQL IKWTNYVIKY GPLPELQVEG AKFSVIKYFG LDIFAALLLL IVIVLAVIVR
     IIRRLVALFR RTRDYLRKKD V
//