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Database: UniProt
Entry: A0A016WFS3_9BILA
LinkDB: A0A016WFS3_9BILA
Original site: A0A016WFS3_9BILA 
ID   A0A016WFS3_9BILA        Unreviewed;       450 AA.
AC   A0A016WFS3;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=UDP-glucuronosyltransferase {ECO:0000256|RuleBase:RU362059};
DE            EC=2.4.1.17 {ECO:0000256|RuleBase:RU362059};
GN   Name=Acey_s0741.g1979 {ECO:0000313|EMBL:EYC38122.1};
GN   ORFNames=Y032_0741g1979 {ECO:0000313|EMBL:EYC38122.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC38122.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EYC38122.1}.
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DR   EMBL; JARK01000341; EYC38122.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016WFS3; -.
DR   Proteomes; UP000024635; 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:SF62; GLUCURONOSYLTRANSFERASE; 1.
DR   Pfam; PF00201; UDPGT; 1.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003718}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..450
FT                   /note="UDP-glucuronosyltransferase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012000214"
SQ   SEQUENCE   450 AA;  51175 MW;  1E449739AAC924D7 CRC64;
     MRLSLVVLLW TSSDAAKIIF NGMHSSDSHI ASMLPLATRL AQEHHSIHFL ETNTKSSHYR
     YPNNISFTHI QLKKDPYFLY VVLKVMWTKI YGPIEFPRVW QTGDNAFVET LEEHPQKVNP
     VIDEPWDLVF ADELFAVSSY ALAMRAQQRG RPFVTLSTCI PTNLLKYHLS LGTPFAMRPS
     MYHRNAVPYL IETFANRLHA VIQETWVAIR VQYVTAYNAV QGLNRIGIVD FDFSKLAKLS
     AYIFLDDVNS LVFPSSVGTE IIEVGFHCPR KEELSQEYLD FVNDPFSRGT ILIAFGSNVV
     WDYASDELME TVVVALNRLS EYRVVFSYNG DRKRVTLLGR HVKITRWAPQ KGILSHNKTV
     AFISHGGLKS LKDTICGGVP VVYIPLFAEQ SHNGEVARSA GFAETLSKTR LTSDLIEKTV
     RRVAECLCIC FHVKLTQELK KKENRARSLL
//
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