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Database: UniProt
Entry: A0A016VW86_9BILA
LinkDB: A0A016VW86_9BILA
Original site: A0A016VW86_9BILA 
ID   A0A016VW86_9BILA        Unreviewed;       518 AA.
AC   A0A016VW86;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EYC31670.1};
GN   Name=Acey_s0003.g1177 {ECO:0000313|EMBL:EYC31670.1};
GN   ORFNames=Y032_0003g1177 {ECO:0000313|EMBL:EYC31670.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC31670.1, 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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:EYC31670.1}.
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DR   EMBL; JARK01001339; EYC31670.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016VW86; -.
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; 2.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   PANTHER; PTHR48043; EG:EG0003.4 PROTEIN-RELATED; 1.
DR   PANTHER; PTHR48043:SF23; UDP-GLUCURONOSYLTRANSFERASE; 1.
DR   Pfam; PF00201; UDPGT; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   4: Predicted;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024635};
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..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..518
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001493988"
FT   TRANSMEM        484..507
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   518 AA;  58973 MW;  4DF6E89C42987D0A CRC64;
     MLKLQFLLLL HLQLADSYKI LIYSAPLGYS HIKFMGRIAD ILQEAGHDVT VLHQVQDQKY
     IPAVSTLTKQ ILHDLPENLQ DKMRPKSFNL WSKESTSLLT HLSLIDTFTQ FHADACDLLL
     GDNHTMDTLR NEHFDVGITE TIGACGFGLF ELVGVDHIVC TSAIGVTDSM VSLFDLPNLP
     SIVPSIFTPH TDKMNFLERT INFVSTFITT TATTQWMAKY ERVWERHGSS LKARDYYDKV
     NYLLSNSDEF LDFARPATPK IVHIGGVTIP EKTELPEELR VLMERKDREG VVYISFGSFV
     PTSQMPGYFR DAIFHVAKTF PQITFIWKID ANDTVSTTIP NLHTFTWLPQ LSILDHPNLR
     CFVSHGGLNS VLEVTRSGKP SILVPIFGDQ FRNARLVKAK NTTILITKED FNSETFEAAL
     RQILSDDSFS VRAKRLASLM VNKPFPLKER LLSTIEFSTR HGKISNLDIN IRELNTLQYY
     SIDVVTFLTT LVVLLVASFV QLCRFCFKVL FVRKLKRE
//
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