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Database: UniProt
Entry: A0A0B1TCV8_OESDE
LinkDB: A0A0B1TCV8_OESDE
Original site: A0A0B1TCV8_OESDE 
ID   A0A0B1TCV8_OESDE        Unreviewed;       672 AA.
AC   A0A0B1TCV8;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Glycosyltransferase family 28 protein {ECO:0000313|EMBL:KHJ93637.1};
GN   ORFNames=OESDEN_06446 {ECO:0000313|EMBL:KHJ93637.1};
OS   Oesophagostomum dentatum (Nodular worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Strongylidae; Oesophagostomum.
OX   NCBI_TaxID=61180 {ECO:0000313|EMBL:KHJ93637.1, ECO:0000313|Proteomes:UP000053660};
RN   [1] {ECO:0000313|EMBL:KHJ93637.1, ECO:0000313|Proteomes:UP000053660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OD-Hann {ECO:0000313|EMBL:KHJ93637.1,
RC   ECO:0000313|Proteomes:UP000053660};
RA   Mitreva M.;
RT   "Draft genome of the hookworm Oesophagostomum dentatum.";
RL   Submitted (MAR-2014) 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   -!- 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   EMBL; KN550675; KHJ93637.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B1TCV8; -.
DR   Proteomes; UP000053660; 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   InterPro; IPR035595; UDP_glycos_trans_CS.
DR   PANTHER; PTHR48043; EG:EG0003.4 PROTEIN-RELATED; 1.
DR   PANTHER; PTHR48043:SF23; UDP-GLUCURONOSYLTRANSFERASE; 1.
DR   Pfam; PF00201; UDPGT; 2.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 2.
DR   PROSITE; PS00375; UDPGT; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053660};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KHJ93637.1}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..672
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002065845"
SQ   SEQUENCE   672 AA;  74883 MW;  12715AA6CF37C7AC CRC64;
     MLLLPALSIL ITCCSSYKIL VYNRKSAYSH MNFLGKVADT LVDAGHDVVT LQPVIVPMGA
     NGTRKSRIIH VELDKKLAAD LMGDRKDNAK MWTNNAANPL LVLEHIPFMR GLTIATTKRI
     LDDKELLEQL KSENFDVGIA ELFDYGGIPV FEAIGLKNII GAHTLSCLSE ATAYAIGVPV
     IPSFMPASQG ITDDSTSFSN RAINLLFTYF SYYFQISIAD AAETVMMEKL GKAAVPVWDV
     VANMSWILTN TEPFLEFAKP TLHKVVDIGG IGVPKPKPLE EKWNKILNLR SRTVLISFGS
     MVKSKAMPYE YKTAIIELVK SYPDITFIWK YEDPDDAPFA AGVENLFLSQ WTPQNDLLAS
     QGITDDSTSF SNRAINLLFT YFSYYFQVSI ADAAETVMME KLGKAAVPIW DVVANMSWIL
     TNTEPFLEFA KPTLHKVVDI GGIGVPKPKP LEEKWNKILN LRSRTVLISF GSMVKSKAMP
     YEYKTAIVEL VKSYPDITFI WKYEDPDDAP FAAGVENLFL SQWTPQNDLL ADDRLTLFIT
     HGGAGSLLES ATSGKPVILI PLYGDQVRNA KLAIRHGFGI MLTKEDLGDS TLMHETVAKI
     LNDKKYTKAA HRIRNLLAKR PFSPEEKLLK TVELAVEFGP IPELYILDTG CYMFFCYLLG
     VPLLKDDFKG CI
//
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