ID W2TUW5_NECAM Unreviewed; 308 AA.
AC W2TUW5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETN85434.1};
GN ORFNames=NECAME_06387 {ECO:0000313|EMBL:ETN85434.1};
OS Necator americanus (Human hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae; Bunostominae;
OC Necator.
OX NCBI_TaxID=51031 {ECO:0000313|EMBL:ETN85434.1, ECO:0000313|Proteomes:UP000053676};
RN [1] {ECO:0000313|Proteomes:UP000053676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24441737; DOI=10.1038/ng.2875;
RA Tang Y.T., Gao X., Rosa B.A., Abubucker S., Hallsworth-Pepin K., Martin J.,
RA Tyagi R., Heizer E., Zhang X., Bhonagiri-Palsikar V., Minx P., Warren W.C.,
RA Wang Q., Zhan B., Hotez P.J., Sternberg P.W., Dougall A., Gaze S.T.,
RA Mulvenna J., Sotillo J., Ranganathan S., Rabelo E.M., Wilson R.K.,
RA Felgner P.L., Bethony J., Hawdon J.M., Gasser R.B., Loukas A., Mitreva M.;
RT "Genome of the human hookworm Necator americanus.";
RL Nat. Genet. 46:261-269(2014).
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}.
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DR EMBL; KI657725; ETN85434.1; -; Genomic_DNA.
DR RefSeq; XP_013307661.1; XM_013452207.1.
DR AlphaFoldDB; W2TUW5; -.
DR STRING; 51031.W2TUW5; -.
DR EnsemblMetazoa; NECAME_06387; NECAME_06387; NECAME_06387.
DR GeneID; 25346419; -.
DR KEGG; nai:NECAME_06387; -.
DR CTD; 25346419; -.
DR OrthoDB; 382054at2759; -.
DR Proteomes; UP000053676; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR InterPro; IPR002213; UDP_glucos_trans.
DR PANTHER; PTHR48043; EG:EG0003.4 PROTEIN-RELATED; 1.
DR PANTHER; PTHR48043:SF159; UDP-GLUCURONOSYLTRANSFERASE; 1.
DR Pfam; PF00201; UDPGT; 2.
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:UP000053676};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 269..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 308 AA; 35505 MW; F635FE02A5BFF1B6 CRC64;
MNEFGLCQRY SYFQYSQAAT RFLPGADEKW NIFVKRGAAE NRCAELLQVQ ASNSQLKEKT
LVSIKMTYLA RTCISSSGFH RRIYSTIQKP RHSSLTQATT AFRQELCRSV KSTTSQSIMF
QEAIHAGVPM ICLALFGDQP KNAKVTEKLG ISTNLRKTEI SLEKIATAIR EVLENDRYRY
PLDISRYCSP TCSDLQCKAK RKTLRMEPSN VFRYRATARR LARMVRKKPV SPKDLLIKWT
EFLAEFKTLE NLVPAGNKLN WIQYHSVDVV LFLATIMFSV ILIFYIVAKL VLALLCRRFE
QKDKEKIL
//