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Database: UniProt
Entry: A0A2G5T954_9PELO
LinkDB: A0A2G5T954_9PELO
Original site: A0A2G5T954_9PELO 
ID   A0A2G5T954_9PELO        Unreviewed;       526 AA.
AC   A0A2G5T954;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PIC23925.1};
GN   Name=Cnig_chr_V.g17453 {ECO:0000313|EMBL:PIC23925.1};
GN   ORFNames=B9Z55_017453 {ECO:0000313|EMBL:PIC23925.1};
OS   Caenorhabditis nigoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC23925.1, ECO:0000313|Proteomes:UP000230233};
RN   [1] {ECO:0000313|Proteomes:UP000230233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA   Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA   Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT   "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT   competition proteins.";
RL   Submitted (OCT-2017) 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   -!- 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:PIC23925.1}.
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DR   EMBL; PDUG01000005; PIC23925.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5T954; -.
DR   STRING; 1611254.A0A2G5T954; -.
DR   Proteomes; UP000230233; Chromosome v.
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:SF3; 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:UP000230233};
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..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..526
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013909015"
FT   TRANSMEM        482..506
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   526 AA;  59476 MW;  0C93C090E1FC06B4 CRC64;
     MKLVVFLLSF VQLAFSYNFL VFCPLFGHSH TTYFAKIADT LTDAGHNVTF FTPTIMRRFS
     KHAYLKSTKN VIHLEPSEKL AILGDKFEAG DTSQFWVSDS TLLKALPVMD TFTRAFEEQT
     AVLGRNLELL DKLKAMKFDA MIFESFVIPA YALLDYLEIP TILPATSIAY DEILARSIGE
     PIMTSAVPAL SSAFTDQMTF VQRIVNTMSS HLKSLIMPKR EFKSLRFPHS TIEISSQGSM
     SSFVFTNSNP YLDYARPTIE KNVQIGGISV DVDQLKSQKV NEDWGEILNL RTKTMLISFG
     SIMLSKDMPL ENRIALVSTM DKFPEVTFIW KYESNDTDEF AKGVKNIHFS NWIPQTALLA
     DSRLSAFFTH AGLGSTNEVS YLGKPAILCP IFADQMRNAK MLARHNGSVE ISKYELGQSE
     KLEEVFKKIL YDQSYTTASE NLALQLANQP VKPRELLVRH AEFAARFGRL PSLDPYSRQM
     SFVSYFLIDV AATLFLISSL ILYMVFKIAR KPINYLFITP VKSKTN
//
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