ID A0A158Q3M9_DRAME Unreviewed; 820 AA.
AC A0A158Q3M9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Protein O-GlcNAcase {ECO:0000313|WBParaSite:DME_0000272001-mRNA-1};
GN ORFNames=DME_LOCUS7080 {ECO:0000313|EMBL:VDN57107.1};
OS Dracunculus medinensis (Guinea worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000272001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:DME_0000272001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN57107.1, ECO:0000313|Proteomes:UP000274756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; UYYG01001158; VDN57107.1; -; Genomic_DNA.
DR STRING; 318479.A0A158Q3M9; -.
DR WBParaSite; DME_0000272001-mRNA-1; DME_0000272001-mRNA-1; DME_0000272001.
DR Proteomes; UP000038040; Unplaced.
DR Proteomes; UP000274756; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; IEA:UniProt.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR011496; O-GlcNAcase_cat.
DR PANTHER; PTHR13170; O-GLCNACASE; 1.
DR PANTHER; PTHR13170:SF16; PROTEIN O-GLCNACASE; 1.
DR Pfam; PF07555; NAGidase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000274756};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 794..819
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..298
FT /note="Beta-N-acetylglucosaminidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF07555"
FT REGION 433..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 820 AA; 93903 MW; 5BE9E9890FC6C7F1 CRC64;
MENFKSFEKM KRLFIYQLSA KKPIVHGFYG RPWANDQRQE LFRWMQKFGM NTYLYAPKDD
IKHRYDWRKL YTTEELDLLQ SLINAAKEYK ITFVYSLSPG LDITYSSDKE VQAIKDKFDQ
VKSIGCEAFA LLFDDVDAIM HEVDKSKFSS FAMAQVTVTN LIYEYLKCPV FYFCPTEYCE
SRAFPSLQES EYLSFLGKKL LPDIYIFWTG PRVVSRSITI EHMRSVADIL KRKPVIWDNL
HASDYDAKRI HLGPFTGRSV KLKDEIAGLL MNPNCRLEAN FVPLHTVAEW NLCEDDAELD
GAFDSDAILE AGDIAVVAAY IVEGDKSKRL YHPLNALNEA LKKWYERLFT EVEITPSCQM
ETEALTSIVE KPPFLDSNTG RPLYKNLGNM LTQSSSDPQM KPTICAMNSL SPDYSEPMDL
ITLAKDEPKI LVDSDSSNKM NNQDMVDTSS DVSMESSITT DSGGSVQPEH LAMFVDLYYL
PFEHGRSCIQ ILEEFTWLHE NSFVIKKKKE ASENKNVQTI INEDWKRRCD SLLRLLHNLT
KFYQLLTALP NKAAVQDLFQ YVYEIQGIAS MLEVILLWMA DGGLTSAPRD SDYFWRKPMI
DGEPWIVSGG SVSDLLKLLF VTPNIMDLIT LKSVIPLFLN CLTMRPYRDK DEKEIYSLYA
QDDSLSTNFD FSNDCKSEQS FDSQIVPFLS HSEPRISFVA VENSSYGKRI TAFSCAVLKA
KEFSKNVQNA YTSKTQLNYE ASPEMEENDC IEGSKLQSEE IDSCVSLQLS DQFYEHFPSQ
VEIRWRSTNH DAVAVRRLIC ASAAALSFNG LIFLILIILF
//
