ID B1C4V1_9FIRM Unreviewed; 1363 AA.
AC B1C4V1;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=O-GlcNAcase NagJ {ECO:0000313|EMBL:EDS73695.1};
DE EC=3.2.1.52 {ECO:0000313|EMBL:EDS73695.1};
GN Name=nagJ {ECO:0000313|EMBL:EDS73695.1};
GN ORFNames=CLOSPI_02120 {ECO:0000313|EMBL:EDS73695.1};
OS Thomasclavelia spiroformis DSM 1552.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Thomasclavelia.
OX NCBI_TaxID=428126 {ECO:0000313|EMBL:EDS73695.1, ECO:0000313|Proteomes:UP000004910};
RN [1] {ECO:0000313|EMBL:EDS73695.1, ECO:0000313|Proteomes:UP000004910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1552 {ECO:0000313|EMBL:EDS73695.1,
RC ECO:0000313|Proteomes:UP000004910};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium spiroforme (DSM 1552).";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS73695.1, ECO:0000313|Proteomes:UP000004910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1552 {ECO:0000313|EMBL:EDS73695.1,
RC ECO:0000313|Proteomes:UP000004910};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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:EDS73695.1}.
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DR EMBL; ABIK02000015; EDS73695.1; -; Genomic_DNA.
DR STRING; 428126.CLOSPI_02120; -.
DR CAZy; CBM32; Carbohydrate-Binding Module Family 32.
DR CAZy; GH84; Glycoside Hydrolase Family 84.
DR eggNOG; COG1538; Bacteria.
DR eggNOG; COG3525; Bacteria.
DR HOGENOM; CLU_001501_1_1_9; -.
DR OrthoDB; 9760892at2; -.
DR Proteomes; UP000004910; Unassembled WGS sequence.
DR GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; IEA:UniProt.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR Gene3D; 1.20.1270.90; AF1782-like; 3.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 1.20.1270.70; Designed single chain three-helix bundle; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 1.20.58.460; Hyaluronidase post-catalytic domain-like; 1.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR015882; HEX_bac_N.
DR InterPro; IPR049019; NagJ-like_helical.
DR InterPro; IPR011496; O-GlcNAcase_cat.
DR PANTHER; PTHR13170; O-GLCNACASE; 1.
DR PANTHER; PTHR13170:SF16; PROTEIN O-GLCNACASE; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF07554; FIVAR; 4.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR Pfam; PF07555; NAGidase; 1.
DR Pfam; PF21774; NagJ_C; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF140657; Hyaluronidase post-catalytic domain-like; 1.
DR PROSITE; PS50022; FA58C_3; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:EDS73695.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EDS73695.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004910};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1363
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039183948"
FT DOMAIN 748..911
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
SQ SEQUENCE 1363 AA; 149430 MW; 8106EB7EB09C7EE3 CRC64;
MKSKAGKILK STLAASFAFS LVTANPVQIL AAPQESSDVK VDVYPKPQEI TYTSGEGMSL
VGEVNVVIHG EQESATLPKL EKILKENGIS YTISDKVDNS KANILISSTS EHCDECAENL
GGNIGALSEE QGYILSANND TNEKGEIKIV GADSDGAYYG LMTLTQMLEQ KTKDNKIAET
VISDYPSVKL RGFVEGFYGY PWSFEDRLSL MSESSDFKMN TYIYAPKDDP YHKDQWRELY
PDDKAEELRQ LAAEGKKDNM NFCWSVHPGN GFNYSTDADY NALINKFEQL YNLGVRQFGI
SYDDLGGYVN GQQHADLINR VNREWVKVKG DVDPLIVVGT RYCNGWGPSM TSYFKPFFST
LDDDVVVMWT GANTMSAITK DAYEWPKNQT GVTDKNLAAW WNYPVNDYCD GNLMMSPLEN
LDNDVDNLSG FFLNPMSQAE ASKVAIFSGA DYSWNIGGFE RTSSWVRAID ELVPEASESF
QRFADNISYI KDGFEFDESR YLVDTIEAFK AALQNKEGIV EAATALKDEF TRMDNDVDAL
RNIEDKNLYE EIEQHLNAYE AVAKAGISSM QAFIDAENGD VDACLSNINT TEIKLKEAET
YKVESLESNG TKMNVVKVCE KRIKPLLKDS VDQIKSNLMD NVFPQTQATV IGTMSGLADK
TVELTKGNYQ VSSIIGTMKA NETVGIALPK AMRVSNVSIT GNNLESLKVQ TSINGIVWED
VEGAIEDGTL KATVDATATC VRVVNKTTAS IDVTIDNIVV APVYNTGTKT VETDLGTYGN
NVIANALDGN INTKFYSSAG ATVGSYVRVD LGKEIPLYDT AIYYAGNPKG PSHGIDGFAA
TKMEISTDGV SWTQIGDIIK DENYQSKTVE GQLVSEAAFN ADGQMARYIR FSATESSDNW
VQVFEIPFNK TVDNLGDDSI DIIDTTITTG NVSNLYDRDL TSAFAPDSVV DEDTLTYAMT
SITNVGRLMI MQDPTSICNA TVSVKDVEGN WSDIGILDKG TNTFDVNKTI LEVKLTFHAN
NPTPSIYEII ASQKEVEEVN KTALKVAVDK ANAVTDEALI NVIPVVVEEF KAARDEANAI
YNNENATQTE VDNAVARLVE VMQKLEFYKG DKTTLKIALD LATTITDEDL ANVVPVVVEE
FKAALQQAKD VYDNVNATQA DVNNAFDRLA EAMHMLNFVK GDKTALKAFI DKVSGLEAVK
YTEATWTPFN DALTAATSVY EDVNAMQEEV NNAYNELVTA FLNLRLIPNK DLLGDLINQA
EGLESANYTK ATFDGLTKAL NEAKVVFDNP NATQKEVDNA KDVLAKAMAD LQTVTVDNTV
KTPVSNGDTT ASVKTGDDVN MLGTLGLISS LGAIAFLKKK KRN
//
