ID   A0A1I0I3M8_9FIRM        Unreviewed;      1080 AA.
AC   A0A1I0I3M8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Glycosyl hydrolase family 20, domain 2 {ECO:0000313|EMBL:SET90858.1};
DE   Flags: Fragment;
GN   ORFNames=SAMN04489758_1792 {ECO:0000313|EMBL:SET90858.1};
OS   Thomasclavelia cocleata.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Coprobacillaceae; Thomasclavelia.
OX   NCBI_TaxID=69824 {ECO:0000313|EMBL:SET90858.1, ECO:0000313|Proteomes:UP000198558};
RN   [1] {ECO:0000313|Proteomes:UP000198558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1551 {ECO:0000313|Proteomes:UP000198558};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC       {ECO:0000256|ARBA:ARBA00006285}.
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DR   EMBL; FOIN01000079; SET90858.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0I3M8; -.
DR   Proteomes; UP000198558; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd06564; GH20_DspB_LnbB-like; 1.
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; 3.10.20.320; Putative peptidoglycan bound protein (lpxtg motif); 1.
DR   InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR015883; Glyco_hydro_20_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR029018; Hex-like_dom2.
DR   InterPro; IPR015882; HEX_bac_N.
DR   InterPro; IPR009459; MucBP_dom.
DR   PANTHER; PTHR43678:SF1; BETA-N-ACETYLHEXOSAMINIDASE; 1.
DR   PANTHER; PTHR43678; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00640)-RELATED; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF07554; FIVAR; 3.
DR   Pfam; PF00728; Glyco_hydro_20; 1.
DR   Pfam; PF02838; Glyco_hydro_20b; 1.
DR   Pfam; PF06458; MucBP; 1.
DR   PRINTS; PR00738; GLHYDRLASE20.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SET90858.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198558};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..1080
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011526111"
FT   DOMAIN          774..921
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   ACT_SITE        345
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
FT   NON_TER         1080
FT                   /evidence="ECO:0000313|EMBL:SET90858.1"
SQ   SEQUENCE   1080 AA;  121801 MW;  B5DBB7AD09FC3F4C CRC64;
     MQGNIKKLKK APLSLLLVAS IVLSNGSYLI QAKDNTPIVY SQEVSNLTDE QLASLTNPIL
     QQYTADESHK IWRMTSDTRL AILANQENLD NERLAEIVKL VNSEFMEKEI VSSAPFAMVY
     AQEKDAGYGD VLITIDDVSS ITEETTSEEA YKIEIDDNGV RLTGASETAV LYGLRTIQNL
     MITNNGLVYG TIIDYPYIAE RRLHVDCARK YISKDWFIRQ IREMSYLKMN AIQMHFSENL
     GFRIECETDP SIVSDQYLTK DEVREILQEA KKYGVKVIPS FDSPGHVDQI LRAHPEYGQV
     NSSGEHFASG LDVTNPEAIA YIRSLYSEYM DLFEGCTDFH IGGDEYMEFD RAPFTTQYKS
     VLDNYAKANI DPNATWKDVL ANYINELAEF VHDRGFTPRI WNDGIYYGEN SYYENPQMIK
     MHDYIGIDFW SQMSWNSSIA RLNTFIQKGH DTIYNINASF FYYVLRNSKP TDGREQHSFD
     NLNADRKIFN EWTPGKFQEN TVADDSDFIK GASIAIWCDN PNLVDEDVIT DDVSDELRAL
     ASKSWNVRSN QITTFEQFQD NYEKLGNVAG FEKQSQLPDS GEFLLAEDLG KVTLKYVSES
     GKVLKNDVVK YGTVGEDFEF SGDNIYGYRL KSDQAVSGKY TKEGVTFTFV YELYCDKTEL
     ANEINNPLLS ENYIRETISD YNSLYQTAKE VYLDENSEQL AVDEALADLV SAKNKVVELK
     YYPLYIEANY PLKDKGYTTG YSQYQSVVAN AKNVLYSEDL TVEKMNEALA AIQTAKDGLM
     LPDGNVPSVS ATDDYYSVGV YPSNKYSYDK MLDNDESTKC WFNKAQEVGT EIVFSFTEPV
     NMSSVRVLTP SDAGGDAIVA ADIQISMDNE NWTTVGSFDD SKLDNTVSFD QTMVKYVRIL
     LTEAKSNWYQ IAEVNFTFEQ VPEDNTLRDL IAEAKEIDLE GKDIEAVADF VDALIEAQKV
     YAENSLETQV VEEALQNAIN NLEKEVTVSK TALSIAVEMA SNVTEADLEN VVPAVVTEFN
     AALEEARAIL ANDNATQEEV DASFARLATA MHMLEFLKGD KAELQDLVDS TAELVEGNYT
//