ID   A0A1I0C1K9_9FIRM        Unreviewed;      1796 AA.
AC   A0A1I0C1K9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Hyaluronoglucosaminidase {ECO:0000313|EMBL:SET12845.1};
GN   ORFNames=SAMN04489758_10215 {ECO:0000313|EMBL:SET12845.1};
OS   Thomasclavelia cocleata.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Coprobacillaceae; Thomasclavelia.
OX   NCBI_TaxID=69824 {ECO:0000313|EMBL:SET12845.1, 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FOIN01000002; SET12845.1; -; Genomic_DNA.
DR   OrthoDB; 9760892at2; -.
DR   Proteomes; UP000198558; Unassembled WGS sequence.
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: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; 2.
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; 2.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
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; IPR011496; O-GlcNAcase_cat.
DR   NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR   PANTHER; PTHR13170; O-GLCNACASE; 1.
DR   PANTHER; PTHR13170:SF16; PROTEIN O-GLCNACASE; 1.
DR   Pfam; PF00754; F5_F8_type_C; 3.
DR   Pfam; PF07554; FIVAR; 5.
DR   Pfam; PF02838; Glyco_hydro_20b; 1.
DR   Pfam; PF07555; NAGidase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 3.
DR   SUPFAM; SSF140657; Hyaluronidase post-catalytic domain-like; 1.
DR   PROSITE; PS50022; FA58C_3; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198558}.
FT   DOMAIN          633..761
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          781..931
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   COILED          1389..1441
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1796 AA;  201108 MW;  C46CFDB5D0099368 CRC64;
     MIKFLDKALK SSLALLVVFS TLFLVSPSIK VEAEEVKYEI YPTPHELIYN SNDYVIRSQV
     NVVFEDEIDE STRKRMTEVL ELKNKQISTS NQKVVGKTNI LVGTHNSNGY VDNYVKANYN
     VEESLFDKFG ANFVASNNGE IIILGKDTDG AFYGITSLKH IFNQMDGSTI RNFEIKDYAD
     TNTRGFIEGY YGIPWSNEDR MSLMKFGGDF KMTSYVFAPK DDSYHKELWR ELYPEEELNA
     IKEMVQVGID SKCRFVWTAH PFMGGFDASR DDEEIAALLN KFDQLYDAGV RQFGVLGDDV
     GNLDRSVVIK MMNAVSNWAK EKGDVYDSVF CPAGYNHSWQ GNYSELNDYD TEFPDDVQIF
     WTGEAVCQPV EQRTLDHFRD YLLPEGASKR RSPLFWLNWP VNDINGSRLM MGKGSLLHTD
     INIEDLNGVV TNPMQEAEAS KIAIFAVADY SWNVKDFDDD QSWADSFKYI DKEANKELHT
     LAKHMSNPQP NGHGLVLAES EELQPLINEF KNKLVNNESI IEIGNQLINE MNIIIDACDG
     FHANSKNENL KEELLPFTNS LKDLTTAIKD FTESSIAIEK NDMVTAFNKY SNASSSLINS
     QNHVRKLLNG TAMVSPGSTH LIPLAQTLQE KLSGPINDYV AGGEVEQPLV ISASSNITSW
     YSGKIEDIVD GNNSTAAWHD GYETVGQYFQ VNLSKPTTIY GIDILNGTTN KPQDTFGFAK
     IQYSTDGTTF QDLNNEVYGE YASQVNVSNI EVENVVAVRY ICTETSSGRK WPAMREFTVI
     TQPVQEEGFT KEVIYTQDGW TASQSELNNI IDGNLDSSVH FNVRQTGYPD ATNSMIPGDY
     IGIKLSKPIT LGKINILQGR NDSDNDYMKN AQLQYSLNGE DWIDVGDIYR NTINVVVDLS
     DQNITAQYVR LVNTENQNNW FAIREFSVDA KVYHNGKVFT NVGEYNTLTA DYFDDTANIT
     PVQDITLAKD EYIGLKLDRI HEIKNIVSDL TNNDVIIQVS KNNYEWETVT TGDIYKDARY
     IRIINNQDMS VTFNINEFVV NTVEVGEKKI SSTNFSVADP LNVFDGDWTT ATAYQSSQNA
     GKYFVYDLGQ EIDMTSFKAV CTDSEWDYPR HGKFSVSVDG ENWVDIMTLG NQNEVNPGEA
     ENTDEIGFVL PDHEISYNTK KVTNLNVKAR YLKFEITRTK VGADKWVRFQ ELEINDGEYI
     PSVNNPTFTS NTQETRNGLF SYMTDGDIST MFIPKDANSY VNYSLSTKNN VNTIKIIQNA
     AVISNATVQA RVLDNTGASQ WINLGTLSQA INEFVLSEDT ILFDVKIEWG DVIPNITELS
     TYQSSFSDVN KDNLQSLIDN KENTSTWIMA SVEAYNAVYN AGKAVLESNY VSQTTVDNAI
     QAINNVITNK LLKGDIRELQ DLLDNALTDE NNYTASTWLV YNKAINAVRN AIENADNTSE
     NDILVLINNL NHARNGLVFN PSNQEEAIIT IESENEFIAS ITNPEDIYTV ASWQNYLDAK
     TELEQLLLDN EITPVHPDVF IKALDKLTSA KDSLEQKVTE VDKVALSIAI DMAEAVTQEQ
     LDKVVPVVAN EFKAALENAK EVYENTDATQ VDVDNAFDRL ASVMQMLEFF KGDKTALQKM
     VDQITNLTAS EYIESTWNAL QAVLPSVNEV LGNENAMQEE IDEVYTELVK AFINLRLKPN
     KDLLQDLINK ANGINRANYT SASLKAVDVE VEKASAVLNN PEATKEEVEA AVSALTKTLS
     GLEAKTGSTV DTSTPVKPGD TTVGVKTGDT TNMMYPLLGL AIASLGVYGN KKRKHK
//