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Database: UniProt
Entry: A0A2M8W3E9_9MICO
LinkDB: A0A2M8W3E9_9MICO
Original site: A0A2M8W3E9_9MICO 
ID   A0A2M8W3E9_9MICO        Unreviewed;       699 AA.
AC   A0A2M8W3E9;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN   ORFNames=CLV34_2950 {ECO:0000313|EMBL:PJI85438.1};
OS   Luteimicrobium subarcticum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Luteimicrobium.
OX   NCBI_TaxID=620910 {ECO:0000313|EMBL:PJI85438.1, ECO:0000313|Proteomes:UP000231586};
RN   [1] {ECO:0000313|EMBL:PJI85438.1, ECO:0000313|Proteomes:UP000231586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22413 {ECO:0000313|EMBL:PJI85438.1,
RC   ECO:0000313|Proteomes:UP000231586};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): From Individual Species to Whole Genera.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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:PJI85438.1}.
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DR   EMBL; PGTZ01000012; PJI85438.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M8W3E9; -.
DR   OrthoDB; 5172397at2; -.
DR   Proteomes; UP000231586; Unassembled WGS sequence.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd02871; GH18_chitinase_D-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR45708; ENDOCHITINASE; 1.
DR   PANTHER; PTHR45708:SF49; ENDOCHITINASE; 1.
DR   Pfam; PF02018; CBM_4_9; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000231586};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           37..699
FT                   /note="chitinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014805741"
FT   DOMAIN          183..264
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          273..354
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          366..699
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   REGION          259..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   699 AA;  71194 MW;  88C89F9B56BF5CD0 CRC64;
     MERTTARRRR LARVAALLST AVLAGAAVLV AGPAGAADGE LAANGGFESG LTGWSCAASS
     GQAVSTPVHT GTGALKATPA GSDNAQCSQT VTVQPNATYT LSAWVQGSYV YLGESGATAS
     PVTTWTPSAA TWQKLSLTFT TSATASTATI FLHGWYGQPA YVVDDVSLVG PGGGTTTPTI
     PAAPTGLKVG TATSSSVPLS WTAVSGATGY AVYRDGTKVS TTTSPSTTVS GLAAATAYSF
     QVTATNAAGE SAKSSAVSAT TASGGTTPTV PAAPTGLAAG TTTTSSVPLT WNAVSGATGY
     AVYRDGTKVS TTTSPSTTVS GLAAATAYSF QVTATNAAGE SAKSSAVTAT TATSGGGTGG
     GALPTHALVG YLHASFANGA GYVRMADVPS SWDVIDLAFG EPTSVTSGDI RFTRCKVSEC
     PNVESDADFK AAIAAKRAAG KKVLLSIGGQ NGQVQLTTTA ARDAFVSSVS TIIDTWGLDG
     VDIDFEGHSL SLNTGDNDFR SPTTPVVVNL ISALKSLKAK YGAGFVLTMA PETFFVQNGY
     QYYGSGPWGG QDPRCGAYLP VIYALRDDLT LLHVQDYNSG SIMGLDDQYH SMGGADFHIA
     MTDMLLTGFP VAKDTTKMFP ALRPDQVAIG LPANSYAGNG YTSPADVTTT LNCLTKGTGC
     GSYKTHGTWP GLRGLMTWSI NWDLYNGSPF TKNFDAYWP
//
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