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Database: UniProt
Entry: G2GKL5_9ACTN
LinkDB: G2GKL5_9ACTN
Original site: G2GKL5_9ACTN 
ID   G2GKL5_9ACTN            Unreviewed;       597 AA.
AC   G2GKL5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN   ORFNames=SZN_30292 {ECO:0000313|EMBL:EGX55956.1};
OS   Streptomyces zinciresistens K42.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=700597 {ECO:0000313|EMBL:EGX55956.1, ECO:0000313|Proteomes:UP000004217};
RN   [1] {ECO:0000313|EMBL:EGX55956.1, ECO:0000313|Proteomes:UP000004217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K42 {ECO:0000313|EMBL:EGX55956.1,
RC   ECO:0000313|Proteomes:UP000004217};
RA   Lin Y., Hao X., Johnstone L., Miller S.J., Wei G., Rensing C.;
RL   Submitted (AUG-2011) 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:EGX55956.1}.
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DR   EMBL; AGBF01000179; EGX55956.1; -; Genomic_DNA.
DR   RefSeq; WP_007502305.1; NZ_AGBF01000179.1.
DR   AlphaFoldDB; G2GKL5; -.
DR   PATRIC; fig|700597.3.peg.5944; -.
DR   OrthoDB; 5172397at2; -.
DR   Proteomes; UP000004217; 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; 1.
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; 1.
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; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00060; FN3; 1.
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; 1.
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:UP000004217};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..597
FT                   /note="chitinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003430263"
FT   DOMAIN          172..253
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          264..597
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
SQ   SEQUENCE   597 AA;  62349 MW;  60E45FC1F9C2B9D4 CRC64;
     MDRSRPLAVL AAAALAVSGL TALSSAARAA DADLARNGGF ESGLDGWSCT AGTTVNSPVR
     SGSSSLQATP AGNDNARCAQ TVTVKPGSQY TLSGYVRGSY VYLGASGTGT TDVSTWTQSA
     AGWQQLTTTF RTGPATTRVT IYTNGWYGTG AYNADDITLV GPGTDAEQPP AAPAGLRTGT
     VTATGVALSW SAVPGATGYA VYRDGVKVQT ASGTSATVGG LSPSTAYSFQ VAAVNAAGES
     AKSATVTATT TAGSGGGGGA LPAKALVGYL HASFANGSGY TRMADVPDSW NVINLAFGEP
     TTATSGDIRF NRCPVTECPN VESDAEFKAA IKAKQAAGKK VLLSIGGQNG QVQLTTTAAR
     DAFVTSVAKI IDEYGLDGLD IDFEGRSLFL NADDTDFKNP RTPVIVNLIS AVKTLKARYG
     DDFVLTMAPE TFFVQLGYQY YGTGKWGGQD PRAGAYLPVI YALRDDLTLL QVQDYNSGPI
     MGLDNQYHSM GSADFHIAMT DMLLTGFPVA GDQNNVFPPL RPDQVAIGMP ASTNAGNGYV
     PPAEVTKTLD CLTRKTNCGS YTTHGTWPGL RGLMTWSINW DRYAGWEFQR TFDGYFR
//
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