ID A0A0U3PI98_9ACTN Unreviewed; 608 AA.
AC A0A0U3PI98;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Chitinase {ECO:0000313|EMBL:ALV33478.1};
GN ORFNames=AS200_16610 {ECO:0000313|EMBL:ALV33478.1};
OS Streptomyces sp. CdTB01.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV33478.1, ECO:0000313|Proteomes:UP000068029};
RN [1] {ECO:0000313|EMBL:ALV33478.1, ECO:0000313|Proteomes:UP000068029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CdTB01 {ECO:0000313|EMBL:ALV33478.1,
RC ECO:0000313|Proteomes:UP000068029};
RA Tian Y., Zhou G., Yang H., Lu X.;
RT "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT bacterium tolerant to cadmium.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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DR EMBL; CP013743; ALV33478.1; -; Genomic_DNA.
DR RefSeq; WP_058923143.1; NZ_CP013743.1.
DR AlphaFoldDB; A0A0U3PI98; -.
DR STRING; 1725411.AS200_16610; -.
DR KEGG; scx:AS200_16610; -.
DR OrthoDB; 9775889at2; -.
DR Proteomes; UP000068029; Chromosome.
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:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR CDD; cd06548; GH18_chitinase; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_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; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS51173; CBM2; 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:UP000068029};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..608
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006842976"
FT DOMAIN 27..134
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT DOMAIN 144..229
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 240..608
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 135..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 608 AA; 63184 MW; 3440BB7C1CE9C236 CRC64;
MRFRHRAAAG FATLLLPLAG LVGLASPAQA ATNATATYTK TQDWGTGFGG QWTIKNTGSS
SISSWTVEWD FPSGTSVTSA WDADVTNSGT HWTAKNKSYN GTLAPGASVS FGFNGAGSGS
PSNCKLNGDS CDGTTVPGDA APSAPGTPTA SSVTDTSVKL SWSAATDDKG VKNYDVLRDG
KVVSTVTGTS WTDSGLTAGT DYSYTVQARD TADQTGPVSG AVAVHTTGGT TDPPPTTGDK
VKLGYFTEWG IYGRNYNVKN LVTSGSAAKI THINYAFGNV TNGQCAIGDS YADYDKAFTA
DQSVSGVADT WDQPLRGNFN QLRELKAKYP NIKVLWSFGG WTWSGGFAQA AANPAAFAQS
CYNLVEDPRW ADVFDGIDID WEYPNACGLS CDTSGAAAFK NVMAALRAKF GSNNLVTAAT
TADGSAGGKI EAADYAGAAQ YVDWYNVMTY DFFGAWDAKG PTAPHSPLTS YSGIPKAGFT
TADAMAKFKA IGVPAKKLLI GIGFYGRGWT GVTQDAPGGT ATGPAAGTYE QGIEDYKVLK
TSCPATGTVA GTAYAHCGSN WWSYDTPSTI AGKMSWAKSQ GLGGAFFWEF SGDTSNGELV
SAISSGMN
//
