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Database: UniProt
Entry: A0A2X0KCB6_9ACTN
LinkDB: A0A2X0KCB6_9ACTN
Original site: A0A2X0KCB6_9ACTN 
ID   A0A2X0KCB6_9ACTN        Unreviewed;       781 AA.
AC   A0A2X0KCB6;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Chitinase {ECO:0000313|EMBL:RAG84889.1};
GN   ORFNames=DN069_14655 {ECO:0000313|EMBL:RAG84889.1};
OS   Streptacidiphilus pinicola.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptacidiphilus.
OX   NCBI_TaxID=2219663 {ECO:0000313|EMBL:RAG84889.1, ECO:0000313|Proteomes:UP000248889};
RN   [1] {ECO:0000313|EMBL:RAG84889.1, ECO:0000313|Proteomes:UP000248889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMS16-CNU450 {ECO:0000313|EMBL:RAG84889.1,
RC   ECO:0000313|Proteomes:UP000248889};
RA   Roh S.G., Park S., Kim M.-K., Yun B.-R., Park J., Kim M.J., Kim Y.S.,
RA   Kim S.B.;
RT   "Streptacidiphilus pinicola sp. nov., isolated from pine grove soil.";
RL   Submitted (JUN-2018) 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:RAG84889.1}.
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DR   EMBL; QKYN01000056; RAG84889.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2X0KCB6; -.
DR   OrthoDB; 9775889at2; -.
DR   Proteomes; UP000248889; 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; cd06548; GH18_chitinase; 1.
DR   Gene3D; 3.10.50.10; -; 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; IPR029070; Chitinase_insertion_sf.
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; PTHR11177; CHITINASE; 1.
DR   PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR   Pfam; PF02018; CBM_4_9; 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; SSF54556; Chitinase insertion domain; 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:UP000248889}.
FT   DOMAIN          245..335
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          339..781
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   REGION          179..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   781 AA;  79965 MW;  858CF950C741960C CRC64;
     MHQRALPAPA APERRLKRST ALAAATALVA GTVALAAGLT GASAAATNLV TNGDFETGNL
     SGWSCSTLDS VVTSPVHGGS YALQGAASSG DDAQCAQTVT VQPNTSYTLS AYVQGNYVYL
     GATGTGVSAS TWTPANSSYG QLTTSFTTGA TTTSVQVYTH GWYGQGTYFA DDVTLTGPAG
     SGGGTTSPSA SPTSASPSAS ATSASPSASP TSASPSPSAS ATSASPSPSA SSTSGGGTAP
     GGDGQVSTPS GVSAKVTNNA VTLSWTGSTD SSGTGDTPAY YVYSGANLMA TAMGSTVTVS
     SLQPNTSYTF TVQGYDKDGH SSAQSTPITV TTGAAQTGAM KSAYFDQWSI YGNAYYPKNV
     GTSGAAAGMK VITYAFENID PTNLNCFETV KASDSTNESD PNAGDGAGDA FADYQKSYTS
     DISVDGTSDT WSQPIKGNFN QLRELKAKYP NLRINLSIGG WTYSKYFSDV AATDASRKKF
     VSSCIDMFIK GNLPTNISGD ASGGTGSAAG LFDGIDIDWE YPASAGGHTG NHYSAADTAN
     YTALLAEFRS ELDAYGSTVG KHYLLTAALP SGQDKISLIQ PAAISKYLDY GDLMTYDMHG
     AWDSTGPTNF QDPLHDTSND PSKAIAPGTA KYNIDETIKA YTTGDSAYGI TGGFPANKLV
     LGVPFYFRGW TGVPAGSNYG LYQSATGASP AQTYTQEAGI ADWKELAAKG LTTGSTVHWD
     PTTQSAWIYD GTNFYTGDTP QAITARGQYA TTNGLGGIFA FSFEGDDASG SLINAMNSSM
     Q
//
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