ID A0A212TZF5_9ACTN Unreviewed; 579 AA.
AC A0A212TZF5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=SAMN06272741_5149 {ECO:0000313|EMBL:SNC71244.1};
OS Streptomyces sp. 2114.4.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938836 {ECO:0000313|EMBL:SNC71244.1, ECO:0000313|Proteomes:UP000198141};
RN [1] {ECO:0000313|Proteomes:UP000198141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2114.4 {ECO:0000313|Proteomes:UP000198141};
RA Varghese N., Submissions S.;
RL Submitted (JUN-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}.
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DR EMBL; FYEY01000001; SNC71244.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212TZF5; -.
DR Proteomes; UP000198141; 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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..47
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 48..579
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011230420"
FT DOMAIN 197..278
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 289..579
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 579 AA; 58937 MW; 791708A7EB70D331 CRC64;
MPRTAHTRPT GRTRPTRPAR HRRLLAAALT ALAAVAATLS GSTPAAAADV NAARNAGFES
GLSNWTCSAG SGSTIGSPVH SGTGALKATP TPSDNATCSQ TVAVKPGSAY RLSAYVQGSY
VYLGASGTGT TDVSTWTPSA TDWQQLSTSF TTGPTTTSVT VYTHGWYGQP AYLADDFSVL
GPDGGGGTDP GPQAPATPGG LTAHAVTSSS VTLSWNQVSG ATGYTVYRDG TKYGTATGTS
ATVTGLAPAT AYRFQVTATN AAGESARSAE ITATTAPSGS GGTPTVPKHA VTGYWQNFNN
GATVQKLSDV PGQYDIIAVA FADATTTPGA VTFTLDSAGL GGYTVDQFKA DIKAKQAAGK
SVILSVGGER GTVSVNDAAS AANFATSLHT LMQQYGFDGV DIDLENGLNP TYMSQALRSL
SQKAGGRLVL TMAPQTLDMQ STSGGYFQTA LNVKDILTVV NMQYYNSGSM LGCDGKVYSQ
GTVDFLTALA CIQLEGGLDP SQVGLGLPAS TRGAGSGYVA PSVVNAALDC LARGTSCGSF
KPARTYPGIR GAMTWSTNWD AANGNAWSNA VGPHVHDLP
//
