ID A0A0N1G5K9_9ACTN Unreviewed; 571 AA.
AC A0A0N1G5K9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
DE Flags: Precursor;
GN ORFNames=OK006_7111 {ECO:0000313|EMBL:KPI04243.1};
OS Actinobacteria bacterium OK006.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592326 {ECO:0000313|EMBL:KPI04243.1, ECO:0000313|Proteomes:UP000037912};
RN [1] {ECO:0000313|EMBL:KPI04243.1, ECO:0000313|Proteomes:UP000037912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK006 {ECO:0000313|EMBL:KPI04243.1,
RC ECO:0000313|Proteomes:UP000037912};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four Actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (SEP-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}.
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:KPI04243.1}.
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DR EMBL; LJCU01000242; KPI04243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1G5K9; -.
DR PATRIC; fig|1592326.3.peg.8795; -.
DR Proteomes; UP000037912; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..39
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 40..571
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005872128"
FT DOMAIN 189..271
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 281..571
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 257..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 571 AA; 57971 MW; 6EF16720A5E3A433 CRC64;
MDRVIRMPRP PRRRWAGALA AVVTASVLSL TGLAGQAQAA DVNNAKNGGY ESGLSNWTCT
AGSGTTVSSP VHGGSAALKG TPAGQDNAQC TQAVAVKPNS TYTLSAWLQG GYAYLGVTGT
GTTDVSTWTP DSASWKQLST TFTTGASTTS VTVYTHGWYG QAPYYADDLS VFGPDGGGGG
DPAPTIPAAP TGLTVSSTTS SSVSLSWNTV SGATGYNVYQ AGTKVQSTTG TSATVSSLAA
STSYSFQVTA TNAAGESAKS TAVTGTTTAS SGGGGGSLPK HAVTGYWQNF NNGATVQKIS
AVQSQYDIIA VAFADATTTP GAVTFNLDSA GLGGYTVDQF KADIKAKQAA GKKVVISIGG
QNGTVSISDS TSATNFANSV YSLMQTYGFD GVDIDLENGL NATYMTQALR SLSAKAGSSL
IITMAPQTID MQSTSNTYFQ TALNIKDILT VVNMQYYNSG SMLGCDGKVY SQGSVDFLTA
LACIQLQGGL APSQVGLGLP ASTSGAGSGY VSPTVVNNAL DCLAKGTNCG SFKPSKTYPD
LRGAMTWSTN WDASAGNAWS NSVGAHVHAL G
//
