ID A0A0M2GI02_9ACTN Unreviewed; 421 AA.
AC A0A0M2GI02;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Chitinase {ECO:0000313|EMBL:KJK37586.1};
GN ORFNames=UK15_20855 {ECO:0000313|EMBL:KJK37586.1};
OS Streptomyces variegatus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=284040 {ECO:0000313|EMBL:KJK37586.1, ECO:0000313|Proteomes:UP000034786};
RN [1] {ECO:0000313|Proteomes:UP000034786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16380 {ECO:0000313|Proteomes:UP000034786};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family.
CC {ECO:0000256|RuleBase:RU004453}.
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:KJK37586.1}.
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DR EMBL; JYJH01000015; KJK37586.1; -; Genomic_DNA.
DR RefSeq; WP_031138867.1; NZ_JYJH01000015.1.
DR AlphaFoldDB; A0A0M2GI02; -.
DR STRING; 284040.UK15_20855; -.
DR PATRIC; fig|284040.3.peg.2054; -.
DR Proteomes; UP000034786; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd06548; GH18_chitinase; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..421
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005632460"
FT DOMAIN 57..421
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 421 AA; 44187 MW; B31C67EAA84CE2A0 CRC64;
MHTPHRSRFR AIVSAACCAV LGAGLLAGAG TSATAATSAQ EAAAGSKAVP RAEAPGSKVI
GYFTEWGTYD RKYYVKNIET SGSGARLTHI NYAFGNVTGG KCAMGDGYAA TDRAHTAAES
VDGKADTWDQ PLRGNFNQLR KLKQKHPNLK VLWSFGGWTW SGGFGEAAKN PAAFAQSCYD
LVENSKWADV FDGIDIDWEY PNACGATCDT SGKAAFTNLM QALRAEFGSR NLVTAAITAD
ATPGGKIDAA DYAGAAPYVD WYNPMTYDFF GAWDAAGPTA PHSPLTSYAG IPKADNHSSA
TIAKLKGLGI PASKLLLGIG FYGRGWTGVT QSAPGGTATG PATGTYEQGI EDYKVLKAKC
PATGTVAGTA YAKCGSDWWS YDTPATIATK SNYKNQQGLG GTFFWELSGD TANGELIKAI
R
//
