ID A0A420F162_9ACTN Unreviewed; 471 AA.
AC A0A420F162;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=D7I43_14990 {ECO:0000313|EMBL:RKF26745.1};
OS Micromonospora globbae.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1894969 {ECO:0000313|EMBL:RKF26745.1, ECO:0000313|Proteomes:UP000285744};
RN [1] {ECO:0000313|EMBL:RKF26745.1, ECO:0000313|Proteomes:UP000285744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WPS1-2 {ECO:0000313|EMBL:RKF26745.1,
RC ECO:0000313|Proteomes:UP000285744};
RX PubMed=29458491; DOI=.1099/ijsem.0.002625;
RA Kuncharoen N., Pittayakhajonwut P., Tanasupawat S.;
RT "Micromonospora globbae sp. nov., an endophytic actinomycete isolated from
RT roots of Globba winitii C. H. Wright.";
RL Int. J. Syst. Evol. Microbiol. 68:1073-1077(2018).
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:RKF26745.1}.
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DR EMBL; RAQQ01000009; RKF26745.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420F162; -.
DR OrthoDB; 5172397at2; -.
DR Proteomes; UP000285744; 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:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd02871; GH18_chitinase_D-like; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR018366; CBM2_CS.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR45708; ENDOCHITINASE; 1.
DR PANTHER; PTHR45708:SF49; ENDOCHITINASE; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00561; CBM2_A; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
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:UP000285744};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..471
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019228253"
FT DOMAIN 26..133
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT DOMAIN 177..471
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 124..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..172
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 471 AA; 48662 MW; 75F106DFCF028517 CRC64;
MRRARYLVLS LVTALVAALG AAWVTLPAYA AGATASFVKT ADWGTGWEGR YTITNGGGTP
VTGWTVSFEL PPGTTVGSYW DALLTTSGQR YTFTNRSWNG SIAPGASVSF GFLGNGSSSP
ANCQLNGAPC GGGTPTTPPT TTPPPTTPPP TTPPPTTPPP TTLPPTTPPP TTGLPAHVLT
GYWHNFDNPA VELRLRDVPA EYDLVAVAFA EATATPGAVT FAVDPGLSAA LGGYTDADFT
ADVRTLQSRG KKVIISVGGE TGRVSVNDAA SAVAFSDSVY ALIQRYGFDG VDIDLENGLN
PTYMAQALRA LRAKAGAGLI IAMAPQTIDM QSPAGSYFKL ALDIRDILTV VNTQYYNSGA
MLGCDHNAAY PQGTVNFIVA LACIQLEAGL RPDQVGLGLP AGPGAAGGGI VAPSVVNAAL
DCLTRGTNCG SFRPPRTYPG LRGAMTWSIN WDVTNGNGFA RTVAPHLDTL P
//
