ID A0A2M8W3E9_9MICO Unreviewed; 699 AA.
AC A0A2M8W3E9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=CLV34_2950 {ECO:0000313|EMBL:PJI85438.1};
OS Luteimicrobium subarcticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Luteimicrobium.
OX NCBI_TaxID=620910 {ECO:0000313|EMBL:PJI85438.1, ECO:0000313|Proteomes:UP000231586};
RN [1] {ECO:0000313|EMBL:PJI85438.1, ECO:0000313|Proteomes:UP000231586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22413 {ECO:0000313|EMBL:PJI85438.1,
RC ECO:0000313|Proteomes:UP000231586};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): From Individual Species to Whole Genera.";
RL Submitted (NOV-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}.
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:PJI85438.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PGTZ01000012; PJI85438.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M8W3E9; -.
DR OrthoDB; 5172397at2; -.
DR Proteomes; UP000231586; 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; 2.
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; 2.
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; 2.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00060; FN3; 2.
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; 2.
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:UP000231586};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..36
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 37..699
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014805741"
FT DOMAIN 183..264
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 273..354
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 366..699
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 259..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 699 AA; 71194 MW; 88C89F9B56BF5CD0 CRC64;
MERTTARRRR LARVAALLST AVLAGAAVLV AGPAGAADGE LAANGGFESG LTGWSCAASS
GQAVSTPVHT GTGALKATPA GSDNAQCSQT VTVQPNATYT LSAWVQGSYV YLGESGATAS
PVTTWTPSAA TWQKLSLTFT TSATASTATI FLHGWYGQPA YVVDDVSLVG PGGGTTTPTI
PAAPTGLKVG TATSSSVPLS WTAVSGATGY AVYRDGTKVS TTTSPSTTVS GLAAATAYSF
QVTATNAAGE SAKSSAVSAT TASGGTTPTV PAAPTGLAAG TTTTSSVPLT WNAVSGATGY
AVYRDGTKVS TTTSPSTTVS GLAAATAYSF QVTATNAAGE SAKSSAVTAT TATSGGGTGG
GALPTHALVG YLHASFANGA GYVRMADVPS SWDVIDLAFG EPTSVTSGDI RFTRCKVSEC
PNVESDADFK AAIAAKRAAG KKVLLSIGGQ NGQVQLTTTA ARDAFVSSVS TIIDTWGLDG
VDIDFEGHSL SLNTGDNDFR SPTTPVVVNL ISALKSLKAK YGAGFVLTMA PETFFVQNGY
QYYGSGPWGG QDPRCGAYLP VIYALRDDLT LLHVQDYNSG SIMGLDDQYH SMGGADFHIA
MTDMLLTGFP VAKDTTKMFP ALRPDQVAIG LPANSYAGNG YTSPADVTTT LNCLTKGTGC
GSYKTHGTWP GLRGLMTWSI NWDLYNGSPF TKNFDAYWP
//