ID A0A081PA80_9BACL Unreviewed; 613 AA.
AC A0A081PA80;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=ET33_12980 {ECO:0000313|EMBL:KEQ27603.1};
OS Paenibacillus tyrfis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1501230 {ECO:0000313|EMBL:KEQ27603.1, ECO:0000313|Proteomes:UP000028123};
RN [1] {ECO:0000313|EMBL:KEQ27603.1, ECO:0000313|Proteomes:UP000028123}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSt1 {ECO:0000313|EMBL:KEQ27603.1,
RC ECO:0000313|Proteomes:UP000028123};
RA Aw Y.K., Ong K.S., Gan H.M., Lee S.M.;
RT "Draft genome sequence of Paenibacillus sp. MSt1.";
RL Submitted (JUN-2014) 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:KEQ27603.1}.
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DR EMBL; JNVM01000002; KEQ27603.1; -; Genomic_DNA.
DR RefSeq; WP_036675352.1; NZ_JNVM01000002.1.
DR AlphaFoldDB; A0A081PA80; -.
DR eggNOG; COG3469; Bacteria.
DR eggNOG; COG4733; Bacteria.
DR OrthoDB; 315328at2; -.
DR Proteomes; UP000028123; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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; cd12214; ChiA1_BD; 1.
DR CDD; cd00063; FN3; 2.
DR CDD; cd02871; GH18_chitinase_D-like; 1.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_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; PF02839; CBM_5_12; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR PRINTS; PR00014; FNTYPEIII.
DR SMART; SM00495; ChtBD3; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 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:ARBA00023024};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
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:ARBA00023024};
KW Reference proteome {ECO:0000313|Proteomes:UP000028123}.
FT DOMAIN 46..376
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 388..472
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 481..564
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
SQ SEQUENCE 613 AA; 64861 MW; A8D1FE15121A3FDC CRC64;
MNFHSSPLYS RLRPRLLLGL VTALIISLFS VIASPLPSAA APAGGYKIVG YWHNFDNGSG
FIRLRDVSPD FDVINVSFAE PTSSGGGVIG FTPYNYTDAD FKADVAYLQS KGKKVVISIG
GANGQVQLAT TAARDAFVSS VTGIIEKYGF DGLDVDFEGH SLYLNAGDSD FRHPTTPVIV
NLIDALKSLN SHFGTDKFIL TMAPETFFVQ LGYSFYGGSC ISCDSRAGAY LPVIYATRDI
LDWLQVQNYN SGPITGLDDQ YHTMGSADFH VAMADMLLTG FPVNKNANLF FPPMRQEQVL
LGLPANGNAG GGFTPVAEVH KALDALVKGQ QLSTYKTRGS ATGYPNFGGL MTWSINWDKF
NQFEFSTKHR AYLNALNPSA PDTQPPTAPT NLVSTGKTAT SVSLSWNAST DNVGVTGYTV
SYGSSQVNVT GTSTTIQGLK PNTSYTFSVT AKDAAGNVSP ASNVVTVKTD ESSGDNQAPT
APTQLSVVSK SATSVTLSWA ASTDNVGVTG YTVAYGSSQV NVTGTSAAIE GLNPNTNYTF
SVTARDAAGN VSPAAVITVT TDAPSGAQPW APGTAYKIGD EVTYAGKTYV CRQNHTSLQG
WEPPNVAALW QLK
//
