ID J4H2J4_9APHY Unreviewed; 509 AA.
AC J4H2J4;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=FIBRA_03690 {ECO:0000313|EMBL:CCM01629.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM01629.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCM01629.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM01629.1,
RC ECO:0000313|Proteomes:UP000006352};
RX PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA Diehl S.V.;
RT "Short-read sequencing for genomic analysis of the brown rot fungus
RT Fibroporia radiculosa.";
RL Appl. Environ. Microbiol. 78:2272-2281(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC Evidence={ECO:0000256|ARBA:ARBA00000822};
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DR EMBL; HE797042; CCM01629.1; -; Genomic_DNA.
DR RefSeq; XP_012180912.1; XM_012325522.1.
DR AlphaFoldDB; J4H2J4; -.
DR STRING; 599839.J4H2J4; -.
DR GeneID; 24096540; -.
DR HOGENOM; CLU_007818_1_2_1; -.
DR InParanoid; J4H2J4; -.
DR OrthoDB; 360175at2759; -.
DR Proteomes; UP000006352; 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:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd12215; ChiC_BD; 1.
DR CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR045321; Cts1-like.
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; PF02839; CBM_5_12; 1.
DR SMART; SM00495; ChtBD3; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 2.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000006352};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..509
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003779180"
FT DOMAIN 36..337
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 400..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 509 AA; 54130 MW; 484214E8BC461E93 CRC64;
MSAAHTTSRR FAYVCIALVA ALNLLGAAAF DVSLYDNVAV YWGQDSYGAT HSDVADYQQP
ISFYCQDDAI DVIPIAFVNS FFGTGGYPVL NLGNTCNSTT NGYFNGTELL NCSFLATDIE
YCQNQGKAVT ISLGGGGASV GFQSDSEAQT FADTIWNLFL GGTSDMRPLG SVVLDGVDLD
IEGGSETGYA AFIAQLRTYF EGADKSYYIS GAPQCEYPDE YLGDALDSAW FDMVYVQFYN
NPCGLQNFDD ASGYDFGIWD IWARNVSINP NVKIFVGAPA STTAAGTGYQ NASQLETIAI
YSRNSYPSFG GVMMWDASQA YQNDQYDLTI KDALVAAGST GFTYPACSAE EWTSGSDYPG
GSKVSWNGYI WESKYYASDE PTMNYNGDWM PISACAGTAP TSSSPTTSTA SSGTTSTSAT
ATTTSTGTGN CAGVAEWSDS TAYTGGSEVQ YNGDLWTAQY WTEDDVPGGS AGVWTNDGAC
SSSDVAARAF APPTPAPVAP RSKSRFFRL
//
