ID A0A0F8AY23_CERFI Unreviewed; 449 AA.
AC A0A0F8AY23;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN Name=Chit1 {ECO:0000313|EMBL:KKF93111.1};
GN ORFNames=CFO_g4541 {ECO:0000313|EMBL:KKF93111.1};
OS Ceratocystis fimbriata f. sp. platani.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX NCBI_TaxID=88771 {ECO:0000313|EMBL:KKF93111.1, ECO:0000313|Proteomes:UP000034841};
RN [1] {ECO:0000313|EMBL:KKF93111.1, ECO:0000313|Proteomes:UP000034841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFO {ECO:0000313|EMBL:KKF93111.1,
RC ECO:0000313|Proteomes:UP000034841};
RA Belbahri L.;
RT "Genome sequence of Ceratocystis platani, a major pathogen of plane
RT trees.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000256|ARBA:ARBA00008682}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00261}.
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:KKF93111.1}.
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DR EMBL; LBBL01000279; KKF93111.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8AY23; -.
DR Proteomes; UP000034841; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.30.60.10; Endochitinase-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF337; CHITINASE; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00270; ChtBD1; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669, ECO:0000256|PROSITE-
KW ProRule:PRU00261}; Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00261};
KW Glycosidase {ECO:0000313|EMBL:KKF93111.1};
KW Hydrolase {ECO:0000313|EMBL:KKF93111.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034841};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..449
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002527237"
FT DOMAIN 46..446
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 316..358
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DISULFID 331..345
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 449 AA; 48820 MW; AA328DD1D4665497 CRC64;
MVRASLLASV LAGWVATAVA APAEGASVVA SSEPSSSDGA GGSDAARYIL YFDKWHTSIL
PNKTMTTNIT HVIMAFAEPL AFTTDPIGEY EPHMELDKVR EMFDENVKIS MAIGGWDFTV
GFSEGVRSPE TRALYAKNIA DTVKRLGYDG VDIVIDWEYP GGHGADSKQV PINPSEAEAY
PLLLAEIKKA IGDKELSVAV PGLERDMMAY TAENVHSINA VVDYVNVMTY DLLNRRDTVS
GHHSGIKNSL AAIDTYIERG FPASKLNLGI RFYAKYFTLK DPKHDGTDAG TSGFLTFEPS
SFPAVVDTSL LTLSPDKTCG IHKGYTCGNM CCSQWGYCGT SDSFCGVGCQ RNYGRCHPVT
VGPKPLSESF KEAFENGIED VENGGQWYVD RQASLFWTWD TPALVERKFA EIIAARGLGG
IMAWSLAGDS YDWRLLAAMQ KGVEKMGLV
//
