ID A0A166V5S5_9PEZI Unreviewed; 1161 AA.
AC A0A166V5S5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
DE Flags: Fragment;
GN ORFNames=CT0861_01798 {ECO:0000313|EMBL:KZL74200.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL74200.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL74200.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL74200.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:KZL74200.1}.
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DR EMBL; LFIV01000035; KZL74200.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166V5S5; -.
DR STRING; 708197.A0A166V5S5; -.
DR OrthoDB; 2582538at2759; -.
DR Proteomes; UP000076552; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
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; cd00035; ChtBD1; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.30.60.10; Endochitinase-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
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; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF333; CHITINASE; 1.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00270; ChtBD1; 2.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 2.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 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 Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669, ECO:0000256|PROSITE-
KW ProRule:PRU00261};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00261};
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:UP000076552};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1161
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007880983"
FT DOMAIN 29..66
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 67..116
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 121..478
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DISULFID 42..56
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 60..64
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 85..97
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 90..104
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KZL74200.1"
SQ SEQUENCE 1161 AA; 129325 MW; 3F2684CFB40ABA8E CRC64;
LRELFTIMNK LLAFVFFLFC LVQLSLQQEA ECSASKQCPA GCCSSAGFCG YGPDYCGKGC
LSTCERKSEC NPGWDSSLYS EKETCPLNVC CSKHGFCGFT EEFCADDKVK RPSCSSDKAV
TRVMGYFESW APSKRPCYSM QPEAIPYGQY THIIFSFATI NPKTFKVSVG DSQTEYLMSR
IGSIKVIQPD IKIWVALGGW AFNDPGPTQT TFSDIAASSA HTKTFLDSLV QMCNKYGFDG
VDIDWEYPVA EDRNGRPEDY KNIVTFMKAL RERMKDSKRG VSMAIPASYW YLQNFDIKAL
EAHVDWFNIM SYDVHGSWDI DNEWTGPWVN SHTNMTEIQL ALDLLWRNDI SPTKVTMGMS
FYSRSFTLTD PGCSKLGCRV SSGGNAGKCS DTVGVLLHPE IQDIIAEKKL TPTLDRDGAV
KMVSWDNQWV SFDDVATWRL KGNIARSQCI EGFMVWAMSQ DDSKGTNIKA LNQALSRKTP
DFPEFTPKEK PVPVLPSMAA KLCRWTSCFE GCPSGFKEVQ RDGHKEIMMD TSICSDQYDN
LGFSRLCCPS SGTLPTCTWR GHKNSGNCQP GCNPGEVEVG SLRTGCKKNW QSACCTSSDV
TKAYGTCLWS GCTKDYDNIC TNKAIATSAQ GWGGHQSCKN GEARALCCPN PAPTEFTNDC
KWVPKNGHLK GGGLDNICEG ACPQDSIKLS LSIGFHLVPG RETACFGYNA FCCADPKPIV
IRDPGEDDTF GSSQAKEFKL LISKYMDNPT CPATILEPTI HDAYGGAGKK RDLQSEAQQY
EILQGRATDC TLANWEKMLA YATLMFSMLQ AGFDGIRSVW NNDFAGHYDS EYEFLQIQDY
LFDYPWLDTR AHLEYVLLNP LSAGQGMRNA RRAGTQLCRL TTTRRRELTI GGGGRGSEVS
KRVVWPMNSD PSDTPNLSTI LDGVLNGDLS LHYARWQYAW GQESNAPPGP FLELAYWIGP
RPGVATTGDT AYDRYRDTRQ RGAEWGTDQW VVFHMHINPR DPDWLTRVGG RTYMGVPGFR
IFHGQQARPF NQEEGAWRVD GSLASPYTAR NGWDCPEDEG YWYVGLPDVP SDPLLLQMQR
WGERLYNDGY VAGIGLRLIV EPPTGDYDTE LNPENPGYVV RPPRGYTSAA GNLNPYELNF
LIERGSYSFV TAPHPPPPSK K
//
