ID A0A066XBM3_COLSU Unreviewed; 800 AA.
AC A0A066XBM3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=CSUB01_06742 {ECO:0000313|EMBL:KDN63420.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN63420.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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: 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:KDN63420.1}.
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DR EMBL; JMSE01001227; KDN63420.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066XBM3; -.
DR STRING; 1173701.A0A066XBM3; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_001482_0_0_1; -.
DR OMA; RDWVKFG; -.
DR OrthoDB; 11640at2759; -.
DR Proteomes; UP000027238; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
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; cd02878; GH18_zymocin_alpha; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR47700:SF2; CHITINASE; 1.
DR PANTHER; PTHR47700; V CHITINASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G13720)-RELATED; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
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 Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000027238};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 690..708
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 49..408
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 800 AA; 88554 MW; BA9EFF5272E76709 CRC64;
MTSDTPYPGG SGMAWPGLVH NSKVGHDPMP VSECSRNNFE ASCSAPASKI KLGYFEGWNY
NRPCLNMDVS QIDTGAFTHV HFAFPNVTRG DFRIEITDPL VKEQFEEFKK LEGVKKIVSL
GGWDFSALPG TFMILREAAL PGNRDVFKRN IISFINEHNL DGIDLDWEYP GAPDIPDIPS
DDPVNGVNYF RLLASVKAEV GTSKSVSFAA PASYWYLRAF PPIKQMAEAL DYIVFMTYDL
HGQWDAGNKW TSPGCPTGNC LRSHVNETET KDALSMVTKA GAASNKILVG VSSYGRSFKM
AQAGCDGETC LFTGDNRNSG AAKGRCTGTA GYISNAEIGE ILVSNRTNKK WTKEGSNMMV
YDNTEWVAWM DNDMKAKRAE FYDSYNFLGT TDWAIDLQNW MDGSGGISDD NNDELIYKEL
SACTASFSTL QQLEERKGSI PSHCLEQYIV DVQVSVFDEA LKKYNKLIED GYDSKFSTWE
GYIKDQIPEQ IKKFMATDKV DKYFKCGETK TVICCCKNGK QLVTRDKCPK VEADPTGSSG
GSNPNTTFTL NDREGFFKDI LETWGIEEGW ITFDKRRMSL ANGCQNAGKD VKDCIAQNSI
FFHDFPTMDS SKTKINNPKD IIVKALPDAK GLLERYRDMK TFAEFEEDIE MSDLVDAGSL
PAFAVDQAVG EMDKIVKEAN EIEKKRREEF ILSMIMSLLF FIPFLGPTGG GAVAVGVRTL
LRLVEVGAEV GLAVYGVVND PNNAFMTVFT TLLAAGFGRS GFRNAANSRR GMSSNEYNSL
GNIKPKLDTI TSLRSGMCSL
//
