ID A0A094CKA7_9PEZI Unreviewed; 1372 AA.
AC A0A094CKA7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=V496_10420 {ECO:0000313|EMBL:KFY47830.1};
OS Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY47830.1, ECO:0000313|Proteomes:UP000029302};
RN [1] {ECO:0000313|EMBL:KFY47830.1, ECO:0000313|Proteomes:UP000029302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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 -!- 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:KFY47830.1}.
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DR EMBL; JPJY01002395; KFY47830.1; -; Genomic_DNA.
DR STRING; 1420909.A0A094CKA7; -.
DR HOGENOM; CLU_001837_2_0_1; -.
DR OrthoDB; 2582538at2759; -.
DR Proteomes; UP000029302; Unassembled WGS sequence.
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; cd00035; ChtBD1; 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; 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:SF401; CHITINASE; 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 SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 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 Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
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:UP000029302};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1372
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001894030"
FT DOMAIN 100..456
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 920..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1372 AA; 151196 MW; EFEA3D93DF08B38D CRC64;
MRLSYGPCIR CPLAALPLLT APTLAAGQAK NAVTEPAVVR AVGVVMVQYT AGTAASQTVM
LKLRVAKFGF CGATTEFCSG KCQSNCEQPK PSAGASNVQK RIVGYWETWN QDHPCGTMNP
SEIPVSMLTH LNVAFGYISH DFQITNMDGI SPTMYQNAAA VKSKNPNLKV LIALGGWTFS
DPGVWQNVFP TMASTAENRA TFIRNALGWL SQYGYDGIDF DWEYPGADDR GGSDGDGENY
TALLKELRAA IDASGREYIV TFTAPSSYWY LRHFDITDMM AYVDWVNLMS YDLHGVWDSD
NPIGNQVLAH TNLTEIDLAL DLFWRNDVEP SKIVLGLGFY GRSFKLSSPA CWKPGCDFTG
PGDEGECTKS AGILSYREIT SILEKTGAKP YFDKAAAAKY LVYGGDNWIS YDDAETFKLK
IDYANKLGLG GLMVLASGDS APFTLVDLYR LFPNEDYPTD DKNPRYGMVN FGNGANLGET
NPSKTGFGFF LVAGESHAVS KLKRQAGDPK PFTFLDCPAN VTSQPDDQAQ VARVVCLSED
VEGCFRVMER GVEGTVIEMP DNCAPGTFAR AISLNASSDV FEFAFDYKFK LVRKDSDQTS
IRMDYASMPG YWDELVDSEA LEKIKKNFFE KSLTQALYWE SVDSCNVDGS EFSEGIGAYV
DGSVHARFEY GFSLYATIKN GELDVSQTNG LLFVQGYSDL TYTIGGVGKF DVAKANNGNP
NWSKGQKQVI DGHTIYSSSM KGWASYKPYM AVDYMVAGEG DDSLSNSAIN FNGLLSARVL
TPIGPLIATF PDIDTSNPPA GQKISEPTLS IPEGNVVYSS SPGKGVSGTS VIGLGCYISF
GLDLDFGIHD DDELVSFEGP NMNIRIDSMV AFENNATSGY GTCVDYNVPS THWVWINDSG
DLKAPWPKGF DGYTAFQNSK TPSGQGTCYP HATTKRSLPS VDEHQTGSEY STSSQSDFAA
KEERSDSDSL ASELTKRGGS FPGFGYPIGK PVTPGLIFNS PDFNVGTEIF ELHDPRAMLR
LHLNGPQIWF SDKPACTTCV ANTEDGAWPN IIFSIPISTR EESSYNDEVL YGDEDSAQYH
HLDERVDGTA TNGVKQLAIC KIKNIRTRQI TNYPSFPAIA SYGWDGIENG KWDSISRYWG
NASASCSDWT VTQLQNHDTT TTPSGIVRSN YQTEHVFEAQ LIADFFDKWL DTGKIYNQVP
FLLAHTQKFS CERIKEYVIN GLDWPGGKRN LGQPFIHYLL EELGSKSKLD RLVIYLARPN
RSKGAPTAGL SYVSMGEEAQ LLAIKEMGMT FEYLRDPTIW GMFCATYEGI YNKMGEFDQW
YALNVGVASF NLQAEWKDYM QIVLDSMVRR LRASLGTYLS MGHKLDKKLE WH
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