ID A0A094F2I6_9PEZI Unreviewed; 1223 AA.
AC A0A094F2I6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 34.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=V498_07750 {ECO:0000313|EMBL:KFY85211.1};
OS Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY85211.1, ECO:0000313|Proteomes:UP000029270};
RN [1] {ECO:0000313|EMBL:KFY85211.1, ECO:0000313|Proteomes:UP000029270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
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: 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:KFY85211.1}.
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DR EMBL; JPKA01002258; KFY85211.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094F2I6; -.
DR HOGENOM; CLU_009688_0_0_1; -.
DR Proteomes; UP000029270; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd11618; ChtBD1_1; 1.
DR CDD; cd06922; ChtBD1_GH18_1; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.30.60.10; Endochitinase-like; 1.
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; 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; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 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, 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 Membrane {ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1223
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001896520"
FT TRANSMEM 737..761
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 773..803
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 138..184
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 199..557
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 20..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1203..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 152..164
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 157..171
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 1223 AA; 130326 MW; 092469F5D87501C7 CRC64;
MRILLPALLA VVSCGISQGH QHHHGKRNHA KPLPEFTPVP QLPKNSSSAL PPLYQPYSKN
KPKFQNEALI RQLSEHPGQR LDHLDSGPGS LRKRDLPVGT CAPGVPCTNG ACCSNTGVCS
YAPSSCGADV CISNCDAKAP CGQYANPDNA ACPLSVCCSQ YGFCGSTDDF CGTGCQEGFG
GCGPAPTPSC SSGSNAAARR RIGYYESWAT VRPCDVFTPE DLELTGLTHI NFAFSFFDPS
TFQISPMDGN AATLYSRFTA LKAKQPGLQT WLAVGGWSFN DATNTPNTQN AFSDMVSTPA
NRQAFITSLR NFMQTYGFDG VDIDWEYPAA DDRGGVPADF SNFPTFLDEL RASFGSGLGI
SATLPSSYWY LQHFDVLNME RSLDWFNVMS YDIHGVWDST NKFTGPYIRP HTNLTEINDG
LSLLWRAGVD PSKVVLGLGW YGRSFTLADP SCTTPNGVCQ FTAGGNAGEC TRSSGTLSNA
EIKRLIAAGT GTESYDATAG VRWLTFNTNQ WVSYDDGVTM QQKLAFANSL CLGGTMIWSI
DQDNTAGDSM NDLMGIGTAN GVSEAAAASF KEQMANATLQ NAIASSCYWS LCGGTCTTGY
FDVTEARGQV AGLQQNSVCA PGEFQTLCCA PGTTMGTCQW EGFRGVGMPC SPACSDSKAT
IVARNSNSYE MNDGGQIQDL TCTGGFQAYC CTGFVPSSIT NSGNLVLYGQ TPVLSKRDGS
NHGLSLYVRN HAVEKRAIPG LLISGLGALC LADAIPAALL APLTFGLSLA AEGAICAVAA
VAAAATAAII GFAILLSVFG WIFSGSPSKP NAGVPTTVAG RSSYGQWPIL DFSGGTTTIN
CDCVVTYTCR YGMGWDEICD NQRWGIDKLL NGKTVYQPLT VSRAAGANQG LWRGQRKEAY
RTAAQLKLPG VTWRCQVDEF PMGNLAESGN NGPQACRLVN GPANGRQGND YQMWKLAQWK
PCSTYRAAVC NSNDGGPPAT WAFGALPAGR GSGSGKRFID AYGFDEQTAN SLCWATYTYT
DQLPGTIATS TPVDHGFRVL DDDPMYGNAY GWPRQSWRMD PAPVANYLDR PGDSQPAIFQ
RDLLANDTSP EKHSDPAGVC HADLRSLGNG NQDAYLDLDY DNLLFVDIDG KPVDGRTCNV
IYEDDGPHSE LRIILDEEGN VVDMYMGDPE AGSWTREAVK SSNSDTVTVD PTTVTVTTGV
AAGSESRPTF PASTIGLQPG SGS
//
