ID A0A094GVZ2_9PEZI Unreviewed; 1328 AA.
AC A0A094GVZ2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 31.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=V498_00181 {ECO:0000313|EMBL:KFZ00286.1};
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:KFZ00286.1, ECO:0000313|Proteomes:UP000029270};
RN [1] {ECO:0000313|EMBL:KFZ00286.1, 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:KFZ00286.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPKA01000028; KFZ00286.1; -; Genomic_DNA.
DR HOGENOM; CLU_001837_0_0_1; -.
DR Proteomes; UP000029270; 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: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; 3.
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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1328
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001903040"
FT DOMAIN 29..66
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 100..154
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 161..519
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 123..135
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 128..142
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 1328 AA; 147137 MW; 319EB5FD0B5E0C10 CRC64;
MVSLQKRGGT TGSFVILAFV FPFIISLALA DCSKTKPCAS GCCSQFGFCG VGDEFCGAGC
LSSCDFQLGC DAKRPCASGC CNKFGFCGLG PDYCDTKVCV AGCGSKSYCD PGYGPKWAEV
AHCPLNVCCS KWGFCGLTEE FCGDKKVKRP SCDALSGPQL QNVVGYYEGW STARPCNTFH
PEQIPLGVYT HINFAFATID PKTFEIRPGS SYDIDLYKRV TALKRQDPDL KVFIAIGGWT
FNDPGPTERT FSDLAASETN QRAFFQSLVS FLATYDFDGV DIDWEYPVTK DRNGREQDFA
NFPKFIRNLQ GAIQGSGRFS GVTVTLPASY WYLRHFDIKE LVKYVEFFNI MSYDMHGPWE
KGNIWTGEFL NGHTNLTEIS GALDLMWRND IPPSKVVLGL AFYARAFTVA NVNCKTPGCL
FASGAKPGRC SHEISILLNS EIDEIVAEKG LQPVLYKDAA VKVVTWDDQW LAYDDEETLS
IKADFARSMC LGGVMVWAIS HDTVAAKYTK ALAKAARRDF VAINNIDATL PGGVFGELPS
SGVPAPTGYK VYTRHQQCKW MGCHENCPSG WQWVRRTGPG SQTKTWEGMS DESACDGDGQ
HNLCCPPTTE QPQCGWYGFN GGKCDPTGAC PFGFKEIGSL SKHCHNGKYQ TACCSVILNS
EGTPIPPVEG LDVYETCEWG AWPKCDDNNC ITNYWMSTTL SQSSTGSGGS VCNFETDYRD
RDIYEKRDYC CDTSNINRRW QSCYIPFGYL GGAAGRENSR FCDSTCPSST VRVSMDLKSD
GCSTNGGGKP MCCIPGLYSS ETVEFPEATA AREVISSYLH QPTCPKAIEL LQRRSLAVET
IGHNSTALVA RSSSPRYDNF VLLLTIAFRA RHFGQTEMME TVVDEELRAA DLATVREIND
WRETDPRAAS MSSEEIAKAF ACDPITVTCM VKVSKKCPFC KDNTCGGPND SYKVPDINCA
GEKDYDDGDA TPRESRVTLL RRHEGDAAVS LREIADGGEE EAYHELSKRA DSASGEITDF
TYRNRDTGAT KPIYYRTQPY YHSRTWPPEH ESYYRMYDYE NEADCANAKV INIDAANPIY
NNRHYQTEHL IEFQGMKAFF LFLGARTLPS GLPSRVLTPV PLIFFTDFFA KPVLRNLTPL
PGGSTAIRIA YPCDRIMEAV GSVDNNENFV HLIDTINGMK MRAWAGKKLA SDDRMEIMIK
GAPGNAIVYI RRGIAVINYL NHPNVNGHLA VISNQIRAQL VIISNEWNSD TTRHQINLAA
DWDEWIRDQL SQVTFNVQSF ALGWLNKMKA YWILQDPEGE ACWIIPAIDR LWASASVTGR
GILVSGFT
//
