ID A0A094KEH7_9PEZI Unreviewed; 1760 AA.
AC A0A094KEH7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 36.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=V501_00309 {ECO:0000313|EMBL:KFZ20083.1};
OS Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ20083.1, ECO:0000313|Proteomes:UP000029315};
RN [1] {ECO:0000313|EMBL:KFZ20083.1, ECO:0000313|Proteomes:UP000029315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
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 -!- 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:KFZ20083.1}.
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DR EMBL; JPKD01000117; KFZ20083.1; -; Genomic_DNA.
DR STRING; 1420914.A0A094KEH7; -.
DR HOGENOM; CLU_002651_0_0_1; -.
DR Proteomes; UP000029315; 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:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd00035; ChtBD1; 1.
DR CDD; cd06922; ChtBD1_GH18_1; 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; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF333; CHITINASE; 1.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF04082; Fungal_trans; 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; PS51910; GH18_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 3: Inferred from homology;
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}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Reference proteome {ECO:0000313|Proteomes:UP000029315};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1760
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001901155"
FT DOMAIN 90..128
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 129..175
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 188..544
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 1156..1183
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 780..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1180..1201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 99..111
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 104..118
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 122..126
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 143..155
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 148..162
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 1760 AA; 194111 MW; 94821E52A2299E26 CRC64;
MKLDTTFRLA ALAVAGLLSN CASASDVFLR YRQDNVTREV YNKTLYKPLF EAPSNSTPRF
LNISQKDINP LRGAAGTLAL AKRQESTAED GTCAPGTPCS NGACCSSSGF CGYSPDFCGA
NCISNCDAKA QCGKYAKAGK EQCPLNVCCS EFGFCGTSEK FCGLGCDESS GLCGPAPTPR
RGGNKAGRKA IAYYESWANT RSCDVVSPED LDVAGLTHLN FAFAFFDPTS FQMTAMDANA
DSLLARFTDL KVNHTSLETW IAIGGWSFND ETNFPNTRTA FSDMASSAGN RKKFINSLVH
FMKAYGFDGA DIDWEYPGAE DRGGKEEDTA NFVDLVKEMK AAFGSRYGLS VTLPASYWYL
QHFDVKGMEP HVDWFNIMSY DIHGVWDSSN RFSGPFARPH ANLTEIDESL SLLWRAGISA
GNVVLGLGWY GRSFKLADPS CTTPGCRFSE GATAGDCTGA PGVLSNAEID RIIEKYDLTP
TYDDKAAVNW IVWNSDQWVS YDNARSFKRK IDYANNLGLG GTMIWAIDQG SSSGKTLDDY
HGGVFLQKAS VFNGKGPTLS KKVLATTQHE TDAQHSCYTT FCGQECAPGY SGVSQMKGRV
GELGAATACT GTDFQTLCCA TATFLGRCKW YGWRGEGLSC QGGCPSDHTL IAVNTNHYFN
YPEQKFLEDQ TCAGGTQSYC CNNVKASPMF GKDIELVDHS DLESDPKNLA KRATAECAVF
GVIAGGIFVW ATVATGGFFA LTGGALAGAI ATNICAKSGM DKASTAALIG GYNTRLAASG
GANQKSNSKP ANTNTKPGKK VDSNAGFYGR YKIANFSTTA TCQVTYTCEY GLGFDQVCDN
QRWGLDKVLG GIHSVFNRET GPRTGRQKGQ WSGKHHANYR GSFPARDQCG DDGNRCRCEL
DEFPLDSLRE AGVLPQALRM LNGNENGRQG RDYQDWLEAV WEPCSSLLQR PPPITWEIGA
IPANDARATS NAIIPKYGWD STSGFDPCFG TYVVGASTVV SDHGFRVHSQ DPLFYQHNWE
AQNYSPDPHG LPAAQRPTDV VSAHLARKRW GEEQVQHLHL DVDITITAGE LIPLPTINAG
IDDGSSTQQD LMEETARVRK LLHEGMPAPT VVEIAAERTD ANLGHMATRT EAARLPPHRD
SINNNAETED NKQRAFACYL CNRQFTRNDL LQVHLRRHES RTLENAETQR DPTPPHQGHR
DALLRRTNPL WNEGLSVPTF HGRSIFATSN VTEPLDSISL EEESAFENSN LLHQGFTTTS
EDAYLEEYEG LQISDESHRS LMEEFPELNY ILKDKGVIKG YFEYGLAYLD ANMPFLHVPT
LHMLPLSSLL LLAICCLGGM LSPISDAKQA ARIFEKSILQ QIQSAILTEL EPSNDSLQVM
VIVEYIGHYS STGEQHRIAN LIHELVILHV RRKRLSLQSY DASVCGEESL NGRWRSWAQH
EALIRLVHCL FLNNTLHSIH FTYPNLQLAS LLKLPLPCSS NLWNAKTPNE WKREVSQIKP
EVGTCYLQTA MRILLGDSQR SDNRIVQGDF EENPFSMCIL IQGIASAVIE LNQAMPSTST
NAVRLLKSAD FKAALAQWWE HFSKMDDKIR EEEMAISALI YYHFTYILLY VDVNRIAMAA
GIPHAHDNAD PLEQDGEAQS NLNGERVCPH LLKILQLCLD ERHKPSLRPL DRGYTEFLTV
LIYSVYLTEL EDQKTRQPDR NRDRTGEHLQ PIAPLDLIAM KIDVHKTMRT VQDRLVCSSW
ELGQEASQVL DSILGGTSLM
//
