ID A0A094H0Y5_9PEZI Unreviewed; 1320 AA.
AC A0A094H0Y5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 26.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=V499_02830 {ECO:0000313|EMBL:KFY77882.1};
OS Pseudogymnoascus sp. VKM F-103.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY77882.1, ECO:0000313|Proteomes:UP000029295};
RN [1] {ECO:0000313|EMBL:KFY77882.1, ECO:0000313|Proteomes:UP000029295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY77882.1,
RC ECO:0000313|Proteomes:UP000029295};
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:KFY77882.1}.
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DR EMBL; JPKB01000433; KFY77882.1; -; Genomic_DNA.
DR HOGENOM; CLU_001482_0_0_1; -.
DR Proteomes; UP000029295; 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; cd00035; ChtBD1; 1.
DR CDD; cd02878; GH18_zymocin_alpha; 1.
DR CDD; cd00118; LysM; 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 Gene3D; 3.10.350.10; LysM domain; 2.
DR InterPro; IPR001002; Chitin-bd_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 InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR PANTHER; PTHR47700:SF1; CHITINASE-RELATED; 1.
DR PANTHER; PTHR47700; V CHITINASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G13720)-RELATED; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR Pfam; PF01476; LysM; 1.
DR SMART; SM00270; ChtBD1; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SMART; SM00257; LysM; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
DR PROSITE; PS51782; LYSM; 2.
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}; Disulfide bond {ECO:0000256|PROSITE-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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1320
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001898257"
FT TRANSMEM 1198..1226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 334..380
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 399..447
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 460..529
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 541..929
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DISULFID 485..497
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 490..504
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 523..527
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 1320 AA; 142147 MW; 781D97812DE5EFF0 CRC64;
MRIAVVAALA ATLPIAHAAP QLAPSPAIIQ GRTPADSQVL HNVQLQYCPL ACEYAGPNTV
SWTTYHSYDE LALCNNTVLF TLNIRGSTLE PRIKACSTTG GGPRMQAGAF YGLRHNNITK
SPSPEIITQM FAPAERKIVS KDGSCGATLR KATLEMETKW SSQQGTSSTH ELSAALSQLE
NYFRNTASCG SALMFARSKN SVVGAFAGGD LTKSTVADLI KGSGELAGIT LPGQYAVQAC
GAQGNEPAFD TRFGLFADLN GNAASVQAFL GDYSAAVGKC VDLKDLETGD GPISKSVTIL
GSSITVDGAV LKNTTSNSTT FNQSRSVHAR ALCRDIKVNQ FDGCPSLAQT CGISGNDFMK
YNSNKANLCS TLMPGQYVCC SAGDLADHTP QTLPGGDCFP YTIKDKDICW DIADAYNIDV
ARIEESNKKT FGFAGCGQLY EHQKICLSSG NPPMPAQDPT TLCGPWVVGT TRPANYDDVA
KLNPCPLNAC CDIWGQCGTT DEFCTKSEVG GHPGTAKPFT NGCISNCGTD IVNNAEKPSK
FARIGYFEGF NKKRPCLRMD VTQFDFTLFT HIHFAFATIS TDFKVTIAAD VKDQFDKMVA
IDSKGSKKIL SFGGWSFSTD YDTAPIFSKS VSPANREIFA TNVVQFLKDN KLDGLDFDWE
YPGATDIPNS VPGNADDGAN YLAFLKSVKS KLAADKTLSI ALPSSYWYLR GFPVQEMAKV
VNYFVYMTYD LHGQWDYGSK WSNPGCPTGN CLRSHVNLTE TVNAISMLTK AGAKGNQIML
GVASYGRSFK MKNPLCTGVT CEFTGSPSVS DADPGICTGE PGYISNAELN FIRNSAEFEE
DNLSMDWVDT DSNSNIMTYD GNWVSYMNDV TKFGRILIAD GLNLGGTTDW AVDLNAFLDP
VEGDNSGGEA IHSEPVPICD ARFDDMGGLA IFALLGKVPA VCRSIYAIDA TATMLDSTIA
NYSDVTNNYD GKFGYFEQYI KDLVDPQLWN WMDYAGTDQE TKQGLGNRFF NCKFVPGDNP
KSAVTYNGPC PVPLSIMSQG KPEAQIPKLA FTITYTMRGD KAAFEEGLAA DLGMMPDYVI
FEDTNMTPGC PAPGPDDPLC YDPPQWHLGT YPRKNESMTV QDPKKIWDQA LPNISRLKNN
LTATAMSIGL GQYDPYYNPE DAAVALFVPV QLLAQAVDNM AQVKEIGEKI EAQKKKELIL
LIVSVILAVV PFLAELSFSM VGLVALARFA FVAGEIGNGA LAISEIIESP TSAPIAIMGM
VLGIGGGAGL RSEEAFAEAG KARRVMTDVH ISGMGKVYKK MDDSIQISMA ACYRKGSILG
//