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Database: UniProt
Entry: A0A094H0Y5_9PEZI
LinkDB: A0A094H0Y5_9PEZI
Original site: A0A094H0Y5_9PEZI 
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
//
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