GenomeNet

Database: UniProt
Entry: A0A094G9G6_9PEZI
LinkDB: A0A094G9G6_9PEZI
Original site: A0A094G9G6_9PEZI 
ID   A0A094G9G6_9PEZI        Unreviewed;      2061 AA.
AC   A0A094G9G6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN   ORFNames=V496_00977 {ECO:0000313|EMBL:KFY68562.1};
OS   Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY68562.1, ECO:0000313|Proteomes:UP000029302};
RN   [1] {ECO:0000313|EMBL:KFY68562.1, ECO:0000313|Proteomes:UP000029302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
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: 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:KFY68562.1}.
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; JPJY01000140; KFY68562.1; -; Genomic_DNA.
DR   STRING; 1420909.A0A094G9G6; -.
DR   HOGENOM; CLU_001614_0_0_1; -.
DR   OrthoDB; 1863779at2759; -.
DR   Proteomes; UP000029302; Unassembled WGS sequence.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
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; cd06548; GH18_chitinase; 1.
DR   Gene3D; 3.10.50.10; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR029070; Chitinase_insertion_sf.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
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:SF317; CHITINASE 11; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR   SUPFAM; SSF81383; F-box domain; 1.
DR   PROSITE; PS50181; FBOX; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000029302}.
FT   DOMAIN          1206..1573
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   DOMAIN          1814..1860
FT                   /note="F-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50181"
FT   REGION          451..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1602..1684
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..470
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..564
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..601
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..653
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2061 AA;  232828 MW;  8B4F013EF73181F0 CRC64;
     MDSCSRICFL YMAFGDELTL QEVGPRLEKN LTMLLPNGST YFGSTWARPK SCLAGVIIRF
     PKEEDWQDWV LSAFGRQVKP QTTRKQRRDQ AEELWLTKST ALFEPITRTD LSTAPDWILA
     NSKNSFDDVN GWARPFTRYS APVQVPQNPS DSEDFLRDKQ ERIVSLGCNK HCGGGVFGDF
     DSLLQTSSKE LSPQRRSARA LEQIQIPCLP LLRSITIYCH IYPILNNLHD PKRKPDLKHT
     SAPYPAKTTM AITRFISPRD ARNVNTSSRP QISTVAAKGG GVNQRLQSNL FQDLEVAVSQ
     HEKSTEAVLQ ILRKLKSKWS MDEPDFTSNP FEDWILRNVN EEVWQSAITI MYKAKIDESD
     IKLKQKVEQI ATSLKIEPNR LFFHIGESVL CSTRGISSLK SLVTLSNNNF DLVLKSIHGA
     RQERLTSKEG KASKKSVRED IITVSDITDA MTEKKERKEE TEKLKAQKEK AQVEAQAQVD
     AETQREREAA EAQAQADAGE REEEAQRERE AAEARAQADA GEREEEAQRE AAEAQAQADA
     GEREEEAQRE GKAAEAQGQT DAEEREEGQE AEPEERAGAQ KDADSQKDTV SQKDQEGADM
     QKDTQSQKNG AQQKQTESLR DRELQTVTGT LQETDVQKDI HTQKNGTQQT QTETLREAPK
     MVKRKYNERQ SKCGAQSKRL RPCVKVGTTQ WSPQKRLPIT GALREKRRRK GRYEEKRKLY
     RQQKRQLSAY PQGIPTQIQF EGLQGLCSAQ KQQDDLFNDE RRHALLRAYH QVCKEDPNTH
     LANAGQLAIY IFQYGRPAKV WTAGSEGSQN VGFSADTISI HGKCNCKYDE ADILLLTERE
     HAMWAANNND PKIIIIRDHK FLDRRPHQTF QRWFDEMEIE AQVSITPMKI DVQVLNEDTS
     TPAVQNMTIQ DAFTLWRDAE ASPEICIQHP PVNFLNIADS GYGCWPGGIT KHYGYLRKIV
     SFCESFNHSR EESNVGKPTS LQLSPVDIQK CMGFSIVAQR GAASGWHEDQ NGVTTVLTLE
     GNDDNSKAED VVKYWPVFPI NRFRPEEQDA FREDFKEHGE KWRPKLQGAQ IPVIALVCGD
     TLIQPPGTIH APITLTNCMF TGAMVWRERD LKQSLTEWLF LAENANCTNE PLPQQTPEIL
     QYLLPRVKLE PRKFGYTAEE LPLFEDTCHR LLFLTTEGRG CGCSTACGKR CGCSKKGIPC
     GVECHKGLGR DWTCCLPLPA VYDRKFFPKD LPAKDLTHVL YAFANIRPDG EVFLSDEEAD
     TKKHFEADSI TNDDGANLYG CLQQLYMLKK KNRYLKVLLS IGGWSYRDNF AVPAATLAGR
     SRFASSVVSL VRNLGLDGVD IDWEYPTDNS QAENFVYLLR EVRTALDAYS NSLSEPYPFL
     LTVAAPAGPQ QYQTLHLAKM DQYVDFWNLM AYDYSSPKTA THRANLFHDS INPKSTPFNT
     NATVDYYVSQ GGIRPKKIVL GIPIYGHAFN HTDGLGHPSI DAVSGTWEAG TYDFKVLPMA
     GSEGHIVDKL GASYSYDNTT RELISYDNMY IVLQKANWLK EMDLGGAMWW ESSADAIGDN
     SLIRAATVTL KIRSNLDNTL NQLDYPDSIY ANIRARMSDS ETNWTTSSKP VKSNACSTTS
     VSTTSDATTF DATPSDATPS DATTSDATTS DATTSDATTS DATLPMLTTS DATSDATTSA
     TTTTSSTAAN HRLTIQKWTG LGCTGSMLEN DYIPSEQELN TLNRSPNPYL SFSISRPLRG
     REQLDLSTEP GVSSCRKFLH SYWPRDSPGS KQSYLKVASQ LKRPHYYGSQ EQFKDDEEAE
     LPLKQQRYSS YNGTITLSQL PVEILLQIMS EIQDRRTLVR LCLVSTVFQG VFNMRKWEFL
     RSAFTKEVTQ TQYHIHNITI IISKHIKKHL KGVSMLFEVT WEGLINEGRL DGAVYFVDSL
     CHGLDRHDYN MLLQLLRTMY DHVVLETSWD VWAGAFTATN FLINYHSWEA YELRLGAPFQ
     SEQSTYNIRE MYDWIEHQSV SRWREIVGQD TLNVNWGNVY FVLTSLQTYG KDEEDELIQA
     IITLFKKRTI AKRDGSPNKV L
//
DBGET integrated database retrieval system