ID G1XS65_ARTOA Unreviewed; 1064 AA.
AC G1XS65;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=AOL_s00210g223 {ECO:0000313|EMBL:EGX44062.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX44062.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX44062.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
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:EGX44062.1}.
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DR EMBL; ADOT01000308; EGX44062.1; -; Genomic_DNA.
DR RefSeq; XP_011127327.1; XM_011129025.1.
DR AlphaFoldDB; G1XS65; -.
DR STRING; 756982.G1XS65; -.
DR GeneID; 22898228; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_010456_0_0_1; -.
DR InParanoid; G1XS65; -.
DR OrthoDB; 2582538at2759; -.
DR Proteomes; UP000008784; 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; 1.
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; 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; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000008784};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1064
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003427639"
FT DOMAIN 22..59
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 60..105
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 117..471
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 698..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 35..49
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 53..57
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 74..86
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 79..93
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 99..103
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 1064 AA; 117012 MW; C6B8F01A005C4D46 CRC64;
MIFHKLLPFL TLLLYLAVVQ AQAKCSAKVP CKVGCCSKYG NCGFGPDFCG TGCLNNCNAK
AECGKDAPAG KKNCPLNVCC SKYGFCGLTK DFCSKSAGCQ SNCSTPAPKC AANALGLRRV
GYYESWATTR RCAAVPPAKI RTTGLTHLIY SFASIDPHSF QIAPTSTLDA QLFGDVTALK
KTSPTLKVFI AVGGWAFNDP GPTRETFSKM VSTARTRKIF VDSVVLFIKS YGFDGIDIDW
EYPGALDRGG KPADTENYVL LVREMRQAFT AEAKGWGISI AIPASYWYLQ HFNLSAMARY
IDWFNLMSYD FVGAWDATNK WTGPYVGAHT NLTMTQQALD LMWRSKISGS KINMGLGFYG
RSFTLKSKAC TKPGCQFSKA GKPGRCSAAA GILMNIEIQD IQKKKKTKPV FDKVAGVKYM
SWDDQWVSFD DAESIAFKRH WAGTKCLGGL MIWALDHDTL DNVGLAAAVG VTPAKFVAMA
ATQERPPRTN CYIAFCGDKC VAGYSVFGYG SGSFSSTDAL GLRGSCDGGK FSSICCPSNS
MTKNPLDTCR WVGDEGLVSV VGPGPSRKRA GPAAPGLCRV GCPAGMTQIA QNTVTSQRRV
TRFDEQWTYG YCLEGYASYC CPDFTVDAKK SPPLLFYEDR TSLRKRGLEF LLAPLFGYGI
MFKELYIDPE PVFKPLKIGI DIGGKEVAGF PALPTDERPW DEFAPDPKDA PGSSSSEQDR
DSTGDYSPPE SESDSEDESD PNWVAYHVRD TVAGRTYGGH VAVASRRLIT TKDLTYICTY
THFPQVCENI RSAILVRGAP GVVNYLHNLG SRVVPRNWAR QHGARNSPQP NQHPNPWLVY
TIRPQRNTRI GANGAVVIRT TFPYFPTCEV DEYPFHSTSQ NNGPIVIGRL VPKEQNQAQG
QDWRNFLIAN RVSPVDRITI TWLLPRSKLN PYPWHSRYDL GQNGGCFPAK NHDPNSRIFD
PVFAVMTDDP FVASVDQKLN FVGGYHNTYP SQGLAIVPTP TDLNFLHLGR RDMTSSSPPI
PVQTRNLLHR RNPSHEVEGQ PVMLEPTRRI VTVPVISPTS QPTN
//
