ID X0CHH6_FUSOX Unreviewed; 471 AA.
AC X0CHH6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Chitin binding protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=FOQG_07101 {ECO:0000313|EMBL:EXK90274.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK90274.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK90274.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK90274.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00261}.
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DR EMBL; JH658375; EXK90274.1; -; Genomic_DNA.
DR AlphaFoldDB; X0CHH6; -.
DR HOGENOM; CLU_021264_11_3_1; -.
DR Proteomes; UP000030663; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd10951; CE4_ClCDA_like; 1.
DR CDD; cd00035; ChtBD1; 1.
DR CDD; cd11618; ChtBD1_1; 2.
DR Gene3D; 3.30.60.10; Endochitinase-like; 3.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR PANTHER; PTHR46471; CHITIN DEACETYLASE; 1.
DR PANTHER; PTHR46471:SF2; CHITIN DEACETYLASE-RELATED; 1.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SMART; SM00270; ChtBD1; 3.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 3.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 3.
DR PROSITE; PS51677; NODB; 1.
PE 4: Predicted;
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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030663};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..471
FT /note="Chitin binding protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004939418"
FT DOMAIN 49..94
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 127..323
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT DOMAIN 364..411
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 423..469
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DISULFID 59..71
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 64..78
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 384..398
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 442..456
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 471 AA; 50879 MW; 2C070942DD18DA00 CRC64;
MKSLTLLSLA ALLSIVFAHG FMVRRKGAEF NIAARHEHAS AQSEGLEKRA SCGKDIGSCP
KGQCCSAAGY CGTTSPYCSS PQCQMDYSNG NCDGSKKPKG GTTANIPRST TGKVPYNVYI
TNCTTPGTFA LTFDDGPYKY TDQVLDVLKQ NNIKATFFIT GTNLGKGQID DETTGWPRIL
RRMYSEGHQL ASHTWSHQDL TASSDEVRQQ QVIYNEMAFR NIFGFFPKYL RPPYGTCNRV
SGCLDYATNL GYHVINWNLD PKDFENNTPD KIQTSKNTFS NGVSTNAKAN AYIELSHDVQ
EQTAYNLTAF MIKTIKDRGY RAVPVGECLG DVRENWYVTD PNFQPSMPVY SATPSPSPTA
ATKDGTCGAK DGGTKCTGSK WGDCCSYNSF CGSTSGYCDG GCQTDFGKCN KWTTGSALIV
SANGLCGDKY HQTCKGSTYG DCCSKGGNCG KTSAYCGTGC QSGFGTCTSS K
//
