ID N1S0G2_FUSC4 Unreviewed; 444 AA.
AC N1S0G2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Bifunctional xylanase/deacetylase {ECO:0000313|EMBL:EMT68005.1};
GN ORFNames=FOC4_g10012404 {ECO:0000313|EMBL:EMT68005.1};
OS Fusarium oxysporum f. sp. cubense (strain race 4) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=2502994 {ECO:0000313|EMBL:EMT68005.1, ECO:0000313|Proteomes:UP000016929};
RN [1] {ECO:0000313|Proteomes:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
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; KB726554; EMT68005.1; -; Genomic_DNA.
DR AlphaFoldDB; N1S0G2; -.
DR STRING; 1229665.N1S0G2; -.
DR HOGENOM; CLU_021264_11_3_1; -.
DR Proteomes; UP000016929; 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:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd10951; CE4_ClCDA_like; 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; 2.
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 Carbohydrate metabolism {ECO:0000313|EMBL:EMT68005.1};
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}; Glycosidase {ECO:0000313|EMBL:EMT68005.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EMT68005.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Polysaccharide degradation {ECO:0000313|EMBL:EMT68005.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016929};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:EMT68005.1}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..444
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004111092"
FT DOMAIN 33..78
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 111..306
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT DOMAIN 344..392
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 399..444
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT REGION 320..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 44..56
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 49..63
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 365..379
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 418..432
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 444 AA; 48572 MW; CAC2F1F263F8A0F9 CRC64;
MKSITLLIAF LVGFSIASPW STLFSRSLDR RQAGRCGTGF GTVCGRNECC SSAGWCGTGY
LYCSAPSCQI EYGPGCDANV RPGGPDTTNV ARPKVGSIPY GQAIYRCNRN GDIALTYDDG
PYTYTEDLLN LLQRYNAKAT FYITGRNLGK GAINDPDTPW PVLIRRMVRD GHQIASHTWS
HQRLTTLSRS KFWNQMIYNE IAFADILGYF PTYMRPPYSA SNTTTDAWLN ELGYHITYFN
LDTEGYLHDS PNMISTSKQI WDNTVEGRSP ATNKWLHIEH DPVYRTVYNL TEYMLRSIRR
NNFTAVTVGQ CLQDPPSNWY RTVSSSPSPT STSSSSPTFP ATTNGRCGSR HGGATCRGEP
NGETCCSQNG WCGGTSDHCG RGCQPVFGTC RDTPEPAAPG RCGAAHGSAR CTESGWGCCS
RAGWCGSTSD HCGTGCQSDF GTCN
//
