ID K3UNZ2_FUSPC Unreviewed; 452 AA.
AC K3UNZ2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=NodB homology domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=FPSE_05810 {ECO:0000313|EMBL:EKJ74036.1};
OS Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ74036.1, ECO:0000313|Proteomes:UP000007978};
RN [1] {ECO:0000313|EMBL:EKJ74036.1, ECO:0000313|Proteomes:UP000007978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS3096 {ECO:0000313|EMBL:EKJ74036.1,
RC ECO:0000313|Proteomes:UP000007978};
RX PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT "Comparative pathogenomics reveals horizontally acquired novel virulence
RT genes in fungi infecting cereal hosts.";
RL PLoS Pathog. 8:E1002952-E1002952(2012).
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}.
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:EKJ74036.1}.
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DR EMBL; AFNW01000123; EKJ74036.1; -; Genomic_DNA.
DR RefSeq; XP_009257203.1; XM_009258928.1.
DR AlphaFoldDB; K3UNZ2; -.
DR SMR; K3UNZ2; -.
DR EnsemblFungi; EKJ74036; EKJ74036; FPSE_05810.
DR GeneID; 20364428; -.
DR KEGG; fpu:FPSE_05810; -.
DR eggNOG; ENOG502S2CW; Eukaryota.
DR HOGENOM; CLU_021264_11_3_1; -.
DR OrthoDB; 1343935at2759; -.
DR Proteomes; UP000007978; Chromosome 3.
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; 2.
DR CDD; cd11618; ChtBD1_1; 1.
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 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:UP000007978};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..452
FT /note="NodB homology domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003866205"
FT DOMAIN 33..78
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 111..309
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT DOMAIN 346..394
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 408..452
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DISULFID 44..56
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 49..63
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 367..381
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 426..440
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 452 AA; 48750 MW; F7C10CBB66AB76C9 CRC64;
MKGSFASLVA LLAVNVVATP SFRNIFGLEK RQAGRCGTGF GGVCAANECC SSAGWCGTGY
LYCSAPSCQI EYGPGCDANV RPTGPDTTNV ARPKVGSIPY GQAIYRCNRN GDIAITYDDG
PYTYTEDLLD LLQRYNVKAT FYITGRNLGK GAINDPATPW PGLIRRMIRD GHQIASHTWS
HQRLTTLSRA KFWNQMIFNE IAFADILGYF PTYMRPPYSA SNATTDAWLG ELGYHVTYFN
LDTEGYLHDS PNTIGTSKQI WDTTVEGKSP ASNKWLHIEH DPVYQSVYNL TEYMLKSLVR
NNFRGVTVGE CLEDPKANWY RSVTPSSAST TTTAATSSAT FPLTTNGRCG SRHGGATCRG
EFNGETCCSQ NGWCGSTDAH CGRGCQPVFG TCSGVSEPAG PEPTATNPGR CGSAFGGKKC
DQWDPCCSRA GWCGTSSDHC GSGCQSAFGT CN
//
