ID A0A1Y2MFK4_EPING Unreviewed; 589 AA.
AC A0A1Y2MFK4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=NodB homology domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=B5807_00423 {ECO:0000313|EMBL:OSS54028.1};
OS Epicoccum nigrum (Soil fungus) (Epicoccum purpurascens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Epicoccum.
OX NCBI_TaxID=105696 {ECO:0000313|EMBL:OSS54028.1, ECO:0000313|Proteomes:UP000193240};
RN [1] {ECO:0000313|EMBL:OSS54028.1, ECO:0000313|Proteomes:UP000193240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP 19927 {ECO:0000313|EMBL:OSS54028.1,
RC ECO:0000313|Proteomes:UP000193240};
RA Fokin M., Fleetwood D., Weir B.S., Villas-Boas S.G.;
RT "Genome sequence of the saprophytic ascomycete Epicoccum nigrum ICMP 19927
RT strain isolated from New Zealand.";
RL Genome Announc. 0:0-0(2017).
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; KZ107838; OSS54028.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2MFK4; -.
DR STRING; 105696.A0A1Y2MFK4; -.
DR InParanoid; A0A1Y2MFK4; -.
DR OMA; HEQTAMN; -.
DR OrthoDB; 1343935at2759; -.
DR Proteomes; UP000193240; 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; cd11618; ChtBD1_1; 3.
DR Gene3D; 3.30.60.10; Endochitinase-like; 4.
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; PF01522; Polysacc_deac_1; 1.
DR SMART; SM00270; ChtBD1; 4.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 4.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 4.
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:UP000193240};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..589
FT /note="NodB homology domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010992809"
FT DOMAIN 67..111
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 145..344
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT DOMAIN 388..434
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 471..517
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 544..589
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT REGION 362..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 77..89
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 82..96
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 407..421
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 490..504
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 563..577
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 589 AA; 60641 MW; 5BA01C0346035C45 CRC64;
MHFSTLAAVA AIAPLVSAHG GMGLPKIAGI NMRDLKSRDL LANLEARIAE VKTAHAHENR
LAARQDDRQC GAGIGSCAAG QCCSGAGYCG TEDDYCYSPG CDYEHGPGCP ENVTPSGTNT
SSIARTKVGN VAYGGAGIYN CVTPGTVALT YDDGPQKEYT EHVMDVFKTY GGKATFFITG
NNINKGQIDI TPEHAAAIKR MDAEGHQIAS HTWTHLDLSA VSSTDRKQQM WKNEMALRNI
VGKIPTYMRP PYSSCTAESG CEKDLADLGY HVTYFDVDTD DYNQDDVNKI QNSKNYFKGN
VTANGASAAS SQWLAIGHDI HYQTVYNLTD YMLSTITQLG YKSVTVGECL GDPEANWYRA
ADGAGTQPSG TQTSTAAAPT GTNKVSTDGN CGSTAGSTCL GSTFGNCCSQ YNYCGSTTDH
CGTGCQSGFG NCGGNGAVSS KAATSTVKPA TSTVKTSAAP TATTASKVST DGTCAGTGKQ
TCAGSTFGNC CSQSGWCGST TDYCGTGCQT GFGTCGSLSA SKAANPTSTK PAATSAAAKK
ISTDGTCAGT GGFTCQGSTF GNCCSQYGWC GSTTGHCTSG CQSGFGTCS
//
