ID M2T626_COCSN Unreviewed; 482 AA.
AC M2T626;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Carbohydrate esterase family 4 protein {ECO:0000313|EMBL:EMD64661.1};
GN ORFNames=COCSADRAFT_115527 {ECO:0000313|EMBL:EMD64661.1};
OS Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot and
OS spot blotch fungus) (Bipolaris sorokiniana).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD64661.1, ECO:0000313|Proteomes:UP000016934};
RN [1] {ECO:0000313|EMBL:EMD64661.1, ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2] {ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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; KB445642; EMD64661.1; -; Genomic_DNA.
DR RefSeq; XP_007699270.1; XM_007701080.1.
DR AlphaFoldDB; M2T626; -.
DR GeneID; 19130285; -.
DR KEGG; bsc:COCSADRAFT_115527; -.
DR eggNOG; ENOG502QRIP; Eukaryota.
DR HOGENOM; CLU_021264_11_3_1; -.
DR OMA; ENWYRSV; -.
DR OrthoDB; 1343935at2759; -.
DR Proteomes; UP000016934; 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; 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; 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}; Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00261};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000016934};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 67..113
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 147..341
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT DOMAIN 379..424
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 436..482
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DISULFID 70..85
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 79..91
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 84..98
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 397..411
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 456..470
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 482 AA; 50561 MW; 1783BD0019933501 CRC64;
MRFSDVATAA LVAPLVAAHG GVPGAPKLFG LPRHLQDDFK APVAARTLRH SSEPRHGLLE
TRQGGQNGRC GPGFGNAKCA AGYCCSGAGY CGTSKDHCSA PDCLIDFGPA CDANKTPGGA
STRNDARPQK GNVPYGGEGI YVCQKPGTVA ITYDDGPYIY TDRVLDQFNK YGFKATFFVT
GINIGKGAID TTAQWANVIK RMVAEGHQVA SHTWSHQDLS VITEEQRYDQ MVKNEMAIRN
IIGKYPTYMR PPYSSCNAAC QGVMKKLGYV VSYFDLDTDD YNQLKNIQVA KDNFKRILDS
TAGGPATGDR LAIAHDIHEQ TALNLTGYML EYLKSKGYRG VTMGECMGEP EANWYRKSGE
VVNPPSNGGG NGGTPVSTDG QCGSGKGTCA GSPFGNCCSS FGWCGSTEGH CKAGCNSAFG
TCTGGSTSPS KPISTDGQCG AKASGATCQG SPFGNCCSQF GWCGSSQGHC GAGCDKTSGT
CS
//
