ID E2LY54_MONPE Unreviewed; 228 AA.
AC E2LY54;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=NodB homology domain-containing protein {ECO:0000259|PROSITE:PS51677};
GN ORFNames=MPER_12235 {ECO:0000313|EMBL:EEB89647.1};
OS Moniliophthora perniciosa (strain FA553 / isolate CP02) (Witches'-broom
OS disease fungus) (Marasmius perniciosus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=554373 {ECO:0000313|EMBL:EEB89647.1, ECO:0000313|Proteomes:UP000000741};
RN [1] {ECO:0000313|EMBL:EEB89647.1, ECO:0000313|Proteomes:UP000000741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FA553 / isolate CP02 {ECO:0000313|Proteomes:UP000000741};
RX PubMed=19019209; DOI=10.1186/1471-2164-9-548;
RA Mondego J.M., Carazzolle M.F., Costa G.G., Formighieri E.F., Parizzi L.P.,
RA Rincones J., Cotomacci C., Carraro D.M., Cunha A.F., Carrer H., Vidal R.O.,
RA Estrela R.C., Garcia O., Thomazella D.P., de Oliveira B.V., Pires A.B.,
RA Rio M.C., Araujo M.R., de Moraes M.H., Castro L.A., Gramacho K.P.,
RA Goncalves M.S., Neto J.P., Neto A.G., Barbosa L.V., Guiltinan M.J.,
RA Bailey B.A., Meinhardt L.W., Cascardo J.C., Pereira G.A.;
RT "A genome survey of Moniliophthora perniciosa gives new insights into
RT Witches' broom disease of cacao.";
RL BMC Genomics 9:548-548(2008).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}.
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:EEB89647.1}.
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DR EMBL; ABRE01017243; EEB89647.1; -; Genomic_DNA.
DR AlphaFoldDB; E2LY54; -.
DR KEGG; mpr:MPER_12235; -.
DR HOGENOM; CLU_021264_11_2_1; -.
DR InParanoid; E2LY54; -.
DR OMA; PWIYNDE; -.
DR OrthoDB; 1343935at2759; -.
DR Proteomes; UP000000741; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004099; F:chitin deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR CDD; cd10951; CE4_ClCDA_like; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
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 SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS51677; NODB; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000741};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..228
FT /note="NodB homology domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003160311"
FT DOMAIN 36..221
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 228 AA; 25399 MW; E8C29FB965C8F717 CRC64;
MKLALLVALV ATASTLAAPG KRQNLATVYT TCSQPNTIAF TFDDGPWIYN DEIVSFLGEQ
GIKATFFFNG NNWDCIYNND AMNRVKNVYN NGHMIGSHTW SHADLTTLSW DQIHDEMWRV
EQALQRIIGV TPAFMRPPYG NYNDLVRQAS AVRGQSLVNW DFDSGDSVGA SPEQSKSDYA
NLIQQHPNTV IALNHETEQS TAEDVIRTVI PELKNAGYTL LRSPNASE
//
