ID E2LRJ2_MONPE Unreviewed; 301 AA.
AC E2LRJ2;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=NodB homology domain-containing protein {ECO:0000259|PROSITE:PS51677};
DE Flags: Fragment;
GN ORFNames=MPER_09604 {ECO:0000313|EMBL:EEB91958.1};
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:EEB91958.1, ECO:0000313|Proteomes:UP000000741};
RN [1] {ECO:0000313|EMBL:EEB91958.1, 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:EEB91958.1}.
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DR EMBL; ABRE01014633; EEB91958.1; -; Genomic_DNA.
DR AlphaFoldDB; E2LRJ2; -.
DR STRING; 554373.E2LRJ2; -.
DR KEGG; mpr:MPER_09604; -.
DR HOGENOM; CLU_029940_0_0_1; -.
DR InParanoid; E2LRJ2; -.
DR OMA; ESCFEYG; -.
DR OrthoDB; 158513at2759; -.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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; PTHR43123; POLYSACCHARIDE DEACETYLASE-RELATED; 1.
DR PANTHER; PTHR43123:SF1; POLYSACCHARIDE 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 Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000000741}.
FT DOMAIN 72..301
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT NON_TER 301
FT /evidence="ECO:0000313|EMBL:EEB91958.1"
SQ SEQUENCE 301 AA; 34672 MW; 2F9A6666DC211B1E CRC64;
MDCPPFLPPR DFVGYGWNTP KDCWPDSAKI AVNFALNFEE GGESTLANGD DYSEGCLHEA
FHKIPYKGRR DQQLETMFEY GIRQGLPRII RLFDKYGYKF TTFAVGRALE LAPQYAKLLP
KLGHEIASHG YRWRSYVAMP PEEEKKHISD AIDSLQRLTG DQDVPAGWYF GRGSNQAKRL
IAREHHKRGL PLLYSSDSFA DELPFWVESP LASEGEKDEG LLIVPYSLDC DDHRFLCQGS
GWSTADDFFW HLKETFDYLY QEGLEGRPKM MTIGLHSRII GRPGRFRSLQ KYVFPEEYAF
M
//
