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Database: UniProt
Entry: V2XB33_MONRO
LinkDB: V2XB33_MONRO
Original site: V2XB33_MONRO 
ID   V2XB33_MONRO            Unreviewed;       394 AA.
AC   V2XB33;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Actin binding protein {ECO:0000313|EMBL:ESK96408.1};
GN   ORFNames=Moror_6916 {ECO:0000313|EMBL:ESK96408.1};
OS   Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS   (Crinipellis roreri).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK96408.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK96408.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK96408.1,
RC   ECO:0000313|Proteomes:UP000017559};
RX   PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA   Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA   Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA   Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA   Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT   "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT   Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT   mechanisms of the biotrophic and necrotrophic phases.";
RL   BMC Genomics 15:164-164(2014).
CC   -!- SIMILARITY: Belongs to the actin family. ARP2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00010121}.
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:ESK96408.1}.
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DR   EMBL; AWSO01000047; ESK96408.1; -; Genomic_DNA.
DR   RefSeq; XP_007844170.1; XM_007845979.1.
DR   AlphaFoldDB; V2XB33; -.
DR   STRING; 1381753.V2XB33; -.
DR   KEGG; mrr:Moror_6916; -.
DR   HOGENOM; CLU_027965_0_0_1; -.
DR   OrthoDB; 176764at2759; -.
DR   Proteomes; UP000017559; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; ACTIN; 1.
DR   PANTHER; PTHR11937:SF37; ACTIN-RELATED PROTEIN 2; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017559}.
SQ   SEQUENCE   394 AA;  45057 MW;  7113E2571037B462 CRC64;
     MDRSELPLVV DNGTGFVKVG YAGSNFPEHV FPSVVGRPIL RAEERISTAQ AQLRDIMVGD
     EAAQNRNYLQ VTQPMEHGII RNWEDMRHLW NYTFDEKLRI DPRGRKVLLT EPPMNPKKNR
     EKMAEVMFEE YGFGGVYVAI QAVLTLYAQG LTTGVVVDSG DGVTHIVPVY DGFSLPHLTR
     RLDIAGRDVT RYLIKLLLMR GYAFNRTADF ETVREIKEKL CYVSYDLDLD TKLSEETTVL
     VENYQLPDGR NIKVGSERFE APECMFQPHL VDVEQPGVAE MLFQTIQSAA VDVRADLYKH
     VVLSGGSSMY PGLPSRLEKE MKQLYLTRVL NGDPERLNKF KIKIEDPPRR KHMVFLGGAV
     LADIMKHREE FWVTREEWYE KGVQALDKLG RGEN
//
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