ID A0A096X9B0_9PEZI Unreviewed; 122 AA. AC A0A096X9B0; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 27-NOV-2024, entry version 11. DE SubName: Full=Actin {ECO:0000313|EMBL:AHE77496.1}; DE Flags: Fragment; GN Name=act {ECO:0000313|EMBL:AHE77496.1}; OS Macrophomina phaseolina. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes; OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae; OC Macrophomina. OX NCBI_TaxID=35725 {ECO:0000313|EMBL:AHE77496.1}; RN [1] {ECO:0000313|EMBL:AHE77496.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CPC 21477 {ECO:0000313|EMBL:AHE77496.1}; RA Sarr M.P., Ndiaye M., Groenewald J.Z., Crous P.W.; RT "Genetic diversity in Macrophomina phaseolina, the causal agent of charcoal RT rot."; RL Phytopathol. Mediterr. 53:250-268(2014). CC -!- FUNCTION: Actins are highly conserved proteins that are involved in CC various types of cell motility and are ubiquitously expressed in all CC eukaryotic cells. {ECO:0000256|ARBA:ARBA00003520}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC Evidence={ECO:0000256|ARBA:ARBA00001836}; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000256|ARBA:ARBA00004245}. CC -!- SIMILARITY: Belongs to the actin family. CC {ECO:0000256|ARBA:ARBA00006752, ECO:0000256|RuleBase:RU000487}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KF951889; AHE77496.1; -; Genomic_DNA. DR AlphaFoldDB; A0A096X9B0; -. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1. DR FunFam; 2.30.36.70:FF:000001; Actin, alpha skeletal muscle; 1. DR FunFam; 3.30.420.40:FF:000291; Actin, alpha skeletal muscle; 1. DR Gene3D; 3.30.420.40; -; 1. DR InterPro; IPR004000; Actin. DR InterPro; IPR020902; Actin/actin-like_CS. DR InterPro; IPR004001; Actin_CS. DR InterPro; IPR043129; ATPase_NBD. DR PANTHER; PTHR11937; ACTIN; 1. DR PANTHER; PTHR11937:SF387; ACTIN; 1. DR Pfam; PF00022; Actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR SUPFAM; SSF53067; Actin-like ATPase domain; 1. DR PROSITE; PS00406; ACTINS_1; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212}; KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}. FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AHE77496.1" FT NON_TER 122 FT /evidence="ECO:0000313|EMBL:AHE77496.1" SQ SEQUENCE 122 AA; 13789 MW; 54E4DC541812E5A4 CRC64; GFAGDDAPRA VFPSIVGRPR HHGIMIGMGQ KDSYVGDEAQ SKRGILTLRY PIEHGVVTNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP INPKSNREKM TQIVFETFNA PAFYVSIQAV LS //