ID A0A2S4PN83_9PEZI Unreviewed; 360 AA.
AC A0A2S4PN83;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Actin-like ATPase {ECO:0000313|EMBL:POS83500.1};
GN ORFNames=EPUL_005113 {ECO:0000313|EMBL:POS83500.1};
OS Erysiphe pulchra.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=225359 {ECO:0000313|EMBL:POS83500.1, ECO:0000313|Proteomes:UP000237438};
RN [1] {ECO:0000313|EMBL:POS83500.1, ECO:0000313|Proteomes:UP000237438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cflorida {ECO:0000313|EMBL:POS83500.1};
RA Wadl P.A., Mack B.M., Moore G., Beltz S.B.;
RT "Development of genomic resources for the powdery mildew, Erysiphe
RT pulchra.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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 + H(+) + phosphate; 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 -!- 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:POS83500.1}.
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DR EMBL; PEDP01001535; POS83500.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4PN83; -.
DR STRING; 225359.A0A2S4PN83; -.
DR OrthoDB; 10at2759; -.
DR Proteomes; UP000237438; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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; 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; 2.
DR PROSITE; PS00406; ACTINS_1; 1.
DR PROSITE; PS00432; ACTINS_2; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000237438}.
SQ SEQUENCE 360 AA; 40108 MW; EF9F9BC4A7D8BB31 CRC64;
MCKAGFAGDD APRAVFPSIV GRPRHHGIMI GMGQKDSYVG DEAQSKRGIL TLRYPIEHGV
VTNWDDMEKI WHHTFYNELR VAPEEHPVLL TEAPINPKSN REKMTQIVFE TFNAPAFYVS
IQAVLSLYAS GRTTGIVLDS GDGVTHVVPI YEGFSLPHAI ARVDMAGRDL TDYLMKILAE
RGYTFSTTAE REIVRDIKEK LCYVALDFEQ EIQTASQSSS LEKSYELPDG QVITIGNERF
RAPEALFQPS VLGLESGGIH VTTFNSIMKC DVDVRKDLYG NIVMSGGTTM YPGISDRMQK
EITALAPSSM KVKIIAPPER KYSVWIGGSI LASLSTFQQM WISKQEYDEA GPSIVHRKCF
//
