ID   A0A0L6VTZ3_9BASI        Unreviewed;       555 AA.
AC   A0A0L6VTZ3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KNZ64161.1};
GN   ORFNames=VP01_105g10 {ECO:0000313|EMBL:KNZ64161.1};
OS   Puccinia sorghi.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ64161.1, ECO:0000313|Proteomes:UP000037035};
RN   [1] {ECO:0000313|EMBL:KNZ64161.1, ECO:0000313|Proteomes:UP000037035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ64161.1,
RC   ECO:0000313|Proteomes:UP000037035};
RA   Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA   Sacco F.;
RT   "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT   Schw, the Causal Agent of Maize Common Rust.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:KNZ64161.1}.
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DR   EMBL; LAVV01000666; KNZ64161.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6VTZ3; -.
DR   STRING; 27349.A0A0L6VTZ3; -.
DR   VEuPathDB; FungiDB:VP01_105g10; -.
DR   OrthoDB; 2641150at2759; -.
DR   Proteomes; UP000037035; Unassembled WGS sequence.
DR   Gene3D; 3.30.420.40; -; 3.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; ACTIN; 1.
DR   PANTHER; PTHR11937:SF387; ACTIN; 1.
DR   Pfam; PF00022; Actin; 1.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
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:UP000037035};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..555
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005568773"
SQ   SEQUENCE   555 AA;  60539 MW;  0A70E7B9F49B8388 CRC64;
     MAAFRDANLL IVFLSTHAHS IQVGLGVSPE VIQTPSITLP TIAYIKPELA QSNLPRKWSD
     YSFEPHPDLV SVPLFSTPSP HDPQLSQSRP LVSDWKALDA LFRYLLFNRL KLSKPPVAQH
     ILLSIPPNLP NSTRDKFTQL FFENLQAPAL FLAESPLLQL LACSCTSGIT IDIGARSTLI
     GVVSDSIVLD HSCHFYPIGE QDCDDYLISL LLNENPELPT QLGWTPANQP ETLYHALLAF
     ISNLKADGHI RFEPQLNTLA LSAADLRSSG EEEGGITDVA QAIVSGKADK IIGRQTSNNS
     SQAARRPTQT GKLLAEIHKE TDTIIVLNSS NSQPASNPSV PPSPLLDCQP SQAIPLSAGS
     LSLPREQAGI RVSKTRHQHA EPFFAPTLLR SIGPVFSRFG LEKYAARYTE ELTAEDDTLV
     DSIHRSISKL ISSEQRKDVV GHSSRLIPSI TQTHTIRSGL GIAISAELQT RNPGLNSLAQ
     AGSNQGEGIF KPLKVPEYFS EFKGKPEYLG FLGGCIVAKL AFNDASSTKL WMSKPDYNKE
     GPYISRKLFG LQSSS
//