ID A0A0D9QQP9_PLAFR Unreviewed; 488 AA.
AC A0A0D9QQP9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Actin-like protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AK88_01126 {ECO:0000313|EMBL:KJP89248.1};
OS Plasmodium fragile.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5857 {ECO:0000313|EMBL:KJP89248.1, ECO:0000313|Proteomes:UP000054561};
RN [1] {ECO:0000313|EMBL:KJP89248.1, ECO:0000313|Proteomes:UP000054561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=nilgiri {ECO:0000313|Proteomes:UP000054561};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Duraisingh M., Young S.K., Zeng Q., Gargeya S., Abouelleil A.,
RA Alvarado L., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium fragile nilgiri.";
RL Submitted (MAR-2014) 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}.
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DR EMBL; KQ001653; KJP89248.1; -; Genomic_DNA.
DR RefSeq; XP_012334187.1; XM_012478764.1.
DR AlphaFoldDB; A0A0D9QQP9; -.
DR EnsemblProtists; KJP89248; KJP89248; AK88_01126.
DR GeneID; 24266440; -.
DR VEuPathDB; PlasmoDB:AK88_01126; -.
DR OMA; GASICSN; -.
DR OrthoDB; 217775at2759; -.
DR Proteomes; UP000054561; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.40; -; 1.
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; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840}.
FT REGION 29..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 488 AA; 56821 MW; A77635B18E72A391 CRC64;
METPDFFRYN EIFHNYSEDK KGVYDVVGTV SEGDDSAGQG EKCANLDQQK KNANQNQSEK
EANPDPNEGS VDQDQRLNSV DPDQRLPGTG SRKNEGSLIY HYEYKFHQDE KLWSKFFEEF
TFHIFRKLIK TSNKAKKVIV LLNMFIPTVI KYSLCKSLIE NYEYASISYI NDLVSPLFLC
NCNTCVVIDL GYLSCRLLPV MNGMPLYHHY AYVDNGGFYI NMEIKRLLKE QYVRRARRRK
AVDDWEASSA SFVQGNDGDI VANTQSPDDD YKATPHEEKN TEGEKGERET SHELLNYYLD
LYPLEEILNV IDSMPDDEIE NMKIKFFYLK NEETKLYSNK MVLYEFQNYE ILVEADTRWM
ACEILFTKDY EQNINSMFAS ILSKLHMFEF SAFHNVLLVG GCSNIKGIIS KIAQSLFQAL
REKKKTSVKD LENRVNFLFP KISPNLRQFI GASICSNLEN LPDYTQEHVH NNVLYDHLNE
DVYFTFKR
//
