ID D2VS98_NAEGR Unreviewed; 347 AA.
AC D2VS98;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Actin {ECO:0008006|Google:ProtNLM};
GN ORFNames=NAEGRDRAFT_83258 {ECO:0000313|EMBL:EFC40304.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC40304.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC40304.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
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; GG738893; EFC40304.1; -; Genomic_DNA.
DR RefSeq; XP_002673048.1; XM_002673002.1.
DR AlphaFoldDB; D2VS98; -.
DR STRING; 5762.D2VS98; -.
DR EnsemblProtists; EFC40304; EFC40304; NAEGRDRAFT_83258.
DR GeneID; 8854819; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_83258; -.
DR eggNOG; KOG0676; Eukaryota.
DR InParanoid; D2VS98; -.
DR OMA; DTMCDED; -.
DR OrthoDB; 3106646at2759; -.
DR Proteomes; UP000006671; 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; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; ACTIN; 1.
DR PANTHER; PTHR11937:SF387; ACTIN; 1.
DR Pfam; PF00022; Actin; 2.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671}.
SQ SEQUENCE 347 AA; 38660 MW; A85F1A7C2C7D060E CRC64;
MEEHQSLVID NGSGMCKAGF AGEDAPRAVF PSLIGRPKQR SIMVGMGNKD AYVGDEAMSK
KGILALKYPI EHGIITNWDD MEKIWHHTFY NELRVGPEEH GVLLTEAPLN PKANREKMTQ
IMFETFRVPA MYVAIQAVLS LYASGRTTGI VLDSGDGVSH TVPIYEGYAL PHAILRLDLA
GRDLTDYLMK ILMERGYSFN TSAEREIVRD IKEKLYGNII TVGNERFRCP EVLFQPNFIG
MEAAGVHETT FNSIGKCDID IRKDLYANVV LSGGTTMFEG IAERMNKELT AMAPASMKIR
VVAPPERKYS VWIGGSILSS LSTFQSMWIT AEEYEDAGCA IVHRKCF
//
