ID   ACT1_NAEFO              Reviewed;         375 AA.
AC   P27131;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Actin-1;
DE   AltName: Full=Actin I;
DE   Flags: Precursor;
OS   Naegleria fowleri (Brain eating amoeba).
OC   Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC   Vahlkampfiidae; Naegleria.
OX   NCBI_TaxID=5763;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 30894 / Lee;
RA   Ahn J., Hu W.-N., Kopachik W.J., Band R.N.;
RT   "Cloning and characterization of two virulent-related actin genes in
RT   Naegleria fowleri.";
RL   Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 30894 / Lee;
RX   PubMed=8768528; DOI=10.1111/j.1574-6968.1996.tb08390.x;
RA   Gorospe S., Band R.N., Kopachik W.J.;
RT   "Molecular cloning of, and phylogenetic analysis of, an actin in Naegleria
RT   fowleri.";
RL   FEMS Microbiol. Lett. 141:233-237(1996).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR   EMBL; M90311; AAA29382.1; -; mRNA.
DR   EMBL; U37719; AAB42183.1; -; Genomic_DNA.
DR   AlphaFoldDB; P27131; -.
DR   SMR; P27131; -.
DR   PRIDE; P27131; -.
DR   VEuPathDB; AmoebaDB:FDP41_006065; -.
DR   VEuPathDB; AmoebaDB:NF0132150; -.
DR   VEuPathDB; AmoebaDB:NfTy_067420; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; PTHR11937; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding.
FT   PROPEP          1..2
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000000702"
FT   CHAIN           3..375
FT                   /note="Actin-1"
FT                   /id="PRO_0000000703"
FT   MOD_RES         3
FT                   /note="N-acetylaspartate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        58
FT                   /note="V -> A (in Ref. 2; AAB42183)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        278
FT                   /note="T -> S (in Ref. 2; AAB42183)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   375 AA;  41728 MW;  049CC3450FA5B8E4 CRC64;
     MCDDVQALVV DNGSGMCKAG FAGDDAPRAV FPSIIGRPKQ KSIMVGMGNK DAYVGDEVQS
     KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT
     QIMFETFSVP AMYVAIQAVL SLYASGRTTG IVLDSGDGVS HTVPIYEGYA LPHAILRLDL
     AGRDLTDYLM KILMERGYSF NTTAEREIVR DIKEKLCYIA LDFEQEMKIA AESSSVEKSY
     ELPDGNVITV GNERFRCPEV LFQPNFIGME AAGVHETTFN SIGKCDIDIR KDLYGNVVLS
     GGTTMFEGIA ERMTKELTNM APASMKIKVV APPERKYSVW IGGSILASLS TFQQMWITKE
     EYEDAGPGIV HRKSF