ACT1_PLABA
ID ACT1_PLABA Reviewed; 376 AA.
AC Q4Z1L3;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2017, sequence version 2.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Actin-1;
DE AltName: Full=Actin I;
GN ORFNames=PB000323.01.0;
OS Plasmodium berghei (strain Anka).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANKA;
RX PubMed=15637271; DOI=10.1126/science.1103717;
RA Hall N., Karras M., Raine J.D., Carlton J.M., Kooij T.W.A., Berriman M.,
RA Florens L., Janssen C.S., Pain A., Christophides G.K., James K.,
RA Rutherford K., Harris B., Harris D., Churcher C.M., Quail M.A., Ormond D.,
RA Doggett J., Trueman H.E., Mendoza J., Bidwell S.L., Rajandream M.A.,
RA Carucci D.J., Yates J.R. III, Kafatos F.C., Janse C.J., Barrell B.G.,
RA Turner C.M.R., Waters A.P., Sinden R.S.;
RT "A comprehensive survey of the Plasmodium life cycle by genomic,
RT transcriptomic, and proteomic analyses.";
RL Science 307:82-86(2005).
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; CAAI01001113; CAH95825.1; -; Genomic_DNA.
DR PDB; 4CBW; X-ray; 2.50 A; A=62-333, A=335-376.
DR PDBsum; 4CBW; -.
DR AlphaFoldDB; Q4Z1L3; -.
DR SMR; Q4Z1L3; -.
DR STRING; 5821.PBANKA_145930; -.
DR ABCD; Q4Z1L3; 1 sequenced antibody.
DR VEuPathDB; PlasmoDB:PBANKA_1459300; -.
DR eggNOG; KOG0676; Eukaryota.
DR InParanoid; Q4Z1L3; -.
DR OMA; FHTTAER; -.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding.
FT CHAIN 1..376
FT /note="Actin-1"
FT /id="PRO_0000233388"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:4CBW"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:4CBW"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:4CBW"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:4CBW"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:4CBW"
FT HELIX 61..65
FT /evidence="ECO:0007829|PDB:4CBW"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:4CBW"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:4CBW"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:4CBW"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:4CBW"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:4CBW"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:4CBW"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:4CBW"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:4CBW"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:4CBW"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:4CBW"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:4CBW"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:4CBW"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:4CBW"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:4CBW"
FT HELIX 206..217
FT /evidence="ECO:0007829|PDB:4CBW"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:4CBW"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:4CBW"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:4CBW"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:4CBW"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:4CBW"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:4CBW"
FT HELIX 275..284
FT /evidence="ECO:0007829|PDB:4CBW"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:4CBW"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:4CBW"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:4CBW"
FT HELIX 303..306
FT /evidence="ECO:0007829|PDB:4CBW"
FT HELIX 310..321
FT /evidence="ECO:0007829|PDB:4CBW"
FT TURN 334..337
FT /evidence="ECO:0007829|PDB:4CBW"
FT HELIX 339..347
FT /evidence="ECO:0007829|PDB:4CBW"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:4CBW"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:4CBW"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:4CBW"
FT HELIX 360..366
FT /evidence="ECO:0007829|PDB:4CBW"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:4CBW"
FT HELIX 371..374
FT /evidence="ECO:0007829|PDB:4CBW"
SQ SEQUENCE 376 AA; 41885 MW; 723AE89106F2870B CRC64;
MGDEEVQALV IDNGSGNVKA GVAGDDAPRS VFPSIVGRPK NPGIMVGMEE KDAFVGDEAQ
TKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRAAPE EHPVLLTEAP LNPKGNRERM
TQIMFESFNV PAMYVAIQAV LSLYSSGRTT GIVLDSGDGV SHTVPIYEGY ALPHAIMRLD
LAGRDLTEYL MKILHERGYG FSTSAEKEIV RDIKEKLCYI ALNFDEEMKT SEQSSDIEKS
YELPDGNIIT VGNERFRCPE ALFQPSFLGK EAAGIHTTTF NSIKKCDVDI RKDLYGNIVL
SGGTTMYEGI GERLTRDITT LAPSTMKIKV VAPPERKYSV WIGGSILSSL STFQQMWITK
EEYDESGPSI VHRKCF
