ACT2_PLABA
ID ACT2_PLABA Reviewed; 376 AA.
AC Q4YU79;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Actin-2;
DE AltName: Full=Actin II;
GN ORFNames=PB001050.02.0;
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; CAAI01002399; CAH98428.1; -; Genomic_DNA.
DR RefSeq; XP_680164.1; XM_675072.1.
DR PDB; 4CBX; X-ray; 2.20 A; A=1-376.
DR PDB; 6I4M; X-ray; 1.87 A; A=1-376.
DR PDBsum; 4CBX; -.
DR PDBsum; 6I4M; -.
DR AlphaFoldDB; Q4YU79; -.
DR SMR; Q4YU79; -.
DR STRING; 5821.PBANKA_103010; -.
DR VEuPathDB; PlasmoDB:PBANKA_1030100; -.
DR eggNOG; KOG0676; Eukaryota.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; Q4YU79; -.
DR OMA; PNIMVGM; -.
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-2"
FT /id="PRO_0000233391"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:6I4M"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:6I4M"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:6I4M"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:6I4M"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:6I4M"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:6I4M"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:6I4M"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:6I4M"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:6I4M"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:6I4M"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:6I4M"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:6I4M"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:6I4M"
FT HELIX 137..144
FT /evidence="ECO:0007829|PDB:6I4M"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:6I4M"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:6I4M"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:6I4M"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:6I4M"
FT HELIX 182..194
FT /evidence="ECO:0007829|PDB:6I4M"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:6I4M"
FT HELIX 203..216
FT /evidence="ECO:0007829|PDB:6I4M"
FT HELIX 223..232
FT /evidence="ECO:0007829|PDB:6I4M"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:6I4M"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:6I4M"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:6I4M"
FT HELIX 254..260
FT /evidence="ECO:0007829|PDB:6I4M"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:6I4M"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:6I4M"
FT HELIX 275..284
FT /evidence="ECO:0007829|PDB:6I4M"
FT HELIX 288..295
FT /evidence="ECO:0007829|PDB:6I4M"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:6I4M"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:6I4M"
FT HELIX 310..321
FT /evidence="ECO:0007829|PDB:6I4M"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:6I4M"
FT HELIX 339..349
FT /evidence="ECO:0007829|PDB:6I4M"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:6I4M"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:6I4M"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:6I4M"
FT HELIX 360..366
FT /evidence="ECO:0007829|PDB:6I4M"
FT HELIX 370..374
FT /evidence="ECO:0007829|PDB:6I4M"
SQ SEQUENCE 376 AA; 42655 MW; F1ACCFD0A839D746 CRC64;
MPEESIALVV DNGSGMVKSG LAGDDAPKCV FPSIIGIPKM PNIMVGMEQK ECYVGDEAQN
KRGILTLKYP IEHGIVTNWD DMEKIWRHTF FNELRVSPEE HPVLLTEAPL NPKTNREKMT
QIMFESFDVP AMYVSIQAIL SLYASGRTTG IVLDSGDGVT HTVPIYEGYV LPHAINRTDM
AGRDLTYYMM KLFTERGYTF TTTAEREIVR DIKEKLCYIA LDYDEELKKS EERTEEVEEM
YELPDGNLIT VGSERFRCPE ALFNPSLIGR ECPGLHITAY QSIMKCDIDI RKELYNNIVL
SGGTTMYNYI GERLTNEMTS LAPPSMKIKV IAPPERKYSV WIGGSILSSL STFQKMWITK
EEYDESGPSI VHRKCF
