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ACT_SACBA
ID   ACT_SACBA               Reviewed;         375 AA.
AC   P60011; P02579;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Actin;
GN   Name=ACT1;
OS   Saccharomyces bayanus (Yeast) (Saccharomyces uvarum x Saccharomyces
OS   eubayanus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4931;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B19-3C;
RA   Kaneko Y., Takeuchi M.;
RL   Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
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; D12534; BAA02097.1; -; Genomic_DNA.
DR   PDB; 5I9E; X-ray; 2.80 A; B/D=1-375.
DR   PDBsum; 5I9E; -.
DR   AlphaFoldDB; P60011; -.
DR   SMR; P60011; -.
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   GO; GO:0006996; P:organelle organization; IEA:UniProt.
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; Acetylation; ATP-binding; Cytoplasm; Cytoskeleton;
KW   Nucleotide-binding.
FT   CHAIN           1..375
FT                   /note="Actin"
FT                   /id="PRO_0000089001"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250"
FT   STRAND          8..12
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   STRAND          14..21
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   STRAND          28..32
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   HELIX           56..60
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   STRAND          70..72
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   HELIX           79..90
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   TURN            91..94
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   HELIX           98..100
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   STRAND          103..107
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   HELIX           113..125
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   STRAND          132..136
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   HELIX           137..144
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   STRAND          148..155
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   STRAND          160..166
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   STRAND          176..179
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   HELIX           182..194
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   HELIX           206..215
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   HELIX           223..231
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   STRAND          238..241
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   STRAND          247..250
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   HELIX           253..256
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   HELIX           258..261
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   HELIX           264..267
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   HELIX           274..282
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   TURN            287..289
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   HELIX           290..294
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   STRAND          297..301
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   HELIX           302..304
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   HELIX           309..320
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   HELIX           335..337
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   HELIX           338..348
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   HELIX           352..354
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   HELIX           359..365
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   HELIX           366..369
FT                   /evidence="ECO:0007829|PDB:5I9E"
FT   HELIX           370..373
FT                   /evidence="ECO:0007829|PDB:5I9E"
SQ   SEQUENCE   375 AA;  41690 MW;  87AC19B0B0BC9E71 CRC64;
     MDSEVAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGIMVGMGQK DSYVGDEAQS
     KRGILTLRYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPM NPKSNREKMT
     QIMFETFNVP AFYVSIQAVL SLYSSGRTTG IVLDSGDGVT HVVPIYAGFS LPHAILRIDL
     AGRDLTDYLM KILSERGYSF STTAEREIVR DIKEKLCYVA LDFEQEMQTA AQSSSIEKSY
     ELPDGQVITI GNERFRAPEA LFHPSVLGLE SAGIDQTTYN SIMKCDVDVR KELYGNIVMS
     GGTTMFPGIA ERMQKEITAL APSSMKVKII APPERKYSVW IGGSILASLT TFQQMWISKQ
     EYDESGPSIV HHKCF
 
 
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