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MYOA_PLAF7
ID   MYOA_PLAF7              Reviewed;         818 AA.
AC   Q8IDR3;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Myosin-A;
DE   AltName: Full=PfMyoA;
GN   Name=MyoA {ECO:0000305}; ORFNames=PF13_0233, PF3D7_1342600;
OS   Plasmodium falciparum (isolate 3D7).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=36329;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3D7;
RX   PubMed=12368864; DOI=10.1038/nature01097;
RA   Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA   Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA   Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA   Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA   Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA   Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA   Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA   Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT   "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL   Nature 419:498-511(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3D7;
RX   PubMed=12368867; DOI=10.1038/nature01095;
RA   Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA   Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA   Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA   Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA   Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA   Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA   Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA   Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA   Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA   Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA   Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA   Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA   Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA   Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT   "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL   Nature 419:527-531(2002).
RN   [3]
RP   DEVELOPMENTAL STAGE, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   PHOSPHORYLATION AT SER-19.
RX   PubMed=26149123; DOI=10.1038/ncomms8285;
RA   Alam M.M., Solyakov L., Bottrill A.R., Flueck C., Siddiqui F.A., Singh S.,
RA   Mistry S., Viskaduraki M., Lee K., Hopp C.S., Chitnis C.E., Doerig C.,
RA   Moon R.W., Green J.L., Holder A.A., Baker D.A., Tobin A.B.;
RT   "Phosphoproteomics reveals malaria parasite Protein Kinase G as a
RT   signalling hub regulating egress and invasion.";
RL   Nat. Commun. 6:7285-7285(2015).
CC   -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC       Unconventional myosins serve in intracellular movements. Their highly
CC       divergent tails are presumed to bind to membranous compartments, which
CC       would be moved relative to actin filaments (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Tightly
CC       associated with the plasma membrane. {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during the parasite blood stage (at
CC       protein level). {ECO:0000269|PubMed:26149123}.
CC   -!- DOMAIN: This protein differs from the typical myosin heavy chain
CC       structure in having head and tail domains but no discernible neck
CC       domain.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000305}.
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DR   EMBL; AL844509; CAD52556.1; -; Genomic_DNA.
DR   RefSeq; XP_001350147.1; XM_001350111.1.
DR   PDB; 4AOM; X-ray; 1.94 A; T=799-816.
DR   PDB; 4MZJ; X-ray; 1.47 A; T=799-816.
DR   PDB; 4MZK; X-ray; 1.82 A; T=799-816.
DR   PDB; 4MZL; X-ray; 2.01 A; C/D=800-816.
DR   PDB; 4R1E; X-ray; 1.98 A; B=803-816.
DR   PDB; 6I7D; X-ray; 2.82 A; A/B/C/D=1-768.
DR   PDB; 6I7E; X-ray; 3.49 A; A=1-768.
DR   PDB; 6TU7; EM; 3.10 A; AP1/GP1=2-818.
DR   PDB; 6YCX; X-ray; 3.99 A; A/B=1-818.
DR   PDB; 6YCY; X-ray; 2.55 A; A=1-818.
DR   PDB; 6YCZ; X-ray; 3.27 A; A=1-818.
DR   PDB; 6ZN3; X-ray; 2.51 A; C/F/I/L/O=775-816.
DR   PDB; 7ALN; EM; 3.77 A; F=1-818.
DR   PDBsum; 4AOM; -.
DR   PDBsum; 4MZJ; -.
DR   PDBsum; 4MZK; -.
DR   PDBsum; 4MZL; -.
DR   PDBsum; 4R1E; -.
DR   PDBsum; 6I7D; -.
DR   PDBsum; 6I7E; -.
DR   PDBsum; 6TU7; -.
DR   PDBsum; 6YCX; -.
DR   PDBsum; 6YCY; -.
DR   PDBsum; 6YCZ; -.
DR   PDBsum; 6ZN3; -.
DR   PDBsum; 7ALN; -.
DR   AlphaFoldDB; Q8IDR3; -.
DR   SASBDB; Q8IDR3; -.
DR   SMR; Q8IDR3; -.
DR   BioGRID; 1209455; 4.
DR   IntAct; Q8IDR3; 4.
DR   STRING; 5833.PF13_0233; -.
DR   PRIDE; Q8IDR3; -.
DR   EnsemblProtists; CAD52556; CAD52556; PF3D7_1342600.
DR   GeneID; 814200; -.
DR   KEGG; pfa:PF3D7_1342600; -.
DR   VEuPathDB; PlasmoDB:PF3D7_1342600; -.
DR   HOGENOM; CLU_000192_7_5_1; -.
DR   InParanoid; Q8IDR3; -.
DR   OMA; NGIMEAR; -.
DR   PhylomeDB; Q8IDR3; -.
DR   Proteomes; UP000001450; Chromosome 13.
DR   GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0070258; C:inner membrane pellicle complex; IDA:GeneDB.
DR   GO; GO:0016459; C:myosin complex; IDA:GeneDB.
DR   GO; GO:0020039; C:pellicle; IDA:GeneDB.
DR   GO; GO:0005886; C:plasma membrane; IDA:GeneDB.
DR   GO; GO:0003779; F:actin binding; IDA:GeneDB.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IDA:GeneDB.
DR   GO; GO:0003774; F:cytoskeletal motor activity; ISS:GeneDB.
DR   GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR   CDD; cd14876; MYSc_Myo14; 1.
DR   Gene3D; 3.40.850.10; -; 1.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR036044; MYSc_Myo14.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; ATP-binding; Cell membrane; Membrane;
KW   Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..818
FT                   /note="Myosin-A"
FT                   /id="PRO_0000123374"
FT   DOMAIN          97..771
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   REGION          661..671
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000255"
FT   REGION          773..818
FT                   /note="Tail"
FT   BINDING         191..198
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         19
FT                   /note="Phosphoserine; by PKG"
FT                   /evidence="ECO:0000269|PubMed:26149123"
FT   HELIX           5..14
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   STRAND          26..29
FT                   /evidence="ECO:0007829|PDB:6I7E"
FT   STRAND          35..39
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           42..46
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   STRAND          53..57
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   STRAND          63..72
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   STRAND          80..82
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           84..86
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   STRAND          87..89
FT                   /evidence="ECO:0007829|PDB:6I7D"
FT   HELIX           96..98
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           102..104
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           110..121
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   TURN            122..124
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   STRAND          127..130
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   STRAND          133..137
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           148..156
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           160..162
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           167..181
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   STRAND          185..192
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           197..208
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   STRAND          212..214
FT                   /evidence="ECO:0007829|PDB:6I7E"
FT   HELIX           218..235
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   STRAND          248..256
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   TURN            258..260
FT                   /evidence="ECO:0007829|PDB:6I7E"
FT   STRAND          262..270
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           274..277
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           288..296
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           299..305
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           310..312
FT                   /evidence="ECO:0007829|PDB:6YCZ"
FT   STRAND          314..316
FT                   /evidence="ECO:0007829|PDB:6I7E"
FT   STRAND          318..320
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           328..341
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           346..362
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   STRAND          367..369
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           372..375
FT                   /evidence="ECO:0007829|PDB:6I7E"
FT   STRAND          379..381
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           383..385
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           386..395
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           400..408
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   STRAND          409..414
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   STRAND          417..422
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           425..455
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   STRAND          465..471
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   STRAND          477..479
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           481..511
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           525..532
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   STRAND          533..537
FT                   /evidence="ECO:0007829|PDB:6I7D"
FT   HELIX           538..547
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   STRAND          548..550
FT                   /evidence="ECO:0007829|PDB:6I7E"
FT   HELIX           553..563
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   TURN            564..566
FT                   /evidence="ECO:0007829|PDB:6I7D"
FT   STRAND          570..572
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   STRAND          574..576
FT                   /evidence="ECO:0007829|PDB:6I7D"
FT   STRAND          577..585
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   STRAND          588..593
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           597..601
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           607..614
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           619..624
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   TURN            625..627
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           637..639
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           641..657
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   STRAND          659..667
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           680..689
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           692..700
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   STRAND          701..703
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   STRAND          705..708
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           709..715
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           717..719
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           721..724
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   STRAND          727..729
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           731..742
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           746..748
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   STRAND          749..751
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   STRAND          753..758
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           760..773
FT                   /evidence="ECO:0007829|PDB:6YCY"
FT   HELIX           775..798
FT                   /evidence="ECO:0007829|PDB:6ZN3"
FT   HELIX           801..815
FT                   /evidence="ECO:0007829|PDB:4MZJ"
SQ   SEQUENCE   818 AA;  92277 MW;  F397875C52B3B19E CRC64;
     MAVTNEEIKT ASKIVRRVSN VEAFDKSGSV FKGYQIWTDI SPTIENDPNI MFVKCVVQQG
     SKKEKLTVVQ IDPPGTGTPY DIDPTHAWNC NSQVDPMSFG DIGLLNHTNI PCVLDFLKHR
     YLKNQIYTTA VPLIVAINPY KDLGNTTNEW IRRYRDTADH TKLPPHVFTC AREALSNLHG
     VNKSQTIIVS GESGAGKTEA TKQIMRYFAS SKSGNMDLRI QTAIMAANPV LEAFGNAKTI
     RNNNSSRFGR FMQLVISHEG GIRYGSVVAF LLEKSRIITQ DDNERSYHIF YQFLKGANST
     MKSKFGLKGV TEYKLLNPNS TEVSGVDDVK DFEEVIESLK NMELSESDIE VIFSIVAGIL
     TLGNVRLIEK QEAGLSDAAA IMDEDMGVFN KACELMYLDP ELIKREILIK VTVAGGTKIE
     GRWNKNDAEV LKSSLCKAMY EKLFLWIIRH LNSRIEPEGG FKTFMGMLDI FGFEVFKNNS
     LEQLFINITN EMLQKNFVDI VFERESKLYK DEGISTAELK YTSNKEVINV LCEKGKSVLS
     YLEDQCLAPG GTDEKFVSSC ATNLKENNKF TPAKVASNKN FIIQHTIGPI QYCAESFLLK
     NKDVLRGDLV EVIKDSPNPI VQQLFEGQVI EKGKIAKGSL IGSQFLNQLT SLMNLINSTE
     PHFIRCIKPN ENKKPLEWCE PKILIQLHAL SILEALVLRQ LGYSYRRTFE EFLYQYKFVD
     IAAAEDSSVE NQNKCVNILK LSGLSESMYK IGKSMVFLKQ EGAKILTKIQ REKLVEWENC
     VSVIEAAILK HKYKQKVNKN IPSLLRVQAH IRKKMVAQ
 
 
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