MYO1_MAGO7
ID MYO1_MAGO7 Reviewed; 1212 AA.
AC A4RE77; G4NEN8;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Myosin-1;
DE AltName: Full=Class I unconventional myosin;
DE AltName: Full=Type I myosin;
GN Name=MYO1; ORFNames=MGG_00748;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
CC -!- FUNCTION: Type-I myosin implicated in the organization of the actin
CC cytoskeleton. Required for proper actin cytoskeleton polarization. At
CC the cell cortex, assembles in patch-like structures together with
CC proteins from the actin-polymerizing machinery and promotes actin
CC assembly. Functions as actin nucleation-promoting factor (NPF) for the
CC Arp2/3 complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000250}.
CC -!- DOMAIN: The myosin motor domain displays actin-stimulated ATPase
CC activity and generates a mechanochemical force. {ECO:0000250}.
CC -!- DOMAIN: The tail domain participates in molecular interactions that
CC specify the role of the motor domain (By similarity). It is composed of
CC several tail homology (TH) domains, namely a putative phospholipid-
CC binding myosin tail domain (also named TH1), an Ala- and Pro-rich
CC domain (TH2), followed by an SH3 domain and a C-terminal acidic domain
CC (TH3). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; CM001235; EHA48668.1; -; Genomic_DNA.
DR RefSeq; XP_003718252.1; XM_003718204.1.
DR AlphaFoldDB; A4RE77; -.
DR SMR; A4RE77; -.
DR STRING; 318829.MGG_00748T0; -.
DR PRIDE; A4RE77; -.
DR EnsemblFungi; MGG_00748T0; MGG_00748T0; MGG_00748.
DR GeneID; 2674396; -.
DR KEGG; mgr:MGG_00748; -.
DR VEuPathDB; FungiDB:MGG_00748; -.
DR eggNOG; KOG0162; Eukaryota.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; A4RE77; -.
DR OMA; NGWWLCK; -.
DR OrthoDB; 122881at2759; -.
DR Proteomes; UP000009058; Chromosome 5.
DR GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR GO; GO:0051285; C:cell cortex of cell tip; IEA:EnsemblFungi.
DR GO; GO:0043332; C:mating projection tip; IEA:EnsemblFungi.
DR GO; GO:0031097; C:medial cortex; IEA:EnsemblFungi.
DR GO; GO:0045160; C:myosin I complex; IEA:EnsemblFungi.
DR GO; GO:0044853; C:plasma membrane raft; IEA:EnsemblFungi.
DR GO; GO:0005628; C:prospore membrane; IEA:EnsemblFungi.
DR GO; GO:0051015; F:actin filament binding; IEA:EnsemblFungi.
DR GO; GO:0071933; F:Arp2/3 complex binding; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IEA:EnsemblFungi.
DR GO; GO:0000147; P:actin cortical patch assembly; IEA:EnsemblFungi.
DR GO; GO:0006897; P:endocytosis; IEA:EnsemblFungi.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IEA:EnsemblFungi.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:EnsemblFungi.
DR GO; GO:0044855; P:plasma membrane raft distribution; IEA:EnsemblFungi.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:EnsemblFungi.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IEA:EnsemblFungi.
DR CDD; cd01378; MYSc_Myo1; 1.
DR CDD; cd11858; SH3_Myosin-I_fungi; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR035535; Fungal_myosin-I_SH3.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_TH1.
DR InterPro; IPR036072; MYSc_Myo1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS51757; TH1; 1.
PE 3: Inferred from homology;
KW Actin-binding; ATP-binding; Cytoplasm; Cytoskeleton; Hydrolase;
KW Motor protein; Myosin; Nucleotide-binding; Reference proteome; Repeat;
KW SH3 domain.
FT CHAIN 1..1212
FT /note="Myosin-1"
FT /id="PRO_0000338555"
FT DOMAIN 41..715
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 719..739
FT /note="IQ 1"
FT DOMAIN 740..765
FT /note="IQ 2"
FT DOMAIN 773..962
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1065..1124
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..487
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 947..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1050
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1146
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 134..141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1212 AA; 134333 MW; 487EA59F5A96028D CRC64;
MGITRRGKDK AAAGQAVAGG ASGGRARPKK ATFETSKKKD VGVSDLTLLS KVSNEAINEN
LQKRFEGREI YTYIGHVLVS VNPFRDLGIY TDQVLDSYKG KNRLEMPPHV FAIAESAYYN
MKAYKDNQCV IISGESGAGK TEAAKRIMQY IASVSGGDST DIQQIKDMVL ATNPLLESFG
NAKTLRNNNS SRFGKYLQIH FNSVGEPVGA DITNYLLEKS RVVGQITNER NFHIFYQFTK
GASEHYRQMF GIQKPETYIY TSRSKCLDVD GIDDLAEFQD TLNAMKVIGL SQEEQDSVFR
ILAAILWTGN LVFREDDEGY AAVTDQSVVE FLAYLLEVDP QQLIKAITIR ILTPRSGEVI
ESPANVAQAM ATRDALAKSL YNNLFDWIVE RINQSLKARQ PTSNSVGILD IYGFEIFEKN
SFEQLCINYV NEKLQQIFIQ LTLKAEQDEY AREQIKWTPI KYFDNKIVCD LIESVRPPGV
FSALKDATKT AHADPAACDR TFMQSVNGMS NAHLIPRQGS FIIKHYAGDV AYTVDGITDK
NKDQLLKGLL GMFQVSQNPF LHTLFPNQVD QDNRKQPPTA GDRIRTSANA LVETLMKCQP
SYIRTIKPNE NKSPTEYNVP NVLHQIKYLG LQENVRIRRA GFAYRQSFEK FVDRFFLLSP
ATSYAGEYTW QGSYEAAVKQ ILKDTSIPQE EWQMGVTKAF IKSPETLFAL EHMRDRYWHN
MATRIQRMWR AYLAYRAESA TRIQTFWRKK RTGAEYLQLR DHGHRVLQGR KERRRMSILG
SRRFIGDYLG INASSGPGAH IRNAIGIGSN EKTVFSCRGE ILEAKFGRSS KASPRILIVT
NSKFYVVAQM LVNGQVQITA EKAIPLGAIK FIGASSSRDD WFSLGVGSPQ EADPLLNCVL
KTEMFTQMER VMPGGFNLKI GDSIEYAKKP GKMQVVKVLK DSPNPVDFYK SGAVHTQQGE
PPNSVSRPTP KGKPVPPRPI TRGKLIRPGG PNGRPARGTT NRTPQPRPGG ASASAVASRP
VPQAQPQAQA QVAASIPVRT QQQSQTSSAS VRAPPPPPPA APPAKAKIMA KVLYDFAGQK
ENEMSIKEGD LIEIVQKENN GWWLAKSGNQ QAWVPAAYVE EQKQAPPPVA ASRPPPPAPP
AANGKNKPLP PAKRPAAGKK PASLQPRDSG MSLNGSDGSR SNTPTPSLGN SLADALLARK
QAMAKKDDDD DW
