MYO1_SCLS1
ID MYO1_SCLS1 Reviewed; 1230 AA.
AC A7EK16;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Myosin-1;
DE AltName: Full=Class I unconventional myosin;
DE AltName: Full=Type I myosin;
GN Name=myoA; ORFNames=SS1G_05662;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476627; EDO03182.1; -; Genomic_DNA.
DR RefSeq; XP_001592741.1; XM_001592691.1.
DR AlphaFoldDB; A7EK16; -.
DR SMR; A7EK16; -.
DR STRING; 665079.A7EK16; -.
DR EnsemblFungi; EDO03182; EDO03182; SS1G_05662.
DR GeneID; 5489556; -.
DR KEGG; ssl:SS1G_05662; -.
DR VEuPathDB; FungiDB:sscle_05g048210; -.
DR eggNOG; KOG0162; Eukaryota.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; A7EK16; -.
DR OMA; NGWWLCK; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0030479; C:actin cortical patch; IBA:GO_Central.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0051285; C:cell cortex of cell tip; IEA:EnsemblFungi.
DR GO; GO:0051286; C:cell tip; IBA:GO_Central.
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:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0000147; P:actin cortical patch assembly; IEA:EnsemblFungi.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
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 GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
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..1230
FT /note="Myosin-1"
FT /id="PRO_0000338561"
FT DOMAIN 39..713
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 717..737
FT /note="IQ 1"
FT DOMAIN 738..763
FT /note="IQ 2"
FT DOMAIN 771..961
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1064..1123
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..485
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 945..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..962
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1018
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1065
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1143
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1179
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1181..1201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 132..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1230 AA; 136341 MW; 4C9217C9FE81FBC3 CRC64;
MGISRRPKAD KNASAADSAP GGKPNIQKAQ FDTTKKKEVG VSDLTLISKV SNEAINENLK
KRFDNREIYT YIGHVLVSVN PFRDLGIYTD AVLESYKGKN RLEMPPHVFA VAESAYYNMN
AYKDNQCVII SGESGAGKTE AAKRIMQYIA NVSGGSNSSI QETKEMVLAT NPLLESFGNA
KTLRNNNSSR FGKYLQLQFN AQGEPVGADI TNYLLEKTRV VTQIKDERNF HIFYQFTKGA
SQAYRESYGI QQPSQYLYTS KAGCFDVDGI DDLAEYQDTL QAMKVIGLSQ AEQDEIFRML
AAILWTGNIQ FREGDDGYAT VVDQSVVDFL AYLLDVDAAH VIQAITIRIL TPRNGEVIES
PANVPQAMAT RDALAKAIYN NLFDWIVERV NKSLTARAET SNSIGILDIY GFEIFEQNSF
EQLCINYVNE KLQQIFIQLT LKTEQEEYAR EQIKWTPIKY FDNKIVCDLI EAIRPPGVFS
AMKDATKTAH ADPAACDRTF MQAISGMSNP HLTPRQGNFI IKHYAGDVSY TVEGITDKNK
DQLLKGLLNL FGQSRNHFIH ELFPHQVDQD NRKQPPSAGD KIKASANDLV TTLMKATPSY
IRTIKPNENK SPTEYNEKNV LHQVKYLGLQ ENVRIRRAGF AYRQTFDKFV ERFYLLSPKT
SYAGDYIWTG DSKTGAMQIL KDTNIPVEEY QMGVTKAFIK APETLFALEH MRDRYWHNMA
ARIQRVWRAF LQIRIEAATR IQRMFRKKRE GKEFLELREK GHQILQGRKE RRRYSLLGSR
RFMGDYLGIA ATTGPGSKIR GSINLPASEV TLFSCRGEIL ETKFGRSSKL SPRIFIMTRT
KFYIVSQLLV NKQVQIAVEK AIPLGAIKFV SISTCRDDWF SLGVGSPQEA DPLLTCVFKT
ELFTHMQAAM PGGGFNLKIG DSIEYAKKPN KMQLIKVVKD SQQAQDHYKS ATIHTQAGEP
PNSRSKPLPK GKPVAAKPFT SGRLIKPGGP GGRPSRLTNG NRPTPKPVPT PAPAAARPVP
AVNPVAASIP VHTRNTSVQS TQSTRAVPPP PPPAPPAPPP APVSKEPQYR VLYEFAGQSA
NEFSLKQGEI VTVLQKETNG WWLTKNVRGQ GWAPTAYLEE VTPPPPPPVA TRPAPPPAPG
PPKMNGTNGA AIRSKPTPPA PPAKRPAAGR KPAPPPAPRD SGMSISSNGS GNNSGRSTPT
PSLAGGLAEA LRARQSAMQG NAKREDEDDW
