(data stored in ACNUC7421 zone)

SWISSPROT: MYO1_ASHGO

ID   MYO1_ASHGO              Reviewed;        1292 AA.
AC   Q758Q9;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   11-DEC-2019, entry version 112.
DE   RecName: Full=Myosin-1;
DE   AltName: Full=Class I unconventional myosin;
DE   AltName: Full=Type I myosin;
GN   Name=MYO1; OrderedLocusNames=AEL306C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 575; 577; 640-641 AND
RP   645-648.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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   -!- PTM: Phosphorylation of the TEDS site (Ser-356) is required for the
CC       polarization of the actin cytoskeleton. Phosphorylation probably
CC       activates the myosin-I ATPase activity (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000305}.
DR   EMBL; AE016818; AAS52378.2; -; Genomic_DNA.
DR   RefSeq; NP_984554.2; NM_209907.2.
DR   SMR; Q758Q9; -.
DR   STRING; 33169.AAS52378; -.
DR   PRIDE; Q758Q9; -.
DR   EnsemblFungi; AAS52378; AAS52378; AGOS_AEL306C.
DR   GeneID; 4620729; -.
DR   KEGG; ago:AGOS_AEL306C; -.
DR   HOGENOM; HOG000260265; -.
DR   InParanoid; Q758Q9; -.
DR   KO; K10356; -.
DR   Proteomes; UP000000591; Chromosome V.
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:0030898; F:actin-dependent ATPase activity; 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: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:0044855; P:plasma membrane raft distribution; 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;
DR   PRODOM; Q758Q9.
DR   SWISS-2DPAGE; Q758Q9.
KW   Actin-binding; ATP-binding; Cytoplasm; Cytoskeleton; Hydrolase;
KW   Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Repeat; SH3 domain.
FT   CHAIN           1..1292
FT                   /note="Myosin-1"
FT                   /id="PRO_0000338535"
FT   DOMAIN          35..714
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   DOMAIN          718..738
FT                   /note="IQ 1"
FT   DOMAIN          739..764
FT                   /note="IQ 2"
FT   DOMAIN          770..960
FT                   /note="TH1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT   DOMAIN          1157..1219
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   NP_BIND         128..135
FT                   /note="ATP"
FT                   /evidence="ECO:0000255"
FT   REGION          403..485
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1076..1160
FT                   /note="Pro-rich"
FT   COMPBIAS        1240..1274
FT                   /note="Ala-rich"
FT   MOD_RES         356
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1292 AA;  143575 MW;  F26EEB3F0234904C CRC64;
     MAIIKRGVRQ KTQPPAKRTT NIKKATFDSG KKKEVGVSDL TLLSKISDEH INENLKRRFE
     NGSIYTYIGH VLISVNPFRD LGIYTDQVLE TYKGRNRLEV PPHVFAIAEA MYYNLKAYNE
     NQCVIISGES GAGKTEAAKR IMQYIAAASS SHEASIGRIK DMVLATNPLL ESFGCAKTLR
     NNNSSRHGKY LEIRFNAQFE PCAGQITNYL LEKQRVVGQI KNERNFHIFY QFSKGASDRY
     RKTYGVQLPE QYVYTSASGC TSVDTIDDLN DYEATLEAMN VIGLSQAEQD EIFRLLSAIL
     WIGNVTFMED DEGNAKIADT SITDFVAYLL QVDAGLLVKS LVERTIETTH GMRRGSIYNV
     PLNIVQATAV RDALAKAIYN NLFEWIVDRV NVSLQALPGA EKSIGILDIY GFEIFEHNSF
     EQICINYVNE KLQQIFIQLT LKSEQEEYAK EQIQWTPIKY FDNKVVCELI EAKRPPGIFA
     ALNDSVATAH ADSNAADQAF AQRLNLFTSN PHFELRSSKF VIKHYAGDVT YDIGGMTDKN
     KDQLQRDLVE LLNSTSNTFL ATIFPDTGDK DSKRRPPTAG DKIIRSANEL VDTLSKAQPS
     YIRTIKPNQT KSPLDYDDRQ VLHQVKYLGL QENVRIRRAG FAYRQTFEKF VERFYLLSPQ
     CSYAGDYTWQ GNTLDAVNLI LRDTSIPVTE YQLGVTKVFI KTPETLFALE NMRDKYWHNM
     ASRIQRAWRR FLQRRIDSAI RIQRAIREMK HGNQFEQLRD YGNKLLGGRK ERRAMSLLGY
     RAFLGDYLSC NELKSKGAFV KRKAGINDHV VFSINGQALH SKFGRSAQRL PKTFILTPSH
     FYIIGKTLVN NQLTYAVDYK IDVRQIVYVS LTNLQDDWVG IFVSNSTQPD PLINTYFKTE
     LITHLKKLNN RIEIKIGPTI EYQKKPGKIH AVKSQINENA PPLGDIYKSS TIMVRRGRPG
     NCSQRKKPLS TRLPDTYTTR ETGYKNAGHP TNIRQVQEPT HISHSQQHTS SNLGFVYSLN
     PSAVNHPRPV PSGSVGTTST PPKQAASAAQ AAYNPHKLGG NMDNSSAAYG NASALPNSAP
     SQAPKPASRP VPKPAPRPGP KPGPKPGPKP GPKPAPKPMP RPAKSVENSV PRPNAIEQGK
     TAPPPPPPPP PPPAAVPSEP VYEAAFDFPG SGSPNEFPLK KGDRIYVTRQ EPSGWSLAKA
     LDGSKEGWVP TAYIVESKAA FSQLEQPVAS SAPLGNSGVA TREAGTTSAA TAAASAATPT
     AFSAGLADAL AARANKMRHE DSGSDDNADD DW
//

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