(data stored in ACNUC16935 zone)

SWISSPROT: MYO1_EMENI

ID   MYO1_EMENI              Reviewed;        1249 AA.
AC   Q00647; C8VMZ7; Q5BD22;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   05-JUL-2017, entry version 101.
DE   RecName: Full=Myosin-1;
DE   AltName: Full=Class I unconventional myosin;
DE   AltName: Full=Type I myosin;
GN   Name=myoA; ORFNames=AN1558;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=7860631; DOI=10.1083/jcb.128.4.577;
RA   McGoldrick C.A., Gruver C., May G.S.;
RT   "myoA of Aspergillus nidulans encodes an essential myosin I required
RT   for secretion and polarized growth.";
RL   J. Cell Biol. 128:577-587(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH CAMA.
RX   PubMed=9756952; DOI=10.1074/jbc.273.41.27017;
RA   Osherov N., Yamashita R.A., Chung Y.-S., May G.S.;
RT   "Structural requirements for in vivo myosin I function in Aspergillus
RT   nidulans.";
RL   J. Biol. Chem. 273:27017-27025(1998).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=10658211;
RX   DOI=10.1002/(SICI)1097-0169(200002)45:2<163::AID-CM7>3.0.CO;2-D;
RA   Yamashita R.A., Osherov N., May G.S.;
RT   "Localization of wild type and mutant class I myosin proteins in
RT   Aspergillus nidulans using GFP-fusion proteins.";
RL   Cell Motil. Cytoskeleton 45:163-172(2000).
CC   -!- FUNCTION: Type-I myosin implicated in the organization of the
CC       actin cytoskeleton. Required for proper actin cytoskeleton
CC       polarization. At the cell cortex, assembles in patch-like
CC       structures together with proteins from the actin-polymerizing
CC       machinery and promotes actin assembly. Functions as actin
CC       nucleation-promoting factor (NPF) for the Arp2/3 complex (By
CC       similarity). Plays an important role in polarized growth, spore
CC       germination, hyphal morphogenesis, and septal wall formation.
CC       {ECO:0000250, ECO:0000269|PubMed:9756952}.
CC   -!- SUBUNIT: Interacts (via IQ domains) with camA.
CC       {ECO:0000269|PubMed:9756952}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC       {ECO:0000269|PubMed:10658211, ECO:0000269|PubMed:7860631}.
CC       Note=Localizes to cortical patch-like structures. Enriched at
CC       sites of polarized growth, like the growing hyphal tips and sites
CC       of septum formation.
CC   -!- DEVELOPMENTAL STAGE: Found in dormant conidiospores.
CC       {ECO:0000269|PubMed:7860631}.
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
CC       that specify the role of the motor domain (By similarity). It is
CC       composed of several tail homology (TH) domains, namely a putative
CC       phospholipid-binding myosin tail domain (also named TH1), an Ala-
CC       and Pro-rich domain (TH2), followed by an SH3 domain and a C-
CC       terminal acidic domain (TH3). {ECO:0000250}.
CC   -!- PTM: Phosphorylation of the TEDS site (Ser-371) is required for
CC       the polarization of the actin cytoskeleton. Phosphorylation
CC       probably activates the myosin-I ATPase activity (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA67877.1; Type=Frameshift; Positions=1000, 1069; Evidence={ECO:0000305};
CC       Sequence=EAA64265.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; U12427; AAA67877.1; ALT_FRAME; mRNA.
DR   EMBL; AACD01000025; EAA64265.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001307; CBF85107.1; -; Genomic_DNA.
DR   PIR; A56511; A56511.
DR   RefSeq; XP_659162.1; XM_654070.1.
DR   ProteinModelPortal; Q00647; -.
DR   SMR; Q00647; -.
DR   STRING; 162425.CADANIAP00008187; -.
DR   EnsemblFungi; CADANIAT00008187; CADANIAP00008187; CADANIAG00008187.
DR   EnsemblFungi; EAA64265; EAA64265; AN1558.2.
DR   GeneID; 2875672; -.
DR   KEGG; ani:AN1558.2; -.
DR   HOGENOM; HOG000260265; -.
DR   InParanoid; Q00647; -.
DR   KO; K10356; -.
DR   OMA; KENWGPW; -.
DR   OrthoDB; EOG092C0QJU; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Partially assembled WGS sequence.
DR   GO; GO:0030479; C:actin cortical patch; IDA:AspGD.
DR   GO; GO:0030428; C:cell septum; IDA:AspGD.
DR   GO; GO:0001411; C:hyphal tip; IDA:AspGD.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:motor activity; IEA:InterPro.
DR   GO; GO:0051666; P:actin cortical patch localization; IDA:AspGD.
DR   GO; GO:0009932; P:cell tip growth; IMP:AspGD.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR010926; Myosin_TH1.
DR   InterPro; IPR027417; P-loop_NTPase.
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   1: Evidence at protein level;
DR   PRODOM; Q00647.
DR   SWISS-2DPAGE; Q00647.
KW   Actin-binding; ATP-binding; Complete proteome; Cytoplasm;
KW   Cytoskeleton; Hydrolase; Motor protein; Myosin; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Repeat; SH3 domain.
FT   CHAIN         1   1249       Myosin-1.
FT                                /FTId=PRO_0000338551.
FT   DOMAIN       50    729       Myosin motor.
FT   DOMAIN      733    753       IQ 1.
FT   DOMAIN      754    779       IQ 2.
FT   DOMAIN      787    979       TH1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01093}.
FT   DOMAIN     1074   1135       SH3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00192}.
FT   NP_BIND     143    150       ATP. {ECO:0000255}.
FT   REGION      418    500       Actin-binding. {ECO:0000250}.
FT   COMPBIAS    970   1194       Pro-rich.
FT   COMPBIAS   1029   1081       Ala-rich.
FT   COMPBIAS   1149   1193       Ala-rich.
FT   COMPBIAS   1244   1248       Poly-Asp.
FT   MOD_RES     371    371       Phosphoserine. {ECO:0000250}.
FT   CONFLICT    608    608       T -> M (in Ref. 1; AAA67877).
FT                                {ECO:0000305}.
FT   CONFLICT    762    762       R -> P (in Ref. 1; AAA67877).
FT                                {ECO:0000305}.
FT   CONFLICT   1223   1223       S -> C (in Ref. 1; AAA67877).
FT                                {ECO:0000305}.
FT   CONFLICT   1234   1234       A -> R (in Ref. 1; AAA67877).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1249 AA;  137074 MW;  6F750DBA67B25186 CRC64;
     MGHSRRPAGG EKKSRFGRSK AAADVGDGRQ AGGKPQVRKA VFESTKKKEI GVSDLTLLSK
     ISNEAINDNL KLRFQHDEIY TYIGHVLVSV NPFRDLGIYT DSVLNSYRGK NRLEVPPHVF
     AVAESAYYNM KSYKDNQCVI ISGESGAGKT EAAKRIMQYI ASVSGGSDSS IQQTKDMVLA
     TNPLLESFGN AKTLRNNNSS RFGKYLELEF NAQGEPVGAN ITNYLLEKSR VVGQITNERN
     FHIFYQFAKG APQKYRDSFG VQQPQSYLYT SRSKCFDVPG VDDVAEFQDT LNAMSVIGMS
     EAEQDNVFRM LAAILWMGNI QFAEDDSGNA AITDQSVVDF VAYLLEVDAG QVNQALTIRM
     METSRGGRRG SVYEVPLNTT QALAVRDALA KAIYFNLFDW IVGRVNQSLT AKGAVANSIG
     ILDIYGFEIF EKNSFEQLCI NYVNEKLQQI FIQLTLKAEQ DEYEREQITW TPIKYFDNKV
     VCSLIEDKRP PGVFAALNDA CATAHADSGA ADNTFVGRLN FLGQNPNFEN RQGQFIIKHY
     AGDVSYAVQG MTDKNKDQLL KDLLNLVQSS SNHFVHTLFP EQVNQDDKRR PPTASDKIKA
     SANDLVATLM KAQPSYIRTI KPNDNKAPKE FNESNVLHQI KYLGLQENVR IRRAGFAYRQ
     TFDKFVERFY LLSPKTSYAG DYTWTGDVET GARQILKDTR IPAEEYQMGI TKVFIKTPET
     LFALEAMRDR YWHNMAIRIQ RAWRNYLRYR TECAIRIQRF WRRMNGGLEL LKLRDQGHTI
     LGGRKERRRM SILGSRRFLG DYVGISNKGG PGEMIRSGAA ISTSDDVLFS CRGEVLVSKF
     GRSSKPSPRI FVLTNRHVYI VSQNFVNNQL VISSERTIPI GAIKTVSASS YRDDWFSLVV
     GGQEPDPLCN CVFKTEFFTH LHNALRGQLN LKIGPEIEYN KKPGKLATVK VVKDGSQVDS
     YKSGTIHTGP GEPPNSVSKP TPRGKQVAAR PVTKGKLLRP GGPGGGPSKL ASRPVPERRP
     IPQPTPQTAA AQPTPASRPV PQPVAAVAAS HSRTSSTASA RAPPPPPPAP PAAAGPKKAK
     ALYDFSSDNN GMLSISAGQI VEIVSKEGNG WWLCMNLETS AQGWTPEAYL EEQVAPTPKP
     APPPPPPVAP RASPAPVNGS AAVAAAKAKA APPPPAKRPN MAGRKTAPAP PPAPRDSAVS
     MNSQGDSSGA SGRGTPSSVS NASLAGGLAE ALRARQSAMQ GKQDDDDDW
//

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