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 03-AUG-2022, entry version 125.
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 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL 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 for
RT 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., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., 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., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT 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 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). Plays an important role in polarized
CC growth, spore germination, hyphal morphogenesis, and septal wall
CC formation. {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 sites of
CC polarized growth, like the growing hyphal tips and sites of septum
CC 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 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-371) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA67877.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=EAA64265.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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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 AlphaFoldDB; Q00647; -.
DR SMR; Q00647; -.
DR STRING; 162425.CADANIAP00008187; -.
DR EnsemblFungi; CBF85107; CBF85107; ANIA_01558.
DR EnsemblFungi; EAA64265; EAA64265; AN1558.2.
DR GeneID; 2875672; -.
DR KEGG; ani:AN1558.2; -.
DR VEuPathDB; FungiDB:AN1558; -.
DR eggNOG; KOG0162; Eukaryota.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; Q00647; -.
DR OMA; NGWWLCK; -.
DR OrthoDB; 122881at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0030479; C:actin cortical patch; IDA:AspGD.
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:0030428; C:cell septum; IDA:AspGD.
DR GO; GO:0051286; C:cell tip; IBA:GO_Central.
DR GO; GO:0001411; C:hyphal tip; IDA:AspGD.
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:0051666; P:actin cortical patch localization; IDA:AspGD.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0009932; P:cell tip growth; IMP:AspGD.
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 Gene3D; 3.40.850.10; -; 1.
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 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Cytoplasm; Cytoskeleton; Hydrolase;
KW Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..1249
FT /note="Myosin-1"
FT /id="PRO_0000338551"
FT DOMAIN 50..729
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 733..753
FT /note="IQ 1"
FT DOMAIN 754..779
FT /note="IQ 2"
FT DOMAIN 787..979
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1074..1135
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..500
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 959..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1127..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1074
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1153
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1195
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 143..150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT CONFLICT 608
FT /note="T -> M (in Ref. 1; AAA67877)"
FT /evidence="ECO:0000305"
FT CONFLICT 762
FT /note="R -> P (in Ref. 1; AAA67877)"
FT /evidence="ECO:0000305"
FT CONFLICT 1223
FT /note="S -> C (in Ref. 1; AAA67877)"
FT /evidence="ECO:0000305"
FT CONFLICT 1234
FT /note="A -> R (in Ref. 1; AAA67877)"
FT /evidence="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
