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Myosin-1 (Class I unconventional myosin) (Type I myosin)

 MYO1_EMENI              Reviewed;        1249 AA.
Q00647; C8VMZ7; Q5BD22;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 2.
12-SEP-2018, entry version 109.
RecName: Full=Myosin-1;
AltName: Full=Class I unconventional myosin;
AltName: Full=Type I myosin;
Name=myoA; ORFNames=AN1558;
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
194 / M139) (Aspergillus nidulans).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=227321;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL
STAGE.
PubMed=7860631; DOI=10.1083/jcb.128.4.577;
McGoldrick C.A., Gruver C., May G.S.;
"myoA of Aspergillus nidulans encodes an essential myosin I required
for secretion and polarized growth.";
J. Cell Biol. 128:577-587(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=16372000; DOI=10.1038/nature04341;
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
"Sequencing of Aspergillus nidulans and comparative analysis with A.
fumigatus and A. oryzae.";
Nature 438:1105-1115(2005).
[3]
GENOME REANNOTATION.
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
"The 2008 update of the Aspergillus nidulans genome annotation: a
community effort.";
Fungal Genet. Biol. 46:S2-13(2009).
[4]
FUNCTION, AND INTERACTION WITH CAMA.
PubMed=9756952; DOI=10.1074/jbc.273.41.27017;
Osherov N., Yamashita R.A., Chung Y.-S., May G.S.;
"Structural requirements for in vivo myosin I function in Aspergillus
nidulans.";
J. Biol. Chem. 273:27017-27025(1998).
[5]
SUBCELLULAR LOCATION.
PubMed=10658211;
DOI=10.1002/(SICI)1097-0169(200002)45:2<163::AID-CM7>3.0.CO;2-D;
Yamashita R.A., Osherov N., May G.S.;
"Localization of wild type and mutant class I myosin proteins in
Aspergillus nidulans using GFP-fusion proteins.";
Cell Motil. Cytoskeleton 45:163-172(2000).
-!- FUNCTION: Type-I myosin implicated in the organization of the
actin cytoskeleton. Required for proper actin cytoskeleton
polarization. At the cell cortex, assembles in patch-like
structures together with proteins from the actin-polymerizing
machinery and promotes actin assembly. Functions as actin
nucleation-promoting factor (NPF) for the Arp2/3 complex (By
similarity). Plays an important role in polarized growth, spore
germination, hyphal morphogenesis, and septal wall formation.
{ECO:0000250, ECO:0000269|PubMed:9756952}.
-!- SUBUNIT: Interacts (via IQ domains) with camA.
{ECO:0000269|PubMed:9756952}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
{ECO:0000269|PubMed:10658211, ECO:0000269|PubMed:7860631}.
Note=Localizes to cortical patch-like structures. Enriched at
sites of polarized growth, like the growing hyphal tips and sites
of septum formation.
-!- DEVELOPMENTAL STAGE: Found in dormant conidiospores.
{ECO:0000269|PubMed:7860631}.
-!- DOMAIN: The myosin motor domain displays actin-stimulated ATPase
activity and generates a mechanochemical force. {ECO:0000250}.
-!- DOMAIN: The tail domain participates in molecular interactions
that specify the role of the motor domain (By similarity). It is
composed of several tail homology (TH) domains, namely a putative
phospholipid-binding myosin tail domain (also named TH1), an
Ala- and Pro-rich domain (TH2), followed by an SH3 domain and a C-
terminal acidic domain (TH3). {ECO:0000250}.
-!- PTM: Phosphorylation of the TEDS site (Ser-371) is required for
the polarization of the actin cytoskeleton. Phosphorylation
probably activates the myosin-I ATPase activity (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
superfamily. Myosin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA67877.1; Type=Frameshift; Positions=1000, 1069; Evidence={ECO:0000305};
Sequence=EAA64265.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U12427; AAA67877.1; ALT_FRAME; mRNA.
EMBL; AACD01000025; EAA64265.1; ALT_SEQ; Genomic_DNA.
EMBL; BN001307; CBF85107.1; -; Genomic_DNA.
PIR; A56511; A56511.
RefSeq; XP_659162.1; XM_654070.1.
ProteinModelPortal; Q00647; -.
SMR; Q00647; -.
STRING; 162425.CADANIAP00008187; -.
PRIDE; Q00647; -.
EnsemblFungi; CBF85107; CBF85107; ANIA_01558.
EnsemblFungi; EAA64265; EAA64265; AN1558.2.
GeneID; 2875672; -.
KEGG; ani:AN1558.2; -.
HOGENOM; HOG000260265; -.
InParanoid; Q00647; -.
KO; K10356; -.
OMA; KENWGPW; -.
OrthoDB; EOG092C0QJU; -.
Proteomes; UP000000560; Chromosome VII.
Proteomes; UP000005890; Unassembled WGS sequence.
GO; GO:0030479; C:actin cortical patch; IDA:AspGD.
GO; GO:0030428; C:cell septum; IDA:AspGD.
GO; GO:0001411; C:hyphal tip; IDA:AspGD.
GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003774; F:motor activity; IEA:InterPro.
GO; GO:0051666; P:actin cortical patch localization; IDA:AspGD.
GO; GO:0009932; P:cell tip growth; IMP:AspGD.
CDD; cd01378; MYSc_Myo1; 1.
Gene3D; 3.40.850.10; -; 3.
InterPro; IPR036961; Kinesin_motor_dom_sf.
InterPro; IPR001609; Myosin_head_motor_dom.
InterPro; IPR010926; Myosin_TH1.
InterPro; IPR036072; MYSc_Myo1.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
Pfam; PF00063; Myosin_head; 1.
Pfam; PF06017; Myosin_TH1; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00193; MYOSINHEAVY.
SMART; SM00242; MYSc; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS51456; MYOSIN_MOTOR; 1.
PROSITE; PS50002; SH3; 1.
PROSITE; PS51757; TH1; 1.
1: Evidence at protein level;
Actin-binding; ATP-binding; Complete proteome; Cytoplasm;
Cytoskeleton; Hydrolase; Motor protein; Myosin; Nucleotide-binding;
Phosphoprotein; Reference proteome; Repeat; SH3 domain.
CHAIN 1 1249 Myosin-1.
/FTId=PRO_0000338551.
DOMAIN 50 729 Myosin motor. {ECO:0000255|PROSITE-
ProRule:PRU00782}.
DOMAIN 733 753 IQ 1.
DOMAIN 754 779 IQ 2.
DOMAIN 787 979 TH1. {ECO:0000255|PROSITE-
ProRule:PRU01093}.
DOMAIN 1074 1135 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
NP_BIND 143 150 ATP. {ECO:0000255}.
REGION 418 500 Actin-binding. {ECO:0000250}.
COMPBIAS 970 1194 Pro-rich.
COMPBIAS 1029 1081 Ala-rich.
COMPBIAS 1149 1193 Ala-rich.
COMPBIAS 1244 1248 Poly-Asp.
MOD_RES 371 371 Phosphoserine. {ECO:0000250}.
CONFLICT 608 608 T -> M (in Ref. 1; AAA67877).
{ECO:0000305}.
CONFLICT 762 762 R -> P (in Ref. 1; AAA67877).
{ECO:0000305}.
CONFLICT 1223 1223 S -> C (in Ref. 1; AAA67877).
{ECO:0000305}.
CONFLICT 1234 1234 A -> R (in Ref. 1; AAA67877).
{ECO:0000305}.
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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