MYO1_ASPOR
ID MYO1_ASPOR Reviewed; 1261 AA.
AC Q2US45;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Myosin-1;
DE AltName: Full=Class I unconventional myosin;
DE AltName: Full=Type I myosin;
GN Name=myoA; ORFNames=AO090005000576;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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. Plays an important role in polarized growth, spore
CC germination, hyphal morphogenesis, and septal wall formation (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000250}. Note=Localizes to cortical patch-like structures.
CC Enriched at sites of polarized growth, like the growing hyphal tips and
CC sites of septum formation (By similarity). {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-370) 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}.
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DR EMBL; AP007151; BAE55620.1; -; Genomic_DNA.
DR RefSeq; XP_001817622.1; XM_001817570.2.
DR AlphaFoldDB; Q2US45; -.
DR SMR; Q2US45; -.
DR STRING; 510516.Q2US45; -.
DR PRIDE; Q2US45; -.
DR EnsemblFungi; BAE55620; BAE55620; AO090005000576.
DR GeneID; 5989567; -.
DR KEGG; aor:AO090005000576; -.
DR VEuPathDB; FungiDB:AO090005000576; -.
DR HOGENOM; CLU_000192_7_6_1; -.
DR OMA; MESKWGT; -.
DR Proteomes; UP000006564; Chromosome 1.
DR GO; GO:0030479; C:actin cortical patch; IDA:AspGD.
DR GO; GO:0051285; C:cell cortex of cell tip; IEA:EnsemblFungi.
DR GO; GO:0030428; C:cell septum; IDA:AspGD.
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; IDA:AspGD.
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: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; IEA:EnsemblFungi.
DR GO; GO:0000147; P:actin cortical patch assembly; IEA:EnsemblFungi.
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:0006898; P:receptor-mediated endocytosis; IMP:AspGD.
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; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..1261
FT /note="Myosin-1"
FT /id="PRO_0000338540"
FT DOMAIN 49..728
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 732..752
FT /note="IQ 1"
FT DOMAIN 753..778
FT /note="IQ 2"
FT DOMAIN 786..973
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1084..1145
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..499
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 956..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1261
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 960..984
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1050
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1084
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1163
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 142..149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1261 AA; 138361 MW; 6A2075AB32358792 CRC64;
MGHSRRPVGG EKKSRGFGRS KVADVGDGRQ AGKPQVKKAT FETTKKKDIG VSDLTLLSKI
SNEAINDNLK LRFEHDEIYT YIGHVLVSVN PFRDLGIYTD NVLDSYRGKN RLEVPPHVFA
VAESSYYNMK SYKDNQCVII SGESGAGKTE AAKRIMQYIA SVSGGSDSSI QQTKDMVLAT
NPLLESFGNA KTLRNNNSSR FGKYLELEFN ANGEPVGANI TNYLLEKSRV VGQIANERNF
HIFYQFTKAA PQKYRDMFGV QQPQSYLYTS RSKCFDVPGV DDNAEFRDTL NAMGVIGMSE
AEQDNVFRML AAILWIGNVQ FAEDDSGNAA ISDQSVVDFV AYLLEVDPAQ VNKALTIRIM
ETARGGRRGS VYEVPLNTVQ ALAVRDALSK AIYFNLFDWI VERVNQSLTA REPVANSIGI
LDIYGFEIFE KNSFEQLCIN YVNEKLQQIF IQLTLKAEQD EYAREQIQWT PIKYFDNKVV
CSLIEDKRPP GVFAALNDAC ATAHADSGAA DNTFVGRLNF LGQNPNFENR QGQFIVKHYA
GDVSYSVEGM TDKNKDQLLK DLLNLVGSSG NQFVHTLFPN QVNQDDKRRP PTASDKIKAS
ANDLVATLMK AQPSYIRTIK PNDNKAPREY NVGNVLHQIK YLGLQENVRI RRAGFAYRQT
FNKFVERFYL LSPKTSYAGD YTWTGDAESG ARQILKDTSI PAEEYQMGIT KVFVKTPETL
FALEAMRDRY WHNMAIRIQR AWRNYLRYRI ECAIRIQRFW RRTTGGLELL KVRDQGHQVL
QGRKERRRMS LLGSRRFLGD YLGIGNKGGP GEMIRNGAGI SGSDDILFSC RGEVLISKFG
RSSKPSPRIL VLTNRHVYIV AQILVNNQLQ ISAERTVPIG AIKAVSTSNL KDDWFSLIIG
GQEPDPLINC VFKTEFFTHL QTALRGQLNL KVSENIEYNK KPGKLATVKA IKDPAASPNV
DTYKSHTIHT SPGEPPSSVS KPTPKAKQVA ARPVTKGKLL RPGGPGGGPS KLASRPASRP
TPKPQPLPQS QPATAQPIPA PQPAAVPRPV PQPVAAAAAS HTRNASSGSV RAPPPPPPAS
PPAPKKATAK ALYDFTSAQS NELDIRAGDV VQIVSKEGNG WWLCMNMATS VQGWTPQAYL
EEQVAPTPKP APPPPPPAAP RASPVPSANG AAATAAAAKA KPAPPAPPAK RPNMAGRKAV
PAPPPAPRDS AVSMNSQDSS GGSGRGTPNS TSNASLAGGL AEALRARQHA MQGKHDDDDE
W
