ID MYO1_ASPTN Reviewed; 1246 AA.
AC Q0CEX5;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Myosin-1;
DE AltName: Full=Class I unconventional myosin;
DE AltName: Full=Type I myosin;
GN Name=myoA; ORFNames=ATEG_07759;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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-372) 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; CH476604; EAU32021.1; -; Genomic_DNA.
DR RefSeq; XP_001216380.1; XM_001216380.1.
DR AlphaFoldDB; Q0CEX5; -.
DR SMR; Q0CEX5; -.
DR STRING; 341663.Q0CEX5; -.
DR EnsemblFungi; EAU32021; EAU32021; ATEG_07759.
DR GeneID; 4322646; -.
DR VEuPathDB; FungiDB:ATEG_07759; -.
DR eggNOG; KOG0162; Eukaryota.
DR HOGENOM; CLU_000192_7_6_1; -.
DR OMA; MAFHWQS; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
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: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:0006897; P:endocytosis; IEA:EnsemblFungi.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:EnsemblFungi.
DR CDD; cd01378; MYSc_Myo1; 1.
DR CDD; cd11858; SH3_Myosin-I_fungi; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 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 PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF837; MYOSIN-3-RELATED; 1.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50044; SH3-domain; 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..1246
FT /note="Myosin-1"
FT /id="PRO_0000338541"
FT DOMAIN 51..730
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 734..754
FT /note="IQ 1"
FT DOMAIN 755..780
FT /note="IQ 2"
FT DOMAIN 788..976
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1077..1138
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..501
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 956..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1127..1246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..984
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1043
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1078
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1150
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1193
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 144..151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1246 AA; 137180 MW; F649735FC2D0C823 CRC64;
MGHSRRPVGG EKKSRGFGRS KAVADVGDGR QTGGKPQVKK ATFESTKKKE IGVSDLTLLS
KISNEAINDN LKLRFQHDEI YTYIGHVLVS VNPFRDLGIY TDKVLESYRG KNRLEVPPHV
FAVAESAYYN MKSYNDNQCV IISGESGAGK TEAAKRIMQY IASVSGGSDS SIQHTKDMVL
ATNPLLESFG NAKTLRNNNS SRFGKYLELE FNSRGEPVGA NITNYLLEKS RVVGQITNER
NFHIFYQFTK AAPQKYRDMF GIQQPQSYLY TSRSKCYDVP GVDDAAEFRD TLNAMGVIGM
SEPEQDQVFR MLSAILWIGN IQFVEDDSGN AAIPDQSTVN YVAYLLEVDP GQVNKALTIR
IMETARGGRR GSVYEVPLNT VQALAVRDAL AKAIYFNLFD WIVERVNQSL TARGTVANSI
GILDIYGFEI FEKNSFEQLC INYVNEKLQQ IFIQLTLKAE QDEYAREQIQ WTPIKYFDNK
VVCSLIEDKR PPGVFAALND ACATAHADSG AADNTFVGRL NFLSQNPNFE NRQGQFIVKH
YAGDVSYAVE GMTDKNKDQL LKDLLNLVGS SSNEFVHTLF PNQVNQDDKR RPPTASDKIK
ASANDLVATL MKAQPSYIRT IKPNDNKAPK EYNEGNVLHQ IKYLGLQENV RIRRAGFAYR
QTFDKFVERF YLLSPKTSYA GDYTWTGDAE SGARQILKDT SIPQEEFQMG ITKVFVKTPE
TLFALEAMRD RYWHNMAIRI QRAWRNYLRY RIECAIRIQR FWRRMTGGLE LIKVRDQGHK
VLQGRKERRR MSLLGSRRFL GDYLGIANKG GPGEMIRNGA GIGSDTVLFS CRGEVLVSKF
GRSSKPSPRI FVLTNRHFII VAQNLVNGQL VISAERTIPI GAIKSVSTSN LKDDWFSFVI
GAQEPDPLMN CVFKTELFTH LSNALHGQLN IKIADHIEYN KKPGKLATVK VVKEPGSSNV
DTYKSSTIHT SAGEPPSSVS KPTPRGKQVA ARPVTKGKLL RPGGPGGGPS KLAARPMPAR
QPVPQPAASQ APAPQPAAVP RPVPQPVAAV AASHTRTASS GSMRAPPPPP PVSPPAPKKP
MAKVLYDFSS AQSNELSIKA GELVEIVSKE GNGWWLCMNT TTSVQGWTPQ AYLEEQKAAP
PPPPPAAPRS TPATNGTATA AAAKAKPAPP APPAKRPNMA GRKMAPPPPS APRDSAVSMN
SQDSSGGSGR GTPNSASNAS LAGGLAEALR QRQEAMHGKQ DDDDEW
//
