MYO1_ASPCL
ID MYO1_ASPCL Reviewed; 1253 AA.
AC A1C4A5;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Myosin-1;
DE AltName: Full=Class I unconventional myosin;
DE AltName: Full=Type I myosin;
GN Name=myoA; ORFNames=ACLA_059080;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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-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=EAW15245.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS026990; EAW15245.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001276671.1; XM_001276670.1.
DR AlphaFoldDB; A1C4A5; -.
DR SMR; A1C4A5; -.
DR STRING; 5057.CADACLAP00005561; -.
DR EnsemblFungi; EAW15245; EAW15245; ACLA_059080.
DR GeneID; 4708852; -.
DR KEGG; act:ACLA_059080; -.
DR eggNOG; KOG0162; Eukaryota.
DR OrthoDB; 122881at2759; -.
DR Proteomes; UP000006701; 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: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 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..1253
FT /note="Myosin-1"
FT /id="PRO_0000338536"
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..977
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1080..1141
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..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1253
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 961..978
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1036
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1080
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1159
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1228
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"
SQ SEQUENCE 1253 AA; 137388 MW; 2B9EE08E2BE77772 CRC64;
MGHSRRPVGG EKKSRGFGRS KAAADVGDGR QAGKPQVKKA VFESTKKKEI GVSDLTLLSK
ISNEAINDNL KLRFEHDEIY TYIGHVLVSV NPFRDLGIYT DNVLESYRGK NRLEVPPHVF
AVAESAYYNM KSYKDNQCVI ISGESGAGKT EAAKRIMQYI ASVSGGTDSS IQQIKEMVLA
TNPLLESFGN AKTLRNNNSS RFGKYLELEF NTNGEPVGAN ITNYLLEKSR VVGQITNERN
FHIFYQFTKA APQKYRDMFG IQQPQSYLYT SRSKCYDVPG IDDSAEFRDT VNAMNVIGMT
ESEQDNVFRM LAAILWIGNV QFAEDDSGNA AITDQSVVDF IAYLLEVDAA QVNKAFTIRV
METARGGRRG SIYEVPLNTV QALAVRDALA KAIYFNLFDW IVQRVNSSLA ARGEIANSIG
ILDIYGFEIF EKNSFEQLCI NYVNEKLQQI FIQLTLKAEQ DEYAREQIQW TPIKYFDNKV
VCSLIEDKRP PGVFAALNDA CATAHADSGA ADNTFVGRLN FLSQNPNFEN RQGQFIVKHY
AGDVSYAVTG MTDKNKDQLL KDLLNLVGSS GNQFVHTLFP EQVNQDDKRR PPTASDKIKA
SANDLVATLM KAQPSYIRTI KPNDNKAPRE YNVGNVLHQI KYLGLQENVR IRRAGFAYRQ
TFDKFVERFY LLSPKTSYAG DYTWTGSAES GARQILKDTS IPAEEYQMGI TKVFVKTPET
LFALEAMRDR YWHNMAIRIQ RAWRNYLRYR IECATRIQRF WRRTTGGLEF IKLRDQGHQL
LNGRKERRRM SLLGSRRFLG DYIGVGNKGG PGEMVRNGAG ISGSEDILFS CRGEVLVSKF
GRSSKPAPRI LVLTNRHIYI IAQNILNNQL VISSERTIPI GAIKAISASN LKDDWFSIVV
GSAQEPDPLL SCVFKTELFT HLNNALRGQL NLKIADHIEY SKKPGKMATV KVVKDPAVTG
DDTYKSSTIH TGAGEPASSV SKPTPRPKPV SARPVTKGKL LRPGGPGGGP SKLASRPTPA
AQPLPRATPQ PAAAQPAAPQ PAARVVPQPV AAVAASHART GSTASVRAPP PPPPAAAPAP
KKPTAKALYD FNSQQPNELS IKAGEIVQIV SKEGNGWWLC MNMATSSQGW TPEAYLEEQV
APAPKPTPPP PPPAAPRSTP TPVNGAAAAA KAKPAPPAPP AKRPNMAGRK AVPAPPPAPR
DSAVSMNSHD SSGGSGRGTP NSASNASLAG GLAEALRARQ HAMQGKNDDD DDW
