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A1C4A5 (MYO1_ASPCL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myosin-1
Alternative name(s):
Class I unconventional myosin
Type I myosin
Gene names
Name:myoA
ORF Names:ACLA_059080
OrganismAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]
Taxonomic identifier344612 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length1253 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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. Plays an important role in polarized growth, spore germination, hyphal morphogenesis, and septal wall formation By similarity.

Subcellular location

Cytoplasmcytoskeletonactin patch By similarity. Note: Localizes to cortical patch-like structures. Enriched at sites of polarized growth, like the growing hyphal tips and sites of septum formation By similarity.

Domain

The myosin head-like domain displays actin-stimulated ATPase activity and constitutes the motor domain by generating a mechanochemical force By similarity.

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 domain (TH1), an Ala- and Pro-rich domain (TH2), followed by an SH3 domain and a C-terminal acidic domain (TH3).

Post-translational modification

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.

Sequence similarities

Contains 2 IQ domains.

Contains 1 myosin head-like domain.

Contains 1 SH3 domain.

Sequence caution

The sequence EAW15245.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   DomainRepeat
SH3 domain
   LigandActin-binding
ATP-binding
Nucleotide-binding
   Molecular functionHydrolase
Motor protein
Myosin
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular_componentactin cortical patch

Inferred from electronic annotation. Source: UniProtKB-SubCell

myosin complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

motor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12531253Myosin-1
PRO_0000338536

Regions

Domain38 – 702665Myosin head-like
Domain733 – 75321IQ 1
Domain754 – 77926IQ 2
Domain1080 – 114162SH3
Nucleotide binding143 – 1508ATP Potential
Region418 – 50083Actin-binding By similarity
Region780 – 977198Basic, putative membrane-binding region By similarity
Compositional bias983 – 1199217Pro-rich
Compositional bias1020 – 108768Ala-rich
Compositional bias1248 – 12525Poly-Asp

Amino acid modifications

Modified residue3711Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1C4A5 [UniParc].

Last modified June 10, 2008. Version 2.
Checksum: 2B9EE08E2BE77772

FASTA1,253137,388
        10         20         30         40         50         60 
MGHSRRPVGG EKKSRGFGRS KAAADVGDGR QAGKPQVKKA VFESTKKKEI GVSDLTLLSK 

        70         80         90        100        110        120 
ISNEAINDNL KLRFEHDEIY TYIGHVLVSV NPFRDLGIYT DNVLESYRGK NRLEVPPHVF 

       130        140        150        160        170        180 
AVAESAYYNM KSYKDNQCVI ISGESGAGKT EAAKRIMQYI ASVSGGTDSS IQQIKEMVLA 

       190        200        210        220        230        240 
TNPLLESFGN AKTLRNNNSS RFGKYLELEF NTNGEPVGAN ITNYLLEKSR VVGQITNERN 

       250        260        270        280        290        300 
FHIFYQFTKA APQKYRDMFG IQQPQSYLYT SRSKCYDVPG IDDSAEFRDT VNAMNVIGMT 

       310        320        330        340        350        360 
ESEQDNVFRM LAAILWIGNV QFAEDDSGNA AITDQSVVDF IAYLLEVDAA QVNKAFTIRV 

       370        380        390        400        410        420 
METARGGRRG SIYEVPLNTV QALAVRDALA KAIYFNLFDW IVQRVNSSLA ARGEIANSIG 

       430        440        450        460        470        480 
ILDIYGFEIF EKNSFEQLCI NYVNEKLQQI FIQLTLKAEQ DEYAREQIQW TPIKYFDNKV 

       490        500        510        520        530        540 
VCSLIEDKRP PGVFAALNDA CATAHADSGA ADNTFVGRLN FLSQNPNFEN RQGQFIVKHY 

       550        560        570        580        590        600 
AGDVSYAVTG MTDKNKDQLL KDLLNLVGSS GNQFVHTLFP EQVNQDDKRR PPTASDKIKA 

       610        620        630        640        650        660 
SANDLVATLM KAQPSYIRTI KPNDNKAPRE YNVGNVLHQI KYLGLQENVR IRRAGFAYRQ 

       670        680        690        700        710        720 
TFDKFVERFY LLSPKTSYAG DYTWTGSAES GARQILKDTS IPAEEYQMGI TKVFVKTPET 

       730        740        750        760        770        780 
LFALEAMRDR YWHNMAIRIQ RAWRNYLRYR IECATRIQRF WRRTTGGLEF IKLRDQGHQL 

       790        800        810        820        830        840 
LNGRKERRRM SLLGSRRFLG DYIGVGNKGG PGEMVRNGAG ISGSEDILFS CRGEVLVSKF 

       850        860        870        880        890        900 
GRSSKPAPRI LVLTNRHIYI IAQNILNNQL VISSERTIPI GAIKAISASN LKDDWFSIVV 

       910        920        930        940        950        960 
GSAQEPDPLL SCVFKTELFT HLNNALRGQL NLKIADHIEY SKKPGKMATV KVVKDPAVTG 

       970        980        990       1000       1010       1020 
DDTYKSSTIH TGAGEPASSV SKPTPRPKPV SARPVTKGKL LRPGGPGGGP SKLASRPTPA 

      1030       1040       1050       1060       1070       1080 
AQPLPRATPQ PAAAQPAAPQ PAARVVPQPV AAVAASHART GSTASVRAPP PPPPAAAPAP 

      1090       1100       1110       1120       1130       1140 
KKPTAKALYD FNSQQPNELS IKAGEIVQIV SKEGNGWWLC MNMATSSQGW TPEAYLEEQV 

      1150       1160       1170       1180       1190       1200 
APAPKPTPPP PPPAAPRSTP TPVNGAAAAA KAKPAPPAPP AKRPNMAGRK AVPAPPPAPR 

      1210       1220       1230       1240       1250 
DSAVSMNSHD SSGGSGRGTP NSASNASLAG GLAEALRARQ HAMQGKNDDD DDW 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS026990 Genomic DNA. Translation: EAW15245.1. Different initiation.
RefSeqXP_001276671.1. XM_001276670.1.

3D structure databases

ProteinModelPortalA1C4A5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5057.CADACLAP00005561.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4708852.
KEGGact:ACLA_059080.

Phylogenomic databases

eggNOGCOG5022.
HOGENOMHOG000260265.
KOK10356.
OrthoDBEOG7VDXXK.

Family and domain databases

InterProIPR001609. Myosin_head_motor_dom.
IPR010926. Myosin_tail_2.
IPR027417. P-loop_NTPase.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00063. Myosin_head. 1 hit.
PF06017. Myosin_TH1. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00193. MYOSINHEAVY.
SMARTSM00242. MYSc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMYO1_ASPCL
AccessionPrimary (citable) accession number: A1C4A5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: April 16, 2014
This is version 43 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families