Myosin-1 - Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Myosin-1

Alternative name(s):
Class I unconventional myosin
Type I myosin

Gene names

Name:	myoA
ORF Names:	ACLA_059080

Organism

Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]

Taxonomic identifier

344612 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus ›

Protein attributes

Sequence length	1253 AA.
Sequence status	Complete.
Protein existence	Inferred 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	Cytoplasm › cytoskeleton › actin 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 component	Cytoplasm Cytoskeleton
Domain	Repeat SH3 domain
Ligand	ATP-binding Actin-binding Nucleotide-binding
Molecular function	Hydrolase Motor protein Myosin
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	actin cortical patch localization Inferred from electronic annotation. Source: EnsemblFungi receptor-mediated endocytosis Inferred from electronic annotation. Source: EnsemblFungi response to salt stress Inferred from electronic annotation. Source: EnsemblFungi
Cellular_component	actin cortical patch Inferred from electronic annotation. Source: UniProtKB-SubCell mating projection tip Inferred from electronic annotation. Source: EnsemblFungi myosin complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW motor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1253

1253

Myosin-1

PRO_0000338536

Regions

Domain

38 – 702

665

Myosin head-like

Domain

733 – 753

21

IQ 1

Domain

754 – 779

26

IQ 2

Domain

1080 – 1141

62

SH3

Nucleotide binding

143 – 150

8

ATP Potential

Region

418 – 500

83

Actin-binding By similarity

Region

780 – 977

198

Basic, putative membrane-binding region By similarity

Compositional bias

983 – 1199

217

Pro-rich

Compositional bias

1020 – 1087

68

Ala-rich

Compositional bias

1248 – 1252

5

Poly-Asp

Amino acid modifications

Modified residue

371

1

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

A1C4A5 [UniParc].

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

1,253

137,388

        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

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References

[1]

"Genomic islands in the pathogenic filamentous fungus Aspergillus fumigatus."
Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.

Nierman W.C.
PLoS Genet. 4:E1000046-E1000046(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DS026990 Genomic DNA. Translation: EAW15245.1. Different initiation.
RefSeq	XP_001276671.1. XM_001276670.1.
3D structure databases
ProteinModelPortal	A1C4A5.
ModBase	Search...
Protein-protein interaction databases
STRING	5057.CADACLAP00005561.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4708852.
KEGG	act:ACLA_059080.
Phylogenomic databases
eggNOG	COG5022.
HOGENOM	HOG000260265.
KO	K10356.
OrthoDB	EOG4M950J.
Family and domain databases
InterPro	IPR001609. Myosin_head_motor_dom. IPR010926. Myosin_tail_2. IPR001452. SH3_domain. [Graphical view]
Pfam	PF00063. Myosin_head. 1 hit. PF06017. Myosin_TH1. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00193. MYOSINHEAVY.
SMART	SM00242. MYSc. 1 hit. SM00326. SH3. 1 hit. [Graphical view]
SUPFAM	SSF50044. SH3. 1 hit.
PROSITE	PS50096. IQ. False negative. PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MYO1_ASPCL

Accession

Primary (citable) accession number: A1C4A5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	June 10, 2008
Last modified:	April 3, 2013
This is version 38 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents