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A1DBH2 (MYO1_NEOFI) 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:NFIA_098420
OrganismNeosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus) [Complete proteome]
Taxonomic identifier331117 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeNeosartorya

Protein attributes

Sequence length1250 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-372) 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.

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 – 12501250Myosin-1
PRO_0000338557

Regions

Domain53 – 717665Myosin head-like
Domain734 – 75421IQ 1
Domain755 – 78026IQ 2
Domain1076 – 113762SH3
Nucleotide binding144 – 1518ATP Potential
Region419 – 50183Actin-binding By similarity
Region781 – 978198Basic, putative membrane-binding region By similarity
Compositional bias974 – 1196223Pro-rich
Compositional bias1015 – 107561Ala-rich
Compositional bias1150 – 118839Ala-rich
Compositional bias1245 – 12495Poly-Asp

Amino acid modifications

Modified residue3721Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1DBH2 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 1E806FE5DAEF438B

FASTA1,250137,301
        10         20         30         40         50         60 
MGHSRRPAGG EKKSRGFGRS KAAADVGDGR QTGGKPQVKK ATFESTKKKE IGVSDLTLLS 

        70         80         90        100        110        120 
KISNEAINDN LKLRFEHDEI YTYIGHVLVS VNPFQDLGIY TDNVLQSYRG KNRLEVPPHV 

       130        140        150        160        170        180 
FAVAESAYYN MKSYKDNQCV IISGESGAGK TEAAKRIMQY IASVSGGTDS SIQHTKEMVL 

       190        200        210        220        230        240 
ATNPLLESFG NAKTLRNNNS SRFGKYLELE FNTNGEPVGA NITNYLLEKS RVVGQITNER 

       250        260        270        280        290        300 
NFHIFYQFTK AAPQKYRDLF GIQQPQSYLY TSRSKCYDVP GVDDSAEFRD TLNAMNVIGM 

       310        320        330        340        350        360 
TEGEQDDVFR MLAAILWIGN VQFAEDDSGN AVITDQSVVD YVAYLLEVDA AQVNKAFTIR 

       370        380        390        400        410        420 
VMETARGGRR GSVYEVPLNT VQALAVRDAL AKAIYFNLFD WIVQRVNASL TARGEVANSI 

       430        440        450        460        470        480 
GILDIYGFEI FEKNSFEQLC INYVNEKLQQ IFIQLTLKAE QDEYAREQIQ WTPIKYFDNK 

       490        500        510        520        530        540 
VVCSLIEDKR PPGVFAALND ACATAHADSS AADNTFVGRL NFLSQNPNFE NRQGQFIVKH 

       550        560        570        580        590        600 
YAGDVSYAVA GMTDKNKDQL LKDLLNLVGT SGNQFVHTLF PEQVNQDDKR RPPTASDKIK 

       610        620        630        640        650        660 
ASANDLVATL MKAQPSYIRT IKPNDNKAPK EYNVGNVLHQ IKYLGLQENV RIRRAGFAYR 

       670        680        690        700        710        720 
QTFDKFVERF YLLSPKTSYA GDYTWTGDAE SGARQILKDT SIPAEEYQMG ITKVFVKTPE 

       730        740        750        760        770        780 
TLFALEAMRD RYWHNMAIRI QRAWRNYLRY RTECAIRIQR FWRRTTGGLE FIKLRDQGHQ 

       790        800        810        820        830        840 
LLNGRKERRR MSLLGSRRFL GDYIGVGNKG GPGEMVRNGA GISGSEDILF SCRGEVLVSK 

       850        860        870        880        890        900 
FGRSSKPAPR ILVLTNRHVY IIAQNLVNNQ LVISSERTIP IGAIKAVSAS NLKDDWFSIV 

       910        920        930        940        950        960 
VGSPQEPDPL VNCVFKTEFF THLNNTLHGQ LNLKIADHIE YNKKPGKLAT VKVVKDPAVA 

       970        980        990       1000       1010       1020 
RDDSYKSGTI HTGPGEPANS VSKPTPRPKQ VSARPVTKGK LLRPGGPGGG PSKLAARPTP 

      1030       1040       1050       1060       1070       1080 
AAQPLPRATP QPAAPQPAAR AVPQPVAAVA ASHTRTGSTA SVRAPPPPPP AAAPAPKKPT 

      1090       1100       1110       1120       1130       1140 
AKVLYDFNSQ QSNELSIKAG EIVQIVSKEG NGWWLCMNMT TSAQGWTPEA YLEEQVAPTP 

      1150       1160       1170       1180       1190       1200 
KPAPPPPPPA APRSTPAPAT NGAAAAAKAK PAPPAPPAKR PNMAARKAVP TPPPAPRDSA 

      1210       1220       1230       1240       1250 
VSMNSHDSSG GSGRGTPNSM SNASLAGGLA EALRARQHAM QGKQDDDDDW 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS027694 Genomic DNA. Translation: EAW20212.1.
RefSeqXP_001262109.1. XM_001262108.1.

3D structure databases

ProteinModelPortalA1DBH2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING36630.CADNFIAP00009077.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADNFIAT00009291; CADNFIAP00009077; CADNFIAG00009291.
GeneID4588724.
KEGGnfi:NFIA_098420.

Phylogenomic databases

eggNOGCOG5022.
HOGENOMHOG000260265.
KOK10356.
OMAGNVLHQI.
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_NEOFI
AccessionPrimary (citable) accession number: A1DBH2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 43 of the entry and version 1 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