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A1C4A5

- MYO1_ASPCL

UniProt

A1C4A5 - MYO1_ASPCL

Protein

Myosin-1

Gene

myoA

Organism
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 45 (01 Oct 2014)
      Sequence version 2 (10 Jun 2008)
      Previous versions | rss
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    Functioni

    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.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi143 – 1508ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. motor activity Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Motor protein, Myosin

    Keywords - Ligandi

    Actin-binding, ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myosin-1
    Alternative name(s):
    Class I unconventional myosin
    Type I myosin
    Gene namesi
    Name:myoA
    ORF Names:ACLA_059080
    OrganismiAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
    Taxonomic identifieri344612 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006701: Unassembled WGS sequence

    Subcellular locationi

    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.By similarity

    GO - Cellular componenti

    1. actin cortical patch Source: UniProtKB-SubCell
    2. myosin complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12531253Myosin-1PRO_0000338536Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei371 – 3711PhosphoserineBy similarity

    Post-translational modificationi

    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.By similarity

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi5057.CADACLAP00005561.

    Structurei

    3D structure databases

    ProteinModelPortaliA1C4A5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini50 – 729680Myosin motorAdd
    BLAST
    Domaini733 – 75321IQ 1Add
    BLAST
    Domaini754 – 77926IQ 2Add
    BLAST
    Domaini1080 – 114162SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni418 – 50083Actin-bindingBy similarityAdd
    BLAST
    Regioni780 – 977198Basic, putative membrane-binding regionBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi983 – 1199217Pro-richAdd
    BLAST
    Compositional biasi1020 – 108768Ala-richAdd
    BLAST
    Compositional biasi1248 – 12525Poly-Asp

    Domaini

    The myosin motor domain displays actin-stimulated ATPase activity and generates 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).By similarity

    Sequence similaritiesi

    Contains 2 IQ domains.Curated
    Contains 1 myosin motor domain.Curated
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH3 domain

    Phylogenomic databases

    eggNOGiCOG5022.
    HOGENOMiHOG000260265.
    KOiK10356.
    OrthoDBiEOG7VDXXK.

    Family and domain databases

    InterProiIPR001609. Myosin_head_motor_dom.
    IPR010926. Myosin_tail_2.
    IPR027417. P-loop_NTPase.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF00063. Myosin_head. 1 hit.
    PF06017. Myosin_TH1. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00193. MYOSINHEAVY.
    SMARTiSM00242. MYSc. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS51456. MYOSIN_MOTOR. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A1C4A5-1 [UniParc]FASTAAdd to Basket

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    MGHSRRPVGG EKKSRGFGRS KAAADVGDGR QAGKPQVKKA VFESTKKKEI     50
    GVSDLTLLSK ISNEAINDNL KLRFEHDEIY TYIGHVLVSV NPFRDLGIYT 100
    DNVLESYRGK NRLEVPPHVF AVAESAYYNM KSYKDNQCVI ISGESGAGKT 150
    EAAKRIMQYI ASVSGGTDSS IQQIKEMVLA TNPLLESFGN AKTLRNNNSS 200
    RFGKYLELEF NTNGEPVGAN ITNYLLEKSR VVGQITNERN FHIFYQFTKA 250
    APQKYRDMFG IQQPQSYLYT SRSKCYDVPG IDDSAEFRDT VNAMNVIGMT 300
    ESEQDNVFRM LAAILWIGNV QFAEDDSGNA AITDQSVVDF IAYLLEVDAA 350
    QVNKAFTIRV METARGGRRG SIYEVPLNTV QALAVRDALA KAIYFNLFDW 400
    IVQRVNSSLA ARGEIANSIG ILDIYGFEIF EKNSFEQLCI NYVNEKLQQI 450
    FIQLTLKAEQ DEYAREQIQW TPIKYFDNKV VCSLIEDKRP PGVFAALNDA 500
    CATAHADSGA ADNTFVGRLN FLSQNPNFEN RQGQFIVKHY AGDVSYAVTG 550
    MTDKNKDQLL KDLLNLVGSS GNQFVHTLFP EQVNQDDKRR PPTASDKIKA 600
    SANDLVATLM KAQPSYIRTI KPNDNKAPRE YNVGNVLHQI KYLGLQENVR 650
    IRRAGFAYRQ TFDKFVERFY LLSPKTSYAG DYTWTGSAES GARQILKDTS 700
    IPAEEYQMGI TKVFVKTPET LFALEAMRDR YWHNMAIRIQ RAWRNYLRYR 750
    IECATRIQRF WRRTTGGLEF IKLRDQGHQL LNGRKERRRM SLLGSRRFLG 800
    DYIGVGNKGG PGEMVRNGAG ISGSEDILFS CRGEVLVSKF GRSSKPAPRI 850
    LVLTNRHIYI IAQNILNNQL VISSERTIPI GAIKAISASN LKDDWFSIVV 900
    GSAQEPDPLL SCVFKTELFT HLNNALRGQL NLKIADHIEY SKKPGKMATV 950
    KVVKDPAVTG DDTYKSSTIH TGAGEPASSV SKPTPRPKPV SARPVTKGKL 1000
    LRPGGPGGGP SKLASRPTPA AQPLPRATPQ PAAAQPAAPQ PAARVVPQPV 1050
    AAVAASHART GSTASVRAPP PPPPAAAPAP KKPTAKALYD FNSQQPNELS 1100
    IKAGEIVQIV SKEGNGWWLC MNMATSSQGW TPEAYLEEQV APAPKPTPPP 1150
    PPPAAPRSTP TPVNGAAAAA KAKPAPPAPP AKRPNMAGRK AVPAPPPAPR 1200
    DSAVSMNSHD SSGGSGRGTP NSASNASLAG GLAEALRARQ HAMQGKNDDD 1250
    DDW 1253
    Length:1,253
    Mass (Da):137,388
    Last modified:June 10, 2008 - v2
    Checksum:i2B9EE08E2BE77772
    GO

    Sequence cautioni

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS026990 Genomic DNA. Translation: EAW15245.1. Different initiation.
    RefSeqiXP_001276671.1. XM_001276670.1.

    Genome annotation databases

    GeneIDi4708852.
    KEGGiact:ACLA_059080.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS026990 Genomic DNA. Translation: EAW15245.1 . Different initiation.
    RefSeqi XP_001276671.1. XM_001276670.1.

    3D structure databases

    ProteinModelPortali A1C4A5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5057.CADACLAP00005561.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 4708852.
    KEGGi act:ACLA_059080.

    Phylogenomic databases

    eggNOGi COG5022.
    HOGENOMi HOG000260265.
    KOi K10356.
    OrthoDBi EOG7VDXXK.

    Family and domain databases

    InterProi IPR001609. Myosin_head_motor_dom.
    IPR010926. Myosin_tail_2.
    IPR027417. P-loop_NTPase.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF00063. Myosin_head. 1 hit.
    PF06017. Myosin_TH1. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00193. MYOSINHEAVY.
    SMARTi SM00242. MYSc. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS51456. MYOSIN_MOTOR. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1.

    Entry informationi

    Entry nameiMYO1_ASPCL
    AccessioniPrimary (citable) accession number: A1C4A5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 45 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3