MYO1_VANPO
ID MYO1_VANPO Reviewed; 1214 AA.
AC A7TDZ8;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Myosin-1;
DE AltName: Full=Class I unconventional myosin;
DE AltName: Full=Type I myosin;
GN Name=MYO1; ORFNames=Kpol_1018p157;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {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-357) 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}.
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DR EMBL; DS480378; EDO19618.1; -; Genomic_DNA.
DR RefSeq; XP_001647476.1; XM_001647426.1.
DR AlphaFoldDB; A7TDZ8; -.
DR SMR; A7TDZ8; -.
DR STRING; 436907.A7TDZ8; -.
DR PRIDE; A7TDZ8; -.
DR EnsemblFungi; EDO19618; EDO19618; Kpol_1018p157.
DR GeneID; 5547982; -.
DR KEGG; vpo:Kpol_1018p157; -.
DR eggNOG; KOG0162; Eukaryota.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; A7TDZ8; -.
DR OMA; MESKWGT; -.
DR OrthoDB; 122881at2759; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
DR GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0051641; P:cellular localization; IEA:UniProt.
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..1214
FT /note="Myosin-1"
FT /id="PRO_0000338563"
FT DOMAIN 36..715
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 719..739
FT /note="IQ 1"
FT DOMAIN 740..765
FT /note="IQ 2"
FT DOMAIN 771..961
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1069..1131
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..486
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 926..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1193..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..980
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1070
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 129..136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1214 AA; 135786 MW; E884360D4C455117 CRC64;
MAIIKRGARN KTAQEPAKRS AKIKKATYDS GKKKEVGVSD LTLLSTISDE AINENLKKRF
TNGTIYTYIG HVLISVNPFR DLGIYTDAVL ESYKGKNRLE VPPHVFAIAE SMYYNLKAYN
ENQCVIISGE SGAGKTEAAK RIMQYIASAS ESNSESIGKI KDMVLATNPL LESFGCAKTL
RNNNSSRHGK YLEIRFNNQF EPCAGNITNY LLEKQRVVSQ IKEERNFHIF YQFTKGASEN
YRQTFGVQKP EQYIYTSAAG CTSVDTIDDV KDYEDTLKAM QVIGLSQDEQ DQIFRMLSSI
LWVGNISFVE NEEGNAQVRD TSVTDFVAYL LQIDSQVLMK ALVERTMETS HGMRRGSVYH
VPLNIVQATA VRDALAKAIY NNMFDWIVER VNISLQAYPG ADKSIGILDI YGFEIFEHNS
FEQICINYVN EKLQQIFIQL TLKSEQETYE REQIQWTPIK FFDNKIVCDL IESRRPPGIF
AAMNDSVATA HADSDAADQA FSQRLNLFST NPHFALRSNK FVIKHYAGDV TYDVNGITDK
NKDQLQRDLV ELIATSSNAF LRTIFPDNVD KDSKRRPPTA GDKIIKSANE LVETLSKAQP
SYIRTIKPNQ TKSPNDYDDQ QVLHQVKYLG LKENVRIRRA GFAYRQVFDK FVERFYLLSP
SCSYAGDYTW QGETLEAVKL ILKEASIPEK EYQVGVSQVF IKTPETLFAL EHMRDKYWYN
MAARIQRAWR RFLQRRIDSA TRIQRAIREK KGGNKYEKLR DEGSKILAAR KERRTMSLLG
FRAFMGDYLL CNERKSRGAY IKKQAGISDK VVFSIKGEQL QSKFGRSSVR VKKVLILTHS
HLYIIGQSMV QNSVQYTTEY KIDVNKIAGV SMTNLQDDWV AINLSNSTQP DPLLHTFFKT
ELVTQLKKLN GRIQVKIGTV IEYQKKPGKM HKVKSQVSEA TPKYNDNYKS GTILVRRGHP
ANSPQKKKPK KGKGHSKHHS TSTSAPRSSV QSSQPSAPVS RKTKKPAPPP PGSKKLSSSV
AQTASRPQPV ANSARGAAQP QATPQPAQVT QPQQKKVAPP PPPPPPMQSS EPKYEAAYDF
PGSGSPSELP LKKGEVVYIT REEPSGWSLA KTLDGSREGW VPTNYVVKHQ GGSVPPPPPA
PAAVQATQAA NVTSTPVSSS QSETATTATP ASVAAAQPNF SDGLASALAA RANKMRVESD
GEDNGNDDDD DDDW
