MYO1_PICGU
ID MYO1_PICGU Reviewed; 1275 AA.
AC A5DKH0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 3.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Myosin-1;
DE AltName: Full=Class I unconventional myosin;
DE AltName: Full=Type I myosin;
GN Name=MYO1; ORFNames=PGUG_03771;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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-361) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDK39673.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CH408158; EDK39673.2; ALT_FRAME; Genomic_DNA.
DR RefSeq; XP_001484390.1; XM_001484340.1.
DR AlphaFoldDB; A5DKH0; -.
DR SMR; A5DKH0; -.
DR STRING; 4929.XP_001484390.1; -.
DR PRIDE; A5DKH0; -.
DR EnsemblFungi; EDK39673; EDK39673; PGUG_03771.
DR GeneID; 5126161; -.
DR KEGG; pgu:PGUG_03771; -.
DR eggNOG; KOG0162; Eukaryota.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; A5DKH0; -.
DR OrthoDB; 122881at2759; -.
DR Proteomes; UP000001997; 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..1275
FT /note="Myosin-1"
FT /id="PRO_0000338559"
FT DOMAIN 35..727
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 731..751
FT /note="IQ 1"
FT DOMAIN 752..777
FT /note="IQ 2"
FT DOMAIN 785..974
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1127..1187
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 410..493
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 966..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1183..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1251..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1045
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1125
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1207
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 128..135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1275 AA; 142433 MW; 2F2699A3388176D1 CRC64;
MAIVKRGARS KAKQEAPAKS GIKKAEFDLH KKKEVGVSDL TLLSKISDDS INDNLHKRFM
NNTIYTYIGH VLISVNPFQD LGIYTKEYLN MYKGKNRLEV PPHVFAIAES MYYHLKSYGE
SQCVIISGES GAGKTEAAKQ IMQYIANVSV DDKVSTTSEI TQIKDMVLAT NPLLESFGCA
KTLRNNNSSR HGKYLEIYFN PSNYQPVAAH ITNYLLEKQR VVSQITNERN FHIFYQLTKS
CPPEYKQSFG LQGPETYVYT SAAKCIDVEG INDGKDFAET LQAMNTIGLS KAEQDNIFRS
LASILWIGNI SFVENEDGNA AIRDDTVTTF VAYLLEVDAN VLKKSILERV IETSHGMRRG
STYHVPLNIV QATASRDALA KGIYNYLFDW IVERVNISLR GRAEAMEKKT IGILDIYGFE
IFEHNSFEQI CINYVNEKLQ QIFIQLTLKA EQDEYVQEQI KWTPIDYFNN KVVCDLIEAT
RPQPGLFAAL NDSIKTAHAD SDAADQVFAQ RLSMVGANNR HFEDRKGKFI IKHYAGDVVY
DVAGMTDKNK DAMLRDLLEM LSTSQNTFVN SVLFPPDLLA VLTDKKKRPE TASDKIKKSA
NLLVDTLSQC QPSYIRTIKP NQTKRPKEYD NAQVLHQVKY LGLKENVRIR RAGFAYRTTF
DKFVQRFYLL SPKTGYAGDY IWNGDDISAV REILKSCHIP DTEFQMGTSK VFIKTPETLF
AMEDMRDKYW HNMAARIQRA WRRYVKRKED AARLIQNAWK VKKHGNQFEQ LRDYGNGLLQ
GRKERRRMSM LGSRAFMGDY LGCNYSSGFG RFVLNQVGLN EHVVFSGKGE ILLSKFGRSS
KRLPRIFVLG RSSLYIIAEN LVERRLQLSK EFVIPINSIN YVGLSTFQDN WLAVSLHSPT
PTTPDVLINL DFKTELVTHL KKLNPGLTIK IGPTIEYQKK PGKFHTVKFV RSDVSTIPIH
GDVYKSGTVS VRPGLSPDSQ NPKRPRATSS KVDYSKYYNR GGRLAPARTV PPAHPTSQQR
TPVAPPSHAT QQQPSYPTPV APVHQQPNNH VRKVPPPAPS LNNNHQEAVT AATAAMNHVN
IQQPATVVQN HNSNPTAPSR PAKKAAPAPP VKKTAPPPPP SLSAAKPKWP TFKANYDYDG
SVSGSMALSA NDIVYITQNN GQWSLAKSLD ESKEGWVPTA YISECPPPSN LGGSKSPPPP
PPPSATTRTV PEQGGNAAAA ASTQQEGGLS NGLAGALLAK KNEETNLAGS IADALKKRSA
TRDSDDEEED DDDDW
