MYO1_LODEL
ID MYO1_LODEL Reviewed; 1279 AA.
AC A5E4A8;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-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=LELG_04447;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
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-371) 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; CH981529; EDK46266.1; -; Genomic_DNA.
DR RefSeq; XP_001524475.1; XM_001524425.1.
DR AlphaFoldDB; A5E4A8; -.
DR SMR; A5E4A8; -.
DR STRING; 379508.A5E4A8; -.
DR PRIDE; A5E4A8; -.
DR EnsemblFungi; EDK46266; EDK46266; LELG_04447.
DR GeneID; 5231750; -.
DR KEGG; lel:LELG_04447; -.
DR VEuPathDB; FungiDB:LELG_04447; -.
DR eggNOG; KOG0162; Eukaryota.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; A5E4A8; -.
DR OMA; NGWWLCK; -.
DR OrthoDB; 122881at2759; -.
DR Proteomes; UP000001996; 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 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..1279
FT /note="Myosin-1"
FT /id="PRO_0000338554"
FT DOMAIN 48..736
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 740..760
FT /note="IQ 1"
FT DOMAIN 761..786
FT /note="IQ 2"
FT DOMAIN 794..984
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1129..1189
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..502
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 980..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1189..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1253..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1077
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1129
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 141..148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1279 AA; 142675 MW; 3C7B245AA11B153E CRC64;
MAIVKRGGRT RAKQQQAPAK VNNGLGAGAG AGGGIQKAEF DITKKKEVGV SDLTLLSKIT
DEAINENLHK RFMNDTIYTY IGHVLISVNP FRDLGIYTLE NLNKYKGRNR LEVPPHVFAI
AESMYYHLKS YGENQCVIIS GESGAGKTEA AKQIMQYIAN VSVDSGNAEI SKIKDMVLAT
NPLLESFGCA KTLRNNNSSR HGKYLEIKFS EGSYQPIAAH ITNYLLEKQR VVSQITNERN
FHIFYQFTKH CPPQYQQQFG IQGPETYVYT SAAKCITVDG IDDGKDFKDT LNAMNIIGLS
QAEQDNIFRI LALILWTGNI SFVEDESGNA AIRDDSVTNF VAYLLDVNAE ILKKAITERT
IETSHGMKRG STYHVPLNIV QATAVRDALA KGLYNNLFDW IVERVNLSLQ GNQGQSEKSI
GILDIYGFEI FEHNSFEQIC INYVNEKLQQ IFIQLTLKAE QDEYVQEQIK WTPIDYFNNK
VVCDLIEATR PQPGLFAALN DSIKTAHADS DAADQVFAQR LSMVGASNRH FEDRRGKFII
KHYAGDVTYD VAGMTDKNKD AMLRDLLELL GTSSNAFVTQ TLFPPNLLSE LVDSKKRPET
ASDKIKKSAN ILVDTLSQAT PSYIRTIKPN QTKKPRDYDN QQVLHQIKYL GLKENVRIRR
AGFAYRSTFQ RFVQRFYLLS PATGYAGDYI WQGDDLTAVK EILRACHIPT SEYQLGTTKV
FIKTPETLFA LEDMRDKYWH NMAARIQRAW RRYIKRKEDA AKTIQRAWRM KNHGNQFEQF
RDYGNSLLQG RKERRRFSML GSRAYMGDYL ACNDKTGFGR FVVNQVGIKE PVVFSAKGVI
LLSKFGRSSK RFPRIFVLTK SNLYIIAEVL VEKRLQLQRE FALPVHLIKS VGLSQLQDNW
VAVCLLSPTT TTPDVFINLD FKTELVAQLK KLNSGLSILI GPTVQYQKKP GKYQTVKFAI
GSGPHIPPLI DSYKSGTVTV NQGLPPTSKN PKRPRAKLGK VDYSKYYNRG VRSLAQPAFQ
SQPTASYRSE PAYPQPTTQL YATQHQPQQP QVPTRTASRK APPPAPSTQT AAQVSTLPQA
ARKPAAPARP AKKIAPQPPV KKAVSPQPPA KKTVAAPPPP PPPPALSKPK HPTYRAMYDY
DGSVAGSVPL VKDTIYYVLQ INGKWGLVKT MDETQEGWSP IDYLQEESSP SASAATQSYA
PTTASSNPVS TASSNTYTNT TQATTMLNGS LGNGLADALK AKKSEETTLA GSLADALKKR
QGVTRDDSDA EDDDDDDDW
