ID MYO1_USTMA Reviewed; 1282 AA.
AC Q7Z8J6; A0A0D1DV68; Q4P701;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=Myosin-1;
DE AltName: Full=Class I unconventional myosin;
DE AltName: Full=Type I myosin;
GN Name=myo1; ORFNames=UMAG_11115;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14615599; DOI=10.1105/tpc.016246;
RA Weber I., Gruber C., Steinberg G.;
RT "A class-V myosin required for mating, hyphal growth, and pathogenicity in
RT the dimorphic plant pathogen Ustilago maydis.";
RL Plant Cell 15:2826-2842(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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-365) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ577237; CAE11865.1; -; Genomic_DNA.
DR EMBL; CM003151; KIS67611.1; -; Genomic_DNA.
DR RefSeq; XP_011390802.1; XM_011392500.1.
DR AlphaFoldDB; Q7Z8J6; -.
DR SMR; Q7Z8J6; -.
DR STRING; 237631.Q7Z8J6; -.
DR EnsemblFungi; KIS67611; KIS67611; UMAG_11115.
DR GeneID; 23567041; -.
DR KEGG; uma:UMAG_11115; -.
DR VEuPathDB; FungiDB:UMAG_11115; -.
DR InParanoid; Q7Z8J6; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000000561; Chromosome 12.
DR GO; GO:0030479; C:actin cortical patch; IBA:GO_Central.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0051285; C:cell cortex of cell tip; IEA:EnsemblFungi.
DR GO; GO:0051286; C:cell tip; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043332; C:mating projection tip; IEA:EnsemblFungi.
DR GO; GO:0031097; C:medial cortex; IEA:EnsemblFungi.
DR GO; GO:0045160; C:myosin I complex; IEA:EnsemblFungi.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0044853; C:plasma membrane raft; IEA:EnsemblFungi.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0071933; F:Arp2/3 complex binding; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0000147; P:actin cortical patch assembly; IEA:EnsemblFungi.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:EnsemblFungi.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd01378; MYSc_Myo1; 1.
DR CDD; cd11858; SH3_Myosin-I_fungi; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 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 PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF837; MYOSIN-3-RELATED; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50044; SH3-domain; 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..1282
FT /note="Myosin-1"
FT /id="PRO_0000338562"
FT DOMAIN 44..723
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 727..747
FT /note="IQ 1"
FT DOMAIN 748..773
FT /note="IQ 2"
FT DOMAIN 781..977
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1074..1135
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..494
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 569..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1237..1282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1071
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 137..144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1282 AA; 139582 MW; C8E066B8902076A1 CRC64;
MAISKKAGAK KAGAVSKPPP SKGASSKGGV AKADWREGFK KAQAGVSDMT LLSKVTNEAI
NDNLQKRFQN AEIYTYIGNV LISVNPFRDL GIYTEDILQS YRGKNRLEMT PHVFAIAEGA
YYNMNAYKEN QCVIISGESG AGKTEAAKRI MQYIAAVSGG SNSGIQDVKD MVLATNPLLE
SFGCAKTLRN NNSSRHGKYL EIMFNAHGEP IGANITNYLL EKNRVVQQIH DERNFHIFYQ
FTKAATATHR ENYGIQGPEA YAYTANSQCL DVNGIDDHAD FRETISAMNT IGLTADEQDN
IFRMIAAILW IGNVQYVENQ EGNAEISDPG VPDFVAYLLE VDAGNVTKAL TQRIMETQRG
GRRGSVYEVP LNPTQAAAAR DALAKAIYNN MFDWIVERIN QSMNPRTQSS NVIGVLDIYG
FEIFDNNSFE QLCINYVNEK LQQIFIELTL KKEQEEYAYE QIQWTPIKYF NNKIVCDLIE
EKRPPGIFSA LNDACATAHA DPTAADNSFI QRTGMLSSNP HFDSRGTKFL IKHYAGDVMY
NVQGMTDKNK DSLLKDILDL VDSSTNSYLQ KLFPDRPDPN SKKRPPTAGD RIKASANALV
ENLMRAQPSY IRTIKPNQNK SPTEYDSQAI LHQIKYLGLQ ENIRVRRAGF AYRNTFEKMV
ERFYLLSPNT SYAGEYTWQG DARSGCERIL TDTGIAREEW QMGVTKAFIK NPETLFALET
MRDRYWHNMA MRIQRAYRNY LRYKEECARR IQRMWKNNKE GLQYIQLRDY GHQVLAGRKE
RRRFSLLGLR RFMGDYLDVG GANGKGGGSA EGQMLRQATG MAAGEAVAFS SRAQLLVSRL
GRSSVRSPRF LILTDKAVYI LVTQLVNKQV STTCERRINL GAISAVGLSN LRDDWLVLNV
NNAEEADPIL HCYFKTELVT HLLQRTNGAI NVIVSNSLEY SKKKGKKAQI TFRKDETVQK
DDVYKSSAVS VCSGEPANSV SRPAPKKKPG LVRPITQGKL LRAGGPSNAN NKPKPRAIPR
STPTPAKLPG SGAAGTARPA AAVGSASAGA GVGATRSAPR PPPPPPAAVA PSEPQVARYK
ALYVFATENA GEMALDKDDV VEVTQKDETG SGWWLVKKNG VEGWAPSNYL ELIVQAAPKP
KAAPAPPVKR AAPVAPSATT ASQRPAVAAK PAFGGAAAGV VQPKPVVKTT PAGGKPHERA
AAVQADAAAA PVSVMPGLGA PGGFAAVLAK KKAENAAAAA AAGAGANGKG AGAPPAVAAK
PVVAPKPAGS NGRAMPPPPP RR
//
