MYO1_COCIM
ID MYO1_COCIM Reviewed; 1251 AA.
AC Q1DLP2; J3K1J7;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Myosin-1;
DE AltName: Full=Class I unconventional myosin;
DE AltName: Full=Type I myosin;
GN Name=MYO1; ORFNames=CIMG_08771;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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-369) 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; GG704913; EAS30025.3; -; Genomic_DNA.
DR RefSeq; XP_001241608.1; XM_001241607.2.
DR AlphaFoldDB; Q1DLP2; -.
DR SMR; Q1DLP2; -.
DR STRING; 246410.Q1DLP2; -.
DR PRIDE; Q1DLP2; -.
DR EnsemblFungi; EAS30025; EAS30025; CIMG_08771.
DR GeneID; 4560098; -.
DR KEGG; cim:CIMG_08771; -.
DR VEuPathDB; FungiDB:CIMG_08771; -.
DR InParanoid; Q1DLP2; -.
DR OMA; NGWWLCK; -.
DR OrthoDB; 122881at2759; -.
DR Proteomes; UP000001261; 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 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..1251
FT /note="Myosin-1"
FT /id="PRO_0000338547"
FT DOMAIN 48..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..980
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..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..498
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 958..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1135..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1074
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1150
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1226
FT /note="Polar 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 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1251 AA; 138865 MW; F240C115D617E4FD CRC64;
MGQSKRPFKN KEEKKSRGFG RSRHDDAGAG GRPQVKKAVF ESTKKKEIGV SDLTLLSKVS
NEAINENLKK RFEHGEIYTY IGHVLVSVNP FRDLGIYTDK VLESYRGKNR LEVPPHVFAV
AEAGYYNMKA YKENQCVIIS GESGAGKTEA AKRLMQYIAN VSGGTDSSIQ QTKDMVLATN
PLLESFGNAK TLRNNNSSRF GKYLELQFNS VGEPVGATIT NYLLEKSRVV GQIKNERNFH
IFYQFTKAAP QSYRDAFGIQ QPQSYVYTSR SQCFDVAGMN DAADFNETIE AMRIIGLRQA
EQDNIFRVLS AILWLGNMQF QEDDHSNASI NDQSIIDFVA YLLEVDAEGV QKALTQRIVE
TARGGRRGSI YEVPLNTVQA TAVRDALAKA LYFNLFDWIV QRVNASLTAK GTVTNTIGIL
DIYGFEIFER NSFEQLCINY VNEKLQQIFI QLTLKTEQEE YAREQIKWTP IKYFDNKVVC
QLIEDKRPPG VFAALNDACA TAHADSGAAD QTFVGRLNFL SQNPNFESRQ GQFIVKHYAG
DVAYAVEGMT DKNKDQLLKD LLNLVNSSTN SFLHTLFPNR VNQDDKRRPP TAGDKIKASA
NDLVTTLAKA QPSYIRTIKP NDNKSPSEYN VANVIHQIKY LGLQENVRIR RAGFAYRQTF
EKFVERFYLL SPKTSYAGEY TWTGDAESGA RQILKDTSIP PEEYQMGVAK AFIKTPETLF
ALEHMRDRYW HNMATRIQRA WRNYLRYRTE CAIRIQRFWR RVTGGLEFIK LRDQGHKILG
GRKERRRYSL VGSRRFLGDY LGISNAGDMG DVIKSSINIS SGENILYSCR CELLVTKFGR
SSKPSPRLLI LTSRNVYVVV QKFVNNQLSI LAERMIPIGA IKFVSTSNLK DDWFSIGVGA
QQEPDPLISC VFKTEFFTYL TNALRGQLNL RIGETIEYNK KPGKLAVVKA VKDPAVPRDD
VYKSGTIRTG PGEPANSVSK PTPRPKQVPG KPITKGKLLR PGGPGGGPSK LAPRPKPVAQ
NLPENPRAAK QPAGEKFKPV AQSVTAVAAA HARTNSGSQN RPPPPPPPTQ PPAPKKDTAK
ALYDFDSGRS NELPLRKGEI VQVVTKESNG WWLCMNLETS AQGWAPEAYL EPIVAKTPSL
PPPPPSLPPQ SKSAVSNTLP NGPSRVNGAA AKAKPAPPAP PFKRPDINRK AAPAAAPRDS
AVSMNSHESP AGSGRATPSS LSNASIAGGL AEALRARQSA MQGKEQDDDD W
