MYO1_LACBS
ID MYO1_LACBS Reviewed; 1252 AA.
AC B0CRJ3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Myosin-1;
DE AltName: Full=Class I unconventional myosin;
DE AltName: Full=Type I myosin;
GN Name=MYO1; ORFNames=LACBIDRAFT_229023;
OS Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS (Laccaria laccata var. bicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomataceae; Laccaria.
OX NCBI_TaxID=486041;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 / ATCC MYA-4686;
RX PubMed=18322534; DOI=10.1038/nature06556;
RA Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA Tuskan G., Grigoriev I.V.;
RT "The genome of Laccaria bicolor provides insights into mycorrhizal
RT symbiosis.";
RL Nature 452:88-92(2008).
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-356) 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=EDR15829.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS547091; EDR15829.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001874037.1; XM_001874002.1.
DR AlphaFoldDB; B0CRJ3; -.
DR SMR; B0CRJ3; -.
DR STRING; 486041.B0CRJ3; -.
DR EnsemblFungi; EDR15829; EDR15829; LACBIDRAFT_229023.
DR GeneID; 6069346; -.
DR KEGG; lbc:LACBIDRAFT_229023; -.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; B0CRJ3; -.
DR OrthoDB; 311886at2759; -.
DR Proteomes; UP000001194; 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; PF07653; SH3_2; 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..1252
FT /note="Myosin-1"
FT /id="PRO_0000338553"
FT DOMAIN 38..712
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 716..736
FT /note="IQ 1"
FT DOMAIN 737..762
FT /note="IQ 2"
FT DOMAIN 770..953
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1046..1104
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..485
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 945..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1048
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1120
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1214
FT /note="Pro 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 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1252 AA; 138491 MW; DC8752475B5B5210 CRC64;
MAPSKKAGKK VTPASKKSAG QGKVAKADWK EGFKKKQVGV SDMTLLTTIS NEGVNENLQK
RWTNGEIYTY IGAVLISVNP FRGRSVETLQ RYRGKNRLEV PPHVFGIAES AYYNMNAYHE
NQCVIISGES GAGKTEAAKR IMQYIAVVSG GQDSSIQEIK DMVLATNPLL ESFGCAKTLR
NNNSSRHGKY LEIMFNGVGE PVGAQITNYL LEKGRVVGQI ENERNFHIFY QFTKGASDEQ
RELFGLQGPE AYAYTSLSNC LEVSDIDDVK DYHDTITAMG VIGLTPDEQN EIFKMLAIVL
WLGNVQFEEM DDGNSSITDT GVTDFVGYLM EADSALVQKV LTSRVIETSK GGRRGSVYDV
PLNPAQATSG RDALAKAIYN NLFEWIVSRI NVSMKTRSAH AQIIGILDIF GFEIFEDNSF
EQLCINYVNE KLQQIFIELT LKTEQEEYVR EQIKWTPIKY FNNKIVCDLI EERRPPGIFA
ALNDACATAH ADPAAADNSF VQRTAMLSSN AHFEARGSQF LVRHYAGDVM YNVAGMTDKN
KDSLIKDLLD LVGSSGNTFL QTLFPDRPDP NSKKRPPTAG DRIKARALVD NLMKAQPSYI
RTIKPNQNRS SSEYDVKAIL HQIKYLGLNE NIRVRRAGFA YRNTFEKMVE RFYLLSSHTS
YAGEYTWTGD SKSGCEQILK DTGIAKDEWQ MGVTKAFIKN PETLFALETM RDKYWHNMAA
RIQRAFRNYM RYKHECARRI QRFWKNNKEG IAYAQTRDYG HQILAGRKER RRFSLLSYRR
FMGDYLDLNG KSSLGEELAG ACNIGGESVT FSSRIHLLVS KLGRSSKPSP RFIVVTEKAV
HILILSVRDG QTQYNLERRI PLSTIKSIGM SNLRDDWLAK EGDPLISCYF KTELVSNLVK
LTRSTVNVVI GPTIEYSKKK DKMAQIKFIK DETVAKDDLY KSHTVHVASG EPPNSVSRPP
AKRKPGVVRP ITQGKLLKAG GPSDKPKPRS VPKPKPVAQP LPGRDSTTVA PKPAIKPSVT
PSSTVGQRPP PAPPRNIAPP PPPAKPETPM YRAKFAFEGQ EGEMSLKKDD VVELVEKDDN
GWWLVKMDGV EGWAPNNYLE LVPPKAVSAP PPPPRSRPAP TTTPKISLTS VVADASSKPV
SVFPGMQPSN GSATPWKKPL TADTTPASSR PSSAIGSKPP PPVAAKPKPP VIPVKPSVSA
KGPAKPPIPT APRPPAASTS RSSKPATAVG QVDLAAAVSL FVTHSRELLL MM
