ID A0A0C9XQC6_9AGAR Unreviewed; 1261 AA.
AC A0A0C9XQC6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Myosin-1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=K443DRAFT_201139 {ECO:0000313|EMBL:KIK07261.1};
OS Laccaria amethystina LaAM-08-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIK07261.1, ECO:0000313|Proteomes:UP000054477};
RN [1] {ECO:0000313|EMBL:KIK07261.1, ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIK07261.1,
RC ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) 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. {ECO:0000256|ARBA:ARBA00025586}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000256|ARBA:ARBA00004134}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; KN838548; KIK07261.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9XQC6; -.
DR STRING; 1095629.A0A0C9XQC6; -.
DR HOGENOM; CLU_000192_7_6_1; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000054477; 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-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051179; P:localization; IEA:UniProt.
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; PF07653; SH3_2; 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 {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Reference proteome {ECO:0000313|Proteomes:UP000054477};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 38..717
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 775..964
FT /note="TH1"
FT /evidence="ECO:0000259|PROSITE:PS51757"
FT DOMAIN 1055..1113
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..612
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 956..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1034
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1058
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1134
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1203
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 131..138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1261 AA; 139281 MW; 5477D3B951686A92 CRC64;
MAPSKKAGKK VTPASKKSAG QGKVAKADWK EGFKKKQVGV SDMTLLTTIS NEGVNENLQK
RWTNGEIYTY IGAVLISVNP FRDLGIYGEE TLQRYRGKNR LEVPPHVFGI AESAYYNMNA
YHENQCVIIS GESGAGKTEA AKRIMQYIAV VSGGQDSSIQ EIKDMVLATN PLLESFGCAK
TLRNNNSSRH GKYLEIMFNG VGEPVGAQIT NYLLEKSRVV GQIENERNFH IFYQFTKGAS
DEQRELFGLQ GPEAYAYTSL SNCLEVSDID DVKDYHDTIT AMGVIGLTPD EQNEIFKMLA
IILWLGNVQF EEKDDGNSSI TDTGVTDFVG YLMEADAALV QKVLTSRVVE TSKGGRRGSI
YDVPLNPAQA TSGRDALAKA IYNNLFEWIV SRINVSMKTR SAHAQIIGIL DIFGFEIFED
NSFEQLCINY VNEKLQQIFI ELTLKTEQEE YVREQIKWNP IKYFNNKIVC DLIEERRPPG
IFAALNDACA TAHADPAAAD NSFVQRTAML SSNAHFEARG SQFLVRHYAG DVMYNVAGMT
DKNKDSLIKD LLDLVGSSGN TFLQTLFPDR PDPNSKKRPP TAGDRIKQSA GALVDNLMKA
QPSYIRTIKP NQNRSSSEYD VKAILHQIKY LGLQENIRVR RAGFAYRNTF EKMVERFYLL
SPHTSYAGEY TWTGDSKSGC EQILKDTGIA KDEWQMGVTK AFIKNPETLF ALETMRDRYW
HNMAARIQRA FRNYMRYKHE CARRIQRFWK NNKEGIVYAQ IRDYGHQILA GRKERRRFSL
LSYRRFMGDY LDLNGKSSLG EELAGACNIG GESVTFSSRI QLLVSKLGRS SKPSPRFIVV
TEKAVHILIV SVRDGQTQYN LERRIALSTI KSIALSNLRD DWLTLNVNAS EEGDPLISCY
FKTELVSNLV KLTRSTANVV IGPTIEYSKK KDKMAQIKFI KDETVAKDDL YKSHAVHVAS
GEPQNSVSRP PARRKPGVVR PITQGKLLKA GGPSDKPKPR SVPKPKPVAQ PLPGRNSTTV
ASKPAIKPSL APTSTAGQRP PPAPPRNVAL PPARPEPPTY RAKFAFEGQE GEMCLKKDDI
VELVEKDENG WWLVKMDGVE GWAPNNYLEL VPPKVVSAPP PPPRSRPAPA PTPKISLTPV
VADASSKPVS VFPGLQPSNG SATPWKKPPT VDTTPASSRP SSAIGSKPPP PVAAKPKPPV
IPVKPSVSAK GSAKPPIPTA PRPPAASTSR PSAFSKPATA VGQVDLAAAL AKRAQRIADS
G
//
