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Database: UniProt
Entry: A0A022PUH6_ERYGU
LinkDB: A0A022PUH6_ERYGU
Original site: A0A022PUH6_ERYGU 
ID   A0A022PUH6_ERYGU        Unreviewed;      1200 AA.
AC   A0A022PUH6;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=MIMGU_mgv1a000381mg {ECO:0000313|EMBL:EYU17905.1};
OS   Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX   NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU17905.1, ECO:0000313|Proteomes:UP000030748};
RN   [1] {ECO:0000313|EMBL:EYU17905.1, ECO:0000313|Proteomes:UP000030748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX   PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA   Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA   Schmutz J., Willis J.H., Rokhsar D.S.;
RT   "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT   population shotgun sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. Plant myosin class XI subfamily.
CC       {ECO:0000256|ARBA:ARBA00008049}.
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DR   EMBL; KI632344; EYU17905.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A022PUH6; -.
DR   STRING; 4155.A0A022PUH6; -.
DR   eggNOG; KOG0160; Eukaryota.
DR   Proteomes; UP000030748; Unassembled WGS sequence.
DR   GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR   CDD; cd01384; MYSc_Myo11; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 3.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.30.70.1590; -; 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   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR004009; Myosin_N.
DR   InterPro; IPR036018; MYSc_Myo11.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF706; MYOSIN-11; 1.
DR   Pfam; PF00612; IQ; 3.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF02736; Myosin_N; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 5.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50096; IQ; 5.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
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|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000030748}.
FT   DOMAIN          70..119
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          124..798
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          679..701
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1133..1163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1176..1200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          943..984
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1041..1103
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        11..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1139..1163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1185..1200
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         218..225
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1200 AA;  136016 MW;  3319FA8FD53E4826 CRC64;
     MPLFHTTPFP SPRTEPESAA AQQPPFTNQN PKTQISHALA VRFTGIFPAS VVSGITAEFK
     FLGLEHFDEK EGSHVWVEDP DIAWIDGQVI NVKGDEVEVQ ISDEKTVVAN ISKVYPKDED
     TPDGGVDDMT KLSYLHEPGV LHNLARRYQL NKIYTYSGGI LIAINPFQRL PDLYDAHMME
     QYKGAPLGKL NPHVFAIADV AFRAMRYEGK SNSILVSGES GAGKTETTKM LMQYLAYLGG
     RNGAEGRTVE QQVLESNPVL EAFGNAKTVR NNNSSRFGKF VELQFDKHGR ISGAAIRTYL
     LERSRVCQIS DPERNYHCFY LLCAAPQEEI EKYKLGHPNT FHYLNQSNCY ELVGVSDAHD
     YLATRKAMDV VGISQNEQDA IFRVVAAILH LGNVTFTKGE DIDSSVLEND VSKFHLQTAA
     ELLMCDPNAL EDALLRRVMV TPEEVIKRSL DPDGALVSRD GLAKTIYSRL FDWLVDKINF
     TIGQDPNSKS LIGVLDIYGF ESFKTNSFEQ FCINFTNEKL QQHFNQHVFK TEQEEYIKEE
     IDWSYIEFVD NQDVLDLIEK KPGGIIALLD EACMFPKSTH ETFSEKLYQT FKNHKRFIKP
     KLARTDFTIS HYAGEVQYQS DQFLDKNKDY VVAEHQDLLT ASQCPFVAAL FPPLPEETTK
     SSNKSSKFSS IGSRFKQQLQ QLMETLNSTE PHYIRCVKPN NHFQPTIFEN ASIMQQLRCG
     GVLEAIRISC SGYPTHKTFS EFLHRFGLLA PEILEENNDE MVACKKIVDK LGLAGAQIGK
     TKLFLRSGQM ADLDSQRAVK LSGAAKTIQA KFRSHNDLKH FVAVYRASVC IQSIARGVLA
     SRFYNYLKRE SASLKIQTNV RGHISRKSYS RLKYSVIVLQ SGMRAMAAHN KYKYRKRSKS
     ATVIQAHWRG HMAFSHYKKI RNATIVIQCG WRGMIARREL RKLKMAARET GALQEAKDKL
     EKRVEDLTLR LKQERRLRAD MEEAKCQEIT KLKQFVKTLQ NMVGETNGPL HEECEGYWTA
     SEEESSITKE TPAPFEDTKK IEALTSQVEK LKDLLEFERK RSDDFQRKYV ESLESEEAKR
     QKLEETERRV HQLQESLNRM IYSMSGQFSE LKMILCASSN STSASGFVAK HDMDDDSSAS
     SDTTSTDSDF TFPAPASTPP NFTSCNSGAF QLIVRDLSTP ETSGTEKWEN DKEGAFDDFF
//
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