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Database: UniProt
Entry: A0A4P1R591_LUPAN
LinkDB: A0A4P1R591_LUPAN
Original site: A0A4P1R591_LUPAN 
ID   A0A4P1R591_LUPAN        Unreviewed;      1690 AA.
AC   A0A4P1R591;
DT   03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   03-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TanjilG_31056 {ECO:0000313|EMBL:OIW01874.1};
OS   Lupinus angustifolius (Narrow-leaved blue lupine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX   NCBI_TaxID=3871 {ECO:0000313|EMBL:OIW01874.1, ECO:0000313|Proteomes:UP000188354};
RN   [1] {ECO:0000313|EMBL:OIW01874.1, ECO:0000313|Proteomes:UP000188354}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tanjil {ECO:0000313|Proteomes:UP000188354};
RC   TISSUE=Whole plant {ECO:0000313|EMBL:OIW01874.1};
RX   PubMed=27557478; DOI=10.1111/pbi.12615;
RA   Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A.,
RA   Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R.,
RA   Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W.,
RA   McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.;
RT   "A comprehensive draft genome sequence for lupin (Lupinus angustifolius),
RT   an emerging health food: insights into plant-microbe interactions and
RT   legume evolution.";
RL   Plant Biotechnol. J. 15:318-330(2017).
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; CM007371; OIW01874.1; -; Genomic_DNA.
DR   RefSeq; XP_019462242.1; XM_019606697.1.
DR   STRING; 3871.A0A4P1R591; -.
DR   GeneID; 109361288; -.
DR   KEGG; lang:109361288; -.
DR   OrthoDB; 942984at2759; -.
DR   Proteomes; UP000188354; Chromosome LG11.
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:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR   GO; GO:0030048; P:actin filament-based movement; IEA:UniProt.
DR   CDD; cd15475; MyosinXI_CBD; 1.
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; IPR002710; Dilute_dom.
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; IPR037975; MyosinXI_CBD.
DR   InterPro; IPR036018; MYSc_Myo11.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF751; MYOSIN HEAVY CHAIN; 1.
DR   Pfam; PF01843; DIL; 1.
DR   Pfam; PF00612; IQ; 3.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM01132; DIL; 1.
DR   SMART; SM00015; IQ; 6.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51126; DILUTE; 1.
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:UP000188354}.
FT   DOMAIN          8..57
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          62..734
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1352..1635
FT                   /note="Dilute"
FT                   /evidence="ECO:0000259|PROSITE:PS51126"
FT   REGION          615..637
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1256..1303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          872..1254
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1280..1294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         156..163
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1690 AA;  192961 MW;  6DA0CAF44D6A349F CRC64;
     MAGQLSFVVG SHIWIEDFDE AWKDVEILES NDQEITVSSE SGTKVISKSS NIYPKDPEFP
     PDGVDDMTRL AYLHEPGVLQ NLQVRYDVNE IYTYTGNILI AVNPFRRLPH LYANETMARY
     KGAGIGEHSP HPFAIADSAY RRMINDGASQ AILVSGESGA GKTESTKMLM HYLAYMGGRA
     VTEGRSVEQQ VLESNPVLEA FGNAKTVRNN NSSRFGKFVE IQFDQKGRIS GAAIRTYLLE
     RSRVCQVSDP ERNYHCFYML CAAPKEDVNR FKLGNPRQFH YLNQSNCYEL DALDDSKEYL
     ATRRAMDVVG ISSDEQDAIF RIVAAVLHLG NIEFVKGVDD GTDSSQPKDD QSRFHLKTAA
     ELLMCDEQSL EDSFCKRVMV TRGEAITRSL DPNSAALSRD ALAKIVYSRL FDWIVDKINN
     SIGQDPNSKN LIGVLDIYGF ESFKTNSFEQ FCINLTNEKL QQHFNQHVFK MEQEEYTKEE
     IDWSYIEFVD NQDVLDLIEK KPGGIIALLD EACMFPRSTN ETFAEKLYQT FRDNKRFSKP
     KLSRTDFTVN HYAGDVTYQT ELFLDKNKDY VVPEHAALLR ASKCSFVAGL FPPLPEDTTK
     STKFSSVATQ FKQQLQSLLE TLSATEPHYI RCVKPNNLLK AGIFENINVL QQLRCGGVME
     AIRISCAGYP TRKSFDEFVQ RFAILEPKVL KACPDEMTAC KRILDKANLK DYQIGQTKVF
     LRAGQMAELD ACRAEVLGRS ATVIQRNGRT YICRKHYVLF RLSTIELQRV ARGQLARYRY
     EYMRREAASL KIQKQCRMYI SRTAYKTIYV SAVHIQAGMR GMTARNDLRF RKRTQAAIVI
     QSHCRSYLAR TRFRRLKKAT IAVQCSWRRT IARRELRKLR MAAREAKALE AAKVNLEKQV
     EELTSCLETE KRMREAKTQE NEKLQSSLHE IELQFQEAKA MLVQEREAAK KAAEHIQQFA
     VNAVDNELLN KLTEENEQLK EQVSSFEKKT NEIPVNVVDN ELLNKLTAEN EQLKELVNSF
     EKKTTNEIPV NVVDNELLNK LTAENEQLKE LVSSLEKKST HEFSVNVTDN ELVNKLTAEN
     EQLKELVNSF EKKTTDEFSV NVTDNELINK LSAENEQLKE RVNSFEKKTT HEFSVNVPDN
     ELINKLSAEN EQLKEMVNSL EKKTKLELPV NISENELISK LSSENEHFKD LVNSLEKKID
     ETERKYQESN KLSDDRMTQI METETRMIDL KTSMQRLEEK LSDMETENQV LRQQTLLSSS
     SRRMSGKFSP AAVPPLENGH QAPPSSTLAK PFGSESMRRS QMERQHESVD ALFKCVAKEL
     GFSEGKPVAA FTIYNCLLHW KAFEAEKTSI FDRLIQLIGS AIEDQDNNDN IAYWLSNTSA
     LLFHLQRCLR VPTTKKPPTP TSFFGRMTQG FRSSNSLSSS AFDVVHQVDA KYPALLFKQQ
     LAAYVEKIYG IIKENLKKDL LPLLSSCTKA HKTTNDNNQP DVSWLSIIEC LNKFLKILKE
     NYVHPVLVQK IFNQIFQYIN VEIFNNLLLH QECCTFINGE HVKAGLAELE LWCSEATEEY
     VGSPLDELKH ATQAIRFLVV RQKDGLSYDD LTNDLCPVLS AHQLYRICTL YQDDSDTMQS
     VSSDVTTSLK FLMSDDEEND SKSFLLEDNS SIPIIVEEVS SSIKEKTIPK VKPPSELLEN
     PAFQFLHDYS
//
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