ID D7MEG3_ARALL Unreviewed; 1155 AA.
AC D7MEG3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ARALYDRAFT_492062 {ECO:0000313|EMBL:EFH43766.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; GL348719; EFH43766.1; -; Genomic_DNA.
DR RefSeq; XP_002867507.1; XM_002867461.1.
DR AlphaFoldDB; D7MEG3; -.
DR STRING; 81972.D7MEG3; -.
DR EnsemblPlants; fgenesh2_kg.7__1495__AT4G27370.1; fgenesh2_kg.7__1495__AT4G27370.1; fgenesh2_kg.7__1495__AT4G27370.1.
DR Gramene; fgenesh2_kg.7__1495__AT4G27370.1; fgenesh2_kg.7__1495__AT4G27370.1; fgenesh2_kg.7__1495__AT4G27370.1.
DR eggNOG; KOG0160; Eukaryota.
DR HOGENOM; CLU_000192_7_2_1; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
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:0030048; P:actin filament-based movement; IEA:UniProt.
DR CDD; cd01383; MYSc_Myo8; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.20.240.20; -; 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; IPR036022; MYSc_Myo8.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF763; MYOSIN-4; 1.
DR Pfam; PF00612; IQ; 3.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 3.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 3.
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:UP000008694}.
FT DOMAIN 118..168
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 172..852
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..754
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 934..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 975..1009
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 9..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..951
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 277..284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1155 AA; 132597 MW; 9080B2CF2020752C CRC64;
MMKISVKETL ESLRQHDASE RFKENSSSSL PSRSTFRAQM PSIRQSLPAN FRNAIAPESE
TIEKEDKDWS TEQITQSPYT AEKEKTENEV VKISTPQMSP AKNSHDPEWI NNAEYFIREK
LCVWFRVANG QWHLGKIHST SSDDVCVMLS TNDDVVKVSM EEIFPANPEI LEGVEDLTQL
SYLNEPSLLY NLRVRYSQEL IYSKAGPVLI AVNPFKNVQI YGEEFLSAYQ TKGLDAPHVY
AVADAAYDEM MRGTRLSIPN AFCAHKKHDL TMHMWSGESG AGKTETAKYA MQYLEALGGG
SFGVENEILK TNCILEAFGN AKTSRNDNSS RFGKLMEIHF SAKGKICGAK LETFSLNQSR
VAQLCNGERS YHIFYQLCAG ASPILKERLK LKAASEYDYL NQSNCLIMDR TDDAQKFHKL
MEAFNIVQIP QEYQERVFAL LAAVLWLGNV SFKVTDNENH VEVVADEAVT NVATLMGCNS
KELMVVLSTC KLQAGRDCIA KRLTLRQATD MRDSLAKIIY ASLFNWLVEK INISLEVGNS
RTGRSISILD IYGFESFENN SFEQFCINYA NERLQQHFNR HLFKLEQEEY EGDGIDWTKV
EFKDNQECLN LIEKKPIGLV SLLDEESNFP KATDTTFANK LKQHLNANSC FKGERGQGFR
IKHYAGEVLY NTNGFLEKNR DPLHVDLIQL LSSCKCQLLN LFSTKMRHEF LKPATFSDSM
NQSVITKFKG QLFKLMNKLE DTTPHFIRCI KPNSNQLPGL YEENHVLQQL RCCGVLEIVR
ISRSGYPTRL THQELAVRYG CLLLDTRISQ EPLSTSNAIL KQCNLPPEMY QVGYTKIYLR
TGLIGVLEER RKYVLRGILG LQKQFRGYQA RECFHNMRNA AVILQSYIRG ENARRNYIVV
KESAIVSTAI TEELDAAIHL QYMVRKWLAR KHLNSMQQKK KPRNEKKQPR RKSTRRVSED
KVVFFPDLCD PPCVLADLQS RVQKVEAAIM QKEDENTALQ EELQRFEERW LENEARMKSM
EETWQKHMSS MQMSLAAACK ILAPDKTASQ GNESEDTMSF GTPTKELKRS LSEVNNLSRE
FDQRSVIIHE DAKSLVEVNS QSSSRKQHAE ELRRLKLRFE KWKKDYKARL RETKARIRSN
GDEGRHRNWW CKKSC
//
