ID A0A3Q7HF14_SOLLC Unreviewed; 1178 AA.
AC A0A3Q7HF14;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Myosin-2-like {ECO:0008006|Google:ProtNLM};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000313|EnsemblPlants:Solyc07g063590.3.1};
RN [1] {ECO:0000313|EnsemblPlants:Solyc07g063590.3.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc07g063590.3.1};
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [2] {ECO:0000313|EnsemblPlants:Solyc07g063590.3.1}
RP IDENTIFICATION.
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc07g063590.3.1};
RG EnsemblPlants;
RL Submitted (JAN-2019) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR RefSeq; XP_010324342.1; XM_010326040.2.
DR AlphaFoldDB; A0A3Q7HF14; -.
DR STRING; 4081.A0A3Q7HF14; -.
DR PaxDb; 4081-Solyc07g063590-2-1; -.
DR EnsemblPlants; Solyc07g063590.3.1; Solyc07g063590.3.1; Solyc07g063590.3.
DR GeneID; 101267827; -.
DR Gramene; Solyc07g063590.3.1; Solyc07g063590.3.1; Solyc07g063590.3.
DR KEGG; sly:101267827; -.
DR InParanoid; A0A3Q7HF14; -.
DR OMA; MNRNLAM; -.
DR OrthoDB; 5489458at2759; -.
DR Proteomes; UP000004994; Chromosome 7.
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; 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:SF706; MYOSIN-11; 1.
DR Pfam; PF00612; IQ; 2.
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:UP000004994}.
FT DOMAIN 133..182
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 186..848
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..750
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1034..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 965..1013
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 12..30
FT /note="Basic and acidic 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 1178 AA; 133529 MW; DCC04593670917EF CRC64;
MSTIVRSSLE EMLDSLRQRD ENEKPKDLPP ALPARPKLTS RTRPPSQRQP LSKRLSKGDV
ELENGKKKEE LKVLKRNVFG AMKVKGIEDS ESPYAMPSVK KNSTGRLREV NGGKVEKWRS
EAEWDDRLDY FVKKKLRIWC RLGNGAWVSG HIQSTSGGKA MVLLSDGSVV TVPVGEVLPS
NPDVLEGVDD LMQLSYLNEP SVLHNLQHRY ARDMIYSKAG PVLIAINPFK DIQLYGNEFV
TAYRQKLLSD PHVYSIADSA YDRMMEDEIS QSIIISGESG SGKTETAKFA MEYLAMLGGG
SNGIEKEVLQ TSYILEAFGN AKTSRNNNSS RFGKLVEIHF SPAGRICGAK IQTLILEKSR
VVQLLDGERS YHIFYQLCAG APPTLRDKLK LKGASEYKYL NQSGCLVIHD VDDAEEFCKL
MEALNTVRIS ERDQEHAFQM IASVLWLGNI TFQVIDDESR AEVVQSEAVT NAASLIGCTV
NDLILALSTC QIRAGKDKIA KSLTVEQATD RRDALAKFIY ANLFDWIVDQ MNRNLAMDKE
QMGRSINILD IYGFESFQGN SFEQFLINYA NERLQQHANR HLLKLEQEEY ELDGIDWSKV
DFEDNQECLN LFEKKPIGLI SLLNEESNSL TATDLTFVCK LKQHIKSSPC FKSEREEFCI
RHYAGEVTYD ATGFLAKNRD VLHPDITQLL SSSDSHLPED KKLSIPSTDA GVLDFQKQSV
ATKFKDNLFK LMQQLENTIP HFICCIKPNN KQLPGMSDKD LVIEQLRCCG VLEVVRISRS
GYPTRLTHQE FTSRYGFLLP KDSACQDPLS MSVAILHQFG ILPELYQVGY TKLYFRSGQI
ASLEDARNQV LQGTLELQKC FRGHRARRHF HELKGGVIIL QSFIRGEIER RLYNTKVMSK
AKVAREGSDE QLVAVVQIQS AIRGWLARRG LRKLRNSKML NVDKRRSGRK TEVKELPREI
LPSVVEDLER RVAKAEATTE QKEKENAALK EQVNQFETRC LEYEVKMRSM EEMWQKQMTS
LQQVSLAAAR NSLTAADTTG RPGKLEGSPS PQYYDSDDAT SMDTPAGRTP VSFSNNSLGV
VANREVNGGL SLISHLAMEF EQRKQNFDNE AMAIVHLKPG QLQSTNNPAD EYRRLKHRFE
EWKKEYKVRL KETKSKVHKL VHSKAGKSRR KWWGKKSK
//
