ID A0A072TQA3_MEDTR Unreviewed; 1178 AA.
AC A0A072TQA3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=P-loop nucleoside triphosphate hydrolase superfamily protein {ECO:0000313|EMBL:KEH19592.1};
DE SubName: Full=Putative myosin ATPase {ECO:0000313|EMBL:RHN40964.1};
DE EC=3.6.4.1 {ECO:0000313|EMBL:RHN40964.1};
GN Name=25502561 {ECO:0000313|EnsemblPlants:KEH19592};
GN OrderedLocusNames=MTR_8g464480 {ECO:0000313|EMBL:KEH19592.1};
GN ORFNames=MtrunA17_Chr8g0360791 {ECO:0000313|EMBL:RHN40964.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880 {ECO:0000313|EMBL:KEH19592.1, ECO:0000313|Proteomes:UP000002051};
RN [1] {ECO:0000313|EMBL:KEH19592.1, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:KEH19592.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:KEH19592,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [2] {ECO:0000313|EMBL:KEH19592.1, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=A17 {ECO:0000313|EMBL:KEH19592.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:KEH19592,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [3] {ECO:0000313|EnsemblPlants:KEH19592}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:KEH19592};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
RN [4] {ECO:0000313|EMBL:RHN40964.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:RHN40964.1};
RA Pecrix Y., Gamas P., Carrere S.;
RT "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL Nat. Plants 0:0-0(2018).
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; CM001224; KEH19592.1; -; Genomic_DNA.
DR EMBL; PSQE01000008; RHN40964.1; -; Genomic_DNA.
DR RefSeq; XP_013445566.1; XM_013590112.1.
DR AlphaFoldDB; A0A072TQA3; -.
DR STRING; 3880.A0A072TQA3; -.
DR EnsemblPlants; KEH19592; KEH19592; MTR_8g464480.
DR GeneID; 25502561; -.
DR Gramene; KEH19592; KEH19592; MTR_8g464480.
DR KEGG; mtr:25502561; -.
DR HOGENOM; CLU_000192_7_2_1; -.
DR OrthoDB; 5489458at2759; -.
DR Proteomes; UP000002051; Chromosome 8.
DR Proteomes; UP000265566; Chromosome 8.
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:0016787; F:hydrolase activity; 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; 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 Hydrolase {ECO:0000313|EMBL:KEH19592.1};
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:UP000002051}.
FT DOMAIN 121..170
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 174..845
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..747
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT COILED 968..1016
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 265..272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1178 AA; 133649 MW; D44B378B928E6C68 CRC64;
MVLSASPNSL TRSSLEEMLD SLRRKDEEEN DKNKELPPAL PSRPASKARL PPARRSLPNN
FKVGSVMNDN VESKRKEISI LTSTSRRESM SSFGRKRVKK DASVESPYAK LDCDTLSYFI
KMKLRVWCRQ PRGQWELGSI QSTSGEEASV LFSSGKVLKV ARSELVPANP DILEVADDLI
KLAYLNEPSV LHNLRFRYSR EMIYSKAGPV LIALNPFKDL QMYGNDYVST YRQRLVDSPH
VYGIAEAAYN QMMRDEVNQS IIISGESGSG KTETAKIAMQ YLAALGSGSF GRANDVLQTN
CILEAFGNAK TSVNDNSSRF GKFIEIHFSA TGKICGANIQ TYLLEKSRVV QLASGERSYH
VFYQLCAGSP SSLKERLNLK AACEYKYLNQ SDCMTIGGID DAKNFHQLMK AFDAVRIFKE
DQEMIFKMLA TILWLGNISF KVTDSENHIE VVGDEAITSA ALLMDCSSQD LMSALSSQKI
QSDQDIVSKS LTLLQAIETR DAIAKFIYSS LFEWLVQQVN KSLEVGENHT EKSISILDIC
GFQSFQKNSF EQFCINYANE RLQQHFYRHL FKLEQEDCES DGIDCTVLDF EDNQECLDLF
EKKPLSLLSL LDEESNFPEA SDLTFANKLK NLLDANHCFK EESGRAFSVR HYAGEVLYDT
NGFLEKNRDT LSSNSIQLLS SSNCELLKLF SEVFNQSEEH GNSTFHVGAA YSQKIGIGTK
FKDQLFKLMH QLESTTPHFI RCIKPNTKKL PGIYDNELVL QQLRCCGLLE AVRISRAGYP
TRIKHQDFSR RYGILLSETD VPQDPLTTTV AVLQKFNIPS EMYQVGYTKL YLRAGQIGAL
EDKRKHFLQA TVGIQKCFRG HQVRSYFCEL KNGVTTLQSF IRGEVTRRKH GVLTKSSITV
YSKKIEEIHA IILLQSVIRG WKVRRDSSNI NKLRKYHENA QPRRKSRVKM PEVKDLSNEL
VQNRPSALAE LQKRVYRAEA IIEQKEDENT ELKEKLKQSE RKRIEYEAKM KSMEDAWQKQ
MASLQTSLAA ARKSLASENG TVQPVRHDLV SPRYYDSEDA TLLGSQTTNG STHMKLSGSF
SVSDAGRQAN GTLTTVSNLM KEFEQRRQTF NDEVKALNEV KPGQSGNTNS ADELRKLKQR
FEGWKKQYKV RLRETKARIS ENEKSRRTWW GGKLSSRA
//
