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Database: UniProt
Entry: G7IEA4_MEDTR
LinkDB: G7IEA4_MEDTR
Original site: G7IEA4_MEDTR 
ID   G7IEA4_MEDTR            Unreviewed;      1159 AA.
AC   G7IEA4;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=P-loop nucleoside triphosphate hydrolase superfamily protein {ECO:0000313|EMBL:AES62989.1};
GN   OrderedLocusNames=MTR_1g114540 {ECO:0000313|EMBL:AES62989.1};
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:AES62989.1, ECO:0000313|Proteomes:UP000002051};
RN   [1] {ECO:0000313|EMBL:AES62989.1, ECO:0000313|Proteomes:UP000002051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A17 {ECO:0000313|EMBL:AES62989.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:AES62989,
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:AES62989.1, ECO:0000313|Proteomes:UP000002051}
RP   GENOME REANNOTATION.
RC   STRAIN=A17 {ECO:0000313|EMBL:AES62989.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:AES62989,
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:AES62989}
RP   IDENTIFICATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES62989};
RG   EnsemblPlants;
RL   Submitted (APR-2015) 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   EMBL; CM001217; AES62989.1; -; Genomic_DNA.
DR   RefSeq; XP_003592738.1; XM_003592690.2.
DR   AlphaFoldDB; G7IEA4; -.
DR   STRING; 3880.G7IEA4; -.
DR   PaxDb; 3880-AES62989; -.
DR   EnsemblPlants; AES62989; AES62989; MTR_1g114540.
DR   Gramene; AES62989; AES62989; MTR_1g114540.
DR   eggNOG; KOG0160; Eukaryota.
DR   HOGENOM; CLU_000192_7_2_1; -.
DR   OMA; PHSYRYL; -.
DR   Proteomes; UP000002051; Chromosome 1.
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; -; 2.
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:SF780; MYOSIN-1; 1.
DR   Pfam; PF00612; IQ; 3.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 4.
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:AES62989.1};
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          126..175
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          179..834
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          1..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          714..736
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1021..1061
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          954..1002
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        93..121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1021..1035
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         270..277
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1159 AA;  131073 MW;  981973FCBFED6D0C CRC64;
     MSQTTGVPPA FQSIKSLPPE FKFDSNRNTG LVEKHGNAKV RSTDLIGSNG RKNGAIVGEV
     SKEVHNRAGG MDVSDEESPY GGNGESFEDR PSYPNEDSVS ASLPQPSIST PSGESRWSDT
     TPYASKKKLQ SWLQLSNGDW ELVKIISTSG TESVISLPDG KVLKVKDEDL VPANPDILDG
     VDDLMQLSYL NEPSVLYNLQ HRYNQNMIYT KAGPVLVAVN PFKKVPLYGT NYIEAYKRKA
     IESPHVYAIT DSAIREMIRD EVNQSIIISG ESGAGKTETA KIAMQYLAAL GGGSGIEHEI
     LKTNPILEAF GNGKTLRNDN SSRFGKLIEI HFSETGKISG ANIQTFLLEK SRVVQCNEGE
     RSYHIFYQLC AGAPSSLREK LNLRSVEDYK YLRQSNCYSI NDVDDAEEFR IVTDALDVVH
     ISKEDQENVF AMLAAVLWLG NISFTVIDNE NHVQAVEDEG LFSTAKLIVG KDTIVQKLTL
     SQASDARDAL AKSIYSCLFD WLVEQINKSL AVGKRQTGRS ISILDIYGFE SFNRNSFEQF
     CINYANERLQ QHFNRHLFKL EQEEYIQDGI DWAKVEFEDN QDCLNLFEKK PLGLLSLLDE
     ESTFPNGTDL TFANKLKQHL NSNSCFKEER EKAFTVRHYA GEVTYDTTAF LEKNRDLMHV
     DSIQLLSSSK CHLPQIFASY MLSQSEKPVV GPLHKLGGAD SQKLSVATKF KGQLFQLMQR
     LESTTPHFIR CIKPNNLQSP GSYEQGLVLQ QLRCCGVLEV VRISRSGFPT RMSHQKFAKR
     YGFLLLENVA SQDPLSVSVA ILHQFNILPE MYQVGYTKLF FRTGQIGVLE DTRNRTLHGI
     LRVQSCFRGY QARCHCKELW RGITTLQSFI RGEKSRKEFA TLLQRHRAAV IIQKHVKTVY
     QSKRMKDTID SAVVIQSFIR GWLVRRCSGD IGFLKSGGMK TNESDEVLVK ASFLAELQRR
     VLKAEAGLRE KDEENDILHQ RLQQYESRWS EYELKMKSME EVWQKQMRSL QSSLSIAKKS
     LAMDDSERNS DASVNASDDK EYSWDMGNNH RRQESSGTRS MSAGLSVISR LAEEFEQRSQ
     VFGDDAKFLV EVKSGQIEAS LNPDRELRRL KQMFEGWKKD YAARLRETKV ILNKLGSEDG
     SIEKAKKKWW GRRNSTRMS
//
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