ID A0A072UBG9_MEDTR Unreviewed; 900 AA.
AC A0A072UBG9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=ATP-binding microtubule motor family protein, putative {ECO:0000313|EMBL:KEH26393.1};
DE SubName: Full=Putative plus-end-directed kinesin ATPase {ECO:0000313|EMBL:RHN51602.1};
DE EC=3.6.4.4 {ECO:0000313|EMBL:RHN51602.1};
GN Name=25496531 {ECO:0000313|EnsemblPlants:KEH26393};
GN OrderedLocusNames=MTR_6g053680 {ECO:0000313|EMBL:KEH26393.1};
GN ORFNames=MtrunA17_Chr6g0470541 {ECO:0000313|EMBL:RHN51602.1};
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:KEH26393.1, ECO:0000313|Proteomes:UP000002051};
RN [1] {ECO:0000313|EMBL:KEH26393.1, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:KEH26393.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:KEH26393,
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:KEH26393.1, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=A17 {ECO:0000313|EMBL:KEH26393.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:KEH26393,
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:KEH26393}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:KEH26393};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
RN [4] {ECO:0000313|Proteomes:UP000265566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17 {ECO:0000313|Proteomes:UP000265566};
RX PubMed=30397259; DOI=10.1038/s41477-018-0286-7;
RA Pecrix Y., Staton S.E., Sallet E., Lelandais-Briere C., Moreau S.,
RA Carrere S., Blein T., Jardinaud M.F., Latrasse D., Zouine M., Zahm M.,
RA Kreplak J., Mayjonade B., Satge C., Perez M., Cauet S., Marande W.,
RA Chantry-Darmon C., Lopez-Roques C., Bouchez O., Berard A., Debelle F.,
RA Munos S., Bendahmane A., Berges H., Niebel A., Buitink J., Frugier F.,
RA Benhamed M., Crespi M., Gouzy J., Gamas P.;
RT "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL Nat. Plants 4:1017-1025(2018).
RN [5] {ECO:0000313|EMBL:RHN51602.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:RHN51602.1};
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. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR EMBL; CM001222; KEH26393.1; -; Genomic_DNA.
DR EMBL; PSQE01000006; RHN51602.1; -; Genomic_DNA.
DR RefSeq; XP_013452365.1; XM_013596911.1.
DR AlphaFoldDB; A0A072UBG9; -.
DR STRING; 3880.A0A072UBG9; -.
DR EnsemblPlants; KEH26393; KEH26393; MTR_6g053680.
DR GeneID; 25496531; -.
DR Gramene; KEH26393; KEH26393; MTR_6g053680.
DR KEGG; mtr:25496531; -.
DR HOGENOM; CLU_001485_27_2_1; -.
DR OrthoDB; 129693at2759; -.
DR Proteomes; UP000002051; Chromosome 6.
DR Proteomes; UP000265566; Chromosome 6.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR Gene3D; 1.10.150.280; AF1531-like domain; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010994; RuvA_2-like.
DR PANTHER; PTHR24115:SF908; KINESIN-LIKE PROTEIN KIN-10C; 1.
DR PANTHER; PTHR24115; KINESIN-RELATED; 1.
DR Pfam; PF12836; HHH_3; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000313|EMBL:KEH26393.1}; Hydrolase {ECO:0000313|EMBL:RHN51602.1};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Reference proteome {ECO:0000313|Proteomes:UP000002051}.
FT DOMAIN 5..320
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 377..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 90..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 900 AA; 98721 MW; 299D7E11BEA38003 CRC64;
MASKKVRVVA KIRGFSDPDT ENSRTVDWVS VKTQDSGDVT ISFKEQSSSR YSVDYCYNQH
DDNEMIYSRE VKPLVSAAFE GFNSTVIAHG ARGSGKTHLI QGSLERPGLA ALATSEFLSM
AEKNGKSIAV SLYEVDHQDH AVDLLNPEQP QILVLEDHGR IQFKGLSQAP VKSISEFQNL
YIAACSANKA APKKGIERAH RSHIGLIVHV FSQNESMNGL VSKMNFVDMA GYEDARRKSS
DASGHVENNK LNKSIYALLN VCQALSTNES RVPFRESKLT RMLQDSLRGT SKVLLVSCLN
PSFCQDTVYM VSLASRSCQS IHQTPLDSMK KTASSTRQIA TWDSTKKSAS SAREIVTLDS
TKKNASSARK IVTLDSTKKN ASSVRQNVAT DSSNKKSSSV RQTVTLDSTK KSASLVRQNV
ASDSSKKISS SVRQTVTLDS TKKSASSAIQ TVTSDSTKKT ASSARQTVAS DSTKKTASSA
IHTVASDSTK KSASSAIQIV ASNSTKKSAN SAILTVTYRK KKIPQSVSAS TTKLPGSISH
IKENGVIATN SAIKGRKLFD EASHSAVKAE KDNSISKDGN DAQVNSRLDK EISIADVTRA
SESLLDNSLS EDGNHDELNS RVEKDNSSLN ASSEVEFDPT VEKVISSEDK HPYIINYSKD
LSIADEGHNM NKENNNLIEN EDFSPPISSQ LRELQSLVSS TPLCMQLPEN ECISHDDDQI
SAKIAEPTTL DTKRRDVMNT KSPWETFNKH GSEMENSTEI TEPRTPDAGR GDVMNTKSPW
ETFNMNGSRM KNSTEITEPR TPDTGRRDVM NTKSPWETFN LHGSGMKNSL VKDYLRILNT
AEKDELKKLK GIGEKRATYI LELREESPEP FKSLDDLKDI GLSEKQIKGM MKKEVGELFN
//
