ID G7IXU3_MEDTR Unreviewed; 1104 AA.
AC G7IXU3; A0A0C3VH20;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 2.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Kinesin heavy chain {ECO:0000313|EMBL:AES70665.2};
GN OrderedLocusNames=MTR_3g060900 {ECO:0000313|EMBL:AES70665.2};
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:AES70665.2, ECO:0000313|Proteomes:UP000002051};
RN [1] {ECO:0000313|EMBL:AES70665.2, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:AES70665.2}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:AES70665,
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:AES70665.2, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES70665,
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:AES70665}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES70665};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-14 subfamily.
CC {ECO:0000256|ARBA:ARBA00010899}.
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DR EMBL; CM001219; AES70665.2; -; Genomic_DNA.
DR RefSeq; XP_003600414.2; XM_003600366.2.
DR AlphaFoldDB; G7IXU3; -.
DR SMR; G7IXU3; -.
DR STRING; 3880.G7IXU3; -.
DR PaxDb; 3880-AES70665; -.
DR EnsemblPlants; AES70665; AES70665; MTR_3g060900.
DR Gramene; AES70665; AES70665; MTR_3g060900.
DR eggNOG; KOG0239; Eukaryota.
DR HOGENOM; CLU_001485_0_0_1; -.
DR Proteomes; UP000002051; Chromosome 3.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; IBA:GO_Central.
DR CDD; cd21203; CH_AtKIN14-like; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
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 PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR PANTHER; PTHR47972:SF28; PROTEIN CLARET SEGREGATIONAL; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00033; CH; 1.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000002051}.
FT DOMAIN 55..177
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 438..758
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 793..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..849
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1092
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 522..529
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1104 AA; 123096 MW; EF937C131B199E54 CRC64;
MPQEGSLSQN SFLISPSKRG LKGIVSMNIK EASCPAIEES FNDHDLAHRK AEEAASRRYE
ASEWLRQIDN VACSLLPPKP SEQQFCLSLR NGLILCNVLN KVNPGAVVKV VDNPALAAAA
SVEGAAHSAI QYFENMRNFL YAVKDMQLLT FEASDLEKGG SSNKVVDCIL CLKGYYEWKL
SGGIGVWRYG GTVRITSLPK MSPSSSVVGS ESADDSLDES ESSQYEHLLE FLHLSEEFLN
EETKTTNVLA FLFDHFGLRL LQAYLRETDG IDDLPLNTMV IDALLGKVVK DFSSLLVSQG
AELGLFLKKI LKGDIGCLSR REFVEAISLY LNQRSSLASN DFSKFCSCGG KRDSVRQNVN
YSAKYAEVIN TQQKQLETVK YYFEDTKLEV KQIHSEWEQE LIRLEHHVKS LEVASSSYHK
VLEENRSLYN QVQDLKGAIR VYCRVRPFLP GQSNGQSTVD YIGENGDMMI VNPIKQGKDA
RRVFSFNKVF GTSVTQEQIY ADTQPLIRSV LDGYNVCVFA YGQTGSGKTY TMSGPDLSAE
DTWGVNYRAL RDLFYISKER SDSIIYEVFV QMIEIYNEQV RDLLVNVRNT SQLNGLNVPD
AYLVPVTCTR DVLYLMRIGQ KNRTVGATAL NERSSRSHSV LTVHVRGREL VSNSILRGCL
HLVDLAGSER VDKSEAVGER LKEAQHINRS LSALGDVISA LAQKSPHIPY RNSKLTQVLQ
DSLGGHAKTL MFVHINPELN AIGETISTLK FAERVASIEL GAAQSNKETG EIRELKEEIS
SLKQALERKE TELEQLKAGN ARNISESPKR RAVSPYHLPR YGTSGSMKPE TSQRVMDDRN
LEARSCSSGK QRRSRFPSAF MDKESMPKMS LLTEEKLAGS GKGRSPSPPV RRSTSTDRGS
VIKNKVKSDT TDNQPVLKHP FPARVPVNKF LGTMPMAAAL ENNARLHLNS PEPVKYEEEQ
FKQALSAVRQ GGVRKSKVES KAKTKHHQLS PFKIQKSDLI PTFISGMETP PKSDHSDPEN
DLRFVDSSVH GALNLSKIRQ NFPRNFQNLE SRRTMQGGEP LSASKVDNKL LNGSASNHKE
GNNTSMPEFR RSRSTPRGNF FGLS
//
