ID A0A0L9TDZ6_PHAAN Unreviewed; 729 AA.
AC A0A0L9TDZ6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN ORFNames=LR48_Vigan569s001400 {ECO:0000313|EMBL:KOM28743.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
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; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM28743.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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; KQ258447; KOM28743.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L9TDZ6; -.
DR STRING; 3914.A0A0L9TDZ6; -.
DR EnsemblPlants; KOM28743; KOM28743; LR48_Vigan569s001400.
DR Gramene; KOM28743; KOM28743; LR48_Vigan569s001400.
DR OMA; HHETSIT; -.
DR Proteomes; UP000053144; Unassembled WGS sequence.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 2.
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; IPR031852; Vik1/Cik1_MT-bd.
DR PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR PANTHER; PTHR47972:SF28; PROTEIN CLARET SEGREGATIONAL; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16796; Microtub_bd; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000053144}.
FT DOMAIN 131..408
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 465..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 415..449
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 481..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 215..222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 729 AA; 82116 MW; 80272B5C6A5A3387 CRC64;
MRNFLEAVKE MQLLTFEASD LEKLGLFLKK ILKGDMGCLS KREFIETISL YLNQRSSLAS
NDFSKFCNCG GKRDSIRQNA NYSAKYAEVI NTQQKQLEDH IKSLEVASTS YHKVLEENRL
LYNEVQDLKG AIRVYCRVRP FLPGQSNGQS TVDYIGENGD MMIINPLKHG KDARRVFSFD
KVFGTTVTQE QIYADTQPLI RSVLDGYNVC IFAYGQTGSG KTYTMYFSSL TRYTLDIRNN
SQMNGINVPD AFLVPVTCTR DVLDLMRIGQ KNRAVGATAL NERSSRSHSV LTVHVRGREL
VSNSILRGCL HLVDLAGSER VDKSEAVGER LKEAQHINRS LSALGDVISA LAQKSPHIPY
RNSKLTQVLQ DSLGGHAKTL MFVHINPELN AFGETTSTLK FAERVSSIEL GAAQSNKETG
EIRELKEEIS NLKLALERKE AELDQWKAGN ARNVIDSQKP RAVSPFQLPK YGTSGNMKHE
TGQRLMDDRS LESRSCSSGK QRRSRFPSTL MEKDSMPKMS FPTEEKLVSS VKGRSPSPPV
RRSQSNDRGT VIKSKVKTET MDNQPILKHP FPAANKSLVT MPVVASTDTR IYVNSQETVK
HENISETIFN LQKFNYKKVH QEHEEEQFKQ ALSAVRQGGI RKSKVESKAK PKHNQLSPFK
IQKPDLTSSF IPDMEYAGES NVESPPKNDY SEAENDLRFM ESAVHGALSL KKLRQNFARN
FQNPESRYD
//
