ID A0A4P1RNH5_LUPAN Unreviewed; 1112 AA.
AC A0A4P1RNH5;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN ORFNames=TanjilG_21464 {ECO:0000313|EMBL:OIW14324.1};
OS Lupinus angustifolius (Narrow-leaved blue lupine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX NCBI_TaxID=3871 {ECO:0000313|EMBL:OIW14324.1, ECO:0000313|Proteomes:UP000188354};
RN [1] {ECO:0000313|EMBL:OIW14324.1, ECO:0000313|Proteomes:UP000188354}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tanjil {ECO:0000313|Proteomes:UP000188354};
RC TISSUE=Whole plant {ECO:0000313|EMBL:OIW14324.1};
RX PubMed=27557478; DOI=10.1111/pbi.12615;
RA Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A.,
RA Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R.,
RA Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W.,
RA McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.;
RT "A comprehensive draft genome sequence for lupin (Lupinus angustifolius),
RT an emerging health food: insights into plant-microbe interactions and
RT legume evolution.";
RL Plant Biotechnol. J. 15:318-330(2017).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR EMBL; CM007364; OIW14324.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4P1RNH5; -.
DR STRING; 3871.A0A4P1RNH5; -.
DR Proteomes; UP000188354; Chromosome LG04.
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; IPR019821; Kinesin_motor_CS.
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:SF22; KINESIN-LIKE PROTEIN KIN-14A-RELATED; 1.
DR PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 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; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000188354}.
FT DOMAIN 78..215
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 262..296
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 432..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 306..347
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 432..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 159..166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OIW14324.1"
SQ SEQUENCE 1112 AA; 123627 MW; A82879152AFAAD3E CRC64;
IRRFAQLARE DYLQLRQEAC ELQEYSNAKI DRVTRYLGVL AEKTRKLDKA ALEAEARISP
LINEKRRLFN DLLTSKGNIR VFCRTRPLFE DEGPSVVEFP DDYTIRVNTG DESLSNPKKD
FEFDRVYGPH VGQAELFSDV QPLVQSALDG YNVSIFAYGQ ANSGKTHTME GSSYDRGLYA
RCFEELFDLV NSDTTFTSQY KFRITVCELY NEQLRGFHVL IFRIVTIHIF YNCMTTGESS
HSKLYLVDLA GSEGLITEDD SGGNSKTLMI VNVCPKFSNL SQTLSSLSFS ARARNSALSL
GNRDTVKKWR DVANDARKEL YEKEKEIHDL KQEGLGLKQA LNDANDQCIL LFNEVQKAWK
HSSALQNDLK SEHILLSDKH KIEQEQNTQL KNQVSQLLQL EQDQKLQIQE QDLAIQSFQA
KITTLETQLN EALSSRETKS PSVPDADSTT LSNSSQTGDG VDTSAVTKKL EEELKKRDAL
IERLHEENEK LFERLTEKAS LAGSPQPTPF SKGSVNAQPR DMGRNGTSNN ATRSTDVLPS
PLGADKNDGT VAIVKSGSEI VKTTPAGEYL TTALNDFDPD QYEGHAAISD GTNKLLMLVL
AAVIKAGASR EHEILAEIKD AVFSFIRKME PKRVMDTMLV SRVRILYIRS FLARSAELQS
IKSRSSSRGS SPGRSPVQYV GEQIHGFKVN LKPEKKSKFS SVVLKIRGID QDIWRQQVTG
GKLREITEEA KSFAVGNKAL AALFVHTPAG ELQRQIRSWL AENFDFLSVS GNHGSEESTG
QLELLSTAIM DGWMAGLGAA LPPHTDALGQ ILYEYSKRVY TSQLQHLKDI AGTLATEEAE
DTAQVSKLRS ALESVDHKRK KIMQQIRSDI ALLTLENGGS PIQNPSTAAE DSRLASLISL
DGILKQIKVL FDQDITRLSS VNTLSKSKKR TIIASLDELT KQMPSLLEID HPCAQRQIAE
ARHMVESIPE EDDHIQDLSH APRQSTDPAF GSEIDVAQWN VLQFNTGANL PFIIKCGANS
NSELVIKADA RVQEPKGPEI VRVAPRPSIL ENMSLEEMKQ VFSELPESLT LLALARTADG
TRARYSRLYK TLASKVPSLK DLAGELEKGG AV
//
