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Database: UniProt
Entry: A0A151TW91_CAJCA
LinkDB: A0A151TW91_CAJCA
Original site: A0A151TW91_CAJCA 
ID   A0A151TW91_CAJCA        Unreviewed;       958 AA.
AC   A0A151TW91;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=KK1_010528 {ECO:0000313|EMBL:KYP71278.1};
OS   Cajanus cajan (Pigeon pea) (Cajanus indicus).
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; Cajanus.
OX   NCBI_TaxID=3821 {ECO:0000313|EMBL:KYP71278.1, ECO:0000313|Proteomes:UP000075243};
RN   [1] {ECO:0000313|EMBL:KYP71278.1, ECO:0000313|Proteomes:UP000075243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Asha {ECO:0000313|Proteomes:UP000075243};
RX   PubMed=22057054; DOI=10.1038/nbt.2022;
RA   Varshney R.K., Chen W., Li Y., Bharti A.K., Saxena R.K., Schlueter J.A.,
RA   Donoghue M.T., Azam S., Fan G., Whaley A.M., Farmer A.D., Sheridan J.,
RA   Iwata A., Tuteja R., Penmetsa R.V., Wu W., Upadhyaya H.D., Yang S.P.,
RA   Shah T., Saxena K.B., Michael T., McCombie W.R., Yang B., Zhang G.,
RA   Yang H., Wang J., Spillane C., Cook D.R., May G.D., Xu X., Jackson S.A.;
RT   "Draft genome sequence of pigeonpea (Cajanus cajan), an orphan legume crop
RT   of resource-poor farmers.";
RL   Nat. Biotechnol. 30:83-89(2012).
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; CM003605; KYP71278.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151TW91; -.
DR   STRING; 3821.A0A151TW91; -.
DR   OMA; NYHIRNS; -.
DR   Proteomes; UP000075243; Chromosome 3.
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   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; 2.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
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:SF12; KINESIN-LIKE PROTEIN KIN-14H; 1.
DR   PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF16796; Microtub_bd; 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; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394};
KW   Microtubule {ECO:0000256|RuleBase:RU000394};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075243}.
FT   DOMAIN          39..163
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          394..674
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          706..745
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          762..833
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          846..958
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        708..742
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        846..862
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         477..484
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   958 AA;  106172 MW;  0F451732D648FD68 CRC64;
     MEAEQVLTFS LASVIEDVLQ QHSGRLGVNL ASRKTEEDSL RRYEAARWLR KTVGVVRGKD
     LPAEPSEEDF RIGLRSGIIL CTVLNKVQPR AVPKVIEGPC DSVIIPDGAA LSTYEYFENV
     RSFLKVVEEM GIPTFEAFDL GGKSSRIVNC VLALKSYAEW KFGGGIGSWK YSGVANAKPP
     ISGKPLLREN SEPLMKPLRT VSSGDIDGYM SDPGLDRNEK GPFSSLNSLV CEYLADKKPE
     EVPIAVESLL SKVIEEFKHH TRIQHEMVCV FLFSLFSTSY YEEKYNQFEL EDSSRQNLIL
     KQQNNQFELE DSSRQNLILK QQNIVEQQNR ITSELKNIVH QTKLGMQSMQ NEHRKEIIYL
     SKHMHSLASA ASGYQKVLEE NRKLYNQVQD LKGNIRVYCR VRPFLGGQPS HYSSVSNVEE
     GSISIITPSK YGKEGKKTFN FNRAFGPSAT QGEVFSDTQP LIRSVLDGYN VCIFAYGQTG
     SGKTFTMSGP DDLNEETIGV NYHIRNSSHN GINVPDANLV PVSCTSDVIN LMNLGHKNRA
     VGSTAMNDRS SRSHSCLTVH VQGKNLTSGS TIRGSMHLVD LAGSERADKT EATGDRLKEA
     QHINKSLSAL GDVISSLAQK NAHVPYRNSK LTQLLQDSLG GQAKTLMFVH ISPEPEALGE
     TLSTLKFAER VSTVELGAAR VNKDNSDVKE LKEQIASLKA ALARKEGEAE NSQQSINSSS
     NEIPKLKSYA SSPIQRSWTS GPHPYNILKG LKNTASTLKR RSLDLHDMRR DSSPWPNVSR
     GLGKEDDKES ISGDSVDKIF MNRNDSMTSE DGLMGPWEAE SKQSSPMLSP TYLTEPSKIC
     MDQQPLHKKD NKDDEDLPKQ GLDTATTEEL DGNETETSES SELDLHWPSH IPKPIIGSSG
     LGIRAKKSSN IRPSLKNPPE VRSMIPSFIP VPTPKKPTPI TQARKPPGSN DIRRRITK
//
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