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Database: UniProt
Entry: A0A151S888_CAJCA
LinkDB: A0A151S888_CAJCA
Original site: A0A151S888_CAJCA 
ID   A0A151S888_CAJCA        Unreviewed;      1018 AA.
AC   A0A151S888;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Kinesin-4 {ECO:0000313|EMBL:KYP50978.1};
GN   ORFNames=KK1_027189 {ECO:0000313|EMBL:KYP50978.1};
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:KYP50978.1, ECO:0000313|Proteomes:UP000075243};
RN   [1] {ECO:0000313|EMBL:KYP50978.1, 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; KQ483445; KYP50978.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151S888; -.
DR   STRING; 3821.A0A151S888; -.
DR   Proteomes; UP000075243; 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   CDD; cd21203; CH_AtKIN14-like; 1.
DR   CDD; cd01366; KISc_C_terminal; 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:SF24; P-LOOP NUCLEOSIDE TRIPHOSPHATE HYDROLASE SUPERFAMILY PROTEIN; 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|PROSITE-ProRule:PRU00283};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
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:UP000075243}.
FT   DOMAIN          40..162
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          411..739
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          776..801
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          959..1018
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          746..773
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        776..797
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        959..997
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1004..1018
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         493..500
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1018 AA;  112533 MW;  7591FBAAF128E8DA CRC64;
     MAADAAFFFS VASVVEDVLQ QHGPRLKDLD LESRKAEEAA SRRYEAAGWL RKMVGVVAAK
     DLPAEPSEEE FRLGLRSGII LCNVINKVQS GAVPKVVESP VDSALIPDGA PLTAYQYFEN
     VRNFLVAVQE IGIPTFEASD LEQGGKSSRI VNCVLALKSY SEWKMSGSNG VWKFGGNLKP
     TVSAKSFVRK NSEPFTNSLS RTSSLNDKSL NALNSDIESN KMSGSHSLST LVRAILSDKK
     PEEVPTLVES VLNKVVEEFE QRIASQDEQT KITPRDPVSQ SNGSVIADAK GEKNIHVVAK
     KEDCIHKNQV SSMVTQNEDR IHKNQVADEE SQRQLLKQQM LFDQQQREIQ ELRHTLHTTK
     SGMQFMQMKF HEEFSNLGMH IHGLANAASG YHRVLEENRK LYNQVQDLKG SIRVYCRVRP
     FFPGQSNHLS AVESIDDGVI TVNVPSKNGK GRRSFNFNKV FGPSATQAEV FLDMQPLIRS
     VLDGYNVCIF AYGQTGSGKT HTMTGPKEIT EKSQGVNYRA LGDLFHIADQ RKDTFHYDVS
     VQMIEIYNEQ VRDLLVTDGT NKRYPFTKIR SSSQKGLSVP DASLVPVSST IDVIELMNLG
     QRNRAVGATA LNDRSSRSHS CLTVHVQGRD LTSGATLRGC MHLVDLAGSE RVDKSEATGD
     RLKEAQHINK SLSALGDVIA SLAQKNSHVP YRNSKLTQLL QDSLGGQAKT LMFVHVSPES
     DAIGETISTL KFAERVATVE LGAARVNKDS ADVKELKDQI ASLKAALARK EGESDYSLSS
     SSEKYRTKAS ELSPYPDSGN QLGYRRPMVE VGNIEEFERF IVQLESNTTV RKKTQSFDFD
     EISANSPPWP PVNNNNSLGQ NYAEDDKETG SGEWVDKVMV NKTENLLECW QASNGNLSEA
     FYQKYPKMHS EQSYNMFIGG NHFNIAGSDD TDDLDAATSD SSEPDLLWQF NHSKLSSIGP
     KTMRSISKTA KSPEFSKNGV HSSPLGPSPS FKQSNGVPHR TGRHPAPVDV KRRTGSRK
//
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