ID A0A151R9H7_CAJCA Unreviewed; 961 AA.
AC A0A151R9H7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=KK1_039547 {ECO:0000313|EMBL:KYP39149.1};
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:KYP39149.1, ECO:0000313|Proteomes:UP000075243};
RN [1] {ECO:0000313|EMBL:KYP39149.1, 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-7 subfamily.
CC {ECO:0000256|ARBA:ARBA00007310}.
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DR EMBL; KQ483933; KYP39149.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151R9H7; -.
DR STRING; 3821.A0A151R9H7; -.
DR OMA; HTIVYKP; -.
DR OrthoDB; 5476186at2759; -.
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; cd01374; KISc_CENP_E; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
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; IPR021881; NACK_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47968; CENTROMERE PROTEIN E; 1.
DR PANTHER; PTHR47968:SF23; KINESIN-LIKE PROTEIN KIN-7A; 1.
DR Pfam; PF11995; DUF3490; 1.
DR Pfam; PF00225; Kinesin; 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; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394}; Coiled coil {ECO:0000256|SAM:Coils};
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 30..352
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 388..429
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 488..537
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 567..594
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 116..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 961 AA; 108847 MW; EB7204AC6838C2BB CRC64;
MTMKTPGTPA SKIDRTPVST PGGARAREEK IVVTVRLRPL NRREQLAKDQ VAWDCINDYT
IVYKPPTHDR ASQPASFTFD KVFGPASLTE AVYEEGVKKV ALSALTGINA TVFAYGQTSS
GKTYTMRGIT EKAVNDIYEH IMNTPERDFT IRISGLEIYN ENVRDLLNSE SGRSLKLLDD
PEKGTVVEKL VEETAKDDQH LRHLISICEA QRQVGETALN DNSSRSHQII RLTIQSTLRE
NADCVKSFVA TLNFVDLAGS ERAAQTHADG TRLKEGCHIN LSLMTLTTVI RKLSVGKRSG
HIPYRDSKLT RILQHSLGGN ARTAIVCTLS PALSHVEQSR NTLLFATRAK EVTNNAQVNV
VVSDKQLVKH LQKEVARLEA VLRTPDPSKE KDWKIQQMEM EIEELKRQRD LAQIQVDELR
RKLQDDQKVS NPVESPHLPV KKCLSFTGAL SSLKPELGCE RVRSSTLRQS IRQSSTAPFT
LMHEIRKLEH LQEQLGEEAN RALEVLQKEV ACHRLGNQDA AETIAKLQAE IREMRSVRST
PKDVEVGSMV SVNKSVSANL KDEITRLHSQ GSTIANLEQQ LENVQRSIDK LVMSLPNNFQ
HSPSEASPKN KKEHKRKKLL PLSSSNITNR PNFLRSPCSP LSTTQQVLES DIENIAPEND
DLVSIDTLPE SEKETPSKSE ETGDVSSKEN PSGYRRSSSV NMKKMQKMFQ NAAEENVRSI
RAYVTELKER VAKLQYQKQL LVCQVLELEA NEANGHNIDN EEYPCEPEEP QVSWQITFKE
QRQQILELWD LCYVSIIHRT QFYLLFKGDP ADQIYMEVEL RRLTWLQEHL AELGNASPAP
HVGEEPAISL SSSLRALKRE REFLAKRLTS RLSLEEREML YMKWDVPLDG KQRRLQFISK
LWTDPHDQNH VQESAEIVAK LVGFQTGGNM SKEMFELNFV LPSDKRPWLM GWNPISNFLN
L
//
