ID A4H4I4_LEIBR Unreviewed; 661 AA.
AC A4H4I4;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 2.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=LBRM_06_0160 {ECO:0000313|EMBL:CAM36974.2};
OS Leishmania braziliensis.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC Leishmania braziliensis species complex.
OX NCBI_TaxID=5660 {ECO:0000313|EMBL:CAM36974.2, ECO:0000313|Proteomes:UP000007258};
RN [1] {ECO:0000313|EMBL:CAM36974.2, ECO:0000313|Proteomes:UP000007258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM36974.2,
RC ECO:0000313|Proteomes:UP000007258};
RX PubMed=17572675; DOI=10.1038/ng2053;
RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA Mottram J.C., Smith D.F., Berriman M.;
RT "Comparative genomic analysis of three Leishmania species that cause
RT diverse human disease.";
RL Nat. Genet. 39:839-847(2007).
RN [2] {ECO:0000313|EMBL:CAM36974.2, ECO:0000313|Proteomes:UP000007258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM36974.2,
RC ECO:0000313|Proteomes:UP000007258};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283,
CC ECO:0000256|RuleBase:RU000394}.
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DR EMBL; FR798980; CAM36974.2; -; Genomic_DNA.
DR RefSeq; XP_001561953.2; XM_001561903.2.
DR AlphaFoldDB; A4H4I4; -.
DR STRING; 5660.A4H4I4; -.
DR GeneID; 4961243; -.
DR KEGG; lbz:LBRM_06_0160; -.
DR VEuPathDB; TriTrypDB:LbrM.06.0160; -.
DR VEuPathDB; TriTrypDB:LBRM2903_060007000; -.
DR InParanoid; A4H4I4; -.
DR Proteomes; UP000007258; Chromosome 6.
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; 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; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24115:SF1024; KINESIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR24115; KINESIN-RELATED; 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|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Reference proteome {ECO:0000313|Proteomes:UP000007258}.
FT DOMAIN 5..486
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 20..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 494..521
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 608..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 158..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 661 AA; 70260 MW; 6550FA50DF02840D CRC64;
MPTTHVKAAV RVRPLVEMEM APTPSASSPP PPPGDSHSHD TGGTKLSYSE VIRVVTAAGR
LTRPMTSPYM LEVLRPPTVR IGCGRSVQRH SMPTRQSRLH NPGNGGGGEG RCEVATVYTF
DYCAGPSTTQ EEFFDMLEMP ALCEAALAGE VVTVLCFGQT GSGKTYSLSG RTLPAPASAG
PVSDVPTPLV AEDGLQYQAV YYIARRLKEL RRSSRKLKSR RQGSDGASVG ASASSATVVT
SKCSYVELYQ ESLYDLLQPD GGDGLQCRWS AAASSFFVEG SLMVECRGRE DFLLVLREGQ
RNRQRGSHAL NLDSSRSHVV FTVFFEARDE AAAATSAGDI GSDGAPSSPL GASAPLCTTR
YGRLVFVDLA GSERLKKTLS TSTAETKSIN KSLFTLGRVL ELLSAPPPAP STKVLTSASS
DAVTPSKALA PPPPFIPYRS SVLTQLLMHS LDGHGRTVMV ACVSPSALHL EESLRTLHYA
ERVRHIRAVP VVHVDTATQE RMALEEKVQA LRKENALLRR ALGLTGVGSL EAGQVEARLE
ELHRAWAAGQ LAALPYEAPS QGAAAPSWPS SAPQQGQVVR ACPSRPAVPF ATSGTIVAAV
PTDLRASTPQ TVVMSSTESE ANDESPSGTD DVVPSSHNPH AAAVNILDLL ESLPDTRLMY
T
//
