ID E9ABZ2_LEIMA Unreviewed; 668 AA.
AC E9ABZ2;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=LMJF_01_0030 {ECO:0000313|EMBL:CBZ11806.1};
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664 {ECO:0000313|EMBL:CBZ11806.1, ECO:0000313|Proteomes:UP000000542};
RN [1] {ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX PubMed=10077609; DOI=10.1073/pnas.96.6.2902;
RA Myler P.J., Audleman L., deVos T., Hixson G., Kiser P., Lemley C.,
RA Magness C., Rickel E., Sisk E., Sunkin S., Swartzell S., Westlake T.,
RA Bastien P., Fu G., Ivens A., Stuart K.;
RT "Leishmania major Friedlin chromosome 1 has an unusual distribution of
RT protein-coding genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:2902-2906(1999).
RN [2] {ECO:0000313|EMBL:CBZ11806.1, ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX PubMed=16020728; DOI=10.1126/science.1112680;
RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M.,
RA De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S.,
RA Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K.,
RA Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA Barrell B., Myler P.J.;
RT "The genome of the kinetoplastid parasite, Leishmania major.";
RL Science 309:436-442(2005).
RN [3] {ECO:0000313|EMBL:CBZ11806.1, ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FR796397; CBZ11806.1; -; Genomic_DNA.
DR RefSeq; XP_003721523.1; XM_003721475.1.
DR AlphaFoldDB; E9ABZ2; -.
DR SMR; E9ABZ2; -.
DR STRING; 5664.E9ABZ2; -.
DR EnsemblProtists; CBZ11806; CBZ11806; LMJF_01_0030.
DR GeneID; 12983096; -.
DR KEGG; lma:LMJF_01_0030; -.
DR VEuPathDB; TriTrypDB:LmjF.01.0030; -.
DR VEuPathDB; TriTrypDB:LMJFC_010005300; -.
DR VEuPathDB; TriTrypDB:LMJLV39_010005200; -.
DR VEuPathDB; TriTrypDB:LMJSD75_010005300; -.
DR eggNOG; KOG0246; Eukaryota.
DR HOGENOM; CLU_001485_19_2_1; -.
DR InParanoid; E9ABZ2; -.
DR OMA; GRRRLYT; -.
DR Proteomes; UP000000542; Chromosome 1.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:GeneDB.
DR GO; GO:0005819; C:spindle; IDA:GeneDB.
DR GO; GO:0000922; C:spindle pole; IDA:GeneDB.
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; IBA:GO_Central.
DR GO; GO:0007019; P:microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0007052; P:mitotic spindle organization; ISO:GeneDB.
DR GO; GO:0051983; P:regulation of chromosome segregation; ISO:GeneDB.
DR CDD; cd01367; KISc_KIF2_like; 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; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47971:SF25; KINESIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR47971; KINESIN-RELATED PROTEIN 6; 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};
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:UP000000542}.
FT DOMAIN 134..453
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 75..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 224..231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 668 AA; 74433 MW; 4D52B98DB7A9C9C3 CRC64;
MMSAEPPSSQ PYISDVLRRY QLERFQCAFA SSMTIKDLLA LQPEDFNRYG VVEAMDILRL
RDAIEYIKAN PLPASRSGSD VLDNDGDGDG EGDDSTPEGK EGCSTERRRQ YTARGTTVLC
RSTDTAEEVK RKSRILVAIR KRPLSAGEQT NGFTDIMDAD NSGEIVLKEP KVKVDLRKYT
HVHRFFFDEV FDEACDNVDV YNRAARALID TVFDGGCATC FAYGQTGSGK THTMLGKGPE
PGLYALAAKD MFDRLTSDTR IVVSFYEIYS GKLFDLLNGR RPLRALEDDK GRVNIRGLTE
HCSTSVEDLM TIIDQGSGVR SCGSTGANDT SSRSHAILEI KLKAKRTSKQ SGKFTFIDLA
GSERGADTVD CARQTRLEGA EINKSLLALK ECIRFLDQNR KHVPFRGSKL TEVLRDSFIG
NCRTVMIGAV SPSNNNAEHT LNTLRYADRV KELKRNATER RTVCMPDDQE EAFFDTTESR
PPSRRTTTRL STAAPLFSGS STAAPALRST LLSSRSVNTL SPSSQAKSTL VTPKPPSRDR
TPDMVCTKRP RDSDRSGEDE VVARPSGRPS FKRFESGAEL VAAQRSRVID QYNAYLETDM
NCIKEEYQVK YDAEQMNANT RSFVERARLL VSEKRRAMES FLTQLEELDK IAQQVADITA
FQQHLPPT
//
