ID A4HGN8_LEIBR Unreviewed; 966 AA.
AC A4HGN8;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 2.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=LBRM_28_2020 {ECO:0000313|EMBL:CAM39732.2};
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:CAM39732.2, ECO:0000313|Proteomes:UP000007258};
RN [1] {ECO:0000313|EMBL:CAM39732.2, ECO:0000313|Proteomes:UP000007258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM39732.2,
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:CAM39732.2, ECO:0000313|Proteomes:UP000007258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM39732.2,
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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; FR799003; CAM39732.2; -; Genomic_DNA.
DR RefSeq; XP_001566232.2; XM_001566182.2.
DR AlphaFoldDB; A4HGN8; -.
DR STRING; 5660.A4HGN8; -.
DR GeneID; 5417108; -.
DR KEGG; lbz:LBRM_28_2020; -.
DR VEuPathDB; TriTrypDB:LbrM.28.2020; -.
DR VEuPathDB; TriTrypDB:LBRM2903_280026500; -.
DR InParanoid; A4HGN8; -.
DR Proteomes; UP000007258; Chromosome 28.
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; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR PANTHER; PTHR47972:SF28; PROTEIN CLARET SEGREGATIONAL; 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; 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|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000007258}.
FT DOMAIN 628..954
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 314..388
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 21..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 689..696
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 966 AA; 104087 MW; 4CFE2B994ABF316C CRC64;
MLPNRKRERG AAGEPESAAP SSTAVKRTPM TSKASSHASP SLHGPLRPRM VNLASDRSSE
KEALALRPPV ATQGAPRDVT AVQAVRRPHH TNSTTTRSVA DSSQGGITNA SPRSRDSAAS
ASSTAARAPL RRGRPQQPLR PPLSRSAMPS TPRRAMLPSG RGRGATGLRS HVDHAITGAT
SLSTAGAKSG NAASPSDPPP TESERQLWAT WREKRERLER EVQSLAQYSH KLTEETQAVQ
DAIEGMLTEF EDEKKRVEEH HNATVARYQG FMSALRVREE ACLSARQRAL DRICTSRETV
SQLQREQAAT QGAIISATDE RDGLEQQLAS ANDAAAERTI SLQQLQQEED RMRDATYGLS
GEVKELVLEM ERLRKEKHRM DVESMETEVA RRELYSLCEE LKGSIRVYCR VKGAALPVEP
QLPRDDTLCD EASEPQAIGL SKPEDIGTHL SESAEATAVA SVEMPPLCRP LSRSGSLESS
LSAAVLAVSS IPTTNTEAMV MTTDARHNTP GGGLRSGNST TRSSVATASI MGDGEADAAA
DEGAAPVFSF PDQGEGDPLS DANRKAGQGG LPQVRGAAPT GTTGSTTTTL AHAVTPLLCT
STAQGGEEEG GHFLTAAAVV GLPYGCGRCI TIHQTRSNAT STGLSSFTET FTYDKVFTGE
AQQAEVYCDV EPLVRNAVDG YRVCIFAYGQ TGSGKTFTME GDVRGRPELY GVTPRALQTV
LQRQAELANE GWSYELSCTF IEIYNDVIRD LFQSGSTRYE AAVQQQQQQA AMTASTTSSA
VYHTIKHSGD RTYITNVVER NIRSMGEFLQ LYKHAVLQRS TAKTGLNNAS SRSHCIFTLH
ISGTNGTIRQ RSDGVLCLVD LAGSERVNDS GVQGKQFKEA VNINRSLLDL GKCIRALRCG
AVVPWRNCKL TYLLQNYLGA KGGKMLMIVT VSHARAHALE SLNSLRFAAQ VQETYVGTSV
KRVTSI
//
