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Database: UniProt
Entry: Q4QE80_LEIMA
LinkDB: Q4QE80_LEIMA
Original site: Q4QE80_LEIMA 
ID   Q4QE80_LEIMA            Unreviewed;      1430 AA.
AC   Q4QE80;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   SubName: Full=Putative kinesin {ECO:0000313|EMBL:CAJ03849.1};
DE            EC=3.6.4.4 {ECO:0000313|EMBL:CAJ03849.1};
GN   ORFNames=LMJF_17_1110 {ECO:0000313|EMBL:CAJ03849.1};
OS   Leishmania major.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5664 {ECO:0000313|EMBL:CAJ03849.1, ECO:0000313|Proteomes:UP000000542};
RN   [1] {ECO:0000313|EMBL:CAJ03849.1, 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   [2] {ECO:0000313|EMBL:CAJ03849.1, 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. Ungrouped subfamily.
CC       {ECO:0000256|ARBA:ARBA00010103}.
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DR   EMBL; FR796413; CAJ03849.1; -; Genomic_DNA.
DR   RefSeq; XP_001682368.1; XM_001682316.1.
DR   STRING; 5664.Q4QE80; -.
DR   EnsemblProtists; CAJ03849; CAJ03849; LMJF_17_1110.
DR   GeneID; 5650842; -.
DR   KEGG; lma:LMJF_17_1110; -.
DR   VEuPathDB; TriTrypDB:LmjF.17.1110; -.
DR   VEuPathDB; TriTrypDB:LMJFC_170019600; -.
DR   VEuPathDB; TriTrypDB:LMJLV39_170018400; -.
DR   VEuPathDB; TriTrypDB:LMJSD75_170018100; -.
DR   eggNOG; KOG0240; Eukaryota.
DR   HOGENOM; CLU_258537_0_0_1; -.
DR   InParanoid; Q4QE80; -.
DR   OMA; DWRCNPQ; -.
DR   Proteomes; UP000000542; Chromosome 17.
DR   GO; GO:0005930; C:axoneme; ISO:GeneDB.
DR   GO; GO:0097542; C:ciliary tip; ISO:GeneDB.
DR   GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   CDD; cd00106; KISc; 1.
DR   Gene3D; 2.60.120.380; -; 2.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR022682; Calpain_domain_III.
DR   InterPro; IPR022683; Calpain_III.
DR   InterPro; IPR036213; Calpain_III_sf.
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; KINESIN-RELATED; 1.
DR   PANTHER; PTHR24115:SF287; PUTATIVE-RELATED; 1.
DR   Pfam; PF01067; Calpain_III; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00185; ARM; 4.
DR   SMART; SM00720; calpain_III; 1.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF49758; Calpain large subunit, middle domain (domain III); 2.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:CAJ03849.1};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000542}.
FT   DOMAIN          8..345
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          401..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1177..1204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1243..1372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          359..386
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1245..1274
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1302..1319
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1352..1372
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         93..100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1430 AA;  158166 MW;  C77FB795823A69F3 CRC64;
     MSTAVVSRPR VYVRIRPLND REVRDGKGEL ACRGDTRQQD LLFLKKDETL EQQVRFDQVF
     DQRSNQQLVF DHIGPEILRT LFSGYNASVF AYGQTGSGKT YTMEGDKGGG VSGGASSEEQ
     EGLIPRIIRG IFSSFKSNAD ITDALVEVSL VQIYQERIQD LLNHRKQVEI HMDRTSQYVA
     RDATWRTVRS LEECMKLYGE ACKMRATSAT EMNLVSSRSH MILMLRMQWD EPALPGSHAQ
     LNMIDLAGSE RLSESGATGE SMKETITINK SLSALGNVVV KLVEQAKKPN KRIHIPYKDS
     KLTYLLQSSL GGANLVHFML AVSGSAMWRS ETTSTIEFGK RALQLVLRPV RNAIDYTRLA
     EMEAMIERMR SHIESLEEEL QLKRNFEAAG FLQLRQIAQS DDDPVQRRRR HETSTNHKHL
     KRQTELTRIM ANLPETFDDL TSHCVLFPES KVTFRELGGL EKLIYFVEKC ASNYYRASAA
     QTIASVIDEP GREVFASLGG LNALAVLLRV QEERCKEAAC VALEAVCRGC VTNKRSLSTD
     VYAELVDLVY GYSNQQVQEA ACAAVASIVD GYAEATRRFE RLDVVPKLLE TIRTCPAEVV
     NLTKAATNCV GRLAHGDKDM QQTIASLGGV DLLIDVLFSS SGDRDHQVPI LASYALVNLC
     CSSHENLKMA MEHSRYGEVK FRLLEGLARA FGTNASREGF GRATAQETAG PFPYYGVTIQ
     DEWTYASSGG RPIFSTFMDN PQFHLYVREE TDIAFIIQDT LYEARMRKKR RNNSVYMGIA
     IFEGEPTLAK LGLKQLDFHG KMIEIGHYTS NCENVLHCTL PASDTPYMVV PFTSQKGRRT
     HFALSAFGNH PIELTSVPDQ VGWVHTVLQG KWTEFTGRGG EAFDWRCNPQ IRLKTKEACR
     VVFVLSYLSL DEQRAQLLQE EEEREGQNTR PRLHGRLFSN AFAAHKRYLK AIVPLPQGST
     FVASNTFASN SYITTSANLD RSGDYAYIPF TEAPFQDTYR VSVYCDSDDV EIKPMQGQSS
     EWMCASLSGV WQGKPVSIDL DTIGKLVAVM YSPGAFVRPR LLSGSNQKRI AGIDSYWNTE
     ATVEYDSDGQ LTLQVEAMMR SGTPGAAAAR GNTQSATNQV TQVPATDIKF DLFIFTDRKC
     TLTRVGFDAS PSSWPCPTQS TSLALLAYPQ LVEDVDAIGG DDEDNSDSLA SELCRDDSDS
     ISAAAQEARE TELLRLLEKQ EAANHILKLQ LAQQARELEE LRNGGASATT LSNSDGKRGS
     SVKPSGTKTP KRTLSATMDG YAGFSEEGHR SRKEVGGDGS AQATLRNPSS GNTSGSAETK
     GAAAKPPSTG LGQRDTNTNG AGAWGQKPLP LAGTTLPTNR SGMADNTASA APSPQVKELV
     DYTLVKLIEM GKRAATSARL ADKKEDRKWR AMLKDIEEVH QRLHDAFSIL
//
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