ID   KINL_LEICH              Reviewed;         955 AA.
AC   P46865;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Kinesin-like protein K39;
DE   Flags: Fragment;
GN   Name=KIN;
OS   Leishmania chagasi.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=44271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MHOM/BR/82/BA-2;
RX   PubMed=8421715; DOI=10.1073/pnas.90.2.775;
RA   Burns J.M. Jr., Shreffler W.G., Benson D.R., Ghalib H.W., Badaro R.,
RA   Reed S.G.;
RT   "Molecular characterization of a kinesin-related antigen of Leishmania
RT   chagasi that detects specific antibody in African and American visceral
RT   leishmaniasis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:775-779(1993).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Predominant in amastigotes.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR   EMBL; L07879; AAA29254.1; -; Genomic_DNA.
DR   PIR; A47334; A47334.
DR   AlphaFoldDB; P46865; -.
DR   SMR; P46865; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; -; 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; PTHR24115; 2.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW   Motor protein; Nucleotide-binding; Repeat.
FT   CHAIN           1..>955
FT                   /note="Kinesin-like protein K39"
FT                   /id="PRO_0000125455"
FT   DOMAIN          12..392
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REPEAT          704..742
FT                   /note="1"
FT   REPEAT          743..781
FT                   /note="2"
FT   REPEAT          782..820
FT                   /note="3"
FT   REPEAT          821..859
FT                   /note="4"
FT   REPEAT          860..898
FT                   /note="5"
FT   REPEAT          899..937
FT                   /note="6"
FT   REPEAT          938..>955
FT                   /note="7"
FT   REGION          682..712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          704..>955
FT                   /note="7 X 39 AA approximate tandem repeats"
FT   REGION          725..955
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          426..>955
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        685..704
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        733..751
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        772..795
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        796..810
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        811..834
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        835..849
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        850..873
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        874..888
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        889..912
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        928..955
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         122..129
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   NON_TER         955
SQ   SEQUENCE   955 AA;  106168 MW;  8CA76815BE84C6E9 CRC64;
     MHPSTVRREA ERVKVSVRVR PLNERENNAP EGTKVTVAAK QAAAVVTVKV LGGSNNSGAA
     ESMGTARRVA QDFQFDHVFW SVETPDACGA TPATQADVFR TIGYPLVQHA FDGFNSCLFA
     YGQTGSGKTY TMMGADVSAL SGEGNGVTPR ICLEIFARKA SVEAQGHSRW IVELGYVEVY
     NERVSDLLGK RKKGVKGGGE EVYVDVREHP SRGVFLEGQR LVEVGSLDDV VRLIEIGNGV
     RHTASTKMND RSSRSHAIIM LLLREERTMT TKSGETIRTA GKSSRMNLVD LAGSERVAQS
     QVEGQQFKEA THINLSLTTL GRVIDVLADM ATKGAKAQYS VAPFRDSKLT FILKDSLGGN
     SKTFMIATVS PSALNYEETL STLRYASRAR DIVNVAQVNE DPRARRIREL EEQMEDMRQA
     MAGGDPAYVS ELKKKLALLE SEAQKRAADL QALEREREHN QVQERLLRAT EAEKSELESR
     AAALQEEMTA TRRQADKMQA LNLRLKEEQA RKERELLKEM AKKDAALSKV RRRKDAEIAS
     EREKLESTVA QLEREQRERE VALDALQTHQ RKLQEALESS ERTAAERDQL LQQLTELQSE
     RTQLSQVVTD RERLTRDLQR IQYEYGETEL ARDVALCAAQ EMEARYHAAV FHLQTLLELA
     TEWEDALRER ALAERDEAAA AELDAAASTS QNARESACER LTSLEQQLRE SEERAAELAS
     QLEATAAAKS SAEQDRENTR ATLEQQLRES EARAAELASQ LEATAAAKMS AEQDRENTRA
     TLEQQLRDSE ERAAELASQL ESTTAAKMSA EQDRESTRAT LEQQLRDSEE RAAELASQLE
     STTAAKMSAE QDRESTRATL EQQLRESEER AAELASQLES TTAAKMSAEQ DRESTRATLE
     QQLRDSEERA AELASQLEAT AAAKSSAEQD RENTRAALEQ QLRDSEERAA ELASQ