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Database: UniProt
Entry: F9WNJ4_TRYVY
LinkDB: F9WNJ4_TRYVY
Original site: F9WNJ4_TRYVY 
ID   F9WNJ4_TRYVY            Unreviewed;       664 AA.
AC   F9WNJ4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   03-MAY-2023, entry version 57.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=TvY486_0018200 {ECO:0000313|EMBL:CCD19112.1};
OS   Trypanosoma vivax (strain Y486).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Duttonella.
OX   NCBI_TaxID=1055687 {ECO:0000313|EMBL:CCD19112.1, ECO:0000313|Proteomes:UP000009027};
RN   [1] {ECO:0000313|EMBL:CCD19112.1, ECO:0000313|Proteomes:UP000009027}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Y486 {ECO:0000313|EMBL:CCD19112.1,
RC   ECO:0000313|Proteomes:UP000009027};
RX   PubMed=22331916; DOI=10.1073/pnas.1117313109;
RA   Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
RA   Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., Gamble J.,
RA   Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A.,
RA   Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D.,
RA   Hertz-Fowler C., Berriman M.;
RT   "Antigenic diversity is generated by distinct evolutionary mechanisms in
RT   African trypanosome species.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
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; CAEX01002639; CCD19112.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9WNJ4; -.
DR   VEuPathDB; TriTrypDB:TvY486_0018200; -.
DR   OMA; CAIMRTR; -.
DR   OrthoDB; 152933at2759; -.
DR   Proteomes; UP000009027; Unassembled WGS sequence.
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   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:SF16; 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:UP000009027}.
FT   DOMAIN          127..443
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          488..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         214..221
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   664 AA;  72708 MW;  A65A5AF545D6944C CRC64;
     MPIIPNIASQ QQHVQSNENL PHAPPLAKQP LPHIPNMLSG RSVASPVLAK VHSPTHQVDE
     FPSVSPRPLK IPRAASPDTK YAGVAAGTCS PKISDGHSFS CLAAEEVNAQ CEPKTGPPLT
     GRTRGGRIKV VIRKRPLPPD DNSGSDCVSI DPPCVHIAMR KQRVDLTEYA DINDFTFDDA
     FAEDKCNEYL FNSCCKELLD TTLQGGSASC FAYGQTGSGK THTMLGNSEE RGLYVLAAAS
     IFSSLEENQE VYASLYEIYC NSLFDLLNNR TPVVVREDHK RRMHISGLTW HAVSSAELLQ
     QLINNGADRR STGSTTANER SSRSHAVLTI QVRHQDDPKF CGTLNMVDLA GSERAADTAT
     TDRQTRQEGA EINKSLLALK ECIRALDEKK KHVPFRGSKL TEILRDSFIG NSRTVMIANI
     SASSQNYEHT LNTLRYAFRV KGLSVATFEP SRARNAPRPA RPVAADVPQL QLPVAFAAAA
     CPGNVGGAVG ARNTPARKRT VSAPAPAGPN RQQGAGAAGQ NKRQGIFSNA VQNPNPKASD
     SCGDCFRALT REKILSFVPN IKIPDRDEEP VSSHRDALEG DVQANPFTQQ QLRDLEDRVM
     AQLRTDMEYN VKQTLLRRDR TLQRLRRENA ALHITVAALE KRAAECPYCR GKQCNRANDN
     VEMQ
//
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