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KIF6_DICDI
ID   KIF6_DICDI              Reviewed;        1030 AA.
AC   Q6S004; Q55F66; Q94499;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Kinesin-related protein 6;
DE   AltName: Full=Kinesin family member 6;
DE   AltName: Full=Kinesin-13;
GN   Name=kif6; Synonyms=K6, ksnF; ORFNames=DDB_G0267404;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, AND NOMENCLATURE.
RC   STRAIN=AX4;
RX   PubMed=14641909; DOI=10.1186/1471-2164-4-47;
RA   Kollmar M., Gloeckner G.;
RT   "Identification and phylogenetic analysis of Dictyostelium discoideum
RT   kinesin proteins.";
RL   BMC Genomics 4:47-47(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 440-758, AND INDUCTION.
RC   STRAIN=AX3;
RX   PubMed=9693369; DOI=10.1091/mbc.9.8.2093;
RA   de Hostos E.L., McCaffrey G., Sucgang R., Pierce D.W., Vale R.D.;
RT   "A developmentally regulated kinesin-related motor protein from
RT   Dictyostelium discoideum.";
RL   Mol. Biol. Cell 9:2093-2106(1998).
CC   -!- FUNCTION: Microtubule-associated force-producing protein that plays a
CC       role in organelle transport. Its motor activity is directed toward the
CC       microtubule's plus end (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC   -!- INDUCTION: During the developmental stage.
CC       {ECO:0000269|PubMed:9693369}.
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; AY484461; AAR39437.1; -; Genomic_DNA.
DR   EMBL; AAFI02000003; EAL73154.1; -; Genomic_DNA.
DR   EMBL; U69984; AAB09082.1; -; mRNA.
DR   RefSeq; XP_647667.1; XM_642575.1.
DR   AlphaFoldDB; Q6S004; -.
DR   SMR; Q6S004; -.
DR   STRING; 44689.DDB0191499; -.
DR   PaxDb; Q6S004; -.
DR   PRIDE; Q6S004; -.
DR   EnsemblProtists; EAL73154; EAL73154; DDB_G0267404.
DR   GeneID; 8616484; -.
DR   KEGG; ddi:DDB_G0267404; -.
DR   dictyBase; DDB_G0267404; kif6.
DR   eggNOG; KOG0246; Eukaryota.
DR   HOGENOM; CLU_001485_19_2_1; -.
DR   InParanoid; Q6S004; -.
DR   OMA; CRENELQ; -.
DR   PRO; PR:Q6S004; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0005813; C:centrosome; TAS:dictyBase.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
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; 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; IMP:dictyBase.
DR   Gene3D; 1.10.150.50; -; 1.
DR   Gene3D; 3.40.850.10; -; 1.
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   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF47769; SSF47769; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Microtubule; Motor protein;
KW   Nucleotide-binding; Reference proteome; Transport.
FT   CHAIN           1..1030
FT                   /note="Kinesin-related protein 6"
FT                   /id="PRO_0000365581"
FT   DOMAIN          3..66
FT                   /note="SAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   DOMAIN          453..775
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          66..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          178..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          826..915
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          981..1030
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..237
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..285
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        826..902
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         543..550
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1030 AA;  118658 MW;  D2A9B57AE3BF16A8 CRC64;
     MDFENDQLYN WLQLANLESF YPNFIKKNVS CDSFLSFTMQ DYGNVGITSL QDRKKLFHLL
     QQLKKQTPPI SNTSSPVINS NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNSSG
     LRQPTSTSSL LSNNNLMSTQ TQQSSSSSSS SSLSSKSNSN SDFMQKAQQL LKQRELERQQ
     YAKQQQQQQS TQTKYQSSLK DFDITSSNKN NNLDDFFEDD NLYSQQQQQQ QQQQQQQDFE
     FEEEEEEEDQ QQQYDEEEEE EEEYEEDFYK EDLGEIDDGN VLDISDDEPD PNSSCIIVEG
     SPDEEDDDVE YIPQNESLVN GFGSMKIQQQ QQQQFQPLQQ QQQQQQQQQQ QFYQQQIQQQ
     QQQQQQQQQQ QVQQQQQQFN NFNYSGLNEE QIKYYQQQAQ YQQQVQQAQQ AAIQQAQQAA
     ALAQASQQQL QQQEQQRQQA SNFFLDMNEY GQRIRVCVRK RPLNKKEIAK SEKDIIEVLP
     KKDLIVNEPK TKLDLSKFIE KHKFTFDGVF DESANNYQVY LHTAYPLVDS IFHKGKATCF
     AYGQTGSGKT HTQMGQQGDG LYALAARDIF HRLETYFKDQ LQVCISFFEI YGGKLFDLLN
     ERKKLACREN ELQNVVIVGL SEKHVTSPQE LMNCIIDGNK IRSTGSTGVN SDSSRSHAIL
     QISLKNIKTN KLHGKFSFID LAGSERGSDT YDNDKQTRKE GADINKSLLA LKECIRALDQ
     SSKHTPFRQS TLTQVLKDSF VGNSRTVMIA NISPNQSSSE HTLNTLRYAD RVKELGTSES
     NSNKKPVATY NIPAPLPPPD HLKQNFNDPI LIPSTTTTTT TTATAINSQQ PIIQQTSQPV
     SKIKQPVKQQ QESQIPQTPQ QQQQQQPPQQ QPQQQQYNIP QTPQQTQQQF NIPQTPKQQQ
     PIQTQPPMSP PKIDFVNYHR NHVDQFADIL KKELISINQF ESSKGSIPLE NYINNIEQFL
     DSKQLLINHL RGIIQQHQQQ PIQQQQQQQQ PIQQQQQSTP QPSQLQTPQQ RERARSQLQP
     PKPSIYSSRN
 
 
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