ID   A0A0C5I3T6_YEASX        Unreviewed;      1111 AA.
AC   A0A0C5I3T6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   22-JUL-2015, entry version 3.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   Name=KIP1 {ECO:0000313|EMBL:AJP37027.1};
GN   ORFNames=F842_YJM1078B00044 {ECO:0000313|EMBL:AJP37027.1};
OS   Saccharomyces cerevisiae YJM1078.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=1296266 {ECO:0000313|EMBL:AJP37027.1};
RN   [1] {ECO:0000313|EMBL:AJP37027.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YJM1078 {ECO:0000313|EMBL:AJP37027.1};
RX   PubMed=25840857; DOI=10.1101/gr.185538.114;
RA   Strope P.K., Skelly D.A., Kozmin S.G., Mahadevan G., Stone E.A.,
RA   Magwene P.M., Dietrich F.S., McCusker J.H.;
RT   "The 100-genomes strains, an S. cerevisiae resource that illuminates
RT   its natural phenotypic and genotypic variation and emergence as an
RT   opportunistic pathogen.";
RL   Genome Res. 25:762-774(2015).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|RuleBase:RU000394}.
CC   -!- SIMILARITY: Contains 1 kinesin motor domain.
CC       {ECO:0000256|RuleBase:RU000394}.
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DR   EMBL; CP004100; AJP37027.1; -; Genomic_DNA.
DR   ProteinModelPortal; A0A0C5I3T6; -.
DR   GO; GO:0005871; C:kinesin complex; IEA:InterPro.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR24115; PTHR24115; 1.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU000394,
KW   ECO:0000256|SAAS:SAAS00175645};
KW   Microtubule {ECO:0000256|RuleBase:RU000394};
KW   Motor protein {ECO:0000256|RuleBase:RU000394};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000394,
KW   ECO:0000256|SAAS:SAAS00175674}.
SQ   SEQUENCE   1111 AA;  125795 MW;  212F8279766137FC CRC64;
     MARSSLPNRR TAQFEANKRR TIAHAPSPSL SNGMHTLTPP TCNNGAATSD SNIHVYVRCR
     SRNKREIEEK SSVVISTLGP QGKEIILSNG SHQSYSSSKK TYQFDQVFGA ESDQETVFNA
     TAKNYIKEML HGYNCTIFAY GQTGTGKTYT MSGDINILGD VQSTDNLLLG EHAGIIPRVL
     VDLFKELSSL NKEYSVKISF LELYNENLKD LLSDSEDDDP AVNDPKRQIR IFDNNNNNSS
     IMVKGMQEIF INSAHEGLNL LMQGSLKRKV AATKCNDLSS RSHTVFTITT NIVEQDSKDH
     GQNKNFVKIG KLNLVDLAGS ENINRSGAEN KRAQEAGLIN KSLLTLGRVI NALVDHSNHI
     PYRESKLTRL LQDSLGGMTK TCIIATISPA KISMEETAST LEYATRAKSI KNTPQVNQSL
     SKDTCLKDYI QEIEKLRNDL KNSRNKQGIF ITQDQLDLYE SNSILIDEQN LKIHNLREQI
     KKFKENYLNQ LDINNLLQSE KEKLIAIIQN FNVDFSNFYS EIQKIHHTNL ELMNEVIQQR
     DFSLENSQKQ YNTNQNMQLK ISQQVLQTLN TLQGSLNNYN SKCSEVIKGV TEELTRNVNT
     HKAKHDSTLK SLLNITTNLL MNQMNELVRS ISTSLEIFQS DSTSHYRKDL NEIYQSHQQF
     LKNLQNDIKS CLDSIGSSIL TSINEISQNC TTNLNSMNVL IENQQSGSSK LIKEQDLEIK
     KLKNDLINER RISNQFNQQL AEMKRYFQDH VSRTRSEFHD ELNKCIDNLK DKQSKLDQDI
     WQKTASIFNE TDIVVNKIHS DSIASLAHNA ENTLKTVSQN NESFTNDLIS LSRGMNMDIS
     SKLRSLPINE FLNKISQTIC ETCGDDNTIA SNPVLTSIKK FQNIICSDIA LTNEKIMSLI
     DEIQSQIETI SNENNINLIA INENFNSLCN FILTDYDENI MQISKTQDEV LSEHCEKLQS
     LKILGMDIFT AHSIEKPLHE HTRPEASVIK ALPLLDYPKQ FQIYRDAENK SKDDTSNSRT
     CIPNLSTNEN FPLSQFSPKT PVPVPDQPLP KVLIPKSINS AKSNRSKTLP NTEGTGRESQ
     NNLKRRFTTE PILKGEETEN NDILQNKKLH Q
//