(data stored in ACNUC8465 zone)

SWISSPROT: C1E175_MICCC

ID   C1E175_MICCC            Unreviewed;      1309 AA.
AC   C1E175;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 49.
DE   SubName: Full=Kinesin-like protein {ECO:0000313|EMBL:ACO61689.1};
GN   ORFNames=MICPUN_56771 {ECO:0000313|EMBL:ACO61689.1};
OS   Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS   green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; prasinophytes; Mamiellophyceae;
OC   Mamiellales; Mamiellaceae; Micromonas.
OX   NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO61689.1, ECO:0000313|Proteomes:UP000002009};
RN   [1] {ECO:0000313|EMBL:ACO61689.1, ECO:0000313|Proteomes:UP000002009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009};
RX   PubMed=19359590; DOI=10.1126/science.1167222;
RA   Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA   Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA   Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA   Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA   Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W.,
RA   Gready J.E., John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F.,
RA   Moreau H., Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I.,
RA   Piegu B., Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T.,
RA   Zelensky A., Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W.,
RA   Van de Peer Y., Grigoriev I.V.;
RT   "Green evolution and dynamic adaptations revealed by genomes of the
RT   marine picoeukaryotes Micromonas.";
RL   Science 324:268-272(2009).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00283}.
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DR   EMBL; CP001324; ACO61689.1; -; Genomic_DNA.
DR   RefSeq; XP_002500431.1; XM_002500385.1.
DR   GeneID; 8241622; -.
DR   KEGG; mis:MICPUN_56771; -.
DR   InParanoid; C1E175; -.
DR   Proteomes; UP000002009; Chromosome 3.
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   Gene3D; 3.40.850.10; -; 1.
DR   InterPro; IPR029329; DUF4472.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF14739; DUF4472; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1E175.
DR   SWISS-2DPAGE; C1E175.
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|SAAS:SAAS00784251}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002009};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|SAAS:SAAS00785115};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002009}.
FT   DOMAIN       17    376       Kinesin motor. {ECO:0000259|PROSITE:
FT                                PS50067}.
FT   NP_BIND      98    105       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00283}.
FT   COILED      429    463       {ECO:0000256|SAM:Coils}.
FT   COILED      492    523       {ECO:0000256|SAM:Coils}.
FT   COILED      538    632       {ECO:0000256|SAM:Coils}.
FT   COILED      637    668       {ECO:0000256|SAM:Coils}.
FT   COILED      844    875       {ECO:0000256|SAM:Coils}.
FT   COILED      985   1019       {ECO:0000256|SAM:Coils}.
FT   COILED     1096   1142       {ECO:0000256|SAM:Coils}.
FT   COILED     1146   1177       {ECO:0000256|SAM:Coils}.
FT   COILED     1194   1221       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1309 AA;  144223 MW;  903EFFFF974CF1BE CRC64;
     MPTRGAGARK VRPEGQNMRT VVQLLTAGNK NLRRDVSVAS RHVSLIRPGY TEAQTDDTYE
     VDDCFGSDLG NTEAYKRVLH PAVKQVIDGF NSSCITIGCS GSGKTTLLHG RTSGDGIVRL
     AIKALFEGLH NKAAQVGLLL SQHKAQGGGG QSMEFAVDAS FCEVYEEKVR DLFAAARDAE
     AAGGKDSVKT EYLEVEETAD DGWHVAGLSH RSAPDAASLQ TAYAGALNHR VTGLSEYGHS
     KHDRAASVLT LKVSQYIPGL PNATGEIAPA QHIVSTIVIA DNPGAEPLAM DPAVLRLREG
     ARLNKAITAL AGVVRALATQ RREFAGHGDS VLTKILSEPL GGNCATTILG TLKLGEWERS
     SAVMDLVGHA RRAPCFPVVQ DDAARGLQQR LRSRLLQIND ARETYRDQIQ STGADGIDPN
     NIGLQMAKLH ELEGQLLNER GDKAELLAEK EALIERLQRL NGMDKANLAE KEELQKALIA
     SEEDRLEIAR ALVEAQLEAN EAALQAEKTR HELVERVHEL EARAIASEVR VKGAEQSYGE
     LQNKAGSLNV ENQRIKEELD QTRQELEKEL KEIRTEHAEV SGEVSSLKAA NEDLSAELED
     FRRKINVERR RAEDAESERD EFRANQEMYQ SNMQKKVEAA ERMAEEAVKV AEETKNRLVQ
     AAKAERDEAV AAARASKDKA VQAAQEERDE EVAKARSARD RAIDEMRMEK EKAVFEARKE
     KDEAVALANA EKAERTAYLE NDRDTRVAKA EKDKDEAIAK ALRERDEAVT EAKRRSSEAI
     AAAQEDKDAA IAEAHRLRDL AQERLKFETE RLGSIANEAN GSIQGVTRAM EEARSAERMA
     RREADRAVGE MTQLREKLEN VRAEFSQRLK EYMLQVGDLE RGAQVLATDP NADHVLRPSQ
     LYEAAQTLAL DLHRASADQV TEYRRVTEDL QQRLTRAQRD VRALHAGYRT LRHRFEDVAP
     ETVDEKGKAA VPHEDDLVGT PPTPAEAREM DARGLAQKLA DLRDENAALQ KELRMAALDG
     RGPLAPHNVR AAKEAAARGG GSRPGTGEDG EIAYYNDGNK QDRDGGFGQV GKGEIVVKKN
     APDDSFGGAM AGAGENARLR AENARLQKTI DELKHRRPST TEEDMRAEVS KLRIQLHALS
     NQDNTRAKLT QEISVLKIQL QERTQELKEH KNHSQREAFK QQKAAIKEFT DRVQSELEKE
     NRALQTRAAM AEEQIKEINA YMAQSTLAYQ KEIMRLRTII QATAPERLRS PVNPGLMGSK
     TQDRSGAGGA QPHQREGRGD KGGGVRASGG WDRSTKPSEP LRPRSNNGA
//

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