ID   ARK1_SCHPO              Reviewed;         355 AA.
AC   O59790;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   16-JUN-2009, entry version 73.
DE   RecName: Full=Serine/threonine-protein kinase ark1;
DE            EC=2.7.11.1;
DE   AltName: Full=Aurora-related kinase 1;
GN   Name=ark1; Synonyms=sex1; ORFNames=SPCC320.13c, SPCC330.16;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SEQUENCE REVISION TO N-TERMINUS.
RA   Gwilliam R., Barrell B.G., Rajandream M.A., Wedler H., Wambutt R.;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION.
RX   MEDLINE=21652847; PubMed=11792803;
RA   Petersen J., Paris J., Willer M., Philippe M., Hagan I.M.;
RT   "The S. pombe aurora-related kinase Ark1 associates with mitotic
RT   structures in a stage dependent manner and is required for chromosome
RT   segregation.";
RL   J. Cell Sci. 114:4371-4384(2001).
RN   [4]
RP   FUNCTION, INTERACTION WITH PIC1, AND MUTAGENESIS OF LYS-147.
RX   PubMed=11950927; DOI=10.1091/mbc.01-07-0330;
RA   Leverson J.D., Huang H.-K., Forsburg S.L., Hunter T.;
RT   "The Schizosaccharomyces pombe aurora-related kinase Ark1 interacts
RT   with the inner centromere protein Pic1 and mediates chromosome
RT   segregation and cytokinesis.";
RL   Mol. Biol. Cell 13:1132-1143(2002).
RN   [5]
RP   FUNCTION, INTERACTION WITH BIR1 AND MAD3, AND IDENTIFICATION OF THE
RP   TRANSLATION INITIATION CODON.
RX   MEDLINE=22563075; PubMed=12676091; DOI=10.1016/S0960-9822(03)00205-7;
RA   Petersen J., Hagan I.M.;
RT   "S. pombe aurora kinase/survivin is required for chromosome
RT   condensation and the spindle checkpoint attachment response.";
RL   Curr. Biol. 13:590-597(2003).
RN   [6]
RP   INTERACTION WITH PIC1.
RX   PubMed=16199877; DOI=10.1128/MCB.25.20.9000-9015.2005;
RA   Huang H.-K., Bailis J.M., Leverson J.D., Gomez E.B., Forsburg S.L.,
RA   Hunter T.;
RT   "Suppressors of Bir1p (Survivin) identify roles for the chromosomal
RT   passenger protein Pic1p (INCENP) and the replication initiation factor
RT   Psf2p in chromosome segregation.";
RL   Mol. Cell. Biol. 25:9000-9015(2005).
RN   [7]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the
RT   fission yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Required for the spindle checkpoint attachment response
CC       during spindle formation, kinetochore microtubule interactions and
CC       chromosome segregation during anaphase. Ark1 activity depends upon
CC       cut17 function and phosphorylation. Ark1 with bir1 is required for
CC       full-scale association with kinetochores and formation of a
CC       complex with mad3. Ark1 is also required for phosphorylation of
CC       histone H3 that accompanies chromosome condensation and condensin
CC       recruitment to mitotic chromatin. Ark1 with pic1 is required for
CC       the execution of cytokinesis.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Interacts with bir1 and mad3 to form part of the mad2
CC       complex involved in checkpoint activation. Interacts with pic1.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Associates with the elongating
CC       spindle during anaphase.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family. Aurora subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CU329672; CAD88263.1; -; Genomic_DNA.
DR   PIR; T41298; T41298.
DR   RefSeq; NP_001018849.1; -.
DR   HSSP; P31751; 1GZK.
DR   GeneID; 3361036; -.
DR   KEGG; spo:SPCC320.13c; -.
DR   NMPDR; fig|4896.1.peg.54; -.
DR   GeneDB_Spombe; SPCC320.13c; -.
DR   OMA; O59790; TATYMEE.
DR   BRENDA; 2.7.11.1; 653.
DR   ArrayExpress; O59790; -.
DR   GO; GO:0032133; C:chromosome passenger complex; NAS:GeneDB_SPombe.
DR   GO; GO:0000777; C:condensed chromosome kinetochore; IDA:GeneDB_SPombe.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051233; C:spindle midzone; IDA:GeneDB_SPombe.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:GeneDB_SPombe.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:GeneDB_SPombe.
DR   GO; GO:0051315; P:attachment of spindle microtubules to kinet...; TAS:GeneDB_SPombe.
DR   GO; GO:0000910; P:cytokinesis; IMP:GeneDB_SPombe.
DR   GO; GO:0007094; P:mitotic cell cycle spindle assembly checkpoint; IMP:GeneDB_SPombe.
DR   GO; GO:0006468; P:protein amino acid phosphorylation; IC:GeneDB_SPombe.
DR   GO; GO:0034501; P:protein localization to kinetochore; IGI:GeneDB_SPombe.
DR   GO; GO:0034503; P:protein localization to nucleolar rDNA repeats; IGI:GeneDB_SPombe.
DR   GO; GO:0031134; P:sister chromatid biorientation; TAS:GeneDB_SPombe.
DR   InterPro; IPR000719; Prot_kinase_core.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_pkinase-rel.
DR   InterPro; IPR008271; Ser_thr_pkin_AS.
DR   InterPro; IPR002290; Ser_thr_pkinase.
DR   Pfam; PF00069; Pkinase; 1.
DR   ProDom; PD000001; Prot_kinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Kinase; Nucleotide-binding; Nucleus;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    355       Serine/threonine-protein kinase ark1.
FT                                /FTId=PRO_0000085634.
FT   DOMAIN       89    340       Protein kinase.
FT   NP_BIND      95    103       ATP (By similarity).
FT   ACT_SITE    212    212       Proton acceptor (By similarity).
FT   BINDING     118    118       ATP (By similarity).
FT   MUTAGEN     147    147       K->R: No phosphorylation of bir1;
FT                                inhibits cytokinesis in a dominant
FT                                negative manner.
SQ   SEQUENCE   355 AA;  40597 MW;  BF15AC7B7571A301 CRC64;
     MSDSKLADSL NCLSVSTPST TANPGRQQLL RLAVSNQRQV NNVSLANGKE NKRTSNSKFN
     SSLRKIEEPI AGVPSSAGPQ WREFHIGMFE IGKPLGKGKF GRVYLAKEKK TGFIVALKTL
     HKSELVQSKI EKQVRREIEI QSNLRHKNIL RLYGHFHDEK RIYLILEFAG RGELYQHLRR
     AKRFSEEVAS KYIFQMANAL SYLHKKHVIH RDIKPENILL GIDGEIKLSD FGWSVHAPSN
     RRTTLCGTLD YLPPEMVEGK EHTEKVDLWS LGVLTYEFLV GAPPFEDMSG HSATYKRIAK
     VDLKIPSFVP PDARDLISRL LQHNPEKRMS LEQVMRHPWI VKYKDSWTRK SSESS
//