IPL1_CANGA
ID IPL1_CANGA Reviewed; 358 AA.
AC Q6FV07;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Spindle assembly checkpoint kinase;
DE EC=2.7.11.1;
DE AltName: Full=Aurora kinase;
GN Name=IPL1; OrderedLocusNames=CAGL0E05720g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Required for high-fidelity chromosome segregation during the
CC later part of each cell cycle. Acts in opposition to the phosphatase
CC PP1. Has a role in attaching the kinetochores to the microtubules and
CC ensuring that sister kinetochores connect to opposite poles. The
CC promotion of bi-orientation is achieved by selectively detaching
CC kinetochore-microtubule attachments that are not under tension.
CC Phosphorylates histone H3 to form H3S10ph during mitosis and meiosis
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250}. Chromosome, centromere, kinetochore
CC {ECO:0000250}. Note=Associates with the mitotic spindle and on
CC elongated and disassembling spindles. Also associated with the
CC kinetochore (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. Aurora subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; CR380951; CAG58856.1; -; Genomic_DNA.
DR RefSeq; XP_445937.1; XM_445937.1.
DR AlphaFoldDB; Q6FV07; -.
DR SMR; Q6FV07; -.
DR STRING; 5478.XP_445937.1; -.
DR EnsemblFungi; CAG58856; CAG58856; CAGL0E05720g.
DR GeneID; 2887534; -.
DR KEGG; cgr:CAGL0E05720g; -.
DR CGD; CAL0128618; CAGL0E05720g.
DR VEuPathDB; FungiDB:CAGL0E05720g; -.
DR eggNOG; KOG0580; Eukaryota.
DR HOGENOM; CLU_000288_63_6_1; -.
DR InParanoid; Q6FV07; -.
DR OMA; PHTKNVD; -.
DR Proteomes; UP000002428; Chromosome E.
DR GO; GO:0032133; C:chromosome passenger complex; IEA:EnsemblFungi.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000939; C:inner kinetochore; IEA:EnsemblFungi.
DR GO; GO:0005828; C:kinetochore microtubule; IEA:EnsemblFungi.
DR GO; GO:1990385; C:meiotic spindle midzone; IEA:EnsemblFungi.
DR GO; GO:1990023; C:mitotic spindle midzone; IEA:EnsemblFungi.
DR GO; GO:0140602; C:nucleolar ring; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035175; F:histone kinase activity (H3-S10 specific); IEA:EnsemblFungi.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0051316; P:attachment of spindle microtubules to kinetochore involved in meiotic chromosome segregation; IEA:EnsemblFungi.
DR GO; GO:0120110; P:interphase mitotic telomere clustering; IEA:EnsemblFungi.
DR GO; GO:0045144; P:meiotic sister chromatid segregation; IEA:EnsemblFungi.
DR GO; GO:0033316; P:meiotic spindle assembly checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:0044774; P:mitotic DNA integrity checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:1990758; P:mitotic sister chromatid biorientation; IEA:EnsemblFungi.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:0051228; P:mitotic spindle disassembly; IEA:EnsemblFungi.
DR GO; GO:1901925; P:negative regulation of protein import into nucleus during spindle assembly checkpoint; IEA:EnsemblFungi.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IEA:EnsemblFungi.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:EnsemblFungi.
DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; IEA:EnsemblFungi.
DR GO; GO:1903380; P:positive regulation of mitotic chromosome condensation; IEA:EnsemblFungi.
DR GO; GO:1905824; P:positive regulation of mitotic sister chromatid arm separation; IEA:EnsemblFungi.
DR GO; GO:0140429; P:positive regulation of mitotic sister chromatid biorientation; IEA:EnsemblFungi.
DR GO; GO:0034501; P:protein localization to kinetochore; IEA:EnsemblFungi.
DR GO; GO:0034503; P:protein localization to nucleolar rDNA repeats; IEA:EnsemblFungi.
DR GO; GO:1902412; P:regulation of mitotic cytokinesis; IEA:EnsemblFungi.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IEA:EnsemblFungi.
DR GO; GO:1904967; P:regulation of monopolar spindle attachment to meiosis I kinetochore; IEA:EnsemblFungi.
DR InterPro; IPR030616; Aur.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24350; PTHR24350; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Centromere; Chromosome; Chromosome partition;
KW Cytoplasm; Cytoskeleton; Kinase; Kinetochore; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..358
FT /note="Spindle assembly checkpoint kinase"
FT /id="PRO_0000086026"
FT DOMAIN 100..358
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 223
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 106..114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 358 AA; 40992 MW; 251500844A6CF5C6 CRC64;
MENKATLARN IGEKRVSPRS KVNGTGKSWR ISYSPQRMDG VSSGRNVSKI PSPVRERLFL
KNQERKPLGV SPLSNLSPNS LGRNSLEKST YNNKLSLKDF EVGRKLGKGK FGKVYCVRHK
KSGFICALKA IEKNEILQFN LLKQLKREVD IQLGMDHPNI IKLYAHFHDE KRVYLLMEHS
INGELYKSLK NNGPFNDVLA SHYIYQIADA LHYMHKKRII HRDVKPENVL IGFDNVVKLA
DFGWSILNPE GSKRKTLCGT IDYLSPEMIT PREYDEQVDV WALGVLAYEL VVGVPPFEEN
SKELTYKRIL KCDLNFPESI SKDAKDLISK LLVTDTTQRL SLTGVKTHPW ILKNKPFW
