IPL1_CANAL
ID IPL1_CANAL Reviewed; 528 AA.
AC Q59S66; A0A1D8PPU6;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Spindle assembly checkpoint kinase;
DE EC=2.7.11.1;
DE AltName: Full=Aurora kinase;
GN Name=IPL1; OrderedLocusNames=CAALFM_C602320CA;
GN ORFNames=CaO19.10978, CaO19.3474;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017628; AOW30167.1; -; Genomic_DNA.
DR RefSeq; XP_712513.2; XM_707420.2.
DR AlphaFoldDB; Q59S66; -.
DR SMR; Q59S66; -.
DR BioGRID; 1228944; 1.
DR STRING; 237561.Q59S66; -.
DR PRIDE; Q59S66; -.
DR GeneID; 3645876; -.
DR KEGG; cal:CAALFM_C602320CA; -.
DR CGD; CAL0000183313; IPL1.
DR VEuPathDB; FungiDB:C6_02320C_A; -.
DR eggNOG; KOG0580; Eukaryota.
DR HOGENOM; CLU_000288_20_0_1; -.
DR InParanoid; Q59S66; -.
DR OrthoDB; 954262at2759; -.
DR PRO; PR:Q59S66; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0032133; C:chromosome passenger complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; IDA:CGD.
DR GO; GO:0005828; C:kinetochore microtubule; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035174; F:histone serine kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IMP:CGD.
DR GO; GO:0045143; P:homologous chromosome segregation; IEA:EnsemblFungi.
DR GO; GO:0045144; P:meiotic sister chromatid segregation; IEA:EnsemblFungi.
DR GO; GO:0044774; P:mitotic DNA integrity checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:0051228; P:mitotic spindle disassembly; IEA:EnsemblFungi.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
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:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:0090266; P:regulation of mitotic cell cycle spindle assembly checkpoint; IEA:EnsemblFungi.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IEA:EnsemblFungi.
DR InterPro; IPR030616; Aur.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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; 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..528
FT /note="Spindle assembly checkpoint kinase"
FT /id="PRO_0000086025"
FT DOMAIN 242..515
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 365
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 248..256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 528 AA; 60193 MW; 67C61FD3EC5054B3 CRC64;
MMLPRNSPHR TESTLAYNNN NSNNNNNNNG SSLFQRKPLA PINSEFKISK PQHIKPTTHS
HTFTTPTPKT RNTATTTTNN NNRNNHQYRN PNLNTSLVFT PTKNSSSSSS SHSSSLLSSS
PFVEEPENQP ESNHTRATSH YRTTSTSQYK SSANKDASHS LITSSKRKTS TKQTSESTNP
KRRTTTTATQ NTNNNKILNP SLSSSTIRFS TVSSSTSSST TSSSSSSHTS PKPQQQLTLD
DFEFGKILGK GKLGRVYCVK HKQSGLIFAL KVMSKSEIMN LKLEKSLRRE IEIQSNLYHI
NITRLYSWFH DSINIYLLLE YSIEGELYTH LKKLKRFDNI MASNYIFQIT QALIFLHQRG
IIHRDLKPEN IMVSLDNQLK LSDFGWSVQI NQNQNQNQIH NQTQTQKTPH QKKQKQKRLT
ICGTLDYLPP EMIESKSHDF SVDIWALGIL CYELLVGKPP FEAINRNITY EKIAKVDIKY
PSNLDVDAID LISKLVVKDP NKRLSLKEVL NHNWIIKNKP KWPKNIYK
