IPL1_DEBHA
ID IPL1_DEBHA Reviewed; 412 AA.
AC Q6BVA0;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Spindle assembly checkpoint kinase;
DE EC=2.7.11.1;
DE AltName: Full=Aurora kinase;
GN Name=IPL1; OrderedLocusNames=DEHA2C04246g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382135; CAG85914.2; -; Genomic_DNA.
DR RefSeq; XP_457869.2; XM_457869.1.
DR AlphaFoldDB; Q6BVA0; -.
DR SMR; Q6BVA0; -.
DR STRING; 4959.XP_457869.2; -.
DR EnsemblFungi; CAG85914; CAG85914; DEHA2C04246g.
DR GeneID; 2900232; -.
DR KEGG; dha:DEHA2C04246g; -.
DR VEuPathDB; FungiDB:DEHA2C04246g; -.
DR eggNOG; KOG0580; Eukaryota.
DR HOGENOM; CLU_000288_63_6_1; -.
DR InParanoid; Q6BVA0; -.
DR OMA; PHTKNVD; -.
DR OrthoDB; 954262at2759; -.
DR Proteomes; UP000000599; Chromosome C.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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..412
FT /note="Spindle assembly checkpoint kinase"
FT /id="PRO_0000086027"
FT DOMAIN 148..401
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 94..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 271
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 154..162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 412 AA; 47856 MW; F6AB35F1D540B1A5 CRC64;
MYCRVFTHFS LYRLYTLSDN ININKTNHNK SIGLHQHRVN YMPRSMTASS SQLKRIETRI
ESLSESLSKS NARKPLGKFQ LNTFDNNKIT KLQNEKVRPS KSSHIPVKSP IRKKGHSPAQ
VLQNERMDTK LLLQKLPSAS RHMTLDDFEI GKVLGKGKLG KVYCVKHKTS GYIAALKVMA
KKDLIDLKLE KNFRREIEIQ SNLIHPKISR LYGFFYDHKN VYLILEYSIH GELYHHLKVQ
RRFNDATASH YIYQVALALD YLHTKHIIHR DIKPENILLS TDNCIKLSDF GWSVKSSPSS
STKRLTICGT LDYLPPEMIE SNEHDYTVDI WSLGILCYEF LVGKPPFEEI DKNSTYKRIA
KVDLKIPSFL SSEATDLILR LLQKSPKKRI TLAEVMNHPW IMNNQQYWPN EN
