IPL1_ENCCU
ID IPL1_ENCCU Reviewed; 272 AA.
AC Q8SRL5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Probable spindle assembly checkpoint kinase homolog;
DE EC=2.7.11.1;
DE AltName: Full=Aurora kinase;
GN Name=IPL1; OrderedLocusNames=ECU07_0360;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [2]
RP PREDICTION OF FUNCTION.
RX PubMed=17784954; DOI=10.1186/1471-2164-8-309;
RA Miranda-Saavedra D., Stark M.J.R., Packer J.C., Vivares C.P., Doerig C.,
RA Barton G.J.;
RT "The complement of protein kinases of the microsporidium Encephalitozoon
RT cuniculi in relation to those of Saccharomyces cerevisiae and
RT Schizosaccharomyces pombe.";
RL BMC Genomics 8:309-309(2007).
CC -!- FUNCTION: Required for high-fidelity chromosome segregation during the
CC later part of each cell cycle. Has a role in attaching the kinetochores
CC to the microtubules and ensuring that sister kinetochores connect to
CC opposite poles. The promotion of bi-orientation is achieved by
CC selectively detaching kinetochore-microtubule attachments that are not
CC under tension (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}.
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; AL590447; CAD25568.1; -; Genomic_DNA.
DR RefSeq; NP_585964.1; NM_001041586.1.
DR AlphaFoldDB; Q8SRL5; -.
DR SMR; Q8SRL5; -.
DR STRING; 284813.Q8SRL5; -.
DR GeneID; 859393; -.
DR KEGG; ecu:ECU07_0360; -.
DR VEuPathDB; MicrosporidiaDB:ECU07_0360; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q8SRL5; -.
DR OMA; PHTKNVD; -.
DR OrthoDB; 954262at2759; -.
DR Proteomes; UP000000819; Chromosome VII.
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; 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..272
FT /note="Probable spindle assembly checkpoint kinase homolog"
FT /id="PRO_0000384423"
FT DOMAIN 10..263
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 134
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 16..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 272 AA; 31717 MW; A533EB142469D689 CRC64;
MVEYWTLDRF EIGRLLGRGK FGQVWLARER EKGFIVALKI IPIKEIQTVE TARQIRREIE
IHSNLKHPNI LRMYGHFHDK DNIYLILEYA GKGEFFKFLS DRGGKFGEKE TSLYIRQVML
ALTYMKECNV IHRDIKPENL LLGSDNQLKI ADFGWAVYNA DKRRMTFCGT MEYLAPEMVN
NDIHDSGIDL WCLGILTYEF LMGKTPFESK NRNMREAYKK INSLKYTIPE TISSNASDFI
SRLLVLSPGD RMELTEALNH PFIVKHHGRS SD
