ID A0DXK6_PARTE Unreviewed; 473 AA.
AC A0DXK6;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Aurora kinase {ECO:0000256|RuleBase:RU367134};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU367134};
GN ORFNames=GSPATT00021397001 {ECO:0000313|EMBL:CAK87773.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK87773.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK87773.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK87773.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
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 Evidence={ECO:0000256|ARBA:ARBA00001433,
CC ECO:0000256|RuleBase:RU367134};
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; Evidence={ECO:0000256|ARBA:ARBA00000775,
CC ECO:0000256|RuleBase:RU367134};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. Aurora subfamily. {ECO:0000256|RuleBase:RU367134}.
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DR EMBL; CT868640; CAK87773.1; -; Genomic_DNA.
DR RefSeq; XP_001455170.1; XM_001455133.1.
DR AlphaFoldDB; A0DXK6; -.
DR STRING; 5888.A0DXK6; -.
DR EnsemblProtists; CAK87773; CAK87773; GSPATT00021397001.
DR GeneID; 5040955; -.
DR KEGG; ptm:GSPATT00021397001; -.
DR eggNOG; KOG0580; Eukaryota.
DR HOGENOM; CLU_000288_63_4_1; -.
DR InParanoid; A0DXK6; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14007; STKc_Aurora; 1.
DR Gene3D; 6.10.140.2220; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR030616; Aur-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR24350:SF33; AURORA KINASE; 1.
DR PANTHER; PTHR24350; SERINE/THREONINE-PROTEIN KINASE IAL-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR630616-
KW 2}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU367134};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR630616-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU000304};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367134};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 10..56
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT DOMAIN 91..342
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 214
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR630616-1"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630616-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 169..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630616-2"
FT BINDING 218..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630616-2"
FT BINDING 232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630616-2"
FT CROSSLNK 216
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000256|PIRSR:PIRSR630616-3"
SQ SEQUENCE 473 AA; 56001 MW; 1B1E986D534DB920 CRC64;
MNRFCDYKSC QYFIKQPTIE QRSKLNKVMC PLCMGANYCS TRCRDLDWPI YHKEICKKSQ
PDRARSCNDT IDSCSTTSVR RRPEEFEIIM IGSKQELGRG SYGSVKLVKD KQNGLLYAMK
IMNKRQVFEY CSVENLKREI KIQRKLVHPH ICKLHHYFED KENVYLILEY AQNGSLFNYI
KKRSKLPENE AFVYFFQTCL GIDYLHKNKI IHRDLKPENL LLDHDGNVKI CDFGWSAESL
TEKRMTFCGT YEYMAPEMLN KQPHDFSLDV WSLGILLYEL LHGNAPYRGR NNEELGNKIK
SGQPINFAPT LSNEVITLIK GILKYIPGER LTMDQIFDHP WMVKHASSYN IDIWTFVYKT
QYPTRQIPTA NFQQKQKIIE IQKKDPIARP ISQDYNKYKE QPINNNATNY KAYQNDYNNN
KQEDFNKPRI SRVSNRNEIM MHQHQLQQQQ QEEKLSFMDR VFLAFGCLNR EKK
//
