AURK_DICDI
ID AURK_DICDI Reviewed; 384 AA.
AC Q54WX4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Aurora kinase;
DE EC=2.7.11.1;
GN Name=aurK; Synonyms=AurB, Aurora; ORFNames=DDB_G0279343;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP INTERACTION WITH ICPA.
RX PubMed=16339076; DOI=10.1091/mbc.e05-08-0704;
RA Chen Q., Li H., De Lozanne A.;
RT "Contractile ring-independent localization of DdINCENP, a protein important
RT for spindle stability and cytokinesis.";
RL Mol. Biol. Cell 17:779-788(2006).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ICPA.
RX PubMed=18326585; DOI=10.1128/ec.00422-07;
RA Li H., Chen Q., Kaller M., Nellen W., Graef R., De Lozanne A.;
RT "Dictyostelium Aurora kinase has properties of both Aurora A and Aurora B
RT kinases.";
RL Eukaryot. Cell 7:894-905(2008).
CC -!- FUNCTION: Part of a chromosomal passenger complex.
CC {ECO:0000269|PubMed:18326585}.
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 -!- SUBUNIT: Interacts with icpA. Forms a complex at the central spindle.
CC {ECO:0000269|PubMed:16339076, ECO:0000269|PubMed:18326585}.
CC -!- INTERACTION:
CC Q54WX4; Q55GF9: icpA; NbExp=4; IntAct=EBI-2939723, EBI-922339;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18326585}.
CC Chromosome, centromere {ECO:0000269|PubMed:18326585}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:18326585}. Cleavage
CC furrow {ECO:0000269|PubMed:18326585}. Cell projection, neuron
CC projection {ECO:0000250|UniProtKB:P97477}. Note=When cells entered
CC mitosis, found at spindle poles during prometaphase. With the onset of
CC anaphase, localized at the central spindle and remained there during
CC telophase and early cytokinesis. At the end of cytokinesis, localized
CC at the cytoplasmic bridge and eventually to breaking points. Also found
CC at the cleavage furrow, late in cytokinesis, when the furrow becomes a
CC thin cytoplasmic bridge.
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; AAFI02000030; EAL67820.1; -; Genomic_DNA.
DR RefSeq; XP_641803.1; XM_636711.1.
DR AlphaFoldDB; Q54WX4; -.
DR SMR; Q54WX4; -.
DR IntAct; Q54WX4; 2.
DR STRING; 44689.DDB0216254; -.
DR PaxDb; Q54WX4; -.
DR PRIDE; Q54WX4; -.
DR EnsemblProtists; EAL67820; EAL67820; DDB_G0279343.
DR GeneID; 8622000; -.
DR KEGG; ddi:DDB_G0279343; -.
DR dictyBase; DDB_G0279343; aurK.
DR eggNOG; KOG0580; Eukaryota.
DR HOGENOM; CLU_000288_63_6_1; -.
DR InParanoid; Q54WX4; -.
DR OMA; PHTKNVD; -.
DR PhylomeDB; Q54WX4; -.
DR Reactome; R-DDI-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-DDI-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR PRO; PR:Q54WX4; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005813; C:centrosome; IDA:dictyBase.
DR GO; GO:0032133; C:chromosome passenger complex; IDA:dictyBase.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0032154; C:cleavage furrow; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0051233; C:spindle midzone; IDA:dictyBase.
DR GO; GO:0000922; C:spindle pole; IDA:dictyBase.
DR GO; GO:0031616; C:spindle pole centrosome; 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:0004672; F:protein kinase activity; ISS:dictyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0000278; P:mitotic cell cycle; ISS:dictyBase.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell projection; Centromere; Chromosome;
KW Cytoplasm; Cytoskeleton; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..384
FT /note="Aurora kinase"
FT /id="PRO_0000362006"
FT DOMAIN 110..360
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 233
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 116..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 384 AA; 42918 MW; F8085ED1A6539D94 CRC64;
MSYPNNKENS NNIGGGSFSV PSKQPQRVLQ QQNTNINNHQ TTSTVKSTIT KPTTTGATTS
TNTSTIPPTT TASSSSSSSS SSSSSSSSSS SSSSSSSQSV PKKKWCIDDF DIGKLLGMGR
FGHVYLAREK KSQFIVALKV LFKNQLQTHN IEHQLRREIE IQSHLRHPNI LRLFGYFYDD
KRVFLIIEFA KGGECFKELQ KVGSFNEQTA ATYTLQIADA LRYCHSKHVI HRDIKPENLL
IGVGGEIKIA DFGWSVHAPN TKRSTFCGTL EYLPPEVIEK KGYDQTADVW SLGILIFEFL
VGRSPFTSDE EKNIFHNIQE NDVYYPSSIS PEAKDLISRL LVSDPHQRIT LKDVINHPWI
KKHAHPKSLE PTKLGLPLPS QMTY
