ID F0WW01_9STRA Unreviewed; 1103 AA.
AC F0WW01;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Aurora kinase {ECO:0000256|RuleBase:RU367134};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU367134};
DE Flags: Fragment;
GN Name=AlNc14C306G10451 {ECO:0000313|EMBL:CCA25603.1};
GN ORFNames=ALNC14_117470 {ECO:0000313|EMBL:CCA25603.1};
OS Albugo laibachii Nc14.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA25603.1};
RN [1] {ECO:0000313|EMBL:CCA25603.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA Jones J.D.;
RT "Gene gain and loss during evolution of obligate parasitism in the white
RT rust pathogen of Arabidopsis thaliana.";
RL PLoS Biol. 9:e1001094-e1001094(2011).
RN [2] {ECO:0000313|EMBL:CCA25603.1}
RP NUCLEOTIDE SEQUENCE.
RA MacLean D.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- SIMILARITY: Belongs to the PIAS family.
CC {ECO:0000256|ARBA:ARBA00005383}.
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; FR824351; CCA25603.1; -; Genomic_DNA.
DR AlphaFoldDB; F0WW01; -.
DR EnsemblProtists; CCA25603; CCA25603; ALNC14_117470.
DR HOGENOM; CLU_006378_0_0_1; -.
DR UniPathway; UPA00886; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
DR CDD; cd16650; SP-RING_PIAS-like; 1.
DR CDD; cd14007; STKc_Aurora; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
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; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR24350:SF0; AURORA KINASE; 1.
DR PANTHER; PTHR24350; SERINE/THREONINE-PROTEIN KINASE IAL-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF02891; zf-MIZ; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF68906; SAP domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50800; SAP; 1.
DR PROSITE; PS51044; ZF_SP_RING; 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 Ligase {ECO:0000313|EMBL:CCA25603.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR630616-2}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU367134};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367134};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00452}.
FT DOMAIN 143..397
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 432..466
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT DOMAIN 791..874
FT /note="SP-RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51044"
FT ACT_SITE 268
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR630616-1"
FT BINDING 153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630616-2"
FT BINDING 172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630616-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 272..273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630616-2"
FT BINDING 286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630616-2"
FT CROSSLNK 270
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000256|PIRSR:PIRSR630616-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CCA25603.1"
SQ SEQUENCE 1103 AA; 125024 MW; 929D15AEC2405FC0 CRC64;
EVFSQCRTIN FEYTQLCILL FELIDLKLNV IRIGNYLEST YQCPLALFPA KCWRNCRYSL
ASNRFDGAEH TGSNIAAKKR DYESETSAQS IPRYPLQDVT GVCRNTVTNP SNSVNLKESE
EWPKCQSEVS TPTTKKSWSI QDFEIGRILG RGRFGRVYLA REKKAKKIVA LKILLKDQLR
NAGVVHQLRK EVEIHSRINH PNILRLYATF QDTRRVYLVL QYASGGDLYR KLQNAPGRRF
SERQTAHYIS QLVSAIQTCH AQNVVHRDIK PENLLLTSDE QLLLADFGWS SHNVTHHNRR
ETLCGTLDYL SPEMVQGTPY DTSVDIWAIG VTLYEFLCGK PPFEAHDQNQ TVNQIIERPV
SVPTFVSPAA RDLIQQILQK SPQARLSLSA IKRHRWFTYH VSACRGEHKE MGKEFRMSQV
RDLRLHQIRI KLNDLRMNEL RNILIAMRLT RSGKKCELVE RIATALEVFD KKAAEYHTSN
AITSAFYVGQ IDAALKYIEM QIYANVQQHV PPPATSVPQT YTNTIPLART YPSGNILSSF
YTGPLQNQSP PISNVEILQL NSYPSMDHAR CFCNPRLGPP VSHRIVSCIA CGLKVHTKCH
QLDANTQIRD RINHYICEFC RSEQLDPFFR LEKTIVKPFF VRFVNSYGAF QLEYTLTDSD
LAILQHRESI SELQLRCFDV KDDLRRGHCW PTSTFITVNG VATPIIQRSP PGHTNPSKVL
REIPLNVFGL SRKGLNIIEI RCKENASIFA FMIQIVKAQT LESIMSLVEK NSSQMTFVEA
KQQVEGSFDK SNDGVETTCT LLSLRCPLGL CMIDRPARGR QCKHLQCFDL KTFLLYSRKA
RSKPWICVIC HKFIRLADLR VDPFLSKLLK ENGQLEGVEH VEIFPDATWK VQLNEEETTS
SSPIVKKLKV DTLQTELDLK TNSNETIAID LLSSDEENER TDSNAMENEV ENSEILLSES
ELWEDLSSST KIAQLNGSNA STSFYKSKQW SASQPDEIVE ADALDSEDSW PPLFPSISSS
LEAVSTEAMQ IGDSNLLPIS TFSEIHKSLT ENSECNGTNV LVQNISLAKT PNSMEIARSM
ENGNGVQSLG CQLNANSASQ SCW
//
