ID   A0A2A4J9P7_HELVI        Unreviewed;       291 AA.
AC   A0A2A4J9P7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   07-APR-2021, entry version 12.
DE   RecName: Full=Aurora kinase {ECO:0000256|RuleBase:RU367134};
DE            EC=2.7.11.1 {ECO:0000256|RuleBase:RU367134};
GN   ORFNames=B5V51_5084 {ECO:0000313|EMBL:PCG68569.1};
OS   Heliothis virescens (Tobacco budworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Holometabola; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Heliothis.
OX   NCBI_TaxID=7102 {ECO:0000313|EMBL:PCG68569.1, ECO:0000313|Proteomes:UP000218220};
RN   [1] {ECO:0000313|EMBL:PCG68569.1, ECO:0000313|Proteomes:UP000218220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HvINT- {ECO:0000313|EMBL:PCG68569.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:PCG68569.1};
RA   Fritz M.L., Deyonke A.M., Papanicolaou A., Micinski S., Westbrook J.,
RA   Gould F.;
RT   "Contemporary evolution of a Lepidopteran species, Heliothis virescens, in
RT   response to modern agricultural practices.";
RL   Submitted (SEP-2017) 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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. Aurora subfamily. {ECO:0000256|RuleBase:RU367134}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PCG68569.1}.
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DR   EMBL; NWSH01002306; PCG68569.1; -; Genomic_DNA.
DR   Proteomes; UP000218220; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0032133; C:chromosome passenger complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0106311; F:protein threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043988; P:histone H3-S28 phosphorylation; IEA:InterPro.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint; IEA:InterPro.
DR   GO; GO:0032467; P:positive regulation of cytokinesis; IEA:InterPro.
DR   InterPro; IPR030616; Aur.
DR   InterPro; IPR028772; AURKB.
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   PANTHER; PTHR24350:SF24; PTHR24350:SF24; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU367134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000218220};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU000304};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367134}.
FT   DOMAIN          31..283
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        156
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630616-1"
FT   BINDING         60
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   291 AA;  33556 MW;  8E8BB12D5E0D67F6 CRC64;
     MTMKSDVLEL ETKIINHDAY GTSYKWAPRD FELGSPLGQG KFGNVNVARE KKTGYLVAIK
     TLFKSQIVRS KCERQVMREI EIQSHLKHPN ILRLLTWFHD ERRIYLVIEF AAGGELYKHL
     TNSPKGRFPE ARAARYIYQV ADAVEYCHQH HVIHRDIKPE NILVAFSGDL KLADFGWSVH
     APSERRKTMC GTLDYLPPEM IKREVYDVSV DHWCIGVLLY EFLVGKPPFE SEGQDKTYAR
     ILALDMVYPS YVPEGAKDLI SSLLRHSSKE RLSLDGVKKH YWVQQFQSNG A
//