ID E1Z2B2_CHLVA Unreviewed; 790 AA.
AC E1Z2B2;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Aurora kinase {ECO:0000256|RuleBase:RU367134};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU367134};
GN ORFNames=CHLNCDRAFT_133081 {ECO:0000313|EMBL:EFN59629.1};
OS Chlorella variabilis (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=554065 {ECO:0000313|Proteomes:UP000008141};
RN [1] {ECO:0000313|EMBL:EFN59629.1, ECO:0000313|Proteomes:UP000008141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NC64A {ECO:0000313|EMBL:EFN59629.1,
RC ECO:0000313|Proteomes:UP000008141};
RX PubMed=20852019; DOI=10.1105/tpc.110.076406;
RA Blanc G., Duncan G., Agarkova I., Borodovsky M., Gurnon J., Kuo A.,
RA Lindquist E., Lucas S., Pangilinan J., Polle J., Salamov A., Terry A.,
RA Yamada T., Dunigan D.D., Grigoriev I.V., Claverie J.M., Van Etten J.L.;
RT "The Chlorella variabilis NC64A genome reveals adaptation to
RT photosymbiosis, coevolution with viruses, and cryptic sex.";
RL Plant Cell 22:2943-2955(2010).
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; GL433835; EFN59629.1; -; Genomic_DNA.
DR RefSeq; XP_005851731.1; XM_005851669.1.
DR AlphaFoldDB; E1Z2B2; -.
DR STRING; 554065.E1Z2B2; -.
DR GeneID; 17359469; -.
DR KEGG; cvr:CHLNCDRAFT_133081; -.
DR eggNOG; KOG0580; Eukaryota.
DR InParanoid; E1Z2B2; -.
DR OMA; TIAMGRH; -.
DR OrthoDB; 3790934at2759; -.
DR Proteomes; UP000008141; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24350:SF30; AURORA KINASE; 1.
DR PANTHER; PTHR24350; SERINE/THREONINE-PROTEIN KINASE IAL-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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|PIRSR:PIRSR630616-
KW 2}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU367134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR630616-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000008141};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU367134};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367134}.
FT DOMAIN 112..382
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 239
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR630616-1"
FT BINDING 122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630616-2"
FT BINDING 141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630616-2"
FT BINDING 243..244
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630616-2"
FT BINDING 257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630616-2"
FT CROSSLNK 241
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000256|PIRSR:PIRSR630616-3"
SQ SEQUENCE 790 AA; 81120 MW; 90300B8125F026E2 CRC64;
MFSHLWLTPR DKQGREDKAR PPHRLALAVA AAGGGDSPRA ASRLTPAAQT ASLSSGSGCR
SPRSPQGCQS SRVAALPAYR ARSSAPGGVQ QLPQVQAAGE QPAAAYTSLD GLSKMAELHK
GKHSTVHNYL DTRSGRVVAV KTYYKRTMAK RHFRNCRREV DINRMLARQG FTGTVQLLGA
FEDDSHIHLV MESCAGGDLY RRLVRAGGVL GEAEVCHNVV VPLLLTLTFL HANHIAHRDI
KPENIMFAAD GSLRLGDFGL SIDAARERPT SRVGTLDYMA PEVVGMPSPD DMQRLGLAPH
KIGHYGCKVD VWAVGVLAYE LLCGRPPFEV EDVKLTEQHI QFAEVAFPPH ISPLCRSFIQ
QALTKRPESR PSAAQLFQHR WVQRHYQQLL AAQAQAQPAA ATMSAAAAAA AVAAAAGLLH
TPELRRTVSQ PPSPSKSMPG GTAGGGAGNA VLTPAAAAAV LAPFLPLSQA KMAHKVRLLS
AGRPPSSGKP ARLRRRVSDP LARVLLQPPP AGAGAAELAV AAAAAAGVPP TTPPPAAAAP
PACASDGAGS VAPAADVGDD AASGAAAPDC FEQPGTPGLK TTPLPRQRPV VQPRAPLGRT
PFLLPLVSPG SSGTAVGTSA PADLQPVAAG VRGKTAAGRS RFAAAAENDE GAASASAAMR
ASAETMLSSP GAALVGRASS LTSLCSRDGG SSSNLQVQER GASFTSAFGG SSGGNLPLQA
RASSFTSYGG GGSSGSLQLA ARASSLTSFG GRSSGNLSSP GSKQLPGKPP AGEAGQQAGT
AAELLQRLQL
//
