ID A0DUX2_PARTE Unreviewed; 371 AA.
AC A0DUX2;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 24-JAN-2024, entry version 84.
DE SubName: Full=Chromosome undetermined scaffold_65, whole genome shotgun sequence {ECO:0000313|EMBL:CAK86839.1};
GN ORFNames=GSPATT00020501001 {ECO:0000313|EMBL:CAK86839.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK86839.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK86839.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK86839.1,
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 -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC {ECO:0000256|RuleBase:RU000304}.
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DR EMBL; CT868596; CAK86839.1; -; Genomic_DNA.
DR RefSeq; XP_001454236.1; XM_001454199.1.
DR AlphaFoldDB; A0DUX2; -.
DR STRING; 5888.A0DUX2; -.
DR EnsemblProtists; CAK86839; CAK86839; GSPATT00020501001.
DR GeneID; 5040021; -.
DR KEGG; ptm:GSPATT00020501001; -.
DR eggNOG; KOG0598; Eukaryota.
DR HOGENOM; CLU_000288_63_5_1; -.
DR InParanoid; A0DUX2; -.
DR OMA; CVIYDMM; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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 CDD; cd05123; STKc_AGC; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045270; STKc_AGC.
DR PANTHER; PTHR24351:SF237; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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}.
FT DOMAIN 56..311
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 312..371
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 371 AA; 43014 MW; C22C49147FE00B65 CRC64;
MGMCQNKPAE YTSTLPSFKD VMPEADDEDD KIGETTQLPI EGESADSKQK LNLDDFELIK
VIGRGSFGKV LLVKKRDDQQ LFAVKILRKK MLSKKKQQDQ AIKERKIMSL INSPFMVKLH
YAFQSHSRLY MVMDFMQGGE LFLHLRKRFK FPEDWVQFYA AELLVAIDLL HQSNIIYRDL
KPENILLDKN GHIVLTDFGL SKLGFEKNEM TYSFCGTPEY VAPEILYQRG HTFVVDFYSY
GAMIYEMLCG SPPFYSKDKR EMLKNRCEKP LEMKSCFSFY AASLLKGLLT KDPGLRLGSN
GIQEIKKHNF FNGIDWKLVE QRKLQPPIIP KIQHVQDLQN FAPAFLQQPI METPESVSNE
YFEGFTYQQV I
//