ID A0BQD7_PARTE Unreviewed; 457 AA.
AC A0BQD7;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=GSPATT00030983001 {ECO:0000313|EMBL:CAK60754.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK60754.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK60754.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK60754.1,
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).
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DR EMBL; CT868009; CAK60754.1; -; Genomic_DNA.
DR RefSeq; XP_001428152.1; XM_001428115.1.
DR AlphaFoldDB; A0BQD7; -.
DR STRING; 5888.A0BQD7; -.
DR EnsemblProtists; CAK60754; CAK60754; GSPATT00030983001.
DR GeneID; 5013936; -.
DR KEGG; ptm:GSPATT00030983001; -.
DR eggNOG; KOG0574; Eukaryota.
DR HOGENOM; CLU_000288_26_6_1; -.
DR InParanoid; A0BQD7; -.
DR OMA; THHQKQK; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd06614; STKc_PAK; 1.
DR Gene3D; 3.90.810.10; CRIB domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR PANTHER; PTHR48015:SF35; SERINE_THREONINE-PROTEIN KINASE PAK; 1.
DR Pfam; PF00786; PBD; 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.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000600}.
FT DOMAIN 179..428
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 457 AA; 52292 MW; 46293312B6012359 CRC64;
MGQKSSKEKN HNAPDGQISN FQSHIQITRD PKTGKLLGVP KEWADLNGLK LEIDQNKTVE
TKNLPASVQP SELPEAILDL INEPIMSAPF NLQHKIHIEI DPTAQLGLKG LPPEWIEKLQ
KADLQKADIE QNPQVMIQII SNYEEGVYRQ TKLTLPTNDE FIKQVMDIKF IEQDPSILYK
FTEQLGKGAM CKVYKAIHRN TNDEVAVRVM KIGNDMQRIK VEIALMKMCA NQNIVKYYDS
YIYQSCLFMV VEYLDGGCLT EIIYQNFKSM KEPEIAYICG EILSGLNYMH QKKKIHRDLK
SDNILMNKKG EIKIADFGFA TQLTAERQHR KSVVGTPAWM SPELILKQDY DEKVDIWSVG
IIAIELAQGE PPYLRVPPLK AMYSITANDA PRLPNKFSKQ FQEFIEKVLD KSSKTRMTAE
QALQLPFFNN RNKEGVLQMI LNKKNIPLNE LIKQAPK
//
