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Database: UniProt
Entry: A0E888_PARTE
LinkDB: A0E888_PARTE
Original site: A0E888_PARTE 
ID   A0E888_PARTE            Unreviewed;       664 AA.
AC   A0E888;
DT   28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=Chromosome undetermined scaffold_82, whole genome shotgun sequence {ECO:0000313|EMBL:CAK91505.1};
GN   ORFNames=GSPATT00024233001 {ECO:0000313|EMBL:CAK91505.1};
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK91505.1, ECO:0000313|Proteomes:UP000000600};
RN   [1] {ECO:0000313|EMBL:CAK91505.1, ECO:0000313|Proteomes:UP000000600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK91505.1,
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; CT868663; CAK91505.1; -; Genomic_DNA.
DR   RefSeq; XP_001458902.1; XM_001458865.1.
DR   AlphaFoldDB; A0E888; -.
DR   STRING; 5888.A0E888; -.
DR   EnsemblProtists; CAK91505; CAK91505; GSPATT00024233001.
DR   GeneID; 5044687; -.
DR   KEGG; ptm:GSPATT00024233001; -.
DR   eggNOG; KOG0603; Eukaryota.
DR   HOGENOM; CLU_413614_0_0_1; -.
DR   InParanoid; A0E888; -.
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; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR045270; STKc_AGC.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   PANTHER; PTHR24351:SF243; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 2.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
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}; Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REPEAT          198..230
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          231..263
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          351..609
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         380
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   664 AA;  76093 MW;  A393445006A2555D CRC64;
     MLAIFQLEIY MINFLNVKQQ SCDLYDSGQV LRFDQKNYLK QSNTMNVQQV PITKPPSRSP
     MQTYNIAKII KTEPSQSDRQ FSAGHRCERS MLSPSLLDEG SVLVQKLPPN KLVINLNIKV
     KASGKYPEFC IRDQDTGKVI DIRFQDWRNN WFLYFQSIRN TKSPNNAKLI KAVKNNSYNE
     VKEILLKDKP DINARDTDGN TVLHLSVMSG NSKLVGLLLY HEAQIDSLNS KLQTPLMIAC
     SLGIEEITQQ LITAGADINS QDINKNTCLH LATMNERQKI MDLLLNKQSL NMTLKNKENK
     IAMDYSSNQQ MFLQAMQKQN NNSIKIYDAR TDFGSENCNS FNEDKVGPHH FKVHALIGKG
     SFGEVYLVEK LDTNQLLAMK VLHKSKIQKQ NLTRYALTER NVLSLTKHPF IVRLRYAFQT
     ADKLCLIMDY CPGGDLSSHL RREQRFPEER VKLYLTQMIL ALEDLHKRDI IFRDLKPDNI
     VLDADGYAML TDFGLSKEGV QEHYTGARSF CGSVAYLAPE MLKRCGHGKA VDWYLLGVVM
     YELLVGQPPY YANDREELFN NIQKADLKLP TYISHDGINL LKALLQRNPA KRLGSGKGDA
     EEIKAHPYFK DIEWGKVKDK EIKMPILSRK TRFIKVEHNV FEIGSFLEQS HLAGWSFAEH
     KIQQ
//
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