ID A0A078ABY5_STYLE Unreviewed; 930 AA.
AC A0A078ABY5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Protein kinase domain containing protein {ECO:0000313|EMBL:CDW79366.1};
GN Name=Contig6267.g6704 {ECO:0000313|EMBL:CDW79366.1};
GN ORFNames=STYLEM_8353 {ECO:0000313|EMBL:CDW79366.1};
OS Stylonychia lemnae (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW79366.1, ECO:0000313|Proteomes:UP000039865};
RN [1] {ECO:0000313|EMBL:CDW79366.1, ECO:0000313|Proteomes:UP000039865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=130c {ECO:0000313|EMBL:CDW79366.1,
RC ECO:0000313|Proteomes:UP000039865};
RA Swart Estienne;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CCKQ01007928; CDW79366.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078ABY5; -.
DR EnsemblProtists; CDW79366; CDW79366; STYLEM_8353.
DR InParanoid; A0A078ABY5; -.
DR OrthoDB; 5591874at2759; -.
DR Proteomes; UP000039865; 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 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; IPR000961; AGC-kinase_C.
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; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045270; STKc_AGC.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR24351:SF243; RIBOSOMAL PROTEIN S6 KINASE; 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; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CDW79366.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000039865};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REPEAT 251..283
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 605..865
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 866..930
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 311..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 634
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 930 AA; 107665 MW; C541F68F99163D99 CRC64;
MRIFIKIYAD DLKSPSSTYP LQLKGTIKDI TIGQLKHEIE NNILPQILQR NQIISIKKSV
VIMRIDHSDS VTLEQAGITD GIKIHVQDQY SLNQKSKFMS QNFHQDQSHI PQTNAQSFIV
SSSPQQKPDL AYVDEILIKF LEFNQLFEFI DVFQMYHIQG ANMQQNLDIN RCIHNAPQQS
MEGKSYLHLA VERKHKQIIA YLLFDAKLDP NRLTEETEMS ALHIAVQMKS SDVIELLLTH
DKTEIDIQSS IHGTPLHLAC RGGSVKIVQQ LLLNNADLSI KNNKFKTAKE VTNNQRIIYL
IEKYEKRNKT NNSSFLSTQS EEEKESSDKK QMPFQSANQS SIKAPLMDCI TEEDIMYEEE
EIENQAGGVL DQAEEFIQDF SCSRIELVPT IRGSLLAQGN LKKKQKQLYF VLKPSKGQLL
KFEKKDHYDK LIKGQSQDEK IFRKYNIEII YLKNILSIYP SFQNQFINKG QHALEMCCYN
DLLTKAKKFY EWYKTILDLL GEEDKLTEQI KYKLQEIEEF CDSYCDTEIK DIPFIEQKQA
EINNRQRLER IKEINQNLKK EEYIESQNGS NSSKHNVSDW DQYASFTKAS RTASDLNFKP
IFKDFEILEQ IGEGSFGRVF RVKLKQTGAE MAMKAMKKQF LIQNSQIKYA VSECKIMQTL
EHPFLLRMNY SLQTPQHLYM ITEYCKNGDL SYHLDQLQFL DEKIAKFIIA ELTLAIEYLH
SNNIIYRDLK PENILIDNQG HVRLADFGLA KQGPDEKTQQ KKGQAFVAQS FCGSPAYLAP
EMLKQQGITS AGDVYQIGVV LYEMLVGMPP YYNDNIKVLY QNIEKGKLKI PKYLTNEAKK
FLLRILNKDP KKRPSLKEVK KDAFFSDIDW TKLENKQIPP PQILKKYSEY DDSDEEDKEE
TKQAADLPIK KLDKLVINIQ LLTSGIGNDV
//
