ID Q24DA7_TETTS Unreviewed; 949 AA.
AC Q24DA7;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 3.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Protein kinase {ECO:0000313|EMBL:EAS05738.3};
GN ORFNames=TTHERM_01038810 {ECO:0000313|EMBL:EAS05738.3};
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017 {ECO:0000313|EMBL:EAS05738.3, ECO:0000313|Proteomes:UP000009168};
RN [1] {ECO:0000313|Proteomes:UP000009168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA Hamilton E.P., Orias E.;
RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT model eukaryote.";
RL PLoS Biol. 4:1620-1642(2006).
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DR EMBL; GG662331; EAS05738.3; -; Genomic_DNA.
DR RefSeq; XP_001025983.3; XM_001025983.3.
DR AlphaFoldDB; Q24DA7; -.
DR STRING; 312017.Q24DA7; -.
DR EnsemblProtists; EAS05738; EAS05738; TTHERM_01038810.
DR GeneID; 7837614; -.
DR KEGG; tet:TTHERM_01038810; -.
DR eggNOG; KOG0575; Eukaryota.
DR HOGENOM; CLU_253559_0_0_1; -.
DR InParanoid; Q24DA7; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR045269; Atg1-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR24348:SF22; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EAS05738.3};
KW Reference proteome {ECO:0000313|Proteomes:UP000009168};
KW Transferase {ECO:0000313|EMBL:EAS05738.3}.
FT DOMAIN 41..404
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 574..935
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 93..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..832
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 949 AA; 110649 MW; 896EA2FE1E3F44F0 CRC64;
MGGCQSEQKE KPVELVEAKD ARDVVDQYNK YQSIGIQKEK LEFRYVYAFK FKNELYEVVK
VYLEPVKIPD FRYQSDTRDD WEKILIKKVN QSDYQAQPEQ QSQANPKEVQ SNENDGDEED
DYLLMMNLLN QNTALVHEKQ VRFFEKLKHP NLVEYMDHYR INNQLTAFKE YCPQGGLIKY
LERNKKELNA DILFDLIEDV CNALKFLYDR AVVDFELSLE MIYVSNNIIK IDLYNGVKMD
EKVIRRLLNE GHKSDSQVFN NLILNSRVQM PTHQFKPVQT AQSTLKTSQK TRIVIDDQAQ
FVEQIQKKFK VDENKINIDF VRLFCLYILF DQDFRVMLKE KQAIPNTRQF SNKGQTQTMA
YKEIDVSEIK EVNKAPKDLK EFMQWTLNQI KSIRPNLTEL HKEIQRIRYQ ADVITYINQL
YIRNASKKQS NQSELPGDEK LKGYQSHYLH TTMYDDCKQN DDDEDFNEQK DELHESSTNA
KQIIFNRHLI KKSAAQKIEQ EEESVQNQLN NSIQNSLNID TVSFNNNHDS VDKQQKKNVK
IWEEVEEIPQ NQIKKIINPT DLMNVQFKFY EENYYVASLI NKSEYGLGFR IENVIKSQPR
ALCLKISKSK SYNPFLEKEF TILKQFGTPY IIKSYSQVHI KGLNGIVVDL YSQNLQQYLI
NSSKLDIACQ LIEFLHQFLS GLHELHVKDI IHRQLSFESI CIQSPSSSAQ NKTIAKISNL
ELAIQLKSQN YISSDIPLNS YSSPEMREKQ AYGIASDVFS AGVIILSALC NVSPKKIQSI
ACPDLLPQGK QNLYVSHIVD QKVDLQQSHY QRVFSKIQKK QPKDEQRKIG TSETKGTTES
NIFKSHSILV DSSPSQSKNQ SKNEIELQQS AMNSQRVQTS RQNINQKGLR EVLGEKCPQL
IIDTFEKMIS KYPQIRGNCS DYLSDLQRLK NQPEVINYVN MQNKQTRLI
//
