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Database: UniProt
Entry: Q22C41_TETTS
LinkDB: Q22C41_TETTS
Original site: Q22C41_TETTS 
ID   Q22C41_TETTS            Unreviewed;       802 AA.
AC   Q22C41;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 2.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=Serine/threonine-protein kinase PLK {ECO:0000256|RuleBase:RU361162};
DE            EC=2.7.11.21 {ECO:0000256|RuleBase:RU361162};
DE   AltName: Full=Polo-like kinase {ECO:0000256|RuleBase:RU361162};
GN   ORFNames=TTHERM_01076980 {ECO:0000313|EMBL:EAR82871.2};
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:EAR82871.2, 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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.21; Evidence={ECO:0000256|RuleBase:RU361162};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. CDC5/Polo subfamily. {ECO:0000256|RuleBase:RU361162}.
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DR   EMBL; GG662686; EAR82871.2; -; Genomic_DNA.
DR   RefSeq; XP_001030534.2; XM_001030534.3.
DR   AlphaFoldDB; Q22C41; -.
DR   STRING; 312017.Q22C41; -.
DR   EnsemblProtists; EAR82871; EAR82871; TTHERM_01076980.
DR   GeneID; 7822848; -.
DR   KEGG; tet:TTHERM_01076980; -.
DR   eggNOG; KOG0575; Eukaryota.
DR   HOGENOM; CLU_479429_0_0_1; -.
DR   InParanoid; Q22C41; -.
DR   OrthoDB; 5471704at2759; -.
DR   Proteomes; UP000009168; 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; cd13118; POLO_box_1; 1.
DR   CDD; cd13117; POLO_box_2; 1.
DR   CDD; cd14099; STKc_PLK; 1.
DR   Gene3D; 3.30.1120.30; POLO box domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR033701; POLO_box_1.
DR   InterPro; IPR033695; POLO_box_2.
DR   InterPro; IPR000959; POLO_box_dom.
DR   InterPro; IPR036947; POLO_box_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR   PANTHER; PTHR24345:SF0; SERINE_THREONINE-PROTEIN KINASE PLK1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00659; POLO_box; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF82615; Polo-box domain; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50078; POLO_BOX; 2.
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};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361162};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000009168};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU361162};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361162}.
FT   DOMAIN          46..301
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          504..570
FT                   /note="POLO box"
FT                   /evidence="ECO:0000259|PROSITE:PS50078"
FT   DOMAIN          616..683
FT                   /note="POLO box"
FT                   /evidence="ECO:0000259|PROSITE:PS50078"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          404..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          693..726
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          764..802
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        693..712
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         75
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   802 AA;  91634 MW;  1CA190DF61F7B33B CRC64;
     MSNQDKQQQQ QQQQPQGAQR AASDTEPLII EERVQIVNGE QIIKRYQRGS LLGKGGFAKC
     FQVTNLENKK VMAAKIIPKS TLVKNRARQK LISEIKIHKS LHHNNIVKFE HVFEDHDNVY
     ILLELCPHQT LNELIKRRKR ITELETLCYT VQIVQALKYL HQNRVIHRDL KLGNLFVGEK
     MEIKLGDFGL ATKLEFDGEK KRTICGTPNY IAPEILDGRV GHSYEVDIWS LGVILYTLLI
     GKPPFETHDV KTTYRKIKSN QYSFPDHAPI PDSAKALIQL ILQQDPAKRP TLDEILAHPF
     INNGGTIPRL LPVSTLTTAP NTSYIKQYAP SASNIKANQQ SMQIGTEVFG SSRKEMTKSQ
     TTTNMNKALF QNENGNKVLD GQKNQATSNP SNQFMSTANL QQNSKNLNSN FNQNDFNQTD
     QRPTTSKVQT GTQQGLYNKQ QTGTQDPNNK QQQGNKYQSV QNLMSMNKTD GFQNPQNQQQ
     LNGEENNQID GSKNNLWVVQ YVDYSSKYGL GYLLSNQSAG VVFNDTTKII LDPKAEYFEY
     IYKKDQDEIT EKHSLTEYPT DLQKKVTLLQ HFRHYLMTEV NKKVCAENGS TQATLYNDSK
     FQMQPNQPLP YLKKWMQTRH AIMFRLSNKI VQVQFSDKTE ILLNSTDKIV SFMNKKGERF
     HYPLADAMNS TNQDMTKRLR YTKEILTHLL KNNQRQNTND EQGNNAANSV APPDDMPQNE
     PNYNKYGMTA TMENEQFPKL NEQKLKGMTS QKSLTEKDQL IYNMTGFNNG SKTPSQQKNP
     SVTAYPNAQQ QPAQLADKNQ KK
//
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