ID Q22D61_TETTS Unreviewed; 1398 AA.
AC Q22D61;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 2.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=TTHERM_01002570 {ECO:0000313|EMBL:EAR83192.2};
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:EAR83192.2, 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).
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DR EMBL; GG662361; EAR83192.2; -; Genomic_DNA.
DR RefSeq; XP_001030855.2; XM_001030855.2.
DR STRING; 312017.Q22D61; -.
DR EnsemblProtists; EAR83192; EAR83192; TTHERM_01002570.
DR GeneID; 7832161; -.
DR KEGG; tet:TTHERM_01002570; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_297474_0_0_1; -.
DR InParanoid; Q22D61; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EAR83192.2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000009168};
KW Transferase {ECO:0000313|EMBL:EAR83192.2}.
FT DOMAIN 652..884
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1264..1390
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1166..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1320
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1398 AA; 162314 MW; AF86CB8A0C6E35ED CRC64;
MSLINNSRIL NVLLIQVTYI EVRNIIGING IDLYTSIQLG VTLAFVYAAS ITSQEVYKMD
SIIDNINYSY NNQNKMDKQP EIFLNCKTLE IKNKIRCTSP SINLHEKVLQ HNAEFIQYAQ
NSLMDDSKCH IQREYNSKSI NNIELMNILE QTNVQQTQNS DLLKISQLSQ YFQIFSTGFS
IIDQNQNVIF QNKAVENIVF QYGLIKNIDQ ASCLNFEQGN KQGLLEIKIK FENDEVQNQK
VHSQKNQKQI VQSSSQNIQK DILNIDQKLF SEKNIDEFHT NTEEAKYENQ NLDNSKKLFT
CETDQNENLL NKMKNDKEIN IFFKQKNNDE NDNFDINNQQ NVFYYNQIQN NQNSQNNISF
FSDSQEIRQQ QNFLNNLNQI NSQAINVNQS LQKIFLSKNL ICDIKTATLK FFSRYNEEAS
LGDLINFIIL SRPYPQINNC SQVLLEPQEI GLSPLIHRKF CKNKKPTNQN SLDQAYKYSF
IDDYLILTLN RKNKSNKNLL IEIKIGCFQF EDDQKEKMNS NTNKSIKSSN NKINNIKVIN
DLNDIKFVSS SLINQHQCNN IKRPSLPTQK ASGFYYLQSK DQQNQNSIKP QGFYDGNFQQ
SKSNLKINTL NCSKNICFKK YFFTIEFNQI SPQFKGVVKN QVNQQKAQIY KQISLELSTP
LSCIINMLDL INSRESTHEF VKNSFINPAL FQSYILLNIV NDLQEKSEIT QPGKVNIILQ
TFSLSDLCLE CLNFIKLPAI KKNIQLEFYS KENVPQMIYS DLSKVRQILI NLLTNALKNT
QKGNICISLS QPFKNFIQVD VKDSGEGIPS DELIQMFQNL YQSTQQHINM RKDKQQDFYH
DSNMSQGLKI CYLLSICLGQ NRPLTASSEV AKGSIFTFYI KNTKKMAKQK KISLDCNKLI
QFEYFQKENS DKRDQETILD LKQIFKLDEK SEKNKNMLDI KNKTENQNNN QRAHKNTMME
STELQSSFIS VEENNQDLNE SLNSSIQNNS SNYKISFLTQ NMIKQSQFIY QIVNKMLSQM
TLEGSQYGQS TFRSKYQENQ KQKSQQDQFN NQLNQINKYN QIQESQFSNQ NIQQDKNFQI
SNQNLMPNLK FEENNINNTQ AQFIQSKQDI DYEFSVFNIN NKAEDNLQES CNIFPAESLE
KLEPNTFIQP RIAQKSNKED QDHIKNLSPF IQPNTPKHIQ PNSQQPISSN SNYYTNSNSF
NNQSRRVSQI VLKTEPSIYH SDSNIGEQKA QLLYFNVTNG FYVNGDIQNN LIQLNQNRKC
DCSQILLIDD NDFNLCALEL RLRQYLFIIE KASSGQQALK LIEQKSINSC CRTFTLVFLD
LDMPVRNGFE VLVDIVDICN DLLIKVPSIS AWTALLSEKD QQKATDFGMS HYLTKPLNLQ
ALENVLFEEF ILKQKKQL
//
