ID A0CG83_PARTE Unreviewed; 863 AA.
AC A0CG83;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 24-JAN-2024, entry version 80.
DE SubName: Full=Chromosome undetermined scaffold_179, whole genome shotgun sequence {ECO:0000313|EMBL:CAK69800.1};
GN ORFNames=GSPATT00038245001 {ECO:0000313|EMBL:CAK69800.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK69800.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK69800.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK69800.1,
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; CT868073; CAK69800.1; -; Genomic_DNA.
DR RefSeq; XP_001437197.1; XM_001437160.1.
DR AlphaFoldDB; A0CG83; -.
DR STRING; 5888.A0CG83; -.
DR EnsemblProtists; CAK69800; CAK69800; GSPATT00038245001.
DR GeneID; 5022982; -.
DR KEGG; ptm:GSPATT00038245001; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_331642_0_0_1; -.
DR InParanoid; A0CG83; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
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; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK1-RELATED; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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 SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 30..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 103..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 129..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 468..691
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 735..863
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 360..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 793
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 863 AA; 99833 MW; 20603B6BD58F0D4E CRC64;
MNNVNLRVVI QLAYFILVLT IKLVNHNSEY FQVILSMILT MLFIPFNRYV NTCVEQQQLI
FKSLCVDLGL INDGFLSRFQ YFWLGLTIQL EFDSTIQNQI VRVGYLLVVI ASANLTSIYL
LIDSSAIGII FGEALYGLLL LYQFIVKTNQ QVKKLPLQKP CSHSFTEKIE SPQQQIFDED
SNQIKFMPLN QGLGKNSSLY SRDPSVLEQI EQQKTFYEIL FNQFPEGILI INDQNKIDYH
NNQVYNLLGR KHIQNRQDQI LPRLYELKNY SSKFQFEEQA QFDKFFSNLD KKLKFNQREY
NQPFDQQFDQ QINNENSKES IFNNNFDDNQ TDYYFQAELS KAETLKQELD KALSEKVTEK
NGLSSPFQRQ QSFPSQRTYK GQDKIKFSPE VKKMLCMIEE SSEDHDNELQ EDKSQSECNT
GLLIQITIKP YIYENKRSVL LLIRDVSLFN QFKVLQQQNK NKSRMLAYVS HELRNPLGAI
IEINQQLKIQ FQQDNNLISK YLQPLQSSAI SIQGLANDLL DLAQLKAGKF NLTCKDFSIY
QLLNDAISIM QYPVSLRNLK LDLQYDDKIP QIINSDSQRI QQIIFNLISN ATKFTKVGGI
TVTAKLLQPK LIEICVEDTG VGLKPEDKNK LFQPFGKLED TKNMNTSGVG LGLMISNVLA
QKLSGNDEGL QVDSKGVDKG TRFVFKIQDV SENQASTPKE SKALIMKESS HRNILIQKRF
EDLSMEPLQN CKCPKIIIAD DEPINLQTLG WKLDRMKYTY LKAQSGQECI EILQNWYKNQ
DYCCNWIKFI ILDINMPYLN GYQTSKLVRQ MEVEKQVKRC KIIGCSGFTD NESKRVGFES
GMDIFISKPI EDKELQSALQ QLQ
//