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Database: UniProt
Entry: A0CG83_PARTE
LinkDB: A0CG83_PARTE
Original site: A0CG83_PARTE 
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
//
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