ID J9G7X2_9SPIT Unreviewed; 793 AA.
AC J9G7X2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=OXYTRI_15060 {ECO:0000313|EMBL:EJY86416.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY86416.1};
RN [1] {ECO:0000313|EMBL:EJY86416.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY86416.1};
RX PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT with 16,000 Tiny Chromosomes.";
RL PLoS Biol. 11:E1001473-E1001473(2013).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJY86416.1}.
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DR EMBL; AMCR01002193; EJY86416.1; -; Genomic_DNA.
DR AlphaFoldDB; J9G7X2; -.
DR EnsemblProtists; EJY86416; EJY86416; OXYTRI_15060.
DR OrthoDB; 1222064at2759; -.
DR GO; GO:0005524; F:ATP binding; 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; IPR004358; Sig_transdc_His_kin-like_C.
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; PF00512; HisKA; 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 ATP-binding {ECO:0000313|EMBL:EJY86416.1};
KW Nucleotide-binding {ECO:0000313|EMBL:EJY86416.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}.
FT DOMAIN 340..558
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 655..790
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 721
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 793 AA; 92164 MW; 84FF6A86FA9F9CB5 CRC64;
MQDTVNLKYL ILVEAHNHYR HEFKNNSSNY RQEIKRRIYH TEVKISYNIE RSNTNHCYLI
FILVVLQHFI KRILANNCIV AYNEPYGNLM KTTYVSLKQN QKLNEDLRNL LLNFPKPLLL
LDQKNKEVVL ANKEAFKLLS VDENKNILEI QNKLSQKILD PYNYIEGLGD TNFEEQQSEQ
ISSKSPITEQ ESAQQKYNLY EAIEKDQKDA CFLIKTTHNF ETGIPHQQNK QSNNLNAANQ
PKILEINGDQ QIQVQDVDHI GVDYEANNNY KNENLNQHSI LNHNDRNQPF IYSEIVNLML
QDMHFLNKEL RLVLFHRITS FVKYEKLKME NNFYEMITAT VSHDMRTPIN SITGLLDSLE
HFIQKSEGKK LIQVIRNSSK ILLFLVNDIL DFFMLKNGKF KSSLQEADPR NCLNEMIDMF
ELVASEKKIE MKAEFDPNMP EKLYFDEQRL KQVLINLITN ALKFTLKGQI TLSISYDFVD
HFLNIRVSDT GIGVKADDEK KLFKLFGKLD AEQQINTKGI GLGLNICKKV VEACGGEIYL
EPDQEEGACF CFNLKAYQDK KQISRREFQI NFDESNHESI HNISKSLNQE NLDLIEKCEN
SHQIFQSFML SMDQSSDRID FEPYLSSRSL LPRQQDTTDE LPIEQAICPC QSRPQILIVD
DNIFNIITLQ TILEMQFSQR VEKATNGLEG LEKIQERIQQ ESLQPCLCGK NNKNYKIVFM
DCNMPIMDGF EATEAIRKLQ NIEQEGLKII ALTANTNKSF KTKCFQSGMD QFMTKPVSAE
QLRQILIQQG LLP
//
