ID A0A1F9X9Y9_9BACT Unreviewed; 298 AA.
AC A0A1F9X9Y9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Response regulatory domain-containing protein {ECO:0000259|PROSITE:PS50110};
GN ORFNames=A2314_00985 {ECO:0000313|EMBL:OGS24200.1};
OS Elusimicrobia bacterium RIFOXYB2_FULL_50_12.
OC Bacteria; Elusimicrobiota.
OX NCBI_TaxID=1797969 {ECO:0000313|EMBL:OGS24200.1, ECO:0000313|Proteomes:UP000176658};
RN [1] {ECO:0000313|EMBL:OGS24200.1, ECO:0000313|Proteomes:UP000176658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGS24200.1}.
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DR EMBL; MGVO01000057; OGS24200.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F9X9Y9; -.
DR STRING; 1797969.A2314_00985; -.
DR Proteomes; UP000176658; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; cd00156; REC; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR44591:SF3; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR44591; STRESS RESPONSE REGULATOR PROTEIN 1; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3..118
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 52
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 298 AA; 34183 MW; 4149A33D6A0FF756 CRC64;
MENILVVDDE VEIWKICERT LSRKDYIIHT ANNADEAADL LNDVVFDLAL VDLRMPGRID
GMELIRVIKE NNPNTQVIVV TAEESIQTAM DALSNGAFDY ILKPFNLQEL LESVERVMRH
GAGRNKNTIF RETNYLYQVF QKLENSKSKN ENLLEFIIRR AVKALKADAG SIHLYIPQRN
TLKIMAFCGS ELDRESEVKL GERIVGWVAE NKKPLLFNNQ LSEYPQFNDL TIRDYIASSM
IVPLVKHNTL LGVICLNRFT EKTNLKFTPS DLEALQLFAL HCSLIIALEH YNLIPRFN
//
