ID A0A1B6Y993_9BACT Unreviewed; 555 AA.
AC A0A1B6Y993;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Fused response regulator/thioredoxin-disulfide reductase {ECO:0000313|EMBL:OAN61730.1};
GN ORFNames=A8B79_04700 {ECO:0000313|EMBL:OAN61730.1};
OS Balneola sp. EhC07.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Balneola.
OX NCBI_TaxID=1849360 {ECO:0000313|EMBL:OAN61730.1, ECO:0000313|Proteomes:UP000078514};
RN [1] {ECO:0000313|EMBL:OAN61730.1, ECO:0000313|Proteomes:UP000078514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EhC08 {ECO:0000313|EMBL:OAN61730.1,
RC ECO:0000313|Proteomes:UP000078514};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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:OAN61730.1}.
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DR EMBL; LXYG01000016; OAN61730.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B6Y993; -.
DR STRING; 1849360.A8B79_04700; -.
DR InParanoid; A0A1B6Y993; -.
DR OrthoDB; 109585at2; -.
DR Proteomes; UP000078514; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd17595; REC_TrxB; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR48105:SF5; BLR1248 PROTEIN; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000078514}.
FT DOMAIN 5..128
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 62
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 555 AA; 61499 MW; 1346018D5A83A434 CRC64;
MKKPIIFTID DDAQVLRAIT RDLRSNYRKD YRVMSTQSPK EALSSLPELK KQGETVALFL
SDQRMPDMIG VDFLEKAKGY FPEAKRVLLT AYSDTDAAIR AINEVQLDYY LLKPWDPPEE
KLYPVLDDLL DEWQANFRPD FTGIRLVGYQ YSPKSHTVKD YLSGNLIPYR WLDIEENAKA
AELLEENQID QKDLPAIFFE DGEFLIDPSP IQIANKLGKN PSASKNVYDV VIVGAGPAGL
AAAVYGGSEG LKTLLIEKRA PGGQAGTSSR IENYLGFPKG LSGSDLARRA ITQATRFGVE
FLSPQEVIDI KLNDQYKTVC LADGSEINAK AVIVTTGVNY RKLESKGISD FTGAGIYYGA
AMTEAHAFKD KQVYIVGGGN SAGQAAMYLS TFAKKVYITI RKDSLVSSMS SYLIDQINRT
ENIELLGNRE IVEASGNGHL QGLKLLNNVD ESESEVEADG LFIFIGAKPY TDWIHDNVIK
NERGFIETGR DLQRYDDYSK VWKLERQPYL LESCAPGIFA AGDVRAGAMN RVASAVGEGS
MAIKYVHEYL ADSNL
//
