ID A0A1H9WQH6_9PSEU Unreviewed; 1440 AA.
AC A0A1H9WQH6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=DNA-binding transcriptional activator of the SARP family {ECO:0000313|EMBL:SES36178.1};
GN ORFNames=SAMN04487818_11192 {ECO:0000313|EMBL:SES36178.1};
OS Actinokineospora terrae.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=155974 {ECO:0000313|EMBL:SES36178.1, ECO:0000313|Proteomes:UP000199051};
RN [1] {ECO:0000313|EMBL:SES36178.1, ECO:0000313|Proteomes:UP000199051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44260 {ECO:0000313|EMBL:SES36178.1,
RC ECO:0000313|Proteomes:UP000199051};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the AfsR/DnrI/RedD regulatory family.
CC {ECO:0000256|ARBA:ARBA00005820}.
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DR EMBL; FOGI01000011; SES36178.1; -; Genomic_DNA.
DR STRING; 155974.SAMN04487818_11192; -.
DR Proteomes; UP000199051; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR005158; BTAD.
DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR SMART; SM01043; BTAD; 1.
DR SMART; SM00862; Trans_reg_C; 1.
DR SUPFAM; SSF46894; C-terminal effector domain of the bipartite response regulators; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000313|EMBL:SES36178.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000199051};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 66..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 790..869
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000259|SMART:SM00862"
FT DOMAIN 876..1015
FT /note="Bacterial transcriptional activator"
FT /evidence="ECO:0000259|SMART:SM01043"
FT REGION 251..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1214..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1346..1371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..308
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1244..1258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1440 AA; 153795 MW; 475F175C20051F22 CRC64;
MWQGIGWVLG FLARLVRALL AAAVLVALLA GLPWALTHFV GWPLPDHLPS WAEVQGVLLG
PMTTTFLLDF LACLTWLVWA FFTLDVARCA VEIARDAAMP DLSAAGPVHR IAAVLVGAVL
ISILGHRAGL PATSPSAADG AAADVVATAP AWNTSTEPAE FTGVRPAAHS VPYPHKATGA
TEQPSRAKSA VVLSYNPDTG VYDSLWRMSE RTLGDGNRWP EIYALNKGKP QPNGGTFTRP
SLIFPGEEMA LPDDATISSP PATAPVPPPV TPPPAPEPPP TSTTTPAPST TEPPATTEAP
PTTQAPPTTQ APPSTDAVGE PGISWGEELF VGLGLAAAVS AALVATRRRN RRRYQPGSGD
RSDLPVAPVV YQLRLAHLRA DHDDTTSADD EVDLDWPSER PPRRPAPPLV LGTHADTDIP
DDQSPVLPVG VRVGREVAVD IASAHGLGLL GAGAPAAVRA LLVTILSTAF TTTHRPATVI
VPVDDLAALF GRRVAQAPLP AGVRVAADLD AALDMLESET LVRVGQLRPT GQPWEPVVLA
ARAPGRQARR LQAVLDNGST VGVTGLLLGQ WSAGVTAYVR DDGTISTTSP GLGEPLRGAR
VFRLGDDHLA DLLDLLRDAN PGDESELTAT AGDEPYPAVV PRPHVVVAGS VPVTVEPPDT
VVDRGARTDD RGHAVGEDTS QSPVADTDLE LLAAPSDDDR RGDGELEILR PEPAPATSPG
LRLRPVQPVR PDAEQATQNA GESHRPAGSR PQGPAEPREV SSAPLRVSVL GPPRVWWRPE
PATPDGEAAE REITSAFQPR LRELLVFLAL HPDGASREAL IAALWATSPP ERTTNAMNTS
LSRLRRALAA ATGNVLSDLV VVGEGRYRLD PDLVEIDYHH FAAAVAARRT AVTDADRVEA
YRRIVDSYTG PLADGLSTDW IETAREAIRR DAIDAVAALA RALVEDDPQQ TLDLLEIARA
FDPHNELIYR DIMRLQERLG QLDAIPRTLT LLTTRLAEVD DRPTHQAVDL ADRLRRRHDA
PGEAGASRPR AQPSRMNPAG TLVRGVGSPD AATGTRATSS GVEPAVTGRG VEIHDIIENG
RLLATATAVR LRLREQFRMS TSPLEQRLCQ RQHLGHRRGQ RVRDFRRKRL IATLADDESL
LAHLFQCARQ NAIVQYSVFV RPILVDGIRV HRGKNLYPTQ RAVPECHQDG GHPLVPEKVL
QVVHSTKDPV VSLRHRASPC ALTGPPLRAR SSRPAARPSP SLPSRRSCLL SATAPSPTAS
PGDGRRAPTL RQTVEIAHRI PTQPNSDEMS PGVAGMEIDS AYGHFRWGFI RGITLGIRLG
ILLERHPLRP VKTPVRGVVG GSAGIPDSLG HKPVNTSGRT GGRLPALSGS SSPLPRDCVL
SALIPPLLMF SKLLSFIPYA SPAFVCPLVS CCLLRSLACG NAMAFRSEMR GRTLAQFPEW
//