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Database: UniProt
Entry: A0A3N6HFC3_9ACTN
LinkDB: A0A3N6HFC3_9ACTN
Original site: A0A3N6HFC3_9ACTN 
ID   A0A3N6HFC3_9ACTN        Unreviewed;      1019 AA.
AC   A0A3N6HFC3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Regulatory protein AfsR {ECO:0000313|EMBL:RPK83176.1};
GN   Name=afsR3 {ECO:0000313|EMBL:RPK83176.1};
GN   ORFNames=EES45_07725 {ECO:0000313|EMBL:RPK83176.1};
OS   Streptomyces sp. ADI97-07.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1522762 {ECO:0000313|EMBL:RPK83176.1, ECO:0000313|Proteomes:UP000281409};
RN   [1] {ECO:0000313|EMBL:RPK83176.1, ECO:0000313|Proteomes:UP000281409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ADI97-07 {ECO:0000313|EMBL:RPK83176.1,
RC   ECO:0000313|Proteomes:UP000281409};
RA   Guerrero-Garzon J.F., Zehl M., Urban E., Schneider O., Ruckert C.,
RA   Busche T., Kalinowski J., Zotchev S.B.;
RT   "Streptomyces spp. from the marine sponge Antho dichothoma: analyses of
RT   secondary metabolite biosynthesis gene clusters and some of their
RT   products.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the AfsR/DnrI/RedD regulatory family.
CC       {ECO:0000256|ARBA:ARBA00005820}.
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:RPK83176.1}.
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DR   EMBL; RPGY01000034; RPK83176.1; -; Genomic_DNA.
DR   RefSeq; WP_056789715.1; NZ_ML123098.1.
DR   AlphaFoldDB; A0A3N6HFC3; -.
DR   Proteomes; UP000281409; Unassembled WGS sequence.
DR   GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd15831; BTAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR   InterPro; IPR005158; BTAD.
DR   InterPro; IPR002182; NB-ARC.
DR   InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR35807:SF1; TRANSCRIPTIONAL REGULATOR REDD; 1.
DR   PANTHER; PTHR35807; TRANSCRIPTIONAL REGULATOR REDD-RELATED; 1.
DR   Pfam; PF03704; BTAD; 1.
DR   Pfam; PF00931; NB-ARC; 1.
DR   Pfam; PF13424; TPR_12; 2.
DR   PRINTS; PR00364; DISEASERSIST.
DR   SMART; SM01043; BTAD; 1.
DR   SMART; SM00028; TPR; 6.
DR   SMART; SM00862; Trans_reg_C; 1.
DR   SUPFAM; SSF46894; C-terminal effector domain of the bipartite response regulators; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48452; TPR-like; 3.
DR   PROSITE; PS50005; TPR; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000281409};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          30..98
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000259|SMART:SM00862"
FT   DOMAIN          105..249
FT                   /note="Bacterial transcriptional activator"
FT                   /evidence="ECO:0000259|SMART:SM01043"
FT   REPEAT          817..850
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ   SEQUENCE   1019 AA;  110062 MW;  88BD214FD4D47DFF CRC64;
     MGEDTGVHAI RFRILGSFEC WDGPDRVRVG GPVHEKVLVT LLLEPQRVLP VHRLVEAAWD
     ENAPATAAHQ VRKAVAELRQ RIPGGRNLIV TEGPGYRALT TPEQVDLSRF TEGLKQAREA
     TAAGQNAYAA TALREALDLW RGPLLSGSGG SVLCAASAAL EERRLTAVEQ LFDLRLAAGE
     NGELIGELRE FIEANPLRET LRGQLMLALF RSGRQAEALE EFAKVREYLV DELGIGPGDA
     LTDLHHAILR NSPELAAPAQ AAGPAPFTPE GSPSTLPYDL GDFTGREEEV SQLLGFVEEA
     PGTGPLIVAI DGMGGSGKTS LAVRAAHQLT ERYPDAQLHI DLRGFTPSEQ PLTAGAAAEA
     LLRMLGAPGE RIPDDAEGRI ALWRRTMSSR RMILLLDNAV DESQIRPLLA SPTQTLVLVT
     SRALLADLDA AHTVSLGVMP PHDSVALVEG VLGSSRARAE PEAVAQLAEL CGHLPLALRI
     AAARLRKRPR WTVRYLVDRL RDDAHRLAEL NSGERSVEVT LRLSYEGLSA ETREAFRLLG
     QHPGAEIEVY AAGALLDKRA RDAEDVLEYL LDMHLLQQHE TGRYAFHDLV RSFAQNLSRV
     GGRAGPETGD GDGDAGNEEA ALAVRRLLDF ALGATDAACD LLFPGRARIH RPEHRSTAEL
     PPLNTSDQAR DWLEREQDSL LAAVSLAYRW ELDSHVGLLA ANVVFPLDLR GRLEEFRELC
     RTAVTASRRL GDPALLRLSL SNLAVACWKL GRFEEGIEMA EEAFGLAVSL ADRRGEAKDT
     GVLGLLLGAL GRYGEALPRL EHSIAIKREL GAERAEAESL ANLSKLYAEW GRFPEAVEAA
     DRAVALSRSI GAVDKEVEGL TDLAVARLGL DAVDEAADLL RRARKLAVDV MSPADMSLLL
     ALSAETADRL GESTQATEWA EAALQLGDLS GAPMREAAVG NIVGRLHARR GRFTLALELH
     QQAHRAASGV DYRVEEARAL AGMAHAMERL GDHEAARTHL ATAEAAYDTM GIPAAGRTD
//
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