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Database: UniProt
Entry: A0A139XFX4_9CYAN
LinkDB: A0A139XFX4_9CYAN
Original site: A0A139XFX4_9CYAN 
ID   A0A139XFX4_9CYAN        Unreviewed;       608 AA.
AC   A0A139XFX4;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Transcriptional regulator {ECO:0000313|EMBL:KYC43522.1};
GN   ORFNames=WA1_10695 {ECO:0000313|EMBL:KYC43522.1};
OS   Scytonema hofmannii PCC 7110.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC   Scytonema.
OX   NCBI_TaxID=128403 {ECO:0000313|EMBL:KYC43522.1, ECO:0000313|Proteomes:UP000076925};
RN   [1] {ECO:0000313|EMBL:KYC43522.1, ECO:0000313|Proteomes:UP000076925}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7110 {ECO:0000313|EMBL:KYC43522.1,
RC   ECO:0000313|Proteomes:UP000076925};
RX   PubMed=23221676; DOI=10.1093/gbe/evs117;
RA   Dagan T., Roettger M., Stucken K., Landan G., Koch R., Major P.,
RA   Gould S.B., Goremykin V.V., Rippka R., Tandeau de Marsac N., Gugger M.,
RA   Lockhart P.J., Allen J.F., Brune I., Maus I., Puhler A., Martin W.F.;
RT   "Genomes of Stigonematalean cyanobacteria (subsection V) and the evolution
RT   of oxygenic photosynthesis from prokaryotes to plastids.";
RL   Genome Biol. Evol. 5:31-44(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:KYC43522.1}.
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DR   EMBL; ANNX02000013; KYC43522.1; -; Genomic_DNA.
DR   RefSeq; WP_017744002.1; NZ_KQ976354.1.
DR   AlphaFoldDB; A0A139XFX4; -.
DR   STRING; 128403.WA1_10695; -.
DR   OrthoDB; 442759at2; -.
DR   Proteomes; UP000076925; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
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; cd00088; HPT; 1.
DR   CDD; cd00156; REC; 2.
DR   CDD; cd00383; trans_reg_C; 1.
DR   Gene3D; 3.40.50.2300; -; 3.
DR   Gene3D; 1.20.120.160; HPT domain; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR036641; HPT_dom_sf.
DR   InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR039420; WalR-like.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR48111; REGULATOR OF RPOS; 1.
DR   PANTHER; PTHR48111:SF1; TWO-COMPONENT RESPONSE REGULATOR ORR33; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   Pfam; PF00072; Response_reg; 3.
DR   Pfam; PF00486; Trans_reg_C; 1.
DR   SMART; SM00448; REC; 3.
DR   SMART; SM00862; Trans_reg_C; 1.
DR   SUPFAM; SSF46894; C-terminal effector domain of the bipartite response regulators; 1.
DR   SUPFAM; SSF52172; CheY-like; 3.
DR   SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   PROSITE; PS51755; OMPR_PHOB; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU01091}; Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076925}.
FT   DOMAIN          2..116
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          124..222
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51755"
FT   DOMAIN          357..473
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          484..600
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DNA_BIND        124..222
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01091"
FT   MOD_RES         51
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         406
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         533
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   608 AA;  68162 MW;  EBC4B2495F5FAEB6 CRC64;
     MKILLVEDDR PTSLVVSDIL IAHNYTVNQA MDGQTGLELA KAFEYDLVLL DIMLPDMDGI
     SVCRRLRSLG YQSPILLLTG KDSTTDRVMG LDAGADDYVV KPFEMNELLA RVRALLRRGK
     TVPSSVIVWE DIHFDTVNNQ VTCGQKPLRL TPKEYCLLEL FLLNPKRVFS RKAVLEKLWD
     FADSPGEETV STHIKCLRQK FRAAGASDPI ETVHGLGYRL KTPSKSKEDD FSVKQTINQK
     KVKATTSKVW EKFKGKYVEH FAVLEQATSA LATGQLTPEL LQQAKYEAHT LAGSLGIFGL
     MHGSELAREL EDFFQPYKQL QADDVKQIVM VVELLGQELQ KTPISETEGE QSSDSPLILI
     VDDDLMLAER IRIEAIAWKL RVEVATDLEV ARKVIAQTPP NVILLDLNFP SSTEDGLTLL
     HELAQQIPKI PVLVFSGEGS LANRLEVARL GGCIFLQKPQ SSYSILKVVT KVLSSTQETS
     SGNRVMVVDK DEAALSHLTN LLQPLGVEVT TLSDPHQFWE VLIASRPDLL ILDVEMPELN
     SLELCQVVRC DPKWYRIPII FWSARTQKSE IDKAFAVGAD DYINKSVEEA ELTTRVLRRL
     SRIRKQQV
//
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