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
//