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Database: UniProt
Entry: A0A2T1DH88_9CYAN
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ID   A0A2T1DH88_9CYAN        Unreviewed;       174 AA.
AC   A0A2T1DH88;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Transcriptional repressor NrdR {ECO:0000256|HAMAP-Rule:MF_00440};
GN   Name=nrdR {ECO:0000256|HAMAP-Rule:MF_00440};
GN   ORFNames=C7B65_09340 {ECO:0000313|EMBL:PSB19870.1};
OS   Phormidesmis priestleyi ULC007.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC   Phormidesmis.
OX   NCBI_TaxID=1920490 {ECO:0000313|EMBL:PSB19870.1, ECO:0000313|Proteomes:UP000238634};
RN   [1] {ECO:0000313|EMBL:PSB19870.1, ECO:0000313|Proteomes:UP000238634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULC007 {ECO:0000313|EMBL:PSB19870.1,
RC   ECO:0000313|Proteomes:UP000238634};
RA   Cohen D.B., Kent A.D.;
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PSB19870.1, ECO:0000313|Proteomes:UP000238634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULC007 {ECO:0000313|EMBL:PSB19870.1,
RC   ECO:0000313|Proteomes:UP000238634};
RA   Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT   "The ancient ancestry and fast evolution of plastids.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Negatively regulates transcription of bacterial
CC       ribonucleotide reductase nrd genes and operons by binding to NrdR-
CC       boxes. {ECO:0000256|HAMAP-Rule:MF_00440}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00440};
CC       Note=Binds 1 zinc ion. {ECO:0000256|HAMAP-Rule:MF_00440};
CC   -!- SIMILARITY: Belongs to the NrdR family. {ECO:0000256|HAMAP-
CC       Rule:MF_00440}.
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:PSB19870.1}.
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DR   EMBL; PVWG01000008; PSB19870.1; -; Genomic_DNA.
DR   RefSeq; WP_073071011.1; NZ_PVWG01000008.1.
DR   AlphaFoldDB; A0A2T1DH88; -.
DR   STRING; 1920490.GCA_001895925_03909; -.
DR   OrthoDB; 9807461at2; -.
DR   Proteomes; UP000238634; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00440; NrdR; 1.
DR   InterPro; IPR005144; ATP-cone_dom.
DR   InterPro; IPR003796; RNR_NrdR-like.
DR   NCBIfam; TIGR00244; transcriptional regulator NrdR; 1.
DR   PANTHER; PTHR30455; TRANSCRIPTIONAL REPRESSOR NRDR; 1.
DR   PANTHER; PTHR30455:SF2; TRANSCRIPTIONAL REPRESSOR NRDR; 1.
DR   Pfam; PF03477; ATP-cone; 1.
DR   PROSITE; PS51161; ATP_CONE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00440};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00440}; Metal-binding {ECO:0000256|HAMAP-Rule:MF_00440};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00440}; Reference proteome {ECO:0000313|Proteomes:UP000238634};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491, ECO:0000256|HAMAP-Rule:MF_00440};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00440};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW   Rule:MF_00440}; Zinc {ECO:0000256|HAMAP-Rule:MF_00440};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00440}.
FT   DOMAIN          49..139
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
FT   ZN_FING         3..34
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00440"
SQ   SEQUENCE   174 AA;  20231 MW;  28421A53C7953E9F CRC64;
     MRCPSCHHPD NRVLESRSAE AGQSVRRRRE CLRCNHRFTT YERIEFVPIV VLKRNGERES
     FDRSKLLREL VRACEKTAIL EPRIEILAEE IESDLQQRVG REVTSAEIIE LVLHHLRSLS
     EVAYIRYASI YCQFAGIQDF VDAIDRLHDR VEPSHPSNQQ SDPEALSEIN AFNC
//
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