HRDD_STRCO
ID HRDD_STRCO Reviewed; 332 AA.
AC P18249; Q9KYU3;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 2.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=RNA polymerase principal sigma factor HrdD;
GN Name=hrdD; OrderedLocusNames=SCO3202; ORFNames=SCE22.19c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=1944221; DOI=10.1007/bf00267453;
RA Tanaka K., Shiina T., Takahashi H.;
RT "Nucleotide sequence of genes hrdA, hrdC, and hrdD from Streptomyces
RT coelicolor A3(2) having similarity to rpoD genes.";
RL Mol. Gen. Genet. 229:334-340(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 128-179.
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=3194753; DOI=10.1126/science.3194753;
RA Tanaka K., Shiina T., Takahashi H.;
RT "Multiple principal sigma factor homologs in eubacteria: identification of
RT the 'rpoD box'.";
RL Science 242:1040-1042(1988).
CC -!- FUNCTION: Sigma factors are initiation factors that promote the
CC attachment of RNA polymerase to specific initiation sites and are then
CC released. {ECO:0000250}.
CC -!- SUBUNIT: Interacts transiently with the RNA polymerase catalytic core.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sigma-70 factor family. {ECO:0000305}.
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DR EMBL; X52982; CAA37174.1; -; Genomic_DNA.
DR EMBL; AL939115; CAB90986.1; -; Genomic_DNA.
DR PIR; D40116; D40116.
DR PIR; S17931; S11714.
DR RefSeq; NP_627416.1; NC_003888.3.
DR RefSeq; WP_003975615.1; NZ_VNID01000013.1.
DR AlphaFoldDB; P18249; -.
DR SMR; P18249; -.
DR STRING; 100226.SCO3202; -.
DR GeneID; 1098636; -.
DR KEGG; sco:SCO3202; -.
DR PATRIC; fig|100226.15.peg.3262; -.
DR eggNOG; COG0568; Bacteria.
DR HOGENOM; CLU_014793_3_4_11; -.
DR InParanoid; P18249; -.
DR OMA; RRVQREF; -.
DR PhylomeDB; P18249; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 2.
DR InterPro; IPR014284; RNA_pol_sigma-70_dom.
DR InterPro; IPR000943; RNA_pol_sigma70.
DR InterPro; IPR009042; RNA_pol_sigma70_r1_2.
DR InterPro; IPR007627; RNA_pol_sigma70_r2.
DR InterPro; IPR007624; RNA_pol_sigma70_r3.
DR InterPro; IPR007630; RNA_pol_sigma70_r4.
DR InterPro; IPR013325; RNA_pol_sigma_r2.
DR InterPro; IPR013324; RNA_pol_sigma_r3/r4-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF00140; Sigma70_r1_2; 1.
DR Pfam; PF04542; Sigma70_r2; 1.
DR Pfam; PF04539; Sigma70_r3; 1.
DR Pfam; PF04545; Sigma70_r4; 1.
DR PRINTS; PR00046; SIGMA70FCT.
DR SUPFAM; SSF88659; SSF88659; 2.
DR SUPFAM; SSF88946; SSF88946; 1.
DR TIGRFAMs; TIGR02937; sigma70-ECF; 1.
DR PROSITE; PS00715; SIGMA70_1; 1.
DR PROSITE; PS00716; SIGMA70_2; 1.
PE 3: Inferred from homology;
KW DNA-binding; Reference proteome; Sigma factor; Transcription;
KW Transcription regulation.
FT CHAIN 1..332
FT /note="RNA polymerase principal sigma factor HrdD"
FT /id="PRO_0000093994"
FT DNA_BIND 294..313
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 124..137
FT /note="Polymerase core binding"
FT CONFLICT 148
FT /note="F -> I (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="Q -> H (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="T -> H (in Ref. 1; CAA37174)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 37155 MW; BEAC010BBC0C442B CRC64;
MATRAVARRK SAAGETSGSA TSVRANGGEL ADRDLVGMYL DEIARTPLLD AAKEVELSQT
IEAGVFARQV LEGYEETGAD ATREELQALI DESERAKDVF IRSNLRLVVA VARRYPRSGL
PLLDLIQEGN AGLVRAVEKF DYRKGFKFST YATWWIRQAI TRSIADQSRT IRLPVHLVEE
LGRIRRVQRE FNREHGREPE PAEIAAELGS TPERVTDVLD WARDPVSLNM SVDDEGETQF
GDLLEDTSAV SPEQSVLTLL RSEELDDLIG RLDPRTASII KMRYGIDDGR ERTLTEVGKE
HGLTRERIRQ IEKHALLELK KLARDTGFEA AA