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Database: UniProt
Entry: A0A1Q8CRD2_9PSEU
LinkDB: A0A1Q8CRD2_9PSEU
Original site: A0A1Q8CRD2_9PSEU 
ID   A0A1Q8CRD2_9PSEU        Unreviewed;       449 AA.
AC   A0A1Q8CRD2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   18-JUN-2025, entry version 32.
DE   RecName: Full=RNA polymerase sigma factor SigA {ECO:0000256|HAMAP-Rule:MF_00963};
GN   Name=sigA {ECO:0000256|HAMAP-Rule:MF_00963};
GN   ORFNames=BU204_14545 {ECO:0000313|EMBL:OLF16912.1};
OS   Actinophytocola xanthii.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae.
OX   NCBI_TaxID=1912961 {ECO:0000313|EMBL:OLF16912.1, ECO:0000313|Proteomes:UP000185596};
RN   [1] {ECO:0000313|EMBL:OLF16912.1, ECO:0000313|Proteomes:UP000185596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11-183 {ECO:0000313|EMBL:OLF16912.1,
RC   ECO:0000313|Proteomes:UP000185596};
RA   Wang W., Yuan L.;
RT   "The draft genome sequence of Actinophytocola sp. 11-183.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Sigma factors are initiation factors that promote the
CC       attachment of RNA polymerase to specific initiation sites and are then
CC       released. This sigma factor is the primary sigma factor during
CC       exponential growth. {ECO:0000256|HAMAP-Rule:MF_00963}.
CC   -!- SUBUNIT: Interacts transiently with the RNA polymerase catalytic core.
CC       {ECO:0000256|HAMAP-Rule:MF_00963}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00963}.
CC   -!- SIMILARITY: Belongs to the sigma-70 factor family. RpoD/SigA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00963}.
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:OLF16912.1}.
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DR   EMBL; MSIE01000024; OLF16912.1; -; Genomic_DNA.
DR   RefSeq; WP_075126185.1; NZ_MSIE01000024.1.
DR   AlphaFoldDB; A0A1Q8CRD2; -.
DR   STRING; 1912961.BU204_14545; -.
DR   OrthoDB; 9809557at2; -.
DR   Proteomes; UP000185596; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006352; P:DNA-templated transcription initiation; IEA:UniProtKB-UniRule.
DR   CDD; cd06171; Sigma70_r4; 1.
DR   FunFam; 1.10.10.10:FF:000002; RNA polymerase sigma factor SigA; 1.
DR   FunFam; 1.10.10.10:FF:000004; RNA polymerase sigma factor SigA; 1.
DR   FunFam; 1.10.601.10:FF:000001; RNA polymerase sigma factor SigA; 1.
DR   FunFam; 1.10.601.10:FF:000003; RNA polymerase sigma factor SigA; 1.
DR   Gene3D; 1.10.601.10; RNA Polymerase Primary Sigma Factor; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR   HAMAP; MF_00963; Sigma70_RpoD_SigA; 1.
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; IPR012760; RNA_pol_sigma_RpoD_C.
DR   InterPro; IPR050239; Sigma-70_RNA_pol_init_factors.
DR   InterPro; IPR028630; Sigma70_RpoD.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   NCBIfam; NF004560; PRK05901.1-1; 1.
DR   NCBIfam; NF004561; PRK05901.1-3; 1.
DR   NCBIfam; NF005920; PRK07921.1; 1.
DR   NCBIfam; TIGR02393; RpoD_Cterm; 1.
DR   NCBIfam; TIGR02937; sigma70-ECF; 1.
DR   PANTHER; PTHR30603:SF59; RNA POLYMERASE PRINCIPAL SIGMA FACTOR HRDA; 1.
DR   PANTHER; PTHR30603; RNA POLYMERASE SIGMA FACTOR RPO; 1.
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; SSF88946; Sigma2 domain of RNA polymerase sigma factors; 1.
DR   SUPFAM; SSF88659; Sigma3 and sigma4 domains of RNA polymerase sigma factors; 2.
DR   PROSITE; PS00715; SIGMA70_1; 1.
DR   PROSITE; PS00716; SIGMA70_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00963};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00963}; Reference proteome {ECO:0000313|Proteomes:UP000185596};
KW   Sigma factor {ECO:0000256|ARBA:ARBA00023082, ECO:0000256|HAMAP-
KW   Rule:MF_00963};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00963};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW   Rule:MF_00963}.
FT   DOMAIN          240..253
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00715"
FT   DOMAIN          409..435
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00716"
FT   DNA_BIND        410..429
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          1..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          216..286
FT                   /note="Sigma-70 factor domain-2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          295..371
FT                   /note="Sigma-70 factor domain-3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          384..437
FT                   /note="Sigma-70 factor domain-4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   MOTIF           240..243
FT                   /note="Interaction with polymerase core subunit RpoC"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   COMPBIAS        1..15
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..60
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..70
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..109
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..121
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..139
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   449 AA;  49987 MW;  E6C3984C1D588768 CRC64;
     MAAARTATRR STASAGDAKP ADAQPDTEST EKPALKTATK KPATRAPRKT AAKSAGAKKT
     KAGETTKKAD GAGAEPDGDE PDLESPDLED LEDVEVDIVE EPVAEEEPAE EKSGKETKDG
     DFVWDEEESE ALRQARKDAE LTASADSVRA YLKQIGKVAL LNAEEEVELA KRIEAGLYAA
     ERVRKAEEES SEKLAPQMRR DLRWIVRDGE RAKNHLLEAN LRLVVSLAKR YTGRGMAFLD
     LIQEGNLGLI RAVEKFDYTK GYKFSTYATW WIRQAITRAM ADQARTIRIP VHMVEVINKL
     GRIQRELLQD LGREPTPEEL AKEMDITPEK VLEIQQYARE PISLDQTIGD EGDSQLGDFI
     EDSEAVVAVD AVSFTLLQDQ LQSVLATLSE REAGVVRLRF GLTDGQPRTL DEIGQVYGVT
     RERIRQIESK TMSKLRHPSR SQVLRDYLE
//
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