GenomeNet

Database: UniProt
Entry: E2S1F6_9CORY
LinkDB: E2S1F6_9CORY
Original site: E2S1F6_9CORY 
ID   E2S1F6_9CORY            Unreviewed;       490 AA.
AC   E2S1F6;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=RNA polymerase sigma factor SigA {ECO:0000256|HAMAP-Rule:MF_00963};
GN   Name=rpoD {ECO:0000313|EMBL:EFQ81472.1};
GN   Synonyms=sigA {ECO:0000256|HAMAP-Rule:MF_00963};
GN   ORFNames=HMPREF0305_10358 {ECO:0000313|EMBL:EFQ81472.1};
OS   Corynebacterium pseudogenitalium ATCC 33035.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=525264 {ECO:0000313|EMBL:EFQ81472.1, ECO:0000313|Proteomes:UP000003020};
RN   [1] {ECO:0000313|EMBL:EFQ81472.1, ECO:0000313|Proteomes:UP000003020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33035 {ECO:0000313|EMBL:EFQ81472.1,
RC   ECO:0000313|Proteomes:UP000003020};
RA   Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA   Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA   Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA   Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA   Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA   Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA   Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA   Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA   Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA   Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA   Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA   Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA   Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA   Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (AUG-2010) 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:EFQ81472.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ABYQ02000003; EFQ81472.1; -; Genomic_DNA.
DR   RefSeq; WP_005325028.1; NZ_GL542877.1.
DR   AlphaFoldDB; E2S1F6; -.
DR   eggNOG; COG0568; Bacteria.
DR   HOGENOM; CLU_014793_2_0_11; -.
DR   OrthoDB; 9809557at2; -.
DR   Proteomes; UP000003020; 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   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; IPR028630; Sigma70_RpoD.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   NCBIfam; TIGR02393; RpoD_Cterm; 1.
DR   NCBIfam; TIGR02937; sigma70-ECF; 1.
DR   PANTHER; PTHR30603; RNA POLYMERASE SIGMA FACTOR RPO; 1.
DR   PANTHER; PTHR30603:SF47; RNA POLYMERASE SIGMA FACTOR SIGF, CHLOROPLASTIC; 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};
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          281..294
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00715"
FT   DOMAIN          450..476
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00716"
FT   DNA_BIND        451..470
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          1..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          257..327
FT                   /note="Sigma-70 factor domain-2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          336..412
FT                   /note="Sigma-70 factor domain-3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          425..478
FT                   /note="Sigma-70 factor domain-4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   MOTIF           281..284
FT                   /note="Interaction with polymerase core subunit RpoC"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   COMPBIAS        27..81
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..161
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   490 AA;  54910 MW;  1C4821284ACFD13D CRC64;
     MAATESSDQA LGEGENAAEA STPAKKTAKK TAKKTAKKTA KKTAKKTAKK TAKKTAKKTA
     KKSAKKTTKK SAKKATKKTV RKSAAKKQES PAESEKQAQP EAEEELEEDE HDEDVDFDPT
     NADIEDDDDF DAGEDLEDDD LEEDLDDDDE EEEEDSSSVW DEEESAALRQ ARKDAQLTAS
     ADSVRAYLKQ IGKVALLNAE QEVSLAKRIE AGLYAQHRMD EMEKARAEGD KAAKLSPMEK
     RDLRSIARDG RKAKNHLLEA NLRLVVSLAK RYTGRGMAFL DLIQEGNLGL IRAVEKFDYT
     KGYKFSTYAT WWIRQAITRA MADQARTIRI PVHMVEVINK LGRIQRELLQ DLGREPTPQE
     LAKEMDITEE KVLEIQQYAR EPISLDQTIG DEGDSQLGDF IEDSEAVIAV DAVSFTLLQD
     QLQDVLTTLS EREAGVVRLR FGLTDGMPRT LDEIGQVYGV TRERIRQIES KTMSKLRHPS
     RSQVLRDYLD
//
DBGET integrated database retrieval system