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Database: UniProt
Entry: A0A1M3DF49_9SPHN
LinkDB: A0A1M3DF49_9SPHN
Original site: A0A1M3DF49_9SPHN 
ID   A0A1M3DF49_9SPHN        Unreviewed;       491 AA.
AC   A0A1M3DF49;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=RNA polymerase sigma-54 factor {ECO:0000256|PIRNR:PIRNR000774};
GN   ORFNames=BGO24_08835 {ECO:0000313|EMBL:OJV33399.1};
OS   Sphingomonas sp. 67-36.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1895849 {ECO:0000313|EMBL:OJV33399.1, ECO:0000313|Proteomes:UP000183964};
RN   [1] {ECO:0000313|EMBL:OJV33399.1, ECO:0000313|Proteomes:UP000183964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=67-36 {ECO:0000313|EMBL:OJV33399.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-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. {ECO:0000256|PIRNR:PIRNR000774}.
CC   -!- SIMILARITY: Belongs to the sigma-54 factor family.
CC       {ECO:0000256|ARBA:ARBA00008798, ECO:0000256|PIRNR:PIRNR000774}.
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:OJV33399.1}.
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DR   EMBL; MKSU01000005; OJV33399.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3DF49; -.
DR   STRING; 1895849.BGO24_08835; -.
DR   Proteomes; UP000183964; Unassembled WGS sequence.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0001216; F:DNA-binding transcription activator activity; IEA:InterPro.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; 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; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 1.10.10.1330; RNA polymerase sigma-54 factor, core-binding domain; 1.
DR   InterPro; IPR000394; RNA_pol_sigma_54.
DR   InterPro; IPR007046; RNA_pol_sigma_54_core-bd.
DR   InterPro; IPR007634; RNA_pol_sigma_54_DNA-bd.
DR   InterPro; IPR038709; RpoN_core-bd_sf.
DR   NCBIfam; TIGR02395; rpoN_sigma; 1.
DR   PANTHER; PTHR32248; RNA POLYMERASE SIGMA-54 FACTOR; 1.
DR   PANTHER; PTHR32248:SF4; RNA POLYMERASE SIGMA-54 FACTOR; 1.
DR   Pfam; PF00309; Sigma54_AID; 1.
DR   Pfam; PF04963; Sigma54_CBD; 1.
DR   Pfam; PF04552; Sigma54_DBD; 1.
DR   PIRSF; PIRSF000774; RpoN; 1.
DR   PRINTS; PR00045; SIGMA54FCT.
DR   PROSITE; PS00717; SIGMA54_1; 1.
DR   PROSITE; PS00718; SIGMA54_2; 1.
DR   PROSITE; PS50044; SIGMA54_3; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR000774};
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|PIRNR:PIRNR000774};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|PIRNR:PIRNR000774};
KW   Sigma factor {ECO:0000256|ARBA:ARBA00023082,
KW   ECO:0000256|PIRNR:PIRNR000774};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|PIRNR:PIRNR000774};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|PIRNR:PIRNR000774};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000774}.
FT   DOMAIN          125..310
FT                   /note="RNA polymerase sigma factor 54 core-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04963"
FT   DOMAIN          325..483
FT                   /note="RNA polymerase sigma factor 54 DNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04552"
FT   REGION          49..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   491 AA;  52913 MW;  FD4604F382E6E32E CRC64;
     MSLAPRLDLR QSQSLVMTPQ LQQAIRLLAL SNLEIEGVIA EELEKNPLLE ATAPADDAPP
     AEREPVEPAR DEPAGADELV MAGEAAGESL DVDIAAERFD DAPADSIGLG GAGAGGMAGE
     DAPDLDAFAQ SPPSLADHLA TQAGHVLSGT DLIVAQHLID LIDEAGYLTA NLLDVATRLG
     VPLALVERML GVIQTFDPTG VGARDLAECI ALQAKEADRY DPCMARLIDH LDLLARGEIA
     RLKRICQVDD EDMADMIREL RGYDPKPGCR YGGEPAPAVV PDLFVARTQG GWAIEINNAT
     LPRVLVNRRY YGELARGPQD KASKAWLSDC LASANWLVKA LDQRQRTIIR VATEIVKQQE
     AFFLRGVAHL RPLTLRQVAD AIEMHESTVS RVTSNKYLSC ARGQFELKYF FTSAIQAADG
     GDAVSAEAVK SAIRALIQNE GAKVLSDDTL VELLNARGFD IARRTVAKYR EAMGIGSSVQ
     RRRQKALEGV G
//
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