※ Protein Information
Tag Content
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA-directed RNA polymerase subunit B
Protein Synonyms/Alias
 
Gene Name
 rpoB
Gene Synonyms/Alias
 Saci_0693
Created Date
 3-June-2014
Organism
 Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
NCBI Taxa ID
 330779
Phosphorylation
Position
Peptide
Code
Type
References
512 QNEDVEKYMSWSKVY Y HTP [1]
378 KVRGRRLSLTALVRA S HTP [1]
Reference
 [1]Archaeal signal transduction: impact of protein phosphatase deletions on cell size, motility, and energy metabolism in Sulfolobus acidocaldarius.
 Reimann J,Esser D,Orell A,Amman F,Pham TK,Noirel J,Lindås AC,Bernander R,Wright PC,Siebers B,Albers SV
 Mol. Cell Proteomics 2013, Dec;12(12):3908-23. [PMID:24078887]
Functional Description From UniProt
 FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
Sequence Annotation From UniProt
 
Key Word From UniProt
 Completeproteome; DNA-directedRNApolymerase; Metal-binding; Nucleotidyltransferase; Transcription; Transferase; Zinc; Zinc-finger
Protein Sequence
 MLDTESRWAI AESFFKTRGL VRQHLDSFND FLRNKLQQVI YEQGEIVTEV PGLKIKLGKI 60
 RYEKPSIRET DKGPMREITP MEARLRNLTY SSPIFLSMIP VENNIEGEPI EIYIGDLPIM 120
 LKSVADPTSN LPIDKLIEIG EDPKDPGGYF IVNGSEKVII AQEDLATNRV LVDYGKSGSN 180
 ITHVAKVTSS AAGYRVQVMI ERLKDSTIQI SFATVPGRIP FAIIMRALGF VTDRDIVYAV 240
 SLDPQIQNEL LPSLEQASSI TSAEEALDFI GNRVAIGQKR ENRIQKAEQV IDKYFLPHLG 300
 TSPEDRKKKG YYLASAVNKI LELYLGRREP DDKDHYANKR VRLAGDLFTS LFRVAFKAFV 360
 KDLVYQLEKS KVRGRRLSLT ALVRADIITE RIRHALATGN WVGGRTGVSQ LLDRTNWLSM 420
 LSHLRRVVSS LARGQPNFEA RDLHGTQWGR MCPFETPEGP NSGLVKNLAL LAQVSVGINE 480
 SVVERVAYEL GVVSVEDVIR RISEQNEDVE KYMSWSKVYL NGRLLGYYED GKELAKKIRE 540
 SRRQGKLSDE VNVAYIATDY LNEVHINCDA GRVRRPLIIV NNGTPLVDTE DIKKLKNGEI 600
 TFDDLVKQGK IEFIDAEEEE NAYVALNPQD LTPDHTHLEI WPSAILGIIA SIIPYPEHNQ 660
 SPRNTYQSAM AKQSLGLYAS NYQIRTDTRA HLLHYPQMPL VQTRMLGVIG YNDRPAGANA 720
 ILAIMSYTGY NMEDSIIMNK SSIERGMYRS TFFRLYSTEE VKYPGGQEDK IVTPEAGVKG 780
 YKGKDYYRLL EDNGVVSPEV EVKGGDVLIG KVSPPRFLQE FKELSPEQAK RDTSIVTRHG 840
 ENGIVDLVLI TETLEGNKLV KVRVRDLRIP EIGDKFATRH GQKGVVGILI DQVDMPYTAK 900
 GIVPDIILNP HALPSRMTIG QIMEAIGGKY AALSGKPVDA TPFLETPKLQ EMQKEILKLG 960
 HLPDSTEVVY DGRTGQKLKS RILFGIVYYQ KLHHMVADKM HARARGPVQI LTRQPTEGRA 1020
 REGGLRFGEM ERDCLIGFGT AMLIKDRLLD NSDKAVVYIC DQCGYVGWYD RSKNRYVCPV 1080
 HGDKSVLHPV TVSYAFKLLI QELMSMVISP RLILGEKVNL GGASNE 1126
  GO:0003677   F:DNA binding IEA:InterPro
  GO:0003899   F:DNA-directed RNA polymerase activity IEA:UniProtKB-KW
  GO:0032549   F:ribonucleoside binding IEA:InterPro
  GO:0008270   F:zinc ion binding IEA:InterPro
  GO:0006351   P:transcription, DNA-templated IEA:InterPro
  IPR015712   DNA-dir_RNA_pol_su2.
  IPR007120   DNA-dir_RNA_pol_su2_6.
  IPR007121   RNA_pol_bsu_CS.
  IPR007644   RNA_pol_bsu_protrusion.
  IPR007642   RNA_pol_Rpb2_2.
  IPR007645   RNA_pol_Rpb2_3.
  IPR007646   RNA_pol_Rpb2_4.
  IPR007647   RNA_pol_Rpb2_5.
  IPR007641   RNA_pol_Rpb2_7.
  IPR014724   RNA_pol_RPB2_OB-fold.
  IPR019969   RNAP_B.
  PF04563   RNA_pol_Rpb2_1.
  PF04561   RNA_pol_Rpb2_2.
  PF04565   RNA_pol_Rpb2_3.
  PF04566   RNA_pol_Rpb2_4.
  PF04567   RNA_pol_Rpb2_5.
  PF00562   RNA_pol_Rpb2_6.
  PF04560   RNA_pol_Rpb2_7.
  PS01166   RNA_POL_BETA.