ACL_RS00565
  | Uniprot: A9NEG0
Description: DNA-directed RNA polymerase subunit alpha EC number: 2.7.7.6 Annotation score: 2 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). {ECO:0000256|HAMAP-Rule:MF_00059}. Cofactor: Enzyme regulation: Function [CC]: FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. {ECO:0000256|HAMAP-Rule:MF_00059}. Pathway: Active site: Binding site: Calcium binding: DNA binding: Metal binding: Nucleotide binding: Site: Gene names (primary): rpoA Gene names (synonym): Mass: 37,022 Subunit structure [CC]: SUBUNIT: Homodimer. The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription. {ECO:0000256|HAMAP-Rule:MF_00059}. Gene ontology (GO): DNA binding [GO:0003677]; DNA-directed RNA polymerase activity [GO:0003899]; transcription, DNA-templated [GO:0006351] Gene ontology IDs: GO:0003677; GO:0003899; GO:0006351 Chain: Signal peptide: Domain [CC]: DOMAIN: The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators and with upstream promoter elements. {ECO:0000256|HAMAP-Rule:MF_00059}. Sequence similarities: SIMILARITY: Belongs to the RNA polymerase alpha chain family. {ECO:0000256|HAMAP-Rule:MF_00059}. Protein families: RNA polymerase alpha chain family Coiled coil: Domain [FT]: DOMAIN 21 228 RPOLD. {ECO:0000259|SMART:SM00662}. Motif: Region: REGION 1 229 Alpha N-terminal domain (alpha-NTD). {ECO:0000256|HAMAP-Rule:MF_00059}.; REGION 247 330 Alpha C-terminal domain (alpha-CTD). {ECO:0000256|HAMAP-Rule:MF_00059}. EMBL: CP000896 ProteinModelPortal: A9NEG0 MEROPS: EnsemblBacteria KO: ABX80740 UniPathway: K03040 CDD: Gene3D: HAMAP: 2.170.120.12 InterPro: MF_00059 PANTHER: IPR011262;IPR011263;IPR011773;IPR009025;IPR011260 PIRSF: PRINTS: PROSITE: Pfam: ProDom: PF01000;PF03118;PF01193 SMART: PD001179 SUPFAM: SM00662 TIGRFAMs: SSF55257;SSF56553 |
97078-98071(+) >nucleotide sequence TTGGGACGTTTCTTAATCAAACCACTTGAACGCGGTTATGGGTTAACCTTAGGTAATGCA TTAAGACGTGTCTTATTATCATCGTTACCAGGTGCTGCAATCGTCAATGTTAAAATTGAA GGTGTGGAGCACGAGTTTTCTACCATTGAAGGCGTTTATGAAGATGTGATGGGAATCGTT CTTAACCTTAAAAAGGTCGTATTCTCAGTTGATTCACAAGATCCACAGTATGAACAACAA TTAGAATTATATGCAGAAGGTCCAGCTGTGATTACTGCAGGTGATTTTAATTTGGCAGAC GACATTGAAGTTGTCAATAAAGACCAACATATTGCAACTCTAGCAGAAGGTGCTAAGTTC AATATGACAGTTACAGTTAGACGTGGTATTGGTTATGTACCAGCTGACCAAAATAAACAA TATTCTAAATACGAATTAAACGTTATTCCAATTGACTCACTTTATACACCAGTTGAACGT GTAATCTACAGTGTAGAAAAAACACGTGGTGATTTAGATGAATTAACAATTGAAATCGAA ACAAACGGTGCTATCTTAGCAAAAGAAGCATTAGCCCTCGCATCTAAGATGTTAGTGGAT CACTTCCAAGTACTTGTAGATATTTCTGAAAAAGCTAGTGAATTTGATTTCATTCGCGAT ATTGAAGAAGAACCAGCAAGCAAAAAATCAGATACTAAGATTGAACAACTTGATTTATCA GTTCGTTTATTCAACTCACTAAAACGTAGTGGTATCACTACAGTTGGTGAATTACTAAAA TTATCTGAAGAAGAAGTTATGAGACTACGTTCATTAGGTAGAAAATCATTCAAAGAATTA AAAGAAAAATTAGCAGAACATGGACTTGAATTCGAGCACTCTACTTCAAAAGAAGCAAGA TTCGGATTTGATTCAGACGAAGATAAGGAGTAA >protein sequence GVEHEFSTIEGVYEDVMGIVLNLKKVVFSVDSQDPQYEQQLELYAEGPAVITAGDFNLAD DIEVVNKDQHIATLAEGAKFNMTVTVRRGIGYVPADQNKQYSKYELNVIPIDSLYTPVER VIYSVEKTRGDLDELTIEIETNGAILAKEALALASKMLVDHFQVLVDISEKASEFDFIRD IEEEPASKKSDTKIEQLDLSVRLFNSLKRSGITTVGELLKLSEEEVMRLRSLGRKSFKEL KEKLAEHGLEFEHSTSKEARFGFDSDEDKE |
© Fisunov Lab of Proteomics, 2016.