RNA polymerase beta' subunit, partial (chloroplast) [Stokesia laevis]
DNA-directed RNA polymerase subunit beta'( domain architecture ID 1004693)
chloroplast DNA-directed RNA polymerase (RNAP) subunit beta' (rpoC1) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
List of domain hits
Name | Accession | Description | Interval | E-value | |||
rpoC1 super family | cl29902 | RNA polymerase beta' subunit |
1-144 | 2.73e-108 | |||
RNA polymerase beta' subunit The actual alignment was detected with superfamily member CHL00018: Pssm-ID: 214336 [Multi-domain] Cd Length: 663 Bit Score: 321.47 E-value: 2.73e-108
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Name | Accession | Description | Interval | E-value | |||
rpoC1 | CHL00018 | RNA polymerase beta' subunit |
1-144 | 2.73e-108 | |||
RNA polymerase beta' subunit Pssm-ID: 214336 [Multi-domain] Cd Length: 663 Bit Score: 321.47 E-value: 2.73e-108
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RNAP_beta'_N | cd01609 | Largest subunit (beta') of bacterial DNA-dependent RNA polymerase (RNAP), N-terminal domain; ... |
10-143 | 3.82e-59 | |||
Largest subunit (beta') of bacterial DNA-dependent RNA polymerase (RNAP), N-terminal domain; Beta' is the largest subunit of bacterial DNA-dependent RNA polymerase (RNAP). This family also includes the eukaryotic plastid-encoded RNAP beta' subunit. Bacterial RNAP is a large multi-subunit complex responsible for the synthesis of all RNAs in the cell. Structure studies suggest that RNA polymerase complexes from different organisms share a crab-claw-shaped structure with two "pincers" defining a central cleft. Beta' and beta, the largest and the second largest subunits of bacterial RNAP, each makes up one pincer and part of the base of the cleft. Beta' contains part of the active site and binds two zinc ions that have a structural role in the formation of the active polymerase. Pssm-ID: 259845 [Multi-domain] Cd Length: 659 Bit Score: 193.50 E-value: 3.82e-59
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rpoC_TIGR | TIGR02386 | DNA-directed RNA polymerase, beta' subunit, predominant form; Bacteria have a single ... |
10-142 | 4.43e-47 | |||
DNA-directed RNA polymerase, beta' subunit, predominant form; Bacteria have a single DNA-directed RNA polymerase, with required subunits that include alpha, beta, and beta-prime. This model describes the predominant architecture of the beta-prime subunit in most bacteria. This model excludes from among the bacterial mostly sequences from the cyanobacteria, where RpoC is replaced by two tandem genes homologous to it but also encoding an additional domain. [Transcription, DNA-dependent RNA polymerase] Pssm-ID: 274103 [Multi-domain] Cd Length: 1140 Bit Score: 162.53 E-value: 4.43e-47
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RpoC | COG0086 | DNA-directed RNA polymerase, beta' subunit/160 kD subunit [Transcription]; DNA-directed RNA ... |
1-143 | 1.68e-45 | |||
DNA-directed RNA polymerase, beta' subunit/160 kD subunit [Transcription]; DNA-directed RNA polymerase, beta' subunit/160 kD subunit is part of the Pathway/BioSystem: RNA polymerase Pssm-ID: 439856 [Multi-domain] Cd Length: 1165 Bit Score: 158.01 E-value: 1.68e-45
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RNA_pol_Rpb1_1 | pfam04997 | RNA polymerase Rpb1, domain 1; RNA polymerases catalyze the DNA dependent polymerization of ... |
10-130 | 5.03e-19 | |||
RNA polymerase Rpb1, domain 1; RNA polymerases catalyze the DNA dependent polymerization of RNA. Prokaryotes contain a single RNA polymerase compared to three in eukaryotes (not including mitochondrial. and chloroplast polymerases). This domain, domain 1, represents the clamp domain, which a mobile domain involved in positioning the DNA, maintenance of the transcription bubble and positioning of the nascent RNA strand. Pssm-ID: 398595 Cd Length: 320 Bit Score: 80.80 E-value: 5.03e-19
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Name | Accession | Description | Interval | E-value | |||
rpoC1 | CHL00018 | RNA polymerase beta' subunit |
1-144 | 2.73e-108 | |||
RNA polymerase beta' subunit Pssm-ID: 214336 [Multi-domain] Cd Length: 663 Bit Score: 321.47 E-value: 2.73e-108
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RNAP_beta'_N | cd01609 | Largest subunit (beta') of bacterial DNA-dependent RNA polymerase (RNAP), N-terminal domain; ... |
10-143 | 3.82e-59 | |||
Largest subunit (beta') of bacterial DNA-dependent RNA polymerase (RNAP), N-terminal domain; Beta' is the largest subunit of bacterial DNA-dependent RNA polymerase (RNAP). This family also includes the eukaryotic plastid-encoded RNAP beta' subunit. Bacterial RNAP is a large multi-subunit complex responsible for the synthesis of all RNAs in the cell. Structure studies suggest that RNA polymerase complexes from different organisms share a crab-claw-shaped structure with two "pincers" defining a central cleft. Beta' and beta, the largest and the second largest subunits of bacterial RNAP, each makes up one pincer and part of the base of the cleft. Beta' contains part of the active site and binds two zinc ions that have a structural role in the formation of the active polymerase. Pssm-ID: 259845 [Multi-domain] Cd Length: 659 Bit Score: 193.50 E-value: 3.82e-59
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rpoC1 | PRK02625 | DNA-directed RNA polymerase subunit gamma; Provisional |
10-142 | 3.98e-56 | |||
DNA-directed RNA polymerase subunit gamma; Provisional Pssm-ID: 235055 [Multi-domain] Cd Length: 627 Bit Score: 184.95 E-value: 3.98e-56
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PRK00566 | PRK00566 | DNA-directed RNA polymerase subunit beta'; Provisional |
9-142 | 1.56e-47 | |||
DNA-directed RNA polymerase subunit beta'; Provisional Pssm-ID: 234794 [Multi-domain] Cd Length: 1156 Bit Score: 163.70 E-value: 1.56e-47
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rpoC_TIGR | TIGR02386 | DNA-directed RNA polymerase, beta' subunit, predominant form; Bacteria have a single ... |
10-142 | 4.43e-47 | |||
DNA-directed RNA polymerase, beta' subunit, predominant form; Bacteria have a single DNA-directed RNA polymerase, with required subunits that include alpha, beta, and beta-prime. This model describes the predominant architecture of the beta-prime subunit in most bacteria. This model excludes from among the bacterial mostly sequences from the cyanobacteria, where RpoC is replaced by two tandem genes homologous to it but also encoding an additional domain. [Transcription, DNA-dependent RNA polymerase] Pssm-ID: 274103 [Multi-domain] Cd Length: 1140 Bit Score: 162.53 E-value: 4.43e-47
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RpoC | COG0086 | DNA-directed RNA polymerase, beta' subunit/160 kD subunit [Transcription]; DNA-directed RNA ... |
1-143 | 1.68e-45 | |||
DNA-directed RNA polymerase, beta' subunit/160 kD subunit [Transcription]; DNA-directed RNA polymerase, beta' subunit/160 kD subunit is part of the Pathway/BioSystem: RNA polymerase Pssm-ID: 439856 [Multi-domain] Cd Length: 1165 Bit Score: 158.01 E-value: 1.68e-45
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PRK14906 | PRK14906 | DNA-directed RNA polymerase subunit beta'; |
10-142 | 3.20e-39 | |||
DNA-directed RNA polymerase subunit beta'; Pssm-ID: 184899 [Multi-domain] Cd Length: 1460 Bit Score: 140.01 E-value: 3.20e-39
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PRK09603 | PRK09603 | DNA-directed RNA polymerase subunit beta/beta'; |
14-142 | 3.33e-37 | |||
DNA-directed RNA polymerase subunit beta/beta'; Pssm-ID: 181983 [Multi-domain] Cd Length: 2890 Bit Score: 134.28 E-value: 3.33e-37
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PRK14844 | PRK14844 | DNA-directed RNA polymerase subunit beta/beta'; |
9-142 | 1.02e-31 | |||
DNA-directed RNA polymerase subunit beta/beta'; Pssm-ID: 173305 [Multi-domain] Cd Length: 2836 Bit Score: 118.57 E-value: 1.02e-31
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RNA_pol_Rpb1_1 | pfam04997 | RNA polymerase Rpb1, domain 1; RNA polymerases catalyze the DNA dependent polymerization of ... |
10-130 | 5.03e-19 | |||
RNA polymerase Rpb1, domain 1; RNA polymerases catalyze the DNA dependent polymerization of RNA. Prokaryotes contain a single RNA polymerase compared to three in eukaryotes (not including mitochondrial. and chloroplast polymerases). This domain, domain 1, represents the clamp domain, which a mobile domain involved in positioning the DNA, maintenance of the transcription bubble and positioning of the nascent RNA strand. Pssm-ID: 398595 Cd Length: 320 Bit Score: 80.80 E-value: 5.03e-19
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RNAP_largest_subunit_N | cd00399 | Largest subunit of RNA polymerase (RNAP), N-terminal domain; This region represents the ... |
16-126 | 7.96e-14 | |||
Largest subunit of RNA polymerase (RNAP), N-terminal domain; This region represents the N-terminal domain of the largest subunit of RNA polymerase (RNAP). RNAP is a large multi-protein complex responsible for the synthesis of RNA. It is the principle enzyme of the transcription process, and is a final target in many regulatory pathways that control gene expression in all living cells. At least three distinct RNAP complexes are found in eukaryotic nuclei; RNAP I transcribes the ribosomal RNA precursor, RNAP II the mRNA precursor, and RNAP III the 5S and tRNA genes. A single distinct RNAP complex is found in prokaryotes and archaea, respectively, which may be responsible for the synthesis of all RNAs. Structure studies reveal that prokaryotic and eukaryotic RNAPs share a conserved crab-claw-shaped structure. The largest and the second largest subunits each make up one clamp, one jaw, and part of the cleft. All RNAPs are metalloenzymes. At least one Mg2+ ion is bound in the catalytic center. In addition, all cellular RNAPs contain several tightly bound zinc ions to different subunits that vary between RNAPs from prokaryotic to eukaryotic lineages. This domain represents the N-terminal region of the largest subunit of RNAP, and includes part of the active site. In archaea and some of the photosynthetic organisms or cellular organelle, however, this domain exists as a separate subunit. Pssm-ID: 259843 [Multi-domain] Cd Length: 528 Bit Score: 67.07 E-value: 7.96e-14
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Blast search parameters | ||||
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