|
Name |
Accession |
Description |
Interval |
E-value |
| rpoC1 |
CHL00018 |
RNA polymerase beta' subunit |
1-194 |
1.34e-168 |
|
RNA polymerase beta' subunit
Pssm-ID: 214336 [Multi-domain] Cd Length: 663 Bit Score: 477.86 E-value: 1.34e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 1 NGIRGQPMREGHNKVYKSFSDVIEGKEGRFRETMLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVIRGLIRQ 80
Cdd:CHL00018 338 NGIRGQPMRDGHNKPYKSFSDVIEGKEGRFRENLLGKRVDYSGRSVIVVGPSLSLHQCGLPREIAIELFQPFVIRGLIRQ 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 81 HFASNIGVAKSKIREKETIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVCKGFNADFDGDQMAV 160
Cdd:CHL00018 418 HLASNIRAAKSKIREKEPIVWEILQEVMQGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVCKGFNADFDGDQMAV 497
|
170 180 190
....*....|....*....|....*....|....
gi 224987229 161 HVPLSLEAQAEARLLMFSHMNLLSPAIGDPISVP 194
Cdd:CHL00018 498 HVPLSLEAQAEARLLMFSHMNLLSPAIGDPISVP 531
|
|
| RNAP_beta'_N |
cd01609 |
Largest subunit (beta') of bacterial DNA-dependent RNA polymerase (RNAP), N-terminal domain; ... |
1-194 |
1.29e-135 |
|
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: 393.81 E-value: 1.29e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 1 NGIRGQPMREGHNKVYKSFSDVIEGKEGRFRETMLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVIRGLIRQ 80
Cdd:cd01609 214 NGRRGKPVTGANNRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPELKLHQCGLPKEMALELFKPFVIRELIER 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 81 HFASNIGVAKSKIREKETIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVCKGFNADFDGDQMAV 160
Cdd:cd01609 294 GLAPNIKSAKKMIERKDPEVWDILEEVIKGHPVLLNRAPTLHRLGIQAFEPVLIEGKAIQLHPLVCTAFNADFDGDQMAV 373
|
170 180 190
....*....|....*....|....*....|....
gi 224987229 161 HVPLSLEAQAEARLLMFSHMNLLSPAIGDPISVP 194
Cdd:cd01609 374 HVPLSLEAQAEARVLMLSSNNILSPASGKPIVTP 407
|
|
| RpoC |
COG0086 |
DNA-directed RNA polymerase, beta' subunit/160 kD subunit [Transcription]; DNA-directed RNA ... |
1-194 |
7.27e-108 |
|
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: 333.67 E-value: 7.27e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 1 NGIRGQPMREGHNKVYKSFSDVIEGKEGRFRETMLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVIRGLIRQ 80
Cdd:COG0086 299 NGRRGRAVTGANKRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPELKLHQCGLPKKMALELFKPFIYRKLEER 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 81 HFASNIGVAKSKIREKETIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVCKGFNADFDGDQMAV 160
Cdd:COG0086 379 GLATTIKSAKKMVEREEPEVWDILEEVIKEHPVLLNRAPTLHRLGIQAFEPVLIEGKAIQLHPLVCTAFNADFDGDQMAV 458
|
170 180 190
....*....|....*....|....*....|....
gi 224987229 161 HVPLSLEAQAEARLLMFSHMNLLSPAIGDPISVP 194
Cdd:COG0086 459 HVPLSLEAQLEARLLMLSTNNILSPANGKPIIVP 492
|
|
| rpoC_TIGR |
TIGR02386 |
DNA-directed RNA polymerase, beta' subunit, predominant form; Bacteria have a single ... |
1-194 |
3.15e-104 |
|
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: 323.54 E-value: 3.15e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 1 NGIRGQPMREGHNKVYKSFSDVIEGKEGRFRETMLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVIRGLIRQ 80
Cdd:TIGR02386 291 NGRRGKPVVGKNNRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPELKMYQCGLPKKMALELFKPFIIKRLIDR 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 81 HFASNIGVAKSKIREKETIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVCKGFNADFDGDQMAV 160
Cdd:TIGR02386 371 ELAANIKSAKKMIEQEDPEVWDVLEDVIKEHPVLLNRAPTLHRLGIQAFEPVLVEGKAIRLHPLVCTAFNADFDGDQMAV 450
|
170 180 190
....*....|....*....|....*....|....
gi 224987229 161 HVPLSLEAQAEARLLMFSHMNLLSPAIGDPISVP 194
Cdd:TIGR02386 451 HVPLSPEAQAEARALMLASNNILNPKDGKPIVTP 484
|
|
| RPOLA_N |
smart00663 |
RNA polymerase I subunit A N-terminus; |
1-194 |
5.01e-100 |
|
RNA polymerase I subunit A N-terminus;
Pssm-ID: 214767 [Multi-domain] Cd Length: 295 Bit Score: 290.96 E-value: 5.01e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 1 NGIRGQPMREGhnKVYKSFSDVIEGKEGRFRETMLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVIRGLIRQ 80
Cdd:smart00663 76 EGLPRANQKSG--RPLKSLSQRLKGKEGRFRQNLLGKRVDFSARSVITPDPNLKLNEVGVPKEIALELTFPEIVTPLNID 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 81 H------------------FASNIGVAK-SKIREKETIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPILVEGRAICL 141
Cdd:smart00663 154 KlrklvrngpngakyiirgKKTNLKLAKkSKIANHLKIGDIVERHVIDGDVVLFNRQPTLHRMSIQAHRVRVLEGKTIRL 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 224987229 142 HPLVCKGFNADFDGDQMAVHVPLSLEAQAEARLLMFSHMNLLSPAIGDPISVP 194
Cdd:smart00663 234 NPLVCSPYNADFDGDEMNLHVPQSLEARAEARELMLVPNNILSPKNGKPIIGP 286
|
|
| RNA_pol_Rpb1_2 |
pfam00623 |
RNA polymerase Rpb1, domain 2; RNA polymerases catalyze the DNA dependent polymerization of ... |
36-176 |
1.00e-45 |
|
RNA polymerase Rpb1, domain 2; 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 2, contains the active site. The invariant motif -NADFDGD- binds the active site magnesium ion.
Pssm-ID: 395498 Cd Length: 166 Bit Score: 148.22 E-value: 1.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 36 GKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVIRGLIRQH----------------FASNIGVAKSKIR----- 94
Cdd:pfam00623 1 GKRVDFSARTVISPDPNLKLDEVGVPISFAKTLTFPEIVTPYNIKRlrqlvengpnvypganYIIRINGARRDLRyqkrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 95 --EKETIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVCKGFNADFDGDQMAVHVPLSLEAQAEA 172
Cdd:pfam00623 81 ldKELEIGDIVERHVIDGDVVLFNRQPSLHRLSIMGHRVRVLPGKTFRLNLSVTTPYNADFDGDEMNLHVPQSEEARAEA 160
|
....
gi 224987229 173 RLLM 176
Cdd:pfam00623 161 EELM 164
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| rpoC1 |
CHL00018 |
RNA polymerase beta' subunit |
1-194 |
1.34e-168 |
|
RNA polymerase beta' subunit
Pssm-ID: 214336 [Multi-domain] Cd Length: 663 Bit Score: 477.86 E-value: 1.34e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 1 NGIRGQPMREGHNKVYKSFSDVIEGKEGRFRETMLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVIRGLIRQ 80
Cdd:CHL00018 338 NGIRGQPMRDGHNKPYKSFSDVIEGKEGRFRENLLGKRVDYSGRSVIVVGPSLSLHQCGLPREIAIELFQPFVIRGLIRQ 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 81 HFASNIGVAKSKIREKETIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVCKGFNADFDGDQMAV 160
Cdd:CHL00018 418 HLASNIRAAKSKIREKEPIVWEILQEVMQGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVCKGFNADFDGDQMAV 497
|
170 180 190
....*....|....*....|....*....|....
gi 224987229 161 HVPLSLEAQAEARLLMFSHMNLLSPAIGDPISVP 194
Cdd:CHL00018 498 HVPLSLEAQAEARLLMFSHMNLLSPAIGDPISVP 531
|
|
| RNAP_beta'_N |
cd01609 |
Largest subunit (beta') of bacterial DNA-dependent RNA polymerase (RNAP), N-terminal domain; ... |
1-194 |
1.29e-135 |
|
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: 393.81 E-value: 1.29e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 1 NGIRGQPMREGHNKVYKSFSDVIEGKEGRFRETMLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVIRGLIRQ 80
Cdd:cd01609 214 NGRRGKPVTGANNRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPELKLHQCGLPKEMALELFKPFVIRELIER 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 81 HFASNIGVAKSKIREKETIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVCKGFNADFDGDQMAV 160
Cdd:cd01609 294 GLAPNIKSAKKMIERKDPEVWDILEEVIKGHPVLLNRAPTLHRLGIQAFEPVLIEGKAIQLHPLVCTAFNADFDGDQMAV 373
|
170 180 190
....*....|....*....|....*....|....
gi 224987229 161 HVPLSLEAQAEARLLMFSHMNLLSPAIGDPISVP 194
Cdd:cd01609 374 HVPLSLEAQAEARVLMLSSNNILSPASGKPIVTP 407
|
|
| PRK00566 |
PRK00566 |
DNA-directed RNA polymerase subunit beta'; Provisional |
1-194 |
3.14e-119 |
|
DNA-directed RNA polymerase subunit beta'; Provisional
Pssm-ID: 234794 [Multi-domain] Cd Length: 1156 Bit Score: 363.62 E-value: 3.14e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 1 NGIRGQPMREGHNKVYKSFSDVIEGKEGRFRETMLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVIRGLIRQ 80
Cdd:PRK00566 299 NGRRGRPVTGPNNRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPELKLHQCGLPKKMALELFKPFIMKKLVER 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 81 HFASNIGVAKSKIREKETIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVCKGFNADFDGDQMAV 160
Cdd:PRK00566 379 GLATTIKSAKKMVEREDPEVWDVLEEVIKEHPVLLNRAPTLHRLGIQAFEPVLIEGKAIQLHPLVCTAFNADFDGDQMAV 458
|
170 180 190
....*....|....*....|....*....|....
gi 224987229 161 HVPLSLEAQAEARLLMFSHMNLLSPAIGDPISVP 194
Cdd:PRK00566 459 HVPLSLEAQAEARVLMLSSNNILSPANGKPIIVP 492
|
|
| rpoC1 |
PRK02625 |
DNA-directed RNA polymerase subunit gamma; Provisional |
1-194 |
7.06e-109 |
|
DNA-directed RNA polymerase subunit gamma; Provisional
Pssm-ID: 235055 [Multi-domain] Cd Length: 627 Bit Score: 324.39 E-value: 7.06e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 1 NGIRGQPMREGHNKVYKSFSDVIEGKEGRFRETMLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVIRGLIRQ 80
Cdd:PRK02625 317 NGRRGRTVVGANNRPLKSLSDIIEGKQGRFRQNLLGKRVDYSGRSVIVVGPKLKMHQCGLPKEMAIELFQPFVIHRLIRQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 81 HFASNIGVAKSKIREKETIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVCKGFNADFDGDQMAV 160
Cdd:PRK02625 397 GIVNNIKAAKKLIQRADPEVWQVLEEVIEGHPVLLNRAPTLHRLGIQAFEPILVEGRAIQLHPLVCPAFNADFDGDQMAV 476
|
170 180 190
....*....|....*....|....*....|....
gi 224987229 161 HVPLSLEAQAEARLLMFSHMNLLSPAIGDPISVP 194
Cdd:PRK02625 477 HVPLSLEAQAEARLLMLASNNILSPATGEPIVTP 510
|
|
| RpoC |
COG0086 |
DNA-directed RNA polymerase, beta' subunit/160 kD subunit [Transcription]; DNA-directed RNA ... |
1-194 |
7.27e-108 |
|
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: 333.67 E-value: 7.27e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 1 NGIRGQPMREGHNKVYKSFSDVIEGKEGRFRETMLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVIRGLIRQ 80
Cdd:COG0086 299 NGRRGRAVTGANKRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPELKLHQCGLPKKMALELFKPFIYRKLEER 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 81 HFASNIGVAKSKIREKETIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVCKGFNADFDGDQMAV 160
Cdd:COG0086 379 GLATTIKSAKKMVEREEPEVWDILEEVIKEHPVLLNRAPTLHRLGIQAFEPVLIEGKAIQLHPLVCTAFNADFDGDQMAV 458
|
170 180 190
....*....|....*....|....*....|....
gi 224987229 161 HVPLSLEAQAEARLLMFSHMNLLSPAIGDPISVP 194
Cdd:COG0086 459 HVPLSLEAQLEARLLMLSTNNILSPANGKPIIVP 492
|
|
| rpoC_TIGR |
TIGR02386 |
DNA-directed RNA polymerase, beta' subunit, predominant form; Bacteria have a single ... |
1-194 |
3.15e-104 |
|
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: 323.54 E-value: 3.15e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 1 NGIRGQPMREGHNKVYKSFSDVIEGKEGRFRETMLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVIRGLIRQ 80
Cdd:TIGR02386 291 NGRRGKPVVGKNNRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPELKMYQCGLPKKMALELFKPFIIKRLIDR 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 81 HFASNIGVAKSKIREKETIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVCKGFNADFDGDQMAV 160
Cdd:TIGR02386 371 ELAANIKSAKKMIEQEDPEVWDVLEDVIKEHPVLLNRAPTLHRLGIQAFEPVLVEGKAIRLHPLVCTAFNADFDGDQMAV 450
|
170 180 190
....*....|....*....|....*....|....
gi 224987229 161 HVPLSLEAQAEARLLMFSHMNLLSPAIGDPISVP 194
Cdd:TIGR02386 451 HVPLSPEAQAEARALMLASNNILNPKDGKPIVTP 484
|
|
| RPOLA_N |
smart00663 |
RNA polymerase I subunit A N-terminus; |
1-194 |
5.01e-100 |
|
RNA polymerase I subunit A N-terminus;
Pssm-ID: 214767 [Multi-domain] Cd Length: 295 Bit Score: 290.96 E-value: 5.01e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 1 NGIRGQPMREGhnKVYKSFSDVIEGKEGRFRETMLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVIRGLIRQ 80
Cdd:smart00663 76 EGLPRANQKSG--RPLKSLSQRLKGKEGRFRQNLLGKRVDFSARSVITPDPNLKLNEVGVPKEIALELTFPEIVTPLNID 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 81 H------------------FASNIGVAK-SKIREKETIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPILVEGRAICL 141
Cdd:smart00663 154 KlrklvrngpngakyiirgKKTNLKLAKkSKIANHLKIGDIVERHVIDGDVVLFNRQPTLHRMSIQAHRVRVLEGKTIRL 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 224987229 142 HPLVCKGFNADFDGDQMAVHVPLSLEAQAEARLLMFSHMNLLSPAIGDPISVP 194
Cdd:smart00663 234 NPLVCSPYNADFDGDEMNLHVPQSLEARAEARELMLVPNNILSPKNGKPIIGP 286
|
|
| PRK14906 |
PRK14906 |
DNA-directed RNA polymerase subunit beta'; |
1-194 |
3.57e-92 |
|
DNA-directed RNA polymerase subunit beta';
Pssm-ID: 184899 [Multi-domain] Cd Length: 1460 Bit Score: 293.70 E-value: 3.57e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 1 NGIRGQPMREGHNKVYKSFSDVIEGKEGRFRETMLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVIRGLIRQ 80
Cdd:PRK14906 387 NGRRGRPVTGPGNRPLKSLADMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPHLKLHQCGLPSAMALELFKPFVMKRLVEL 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 81 HFASNIGVAKSKIREKETIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVCKGFNADFDGDQMAV 160
Cdd:PRK14906 467 EYAANIKAAKRAVDRGASYVWDVLEEVIQDHPVLLNRAPTLHRLGIQAFEPVLVEGKAIKLHPLVCTAFNADFDGDQMAV 546
|
170 180 190
....*....|....*....|....*....|....
gi 224987229 161 HVPLSLEAQAEARLLMFSHMNLLSPAIGDPISVP 194
Cdd:PRK14906 547 HVPLSTQAQAEARVLMLSSNNIKSPAHGRPLTVP 580
|
|
| PRK14844 |
PRK14844 |
DNA-directed RNA polymerase subunit beta/beta'; |
17-194 |
8.42e-81 |
|
DNA-directed RNA polymerase subunit beta/beta';
Pssm-ID: 173305 [Multi-domain] Cd Length: 2836 Bit Score: 261.48 E-value: 8.42e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 17 KSFSDVIEGKEGRFRETMLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVIRGLIRQHFASNIGVAKSKIREK 96
Cdd:PRK14844 1758 KSISDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPTLKLNQCGLPKRMALELFKPFVYSKLKMYGMAPTIKFASKLIRAE 1837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 97 ETIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVCKGFNADFDGDQMAVHVPLSLEAQAEARLLM 176
Cdd:PRK14844 1838 KPEVWDMLEEVIKEHPVLLNRAPTLHRLGIQAFEPILIEGKAIQLHPLVCTAFNADFDGDQMAVHVPISLEAQLEARVLM 1917
|
170
....*....|....*...
gi 224987229 177 FSHMNLLSPAIGDPISVP 194
Cdd:PRK14844 1918 MSTNNVLSPSNGRPIIVP 1935
|
|
| PRK09603 |
PRK09603 |
DNA-directed RNA polymerase subunit beta/beta'; |
1-194 |
3.60e-78 |
|
DNA-directed RNA polymerase subunit beta/beta';
Pssm-ID: 181983 [Multi-domain] Cd Length: 2890 Bit Score: 254.08 E-value: 3.60e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 1 NGIRGQPMREGHNKVYKSFSDVIEGKEGRFRETMLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVIRGLIRQ 80
Cdd:PRK09603 1698 NGRSTNAVKGANKRPLKSLSEIIKGKQGRFRQNLLGKRVDFSGRSVIVVGPNLKMDECGLPKNMALELFKPHLLSKLEER 1777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 81 HFASNIGVAKSKIREKETIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVCKGFNADFDGDQMAV 160
Cdd:PRK09603 1778 GYATTLKQAKRMIEQKSNEVWECLQEITEGYPVLLNRAPTLHKQSIQAFHPKLIDGKAIQLHPLVCSAFNADFDGDQMAV 1857
|
170 180 190
....*....|....*....|....*....|....
gi 224987229 161 HVPLSLEAQAEARLLMFSHMNLLSPAIGDPISVP 194
Cdd:PRK09603 1858 HVPLSQEAIAECKVLMLSSMNILLPASGKAVAIP 1891
|
|
| RNAP_largest_subunit_N |
cd00399 |
Largest subunit of RNA polymerase (RNAP), N-terminal domain; This region represents the ... |
1-194 |
2.70e-67 |
|
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: 214.22 E-value: 2.70e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 1 NGIRGQPMREGHNKVYKSFSDVIEGKEGRFRETMLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELfqafvirglirq 80
Cdd:cd00399 122 NGIAGQPQTQKSGRPLRSLAQRLKGKEGRFRGNLMGKRVDFSGRSVISPDPNLRLDQVGVPKSIALTL------------ 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 81 hfasnigvakskireketiiweilqevmRGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVCKGFNADFDGDQMAV 160
Cdd:cd00399 190 ----------------------------DGDPVLFNRQPSLHKLSIMAHRVRVLPGSTFRLNPLVCSPYNADFDGDEMNL 241
|
170 180 190
....*....|....*....|....*....|....
gi 224987229 161 HVPLSLEAQAEARLLMFSHMNLLSPAIGDPISVP 194
Cdd:cd00399 242 HVPQSEEARAEARELMLVPNNILSPQNGEPLIGL 275
|
|
| RNA_pol_Rpb1_2 |
pfam00623 |
RNA polymerase Rpb1, domain 2; RNA polymerases catalyze the DNA dependent polymerization of ... |
36-176 |
1.00e-45 |
|
RNA polymerase Rpb1, domain 2; 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 2, contains the active site. The invariant motif -NADFDGD- binds the active site magnesium ion.
Pssm-ID: 395498 Cd Length: 166 Bit Score: 148.22 E-value: 1.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 36 GKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVIRGLIRQH----------------FASNIGVAKSKIR----- 94
Cdd:pfam00623 1 GKRVDFSARTVISPDPNLKLDEVGVPISFAKTLTFPEIVTPYNIKRlrqlvengpnvypganYIIRINGARRDLRyqkrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 95 --EKETIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVCKGFNADFDGDQMAVHVPLSLEAQAEA 172
Cdd:pfam00623 81 ldKELEIGDIVERHVIDGDVVLFNRQPSLHRLSIMGHRVRVLPGKTFRLNLSVTTPYNADFDGDEMNLHVPQSEEARAEA 160
|
....
gi 224987229 173 RLLM 176
Cdd:pfam00623 161 EELM 164
|
|
| RNAP_archeal_A' |
cd02582 |
A' subunit of archaeal RNA polymerase (RNAP); A' is the largest subunit of the archaeal RNA ... |
7-191 |
3.09e-43 |
|
A' subunit of archaeal RNA polymerase (RNAP); A' is the largest subunit of the archaeal RNA polymerase (RNAP). Archaeal RNAP is closely related to RNA polymerases in eukaryotes based on the subunit compositions. Archaeal RNAP is a large multi-protein complex, made up of 11 to 13 subunits, depending on the species, that are responsible for the synthesis of RNA. Structure studies suggest that RNAP complexes from different organisms share a crab-claw-shaped structure. The largest eukaryotic RNAP subunit is encoded by two separate archaeal subunits (A' and A'') which correspond to the N- and C-terminal domains of eukaryotic RNAP II Rpb1, respectively. The N-terminal domain of Rpb1 forms part of the active site and includes the head and the core of one clamp as well as the pore and funnel structures of RNAP II. Based on a structural comparison among the archaeal, bacterial and eukaryotic RNAPs the DNA binding channel and the active site are part of A' subunit which is conserved. The strong similarity between subunit A' and the N-terminal domain of Rpb1 suggests a similar functional and structural role for these two proteins.
Pssm-ID: 259846 [Multi-domain] Cd Length: 861 Bit Score: 153.56 E-value: 3.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 7 PMREGHNKVYKSFSDVIEGKEGRFRETMLGKRVDYSGRSVIVVGPSLSLHRCGLPREIA-------------IELFQAFV 73
Cdd:cd02582 284 PARHRSGRPLKTLAQRLKGKEGRFRGNLSGKRVNFSARTVISPDPNLSINEVGVPEDIAkeltvpervtewnIEKMRKLV 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 74 IRGLIRQHFASNI-----------GVAKSKIREKETIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLH 142
Cdd:cd02582 364 LNGPDKWPGANYVirpdgrrirlrYVNREELAERLEPGWIVERHLIDGDIVLFNRQPSLHRMSIMAHRVRVLPGKTFRLN 443
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 224987229 143 PLVCKGFNADFDGDQMAVHVPLSLEAQAEARLLMFSHMNLLSPAIGDPI 191
Cdd:cd02582 444 LAVCPPYNADFDGDEMNLHVPQSEEARAEARELMLVQEHILSPRYGGPI 492
|
|
| PRK08566 |
PRK08566 |
DNA-directed RNA polymerase subunit A'; Validated |
25-191 |
2.39e-40 |
|
DNA-directed RNA polymerase subunit A'; Validated
Pssm-ID: 236292 [Multi-domain] Cd Length: 882 Bit Score: 145.38 E-value: 2.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 25 GKEGRFRETMLGKRVDYSGRSVIVVGPSLSLHRCGLPREIA-------------IELFQAFVIRG---------LIRQH- 81
Cdd:PRK08566 306 GKEGRFRGNLSGKRVNFSARTVISPDPNLSINEVGVPEAIAkeltvpervtewnIEELREYVLNGpekhpganyVIRPDg 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 82 -----FASNigvaKSKIREKETIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVCKGFNADFDGD 156
Cdd:PRK08566 386 rriklTDKN----KEELAEKLEPGWIVERHLIDGDIVLFNRQPSLHRMSIMAHRVRVLPGKTFRLNLAVCPPYNADFDGD 461
|
170 180 190
....*....|....*....|....*....|....*
gi 224987229 157 QMAVHVPLSLEAQAEARLLMFSHMNLLSPAIGDPI 191
Cdd:PRK08566 462 EMNLHVPQTEEARAEARILMLVQEHILSPRYGGPI 496
|
|
| PRK14977 |
PRK14977 |
bifunctional DNA-directed RNA polymerase A'/A'' subunit; Provisional |
1-191 |
7.06e-38 |
|
bifunctional DNA-directed RNA polymerase A'/A'' subunit; Provisional
Pssm-ID: 184940 [Multi-domain] Cd Length: 1321 Bit Score: 138.62 E-value: 7.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 1 NGIRGQP--MREGHNKVYKSFSDVIEGKEGRFRETMLGKRVDYSGRSVIVVGPSLSLHRCGLPREIA------------- 65
Cdd:PRK14977 290 NATAGIPqaHHKGSGRPLKSLFQRLKGKEGRFRGNLIGKRVDFSARTVISPDPMIDIDEVGVPEAIAmkltipeivnenn 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 66 IELFQAFVIRG----------------LIRQHFASNIGV-AKSKIREKETIIWEILQEVMRGHPVLLNRAPTLHRLGIQA 128
Cdd:PRK14977 370 IEKMKELVINGpdefpganairkgdgtKIRLDFLEDKGKdALREAAEQLEIGDIVERHLADGDIVIFNRQPSLHKLSILA 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224987229 129 FQPILVEGRAICLHPLVCKGFNADFDGDQMAVHVPLSLEAQAEARLLMFSHMNLLSPAIGDPI 191
Cdd:PRK14977 450 HRVKVLPGATFRLHPAVCPPYNADFDGDEMNLHVPQIEDARAEAIELMGVKDNLISPRTGGPI 512
|
|
| RNAP_III_RPC1_N |
cd02583 |
Largest subunit (RPC1) of eukaryotic RNA polymerase III (RNAP III), N-terminal domain; Rpc1 ... |
25-191 |
1.25e-34 |
|
Largest subunit (RPC1) of eukaryotic RNA polymerase III (RNAP III), N-terminal domain; Rpc1 (C160) subunit forms part of the active site region of RNAP III. RNAP III is one of the three distinct classes of nuclear RNAP in eukaryotes that is responsible for the synthesis of tRNAs, 5SrRNA, Alu-RNA, U6 snRNA genes, and some others. RNAP III is the largest nuclear RNA polymerase with 17 subunits. Structure studies suggest that different RNA polymerase complexes share a similar crab-claw-shaped structure. The N-terminal domain of Rpb1, the largest subunit of RNAP II in yeast, forms part of the active site, making up the head and core of the one clamp, as well as the pore and funnel structures of RNAP II. The strong homology between Rpc1 and Rpb1 suggests a similar functional and structural role.
Pssm-ID: 259847 [Multi-domain] Cd Length: 816 Bit Score: 128.82 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 25 GKEGRFRETMLGKRVDYSGRSVIVVGPSLSLHRCGLPREIA-------------IELFQAFVIRG---------LIRQH- 81
Cdd:cd02583 275 GKQGRFRGNLSGKRVDFSGRTVISPDPNLRIDQVGVPEHVAkiltypervtrynIEKLRKLVLNGpdvhpganfVIKRDg 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 82 -FASNIGVAKSKIREKETIIWEILQ-EVMRGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVCKGFNADFDGDQMA 159
Cdd:cd02583 355 gKKKFLKYGNRRKIARELKIGDIVErHLEDGDIVLFNRQPSLHRLSIMAHRAKVMPWRTFRFNECVCTPYNADFDGDEMN 434
|
170 180 190
....*....|....*....|....*....|..
gi 224987229 160 VHVPLSLEAQAEARLLMFSHMNLLSPAIGDPI 191
Cdd:cd02583 435 LHVPQTEEARAEALELMGVKNNLVTPRNGEPL 466
|
|
| RNAP_II_RPB1_N |
cd02733 |
Largest subunit (Rpb1) of eukaryotic RNA polymerase II (RNAP II), N-terminal domain; The two ... |
1-185 |
1.51e-29 |
|
Largest subunit (Rpb1) of eukaryotic RNA polymerase II (RNAP II), N-terminal domain; The two largest subunits of RNA polymerase II (RNAP II), Rpb1 and Rpb2, form the active site, DNA entry channel and RNA exit channel. RNAP II is a large multi-subunit complex responsible for the synthesis of mRNA in eukaryotes. RNAP II consists of a 10-subunit core enzyme and a peripheral heterodimer of two subunits. Structure studies suggest that RNAP complexes from different organisms share a crab-claw-shape structure. In yeast, Rpb1 and Rpb2, each makes up one clamp, one jaw, and part of the cleft. Rpb1_N contains part of the active site, forms the head and core of the one clamp, and makes up the pore and funnel regions of RNAP II.
Pssm-ID: 259848 [Multi-domain] Cd Length: 751 Bit Score: 114.17 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 1 NGIRGQPM---REGhnKVYKSFSDVIEGKEGRFRETMLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIEL-FQAFV--- 73
Cdd:cd02733 200 NEIPGLPQatqKSG--RPLKSIRQRLKGKEGRIRGNLMGKRVDFSARTVITPDPNLELDQVGVPRSIAMNLtFPEIVtpf 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 74 ----IRGLIRQHFASNIGvAKSKIREKETII---------WEILQE---VMR----GHPVLLNRAPTLHRLGIQAFqpil 133
Cdd:cd02733 278 nidrLQELVRNGPNEYPG-AKYIIRDDGERIdlrylkkasDLHLQYgyiVERhlqdGDVVLFNRQPSLHKMSMMGH---- 352
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 224987229 134 vegRAICLHPL-------VCKGFNADFDGDQMAVHVPLSLEAQAEARLLMFSHMNLLSP 185
Cdd:cd02733 353 ---RVKVLPYStfrlnlsVTTPYNADFDGDEMNLHVPQSLETRAELKELMMVPRQIVSP 408
|
|
| RNAP_I_RPA1_N |
cd01435 |
Largest subunit (RPA1) of eukaryotic RNA polymerase I (RNAP I), N-terminal domain; RPA1 is the ... |
22-191 |
5.99e-29 |
|
Largest subunit (RPA1) of eukaryotic RNA polymerase I (RNAP I), N-terminal domain; RPA1 is the largest subunit of the eukaryotic RNA polymerase I (RNAP I). RNAP I is a multi-subunit protein complex responsible for the synthesis of rRNA precursors. RNAP I consists of at least 14 different subunits, the largest being homologous to subunit Rpb1 of yeast RNAP II and subunit beta' of bacterial RNAP. The yeast member of this family is known as Rpb190. Structure studies suggest that different RNA polymerase complexes share a similar crab-claw-shaped structure. The N-terminal domain of Rpb1, the largest subunit of RNAP II in yeast, forms part of the active site. It makes up the head and core of one clamp, as well as the pore and funnel structures of RNAP II. The strong homology between RPA1 and Rpb1 suggests a similar functional and structural role.
Pssm-ID: 259844 [Multi-domain] Cd Length: 779 Bit Score: 112.66 E-value: 5.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 22 VIEGKEGRFRETMLGKRVDYSGRSVIVVGPSLSLHRCGLPREIA-------------IELFQAFVIRG--------LIRQ 80
Cdd:cd01435 233 LLEKKEGLFRMNMMGKRVNYAARSVISPDPFIETNEIGIPLVFAkkltfpepvtpfnVEELRQAVINGpdvypganAIED 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 81 HFASNIGVAKSKIREKETIIWEILQE------------VMR----GHPVLLNRAPTLHRLGIQAFQ-PILVEGRAICLHP 143
Cdd:cd01435 313 EDGRLILLSALSEERRKALAKLLLLLssaklllngpkkVYRhlldGDVVLLNRQPTLHKPSIMAHKvRVLPGEKTLRLHY 392
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 224987229 144 LVCKGFNADFDGDQMAVHVPLSLEAQAEARLLMFSHMNLLSPAIGDPI 191
Cdd:cd01435 393 ANCKSYNADFDGDEMNLHFPQSELARAEAYYIASTDNQYLVPTDGKPL 440
|
|
| RNAP_IV_RPD1_N |
cd10506 |
Largest subunit (NRPD1) of higher plant RNA polymerase IV, N-terminal domain; NRPD1 and NRPE1 ... |
30-176 |
3.19e-20 |
|
Largest subunit (NRPD1) of higher plant RNA polymerase IV, N-terminal domain; NRPD1 and NRPE1 are the largest subunits of plant DNA-dependent RNA polymerase IV and V that, together with second largest subunits (NRPD2 and NRPE2), form the active site region of the DNA entry and RNA exit channel. Higher plants have five multi-subunit nuclear RNA polymerases; RNAP I, RNAP II and RNAP III, which are essential for viability, plus the two isoforms of the non-essential polymerase RNAP IV and V, which specialize in small RNA-mediated gene silencing pathways. RNAP IV and/or V might be involved in RNA-directed DNA methylation of endogenous repetitive elements, silencing of transgenes, regulation of flowering-time genes, inducible regulation of adjacent gene pairs, and spreading of mobile silencing signals. The subunit compositions of RNAP IV and V reveal that they evolved from RNAP II.
Pssm-ID: 259849 [Multi-domain] Cd Length: 744 Bit Score: 87.46 E-value: 3.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 30 FRETMLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIEL-------------FQAFVIRGLI---RQHFASNIGVAKSKI 93
Cdd:cd10506 206 MKDLLLGKRSGHSFRSVVVGDPYLELNEIGIPCEIAERLtvservsswnrerLQEYCDLTLLlkgVIGVRRNGRLVGVRS 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224987229 94 REKETIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQ-PILVEGRAICLHPLVCKGFNADFDGDQMAVHVPLSLEAQAEA 172
Cdd:cd10506 286 HNTLQIGDVIHRPLVDGDVVLVNRPPSIHQHSLIALSvKVLPTNSVVSINPLCCSPFRGDFDGDCLHGYIPQSLQARAEL 365
|
....
gi 224987229 173 RLLM 176
Cdd:cd10506 366 EELV 369
|
|
| |
