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Conserved domains on  [gi|1002153229|gb|AMM73284|]
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RNA polymerase C, partial (chloroplast) [Acer pseudoplatanus]

Protein Classification

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.

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
rpoC1 super family cl29902
RNA polymerase beta' subunit
1-169 5.05e-145

RNA polymerase beta' subunit


The actual alignment was detected with superfamily member CHL00018:

Pssm-ID: 214336 [Multi-domain]  Cd Length: 663  Bit Score: 417.00  E-value: 5.05e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229   1 IRGQPMRDGHNKVYKSFSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVICSLIRQHL 80
Cdd:CHL00018  340 IRGQPMRDGHNKPYKSFSDVIEGKEGRFRENLLGKRVDYSGRSVIVVGPSLSLHQCGLPREIAIELFQPFVIRGLIRQHL 419
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229  81 ASNIGVAKSQIRDKGPIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPVLVEGRAICLHPLVCKGFNADFDGDQMAVHV 160
Cdd:CHL00018  420 ASNIRAAKSKIREKEPIVWEILQEVMQGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVCKGFNADFDGDQMAVHV 499

                  ....*....
gi 1002153229 161 PLSLEAQAE 169
Cdd:CHL00018  500 PLSLEAQAE 508
 
Name Accession Description Interval E-value
rpoC1 CHL00018
RNA polymerase beta' subunit
1-169 5.05e-145

RNA polymerase beta' subunit


Pssm-ID: 214336 [Multi-domain]  Cd Length: 663  Bit Score: 417.00  E-value: 5.05e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229   1 IRGQPMRDGHNKVYKSFSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVICSLIRQHL 80
Cdd:CHL00018  340 IRGQPMRDGHNKPYKSFSDVIEGKEGRFRENLLGKRVDYSGRSVIVVGPSLSLHQCGLPREIAIELFQPFVIRGLIRQHL 419
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229  81 ASNIGVAKSQIRDKGPIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPVLVEGRAICLHPLVCKGFNADFDGDQMAVHV 160
Cdd:CHL00018  420 ASNIRAAKSKIREKEPIVWEILQEVMQGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVCKGFNADFDGDQMAVHV 499

                  ....*....
gi 1002153229 161 PLSLEAQAE 169
Cdd:CHL00018  500 PLSLEAQAE 508
RNAP_beta'_N cd01609
Largest subunit (beta') of bacterial DNA-dependent RNA polymerase (RNAP), N-terminal domain; ...
2-169 2.70e-117

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: 345.66  E-value: 2.70e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229   2 RGQPMRDGHNKVYKSFSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVICSLIRQHLA 81
Cdd:cd01609   217 RGKPVTGANNRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPELKLHQCGLPKEMALELFKPFVIRELIERGLA 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229  82 SNIGVAKSQIRDKGPIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPVLVEGRAICLHPLVCKGFNADFDGDQMAVHVP 161
Cdd:cd01609   297 PNIKSAKKMIERKDPEVWDILEEVIKGHPVLLNRAPTLHRLGIQAFEPVLIEGKAIQLHPLVCTAFNADFDGDQMAVHVP 376

                  ....*...
gi 1002153229 162 LSLEAQAE 169
Cdd:cd01609   377 LSLEAQAE 384
RpoC COG0086
DNA-directed RNA polymerase, beta' subunit/160 kD subunit [Transcription]; DNA-directed RNA ...
2-169 4.20e-95

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: 298.23  E-value: 4.20e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229    2 RGQPMRDGHNKVYKSFSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVICSLIRQHLA 81
Cdd:COG0086    302 RGRAVTGANKRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPELKLHQCGLPKKMALELFKPFIYRKLEERGLA 381
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229   82 SNIGVAKSQIRDKGPIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPVLVEGRAICLHPLVCKGFNADFDGDQMAVHVP 161
Cdd:COG0086    382 TTIKSAKKMVEREEPEVWDILEEVIKEHPVLLNRAPTLHRLGIQAFEPVLIEGKAIQLHPLVCTAFNADFDGDQMAVHVP 461

                   ....*...
gi 1002153229  162 LSLEAQAE 169
Cdd:COG0086    462 LSLEAQLE 469
rpoC_TIGR TIGR02386
DNA-directed RNA polymerase, beta' subunit, predominant form; Bacteria have a single ...
2-169 3.62e-93

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: 292.72  E-value: 3.62e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229    2 RGQPMRDGHNKVYKSFSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVICSLIRQHLA 81
Cdd:TIGR02386  294 RGKPVVGKNNRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPELKMYQCGLPKKMALELFKPFIIKRLIDRELA 373
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229   82 SNIGVAKSQIRDKGPIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPVLVEGRAICLHPLVCKGFNADFDGDQMAVHVP 161
Cdd:TIGR02386  374 ANIKSAKKMIEQEDPEVWDVLEDVIKEHPVLLNRAPTLHRLGIQAFEPVLVEGKAIRLHPLVCTAFNADFDGDQMAVHVP 453

                   ....*...
gi 1002153229  162 LSLEAQAE 169
Cdd:TIGR02386  454 LSPEAQAE 461
RPOLA_N smart00663
RNA polymerase I subunit A N-terminus;
1-169 3.81e-89

RNA polymerase I subunit A N-terminus;


Pssm-ID: 214767 [Multi-domain]  Cd Length: 295  Bit Score: 262.07  E-value: 3.81e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229    1 IRGQPMRDGhnKVYKSFSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVICSLIRQHL 80
Cdd:smart00663  78 LPRANQKSG--RPLKSLSQRLKGKEGRFRQNLLGKRVDFSARSVITPDPNLKLNEVGVPKEIALELTFPEIVTPLNIDKL 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229   81 ------------------ASNIGVAK-SQIRDKGPIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPVLVEGRAICLHP 141
Cdd:smart00663 156 rklvrngpngakyiirgkKTNLKLAKkSKIANHLKIGDIVERHVIDGDVVLFNRQPTLHRMSIQAHRVRVLEGKTIRLNP 235
                          170       180
                   ....*....|....*....|....*...
gi 1002153229  142 LVCKGFNADFDGDQMAVHVPLSLEAQAE 169
Cdd:smart00663 236 LVCSPYNADFDGDEMNLHVPQSLEARAE 263
RNA_pol_Rpb1_2 pfam00623
RNA polymerase Rpb1, domain 2; RNA polymerases catalyze the DNA dependent polymerization of ...
34-169 6.30e-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: 145.52  E-value: 6.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229  34 GKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVICSLIRQHL--ASNIG-----VAKSQIRDKGPII-------- 98
Cdd:pfam00623   1 GKRVDFSARTVISPDPNLKLDEVGVPISFAKTLTFPEIVTPYNIKRLrqLVENGpnvypGANYIIRINGARRdlryqkrr 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002153229  99 --------WEILQEVMRGHPVLLNRAPTLHRLGIQAFQPVLVEGRAICLHPLVCKGFNADFDGDQMAVHVPLSLEAQAE 169
Cdd:pfam00623  81 ldkeleigDIVERHVIDGDVVLFNRQPSLHRLSIMGHRVRVLPGKTFRLNLSVTTPYNADFDGDEMNLHVPQSEEARAE 159
 
Name Accession Description Interval E-value
rpoC1 CHL00018
RNA polymerase beta' subunit
1-169 5.05e-145

RNA polymerase beta' subunit


Pssm-ID: 214336 [Multi-domain]  Cd Length: 663  Bit Score: 417.00  E-value: 5.05e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229   1 IRGQPMRDGHNKVYKSFSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVICSLIRQHL 80
Cdd:CHL00018  340 IRGQPMRDGHNKPYKSFSDVIEGKEGRFRENLLGKRVDYSGRSVIVVGPSLSLHQCGLPREIAIELFQPFVIRGLIRQHL 419
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229  81 ASNIGVAKSQIRDKGPIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPVLVEGRAICLHPLVCKGFNADFDGDQMAVHV 160
Cdd:CHL00018  420 ASNIRAAKSKIREKEPIVWEILQEVMQGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVCKGFNADFDGDQMAVHV 499

                  ....*....
gi 1002153229 161 PLSLEAQAE 169
Cdd:CHL00018  500 PLSLEAQAE 508
RNAP_beta'_N cd01609
Largest subunit (beta') of bacterial DNA-dependent RNA polymerase (RNAP), N-terminal domain; ...
2-169 2.70e-117

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: 345.66  E-value: 2.70e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229   2 RGQPMRDGHNKVYKSFSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVICSLIRQHLA 81
Cdd:cd01609   217 RGKPVTGANNRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPELKLHQCGLPKEMALELFKPFVIRELIERGLA 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229  82 SNIGVAKSQIRDKGPIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPVLVEGRAICLHPLVCKGFNADFDGDQMAVHVP 161
Cdd:cd01609   297 PNIKSAKKMIERKDPEVWDILEEVIKGHPVLLNRAPTLHRLGIQAFEPVLIEGKAIQLHPLVCTAFNADFDGDQMAVHVP 376

                  ....*...
gi 1002153229 162 LSLEAQAE 169
Cdd:cd01609   377 LSLEAQAE 384
PRK00566 PRK00566
DNA-directed RNA polymerase subunit beta'; Provisional
2-169 1.81e-105

DNA-directed RNA polymerase subunit beta'; Provisional


Pssm-ID: 234794 [Multi-domain]  Cd Length: 1156  Bit Score: 325.87  E-value: 1.81e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229    2 RGQPMRDGHNKVYKSFSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVICSLIRQHLA 81
Cdd:PRK00566   302 RGRPVTGPNNRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPELKLHQCGLPKKMALELFKPFIMKKLVERGLA 381
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229   82 SNIGVAKSQIRDKGPIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPVLVEGRAICLHPLVCKGFNADFDGDQMAVHVP 161
Cdd:PRK00566   382 TTIKSAKKMVEREDPEVWDVLEEVIKEHPVLLNRAPTLHRLGIQAFEPVLIEGKAIQLHPLVCTAFNADFDGDQMAVHVP 461

                   ....*...
gi 1002153229  162 LSLEAQAE 169
Cdd:PRK00566   462 LSLEAQAE 469
rpoC1 PRK02625
DNA-directed RNA polymerase subunit gamma; Provisional
2-169 6.66e-97

DNA-directed RNA polymerase subunit gamma; Provisional


Pssm-ID: 235055 [Multi-domain]  Cd Length: 627  Bit Score: 292.42  E-value: 6.66e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229   2 RGQPMRDGHNKVYKSFSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVICSLIRQHLA 81
Cdd:PRK02625  320 RGRTVVGANNRPLKSLSDIIEGKQGRFRQNLLGKRVDYSGRSVIVVGPKLKMHQCGLPKEMAIELFQPFVIHRLIRQGIV 399
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229  82 SNIGVAKSQIRDKGPIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPVLVEGRAICLHPLVCKGFNADFDGDQMAVHVP 161
Cdd:PRK02625  400 NNIKAAKKLIQRADPEVWQVLEEVIEGHPVLLNRAPTLHRLGIQAFEPILVEGRAIQLHPLVCPAFNADFDGDQMAVHVP 479

                  ....*...
gi 1002153229 162 LSLEAQAE 169
Cdd:PRK02625  480 LSLEAQAE 487
RpoC COG0086
DNA-directed RNA polymerase, beta' subunit/160 kD subunit [Transcription]; DNA-directed RNA ...
2-169 4.20e-95

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: 298.23  E-value: 4.20e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229    2 RGQPMRDGHNKVYKSFSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVICSLIRQHLA 81
Cdd:COG0086    302 RGRAVTGANKRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPELKLHQCGLPKKMALELFKPFIYRKLEERGLA 381
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229   82 SNIGVAKSQIRDKGPIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPVLVEGRAICLHPLVCKGFNADFDGDQMAVHVP 161
Cdd:COG0086    382 TTIKSAKKMVEREEPEVWDILEEVIKEHPVLLNRAPTLHRLGIQAFEPVLIEGKAIQLHPLVCTAFNADFDGDQMAVHVP 461

                   ....*...
gi 1002153229  162 LSLEAQAE 169
Cdd:COG0086    462 LSLEAQLE 469
rpoC_TIGR TIGR02386
DNA-directed RNA polymerase, beta' subunit, predominant form; Bacteria have a single ...
2-169 3.62e-93

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: 292.72  E-value: 3.62e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229    2 RGQPMRDGHNKVYKSFSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVICSLIRQHLA 81
Cdd:TIGR02386  294 RGKPVVGKNNRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPELKMYQCGLPKKMALELFKPFIIKRLIDRELA 373
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229   82 SNIGVAKSQIRDKGPIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPVLVEGRAICLHPLVCKGFNADFDGDQMAVHVP 161
Cdd:TIGR02386  374 ANIKSAKKMIEQEDPEVWDVLEDVIKEHPVLLNRAPTLHRLGIQAFEPVLVEGKAIRLHPLVCTAFNADFDGDQMAVHVP 453

                   ....*...
gi 1002153229  162 LSLEAQAE 169
Cdd:TIGR02386  454 LSPEAQAE 461
RPOLA_N smart00663
RNA polymerase I subunit A N-terminus;
1-169 3.81e-89

RNA polymerase I subunit A N-terminus;


Pssm-ID: 214767 [Multi-domain]  Cd Length: 295  Bit Score: 262.07  E-value: 3.81e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229    1 IRGQPMRDGhnKVYKSFSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVICSLIRQHL 80
Cdd:smart00663  78 LPRANQKSG--RPLKSLSQRLKGKEGRFRQNLLGKRVDFSARSVITPDPNLKLNEVGVPKEIALELTFPEIVTPLNIDKL 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229   81 ------------------ASNIGVAK-SQIRDKGPIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPVLVEGRAICLHP 141
Cdd:smart00663 156 rklvrngpngakyiirgkKTNLKLAKkSKIANHLKIGDIVERHVIDGDVVLFNRQPTLHRMSIQAHRVRVLEGKTIRLNP 235
                          170       180
                   ....*....|....*....|....*...
gi 1002153229  142 LVCKGFNADFDGDQMAVHVPLSLEAQAE 169
Cdd:smart00663 236 LVCSPYNADFDGDEMNLHVPQSLEARAE 263
PRK14906 PRK14906
DNA-directed RNA polymerase subunit beta';
2-169 3.33e-81

DNA-directed RNA polymerase subunit beta';


Pssm-ID: 184899 [Multi-domain]  Cd Length: 1460  Bit Score: 261.34  E-value: 3.33e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229    2 RGQPMRDGHNKVYKSFSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVICSLIRQHLA 81
Cdd:PRK14906   390 RGRPVTGPGNRPLKSLADMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPHLKLHQCGLPSAMALELFKPFVMKRLVELEYA 469
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229   82 SNIGVAKSQIRDKGPIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPVLVEGRAICLHPLVCKGFNADFDGDQMAVHVP 161
Cdd:PRK14906   470 ANIKAAKRAVDRGASYVWDVLEEVIQDHPVLLNRAPTLHRLGIQAFEPVLVEGKAIKLHPLVCTAFNADFDGDQMAVHVP 549

                   ....*...
gi 1002153229  162 LSLEAQAE 169
Cdd:PRK14906   550 LSTQAQAE 557
PRK14844 PRK14844
DNA-directed RNA polymerase subunit beta/beta';
15-169 3.67e-73

DNA-directed RNA polymerase subunit beta/beta';


Pssm-ID: 173305 [Multi-domain]  Cd Length: 2836  Bit Score: 238.37  E-value: 3.67e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229   15 KSFSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVICSLIRQHLASNIGVAKSQIRDK 94
Cdd:PRK14844  1758 KSISDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPTLKLNQCGLPKRMALELFKPFVYSKLKMYGMAPTIKFASKLIRAE 1837
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002153229   95 GPIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPVLVEGRAICLHPLVCKGFNADFDGDQMAVHVPLSLEAQAE 169
Cdd:PRK14844  1838 KPEVWDMLEEVIKEHPVLLNRAPTLHRLGIQAFEPILIEGKAIQLHPLVCTAFNADFDGDQMAVHVPISLEAQLE 1912
PRK09603 PRK09603
DNA-directed RNA polymerase subunit beta/beta';
9-169 1.35e-68

DNA-directed RNA polymerase subunit beta/beta';


Pssm-ID: 181983 [Multi-domain]  Cd Length: 2890  Bit Score: 225.19  E-value: 1.35e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229    9 GHNK-VYKSFSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVICSLIRQHLASNIGVA 87
Cdd:PRK09603  1707 GANKrPLKSLSEIIKGKQGRFRQNLLGKRVDFSGRSVIVVGPNLKMDECGLPKNMALELFKPHLLSKLEERGYATTLKQA 1786
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229   88 KSQIRDKGPIIWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPVLVEGRAICLHPLVCKGFNADFDGDQMAVHVPLSLEAQ 167
Cdd:PRK09603  1787 KRMIEQKSNEVWECLQEITEGYPVLLNRAPTLHKQSIQAFHPKLIDGKAIQLHPLVCSAFNADFDGDQMAVHVPLSQEAI 1866

                   ..
gi 1002153229  168 AE 169
Cdd:PRK09603  1867 AE 1868
RNAP_largest_subunit_N cd00399
Largest subunit of RNA polymerase (RNAP), N-terminal domain; This region represents the ...
1-169 1.15e-57

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: 188.03  E-value: 1.15e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229   1 IRGQPMRDGHNKVYKSFSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELfqafvicslirqhl 80
Cdd:cd00399   124 IAGQPQTQKSGRPLRSLAQRLKGKEGRFRGNLMGKRVDFSGRSVISPDPNLRLDQVGVPKSIALTL-------------- 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229  81 asnigvaksqirdkgpiiweilqevmRGHPVLLNRAPTLHRLGIQAFQPVLVEGRAICLHPLVCKGFNADFDGDQMAVHV 160
Cdd:cd00399   190 --------------------------DGDPVLFNRQPSLHKLSIMAHRVRVLPGSTFRLNPLVCSPYNADFDGDEMNLHV 243

                  ....*....
gi 1002153229 161 PLSLEAQAE 169
Cdd:cd00399   244 PQSEEARAE 252
RNA_pol_Rpb1_2 pfam00623
RNA polymerase Rpb1, domain 2; RNA polymerases catalyze the DNA dependent polymerization of ...
34-169 6.30e-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: 145.52  E-value: 6.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229  34 GKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVICSLIRQHL--ASNIG-----VAKSQIRDKGPII-------- 98
Cdd:pfam00623   1 GKRVDFSARTVISPDPNLKLDEVGVPISFAKTLTFPEIVTPYNIKRLrqLVENGpnvypGANYIIRINGARRdlryqkrr 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002153229  99 --------WEILQEVMRGHPVLLNRAPTLHRLGIQAFQPVLVEGRAICLHPLVCKGFNADFDGDQMAVHVPLSLEAQAE 169
Cdd:pfam00623  81 ldkeleigDIVERHVIDGDVVLFNRQPSLHRLSIMGHRVRVLPGKTFRLNLSVTTPYNADFDGDEMNLHVPQSEEARAE 159
RNAP_archeal_A' cd02582
A' subunit of archaeal RNA polymerase (RNAP); A' is the largest subunit of the archaeal RNA ...
5-169 2.03e-35

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: 130.06  E-value: 2.03e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229   5 PMRDGHNKVYKSFSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVICslirqhlASNI 84
Cdd:cd02582   284 PARHRSGRPLKTLAQRLKGKEGRFRGNLSGKRVNFSARTVISPDPNLSINEVGVPEDIAKELTVPERVT-------EWNI 356
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229  85 GVAKSQIRDkGPIIW----------------------EILQEV----------MRGHPVLLNRAPTLHRLGIQAFQPVLV 132
Cdd:cd02582   357 EKMRKLVLN-GPDKWpganyvirpdgrrirlryvnreELAERLepgwiverhlIDGDIVLFNRQPSLHRMSIMAHRVRVL 435
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1002153229 133 EGRAICLHPLVCKGFNADFDGDQMAVHVPLSLEAQAE 169
Cdd:cd02582   436 PGKTFRLNLAVCPPYNADFDGDEMNLHVPQSEEARAE 472
PRK08566 PRK08566
DNA-directed RNA polymerase subunit A'; Validated
23-169 1.30e-32

DNA-directed RNA polymerase subunit A'; Validated


Pssm-ID: 236292 [Multi-domain]  Cd Length: 882  Bit Score: 122.27  E-value: 1.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229  23 GKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVICSLirqhlasNIGVAKSQIRdKGPIIW--- 99
Cdd:PRK08566  306 GKEGRFRGNLSGKRVNFSARTVISPDPNLSINEVGVPEAIAKELTVPERVTEW-------NIEELREYVL-NGPEKHpga 377
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229 100 ------------------EILQE-------VMR----GHPVLLNRAPTLHRLGIQAFQPVLVEGRAICLHPLVCKGFNAD 150
Cdd:PRK08566  378 nyvirpdgrrikltdknkEELAEklepgwiVERhlidGDIVLFNRQPSLHRMSIMAHRVRVLPGKTFRLNLAVCPPYNAD 457
                         170
                  ....*....|....*....
gi 1002153229 151 FDGDQMAVHVPLSLEAQAE 169
Cdd:PRK08566  458 FDGDEMNLHVPQTEEARAE 476
PRK14977 PRK14977
bifunctional DNA-directed RNA polymerase A'/A'' subunit; Provisional
4-169 9.36e-30

bifunctional DNA-directed RNA polymerase A'/A'' subunit; Provisional


Pssm-ID: 184940 [Multi-domain]  Cd Length: 1321  Bit Score: 113.97  E-value: 9.36e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229    4 QPMRDGHNKVYKSFSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIA-------------IELFQAF 70
Cdd:PRK14977   297 QAHHKGSGRPLKSLFQRLKGKEGRFRGNLIGKRVDFSARTVISPDPMIDIDEVGVPEAIAmkltipeivnennIEKMKEL 376
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229   71 VI--------CSLIRQHLASNIGVAKSQIRDKGPI--IWEILQ-------EVMRGHPVLLNRAPTLHRLGIQAFQPVLVE 133
Cdd:PRK14977   377 VIngpdefpgANAIRKGDGTKIRLDFLEDKGKDALreAAEQLEigdiverHLADGDIVIFNRQPSLHKLSILAHRVKVLP 456
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1002153229  134 GRAICLHPLVCKGFNADFDGDQMAVHVPLSLEAQAE 169
Cdd:PRK14977   457 GATFRLHPAVCPPYNADFDGDEMNLHVPQIEDARAE 492
RNAP_II_RPB1_N cd02733
Largest subunit (Rpb1) of eukaryotic RNA polymerase II (RNAP II), N-terminal domain; The two ...
1-169 5.33e-28

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: 108.78  E-value: 5.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229   1 IRGQPM---RDGhnKVYKSFSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAI-----ELFQAFVI 72
Cdd:cd02733   202 IPGLPQatqKSG--RPLKSIRQRLKGKEGRIRGNLMGKRVDFSARTVITPDPNLELDQVGVPRSIAMnltfpEIVTPFNI 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229  73 CSLirQHLASNiGV-----AKSQIRDKGPII---------WEILQE---VMR----GHPVLLNRAPTLHRLGIQAFqpvl 131
Cdd:cd02733   280 DRL--QELVRN-GPneypgAKYIIRDDGERIdlrylkkasDLHLQYgyiVERhlqdGDVVLFNRQPSLHKMSMMGH---- 352
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1002153229 132 vegRAICLHPL-------VCKGFNADFDGDQMAVHVPLSLEAQAE 169
Cdd:cd02733   353 ---RVKVLPYStfrlnlsVTTPYNADFDGDEMNLHVPQSLETRAE 394
RNAP_III_RPC1_N cd02583
Largest subunit (RPC1) of eukaryotic RNA polymerase III (RNAP III), N-terminal domain; Rpc1 ...
23-169 2.31e-27

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: 106.86  E-value: 2.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229  23 GKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIA-------------IELFQAFVI---------CSLI---- 76
Cdd:cd02583   275 GKQGRFRGNLSGKRVDFSGRTVISPDPNLRIDQVGVPEHVAkiltypervtrynIEKLRKLVLngpdvhpgaNFVIkrdg 354
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229  77 ----------RQHLASNIgvaksQIRDKgpiiweILQEVMRGHPVLLNRAPTLHRLGIQAFQPVLVEGRAICLHPLVCKG 146
Cdd:cd02583   355 gkkkflkygnRRKIAREL-----KIGDI------VERHLEDGDIVLFNRQPSLHRLSIMAHRAKVMPWRTFRFNECVCTP 423
                         170       180
                  ....*....|....*....|...
gi 1002153229 147 FNADFDGDQMAVHVPLSLEAQAE 169
Cdd:cd02583   424 YNADFDGDEMNLHVPQTEEARAE 446
RNAP_I_RPA1_N cd01435
Largest subunit (RPA1) of eukaryotic RNA polymerase I (RNAP I), N-terminal domain; RPA1 is the ...
20-169 9.77e-22

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: 90.71  E-value: 9.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229  20 VIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAI--------------ELFQAFVI-------CSLIRQ 78
Cdd:cd01435   233 LLEKKEGLFRMNMMGKRVNYAARSVISPDPFIETNEIGIPLVFAKkltfpepvtpfnveELRQAVINgpdvypgANAIED 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229  79 HLASNIGVAKSQIRDKGPIIWEILQE------------VMR----GHPVLLNRAPTLHRLGIQAFQ-PVLVEGRAICLHP 141
Cdd:cd01435   313 EDGRLILLSALSEERRKALAKLLLLLssaklllngpkkVYRhlldGDVVLLNRQPTLHKPSIMAHKvRVLPGEKTLRLHY 392
                         170       180
                  ....*....|....*....|....*...
gi 1002153229 142 LVCKGFNADFDGDQMAVHVPLSLEAQAE 169
Cdd:cd01435   393 ANCKSYNADFDGDEMNLHFPQSELARAE 420
RNAP_IV_RPD1_N cd10506
Largest subunit (NRPD1) of higher plant RNA polymerase IV, N-terminal domain; NRPD1 and NRPE1 ...
28-169 9.46e-21

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: 88.23  E-value: 9.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229  28 FRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIEL----------FQAFVICSLIRQHLASNIGVAKSQIRD---- 93
Cdd:cd10506   206 MKDLLLGKRSGHSFRSVVVGDPYLELNEIGIPCEIAERLtvservsswnRERLQEYCDLTLLLKGVIGVRRNGRLVgvrs 285
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002153229  94 -----KGPIIWEILQEvmrGHPVLLNRAPTLHRLGIQAFQ-PVLVEGRAICLHPLVCKGFNADFDGDQMAVHVPLSLEAQ 167
Cdd:cd10506   286 hntlqIGDVIHRPLVD---GDVVLVNRPPSIHQHSLIALSvKVLPTNSVVSINPLCCSPFRGDFDGDCLHGYIPQSLQAR 362

                  ..
gi 1002153229 168 AE 169
Cdd:cd10506   363 AE 364
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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