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Conserved domains on  [gi|394792899|gb|AFN40975|]
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RNA polymerase II beta subunit, partial [Alternaria cucurbitae]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK09606 super family cl35871
DNA-directed RNA polymerase subunit B''; Validated
3-182 2.11e-52

DNA-directed RNA polymerase subunit B''; Validated


The actual alignment was detected with superfamily member PRK09606:

Pssm-ID: 236587 [Multi-domain]  Cd Length: 494  Bit Score: 174.37  E-value: 2.11e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394792899   3 VQDRETALDFIAKRGANSGTKDRRLKFARDIMQREFLPHISQKEGQDTRKAYFFGYMIHRLLQCVLGRRDEDDRDHFGKK 82
Cdd:PRK09606 257 VDTQEEALEYIGKRVAPGQTKEYRIKRAEYVIDRYLLPHLGVEPEVRRAKAHYLGRMAEACFELALGRREEDDKDHYANK 336
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394792899  83 RLDLAGPLVANLFRILFLKLTKDVyKY-LQRCVENNQDFNVQMAVKASIITNGLKYSLATGNWgdqkkaASAKAGVSQVL 161
Cdd:PRK09606 337 RLKLAGDLMEDLFRVAFNRLARDV-KYqLERANMRNRELSIKTAVRSDVLTERLEHAMATGNW------VGGRTGVSQLL 409
                        170       180
                 ....*....|....*....|.
gi 394792899 162 NRYTYASTLSHLRRTNTPVGR 182
Cdd:PRK09606 410 DRTDYMATLSHLRRVVSPLSR 430
 
Name Accession Description Interval E-value
PRK09606 PRK09606
DNA-directed RNA polymerase subunit B''; Validated
3-182 2.11e-52

DNA-directed RNA polymerase subunit B''; Validated


Pssm-ID: 236587 [Multi-domain]  Cd Length: 494  Bit Score: 174.37  E-value: 2.11e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394792899   3 VQDRETALDFIAKRGANSGTKDRRLKFARDIMQREFLPHISQKEGQDTRKAYFFGYMIHRLLQCVLGRRDEDDRDHFGKK 82
Cdd:PRK09606 257 VDTQEEALEYIGKRVAPGQTKEYRIKRAEYVIDRYLLPHLGVEPEVRRAKAHYLGRMAEACFELALGRREEDDKDHYANK 336
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394792899  83 RLDLAGPLVANLFRILFLKLTKDVyKY-LQRCVENNQDFNVQMAVKASIITNGLKYSLATGNWgdqkkaASAKAGVSQVL 161
Cdd:PRK09606 337 RLKLAGDLMEDLFRVAFNRLARDV-KYqLERANMRNRELSIKTAVRSDVLTERLEHAMATGNW------VGGRTGVSQLL 409
                        170       180
                 ....*....|....*....|.
gi 394792899 162 NRYTYASTLSHLRRTNTPVGR 182
Cdd:PRK09606 410 DRTDYMATLSHLRRVVSPLSR 430
RNA_pol_Rpb2_1 pfam04563
RNA polymerase beta subunit; RNA polymerases catalyze the DNA dependent polymerization of RNA. ...
3-133 7.94e-51

RNA polymerase beta subunit; 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 forms one of the two distinctive lobes of the Rpb2 structure. This domain is also known as the protrusion domain. The other lobe (pfam04561) is nested within this domain.


Pssm-ID: 367994 [Multi-domain]  Cd Length: 396  Bit Score: 168.33  E-value: 7.94e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394792899    3 VQDRETALDFIAKRGAN----SGTKDRRLKFARDIMQREFLPHISQKEGQDTRKAYFFGYMIHRLLQCVLGRRDEDDRDH 78
Cdd:pfam04563 262 IQTQEQALDYIGGRGRAifrmGRPREPRIKYAEEILQKEVLPHLGTYELDETKKAYFIGYMIRRLLLLALGRREVDDRDH 341
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 394792899   79 FGKKRLDLAGPLVANLFRILFLKLTKDVYKYLQRCVENNQDFNVQMAVKASIITN 133
Cdd:pfam04563 342 LGNKRLRLAGPLLASLFRVLFKKLVRDVRERLQKVLGSPDDLMLQLLVNAKPITS 396
 
Name Accession Description Interval E-value
PRK09606 PRK09606
DNA-directed RNA polymerase subunit B''; Validated
3-182 2.11e-52

DNA-directed RNA polymerase subunit B''; Validated


Pssm-ID: 236587 [Multi-domain]  Cd Length: 494  Bit Score: 174.37  E-value: 2.11e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394792899   3 VQDRETALDFIAKRGANSGTKDRRLKFARDIMQREFLPHISQKEGQDTRKAYFFGYMIHRLLQCVLGRRDEDDRDHFGKK 82
Cdd:PRK09606 257 VDTQEEALEYIGKRVAPGQTKEYRIKRAEYVIDRYLLPHLGVEPEVRRAKAHYLGRMAEACFELALGRREEDDKDHYANK 336
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394792899  83 RLDLAGPLVANLFRILFLKLTKDVyKY-LQRCVENNQDFNVQMAVKASIITNGLKYSLATGNWgdqkkaASAKAGVSQVL 161
Cdd:PRK09606 337 RLKLAGDLMEDLFRVAFNRLARDV-KYqLERANMRNRELSIKTAVRSDVLTERLEHAMATGNW------VGGRTGVSQLL 409
                        170       180
                 ....*....|....*....|.
gi 394792899 162 NRYTYASTLSHLRRTNTPVGR 182
Cdd:PRK09606 410 DRTDYMATLSHLRRVVSPLSR 430
PRK08565 PRK08565
DNA-directed RNA polymerase subunit B; Provisional
1-183 2.89e-51

DNA-directed RNA polymerase subunit B; Provisional


Pssm-ID: 236291 [Multi-domain]  Cd Length: 1103  Bit Score: 176.69  E-value: 2.89e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394792899    1 SVVQDRETALDFIAKRGANSGTKDRRLKFARDIMQREFLPHISQKEGQDTRKAYFFGYMIHRLLQCVLGRRDEDDRDHFG 80
Cdd:PRK08565  252 SIAATVEDALDYIGKRVAIGQPREYRIERAEQILDKYLLPHLGTSPEDRIKKAYFLGQMASKLLELYLGRREPDDKDHYA 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394792899   81 KKRLDLAGPLVANLFRILFLKLTKDVYKYLQRCVENNQDFNVQMAVKASIITNGLKYSLATGNWGdqkkaaSAKAGVSQV 160
Cdd:PRK08565  332 NKRLRLAGDLLAELFRVAFKQLVKDLKYQLEKSYARGRKLDLRAIVRPDIITERIRHALATGNWV------GGRTGVSQL 405
                         170       180
                  ....*....|....*....|...
gi 394792899  161 LNRYTYASTLSHLRRTNTPVGRD 183
Cdd:PRK08565  406 LDRTNYLSTLSHLRRVVSPLSRG 428
RNA_pol_Rpb2_1 pfam04563
RNA polymerase beta subunit; RNA polymerases catalyze the DNA dependent polymerization of RNA. ...
3-133 7.94e-51

RNA polymerase beta subunit; 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 forms one of the two distinctive lobes of the Rpb2 structure. This domain is also known as the protrusion domain. The other lobe (pfam04561) is nested within this domain.


Pssm-ID: 367994 [Multi-domain]  Cd Length: 396  Bit Score: 168.33  E-value: 7.94e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394792899    3 VQDRETALDFIAKRGAN----SGTKDRRLKFARDIMQREFLPHISQKEGQDTRKAYFFGYMIHRLLQCVLGRRDEDDRDH 78
Cdd:pfam04563 262 IQTQEQALDYIGGRGRAifrmGRPREPRIKYAEEILQKEVLPHLGTYELDETKKAYFIGYMIRRLLLLALGRREVDDRDH 341
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 394792899   79 FGKKRLDLAGPLVANLFRILFLKLTKDVYKYLQRCVENNQDFNVQMAVKASIITN 133
Cdd:pfam04563 342 LGNKRLRLAGPLLASLFRVLFKKLVRDVRERLQKVLGSPDDLMLQLLVNAKPITS 396
RNA_pol_Rpb2_2 pfam04561
RNA polymerase Rpb2, domain 2; RNA polymerases catalyze the DNA dependent polymerization of ...
1-85 2.41e-21

RNA polymerase Rpb2, 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). Rpb2 is the second largest subunit of the RNA polymerase. This domain forms one of the two distinctive lobes of the Rpb2 structure. This domain is also known as the lobe domain. DNA has been demonstrated to bind to the concave surface of the lobe domain, and plays a role in maintaining the transcription bubble. Many of the bacterial members contain large insertions within this domain, as region known as dispensable region 1 (DRI).


Pssm-ID: 398318 [Multi-domain]  Cd Length: 185  Bit Score: 86.25  E-value: 2.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394792899    1 SVVQDRETALDFIAKRGANSGTKDRRLKFARDIMQ-----REFLPHISQKEGQDTR--KAYFFGYMIHRLLQCVLGRRDE 73
Cdd:pfam04561  94 ENIYTQEEALDYIGKGFALRRGEEPRLQRAREILYsrdpkYNLNKHLGLNEPFENErlKAQDILYMIDRLLNLKLGRRKP 173
                          90
                  ....*....|..
gi 394792899   74 DDRDHFGKKRLD 85
Cdd:pfam04561 174 DDIDHLGNKRVR 185
RNA_pol_Rpb2_3 pfam04565
RNA polymerase Rpb2, domain 3; RNA polymerases catalyze the DNA dependent polymerization of ...
159-191 1.96e-07

RNA polymerase Rpb2, domain 3; 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). Domain 3, s also known as the fork domain and is proximal to catalytic site.


Pssm-ID: 428011 [Multi-domain]  Cd Length: 67  Bit Score: 46.37  E-value: 1.96e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 394792899  159 QVLNRYTYASTLSHLRRTNTPVG---RDGKLAKPRQ 191
Cdd:pfam04565   1 QVLDRTNYLSTLSHLRRVNSPRGglfREMKTTEVRD 36
 
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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