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Conserved domains on  [gi|568984179|ref|XP_006517573|]
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poly(A) RNA polymerase GLD2 isoform X1 [Mus musculus]

Protein Classification

nucleotidyltransferase domain-containing protein( domain architecture ID 1001423)

nucleotidyltransferase domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TRF4 super family cl34961
DNA polymerase sigma [Replication, recombination and repair];
121-468 1.96e-37

DNA polymerase sigma [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG5260:

Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 143.37  E-value: 1.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984179 121 FHTHYIPDIVRCVPpLREIPLLEPREITLPEAkDKLSQQILELFETCQQQASDLKKKELCRAQLQREIQLLFPQSRLFLV 200
Cdd:COG5260   24 EQKERRPLDAKKVS-IQELLELSIDSVFNEES-DELTSELLEFYDYIAPSDEELKRRKALLEKLRTLLKKEFPDADLKVF 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984179 201 GSSLNGFGARSSDGDLCLVVKEEPCFFQVNQKTEARHiltlvhkhfCTRLSGYIERPQLIRAKVPIVKFRDKVSCVEFDL 280
Cdd:COG5260  102 GSTETGLALPKSDIDLCIISDPRGYKETRNAGSLASH---------LFKKNLAKEVVVVSTARVPIIKLVDPQSGLHCDI 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984179 281 NVNNTVGIRNTFLLRTYAYLENRVRPLVLVIKKWASHHDINDASRGTLSSYSLVLMVLHYLQTLPEPilpslqkiypesf 360
Cdd:COG5260  173 SFNNTNGIVNAKLIRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSSYTISCMVLSFLQMHPPF------------- 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984179 361 stsvqlhLVHHAPCNVPPYLSKNESSLGDLLLGFLKYYATEFDWNTQMISVREAKAIPRPDDMEW----RNKYICVEEPF 436
Cdd:COG5260  240 -------LFFDNGLLSPLKYNKNIDNLGVLFDDFFELYGKSFNYSLVVLSINSGDFYLPKYEKGWlkpsKPNSLSIQDPG 312
                        330       340       350
                 ....*....|....*....|....*....|...
gi 568984179 437 -DGTNTARAVHEKQKfdMIKDQFLKSWQRLKNK 468
Cdd:COG5260  313 tDRNNDISAVSFNIK--DIKAAFIRAFELLSNK 343
 
Name Accession Description Interval E-value
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
121-468 1.96e-37

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 143.37  E-value: 1.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984179 121 FHTHYIPDIVRCVPpLREIPLLEPREITLPEAkDKLSQQILELFETCQQQASDLKKKELCRAQLQREIQLLFPQSRLFLV 200
Cdd:COG5260   24 EQKERRPLDAKKVS-IQELLELSIDSVFNEES-DELTSELLEFYDYIAPSDEELKRRKALLEKLRTLLKKEFPDADLKVF 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984179 201 GSSLNGFGARSSDGDLCLVVKEEPCFFQVNQKTEARHiltlvhkhfCTRLSGYIERPQLIRAKVPIVKFRDKVSCVEFDL 280
Cdd:COG5260  102 GSTETGLALPKSDIDLCIISDPRGYKETRNAGSLASH---------LFKKNLAKEVVVVSTARVPIIKLVDPQSGLHCDI 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984179 281 NVNNTVGIRNTFLLRTYAYLENRVRPLVLVIKKWASHHDINDASRGTLSSYSLVLMVLHYLQTLPEPilpslqkiypesf 360
Cdd:COG5260  173 SFNNTNGIVNAKLIRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSSYTISCMVLSFLQMHPPF------------- 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984179 361 stsvqlhLVHHAPCNVPPYLSKNESSLGDLLLGFLKYYATEFDWNTQMISVREAKAIPRPDDMEW----RNKYICVEEPF 436
Cdd:COG5260  240 -------LFFDNGLLSPLKYNKNIDNLGVLFDDFFELYGKSFNYSLVVLSINSGDFYLPKYEKGWlkpsKPNSLSIQDPG 312
                        330       340       350
                 ....*....|....*....|....*....|...
gi 568984179 437 -DGTNTARAVHEKQKfdMIKDQFLKSWQRLKNK 468
Cdd:COG5260  313 tDRNNDISAVSFNIK--DIKAAFIRAFELLSNK 343
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
176-298 5.12e-31

Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; Poly(A) polymerases (PAPs) catalyze mRNA poly(A) tail synthesis, and terminal uridylyl transferases (TUTases) uridylate RNA. PAPs in this subgroup include human PAP alpha, mouse testis-specific cytoplasmic PAP beta, human nuclear PAP gamma, Saccharomyces cerevisiae PAP1, TRF4 and-5, Schizosaccharomyces pombe caffeine-induced death proteins -1, and -14, Caenorhabditis elegans Germ Line Development-2, and Chlamydomonas reinhardtii MUT68. This family also includes human U6 snRNA-specific TUTase1, and Trypanosoma brucei 3'-TUTase-1,-2, and 4. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.


Pssm-ID: 143392 [Multi-domain]  Cd Length: 114  Bit Score: 115.73  E-value: 5.12e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984179 176 KKELCRAQLQREIQLLFPQSRLFLVGSSLNGFGARSSDGDLCLVVKeepcffqvNQKTEARHILTLVHKHFCtRLSGYIE 255
Cdd:cd05402    1 KREEVLDRLQELIKEWFPGAKLYPFGSYVTGLGLPGSDIDLCLLGP--------NHRVDREDFLRKLAKLLK-KSGEVVE 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568984179 256 RPQLIRAKVPIVKFRDKVSCVEFDLNVNNTVGIRNTFLLRTYA 298
Cdd:cd05402   72 VEPIINARVPIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
PAP_assoc pfam03828
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ...
386-440 1.31e-14

Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown to have polynucleotide adenylyltransferase activity. Proteins in this family have been located to both the nucleus and the cytoplasm.


Pssm-ID: 427532  Cd Length: 60  Bit Score: 67.98  E-value: 1.31e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568984179  386 SLGDLLLGFLKYYATEFDWNTQMISVREAKAIPRpDDMEW------RNKYICVEEPFDGTN 440
Cdd:pfam03828   1 SLGELLIGFFEYYGREFDYENVVISIRTGGILSK-KEKGWlrnegrRPFLLCIEDPFDLDN 60
 
Name Accession Description Interval E-value
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
121-468 1.96e-37

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 143.37  E-value: 1.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984179 121 FHTHYIPDIVRCVPpLREIPLLEPREITLPEAkDKLSQQILELFETCQQQASDLKKKELCRAQLQREIQLLFPQSRLFLV 200
Cdd:COG5260   24 EQKERRPLDAKKVS-IQELLELSIDSVFNEES-DELTSELLEFYDYIAPSDEELKRRKALLEKLRTLLKKEFPDADLKVF 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984179 201 GSSLNGFGARSSDGDLCLVVKEEPCFFQVNQKTEARHiltlvhkhfCTRLSGYIERPQLIRAKVPIVKFRDKVSCVEFDL 280
Cdd:COG5260  102 GSTETGLALPKSDIDLCIISDPRGYKETRNAGSLASH---------LFKKNLAKEVVVVSTARVPIIKLVDPQSGLHCDI 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984179 281 NVNNTVGIRNTFLLRTYAYLENRVRPLVLVIKKWASHHDINDASRGTLSSYSLVLMVLHYLQTLPEPilpslqkiypesf 360
Cdd:COG5260  173 SFNNTNGIVNAKLIRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSSYTISCMVLSFLQMHPPF------------- 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984179 361 stsvqlhLVHHAPCNVPPYLSKNESSLGDLLLGFLKYYATEFDWNTQMISVREAKAIPRPDDMEW----RNKYICVEEPF 436
Cdd:COG5260  240 -------LFFDNGLLSPLKYNKNIDNLGVLFDDFFELYGKSFNYSLVVLSINSGDFYLPKYEKGWlkpsKPNSLSIQDPG 312
                        330       340       350
                 ....*....|....*....|....*....|...
gi 568984179 437 -DGTNTARAVHEKQKfdMIKDQFLKSWQRLKNK 468
Cdd:COG5260  313 tDRNNDISAVSFNIK--DIKAAFIRAFELLSNK 343
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
176-298 5.12e-31

Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; Poly(A) polymerases (PAPs) catalyze mRNA poly(A) tail synthesis, and terminal uridylyl transferases (TUTases) uridylate RNA. PAPs in this subgroup include human PAP alpha, mouse testis-specific cytoplasmic PAP beta, human nuclear PAP gamma, Saccharomyces cerevisiae PAP1, TRF4 and-5, Schizosaccharomyces pombe caffeine-induced death proteins -1, and -14, Caenorhabditis elegans Germ Line Development-2, and Chlamydomonas reinhardtii MUT68. This family also includes human U6 snRNA-specific TUTase1, and Trypanosoma brucei 3'-TUTase-1,-2, and 4. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.


Pssm-ID: 143392 [Multi-domain]  Cd Length: 114  Bit Score: 115.73  E-value: 5.12e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568984179 176 KKELCRAQLQREIQLLFPQSRLFLVGSSLNGFGARSSDGDLCLVVKeepcffqvNQKTEARHILTLVHKHFCtRLSGYIE 255
Cdd:cd05402    1 KREEVLDRLQELIKEWFPGAKLYPFGSYVTGLGLPGSDIDLCLLGP--------NHRVDREDFLRKLAKLLK-KSGEVVE 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568984179 256 RPQLIRAKVPIVKFRDKVSCVEFDLNVNNTVGIRNTFLLRTYA 298
Cdd:cd05402   72 VEPIINARVPIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
PAP_assoc pfam03828
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ...
386-440 1.31e-14

Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown to have polynucleotide adenylyltransferase activity. Proteins in this family have been located to both the nucleus and the cytoplasm.


Pssm-ID: 427532  Cd Length: 60  Bit Score: 67.98  E-value: 1.31e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568984179  386 SLGDLLLGFLKYYATEFDWNTQMISVREAKAIPRpDDMEW------RNKYICVEEPFDGTN 440
Cdd:pfam03828   1 SLGELLIGFFEYYGREFDYENVVISIRTGGILSK-KEKGWlrnegrRPFLLCIEDPFDLDN 60
 
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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