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Conserved domains on  [gi|2217354847|ref|XP_047272816|]
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poly(A) RNA polymerase GLD2 isoform X8 [Homo sapiens]

Protein Classification

nucleotidyltransferase domain-containing protein( domain architecture ID 10143992)

nucleotidyltransferase domain-containing protein similar to Trypanosoma brucei terminal uridylyltransferase 7 (TUTase 7) which, during post-transcriptional editing of mitochondrial RNA, catalyzes the addition of uridine (U) to ssRNA with a preference for a 3'-terminal U and adds the number of Us specified by a guide RNA to precleaved dsRNA editing substrates, and to Drosophila melanogaster Monkey king protein (Mkg)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
 176-323 4.46e-28

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: 106.10  E-value: 4.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354847 176 KKELCRTQLQREIQLLFPQSRLFLVGSSLNGFGTRSSDGDLCLVVKeepcffqvNQKTEARHILTLVHKHFCTRLCKSDM 255
Cdd:cd05402     1 KREEVLDRLQELIKEWFPGAKLYPFGSYVTGLGLPGSDIDLCLLGP--------NHRVDREDFLRKLAKLLKKSGEVVEV 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217354847 256 PQVcmspdvtllkmpltlssagyierpqlIRAKVPIVKFRDKVSCVEFDLNVNNIVGIRNTFLLRTYA 323
Cdd:cd05402    73 EPI--------------------------INARVPIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
 
Name Accession Description Interval E-value
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
 176-323 4.46e-28

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: 106.10  E-value: 4.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354847 176 KKELCRTQLQREIQLLFPQSRLFLVGSSLNGFGTRSSDGDLCLVVKeepcffqvNQKTEARHILTLVHKHFCTRLCKSDM 255
Cdd:cd05402     1 KREEVLDRLQELIKEWFPGAKLYPFGSYVTGLGLPGSDIDLCLLGP--------NHRVDREDFLRKLAKLLKKSGEVVEV 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217354847 256 PQVcmspdvtllkmpltlssagyierpqlIRAKVPIVKFRDKVSCVEFDLNVNNIVGIRNTFLLRTYA 323
Cdd:cd05402    73 EPI--------------------------INARVPIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
154-367 3.69e-27

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 111.79  E-value: 3.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354847 154 DKLSQQILELFetcqQQISdLKKKEL-CRTQLQREIQLL----FPQSRLFLVGSSLNGFGTRSSDGDLCLvvkeepcffq 228
Cdd:COG5260    55 DELTSELLEFY----DYIA-PSDEELkRRKALLEKLRTLlkkeFPDADLKVFGSTETGLALPKSDIDLCI---------- 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354847 229 vnqKTEARHiltlvhkhfctrlcksDMPQVCMSPDVTLLKmpltlSSAGYIERPQLIRAKVPIVKFRDKVSCVEFDLNVN 308
Cdd:COG5260   120 ---ISDPRG----------------YKETRNAGSLASHLF-----KKNLAKEVVVVSTARVPIIKLVDPQSGLHCDISFN 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217354847 309 NIVGIRNTFLLRTYAYLENRVRPLVLVIKKWASHHQINDASRGTLSSYSLVLMVLHYLQ 367
Cdd:COG5260   176 NTNGIVNAKLIRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSSYTISCMVLSFLQ 234
 
Name Accession Description Interval E-value
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
 176-323 4.46e-28

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: 106.10  E-value: 4.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354847 176 KKELCRTQLQREIQLLFPQSRLFLVGSSLNGFGTRSSDGDLCLVVKeepcffqvNQKTEARHILTLVHKHFCTRLCKSDM 255
Cdd:cd05402     1 KREEVLDRLQELIKEWFPGAKLYPFGSYVTGLGLPGSDIDLCLLGP--------NHRVDREDFLRKLAKLLKKSGEVVEV 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217354847 256 PQVcmspdvtllkmpltlssagyierpqlIRAKVPIVKFRDKVSCVEFDLNVNNIVGIRNTFLLRTYA 323
Cdd:cd05402    73 EPI--------------------------INARVPIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
154-367 3.69e-27

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 111.79  E-value: 3.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354847 154 DKLSQQILELFetcqQQISdLKKKEL-CRTQLQREIQLL----FPQSRLFLVGSSLNGFGTRSSDGDLCLvvkeepcffq 228
Cdd:COG5260    55 DELTSELLEFY----DYIA-PSDEELkRRKALLEKLRTLlkkeFPDADLKVFGSTETGLALPKSDIDLCI---------- 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354847 229 vnqKTEARHiltlvhkhfctrlcksDMPQVCMSPDVTLLKmpltlSSAGYIERPQLIRAKVPIVKFRDKVSCVEFDLNVN 308
Cdd:COG5260   120 ---ISDPRG----------------YKETRNAGSLASHLF-----KKNLAKEVVVVSTARVPIIKLVDPQSGLHCDISFN 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217354847 309 NIVGIRNTFLLRTYAYLENRVRPLVLVIKKWASHHQINDASRGTLSSYSLVLMVLHYLQ 367
Cdd:COG5260   176 NTNGIVNAKLIRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSSYTISCMVLSFLQ 234
 
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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