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Conserved domains on  [gi|1917203229|ref|NP_001375026|]
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poly(A) RNA polymerase GLD2 isoform 6 [Homo sapiens]

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];
154-489 3.88e-35

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: 137.21  E-value: 3.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203229 154 DKLSQQILELFetcqQQISdLKKKEL-CRTQLQREIQLL----FPQSRLFLVGSSLNGFGTRSSDGDLClVVKEEPVNQK 228
Cdd:COG5260    55 DELTSELLEFY----DYIA-PSDEELkRRKALLEKLRTLlkkeFPDADLKVFGSTETGLALPKSDIDLC-IISDPRGYKE 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203229 229 TEARHILtlvhkhfctrlcksdmpqvcmspdVTLLKmpltlSSAGYIERPQLIRAKVPIVKFRDKVSCVEFDLNVNNIVG 308
Cdd:COG5260   129 TRNAGSL------------------------ASHLF-----KKNLAKEVVVVSTARVPIIKLVDPQSGLHCDISFNNTNG 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203229 309 IRNTFLLRTYAYLENRVRPLVLVIKKWASHHQINDASRGTLSSYSLVLMVLHYLQTLPEPilpslqkiypesfspaiqlh 388
Cdd:COG5260   180 IVNAKLIRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSSYTISCMVLSFLQMHPPF-------------------- 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203229 389 LVHQAPCNVPPYLSKNESNLGDLLLGFLKYYATEFDWNSQMISVREAKAIPRPDGIEW----RNKYICVEEPF-DGTNTA 463
Cdd:COG5260   240 LFFDNGLLSPLKYNKNIDNLGVLFDDFFELYGKSFNYSLVVLSINSGDFYLPKYEKGWlkpsKPNSLSIQDPGtDRNNDI 319
                         330       340
                  ....*....|....*....|....*.
gi 1917203229 464 RAVHEKQKfdMIKDQFLKSWHRLKNK 489
Cdd:COG5260   320 SAVSFNIK--DIKAAFIRAFELLSNK 343
 
Name Accession Description Interval E-value
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
154-489 3.88e-35

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 137.21  E-value: 3.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203229 154 DKLSQQILELFetcqQQISdLKKKEL-CRTQLQREIQLL----FPQSRLFLVGSSLNGFGTRSSDGDLClVVKEEPVNQK 228
Cdd:COG5260    55 DELTSELLEFY----DYIA-PSDEELkRRKALLEKLRTLlkkeFPDADLKVFGSTETGLALPKSDIDLC-IISDPRGYKE 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203229 229 TEARHILtlvhkhfctrlcksdmpqvcmspdVTLLKmpltlSSAGYIERPQLIRAKVPIVKFRDKVSCVEFDLNVNNIVG 308
Cdd:COG5260   129 TRNAGSL------------------------ASHLF-----KKNLAKEVVVVSTARVPIIKLVDPQSGLHCDISFNNTNG 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203229 309 IRNTFLLRTYAYLENRVRPLVLVIKKWASHHQINDASRGTLSSYSLVLMVLHYLQTLPEPilpslqkiypesfspaiqlh 388
Cdd:COG5260   180 IVNAKLIRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSSYTISCMVLSFLQMHPPF-------------------- 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203229 389 LVHQAPCNVPPYLSKNESNLGDLLLGFLKYYATEFDWNSQMISVREAKAIPRPDGIEW----RNKYICVEEPF-DGTNTA 463
Cdd:COG5260   240 LFFDNGLLSPLKYNKNIDNLGVLFDDFFELYGKSFNYSLVVLSINSGDFYLPKYEKGWlkpsKPNSLSIQDPGtDRNNDI 319
                         330       340
                  ....*....|....*....|....*.
gi 1917203229 464 RAVHEKQKfdMIKDQFLKSWHRLKNK 489
Cdd:COG5260   320 SAVSFNIK--DIKAAFIRAFELLSNK 343
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
176-319 1.05e-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: 109.57  E-value: 1.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203229 176 KKELCRTQLQREIQLLFPQSRLFLVGSSLNGFGTRSSDGDLCLVVKEEPVNQKtearHILTLVHKHFCtrlcksdmpqvc 255
Cdd:cd05402     1 KREEVLDRLQELIKEWFPGAKLYPFGSYVTGLGLPGSDIDLCLLGPNHRVDRE----DFLRKLAKLLK------------ 64
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1917203229 256 mspdvtllkmpltlSSAGYIERPQLIRAKVPIVKFRDKVSCVEFDLNVNNIVGIRNTFLLRTYA 319
Cdd:cd05402    65 --------------KSGEVVEVEPIINARVPIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
PAP_assoc pfam03828
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ...
407-461 5.08e-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: 66.44  E-value: 5.08e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203229 407 NLGDLLLGFLKYYATEFDWNSQMISVREAKAIPRPD-----GIEWRNKYICVEEPFDGTN 461
Cdd:pfam03828   1 SLGELLIGFFEYYGREFDYENVVISIRTGGILSKKEkgwlrNEGRRPFLLCIEDPFDLDN 60
 
Name Accession Description Interval E-value
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
154-489 3.88e-35

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 137.21  E-value: 3.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203229 154 DKLSQQILELFetcqQQISdLKKKEL-CRTQLQREIQLL----FPQSRLFLVGSSLNGFGTRSSDGDLClVVKEEPVNQK 228
Cdd:COG5260    55 DELTSELLEFY----DYIA-PSDEELkRRKALLEKLRTLlkkeFPDADLKVFGSTETGLALPKSDIDLC-IISDPRGYKE 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203229 229 TEARHILtlvhkhfctrlcksdmpqvcmspdVTLLKmpltlSSAGYIERPQLIRAKVPIVKFRDKVSCVEFDLNVNNIVG 308
Cdd:COG5260   129 TRNAGSL------------------------ASHLF-----KKNLAKEVVVVSTARVPIIKLVDPQSGLHCDISFNNTNG 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203229 309 IRNTFLLRTYAYLENRVRPLVLVIKKWASHHQINDASRGTLSSYSLVLMVLHYLQTLPEPilpslqkiypesfspaiqlh 388
Cdd:COG5260   180 IVNAKLIRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSSYTISCMVLSFLQMHPPF-------------------- 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203229 389 LVHQAPCNVPPYLSKNESNLGDLLLGFLKYYATEFDWNSQMISVREAKAIPRPDGIEW----RNKYICVEEPF-DGTNTA 463
Cdd:COG5260   240 LFFDNGLLSPLKYNKNIDNLGVLFDDFFELYGKSFNYSLVVLSINSGDFYLPKYEKGWlkpsKPNSLSIQDPGtDRNNDI 319
                         330       340
                  ....*....|....*....|....*.
gi 1917203229 464 RAVHEKQKfdMIKDQFLKSWHRLKNK 489
Cdd:COG5260   320 SAVSFNIK--DIKAAFIRAFELLSNK 343
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
176-319 1.05e-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: 109.57  E-value: 1.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203229 176 KKELCRTQLQREIQLLFPQSRLFLVGSSLNGFGTRSSDGDLCLVVKEEPVNQKtearHILTLVHKHFCtrlcksdmpqvc 255
Cdd:cd05402     1 KREEVLDRLQELIKEWFPGAKLYPFGSYVTGLGLPGSDIDLCLLGPNHRVDRE----DFLRKLAKLLK------------ 64
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1917203229 256 mspdvtllkmpltlSSAGYIERPQLIRAKVPIVKFRDKVSCVEFDLNVNNIVGIRNTFLLRTYA 319
Cdd:cd05402    65 --------------KSGEVVEVEPIINARVPIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
PAP_assoc pfam03828
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ...
407-461 5.08e-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: 66.44  E-value: 5.08e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203229 407 NLGDLLLGFLKYYATEFDWNSQMISVREAKAIPRPD-----GIEWRNKYICVEEPFDGTN 461
Cdd:pfam03828   1 SLGELLIGFFEYYGREFDYENVVISIRTGGILSKKEkgwlrNEGRRPFLLCIEDPFDLDN 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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