Poly(A) polymerase central domain; The central domain of Poly(A) polymerase shares structural ...
18-360
0e+00
Poly(A) polymerase central domain; The central domain of Poly(A) polymerase shares structural similarity with the allosteric activity domain of ribonucleotide reductase R1, which comprises a four-helix bundle and a three-stranded mixed beta- sheet. Even though the two enzymes bind ATP, the ATP-recognition motifs are different.
:
Pssm-ID: 461486 [Multi-domain] Cd Length: 344 Bit Score: 650.35 E-value: 0e+00
Poly(A) polymerase predicted RNA binding domain; Based on its similarity structurally to the ...
364-492
2.35e-31
Poly(A) polymerase predicted RNA binding domain; Based on its similarity structurally to the RNA recognition motif this domain is thought to be RNA binding.
:
Pssm-ID: 461484 Cd Length: 177 Bit Score: 120.47 E-value: 2.35e-31
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
527-722
1.35e-04
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
The actual alignment was detected with superfamily member pfam05109:
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 45.29 E-value: 1.35e-04
Poly(A) polymerase central domain; The central domain of Poly(A) polymerase shares structural ...
18-360
0e+00
Poly(A) polymerase central domain; The central domain of Poly(A) polymerase shares structural similarity with the allosteric activity domain of ribonucleotide reductase R1, which comprises a four-helix bundle and a three-stranded mixed beta- sheet. Even though the two enzymes bind ATP, the ATP-recognition motifs are different.
Pssm-ID: 461486 [Multi-domain] Cd Length: 344 Bit Score: 650.35 E-value: 0e+00
Poly(A) polymerase predicted RNA binding domain; Based on its similarity structurally to the ...
364-492
2.35e-31
Poly(A) polymerase predicted RNA binding domain; Based on its similarity structurally to the RNA recognition motif this domain is thought to be RNA binding.
Pssm-ID: 461484 Cd Length: 177 Bit Score: 120.47 E-value: 2.35e-31
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
57-211
2.14e-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: 109.95 E-value: 2.14e-28
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
527-722
1.35e-04
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 45.29 E-value: 1.35e-04
Poly(A) polymerase central domain; The central domain of Poly(A) polymerase shares structural ...
18-360
0e+00
Poly(A) polymerase central domain; The central domain of Poly(A) polymerase shares structural similarity with the allosteric activity domain of ribonucleotide reductase R1, which comprises a four-helix bundle and a three-stranded mixed beta- sheet. Even though the two enzymes bind ATP, the ATP-recognition motifs are different.
Pssm-ID: 461486 [Multi-domain] Cd Length: 344 Bit Score: 650.35 E-value: 0e+00
Poly(A) polymerase predicted RNA binding domain; Based on its similarity structurally to the ...
364-492
2.35e-31
Poly(A) polymerase predicted RNA binding domain; Based on its similarity structurally to the RNA recognition motif this domain is thought to be RNA binding.
Pssm-ID: 461484 Cd Length: 177 Bit Score: 120.47 E-value: 2.35e-31
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
57-211
2.14e-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: 109.95 E-value: 2.14e-28
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
80-172
4.45e-14
Nucleotidyltransferase domain; Members of this family belong to a large family of nucleotidyltransferases. This family includes kanamycin nucleotidyltransferase (KNTase) which is a plasmid-coded enzyme responsible for some types of bacterial resistance to aminoglycosides. KNTase in-activates antibiotics by catalysing the addition of a nucleotidyl group onto the drug.
Pssm-ID: 396474 Cd Length: 91 Bit Score: 68.21 E-value: 4.45e-14
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
527-722
1.35e-04
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 45.29 E-value: 1.35e-04
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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