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Conserved domains on  [gi|306869132|gb|EFN00934|]
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Phosphatase [Actinobacillus pleuropneumoniae serovar 12 str. 1096]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cca super family cl42923
multifunctional CCA addition/repair protein;
1-49 2.39e-35

multifunctional CCA addition/repair protein;


The actual alignment was detected with superfamily member PRK10885:

Pssm-ID: 182810 [Multi-domain]  Cd Length: 409  Bit Score: 121.89  E-value: 2.39e-35
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 306869132   1 MQIYLVGGAVRDQLLNLPVKDRDYLVVGATPEQLLAQGYQQVGNDFPVF 49
Cdd:PRK10885   1 MKIYLVGGAVRDALLGLPVKDRDWVVVGATPEEMLAQGYQQVGKDFPVF 49
 
Name Accession Description Interval E-value
cca PRK10885
multifunctional CCA addition/repair protein;
1-49 2.39e-35

multifunctional CCA addition/repair protein;


Pssm-ID: 182810 [Multi-domain]  Cd Length: 409  Bit Score: 121.89  E-value: 2.39e-35
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 306869132   1 MQIYLVGGAVRDQLLNLPVKDRDYLVVGATPEQLLAQGYQQVGNDFPVF 49
Cdd:PRK10885   1 MKIYLVGGAVRDALLGLPVKDRDWVVVGATPEEMLAQGYQQVGKDFPVF 49
PcnB COG0617
tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and ...
 1-49 2.09e-18

tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and biogenesis]; tRNA nucleotidyltransferase/poly(A) polymerase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440382 [Multi-domain]  Cd Length: 391  Bit Score: 76.01  E-value: 2.09e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 306869132   1 MQIYLVGGAVRDQLLNLPVKDRDYLVVgATPEQLLAQG-----YQQVGNDFPVF 49
Cdd:COG0617   18 FEAYLVGGAVRDLLLGRPPKDIDIVTV-ATPEEVAALFrkalrTVPVGRDFGTV 70
NT_ClassII-CCAase cd05398
Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the ...
 1-36 9.84e-11

Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the sequence [cytidine(C)-cytidine-adenosine (A)], one nucleotide at a time, onto the 3' end of tRNA, in a template-independent reaction. This Class II group is comprised mainly of eubacterial and eukaryotic enzymes and includes Bacillus stearothermophilus CCAase, Escherichia coli poly(A) polymerase I, human mitochondrial CCAase, and Saccharomyces cerevisiae CCAase (CCA1). CCA-adding enzymes have a single catalytic pocket, which recognizes both ATP and CTP substrates. Included in this subgroup are CC- and A-adding enzymes from various ancient species of bacteria such as Aquifex aeolicus; these enzymes collaborate to add CCA to tRNAs. 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. These carboxylate residues are fairly well conserved in this family. Escherichia coli CCAase is related to this group but has not been included in this alignment as this enzyme lacks the N-terminal helix conserved in the remainder of the NT superfamily.


Pssm-ID: 143388 [Multi-domain]  Cd Length: 139  Bit Score: 52.60  E-value: 9.84e-11
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 306869132   1 MQIYLVGGAVRDQLLNLPVKDRDYLVVGATPEQLLA 36
Cdd:cd05398   17 YEAYLVGGAVRDLLLGRPPKDIDIATDADGPEFAEA 52
PolyA_pol pfam01743
Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, ...
 3-34 4.98e-08

Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, such as Poly(A) polymerase, which adds the poly (A) tail to mRNA EC:2.7.7.19. This family also includes the tRNA nucleotidyltransferase that adds the CCA to the 3' of the tRNA EC:2.7.7.25. This family is part of the nucleotidyltransferase superfamily.


Pssm-ID: 396348 [Multi-domain]  Cd Length: 126  Bit Score: 45.35  E-value: 4.98e-08
                          10        20        30
                  ....*....|....*....|....*....|..
gi 306869132    3 IYLVGGAVRDQLLNLPVKDRDyLVVGATPEQL 34
Cdd:pfam01743   1 LYIVGGAVRDLLLGKTPKDVD-IATDATPEQV 31
pcnB TIGR01942
poly(A) polymerase; This model describes the pcnB family of poly(A) polymerases (also known as ...
 2-34 2.48e-06

poly(A) polymerase; This model describes the pcnB family of poly(A) polymerases (also known as plasmid copy number protein). These enzymes sequentially add adenosine nucleotides to the 3' end of RNAs, targeting them for degradation by the cell. This was originally described for anti-sense RNAs, but was later demonstrated for mRNAs as well. Members of this family are as yet limited to the gamma- and beta-proteobacteria, with putative members in the Chlamydiacae and spirochetes. This family has homology to tRNA nucleotidyltransferase (cca).


Pssm-ID: 130997 [Multi-domain]  Cd Length: 410  Bit Score: 42.09  E-value: 2.48e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 306869132    2 QIYLVGGAVRDQLLNLPVKDRDyLVVGATPEQL 34
Cdd:TIGR01942  31 QAYIVGGAVRDLLLGIEPKDFD-VVTSATPEEV 62
 
Name Accession Description Interval E-value
cca PRK10885
multifunctional CCA addition/repair protein;
1-49 2.39e-35

multifunctional CCA addition/repair protein;


Pssm-ID: 182810 [Multi-domain]  Cd Length: 409  Bit Score: 121.89  E-value: 2.39e-35
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 306869132   1 MQIYLVGGAVRDQLLNLPVKDRDYLVVGATPEQLLAQGYQQVGNDFPVF 49
Cdd:PRK10885   1 MKIYLVGGAVRDALLGLPVKDRDWVVVGATPEEMLAQGYQQVGKDFPVF 49
PRK13298 PRK13298
tRNA CCA-pyrophosphorylase; Provisional
 1-49 7.26e-26

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 237338 [Multi-domain]  Cd Length: 417  Bit Score: 96.72  E-value: 7.26e-26
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 306869132   1 MQIYLVGGAVRDQLLNLPVKDRDYLVVGATPEQLLAQGYQQVGNDFPVF 49
Cdd:PRK13298   1 MKIYLVGGAVRDSLLNLPVKDKDWVVVGGTPKILLSINFQQVGKDFPVF 49
PRK13297 PRK13297
tRNA CCA-pyrophosphorylase; Provisional
 1-49 1.17e-18

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 139469 [Multi-domain]  Cd Length: 364  Bit Score: 76.57  E-value: 1.17e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 306869132   1 MQIYLVGGAVRDQLLNLPVKDRDYLVVGATPEQLLAQGYQQVGNDFPVF 49
Cdd:PRK13297  12 LQVYIVGGAVRDALLGLPAGDRDWVVVGATPEDMARRGFIPVGGDFPVF 60
PcnB COG0617
tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and ...
 1-49 2.09e-18

tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and biogenesis]; tRNA nucleotidyltransferase/poly(A) polymerase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440382 [Multi-domain]  Cd Length: 391  Bit Score: 76.01  E-value: 2.09e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 306869132   1 MQIYLVGGAVRDQLLNLPVKDRDYLVVgATPEQLLAQG-----YQQVGNDFPVF 49
Cdd:COG0617   18 FEAYLVGGAVRDLLLGRPPKDIDIVTV-ATPEEVAALFrkalrTVPVGRDFGTV 70
PRK13296 PRK13296
CCA tRNA nucleotidyltransferase;
1-49 6.27e-16

CCA tRNA nucleotidyltransferase;


Pssm-ID: 106256 [Multi-domain]  Cd Length: 360  Bit Score: 69.24  E-value: 6.27e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 306869132   1 MQIYLVGGAVRDQLLNLPVKDRDYLVVGATPEQLLAQGYQQVGNDFPVF 49
Cdd:PRK13296   1 MKFYLVGGAVRDMLLGITPKDKDWVVVGATEDEMLANGFIKIAANFPVF 49
NT_ClassII-CCAase cd05398
Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the ...
 1-36 9.84e-11

Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the sequence [cytidine(C)-cytidine-adenosine (A)], one nucleotide at a time, onto the 3' end of tRNA, in a template-independent reaction. This Class II group is comprised mainly of eubacterial and eukaryotic enzymes and includes Bacillus stearothermophilus CCAase, Escherichia coli poly(A) polymerase I, human mitochondrial CCAase, and Saccharomyces cerevisiae CCAase (CCA1). CCA-adding enzymes have a single catalytic pocket, which recognizes both ATP and CTP substrates. Included in this subgroup are CC- and A-adding enzymes from various ancient species of bacteria such as Aquifex aeolicus; these enzymes collaborate to add CCA to tRNAs. 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. These carboxylate residues are fairly well conserved in this family. Escherichia coli CCAase is related to this group but has not been included in this alignment as this enzyme lacks the N-terminal helix conserved in the remainder of the NT superfamily.


Pssm-ID: 143388 [Multi-domain]  Cd Length: 139  Bit Score: 52.60  E-value: 9.84e-11
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 306869132   1 MQIYLVGGAVRDQLLNLPVKDRDYLVVGATPEQLLA 36
Cdd:cd05398   17 YEAYLVGGAVRDLLLGRPPKDIDIATDADGPEFAEA 52
PolyA_pol pfam01743
Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, ...
 3-34 4.98e-08

Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, such as Poly(A) polymerase, which adds the poly (A) tail to mRNA EC:2.7.7.19. This family also includes the tRNA nucleotidyltransferase that adds the CCA to the 3' of the tRNA EC:2.7.7.25. This family is part of the nucleotidyltransferase superfamily.


Pssm-ID: 396348 [Multi-domain]  Cd Length: 126  Bit Score: 45.35  E-value: 4.98e-08
                          10        20        30
                  ....*....|....*....|....*....|..
gi 306869132    3 IYLVGGAVRDQLLNLPVKDRDyLVVGATPEQL 34
Cdd:pfam01743   1 LYIVGGAVRDLLLGKTPKDVD-IATDATPEQV 31
pcnB TIGR01942
poly(A) polymerase; This model describes the pcnB family of poly(A) polymerases (also known as ...
 2-34 2.48e-06

poly(A) polymerase; This model describes the pcnB family of poly(A) polymerases (also known as plasmid copy number protein). These enzymes sequentially add adenosine nucleotides to the 3' end of RNAs, targeting them for degradation by the cell. This was originally described for anti-sense RNAs, but was later demonstrated for mRNAs as well. Members of this family are as yet limited to the gamma- and beta-proteobacteria, with putative members in the Chlamydiacae and spirochetes. This family has homology to tRNA nucleotidyltransferase (cca).


Pssm-ID: 130997 [Multi-domain]  Cd Length: 410  Bit Score: 42.09  E-value: 2.48e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 306869132    2 QIYLVGGAVRDQLLNLPVKDRDyLVVGATPEQL 34
Cdd:TIGR01942  31 QAYIVGGAVRDLLLGIEPKDFD-VVTSATPEEV 62
PRK13299 PRK13299
tRNA CCA-pyrophosphorylase; Provisional
 4-33 1.13e-05

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 237339 [Multi-domain]  Cd Length: 394  Bit Score: 40.21  E-value: 1.13e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 306869132   4 YLVGGAVRDQLLNLPVKDRDyLVVGATPEQ 33
Cdd:PRK13299  24 YFVGGSVRDYLLGRPIHDVD-IATSAYPEE 52
pcnB PRK11623
poly(A) polymerase I; Provisional
 2-34 4.01e-04

poly(A) polymerase I; Provisional


Pssm-ID: 236939 [Multi-domain]  Cd Length: 472  Bit Score: 35.88  E-value: 4.01e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 306869132   2 QIYLVGGAVRDQLLNLPVKDRDyLVVGATPEQL 34
Cdd:PRK11623  68 EAYLVGGGVRDLLLGKKPKDFD-VTTNATPEQV 99
 
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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