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Conserved domains on  [gi|54215|emb|CAA28620|]
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unnamed protein product [Mus musculus]

Protein Classification

nucleotidyltransferase domain-containing protein; CCA tRNA nucleotidyltransferase( domain architecture ID 10143812)

nucleotidyltransferase domain-containing protein, similar to African swine fever virus repair DNA polymerase X| [cytidine(C)-cytidine(C)-adenosine (A)] tRNA nucleotidyltransferase adds the CCA sequence one nucleotide at a time onto the 3' end of tRNA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
 164-349 2.96e-140

2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, C-terminal half of 2'-5'-oligoadenylate synthetase 1, being described as domain 2 of the enzyme and homologous to a tandem ubiquitin repeat. It carries the region of enzymic activity between 320 and 344 at the extreme C-terminal end. Oligoadenylate synthetases are antiviral enzymes that counteract vial attack by degrading viral RNA. The enzyme uses ATP in 2'-specific nucleotidyl transfer reactions to synthesize 2'.5'-oligoadenylates, which activate latent ribonuclease, resulting in degradation of viral RNA and inhibition of virus replication. This domain is often associated with NTP_transf_2 pfam01909.


:

Pssm-ID: 463087  Cd Length: 188  Bit Score: 395.70  E-value: 2.96e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54215      164 SKPDPRIYAILIEECTSLGKDGEFSTCFTELQRNFLKQRPTKLKSLIRLVKHWYQLCKEKL-GKPLPPQYALELLTVFAW 242
Cdd:pfam10421   1 SKPSPEVYVDLIRSCTSLAKPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLkGASLPPQYALELLTVYAW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54215      243 EQGNGCYEFNTAQGFRTVLELVINYQHLRIYWTKYYDFQHQEVSKYLHRQLRKARPVILDPADPTGNVAGGNPEGWRRLA 322
Cdd:pfam10421  81 EQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDRWRWDLLA 160

                         170       180
                  ....*....|....*....|....*..
gi 54215      323 EEADVWLWYPCFIKKDGSRVSSWDVPT 349
Cdd:pfam10421 161 QEAAAWLSQPCFKNGDGSPVPSWDVPP 187
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 29-212 1.47e-20

Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class I CCA-adding enzyme; In vertebrates, 2-5OASs are induced by interferon during the innate immune response to protect against RNA virus infections. In the presence of an RNA activator, 2-5OASs catalyze the oligomerization of ATP into 2-5A. 2-5A activates endoribonuclease L, which leads to degradation of the viral RNA. 2-5OASs are also implicated in cell growth control, differentiation, and apoptosis. This family includes human OAS1, -2, -3, and OASL. 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 I group includes the archaeal Sulfolobus shibatae and Archeoglobus fulgidus CCA-adding enzymes. It 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 conserved in this family.


:

Pssm-ID: 143390 [Multi-domain]  Cd Length: 143  Bit Score: 86.68  E-value: 1.47e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54215     29 ADVKSAVNVVCDFLKERCFQGAahpVRVSKVVKGGSSGKGTTLKGRSDADLVVFLNNLTSFedQLNRRGEFIKEIKKQLy 108
Cdd:cd05400   3 EEAKERYREIREALKESLSELA---GRVAEVFLQGSYARGTALRGDSDIDLVVVLPDDTSF--AEYGPAELLDELGEAL- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54215    109 evqhERRFRVKFEVQsswwPNARSLSFKLSaphlHQEVEFDVLPAFDVLGHVntsskpdpriyailieectslgkdgEFS 188
Cdd:cd05400  77 ----KEYYGANEEVK----AQHRSVTVKFK----GQGFHVDVVPAFEADSGS-------------------------KYG 119

                       170       180
                ....*....|....*....|....
gi 54215    189 TCFTELQRNFLKQRPTKLKSLIRL 212
Cdd:cd05400 120 SVPDRDGGSWVDRNPKHHAELLRR 143
 
Name Accession Description Interval E-value
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
 164-349 2.96e-140

2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, C-terminal half of 2'-5'-oligoadenylate synthetase 1, being described as domain 2 of the enzyme and homologous to a tandem ubiquitin repeat. It carries the region of enzymic activity between 320 and 344 at the extreme C-terminal end. Oligoadenylate synthetases are antiviral enzymes that counteract vial attack by degrading viral RNA. The enzyme uses ATP in 2'-specific nucleotidyl transfer reactions to synthesize 2'.5'-oligoadenylates, which activate latent ribonuclease, resulting in degradation of viral RNA and inhibition of virus replication. This domain is often associated with NTP_transf_2 pfam01909.


Pssm-ID: 463087  Cd Length: 188  Bit Score: 395.70  E-value: 2.96e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54215      164 SKPDPRIYAILIEECTSLGKDGEFSTCFTELQRNFLKQRPTKLKSLIRLVKHWYQLCKEKL-GKPLPPQYALELLTVFAW 242
Cdd:pfam10421   1 SKPSPEVYVDLIRSCTSLAKPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLkGASLPPQYALELLTVYAW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54215      243 EQGNGCYEFNTAQGFRTVLELVINYQHLRIYWTKYYDFQHQEVSKYLHRQLRKARPVILDPADPTGNVAGGNPEGWRRLA 322
Cdd:pfam10421  81 EQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDRWRWDLLA 160

                         170       180
                  ....*....|....*....|....*..
gi 54215      323 EEADVWLWYPCFIKKDGSRVSSWDVPT 349
Cdd:pfam10421 161 QEAAAWLSQPCFKNGDGSPVPSWDVPP 187
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 29-212 1.47e-20

Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class I CCA-adding enzyme; In vertebrates, 2-5OASs are induced by interferon during the innate immune response to protect against RNA virus infections. In the presence of an RNA activator, 2-5OASs catalyze the oligomerization of ATP into 2-5A. 2-5A activates endoribonuclease L, which leads to degradation of the viral RNA. 2-5OASs are also implicated in cell growth control, differentiation, and apoptosis. This family includes human OAS1, -2, -3, and OASL. 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 I group includes the archaeal Sulfolobus shibatae and Archeoglobus fulgidus CCA-adding enzymes. It 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 conserved in this family.


Pssm-ID: 143390 [Multi-domain]  Cd Length: 143  Bit Score: 86.68  E-value: 1.47e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54215     29 ADVKSAVNVVCDFLKERCFQGAahpVRVSKVVKGGSSGKGTTLKGRSDADLVVFLNNLTSFedQLNRRGEFIKEIKKQLy 108
Cdd:cd05400   3 EEAKERYREIREALKESLSELA---GRVAEVFLQGSYARGTALRGDSDIDLVVVLPDDTSF--AEYGPAELLDELGEAL- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54215    109 evqhERRFRVKFEVQsswwPNARSLSFKLSaphlHQEVEFDVLPAFDVLGHVntsskpdpriyailieectslgkdgEFS 188
Cdd:cd05400  77 ----KEYYGANEEVK----AQHRSVTVKFK----GQGFHVDVVPAFEADSGS-------------------------KYG 119

                       170       180
                ....*....|....*....|....
gi 54215    189 TCFTELQRNFLKQRPTKLKSLIRL 212
Cdd:cd05400 120 SVPDRDGGSWVDRNPKHHAELLRR 143
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
 38-107 4.47e-05

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: 41.63  E-value: 4.47e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54215       38 VCDFLKERCFqgaahPVRVSKVVKGGSSGKGTTLKGrSDADLVVFLNNLTSfEDQLNRRGEFIKEIKKQL 107
Cdd:pfam01909   1 LRKLREILKE-----LFPVAEVVLFGSYARGTALPG-SDIDLLVVFPEPVE-EERLLKLAKIIKELEELL 63
 
Name Accession Description Interval E-value
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
 164-349 2.96e-140

2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, C-terminal half of 2'-5'-oligoadenylate synthetase 1, being described as domain 2 of the enzyme and homologous to a tandem ubiquitin repeat. It carries the region of enzymic activity between 320 and 344 at the extreme C-terminal end. Oligoadenylate synthetases are antiviral enzymes that counteract vial attack by degrading viral RNA. The enzyme uses ATP in 2'-specific nucleotidyl transfer reactions to synthesize 2'.5'-oligoadenylates, which activate latent ribonuclease, resulting in degradation of viral RNA and inhibition of virus replication. This domain is often associated with NTP_transf_2 pfam01909.


Pssm-ID: 463087  Cd Length: 188  Bit Score: 395.70  E-value: 2.96e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54215      164 SKPDPRIYAILIEECTSLGKDGEFSTCFTELQRNFLKQRPTKLKSLIRLVKHWYQLCKEKL-GKPLPPQYALELLTVFAW 242
Cdd:pfam10421   1 SKPSPEVYVDLIRSCTSLAKPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLkGASLPPQYALELLTVYAW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54215      243 EQGNGCYEFNTAQGFRTVLELVINYQHLRIYWTKYYDFQHQEVSKYLHRQLRKARPVILDPADPTGNVAGGNPEGWRRLA 322
Cdd:pfam10421  81 EQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDRWRWDLLA 160

                         170       180
                  ....*....|....*....|....*..
gi 54215      323 EEADVWLWYPCFIKKDGSRVSSWDVPT 349
Cdd:pfam10421 161 QEAAAWLSQPCFKNGDGSPVPSWDVPP 187
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 29-212 1.47e-20

Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class I CCA-adding enzyme; In vertebrates, 2-5OASs are induced by interferon during the innate immune response to protect against RNA virus infections. In the presence of an RNA activator, 2-5OASs catalyze the oligomerization of ATP into 2-5A. 2-5A activates endoribonuclease L, which leads to degradation of the viral RNA. 2-5OASs are also implicated in cell growth control, differentiation, and apoptosis. This family includes human OAS1, -2, -3, and OASL. 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 I group includes the archaeal Sulfolobus shibatae and Archeoglobus fulgidus CCA-adding enzymes. It 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 conserved in this family.


Pssm-ID: 143390 [Multi-domain]  Cd Length: 143  Bit Score: 86.68  E-value: 1.47e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54215     29 ADVKSAVNVVCDFLKERCFQGAahpVRVSKVVKGGSSGKGTTLKGRSDADLVVFLNNLTSFedQLNRRGEFIKEIKKQLy 108
Cdd:cd05400   3 EEAKERYREIREALKESLSELA---GRVAEVFLQGSYARGTALRGDSDIDLVVVLPDDTSF--AEYGPAELLDELGEAL- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54215    109 evqhERRFRVKFEVQsswwPNARSLSFKLSaphlHQEVEFDVLPAFDVLGHVntsskpdpriyailieectslgkdgEFS 188
Cdd:cd05400  77 ----KEYYGANEEVK----AQHRSVTVKFK----GQGFHVDVVPAFEADSGS-------------------------KYG 119

                       170       180
                ....*....|....*....|....
gi 54215    189 TCFTELQRNFLKQRPTKLKSLIRL 212
Cdd:cd05400 120 SVPDRDGGSWVDRNPKHHAELLRR 143
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
 38-107 4.47e-05

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: 41.63  E-value: 4.47e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54215       38 VCDFLKERCFqgaahPVRVSKVVKGGSSGKGTTLKGrSDADLVVFLNNLTSfEDQLNRRGEFIKEIKKQL 107
Cdd:pfam01909   1 LRKLREILKE-----LFPVAEVVLFGSYARGTALPG-SDIDLLVVFPEPVE-EERLLKLAKIIKELEELL 63
SMODS pfam18144
Second Messenger Oligonucleotide or Dinucleotide Synthetase domain; Nucleotide synthetase ...
 12-140 7.88e-03

Second Messenger Oligonucleotide or Dinucleotide Synthetase domain; Nucleotide synthetase enzyme of the DNA polymerase beta superfamily. Experimental studies have demonstrated cGAMP synthetase activity in the Vibrio cholerae DncV protein, a member of the SMODS family. The diversity inherent to the SMODS family suggests members of the family could generate a range of nucleotides, cyclic and/or linear. The nucleotide second messengers generated by the SMODS domains are predicted to activate effectors in a class of conflict systems reliant on the production and sensing of the nucleotide second messengers.


Pssm-ID: 436305  Cd Length: 164  Bit Score: 36.85  E-value: 7.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54215       12 TLDKFIEDYLLPDTTfGADVKSAVNVVCDFLKErCFQGAAHPVRVSKVVkgGSSGKGTTLKG--------RSDADLVVFL 83
Cdd:pfam18144   6 YFTTFLSNINLSTTT-KDSISSRYGTITKRLNT-DFWDFGSKTSESFLV--GSYARGTIIRPvsdldmlfRLDADILVVY 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 54215       84 NNLTSFEDQ--LNRRGEFIkeikKQLYEVQHERRFR---------VKFEVQ-------SSWW-PNARSLSFKLSAP 140
Cdd:pfam18144  82 DPYDGWGPSdyLQKLKRAI----EKTYSTSEIRQDRcvivvyfnhIKFDVVpafknrdGSYTiPDRNNGEWKKTNP 153
 
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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