NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|74229019|ref|NP_058197|]
View 

2'-5'-oligoadenylate synthase 2 isoform 1 [Homo sapiens]

Protein Classification

nucleotidyltransferase( domain architecture ID 10143820)

nucleotidyltransferase (NT), similar to the small 65-kd isoform of human 2'-5'-oligoadenylate synthase-like protein, belongs to the Pol beta-like NT superfamily

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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, ...
 496-685 2.14e-134

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: 393.77  E-value: 2.14e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229019   496 STPSPEVYAGLIDLYKSSDLPGgEFSTCFTVLQRNFIRSRPTKLKDLIRLVKHWYKECERKLKpKGSLPPKYALELLTIY 575
Cdd:pfam10421   1 SKPSPEVYVDLIRSCTSLAKPG-EFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLK-GASLPPQYALELLTVY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229019   576 AWEQGSGVPDFDTAEGFRTVLELVTQYQQLCIFWKVNYNFEDETVRKFLLSQLQKTRPVILDPAEPTGDVGGGDRWCWHL 655
Cdd:pfam10421  79 AWEQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDRWRWDL 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 74229019   656 LAKEAKEWLSSPCFKDGTGNPIPPWKVPTM 685
Cdd:pfam10421 159 LAQEAAAWLSQPCFKNGDGSPVPSWDVPPA 188
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
 154-338 2.30e-113

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: 339.85  E-value: 2.30e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229019   154 NPSPWIYRELKRSLDKTnASPGEFAVCFTELQQKFFDNRPGKLKDLILLIKHWHQQCQKKIKDLPSLSPYALELLTVYAW 233
Cdd:pfam10421   2 KPSPEVYVDLIRSCTSL-AKPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLKGASLPPQYALELLTVYAW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229019   234 EQGCRKDNFDIAEGVRTVLELIKCQEKLCIYWMVNYNFEDETIRNILLHQLQSARPVILDPVDPTNNVSGDKI-CWQWLK 312
Cdd:pfam10421  81 EQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDRwRWDLLA 160

                         170       180
                  ....*....|....*....|....*...
gi 74229019   313 KEAQTWLTSP--NLDNELPAPSWNVLPA 338
Cdd:pfam10421 161 QEAAAWLSQPcfKNGDGSPVPSWDVPPA 188
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 362-545 5.29e-18

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: 81.29  E-value: 5.29e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229019 362 FLEQIDSAVNIIRTFLKENCFRQSTAKIQIVRGGSTAKGTALKTGSDADLVVFHNSLKSYtsQKNERHKIVKEIHEQLKA 441
Cdd:cd05400   1 PLEEAKERYREIREALKESLSELAGRVAEVFLQGSYARGTALRGDSDIDLVVVLPDDTSF--AEYGPAELLDELGEALKE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229019 442 FWREKEEElevsfeppkwKAPRvLSFSLKSKvlNESVSFDVLPAFNALGQLSSGStpspevyaglidlykssdlpggefs 521
Cdd:cd05400  79 YYGANEEV----------KAQH-RSVTVKFK--GQGFHVDVVPAFEADSGSKYGS------------------------- 120

                       170       180
                ....*....|....*....|....
gi 74229019 522 tCFTVLQRNFIRSRPTKLKDLIRL 545
Cdd:cd05400 121 -VPDRDGGSWVDRNPKHHAELLRR 143
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 31-165 4.07e-16

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: 75.90  E-value: 4.07e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229019  31 QTLIDEMVNTICDVLQEPEQFP--LVQGVAIGGSYGRKTVLRGNSDGTLVLFFSDLKQFQDqkRSQRDILDKTGDKLKfc 108
Cdd:cd05400   2 LEEAKERYREIREALKESLSELagRVAEVFLQGSYARGTALRGDSDIDLVVVLPDDTSFAE--YGPAELLDELGEALK-- 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229019 109 lftKWLKNNFEIQKSLDGFTIQVftKNQRISFEVLAAFNALSLNDNPS-------------PWIYRELKR 165
Cdd:cd05400  78 ---EYYGANEEVKAQHRSVTVKF--KGQGFHVDVVPAFEADSGSKYGSvpdrdggswvdrnPKHHAELLR 142
 
Name Accession Description Interval E-value
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
 496-685 2.14e-134

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: 393.77  E-value: 2.14e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229019   496 STPSPEVYAGLIDLYKSSDLPGgEFSTCFTVLQRNFIRSRPTKLKDLIRLVKHWYKECERKLKpKGSLPPKYALELLTIY 575
Cdd:pfam10421   1 SKPSPEVYVDLIRSCTSLAKPG-EFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLK-GASLPPQYALELLTVY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229019   576 AWEQGSGVPDFDTAEGFRTVLELVTQYQQLCIFWKVNYNFEDETVRKFLLSQLQKTRPVILDPAEPTGDVGGGDRWCWHL 655
Cdd:pfam10421  79 AWEQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDRWRWDL 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 74229019   656 LAKEAKEWLSSPCFKDGTGNPIPPWKVPTM 685
Cdd:pfam10421 159 LAQEAAAWLSQPCFKNGDGSPVPSWDVPPA 188
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
 154-338 2.30e-113

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: 339.85  E-value: 2.30e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229019   154 NPSPWIYRELKRSLDKTnASPGEFAVCFTELQQKFFDNRPGKLKDLILLIKHWHQQCQKKIKDLPSLSPYALELLTVYAW 233
Cdd:pfam10421   2 KPSPEVYVDLIRSCTSL-AKPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLKGASLPPQYALELLTVYAW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229019   234 EQGCRKDNFDIAEGVRTVLELIKCQEKLCIYWMVNYNFEDETIRNILLHQLQSARPVILDPVDPTNNVSGDKI-CWQWLK 312
Cdd:pfam10421  81 EQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDRwRWDLLA 160

                         170       180
                  ....*....|....*....|....*...
gi 74229019   313 KEAQTWLTSP--NLDNELPAPSWNVLPA 338
Cdd:pfam10421 161 QEAAAWLSQPcfKNGDGSPVPSWDVPPA 188
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 362-545 5.29e-18

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: 81.29  E-value: 5.29e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229019 362 FLEQIDSAVNIIRTFLKENCFRQSTAKIQIVRGGSTAKGTALKTGSDADLVVFHNSLKSYtsQKNERHKIVKEIHEQLKA 441
Cdd:cd05400   1 PLEEAKERYREIREALKESLSELAGRVAEVFLQGSYARGTALRGDSDIDLVVVLPDDTSF--AEYGPAELLDELGEALKE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229019 442 FWREKEEElevsfeppkwKAPRvLSFSLKSKvlNESVSFDVLPAFNALGQLSSGStpspevyaglidlykssdlpggefs 521
Cdd:cd05400  79 YYGANEEV----------KAQH-RSVTVKFK--GQGFHVDVVPAFEADSGSKYGS------------------------- 120

                       170       180
                ....*....|....*....|....
gi 74229019 522 tCFTVLQRNFIRSRPTKLKDLIRL 545
Cdd:cd05400 121 -VPDRDGGSWVDRNPKHHAELLRR 143
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 31-165 4.07e-16

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: 75.90  E-value: 4.07e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229019  31 QTLIDEMVNTICDVLQEPEQFP--LVQGVAIGGSYGRKTVLRGNSDGTLVLFFSDLKQFQDqkRSQRDILDKTGDKLKfc 108
Cdd:cd05400   2 LEEAKERYREIREALKESLSELagRVAEVFLQGSYARGTALRGDSDIDLVVVLPDDTSFAE--YGPAELLDELGEALK-- 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229019 109 lftKWLKNNFEIQKSLDGFTIQVftKNQRISFEVLAAFNALSLNDNPS-------------PWIYRELKR 165
Cdd:cd05400  78 ---EYYGANEEVKAQHRSVTVKF--KGQGFHVDVVPAFEADSGSKYGSvpdrdggswvdrnPKHHAELLR 142
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
 373-439 3.45e-06

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: 45.87  E-value: 3.45e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74229019   373 IRTFLKENCFRQSTAKIQIVrgGSTAKGTALKtGSDADLVVFHNSlKSYTSQKNERHKIVKEIHEQL 439
Cdd:pfam01909   1 LRKLREILKELFPVAEVVLF--GSYARGTALP-GSDIDLLVVFPE-PVEEERLLKLAKIIKELEELL 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, ...
 496-685 2.14e-134

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: 393.77  E-value: 2.14e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229019   496 STPSPEVYAGLIDLYKSSDLPGgEFSTCFTVLQRNFIRSRPTKLKDLIRLVKHWYKECERKLKpKGSLPPKYALELLTIY 575
Cdd:pfam10421   1 SKPSPEVYVDLIRSCTSLAKPG-EFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLK-GASLPPQYALELLTVY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229019   576 AWEQGSGVPDFDTAEGFRTVLELVTQYQQLCIFWKVNYNFEDETVRKFLLSQLQKTRPVILDPAEPTGDVGGGDRWCWHL 655
Cdd:pfam10421  79 AWEQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDRWRWDL 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 74229019   656 LAKEAKEWLSSPCFKDGTGNPIPPWKVPTM 685
Cdd:pfam10421 159 LAQEAAAWLSQPCFKNGDGSPVPSWDVPPA 188
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
 154-338 2.30e-113

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: 339.85  E-value: 2.30e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229019   154 NPSPWIYRELKRSLDKTnASPGEFAVCFTELQQKFFDNRPGKLKDLILLIKHWHQQCQKKIKDLPSLSPYALELLTVYAW 233
Cdd:pfam10421   2 KPSPEVYVDLIRSCTSL-AKPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLKGASLPPQYALELLTVYAW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229019   234 EQGCRKDNFDIAEGVRTVLELIKCQEKLCIYWMVNYNFEDETIRNILLHQLQSARPVILDPVDPTNNVSGDKI-CWQWLK 312
Cdd:pfam10421  81 EQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDRwRWDLLA 160

                         170       180
                  ....*....|....*....|....*...
gi 74229019   313 KEAQTWLTSP--NLDNELPAPSWNVLPA 338
Cdd:pfam10421 161 QEAAAWLSQPcfKNGDGSPVPSWDVPPA 188
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 362-545 5.29e-18

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: 81.29  E-value: 5.29e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229019 362 FLEQIDSAVNIIRTFLKENCFRQSTAKIQIVRGGSTAKGTALKTGSDADLVVFHNSLKSYtsQKNERHKIVKEIHEQLKA 441
Cdd:cd05400   1 PLEEAKERYREIREALKESLSELAGRVAEVFLQGSYARGTALRGDSDIDLVVVLPDDTSF--AEYGPAELLDELGEALKE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229019 442 FWREKEEElevsfeppkwKAPRvLSFSLKSKvlNESVSFDVLPAFNALGQLSSGStpspevyaglidlykssdlpggefs 521
Cdd:cd05400  79 YYGANEEV----------KAQH-RSVTVKFK--GQGFHVDVVPAFEADSGSKYGS------------------------- 120

                       170       180
                ....*....|....*....|....
gi 74229019 522 tCFTVLQRNFIRSRPTKLKDLIRL 545
Cdd:cd05400 121 -VPDRDGGSWVDRNPKHHAELLRR 143
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 31-165 4.07e-16

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: 75.90  E-value: 4.07e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229019  31 QTLIDEMVNTICDVLQEPEQFP--LVQGVAIGGSYGRKTVLRGNSDGTLVLFFSDLKQFQDqkRSQRDILDKTGDKLKfc 108
Cdd:cd05400   2 LEEAKERYREIREALKESLSELagRVAEVFLQGSYARGTALRGDSDIDLVVVLPDDTSFAE--YGPAELLDELGEALK-- 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229019 109 lftKWLKNNFEIQKSLDGFTIQVftKNQRISFEVLAAFNALSLNDNPS-------------PWIYRELKR 165
Cdd:cd05400  78 ---EYYGANEEVKAQHRSVTVKF--KGQGFHVDVVPAFEADSGSKYGSvpdrdggswvdrnPKHHAELLR 142
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
 373-439 3.45e-06

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: 45.87  E-value: 3.45e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74229019   373 IRTFLKENCFRQSTAKIQIVrgGSTAKGTALKtGSDADLVVFHNSlKSYTSQKNERHKIVKEIHEQL 439
Cdd:pfam01909   1 LRKLREILKELFPVAEVVLF--GSYARGTALP-GSDIDLLVVFPE-PVEEERLLKLAKIIKELEELL 63
SMODS pfam18144
Second Messenger Oligonucleotide or Dinucleotide Synthetase domain; Nucleotide synthetase ...
 348-486 5.69e-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: 38.40  E-value: 5.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229019   348 LDKFIKEfLQPNKCFLEQIDSAVNIIRTFLKeNCFRQSTAKI-QIVRGGSTAKGTALK--------TGSDADLVVFHNSL 418
Cdd:pfam18144   7 FTTFLSN-INLSTTTKDSISSRYGTITKRLN-TDFWDFGSKTsESFLVGSYARGTIIRpvsdldmlFRLDADILVVYDPY 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74229019   419 KSYTSQknerhKIVKEIHEQLKAFWREKEEelevsfeppKWKAPR-VLSFSlkskvlneSVSFDVLPAF 486
Cdd:pfam18144  85 DGWGPS-----DYLQKLKRAIEKTYSTSEI---------RQDRCViVVYFN--------HIKFDVVPAF 131
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH