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Conserved domains on  [gi|1720413582|ref|XP_030110371|]
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2'-5'-oligoadenylate synthase 3 isoform X1 [Mus musculus]

Protein Classification

NT_2-5OAS_ClassI-CCAase and OAS1_C domain-containing protein( domain architecture ID 10143821)

NT_2-5OAS_ClassI-CCAase and OAS1_C domain-containing protein

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, ...
 954-1136 9.36e-119

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: 364.11  E-value: 9.36e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582  954 SRPDPRVYTDLIHSCSN---AGEFSTCFTELQRDFITSRPTKLKSLIRLVKYWYQQCNKTIKgKGSLPPQHGLELLTVYA 1030
Cdd:pfam10421    1 SKPSPEVYVDLIRSCTSlakPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLK-GASLPPQYALELLTVYA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582 1031 WEQGGQNPQFNMAEGFRTVLELIVQYRQLCVYWTINYSAEDKTIGDFLKMQLRKPRPVILDPADPTGNLGHNA--RWDLL 1108
Cdd:pfam10421   80 WEQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDrwRWDLL 159

                          170       180
                   ....*....|....*....|....*...
gi 1720413582 1109 AKEATVYASALCCVDRDGNPIKPWPVKV 1136
Cdd:pfam10421  160 AQEAAAWLSQPCFKNGDGSPVPSWDVPP 187
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
 160-341 1.11e-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: 350.63  E-value: 1.11e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582  160 KPTPNVYSSLLSSHCQ---AGEYSACFTEPRKNFVNTRPAKLKNLILLVKHWYHQVQTRAVRATLPPSYALELLTIFAWE 236
Cdd:pfam10421    2 KPSPEVYVDLIRSCTSlakPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLKGASLPPQYALELLTVYAWE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582  237 QGCGKDSFSLAQGLRTVLALIQHSKYLCIFWTENYGFEDPAVGEFLRRQLKRPRPVILDPADPTWDVGNGTAWRWDVLAQ 316
Cdd:pfam10421   82 QGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDRWRWDLLAQ 161

                          170       180
                   ....*....|....*....|....*
gi 1720413582  317 EAESSFSQQCFKQASGVLVQPWEGP 341
Cdd:pfam10421  162 EAAAWLSQPCFKNGDGSPVPSWDVP 186
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
 610-796 1.70e-110

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: 342.16  E-value: 1.70e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582  610 TKPQPQVYSSLLSSGCQ---AGEHAACFAELRRNFINTCPPKLKSLMLLVKHWYRQVVTRYKGGeaagdAPPPAYALELL 686
Cdd:pfam10421    1 SKPSPEVYVDLIRSCTSlakPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLKGA-----SLPPQYALELL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582  687 TIFAWEQGCGEQKFSLAEGLRTILRLIQQHQSLCIYWTVNYSVQDPAIRAHLLCQLRKARPLVLDPADPTWNVGQGD--- 763
Cdd:pfam10421   76 TVYAWEQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDrwr 155

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1720413582  764 WKLLAQEAAALGSQVCLQSGDGTLVPPWDVTPA 796
Cdd:pfam10421  156 WDLLAQEAAAWLSQPCFKNGDGSPVPSWDVPPA 188
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 820-999 9.11e-25

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: 101.32  E-value: 9.11e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582  820 FLTQVKRAVDTICSFLKENCFrNSTIKVLKVVKGGSSAKGTALQGRSDADLVVFLSCFrqFSEQGSHRAEIISEIQAHLE 899
Cdd:cd05400      1 PLEEAKERYREIREALKESLS-ELAGRVAEVFLQGSYARGTALRGDSDIDLVVVLPDD--TSFAEYGPAELLDELGEALK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582  900 ACQQmhsfdvKFEVSKRKNPrvlSFTLTSQtllDQSVDFDVLPAFDALGQLrsgsrpdprvytdlihscsnagEFSTCFT 979
Cdd:cd05400     78 EYYG------ANEEVKAQHR---SVTVKFK---GQGFHVDVVPAFEADSGS----------------------KYGSVPD 123

                          170       180
                   ....*....|....*....|
gi 1720413582  980 ELQRDFITSRPTKLKSLIRL 999
Cdd:cd05400    124 RDGGSWVDRNPKHHAELLRR 143
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 482-612 3.09e-15

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: 73.97  E-value: 3.09e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582  482 FQQQVKQAIDAILCCLRE---KSVYKVLRVSKGGSFGRGTDLRGSCDVELVIFYKtlGDFKGQKPHQAEILRDMQAQLRH 558
Cdd:cd05400      1 PLEEAKERYREIREALKEslsELAGRVAEVFLQGSYARGTALRGDSDIDLVVVLP--DDTSFAEYGPAELLDELGEALKE 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720413582  559 WcqnpvPGLSLQFIEQKPnALQLQLASTdlsnRVDLSVLPAFDAVGPLKSGTKP 612
Cdd:cd05400     79 Y-----YGANEEVKAQHR-SVTVKFKGQ----GFHVDVVPAFEADSGSKYGSVP 122
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 51-202 1.52e-10

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: 60.49  E-value: 1.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582   51 PRVIRIAKGGAYARGTALRGGTDVELVIFLDCFQSFGDQKtcHSETLGAMRMLLESWGGHPgpglTFEFSQSKAsrilqF 130
Cdd:cd05400     25 GRVAEVFLQGSYARGTALRGDSDIDLVVVLPDDTSFAEYG--PAELLDELGEALKEYYGAN----EEVKAQHRS-----V 93

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720413582  131 RLASADGEHWIDVslVPAFDVLGQPrsgvkptpnvyssllsshcqagEYSACFTEPRKNFVNTRPAKLKNLI 202
Cdd:cd05400     94 TVKFKGQGFHVDV--VPAFEADSGS----------------------KYGSVPDRDGGSWVDRNPKHHAELL 141
 
Name Accession Description Interval E-value
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
 954-1136 9.36e-119

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: 364.11  E-value: 9.36e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582  954 SRPDPRVYTDLIHSCSN---AGEFSTCFTELQRDFITSRPTKLKSLIRLVKYWYQQCNKTIKgKGSLPPQHGLELLTVYA 1030
Cdd:pfam10421    1 SKPSPEVYVDLIRSCTSlakPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLK-GASLPPQYALELLTVYA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582 1031 WEQGGQNPQFNMAEGFRTVLELIVQYRQLCVYWTINYSAEDKTIGDFLKMQLRKPRPVILDPADPTGNLGHNA--RWDLL 1108
Cdd:pfam10421   80 WEQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDrwRWDLL 159

                          170       180
                   ....*....|....*....|....*...
gi 1720413582 1109 AKEATVYASALCCVDRDGNPIKPWPVKV 1136
Cdd:pfam10421  160 AQEAAAWLSQPCFKNGDGSPVPSWDVPP 187
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
 160-341 1.11e-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: 350.63  E-value: 1.11e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582  160 KPTPNVYSSLLSSHCQ---AGEYSACFTEPRKNFVNTRPAKLKNLILLVKHWYHQVQTRAVRATLPPSYALELLTIFAWE 236
Cdd:pfam10421    2 KPSPEVYVDLIRSCTSlakPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLKGASLPPQYALELLTVYAWE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582  237 QGCGKDSFSLAQGLRTVLALIQHSKYLCIFWTENYGFEDPAVGEFLRRQLKRPRPVILDPADPTWDVGNGTAWRWDVLAQ 316
Cdd:pfam10421   82 QGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDRWRWDLLAQ 161

                          170       180
                   ....*....|....*....|....*
gi 1720413582  317 EAESSFSQQCFKQASGVLVQPWEGP 341
Cdd:pfam10421  162 EAAAWLSQPCFKNGDGSPVPSWDVP 186
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
 610-796 1.70e-110

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: 342.16  E-value: 1.70e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582  610 TKPQPQVYSSLLSSGCQ---AGEHAACFAELRRNFINTCPPKLKSLMLLVKHWYRQVVTRYKGGeaagdAPPPAYALELL 686
Cdd:pfam10421    1 SKPSPEVYVDLIRSCTSlakPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLKGA-----SLPPQYALELL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582  687 TIFAWEQGCGEQKFSLAEGLRTILRLIQQHQSLCIYWTVNYSVQDPAIRAHLLCQLRKARPLVLDPADPTWNVGQGD--- 763
Cdd:pfam10421   76 TVYAWEQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDrwr 155

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1720413582  764 WKLLAQEAAALGSQVCLQSGDGTLVPPWDVTPA 796
Cdd:pfam10421  156 WDLLAQEAAAWLSQPCFKNGDGSPVPSWDVPPA 188
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 820-999 9.11e-25

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: 101.32  E-value: 9.11e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582  820 FLTQVKRAVDTICSFLKENCFrNSTIKVLKVVKGGSSAKGTALQGRSDADLVVFLSCFrqFSEQGSHRAEIISEIQAHLE 899
Cdd:cd05400      1 PLEEAKERYREIREALKESLS-ELAGRVAEVFLQGSYARGTALRGDSDIDLVVVLPDD--TSFAEYGPAELLDELGEALK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582  900 ACQQmhsfdvKFEVSKRKNPrvlSFTLTSQtllDQSVDFDVLPAFDALGQLrsgsrpdprvytdlihscsnagEFSTCFT 979
Cdd:cd05400     78 EYYG------ANEEVKAQHR---SVTVKFK---GQGFHVDVVPAFEADSGS----------------------KYGSVPD 123

                          170       180
                   ....*....|....*....|
gi 1720413582  980 ELQRDFITSRPTKLKSLIRL 999
Cdd:cd05400    124 RDGGSWVDRNPKHHAELLRR 143
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 482-612 3.09e-15

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: 73.97  E-value: 3.09e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582  482 FQQQVKQAIDAILCCLRE---KSVYKVLRVSKGGSFGRGTDLRGSCDVELVIFYKtlGDFKGQKPHQAEILRDMQAQLRH 558
Cdd:cd05400      1 PLEEAKERYREIREALKEslsELAGRVAEVFLQGSYARGTALRGDSDIDLVVVLP--DDTSFAEYGPAELLDELGEALKE 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720413582  559 WcqnpvPGLSLQFIEQKPnALQLQLASTdlsnRVDLSVLPAFDAVGPLKSGTKP 612
Cdd:cd05400     79 Y-----YGANEEVKAQHR-SVTVKFKGQ----GFHVDVVPAFEADSGSKYGSVP 122
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 51-202 1.52e-10

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: 60.49  E-value: 1.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582   51 PRVIRIAKGGAYARGTALRGGTDVELVIFLDCFQSFGDQKtcHSETLGAMRMLLESWGGHPgpglTFEFSQSKAsrilqF 130
Cdd:cd05400     25 GRVAEVFLQGSYARGTALRGDSDIDLVVVLPDDTSFAEYG--PAELLDELGEALKEYYGAN----EEVKAQHRS-----V 93

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720413582  131 RLASADGEHWIDVslVPAFDVLGQPrsgvkptpnvyssllsshcqagEYSACFTEPRKNFVNTRPAKLKNLI 202
Cdd:cd05400     94 TVKFKGQGFHVDV--VPAFEADSGS----------------------KYGSVPDRDGGSWVDRNPKHHAELL 141
SMODS pfam18144
Second Messenger Oligonucleotide or Dinucleotide Synthetase domain; Nucleotide synthetase ...
 801-871 4.25e-07

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: 51.11  E-value: 4.25e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720413582  801 TLAEDLDKFISEfLQPNRHFLTQVKRAVDTICSFLKeNCFRNSTIKVLKVVKGGSSAKGTALQGRSDADLV 871
Cdd:pfam18144    2 SVSSYFTTFLSN-INLSTTTKDSISSRYGTITKRLN-TDFWDFGSKTSESFLVGSYARGTIIRPVSDLDML 70
 
Name Accession Description Interval E-value
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
 954-1136 9.36e-119

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: 364.11  E-value: 9.36e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582  954 SRPDPRVYTDLIHSCSN---AGEFSTCFTELQRDFITSRPTKLKSLIRLVKYWYQQCNKTIKgKGSLPPQHGLELLTVYA 1030
Cdd:pfam10421    1 SKPSPEVYVDLIRSCTSlakPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLK-GASLPPQYALELLTVYA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582 1031 WEQGGQNPQFNMAEGFRTVLELIVQYRQLCVYWTINYSAEDKTIGDFLKMQLRKPRPVILDPADPTGNLGHNA--RWDLL 1108
Cdd:pfam10421   80 WEQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDrwRWDLL 159

                          170       180
                   ....*....|....*....|....*...
gi 1720413582 1109 AKEATVYASALCCVDRDGNPIKPWPVKV 1136
Cdd:pfam10421  160 AQEAAAWLSQPCFKNGDGSPVPSWDVPP 187
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
 160-341 1.11e-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: 350.63  E-value: 1.11e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582  160 KPTPNVYSSLLSSHCQ---AGEYSACFTEPRKNFVNTRPAKLKNLILLVKHWYHQVQTRAVRATLPPSYALELLTIFAWE 236
Cdd:pfam10421    2 KPSPEVYVDLIRSCTSlakPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLKGASLPPQYALELLTVYAWE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582  237 QGCGKDSFSLAQGLRTVLALIQHSKYLCIFWTENYGFEDPAVGEFLRRQLKRPRPVILDPADPTWDVGNGTAWRWDVLAQ 316
Cdd:pfam10421   82 QGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDRWRWDLLAQ 161

                          170       180
                   ....*....|....*....|....*
gi 1720413582  317 EAESSFSQQCFKQASGVLVQPWEGP 341
Cdd:pfam10421  162 EAAAWLSQPCFKNGDGSPVPSWDVP 186
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
 610-796 1.70e-110

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: 342.16  E-value: 1.70e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582  610 TKPQPQVYSSLLSSGCQ---AGEHAACFAELRRNFINTCPPKLKSLMLLVKHWYRQVVTRYKGGeaagdAPPPAYALELL 686
Cdd:pfam10421    1 SKPSPEVYVDLIRSCTSlakPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLKGA-----SLPPQYALELL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582  687 TIFAWEQGCGEQKFSLAEGLRTILRLIQQHQSLCIYWTVNYSVQDPAIRAHLLCQLRKARPLVLDPADPTWNVGQGD--- 763
Cdd:pfam10421   76 TVYAWEQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDrwr 155

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1720413582  764 WKLLAQEAAALGSQVCLQSGDGTLVPPWDVTPA 796
Cdd:pfam10421  156 WDLLAQEAAAWLSQPCFKNGDGSPVPSWDVPPA 188
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 820-999 9.11e-25

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: 101.32  E-value: 9.11e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582  820 FLTQVKRAVDTICSFLKENCFrNSTIKVLKVVKGGSSAKGTALQGRSDADLVVFLSCFrqFSEQGSHRAEIISEIQAHLE 899
Cdd:cd05400      1 PLEEAKERYREIREALKESLS-ELAGRVAEVFLQGSYARGTALRGDSDIDLVVVLPDD--TSFAEYGPAELLDELGEALK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582  900 ACQQmhsfdvKFEVSKRKNPrvlSFTLTSQtllDQSVDFDVLPAFDALGQLrsgsrpdprvytdlihscsnagEFSTCFT 979
Cdd:cd05400     78 EYYG------ANEEVKAQHR---SVTVKFK---GQGFHVDVVPAFEADSGS----------------------KYGSVPD 123

                          170       180
                   ....*....|....*....|
gi 1720413582  980 ELQRDFITSRPTKLKSLIRL 999
Cdd:cd05400    124 RDGGSWVDRNPKHHAELLRR 143
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 482-612 3.09e-15

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: 73.97  E-value: 3.09e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582  482 FQQQVKQAIDAILCCLRE---KSVYKVLRVSKGGSFGRGTDLRGSCDVELVIFYKtlGDFKGQKPHQAEILRDMQAQLRH 558
Cdd:cd05400      1 PLEEAKERYREIREALKEslsELAGRVAEVFLQGSYARGTALRGDSDIDLVVVLP--DDTSFAEYGPAELLDELGEALKE 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720413582  559 WcqnpvPGLSLQFIEQKPnALQLQLASTdlsnRVDLSVLPAFDAVGPLKSGTKP 612
Cdd:cd05400     79 Y-----YGANEEVKAQHR-SVTVKFKGQ----GFHVDVVPAFEADSGSKYGSVP 122
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 51-202 1.52e-10

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: 60.49  E-value: 1.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413582   51 PRVIRIAKGGAYARGTALRGGTDVELVIFLDCFQSFGDQKtcHSETLGAMRMLLESWGGHPgpglTFEFSQSKAsrilqF 130
Cdd:cd05400     25 GRVAEVFLQGSYARGTALRGDSDIDLVVVLPDDTSFAEYG--PAELLDELGEALKEYYGAN----EEVKAQHRS-----V 93

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720413582  131 RLASADGEHWIDVslVPAFDVLGQPrsgvkptpnvyssllsshcqagEYSACFTEPRKNFVNTRPAKLKNLI 202
Cdd:cd05400     94 TVKFKGQGFHVDV--VPAFEADSGS----------------------KYGSVPDRDGGSWVDRNPKHHAELL 141
SMODS pfam18144
Second Messenger Oligonucleotide or Dinucleotide Synthetase domain; Nucleotide synthetase ...
 801-871 4.25e-07

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: 51.11  E-value: 4.25e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720413582  801 TLAEDLDKFISEfLQPNRHFLTQVKRAVDTICSFLKeNCFRNSTIKVLKVVKGGSSAKGTALQGRSDADLV 871
Cdd:pfam18144    2 SVSSYFTTFLSN-INLSTTTKDSISSRYGTITKRLN-TDFWDFGSKTSESFLVGSYARGTIIRPVSDLDML 70
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
 831-895 1.20e-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: 44.71  E-value: 1.20e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720413582  831 ICSFLKENCFRNstiKVLKVVKGGSSAKGTALQGrSDADLVVFLSCFRQFSEQgSHRAEIISEIQ 895
Cdd:pfam01909    1 LRKLREILKELF---PVAEVVLFGSYARGTALPG-SDIDLLVVFPEPVEEERL-LKLAKIIKELE 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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