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Conserved domains on  [gi|45007007|ref|NP_006178|]
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2'-5'-oligoadenylate synthase 3 isoform 1 [Homo sapiens]

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, ...
 161-343 2.92e-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: 2.92e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007    161 KPKPQVYSTLLNSGCQ---GGEHAACFTELRRNFVNIRPAKLKNLILLVKHWYHQvCLQGLWKETLPPVYALELLTIFAW 237
Cdd:pfam10421    2 KPSPEVYVDLIRSCTSlakPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQ-CKKKLKGASLPPQYALELLTVYAW 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007    238 EQGCKKDAFSLAEGLRTVLGLIQQHQHLCVFWTVNYGFEDPAVGQFLQRQLKRPRPVILDPADPTWDLGNGAAWHWDLLA 317
Cdd:pfam10421   81 EQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDRWRWDLLA 160

                          170       180
                   ....*....|....*....|....*.
gi 45007007    318 QEAASCYDHPCFLRGMGDPVQSWKGP 343
Cdd:pfam10421  161 QEAAAWLSQPCFKNGDGSPVPSWDVP 186
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
 903-1086 2.71e-118

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: 361.80  E-value: 2.71e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007    903 SRPSSQVYVDLIHSYSN---AGEYSTCFTELQRDFIISRPTKLKSLIRLVKHWYQQCTKiSKGRGSLPPQHGLELLTVYA 979
Cdd:pfam10421    1 SKPSPEVYVDLIRSCTSlakPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKK-KLKGASLPPQYALELLTVYA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007    980 WEQGGKDSQFNMAEGFRTVLELVTQYRQLCIYWTINYNAKDKTVGDFLKQQLQKPRPIILDPADPTGNLGHNA--RWDLL 1057
Cdd:pfam10421   80 WEQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDrwRWDLL 159

                          170       180
                   ....*....|....*....|....*....
gi 45007007   1058 AKEAAACTSALCCMGRNGIPIQPWPVKAA 1086
Cdd:pfam10421  160 AQEAAAWLSQPCFKNGDGSPVPSWDVPPA 188
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
 559-745 5.90e-116

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: 355.64  E-value: 5.90e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007    559 TKPNPQVYSRLLTSGCQ---EGEHKACFAELRRNFMNIRPVKLKNLILLVKHWYRQVAAQNKGkgpapASLPPAYALELL 635
Cdd:pfam10421    1 SKPSPEVYVDLIRSCTSlakPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLKG-----ASLPPQYALELL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007    636 TIFAWEQGCRQDCFNMAQGFRTVLGLVQQHQQLCVYWTVNYSTEDPAMRMHLLGQLRKPRPLVLDPADPTWNVGHG---S 712
Cdd:pfam10421   76 TVYAWEQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGdrwR 155

                          170       180       190
                   ....*....|....*....|....*....|...
gi 45007007    713 WELLAQEAAALGMQACFLSRDGTSVQPWDVMPA 745
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 ...
 769-948 4.98e-26

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: 104.79  E-value: 4.98e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007  769 FLAQVNKAVDTICSFLKENCFrNSPIKVIKVVKGGSSAKGTALRGRSDADLVVFLSCFSQFTEQGnkRAEIISEIRAQLE 848
Cdd:cd05400    1 PLEEAKERYREIREALKESLS-ELAGRVAEVFLQGSYARGTALRGDSDIDLVVVLPDDTSFAEYG--PAELLDELGEALK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007  849 ACQQERQFEVKfevskwENPRV-LSFSltsqtmlDQSVDFDVLPAFDALGQLvsgsrpssqvyvdlihsysnagEYSTCF 927
Cdd:cd05400   78 EYYGANEEVKA------QHRSVtVKFK-------GQGFHVDVVPAFEADSGS----------------------KYGSVP 122

                        170       180
                 ....*....|....*....|.
gi 45007007  928 TELQRDFIISRPTKLKSLIRL 948
Cdd:cd05400  123 DRDGGSWVDRNPKHHAELLRR 143
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 430-571 2.49e-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: 82.83  E-value: 2.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007  430 FQEQVKKAIDIILRCLHENCVHKASRVSK---GGSFGRGTDLRDGCDVELIIFLNCFTDYKDQGPrrAEILDEMRAQLES 506
Cdd:cd05400    1 PLEEAKERYREIREALKESLSELAGRVAEvflQGSYARGTALRGDSDIDLVVVLPDDTSFAEYGP--AELLDELGEALKE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007  507 WWQD------QVPSLSLQFPEQNVpealqfqlvstalkswtDVSLLPAFDAVGQLSSGT----------KPNPQVYSRLL 570
Cdd:cd05400   79 YYGAneevkaQHRSVTVKFKGQGF-----------------HVDVVPAFEADSGSKYGSvpdrdggswvDRNPKHHAELL 141


                 .
gi 45007007  571 T 571
Cdd:cd05400  142 R 142
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 46-172 6.70e-11

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: 61.26  E-value: 6.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007   46 RLGAAAPRVLKTVKGGSSGRGTALKGGCDSELVIFLDCFKSYvdQRARRAEILSEMRASLESWWQNPvpglrlTFPEQSV 125
Cdd:cd05400   19 SLSELAGRVAEVFLQGSYARGTALRGDSDIDLVVVLPDDTSF--AEYGPAELLDELGEALKEYYGAN------EEVKAQH 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 45007007  126 PGA-LQFRLTsvdledWMDVSLVPAFNVLGQ----------AGSGVKPKPQVYSTLLN 172
Cdd:cd05400   91 RSVtVKFKGQ------GFHVDVVPAFEADSGskygsvpdrdGGSWVDRNPKHHAELLR 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, ...
 161-343 2.92e-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: 2.92e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007    161 KPKPQVYSTLLNSGCQ---GGEHAACFTELRRNFVNIRPAKLKNLILLVKHWYHQvCLQGLWKETLPPVYALELLTIFAW 237
Cdd:pfam10421    2 KPSPEVYVDLIRSCTSlakPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQ-CKKKLKGASLPPQYALELLTVYAW 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007    238 EQGCKKDAFSLAEGLRTVLGLIQQHQHLCVFWTVNYGFEDPAVGQFLQRQLKRPRPVILDPADPTWDLGNGAAWHWDLLA 317
Cdd:pfam10421   81 EQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDRWRWDLLA 160

                          170       180
                   ....*....|....*....|....*.
gi 45007007    318 QEAASCYDHPCFLRGMGDPVQSWKGP 343
Cdd:pfam10421  161 QEAAAWLSQPCFKNGDGSPVPSWDVP 186
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
 903-1086 2.71e-118

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: 361.80  E-value: 2.71e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007    903 SRPSSQVYVDLIHSYSN---AGEYSTCFTELQRDFIISRPTKLKSLIRLVKHWYQQCTKiSKGRGSLPPQHGLELLTVYA 979
Cdd:pfam10421    1 SKPSPEVYVDLIRSCTSlakPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKK-KLKGASLPPQYALELLTVYA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007    980 WEQGGKDSQFNMAEGFRTVLELVTQYRQLCIYWTINYNAKDKTVGDFLKQQLQKPRPIILDPADPTGNLGHNA--RWDLL 1057
Cdd:pfam10421   80 WEQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDrwRWDLL 159

                          170       180
                   ....*....|....*....|....*....
gi 45007007   1058 AKEAAACTSALCCMGRNGIPIQPWPVKAA 1086
Cdd:pfam10421  160 AQEAAAWLSQPCFKNGDGSPVPSWDVPPA 188
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
 559-745 5.90e-116

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: 355.64  E-value: 5.90e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007    559 TKPNPQVYSRLLTSGCQ---EGEHKACFAELRRNFMNIRPVKLKNLILLVKHWYRQVAAQNKGkgpapASLPPAYALELL 635
Cdd:pfam10421    1 SKPSPEVYVDLIRSCTSlakPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLKG-----ASLPPQYALELL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007    636 TIFAWEQGCRQDCFNMAQGFRTVLGLVQQHQQLCVYWTVNYSTEDPAMRMHLLGQLRKPRPLVLDPADPTWNVGHG---S 712
Cdd:pfam10421   76 TVYAWEQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGdrwR 155

                          170       180       190
                   ....*....|....*....|....*....|...
gi 45007007    713 WELLAQEAAALGMQACFLSRDGTSVQPWDVMPA 745
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 ...
 769-948 4.98e-26

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: 104.79  E-value: 4.98e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007  769 FLAQVNKAVDTICSFLKENCFrNSPIKVIKVVKGGSSAKGTALRGRSDADLVVFLSCFSQFTEQGnkRAEIISEIRAQLE 848
Cdd:cd05400    1 PLEEAKERYREIREALKESLS-ELAGRVAEVFLQGSYARGTALRGDSDIDLVVVLPDDTSFAEYG--PAELLDELGEALK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007  849 ACQQERQFEVKfevskwENPRV-LSFSltsqtmlDQSVDFDVLPAFDALGQLvsgsrpssqvyvdlihsysnagEYSTCF 927
Cdd:cd05400   78 EYYGANEEVKA------QHRSVtVKFK-------GQGFHVDVVPAFEADSGS----------------------KYGSVP 122

                        170       180
                 ....*....|....*....|.
gi 45007007  928 TELQRDFIISRPTKLKSLIRL 948
Cdd:cd05400  123 DRDGGSWVDRNPKHHAELLRR 143
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 430-571 2.49e-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: 82.83  E-value: 2.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007  430 FQEQVKKAIDIILRCLHENCVHKASRVSK---GGSFGRGTDLRDGCDVELIIFLNCFTDYKDQGPrrAEILDEMRAQLES 506
Cdd:cd05400    1 PLEEAKERYREIREALKESLSELAGRVAEvflQGSYARGTALRGDSDIDLVVVLPDDTSFAEYGP--AELLDELGEALKE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007  507 WWQD------QVPSLSLQFPEQNVpealqfqlvstalkswtDVSLLPAFDAVGQLSSGT----------KPNPQVYSRLL 570
Cdd:cd05400   79 YYGAneevkaQHRSVTVKFKGQGF-----------------HVDVVPAFEADSGSKYGSvpdrdggswvDRNPKHHAELL 141


                 .
gi 45007007  571 T 571
Cdd:cd05400  142 R 142
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 46-172 6.70e-11

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: 61.26  E-value: 6.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007   46 RLGAAAPRVLKTVKGGSSGRGTALKGGCDSELVIFLDCFKSYvdQRARRAEILSEMRASLESWWQNPvpglrlTFPEQSV 125
Cdd:cd05400   19 SLSELAGRVAEVFLQGSYARGTALRGDSDIDLVVVLPDDTSF--AEYGPAELLDELGEALKEYYGAN------EEVKAQH 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 45007007  126 PGA-LQFRLTsvdledWMDVSLVPAFNVLGQ----------AGSGVKPKPQVYSTLLN 172
Cdd:cd05400   91 RSVtVKFKGQ------GFHVDVVPAFEADSGskygsvpdrdGGSWVDRNPKHHAELLR 142
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
 780-871 5.51e-08

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: 51.26  E-value: 5.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007    780 ICSFLKENCFRNspiKVIKVVKGGSSAKGTALRGrSDADLVVFLSCFSQFTEQgNKRAEIISEIR--AQLEACQQER-QF 856
Cdd:pfam01909    1 LRKLREILKELF---PVAEVVLFGSYARGTALPG-SDIDLLVVFPEPVEEERL-LKLAKIIKELEelLGLEVDLVTReKI 75

                           90
                   ....*....|....*
gi 45007007    857 EVKFEVSKWENPRVL 871
Cdd:pfam01909   76 EFPLVKIDILEERIL 90
 
Name Accession Description Interval E-value
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
 161-343 2.92e-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: 2.92e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007    161 KPKPQVYSTLLNSGCQ---GGEHAACFTELRRNFVNIRPAKLKNLILLVKHWYHQvCLQGLWKETLPPVYALELLTIFAW 237
Cdd:pfam10421    2 KPSPEVYVDLIRSCTSlakPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQ-CKKKLKGASLPPQYALELLTVYAW 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007    238 EQGCKKDAFSLAEGLRTVLGLIQQHQHLCVFWTVNYGFEDPAVGQFLQRQLKRPRPVILDPADPTWDLGNGAAWHWDLLA 317
Cdd:pfam10421   81 EQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDRWRWDLLA 160

                          170       180
                   ....*....|....*....|....*.
gi 45007007    318 QEAASCYDHPCFLRGMGDPVQSWKGP 343
Cdd:pfam10421  161 QEAAAWLSQPCFKNGDGSPVPSWDVP 186
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
 903-1086 2.71e-118

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: 361.80  E-value: 2.71e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007    903 SRPSSQVYVDLIHSYSN---AGEYSTCFTELQRDFIISRPTKLKSLIRLVKHWYQQCTKiSKGRGSLPPQHGLELLTVYA 979
Cdd:pfam10421    1 SKPSPEVYVDLIRSCTSlakPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKK-KLKGASLPPQYALELLTVYA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007    980 WEQGGKDSQFNMAEGFRTVLELVTQYRQLCIYWTINYNAKDKTVGDFLKQQLQKPRPIILDPADPTGNLGHNA--RWDLL 1057
Cdd:pfam10421   80 WEQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDrwRWDLL 159

                          170       180
                   ....*....|....*....|....*....
gi 45007007   1058 AKEAAACTSALCCMGRNGIPIQPWPVKAA 1086
Cdd:pfam10421  160 AQEAAAWLSQPCFKNGDGSPVPSWDVPPA 188
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
 559-745 5.90e-116

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: 355.64  E-value: 5.90e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007    559 TKPNPQVYSRLLTSGCQ---EGEHKACFAELRRNFMNIRPVKLKNLILLVKHWYRQVAAQNKGkgpapASLPPAYALELL 635
Cdd:pfam10421    1 SKPSPEVYVDLIRSCTSlakPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLKG-----ASLPPQYALELL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007    636 TIFAWEQGCRQDCFNMAQGFRTVLGLVQQHQQLCVYWTVNYSTEDPAMRMHLLGQLRKPRPLVLDPADPTWNVGHG---S 712
Cdd:pfam10421   76 TVYAWEQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGdrwR 155

                          170       180       190
                   ....*....|....*....|....*....|...
gi 45007007    713 WELLAQEAAALGMQACFLSRDGTSVQPWDVMPA 745
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 ...
 769-948 4.98e-26

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: 104.79  E-value: 4.98e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007  769 FLAQVNKAVDTICSFLKENCFrNSPIKVIKVVKGGSSAKGTALRGRSDADLVVFLSCFSQFTEQGnkRAEIISEIRAQLE 848
Cdd:cd05400    1 PLEEAKERYREIREALKESLS-ELAGRVAEVFLQGSYARGTALRGDSDIDLVVVLPDDTSFAEYG--PAELLDELGEALK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007  849 ACQQERQFEVKfevskwENPRV-LSFSltsqtmlDQSVDFDVLPAFDALGQLvsgsrpssqvyvdlihsysnagEYSTCF 927
Cdd:cd05400   78 EYYGANEEVKA------QHRSVtVKFK-------GQGFHVDVVPAFEADSGS----------------------KYGSVP 122

                        170       180
                 ....*....|....*....|.
gi 45007007  928 TELQRDFIISRPTKLKSLIRL 948
Cdd:cd05400  123 DRDGGSWVDRNPKHHAELLRR 143
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 430-571 2.49e-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: 82.83  E-value: 2.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007  430 FQEQVKKAIDIILRCLHENCVHKASRVSK---GGSFGRGTDLRDGCDVELIIFLNCFTDYKDQGPrrAEILDEMRAQLES 506
Cdd:cd05400    1 PLEEAKERYREIREALKESLSELAGRVAEvflQGSYARGTALRGDSDIDLVVVLPDDTSFAEYGP--AELLDELGEALKE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007  507 WWQD------QVPSLSLQFPEQNVpealqfqlvstalkswtDVSLLPAFDAVGQLSSGT----------KPNPQVYSRLL 570
Cdd:cd05400   79 YYGAneevkaQHRSVTVKFKGQGF-----------------HVDVVPAFEADSGSKYGSvpdrdggswvDRNPKHHAELL 141


                 .
gi 45007007  571 T 571
Cdd:cd05400  142 R 142
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 46-172 6.70e-11

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: 61.26  E-value: 6.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007   46 RLGAAAPRVLKTVKGGSSGRGTALKGGCDSELVIFLDCFKSYvdQRARRAEILSEMRASLESWWQNPvpglrlTFPEQSV 125
Cdd:cd05400   19 SLSELAGRVAEVFLQGSYARGTALRGDSDIDLVVVLPDDTSF--AEYGPAELLDELGEALKEYYGAN------EEVKAQH 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 45007007  126 PGA-LQFRLTsvdledWMDVSLVPAFNVLGQ----------AGSGVKPKPQVYSTLLN 172
Cdd:cd05400   91 RSVtVKFKGQ------GFHVDVVPAFEADSGskygsvpdrdGGSWVDRNPKHHAELLR 142
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
 780-871 5.51e-08

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: 51.26  E-value: 5.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45007007    780 ICSFLKENCFRNspiKVIKVVKGGSSAKGTALRGrSDADLVVFLSCFSQFTEQgNKRAEIISEIR--AQLEACQQER-QF 856
Cdd:pfam01909    1 LRKLREILKELF---PVAEVVLFGSYARGTALPG-SDIDLLVVFPEPVEEERL-LKLAKIIKELEelLGLEVDLVTReKI 75

                           90
                   ....*....|....*
gi 45007007    857 EVKFEVSKWENPRVL 871
Cdd:pfam01909   76 EFPLVKIDILEERIL 90
SMODS pfam18144
Second Messenger Oligonucleotide or Dinucleotide Synthetase domain; Nucleotide synthetase ...
 754-820 1.03e-05

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: 46.87  E-value: 1.03e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45007007    754 DLDKFISEfLQPNRQFLAQVNKAVDTICSFLKeNCFRNSPIKVIKVVKGGSSAKGTALRGRSDADLV 820
Cdd:pfam18144    6 YFTTFLSN-INLSTTTKDSISSRYGTITKRLN-TDFWDFGSKTSESFLVGSYARGTIIRPVSDLDML 70
 
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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