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Conserved domains on  [gi|491147960|ref|WP_005006358|]
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MULTISPECIES: nucleotidyltransferase [Acinetobacter]

Protein Classification

nucleotidyltransferase( domain architecture ID 10143781)

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

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List of domain hits

Name Accession Description Interval E-value
cGAS super family cl46119
CBASS cGAMP synthase;
11-314 2.58e-28

CBASS cGAMP synthase;


The actual alignment was detected with superfamily member NF041078:

Pssm-ID: 469005  Cd Length: 339  Bit Score: 112.37  E-value: 2.58e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147960  11 FHTNIRLGRyDEESTLREKRDLLISTLKDELKK--DPNGPQFVE--YFNQGSYALGTGIKP--KNGDYDIDVGVLL--DC 82
Cdd:NF041078  17 FLKRLDLSD-EQRDFLKEARNKVRDHLRDGFKEalDKYGGTKVTprFFTQGSWAYGTLNRPaqPPQEMDVDDGVYLpmSF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147960  83 DKEEYGSVEIK---KIVRDAL---THSN--RTVTIKRPCVTVTYlkngSPDYHVDLPIYA-EDDKGNMYLARGKEFSSED 153
Cdd:NF041078  96 FEDERPSVAAKtffEWVEEALkelCEEEgwKLDTDKPTCIRIII----AADAHIDVPLYAiPDDEFDTLQEAVAKYAYDS 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147960 154 L-----------------------KTWDISNPTELTDTILGKFEDDSDlrhQFRRCTRYLKQWRNEK-GLDFFKSIAITT 209
Cdd:NF041078 172 LdeavdfaewealpidvvllahrdGGWIESDPRAVKEWFLDEVDRKGE---QLRRIVRYLKAWRDWQwEDGGPSSILLMI 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147960 210 AVYEHITAEDYEnDNKVLLSIVNNVldqfttfsidPEnneyYFRLVINLPAH-QGVDLLEKLTRKQMEHLKSKLEDLKSS 288
Cdd:NF041078 249 LAANAFEKRPDR-DDLALLDVLKAL----------PE----RLRGGVYNPTVdDGEDLFRRLSEEEREEFLDALEELIES 313
                        330       340
                 ....*....|....*....|....*.
gi 491147960 289 LEAVNEETDTVEACKILNKTFGRQFP 314
Cdd:NF041078 314 LRQALEAESKSDALKWLQEHFGDRFP 339
 
Name Accession Description Interval E-value
cGAS NF041078
CBASS cGAMP synthase;
11-314 2.58e-28

CBASS cGAMP synthase;


Pssm-ID: 469005  Cd Length: 339  Bit Score: 112.37  E-value: 2.58e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147960  11 FHTNIRLGRyDEESTLREKRDLLISTLKDELKK--DPNGPQFVE--YFNQGSYALGTGIKP--KNGDYDIDVGVLL--DC 82
Cdd:NF041078  17 FLKRLDLSD-EQRDFLKEARNKVRDHLRDGFKEalDKYGGTKVTprFFTQGSWAYGTLNRPaqPPQEMDVDDGVYLpmSF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147960  83 DKEEYGSVEIK---KIVRDAL---THSN--RTVTIKRPCVTVTYlkngSPDYHVDLPIYA-EDDKGNMYLARGKEFSSED 153
Cdd:NF041078  96 FEDERPSVAAKtffEWVEEALkelCEEEgwKLDTDKPTCIRIII----AADAHIDVPLYAiPDDEFDTLQEAVAKYAYDS 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147960 154 L-----------------------KTWDISNPTELTDTILGKFEDDSDlrhQFRRCTRYLKQWRNEK-GLDFFKSIAITT 209
Cdd:NF041078 172 LdeavdfaewealpidvvllahrdGGWIESDPRAVKEWFLDEVDRKGE---QLRRIVRYLKAWRDWQwEDGGPSSILLMI 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147960 210 AVYEHITAEDYEnDNKVLLSIVNNVldqfttfsidPEnneyYFRLVINLPAH-QGVDLLEKLTRKQMEHLKSKLEDLKSS 288
Cdd:NF041078 249 LAANAFEKRPDR-DDLALLDVLKAL----------PE----RLRGGVYNPTVdDGEDLFRRLSEEEREEFLDALEELIES 313
                        330       340
                 ....*....|....*....|....*.
gi 491147960 289 LEAVNEETDTVEACKILNKTFGRQFP 314
Cdd:NF041078 314 LRQALEAESKSDALKWLQEHFGDRFP 339
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
34-163 1.65e-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: 72.43  E-value: 1.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147960  34 ISTLKDELKKDPNGPQFVEY--FNQGSYALGTGIKpknGDYDIDVGVLLDCDK--EEYGSVEIKKIVRDALTH---SNRT 106
Cdd:cd05400    9 YREIREALKESLSELAGRVAevFLQGSYARGTALR---GDSDIDLVVVLPDDTsfAEYGPAELLDELGEALKEyygANEE 85
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491147960 107 VTIKRPCVTVTYlknGSPDYHVD-LPIYAEDDKGNMYLargkeFSSEDLKTWDISNPT 163
Cdd:cd05400   86 VKAQHRSVTVKF---KGQGFHVDvVPAFEADSGSKYGS-----VPDRDGGSWVDRNPK 135
SMODS pfam18144
Second Messenger Oligonucleotide or Dinucleotide Synthetase domain; Nucleotide synthetase ...
34-169 5.51e-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: 43.02  E-value: 5.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147960   34 ISTLKDELKKDPNGP--QFVEYFNQGSYALGTGIKPKNGDY-----DIDVGVLLDcDKEEYGSVEIKKIVRDAL--THSN 104
Cdd:pfam18144  28 YGTITKRLNTDFWDFgsKTSESFLVGSYARGTIIRPVSDLDmlfrlDADILVVYD-PYDGWGPSDYLQKLKRAIekTYST 106
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491147960  105 RTVTIKRpCVTVTYLKngspDYHVDL-PIYAEDDKGNMYLARGKEfssedlkTWDISNPTELTDTI 169
Cdd:pfam18144 107 SEIRQDR-CVIVVYFN----HIKFDVvPAFKNRDGSYTIPDRNNG-------EWKKTNPREETDWL 160
PRK13300 PRK13300
CCA tRNA nucleotidyltransferase;
21-133 1.23e-04

CCA tRNA nucleotidyltransferase;


Pssm-ID: 237340 [Multi-domain]  Cd Length: 447  Bit Score: 43.73  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147960  21 DEESTLREKRDLLISTLKDELKKDPNGpqfVEYFNQGSYALGTGIKpknGDYDIDVGVLLDCDK-----EEYGsveiKKI 95
Cdd:PRK13300  15 EEREKLKKVAEELIERLEEAIKELGLD---AEVELVGSTARGTWLS---GDRDIDIFVLFPKDTsreelEEKG----LEI 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 491147960  96 VRDALTHSNRTVTIK---RPCVTVTYlkngsPDYHVDL-PIY 133
Cdd:PRK13300  85 GKEVAKELLGDYEERyaeHPYVTGEI-----DGFEVDIvPCY 121
 
Name Accession Description Interval E-value
cGAS NF041078
CBASS cGAMP synthase;
11-314 2.58e-28

CBASS cGAMP synthase;


Pssm-ID: 469005  Cd Length: 339  Bit Score: 112.37  E-value: 2.58e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147960  11 FHTNIRLGRyDEESTLREKRDLLISTLKDELKK--DPNGPQFVE--YFNQGSYALGTGIKP--KNGDYDIDVGVLL--DC 82
Cdd:NF041078  17 FLKRLDLSD-EQRDFLKEARNKVRDHLRDGFKEalDKYGGTKVTprFFTQGSWAYGTLNRPaqPPQEMDVDDGVYLpmSF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147960  83 DKEEYGSVEIK---KIVRDAL---THSN--RTVTIKRPCVTVTYlkngSPDYHVDLPIYA-EDDKGNMYLARGKEFSSED 153
Cdd:NF041078  96 FEDERPSVAAKtffEWVEEALkelCEEEgwKLDTDKPTCIRIII----AADAHIDVPLYAiPDDEFDTLQEAVAKYAYDS 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147960 154 L-----------------------KTWDISNPTELTDTILGKFEDDSDlrhQFRRCTRYLKQWRNEK-GLDFFKSIAITT 209
Cdd:NF041078 172 LdeavdfaewealpidvvllahrdGGWIESDPRAVKEWFLDEVDRKGE---QLRRIVRYLKAWRDWQwEDGGPSSILLMI 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147960 210 AVYEHITAEDYEnDNKVLLSIVNNVldqfttfsidPEnneyYFRLVINLPAH-QGVDLLEKLTRKQMEHLKSKLEDLKSS 288
Cdd:NF041078 249 LAANAFEKRPDR-DDLALLDVLKAL----------PE----RLRGGVYNPTVdDGEDLFRRLSEEEREEFLDALEELIES 313
                        330       340
                 ....*....|....*....|....*.
gi 491147960 289 LEAVNEETDTVEACKILNKTFGRQFP 314
Cdd:NF041078 314 LRQALEAESKSDALKWLQEHFGDRFP 339
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
34-163 1.65e-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: 72.43  E-value: 1.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147960  34 ISTLKDELKKDPNGPQFVEY--FNQGSYALGTGIKpknGDYDIDVGVLLDCDK--EEYGSVEIKKIVRDALTH---SNRT 106
Cdd:cd05400    9 YREIREALKESLSELAGRVAevFLQGSYARGTALR---GDSDIDLVVVLPDDTsfAEYGPAELLDELGEALKEyygANEE 85
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491147960 107 VTIKRPCVTVTYlknGSPDYHVD-LPIYAEDDKGNMYLargkeFSSEDLKTWDISNPT 163
Cdd:cd05400   86 VKAQHRSVTVKF---KGQGFHVDvVPAFEADSGSKYGS-----VPDRDGGSWVDRNPK 135
SMODS pfam18144
Second Messenger Oligonucleotide or Dinucleotide Synthetase domain; Nucleotide synthetase ...
34-169 5.51e-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: 43.02  E-value: 5.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147960   34 ISTLKDELKKDPNGP--QFVEYFNQGSYALGTGIKPKNGDY-----DIDVGVLLDcDKEEYGSVEIKKIVRDAL--THSN 104
Cdd:pfam18144  28 YGTITKRLNTDFWDFgsKTSESFLVGSYARGTIIRPVSDLDmlfrlDADILVVYD-PYDGWGPSDYLQKLKRAIekTYST 106
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491147960  105 RTVTIKRpCVTVTYLKngspDYHVDL-PIYAEDDKGNMYLARGKEfssedlkTWDISNPTELTDTI 169
Cdd:pfam18144 107 SEIRQDR-CVIVVYFN----HIKFDVvPAFKNRDGSYTIPDRNNG-------EWKKTNPREETDWL 160
PRK13300 PRK13300
CCA tRNA nucleotidyltransferase;
21-133 1.23e-04

CCA tRNA nucleotidyltransferase;


Pssm-ID: 237340 [Multi-domain]  Cd Length: 447  Bit Score: 43.73  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147960  21 DEESTLREKRDLLISTLKDELKKDPNGpqfVEYFNQGSYALGTGIKpknGDYDIDVGVLLDCDK-----EEYGsveiKKI 95
Cdd:PRK13300  15 EEREKLKKVAEELIERLEEAIKELGLD---AEVELVGSTARGTWLS---GDRDIDIFVLFPKDTsreelEEKG----LEI 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 491147960  96 VRDALTHSNRTVTIK---RPCVTVTYlkngsPDYHVDL-PIY 133
Cdd:PRK13300  85 GKEVAKELLGDYEERyaeHPYVTGEI-----DGFEVDIvPCY 121
 
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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