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Conserved domains on  [gi|1545329514|ref|WP_126497733|]
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MULTISPECIES: nucleotidyltransferase [Enterobacter cloacae complex]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AGS_C pfam18134
Adenylyl/Guanylyl and SMODS C-terminal sensor domain; Predicted to function as a sensor domain, ...
 303-431 9.61e-67

Adenylyl/Guanylyl and SMODS C-terminal sensor domain; Predicted to function as a sensor domain, sensing nucleotides or nucleotide derivatives generated by bacterial adenylyl/guanylyl cyclase domains. The sensing of ligands by AGS-C is predicted to activate effectors deployed by a class of conflict systems which are reliant on the on the production and sensing of the nucleotide second messengers.


:

Pssm-ID: 436297  Cd Length: 129  Bit Score: 209.01  E-value: 9.61e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545329514 303 DDTEEFIEDKFPVDIRESMQLDCEVKQNGFrEFFLSDMLARRIPLMTKKSLRFEITD-VSVSEPYDIYWKVLNRGDAARK 381
Cdd:pfam18134   1 FDTEEFIEPLFPVDIRYDLEIDCEVTQNGF-PGSLREYLSSSEPLPKGKSLRFEIKNtHDVPKPYKVKWKVRNRGDEAER 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1545329514 382 RNCIRGQIIKDDGLMQRTESTSFRGDHIVECYCVKDGVVVAKNRIHVPIN 431
Cdd:pfam18134  80 RNCLRGQIFDDEGSLTRKESTAYRGDHYVECYIVKNGVVVARDRIDVPIR 129
SMODS super family cl39525
Second Messenger Oligonucleotide or Dinucleotide Synthetase domain; Nucleotide synthetase ...
 1-160 4.56e-46

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.


The actual alignment was detected with superfamily member pfam18144:

Pssm-ID: 477034  Cd Length: 164  Bit Score: 156.65  E-value: 4.56e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545329514   1 MSVAQMFSDFVGNLAIG--NAETISLRYSELTAALNKQFQDSESKTANTLQVGSFGRKTGINGISDLDMLYIMPKTKWGD 78
Cdd:pfam18144   1 MSVSSYFTTFLSNINLSttTKDSISSRYGTITKRLNTDFWDFGSKTSESFLVGSYARGTIIRPVSDLDMLFRLDADILVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545329514  79 YN--KAGGQLSLLRDAKDAILKRYPTTKVKVDRLVVTVTYTNFHVEVQPVFEQDDQSYLYPDTKNgGSWKTTKPRAEMTA 156
Cdd:pfam18144  81 YDpyDGWGPSDYLQKLKRAIEKTYSTSEIRQDRCVIVVYFNHIKFDVVPAFKNRDGSYTIPDRNN-GEWKKTNPREETDW 159


                  ....
gi 1545329514 157 VADL 160
Cdd:pfam18144 160 LREK 163
 
Name Accession Description Interval E-value
AGS_C pfam18134
Adenylyl/Guanylyl and SMODS C-terminal sensor domain; Predicted to function as a sensor domain, ...
 303-431 9.61e-67

Adenylyl/Guanylyl and SMODS C-terminal sensor domain; Predicted to function as a sensor domain, sensing nucleotides or nucleotide derivatives generated by bacterial adenylyl/guanylyl cyclase domains. The sensing of ligands by AGS-C is predicted to activate effectors deployed by a class of conflict systems which are reliant on the on the production and sensing of the nucleotide second messengers.


Pssm-ID: 436297  Cd Length: 129  Bit Score: 209.01  E-value: 9.61e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545329514 303 DDTEEFIEDKFPVDIRESMQLDCEVKQNGFrEFFLSDMLARRIPLMTKKSLRFEITD-VSVSEPYDIYWKVLNRGDAARK 381
Cdd:pfam18134   1 FDTEEFIEPLFPVDIRYDLEIDCEVTQNGF-PGSLREYLSSSEPLPKGKSLRFEIKNtHDVPKPYKVKWKVRNRGDEAER 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1545329514 382 RNCIRGQIIKDDGLMQRTESTSFRGDHIVECYCVKDGVVVAKNRIHVPIN 431
Cdd:pfam18134  80 RNCLRGQIFDDEGSLTRKESTAYRGDHYVECYIVKNGVVVARDRIDVPIR 129
SMODS pfam18144
Second Messenger Oligonucleotide or Dinucleotide Synthetase domain; Nucleotide synthetase ...
 1-160 4.56e-46

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: 156.65  E-value: 4.56e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545329514   1 MSVAQMFSDFVGNLAIG--NAETISLRYSELTAALNKQFQDSESKTANTLQVGSFGRKTGINGISDLDMLYIMPKTKWGD 78
Cdd:pfam18144   1 MSVSSYFTTFLSNINLSttTKDSISSRYGTITKRLNTDFWDFGSKTSESFLVGSYARGTIIRPVSDLDMLFRLDADILVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545329514  79 YN--KAGGQLSLLRDAKDAILKRYPTTKVKVDRLVVTVTYTNFHVEVQPVFEQDDQSYLYPDTKNgGSWKTTKPRAEMTA 156
Cdd:pfam18144  81 YDpyDGWGPSDYLQKLKRAIEKTYSTSEIRQDRCVIVVYFNHIKFDVVPAFKNRDGSYTIPDRNN-GEWKKTNPREETDW 159


                  ....
gi 1545329514 157 VADL 160
Cdd:pfam18144 160 LREK 163
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 18-151 3.88e-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: 102.86  E-value: 3.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545329514  18 NAETISLRYSELTAALNKQFQDSESKTANTLQVGSFGRKTGINGISDLDMLYIMPKTkwgDYNKAGGQLSLLRDAKDAIL 97
Cdd:cd05400     1 PLEEAKERYREIREALKESLSELAGRVAEVFLQGSYARGTALRGDSDIDLVVVLPDD---TSFAEYGPAELLDELGEALK 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1545329514  98 KRYP-TTKVKVDRLVVTVTY--TNFHVEVQPVFEQDDQS-YLYPDTKNGGSWKTTKPR 151
Cdd:cd05400    78 EYYGaNEEVKAQHRSVTVKFkgQGFHVDVVPAFEADSGSkYGSVPDRDGGSWVDRNPK 135
 
Name Accession Description Interval E-value
AGS_C pfam18134
Adenylyl/Guanylyl and SMODS C-terminal sensor domain; Predicted to function as a sensor domain, ...
 303-431 9.61e-67

Adenylyl/Guanylyl and SMODS C-terminal sensor domain; Predicted to function as a sensor domain, sensing nucleotides or nucleotide derivatives generated by bacterial adenylyl/guanylyl cyclase domains. The sensing of ligands by AGS-C is predicted to activate effectors deployed by a class of conflict systems which are reliant on the on the production and sensing of the nucleotide second messengers.


Pssm-ID: 436297  Cd Length: 129  Bit Score: 209.01  E-value: 9.61e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545329514 303 DDTEEFIEDKFPVDIRESMQLDCEVKQNGFrEFFLSDMLARRIPLMTKKSLRFEITD-VSVSEPYDIYWKVLNRGDAARK 381
Cdd:pfam18134   1 FDTEEFIEPLFPVDIRYDLEIDCEVTQNGF-PGSLREYLSSSEPLPKGKSLRFEIKNtHDVPKPYKVKWKVRNRGDEAER 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1545329514 382 RNCIRGQIIKDDGLMQRTESTSFRGDHIVECYCVKDGVVVAKNRIHVPIN 431
Cdd:pfam18134  80 RNCLRGQIFDDEGSLTRKESTAYRGDHYVECYIVKNGVVVARDRIDVPIR 129
SMODS pfam18144
Second Messenger Oligonucleotide or Dinucleotide Synthetase domain; Nucleotide synthetase ...
 1-160 4.56e-46

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: 156.65  E-value: 4.56e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545329514   1 MSVAQMFSDFVGNLAIG--NAETISLRYSELTAALNKQFQDSESKTANTLQVGSFGRKTGINGISDLDMLYIMPKTKWGD 78
Cdd:pfam18144   1 MSVSSYFTTFLSNINLSttTKDSISSRYGTITKRLNTDFWDFGSKTSESFLVGSYARGTIIRPVSDLDMLFRLDADILVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545329514  79 YN--KAGGQLSLLRDAKDAILKRYPTTKVKVDRLVVTVTYTNFHVEVQPVFEQDDQSYLYPDTKNgGSWKTTKPRAEMTA 156
Cdd:pfam18144  81 YDpyDGWGPSDYLQKLKRAIEKTYSTSEIRQDRCVIVVYFNHIKFDVVPAFKNRDGSYTIPDRNN-GEWKKTNPREETDW 159


                  ....
gi 1545329514 157 VADL 160
Cdd:pfam18144 160 LREK 163
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 18-151 3.88e-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: 102.86  E-value: 3.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545329514  18 NAETISLRYSELTAALNKQFQDSESKTANTLQVGSFGRKTGINGISDLDMLYIMPKTkwgDYNKAGGQLSLLRDAKDAIL 97
Cdd:cd05400     1 PLEEAKERYREIREALKESLSELAGRVAEVFLQGSYARGTALRGDSDIDLVVVLPDD---TSFAEYGPAELLDELGEALK 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1545329514  98 KRYP-TTKVKVDRLVVTVTY--TNFHVEVQPVFEQDDQS-YLYPDTKNGGSWKTTKPR 151
Cdd:cd05400    78 EYYGaNEEVKAQHRSVTVKFkgQGFHVDVVPAFEADSGSkYGSVPDRDGGSWVDRNPK 135
 
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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