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Conserved domains on  [gi|1709983880|ref|WP_143334237|]
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SAVED domain-containing protein [Desulfonispora thiosulfatigenes]

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, ...
702-835 6.60e-34

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: 126.19  E-value: 6.60e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 702 DDTEEFIENIMPIEDRYLVKLDCKVAdyeiENGDIQikqiiKLSTLRNEGKKIPLNRILEFYL-DINKVPYPFQVYWKVK 780
Cdd:pfam18134   1 FDTEEFIEPLFPVDIRYDLEIDCEVT----QNGFPG-----SLREYLSSSEPLPKGKSLRFEIkNTHDVPKPYKVKWKVR 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1709983880 781 NNGKKAIENNCIRGEIFKiKEEQFDRlIEESSFEGDHYVECYIVKNGVCVAKDRI 835
Cdd:pfam18134  72 NRGDEAERRNCLRGQIFD-DEGSLTR-KESTAYRGDHYVECYIVKNGVVVARDRI 124
SAVED pfam18145
SMODS-associated and fused to various effectors sensor domain; Predicted to function as a ...
159-354 2.70e-23

SMODS-associated and fused to various effectors sensor domain; Predicted to function as a sensor domain, sensing nucleotides or nucleotide derivatives generated by SMODS and other nucleotide synthetase domains. This domain has been characterized in CD-NTase-associated protein 4 (Cap4), the founding member of a major family of downstream receptors that specifically respond to nucleotide second messenger signals in CBASS immunity, a bacterial system that provides immunity against bacteriophage. SAVED exhibits divergence in its nucleotide binding pocket which enables the recognition of a wide range of CD-NTase products such as bacterial second messengers with alternative ring size, nucleobase, and 3'-5' or 2'-5' phosphodiester linkages. The sensing of ligands by SAVED activates effectors that are essential for CBASS-mediated protection of bacteria from phage infection.


:

Pssm-ID: 436306  Cd Length: 190  Bit Score: 98.15  E-value: 2.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 159 IEEKAKNFINQSGDFKK-AFTGMFSIPFTILAGTYLSATEIDEYLEYNRNKGKYSSLGLKkwyqkkiSYPDLNITTQNTN 237
Cdd:pfam18145   1 LLRQLKRFLKDAIAKGEiAVFGLAPIPLLFLLGSLLGDKSGVDVFQRHREGELWRWDDKD-------DEPSLKIEVEEIG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 238 KQSKEIVVAVSITKNITDEDL--VQFRGKDTLNIGLQNPKDNVIELRKQLEDYVKSIIDNIENLKTVYpNLEIVHLVGAI 315
Cdd:pfam18145  74 NGANEVALAISLSADIDDDRIkeVLGDNLPIIRITLPNPGNDSIRSPEDAAALAQAIRDALDRLKAKY-GVKEIHLFPAA 152
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1709983880 316 PSCLSIELGRKisLNRNRLPLIMSYHFKFGNtPKYNFGI 354
Cdd:pfam18145 153 PASLAFFLGRV--LNPKADPPVIVYEYDRGA-PGYKPAI 188
cGAS super family cl46119
CBASS cGAMP synthase;
374-661 7.31e-17

CBASS cGAMP synthase;


The actual alignment was detected with superfamily member NF041078:

Pssm-ID: 469005  Cd Length: 339  Bit Score: 82.71  E-value: 7.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 374 MYDLSSDFKKF-----YYNEVVLPKEETNNLREKKKLNIQRLKDGLDEYNTKNN-TNYKVaETLEQGSVAMSTVTQ--NE 445
Cdd:NF041078    1 MANLSKLFYSTtdddgFLKRLDLSDEQRDFLKEARNKVRDHLRDGFKEALDKYGgTKVTP-RFFTQGSWAYGTLNRpaQP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 446 KNDYDIDVAIVFDDTNLNG--------LGHRCVKNVIVDRKCNNFKTPPEALTNCVRIVYSDNYHIDFAIY-------KR 510
Cdd:NF041078   80 PQEMDVDDGVYLPMSFFEDerpsvaakTFFEWVEEALKELCEEEGWKLDTDKPTCIRIIIAADAHIDVPLYaipddefDT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 511 IKNDDGSYNYEHAGA---------------------EKWNSRNPRAINNWFKDEIKIHGEKLRQAVRlskmFCKSRSDWK 569
Cdd:NF041078  160 LQEAVAKYAYDSLDEavdfaewealpidvvllahrdGGWIESDPRAVKEWFLDEVDRKGEQLRRIVR----YLKAWRDWQ 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 570 MPGGLIQSVL---CDEKILDY--DRIDEMFYYTIKEIKNRLENDieVYNPTDFEQslllkESDRDKMNnlANRLKDRLSK 644
Cdd:NF041078  236 WEDGGPSSILlmiLAANAFEKrpDRDDLALLDVLKALPERLRGG--VYNPTVDDG-----EDLFRRLS--EEEREEFLDA 306
                         330
                  ....*....|....*..
gi 1709983880 645 LDILFDNnctFKEAIEA 661
Cdd:NF041078  307 LEELIES---LRQALEA 320
 
Name Accession Description Interval E-value
AGS_C pfam18134
Adenylyl/Guanylyl and SMODS C-terminal sensor domain; Predicted to function as a sensor domain, ...
702-835 6.60e-34

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: 126.19  E-value: 6.60e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 702 DDTEEFIENIMPIEDRYLVKLDCKVAdyeiENGDIQikqiiKLSTLRNEGKKIPLNRILEFYL-DINKVPYPFQVYWKVK 780
Cdd:pfam18134   1 FDTEEFIEPLFPVDIRYDLEIDCEVT----QNGFPG-----SLREYLSSSEPLPKGKSLRFEIkNTHDVPKPYKVKWKVR 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1709983880 781 NNGKKAIENNCIRGEIFKiKEEQFDRlIEESSFEGDHYVECYIVKNGVCVAKDRI 835
Cdd:pfam18134  72 NRGDEAERRNCLRGQIFD-DEGSLTR-KESTAYRGDHYVECYIVKNGVVVARDRI 124
SAVED pfam18145
SMODS-associated and fused to various effectors sensor domain; Predicted to function as a ...
159-354 2.70e-23

SMODS-associated and fused to various effectors sensor domain; Predicted to function as a sensor domain, sensing nucleotides or nucleotide derivatives generated by SMODS and other nucleotide synthetase domains. This domain has been characterized in CD-NTase-associated protein 4 (Cap4), the founding member of a major family of downstream receptors that specifically respond to nucleotide second messenger signals in CBASS immunity, a bacterial system that provides immunity against bacteriophage. SAVED exhibits divergence in its nucleotide binding pocket which enables the recognition of a wide range of CD-NTase products such as bacterial second messengers with alternative ring size, nucleobase, and 3'-5' or 2'-5' phosphodiester linkages. The sensing of ligands by SAVED activates effectors that are essential for CBASS-mediated protection of bacteria from phage infection.


Pssm-ID: 436306  Cd Length: 190  Bit Score: 98.15  E-value: 2.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 159 IEEKAKNFINQSGDFKK-AFTGMFSIPFTILAGTYLSATEIDEYLEYNRNKGKYSSLGLKkwyqkkiSYPDLNITTQNTN 237
Cdd:pfam18145   1 LLRQLKRFLKDAIAKGEiAVFGLAPIPLLFLLGSLLGDKSGVDVFQRHREGELWRWDDKD-------DEPSLKIEVEEIG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 238 KQSKEIVVAVSITKNITDEDL--VQFRGKDTLNIGLQNPKDNVIELRKQLEDYVKSIIDNIENLKTVYpNLEIVHLVGAI 315
Cdd:pfam18145  74 NGANEVALAISLSADIDDDRIkeVLGDNLPIIRITLPNPGNDSIRSPEDAAALAQAIRDALDRLKAKY-GVKEIHLFPAA 152
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1709983880 316 PSCLSIELGRKisLNRNRLPLIMSYHFKFGNtPKYNFGI 354
Cdd:pfam18145 153 PASLAFFLGRV--LNPKADPPVIVYEYDRGA-PGYKPAI 188
SAVED NF033611
SAVED domain; The SAVED (SMODS-Associated and fused to Various Effector Domains) domain is ...
103-357 1.18e-21

SAVED domain; The SAVED (SMODS-Associated and fused to Various Effector Domains) domain is predicted to function as a sensor domain, sensing nucleotides or nucleotide derivatives generated by SMODS and other nucleotide synthetase domains. The sensing of ligands by SAVED 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: 468112  Cd Length: 261  Bit Score: 95.23  E-value: 1.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 103 VLNILSKDRRLISDRKTVKDLN-ISDFKLKEHQ---IDVVRMFNDANNITQSSCKYIVEEIEEKAKNFINQSGDFKK--- 175
Cdd:NF033611    5 RELLIAEIGGLRSPLTESEALAaLPPDRLEDRPdlvLDLTQAFSDRKIPSPEDWDEELLELLEKLAKFLRQALRAGDgvr 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 176 -AFTGMFSIPFTILAGTYLSATEIDEYLEYNRNKGKysslglkKWY--QKKISYPDLNITTQNTNKQSKEIVVAVSITKN 252
Cdd:NF033611   85 lALFGLAPVPLAFALGAILGDKSGVTVYQYQRDSSW-------AWStrDPDPEGPPFEVEELEVLQGGDEVALAVSLSYD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 253 ITDEDLVQ---FRGKDTLNIGLQNPKDNVIELRKQLEDYVKSIIDNIENLKTvYPNLEIVHLVGAIPSCLSIELGRKISL 329
Cdd:NF033611  158 INDEDLIEelgPNVGRIISLSLPGPGNDSIRSPEDAAALAKEIREAIRALRA-KPGVKRIHLFLAAPASLAFLLGQRLNA 236
                         250       260
                  ....*....|....*....|....*...
gi 1709983880 330 NRnrlPLIMSYHFKFGNtPKYNFGIIVT 357
Cdd:NF033611  237 RG---PPIVVYEYDRDN-GTYPPALTLP 260
cGAS NF041078
CBASS cGAMP synthase;
374-661 7.31e-17

CBASS cGAMP synthase;


Pssm-ID: 469005  Cd Length: 339  Bit Score: 82.71  E-value: 7.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 374 MYDLSSDFKKF-----YYNEVVLPKEETNNLREKKKLNIQRLKDGLDEYNTKNN-TNYKVaETLEQGSVAMSTVTQ--NE 445
Cdd:NF041078    1 MANLSKLFYSTtdddgFLKRLDLSDEQRDFLKEARNKVRDHLRDGFKEALDKYGgTKVTP-RFFTQGSWAYGTLNRpaQP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 446 KNDYDIDVAIVFDDTNLNG--------LGHRCVKNVIVDRKCNNFKTPPEALTNCVRIVYSDNYHIDFAIY-------KR 510
Cdd:NF041078   80 PQEMDVDDGVYLPMSFFEDerpsvaakTFFEWVEEALKELCEEEGWKLDTDKPTCIRIIIAADAHIDVPLYaipddefDT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 511 IKNDDGSYNYEHAGA---------------------EKWNSRNPRAINNWFKDEIKIHGEKLRQAVRlskmFCKSRSDWK 569
Cdd:NF041078  160 LQEAVAKYAYDSLDEavdfaewealpidvvllahrdGGWIESDPRAVKEWFLDEVDRKGEQLRRIVR----YLKAWRDWQ 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 570 MPGGLIQSVL---CDEKILDY--DRIDEMFYYTIKEIKNRLENDieVYNPTDFEQslllkESDRDKMNnlANRLKDRLSK 644
Cdd:NF041078  236 WEDGGPSSILlmiLAANAFEKrpDRDDLALLDVLKALPERLRGG--VYNPTVDDG-----EDLFRRLS--EEEREEFLDA 306
                         330
                  ....*....|....*..
gi 1709983880 645 LDILFDNnctFKEAIEA 661
Cdd:NF041078  307 LEELIES---LRQALEA 320
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
421-542 5.37e-08

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: 52.79  E-value: 5.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 421 NNTNYKVAETLEQGSVAMSTVTqneKNDYDIDVAIVFDDTNLNGLGH-----RCVKNVIvdRKCNNFKTPPEALTNCVRI 495
Cdd:cd05400    21 SELAGRVAEVFLQGSYARGTAL---RGDSDIDLVVVLPDDTSFAEYGpaellDELGEAL--KEYYGANEEVKAQHRSVTV 95
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1709983880 496 VYSD-NYHIDFAIYKRIKNDDGSYNYEHAGAEKWNSRNPRAINNWFKD 542
Cdd:cd05400    96 KFKGqGFHVDVVPAFEADSGSKYGSVPDRDGGSWVDRNPKHHAELLRR 143
SMODS pfam18144
Second Messenger Oligonucleotide or Dinucleotide Synthetase domain; Nucleotide synthetase ...
377-542 3.14e-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: 44.94  E-value: 3.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 377 LSSDFKKFYYNeVVLPKEETNNLrekkKLNIQRLKDGLDEYNtkNNTNYKVAETLEQGSVAMST-----VTQNEKNDYDI 451
Cdd:pfam18144   3 VSSYFTTFLSN-INLSTTTKDSI----SSRYGTITKRLNTDF--WDFGSKTSESFLVGSYARGTiirpvSDLDMLFRLDA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 452 DVAIVFDDTNLNGlghrcvKNVIVDRKCN----NFKTPPEALTNCVRIVYSDNYHIDfaIYKRIKNDDGSYNYEHAGAEK 527
Cdd:pfam18144  76 DILVVYDPYDGWG------PSDYLQKLKRaiekTYSTSEIRQDRCVIVVYFNHIKFD--VVPAFKNRDGSYTIPDRNNGE 147
                         170
                  ....*....|....*
gi 1709983880 528 WNSRNPRAINNWFKD 542
Cdd:pfam18144 148 WKKTNPREETDWLRE 162
 
Name Accession Description Interval E-value
AGS_C pfam18134
Adenylyl/Guanylyl and SMODS C-terminal sensor domain; Predicted to function as a sensor domain, ...
702-835 6.60e-34

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: 126.19  E-value: 6.60e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 702 DDTEEFIENIMPIEDRYLVKLDCKVAdyeiENGDIQikqiiKLSTLRNEGKKIPLNRILEFYL-DINKVPYPFQVYWKVK 780
Cdd:pfam18134   1 FDTEEFIEPLFPVDIRYDLEIDCEVT----QNGFPG-----SLREYLSSSEPLPKGKSLRFEIkNTHDVPKPYKVKWKVR 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1709983880 781 NNGKKAIENNCIRGEIFKiKEEQFDRlIEESSFEGDHYVECYIVKNGVCVAKDRI 835
Cdd:pfam18134  72 NRGDEAERRNCLRGQIFD-DEGSLTR-KESTAYRGDHYVECYIVKNGVVVARDRI 124
SAVED pfam18145
SMODS-associated and fused to various effectors sensor domain; Predicted to function as a ...
159-354 2.70e-23

SMODS-associated and fused to various effectors sensor domain; Predicted to function as a sensor domain, sensing nucleotides or nucleotide derivatives generated by SMODS and other nucleotide synthetase domains. This domain has been characterized in CD-NTase-associated protein 4 (Cap4), the founding member of a major family of downstream receptors that specifically respond to nucleotide second messenger signals in CBASS immunity, a bacterial system that provides immunity against bacteriophage. SAVED exhibits divergence in its nucleotide binding pocket which enables the recognition of a wide range of CD-NTase products such as bacterial second messengers with alternative ring size, nucleobase, and 3'-5' or 2'-5' phosphodiester linkages. The sensing of ligands by SAVED activates effectors that are essential for CBASS-mediated protection of bacteria from phage infection.


Pssm-ID: 436306  Cd Length: 190  Bit Score: 98.15  E-value: 2.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 159 IEEKAKNFINQSGDFKK-AFTGMFSIPFTILAGTYLSATEIDEYLEYNRNKGKYSSLGLKkwyqkkiSYPDLNITTQNTN 237
Cdd:pfam18145   1 LLRQLKRFLKDAIAKGEiAVFGLAPIPLLFLLGSLLGDKSGVDVFQRHREGELWRWDDKD-------DEPSLKIEVEEIG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 238 KQSKEIVVAVSITKNITDEDL--VQFRGKDTLNIGLQNPKDNVIELRKQLEDYVKSIIDNIENLKTVYpNLEIVHLVGAI 315
Cdd:pfam18145  74 NGANEVALAISLSADIDDDRIkeVLGDNLPIIRITLPNPGNDSIRSPEDAAALAQAIRDALDRLKAKY-GVKEIHLFPAA 152
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1709983880 316 PSCLSIELGRKisLNRNRLPLIMSYHFKFGNtPKYNFGI 354
Cdd:pfam18145 153 PASLAFFLGRV--LNPKADPPVIVYEYDRGA-PGYKPAI 188
SAVED NF033611
SAVED domain; The SAVED (SMODS-Associated and fused to Various Effector Domains) domain is ...
103-357 1.18e-21

SAVED domain; The SAVED (SMODS-Associated and fused to Various Effector Domains) domain is predicted to function as a sensor domain, sensing nucleotides or nucleotide derivatives generated by SMODS and other nucleotide synthetase domains. The sensing of ligands by SAVED 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: 468112  Cd Length: 261  Bit Score: 95.23  E-value: 1.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 103 VLNILSKDRRLISDRKTVKDLN-ISDFKLKEHQ---IDVVRMFNDANNITQSSCKYIVEEIEEKAKNFINQSGDFKK--- 175
Cdd:NF033611    5 RELLIAEIGGLRSPLTESEALAaLPPDRLEDRPdlvLDLTQAFSDRKIPSPEDWDEELLELLEKLAKFLRQALRAGDgvr 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 176 -AFTGMFSIPFTILAGTYLSATEIDEYLEYNRNKGKysslglkKWY--QKKISYPDLNITTQNTNKQSKEIVVAVSITKN 252
Cdd:NF033611   85 lALFGLAPVPLAFALGAILGDKSGVTVYQYQRDSSW-------AWStrDPDPEGPPFEVEELEVLQGGDEVALAVSLSYD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 253 ITDEDLVQ---FRGKDTLNIGLQNPKDNVIELRKQLEDYVKSIIDNIENLKTvYPNLEIVHLVGAIPSCLSIELGRKISL 329
Cdd:NF033611  158 INDEDLIEelgPNVGRIISLSLPGPGNDSIRSPEDAAALAKEIREAIRALRA-KPGVKRIHLFLAAPASLAFLLGQRLNA 236
                         250       260
                  ....*....|....*....|....*...
gi 1709983880 330 NRnrlPLIMSYHFKFGNtPKYNFGIIVT 357
Cdd:NF033611  237 RG---PPIVVYEYDRDN-GTYPPALTLP 260
cGAS NF041078
CBASS cGAMP synthase;
374-661 7.31e-17

CBASS cGAMP synthase;


Pssm-ID: 469005  Cd Length: 339  Bit Score: 82.71  E-value: 7.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 374 MYDLSSDFKKF-----YYNEVVLPKEETNNLREKKKLNIQRLKDGLDEYNTKNN-TNYKVaETLEQGSVAMSTVTQ--NE 445
Cdd:NF041078    1 MANLSKLFYSTtdddgFLKRLDLSDEQRDFLKEARNKVRDHLRDGFKEALDKYGgTKVTP-RFFTQGSWAYGTLNRpaQP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 446 KNDYDIDVAIVFDDTNLNG--------LGHRCVKNVIVDRKCNNFKTPPEALTNCVRIVYSDNYHIDFAIY-------KR 510
Cdd:NF041078   80 PQEMDVDDGVYLPMSFFEDerpsvaakTFFEWVEEALKELCEEEGWKLDTDKPTCIRIIIAADAHIDVPLYaipddefDT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 511 IKNDDGSYNYEHAGA---------------------EKWNSRNPRAINNWFKDEIKIHGEKLRQAVRlskmFCKSRSDWK 569
Cdd:NF041078  160 LQEAVAKYAYDSLDEavdfaewealpidvvllahrdGGWIESDPRAVKEWFLDEVDRKGEQLRRIVR----YLKAWRDWQ 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 570 MPGGLIQSVL---CDEKILDY--DRIDEMFYYTIKEIKNRLENDieVYNPTDFEQslllkESDRDKMNnlANRLKDRLSK 644
Cdd:NF041078  236 WEDGGPSSILlmiLAANAFEKrpDRDDLALLDVLKALPERLRGG--VYNPTVDDG-----EDLFRRLS--EEEREEFLDA 306
                         330
                  ....*....|....*..
gi 1709983880 645 LDILFDNnctFKEAIEA 661
Cdd:NF041078  307 LEELIES---LRQALEA 320
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
421-542 5.37e-08

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: 52.79  E-value: 5.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 421 NNTNYKVAETLEQGSVAMSTVTqneKNDYDIDVAIVFDDTNLNGLGH-----RCVKNVIvdRKCNNFKTPPEALTNCVRI 495
Cdd:cd05400    21 SELAGRVAEVFLQGSYARGTAL---RGDSDIDLVVVLPDDTSFAEYGpaellDELGEAL--KEYYGANEEVKAQHRSVTV 95
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1709983880 496 VYSD-NYHIDFAIYKRIKNDDGSYNYEHAGAEKWNSRNPRAINNWFKD 542
Cdd:cd05400    96 KFKGqGFHVDVVPAFEADSGSKYGSVPDRDGGSWVDRNPKHHAELLRR 143
SMODS pfam18144
Second Messenger Oligonucleotide or Dinucleotide Synthetase domain; Nucleotide synthetase ...
377-542 3.14e-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: 44.94  E-value: 3.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 377 LSSDFKKFYYNeVVLPKEETNNLrekkKLNIQRLKDGLDEYNtkNNTNYKVAETLEQGSVAMST-----VTQNEKNDYDI 451
Cdd:pfam18144   3 VSSYFTTFLSN-INLSTTTKDSI----SSRYGTITKRLNTDF--WDFGSKTSESFLVGSYARGTiirpvSDLDMLFRLDA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709983880 452 DVAIVFDDTNLNGlghrcvKNVIVDRKCN----NFKTPPEALTNCVRIVYSDNYHIDfaIYKRIKNDDGSYNYEHAGAEK 527
Cdd:pfam18144  76 DILVVYDPYDGWG------PSDYLQKLKRaiekTYSTSEIRQDRCVIVVYFNHIKFD--VVPAFKNRDGSYTIPDRNNGE 147
                         170
                  ....*....|....*
gi 1709983880 528 WNSRNPRAINNWFKD 542
Cdd:pfam18144 148 WKKTNPREETDWLRE 162
 
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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