NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|732163804|emb|CEG87911|]
View 

Putative uncharacterized protein [Propionibacterium freudenreichii]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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, ...
 298-426 8.07e-65

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: 204.00  E-value: 8.07e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732163804  298 KNTEEFIEDRYPVDISDTVSIDCDVTQDGWrPMKLREMLRTGTLLKADKRLRFTVVAC-SVPQPYTVKWKVLNRGPEAER 376
Cdd:pfam18134   1 FDTEEFIEPLFPVDIRYDLEIDCEVTQNGF-PGSLREYLSSSEPLPKGKSLRFEIKNThDVPKPYKVKWKVRNRGDEAER 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 732163804  377 RNNIRGQIVDPTASGVRTEHSDFRGEHIVECYIVKGGIVVARDRIDVPIS 426
Cdd:pfam18134  80 RNCLRGQIFDDEGSLTRKESTAYRGDHYVECYIVKNGVVVARDRIDVPIR 129
SMODS pfam18144
Second Messenger Oligonucleotide or Dinucleotide Synthetase domain; Nucleotide synthetase ...
 1-163 4.19e-55

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: 180.15  E-value: 4.19e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732163804    1 MKTAEIFDGLLSALKLGDT-ASVIASRRDEIAKALNKDFREKDGCSDYKLMVGSFGRHTAIKGVSDLDMIYILPPGIRDA 79
Cdd:pfam18144   1 MSVSSYFTTFLSNINLSTTtKDSISSRYGTITKRLNTDFWDFGSKTSESFLVGSYARGTIIRPVSDLDMLFRLDADILVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732163804   80 YA--SDSGPRRMLERVRDDLKARYPSTDIRVDQCVVRVQFaaNAFKFDVQPAFDNADGSFSYPDTKSESWKTTKPRDEIQ 157
Cdd:pfam18144  81 YDpyDGWGPSDYLQKLKRAIEKTYSTSEIRQDRCVIVVYF--NHIKFDVVPAFKNRDGSYTIPDRNNGEWKKTNPREETD 158


                  ....*.
gi 732163804  158 ATRECN 163
Cdd:pfam18144 159 WLREKN 164
 
Name Accession Description Interval E-value
AGS_C pfam18134
Adenylyl/Guanylyl and SMODS C-terminal sensor domain; Predicted to function as a sensor domain, ...
 298-426 8.07e-65

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: 204.00  E-value: 8.07e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732163804  298 KNTEEFIEDRYPVDISDTVSIDCDVTQDGWrPMKLREMLRTGTLLKADKRLRFTVVAC-SVPQPYTVKWKVLNRGPEAER 376
Cdd:pfam18134   1 FDTEEFIEPLFPVDIRYDLEIDCEVTQNGF-PGSLREYLSSSEPLPKGKSLRFEIKNThDVPKPYKVKWKVRNRGDEAER 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 732163804  377 RNNIRGQIVDPTASGVRTEHSDFRGEHIVECYIVKGGIVVARDRIDVPIS 426
Cdd:pfam18134  80 RNCLRGQIFDDEGSLTRKESTAYRGDHYVECYIVKNGVVVARDRIDVPIR 129
SMODS pfam18144
Second Messenger Oligonucleotide or Dinucleotide Synthetase domain; Nucleotide synthetase ...
 1-163 4.19e-55

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: 180.15  E-value: 4.19e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732163804    1 MKTAEIFDGLLSALKLGDT-ASVIASRRDEIAKALNKDFREKDGCSDYKLMVGSFGRHTAIKGVSDLDMIYILPPGIRDA 79
Cdd:pfam18144   1 MSVSSYFTTFLSNINLSTTtKDSISSRYGTITKRLNTDFWDFGSKTSESFLVGSYARGTIIRPVSDLDMLFRLDADILVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732163804   80 YA--SDSGPRRMLERVRDDLKARYPSTDIRVDQCVVRVQFaaNAFKFDVQPAFDNADGSFSYPDTKSESWKTTKPRDEIQ 157
Cdd:pfam18144  81 YDpyDGWGPSDYLQKLKRAIEKTYSTSEIRQDRCVIVVYF--NHIKFDVVPAFKNRDGSYTIPDRNNGEWKKTNPREETD 158


                  ....*.
gi 732163804  158 ATRECN 163
Cdd:pfam18144 159 WLREKN 164
CBASS_cyclase_b NF041117
CBASS oligonucleotide cyclase;
7-282 2.76e-30

CBASS oligonucleotide cyclase;


Pssm-ID: 469040  Cd Length: 273  Bit Score: 118.08  E-value: 2.76e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732163804   7 FDGLLSALKLGDT-ASVIASRRDEIAKALNKDFREKDgcsdyKLMVGSFGRHTAIKGVSDLDMIYILppgiRDAYASDSG 85
Cdd:NF041117   1 FEKFKSRLELNDReQELASERLDEIRDALEEEIEIED-----DFLFGSYRRHTKTKGLSDVDILVVL----NDTSLRDKS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732163804  86 PRRMLERVRDDLKARYPSTDIRVDQCVVRVQFAANaFKFDVQPAFDNADGsFSYPDTKS-ESWKTTKPRDEIQATRECNL 164
Cdd:NF041117  72 PSEVLDAFARRLREKLPNTEVSVGRLAVTVDFGDG-MSIQVLPAFKTGDG-YKIPDTRDgKSWSKTNPKKFAEKLTAANQ 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732163804 165 RTSTNMRHLARMARAWKNANGV-VMGGLLIDTLVYRFFEQTREfdavGTGSFDRMARDFFEFLKN---EPEK---GYYLA 237
Cdd:NF041117 150 ACSGKVVPLVKMIKAWNRNLPKpVQPSYHIEVMAIDAFKGPYG----GPKTYKRMLRHFFATAADrvlSPWPdpaGQSPH 225

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 732163804 238 ----LGSHQRVDVKAKFQpKATKAYNRCVEAMEADGASSANATWREVFG 282
Cdd:NF041117 226 vddyLGAARRARASRKRK-AASQALERAIKLMRNGRTGESLEAWRELFG 273
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 23-161 5.43e-24

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: 97.09  E-value: 5.43e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732163804  23 IASRRDEIAKALNKDFREKDGCSDYKLMVGSFGRHTAIKGVSDLDMIYILPpgiRDAYASDSGPRRMLERVRDDLKARYP 102
Cdd:cd05400    5 AKERYREIREALKESLSELAGRVAEVFLQGSYARGTALRGDSDIDLVVVLP---DDTSFAEYGPAELLDELGEALKEYYG 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732163804 103 -STDIRVDQCVVRVQFAANAFKFDVQPAFDNADGSF--SYPDTKSESWKTTKPRDEIQATRE 161
Cdd:cd05400   82 aNEEVKAQHRSVTVKFKGQGFHVDVVPAFEADSGSKygSVPDRDGGSWVDRNPKHHAELLRR 143
 
Name Accession Description Interval E-value
AGS_C pfam18134
Adenylyl/Guanylyl and SMODS C-terminal sensor domain; Predicted to function as a sensor domain, ...
 298-426 8.07e-65

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: 204.00  E-value: 8.07e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732163804  298 KNTEEFIEDRYPVDISDTVSIDCDVTQDGWrPMKLREMLRTGTLLKADKRLRFTVVAC-SVPQPYTVKWKVLNRGPEAER 376
Cdd:pfam18134   1 FDTEEFIEPLFPVDIRYDLEIDCEVTQNGF-PGSLREYLSSSEPLPKGKSLRFEIKNThDVPKPYKVKWKVRNRGDEAER 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 732163804  377 RNNIRGQIVDPTASGVRTEHSDFRGEHIVECYIVKGGIVVARDRIDVPIS 426
Cdd:pfam18134  80 RNCLRGQIFDDEGSLTRKESTAYRGDHYVECYIVKNGVVVARDRIDVPIR 129
SMODS pfam18144
Second Messenger Oligonucleotide or Dinucleotide Synthetase domain; Nucleotide synthetase ...
 1-163 4.19e-55

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: 180.15  E-value: 4.19e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732163804    1 MKTAEIFDGLLSALKLGDT-ASVIASRRDEIAKALNKDFREKDGCSDYKLMVGSFGRHTAIKGVSDLDMIYILPPGIRDA 79
Cdd:pfam18144   1 MSVSSYFTTFLSNINLSTTtKDSISSRYGTITKRLNTDFWDFGSKTSESFLVGSYARGTIIRPVSDLDMLFRLDADILVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732163804   80 YA--SDSGPRRMLERVRDDLKARYPSTDIRVDQCVVRVQFaaNAFKFDVQPAFDNADGSFSYPDTKSESWKTTKPRDEIQ 157
Cdd:pfam18144  81 YDpyDGWGPSDYLQKLKRAIEKTYSTSEIRQDRCVIVVYF--NHIKFDVVPAFKNRDGSYTIPDRNNGEWKKTNPREETD 158


                  ....*.
gi 732163804  158 ATRECN 163
Cdd:pfam18144 159 WLREKN 164
CBASS_cyclase_b NF041117
CBASS oligonucleotide cyclase;
7-282 2.76e-30

CBASS oligonucleotide cyclase;


Pssm-ID: 469040  Cd Length: 273  Bit Score: 118.08  E-value: 2.76e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732163804   7 FDGLLSALKLGDT-ASVIASRRDEIAKALNKDFREKDgcsdyKLMVGSFGRHTAIKGVSDLDMIYILppgiRDAYASDSG 85
Cdd:NF041117   1 FEKFKSRLELNDReQELASERLDEIRDALEEEIEIED-----DFLFGSYRRHTKTKGLSDVDILVVL----NDTSLRDKS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732163804  86 PRRMLERVRDDLKARYPSTDIRVDQCVVRVQFAANaFKFDVQPAFDNADGsFSYPDTKS-ESWKTTKPRDEIQATRECNL 164
Cdd:NF041117  72 PSEVLDAFARRLREKLPNTEVSVGRLAVTVDFGDG-MSIQVLPAFKTGDG-YKIPDTRDgKSWSKTNPKKFAEKLTAANQ 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732163804 165 RTSTNMRHLARMARAWKNANGV-VMGGLLIDTLVYRFFEQTREfdavGTGSFDRMARDFFEFLKN---EPEK---GYYLA 237
Cdd:NF041117 150 ACSGKVVPLVKMIKAWNRNLPKpVQPSYHIEVMAIDAFKGPYG----GPKTYKRMLRHFFATAADrvlSPWPdpaGQSPH 225

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 732163804 238 ----LGSHQRVDVKAKFQpKATKAYNRCVEAMEADGASSANATWREVFG 282
Cdd:NF041117 226 vddyLGAARRARASRKRK-AASQALERAIKLMRNGRTGESLEAWRELFG 273
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 23-161 5.43e-24

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: 97.09  E-value: 5.43e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732163804  23 IASRRDEIAKALNKDFREKDGCSDYKLMVGSFGRHTAIKGVSDLDMIYILPpgiRDAYASDSGPRRMLERVRDDLKARYP 102
Cdd:cd05400    5 AKERYREIREALKESLSELAGRVAEVFLQGSYARGTALRGDSDIDLVVVLP---DDTSFAEYGPAELLDELGEALKEYYG 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732163804 103 -STDIRVDQCVVRVQFAANAFKFDVQPAFDNADGSF--SYPDTKSESWKTTKPRDEIQATRE 161
Cdd:cd05400   82 aNEEVKAQHRSVTVKFKGQGFHVDVVPAFEADSGSKygSVPDRDGGSWVDRNPKHHAELLRR 143
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH