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Conserved domains on  [gi|2214762279|ref|WP_242996223|]
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MULTISPECIES: BTAD domain-containing putative transcriptional regulator [Clostridia]

Protein Classification

BTAD and Nucleotidyl_cyc_III domain-containing protein( domain architecture ID 12224432)

BTAD and Nucleotidyl_cyc_III domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BTAD smart01043
Bacterial transcriptional activator domain; Found in the DNRI/REDD/AFSR family of regulators. ...
 117-249 5.50e-13

Bacterial transcriptional activator domain; Found in the DNRI/REDD/AFSR family of regulators. This region of AFSR along with the C terminal region is capable of independently directing actinorhodin production. This family contains TPR repeats.


:

Pssm-ID: 198111 [Multi-domain]  Cd Length: 145  Bit Score: 65.79  E-value: 5.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214762279  117 DASEFDRLYQEALN--EEDIDCRLQLLLDACHCYTGEFLIMYAGVLWAASEARRYRAQFCTCVEEAAGILKEKEDYLQLQ 194
Cdd:smart01043   2 DVDRFERLVAAARAalAADPEAALALLEAALALYRGPLLADVPDEDWAEAERERLRELRLEALEALAEALLALGRHEEAL 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2214762279  195 ELGVYATAISPFSD--WESItMDALISMGCYEEASDLYAETVERYFKERGIRPSQKL 249
Cdd:smart01043  82 ALLERLLALDPLRErlHRLL-MRALYRAGRRAEALRAYRRLRRLLADELGVEPGPEL 137
Nucleotidyl_cyc_III super family cl11967
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 303-379 2.12e-05

Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.


The actual alignment was detected with superfamily member pfam00990:

Pssm-ID: 448371 [Multi-domain]  Cd Length: 160  Bit Score: 44.55  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214762279 303 AERSGQSIYLMLC------TIVDSKGNrmKSGEQ-LEQLAGRLGDaickSIRRGDAVNRYGRGQYLVLLVNTTLESCAIV 375
Cdd:pfam00990  26 ALREGSPVAVLLIdldnfkRINDTYGH--SVGDEvLQEVAQRLSS----SLRRSDLVARLGGDEFAILLPETSLEGAQEL 99


                  ....
gi 2214762279 376 QKRI 379
Cdd:pfam00990 100 AERI 103
 
Name Accession Description Interval E-value
BTAD smart01043
Bacterial transcriptional activator domain; Found in the DNRI/REDD/AFSR family of regulators. ...
 117-249 5.50e-13

Bacterial transcriptional activator domain; Found in the DNRI/REDD/AFSR family of regulators. This region of AFSR along with the C terminal region is capable of independently directing actinorhodin production. This family contains TPR repeats.


Pssm-ID: 198111 [Multi-domain]  Cd Length: 145  Bit Score: 65.79  E-value: 5.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214762279  117 DASEFDRLYQEALN--EEDIDCRLQLLLDACHCYTGEFLIMYAGVLWAASEARRYRAQFCTCVEEAAGILKEKEDYLQLQ 194
Cdd:smart01043   2 DVDRFERLVAAARAalAADPEAALALLEAALALYRGPLLADVPDEDWAEAERERLRELRLEALEALAEALLALGRHEEAL 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2214762279  195 ELGVYATAISPFSD--WESItMDALISMGCYEEASDLYAETVERYFKERGIRPSQKL 249
Cdd:smart01043  82 ALLERLLALDPLRErlHRLL-MRALYRAGRRAEALRAYRRLRRLLADELGVEPGPEL 137
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 303-379 2.12e-05

Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.


Pssm-ID: 425976 [Multi-domain]  Cd Length: 160  Bit Score: 44.55  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214762279 303 AERSGQSIYLMLC------TIVDSKGNrmKSGEQ-LEQLAGRLGDaickSIRRGDAVNRYGRGQYLVLLVNTTLESCAIV 375
Cdd:pfam00990  26 ALREGSPVAVLLIdldnfkRINDTYGH--SVGDEvLQEVAQRLSS----SLRRSDLVARLGGDEFAILLPETSLEGAQEL 99


                  ....
gi 2214762279 376 QKRI 379
Cdd:pfam00990 100 AERI 103
 
Name Accession Description Interval E-value
BTAD smart01043
Bacterial transcriptional activator domain; Found in the DNRI/REDD/AFSR family of regulators. ...
 117-249 5.50e-13

Bacterial transcriptional activator domain; Found in the DNRI/REDD/AFSR family of regulators. This region of AFSR along with the C terminal region is capable of independently directing actinorhodin production. This family contains TPR repeats.


Pssm-ID: 198111 [Multi-domain]  Cd Length: 145  Bit Score: 65.79  E-value: 5.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214762279  117 DASEFDRLYQEALN--EEDIDCRLQLLLDACHCYTGEFLIMYAGVLWAASEARRYRAQFCTCVEEAAGILKEKEDYLQLQ 194
Cdd:smart01043   2 DVDRFERLVAAARAalAADPEAALALLEAALALYRGPLLADVPDEDWAEAERERLRELRLEALEALAEALLALGRHEEAL 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2214762279  195 ELGVYATAISPFSD--WESItMDALISMGCYEEASDLYAETVERYFKERGIRPSQKL 249
Cdd:smart01043  82 ALLERLLALDPLRErlHRLL-MRALYRAGRRAEALRAYRRLRRLLADELGVEPGPEL 137
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 303-379 2.12e-05

Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.


Pssm-ID: 425976 [Multi-domain]  Cd Length: 160  Bit Score: 44.55  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214762279 303 AERSGQSIYLMLC------TIVDSKGNrmKSGEQ-LEQLAGRLGDaickSIRRGDAVNRYGRGQYLVLLVNTTLESCAIV 375
Cdd:pfam00990  26 ALREGSPVAVLLIdldnfkRINDTYGH--SVGDEvLQEVAQRLSS----SLRRSDLVARLGGDEFAILLPETSLEGAQEL 99


                  ....
gi 2214762279 376 QKRI 379
Cdd:pfam00990 100 AERI 103
 
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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