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Conserved domains on  [gi|1293299366|gb|AUA21446|]
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GGDEF domain-containing protein [Clostridioides difficile]

Protein Classification

GGDEF domain-containing protein( domain architecture ID 10005578)

GGDEF domain-containing protein may have diguanylate cyclase (DGC) activity, similar to Escherichia coli DgcT (YcdT) and to E. coli CdgI (YeaI), a c-di-GMP-binding effector with a degenerate GGDEF domain which binds c-di-GMP

CATH:  3.30.70.270
EC:  2.7.7.65
Gene Ontology:  GO:0005525|GO:0046872|GO:0052621|GO:0005886
PubMed:  11119645|15063857|15289546|15306016|16530465|16045609

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 111-247 6.13e-32

GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];


:

Pssm-ID: 441801 [Multi-domain]  Cd Length: 275  Bit Score: 118.93  E-value: 6.13e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299366 111 IITMANDITKLYEENKRNLHYSITDPLTGAYNRKYLNDRFDIFIGD--------YIVLIDLDNFKMINDYEGHNVGDKIL 182
Cdd:COG2199    93 LLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARarregrplALLLIDLDHFKRINDTYGHAAGDEVL 172

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1293299366 183 CDFVSLLNKELINSTSIIRLGGDEFIVIFsSDVDKNYVYSQLEALRENF----LKVFSKYKYLSFSYGV 247
Cdd:COG2199   173 KEVARRLRASLRESDLVARLGGDEFAVLL-PGTDLEEAEALAERLREALeqlpFELEGKELRVTVSIGV 240
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 111-247 6.13e-32

GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];


Pssm-ID: 441801 [Multi-domain]  Cd Length: 275  Bit Score: 118.93  E-value: 6.13e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299366 111 IITMANDITKLYEENKRNLHYSITDPLTGAYNRKYLNDRFDIFIGD--------YIVLIDLDNFKMINDYEGHNVGDKIL 182
Cdd:COG2199    93 LLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARarregrplALLLIDLDHFKRINDTYGHAAGDEVL 172

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1293299366 183 CDFVSLLNKELINSTSIIRLGGDEFIVIFsSDVDKNYVYSQLEALRENF----LKVFSKYKYLSFSYGV 247
Cdd:COG2199   173 KEVARRLRASLRESDLVARLGGDEFAVLL-PGTDLEEAEALAERLREALeqlpFELEGKELRVTVSIGV 240
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 134-247 2.41e-28

Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This 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. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.


Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 106.10  E-value: 2.41e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299366 134 TDPLTGAYNRKYLNDRFDIFIGD--------YIVLIDLDNFKMINDYEGHNVGDKILCDFVSLLNKELINSTSIIRLGGD 205
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLARarrsgrplALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1293299366 206 EFIVIFsSDVDKNYVYSQLEALRENFLKVFSKYK---YLSFSYGV 247
Cdd:cd01949    82 EFAILL-PGTDLEEAEALAERLREAIEEPFFIDGqeiRVTASIGI 125
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 130-247 7.97e-24

diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 94.24  E-value: 7.97e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299366  130 HYSITDPLTGAYNRKYLNDRFDIFIGD--------YIVLIDLDNFKMINDYEGHNVGDKILCDFVSLLNKELINSTSIIR 201
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRaqrqgspfALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1293299366  202 LGGDEFIVIFsSDVDKnyvySQLEALRENFLKVFSKYK-------YLSFSYGV 247
Cdd:smart00267  81 LGGDEFALLL-PETSL----EEAIALAERILQQLREPIiihgiplYLTISIGV 128
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 132-247 4.38e-22

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: 89.62  E-value: 4.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299366 132 SITDPLTGAYNRKYLNDRFDIFIGD--------YIVLIDLDNFKMINDYEGHNVGDKILCDFVSLLNKELINSTSIIRLG 203
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRalregspvAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1293299366 204 GDEFIVIFsSDVDKNYVYSQLEALRENfLKVFSKY-------KYLSFSYGV 247
Cdd:pfam00990  81 GDEFAILL-PETSLEGAQELAERIRRL-LAKLKIPhtvsglpLYVTISIGI 129
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 131-212 1.26e-20

diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]


Pssm-ID: 272984 [Multi-domain]  Cd Length: 165  Bit Score: 85.85  E-value: 1.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299366 131 YSITDPLTGAYNRKYLNDRFDIFIGDY--------IVLIDLDNFKMINDYEGHNVGDKILCDFVSLLNKELINSTSIIRL 202
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRArrfqrsfsVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90
                  ....*....|
gi 1293299366 203 GGDEFIVIFS 212
Cdd:TIGR00254  81 GGEEFVVILP 90
pleD PRK09581
response regulator PleD; Reviewed
 126-210 9.42e-17

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 79.56  E-value: 9.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299366 126 KRNLHYSITDPLTGAYNRKYLNDRFDIFIGD--------YIVLIDLDNFKMINDYEGHNVGDKILCDFVSLLNKELINST 197
Cdd:PRK09581  286 EQSIEMAVTDGLTGLHNRRYFDMHLKNLIERanergkplSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTD 365

                          90
                  ....*....|...
gi 1293299366 198 SIIRLGGDEFIVI 210
Cdd:PRK09581  366 LIARYGGEEFVVV 378
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 111-247 6.13e-32

GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];


Pssm-ID: 441801 [Multi-domain]  Cd Length: 275  Bit Score: 118.93  E-value: 6.13e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299366 111 IITMANDITKLYEENKRNLHYSITDPLTGAYNRKYLNDRFDIFIGD--------YIVLIDLDNFKMINDYEGHNVGDKIL 182
Cdd:COG2199    93 LLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARarregrplALLLIDLDHFKRINDTYGHAAGDEVL 172

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1293299366 183 CDFVSLLNKELINSTSIIRLGGDEFIVIFsSDVDKNYVYSQLEALRENF----LKVFSKYKYLSFSYGV 247
Cdd:COG2199   173 KEVARRLRASLRESDLVARLGGDEFAVLL-PGTDLEEAEALAERLREALeqlpFELEGKELRVTVSIGV 240
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 134-247 2.41e-28

Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This 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. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.


Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 106.10  E-value: 2.41e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299366 134 TDPLTGAYNRKYLNDRFDIFIGD--------YIVLIDLDNFKMINDYEGHNVGDKILCDFVSLLNKELINSTSIIRLGGD 205
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLARarrsgrplALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1293299366 206 EFIVIFsSDVDKNYVYSQLEALRENFLKVFSKYK---YLSFSYGV 247
Cdd:cd01949    82 EFAILL-PGTDLEEAEALAERLREAIEEPFFIDGqeiRVTASIGI 125
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 130-247 7.97e-24

diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 94.24  E-value: 7.97e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299366  130 HYSITDPLTGAYNRKYLNDRFDIFIGD--------YIVLIDLDNFKMINDYEGHNVGDKILCDFVSLLNKELINSTSIIR 201
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRaqrqgspfALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1293299366  202 LGGDEFIVIFsSDVDKnyvySQLEALRENFLKVFSKYK-------YLSFSYGV 247
Cdd:smart00267  81 LGGDEFALLL-PETSL----EEAIALAERILQQLREPIiihgiplYLTISIGV 128
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 132-247 4.38e-22

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: 89.62  E-value: 4.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299366 132 SITDPLTGAYNRKYLNDRFDIFIGD--------YIVLIDLDNFKMINDYEGHNVGDKILCDFVSLLNKELINSTSIIRLG 203
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRalregspvAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1293299366 204 GDEFIVIFsSDVDKNYVYSQLEALRENfLKVFSKY-------KYLSFSYGV 247
Cdd:pfam00990  81 GDEFAILL-PETSLEGAQELAERIRRL-LAKLKIPhtvsglpLYVTISIGI 129
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 131-212 1.26e-20

diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]


Pssm-ID: 272984 [Multi-domain]  Cd Length: 165  Bit Score: 85.85  E-value: 1.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299366 131 YSITDPLTGAYNRKYLNDRFDIFIGDY--------IVLIDLDNFKMINDYEGHNVGDKILCDFVSLLNKELINSTSIIRL 202
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRArrfqrsfsVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90
                  ....*....|
gi 1293299366 203 GGDEFIVIFS 212
Cdd:TIGR00254  81 GGEEFVVILP 90
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 117-212 2.58e-20

Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];


Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 90.22  E-value: 2.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299366 117 DITKLYEENKRNLHYSITDPLTGAYNRKYLNDRFDIFIGDY--------IVLIDLDNFKMINDYEGHNVGDKILCDFVSL 188
Cdd:COG5001   236 LITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARArrsgrrlaLLFIDLDRFKEINDTLGHAAGDELLREVARR 315

                          90       100
                  ....*....|....*....|....
gi 1293299366 189 LNKELINSTSIIRLGGDEFIVIFS 212
Cdd:COG5001   316 LRACLREGDTVARLGGDEFAVLLP 339
pleD PRK09581
response regulator PleD; Reviewed
 126-210 9.42e-17

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 79.56  E-value: 9.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299366 126 KRNLHYSITDPLTGAYNRKYLNDRFDIFIGD--------YIVLIDLDNFKMINDYEGHNVGDKILCDFVSLLNKELINST 197
Cdd:PRK09581  286 EQSIEMAVTDGLTGLHNRRYFDMHLKNLIERanergkplSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTD 365

                          90
                  ....*....|...
gi 1293299366 198 SIIRLGGDEFIVI 210
Cdd:PRK09581  366 LIARYGGEEFVVV 378
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
110-212 8.01e-16

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 77.03  E-value: 8.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299366 110 YIITMANDITKLYEENKRNLHYSITDPLTGAYNRKYLNDRFDIFIGDY------IVLIDLDNFKMINDYEGHNVGDKILC 183
Cdd:PRK10060  215 FLICSGTDITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAAdnnqvgIVYLDLDNFKKVNDAYGHMFGDQLLQ 294

                          90       100       110
                  ....*....|....*....|....*....|
gi 1293299366 184 DfVSLLNKELINSTSII-RLGGDEFIVIFS 212
Cdd:PRK10060  295 D-VSLAILSCLEEDQTLaRLGGDEFLVLAS 323
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 119-228 3.40e-13

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 68.70  E-value: 3.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299366 119 TKLyEENKRNLH-YSITDPLTGAYNRKY----LNDRFDIFIGDY----IVLIDLDNFKMINDYEGHNVGDKILCDFVSLL 189
Cdd:PRK10245  192 TKL-AEHKRRLQvMSTRDGMTGVYNRRHwetlLRNEFDNCRRHHrdatLLIIDIDHFKSINDTWGHDVGDEAIVALTRQL 270

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1293299366 190 NKELINSTSIIRLGGDEFIVIFSSDVDKN------YVYSQLEALR 228
Cdd:PRK10245  271 QITLRGSDVIGRFGGDEFAVIMSGTPAESaitamsRVHEGLNTLR 315
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
134-210 2.75e-12

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 66.58  E-value: 2.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299366 134 TDPLTGAYNRKYLNDRFDIFIGDY--------IVLIDLDNFKMINDYEGHNVGDKILCDFVSLLNKELINSTSIIRLGGD 205
Cdd:PRK15426  400 HDPLTRLYNRGALFEKARALAKRCqrdqqpfsVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGE 479


                  ....*
gi 1293299366 206 EFIVI 210
Cdd:PRK15426  480 EFCVV 484
PRK09894 PRK09894
diguanylate cyclase; Provisional
 135-210 2.80e-12

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 65.47  E-value: 2.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299366 135 DPLTGAYNRKYLNDRFD---IFIGD---YIVLIDLDNFKMINDYEGHNVGDKILCDFVSLLNKELINSTSIIRLGGDEFI 208
Cdd:PRK09894  132 DVLTGLPGRRVLDESFDhqlRNREPqnlYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFI 211


                  ..
gi 1293299366 209 VI 210
Cdd:PRK09894  212 IC 213
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 127-207 3.50e-10

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 60.46  E-value: 3.50e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299366  127 RNLHYSIT-DPLTGAYNRKYLNDRFDIFIGDYI--------VLIDLDNFKMINDYEGHNVGDKILCDFVSLLNKELINST 197
Cdd:PRK09776   659 RQLSYSAShDALTHLANRASFEKQLRRLLQTVNsthqrhalVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSD 738

                           90
                   ....*....|
gi 1293299366  198 SIIRLGGDEF 207
Cdd:PRK09776   739 VLARLGGDEF 748
PRK09966 PRK09966
diguanylate cyclase DgcN;
120-235 9.15e-10

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 58.48  E-value: 9.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299366 120 KLYEENKRNLHYSITDPLTGAYNRKYLNDRFDIFIGD-------YIVLIDLDNFKMINDYEGHNVGDKILCDFVSLLNKE 192
Cdd:PRK09966  236 RLQAKNAQLLRTALHDPLTGLANRAAFRSGINTLMNNsdarktsALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEF 315

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1293299366 193 LINSTSIIRLGGDEFIVIFsSDVDKNYVYSQL-EALRENFLKVF 235
Cdd:PRK09966  316 GGLRHKAYRLGGDEFAMVL-YDVQSESEVQQIcSALTQIFNLPF 358
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 123-216 1.27e-07

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 52.46  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299366 123 EENKRNLHYSIT-DPLTGAYNRKYLNDRFDIFIGD----YIVLIDLDNFKMINDYEGHNVGDKILCDFVSLLNKELINST 197
Cdd:PRK11359  366 EKSRQHIEQLIQfDPLTGLPNRNNLHNYLDDLVDKavspVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQ 445

                          90
                  ....*....|....*....
gi 1293299366 198 SIIRLGGDEFiVIFSSDVD 216
Cdd:PRK11359  446 YLCRIEGTQF-VLVSLEND 463
 
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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