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Conserved domains on  [gi|567930787|ref|WP_024033165|]
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MULTISPECIES: GGDEF domain-containing protein [Pseudoalteromonas]

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 ...
 24-306 2.41e-51

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: 170.93  E-value: 2.41e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787  24 DASLVQIIGDLLEVENFAIYINKHFSAQLPPTLINTHTRLEVLESNEALALLNKVTQNKIRVSRALGVVTTYVPVYYFgk 103
Cdd:COG2199    1 VLLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLS-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 104 vIGILLIETTKELAQTTTMLAvHILNIYANQLGLLHKSRLDPLTELLNRQTFDKKVIEIVSgkgfllprDDTNEKRRWYL 183
Cdd:COG2199   79 -LVLELLLLLLALLLLLLALE-DITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELA--------RARREGRPLAL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 184 AIADIDHFKRVNDSYGHVIGDEVILLVARLLKNNFRLEDYVFRYGGEEFAVLFQTKTEAQAHIALNRLRSNIAEYPFPQV 263
Cdd:COG2199  149 LLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELE 228

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 567930787 264 GQ---LTISIGFLEL-ASIDTVSSIVNQADMALYHSKNSGRNKVTAY 306
Cdd:COG2199  229 GKelrVTVSIGVALYpEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 24-306 2.41e-51

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: 170.93  E-value: 2.41e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787  24 DASLVQIIGDLLEVENFAIYINKHFSAQLPPTLINTHTRLEVLESNEALALLNKVTQNKIRVSRALGVVTTYVPVYYFgk 103
Cdd:COG2199    1 VLLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLS-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 104 vIGILLIETTKELAQTTTMLAvHILNIYANQLGLLHKSRLDPLTELLNRQTFDKKVIEIVSgkgfllprDDTNEKRRWYL 183
Cdd:COG2199   79 -LVLELLLLLLALLLLLLALE-DITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELA--------RARREGRPLAL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 184 AIADIDHFKRVNDSYGHVIGDEVILLVARLLKNNFRLEDYVFRYGGEEFAVLFQTKTEAQAHIALNRLRSNIAEYPFPQV 263
Cdd:COG2199  149 LLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELE 228

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 567930787 264 GQ---LTISIGFLEL-ASIDTVSSIVNQADMALYHSKNSGRNKVTAY 306
Cdd:COG2199  229 GKelrVTVSIGVALYpEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 144-303 1.70e-50

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: 164.65  E-value: 1.70e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 144 DPLTELLNRQTFDKKVIEIVSgkgfllprDDTNEKRRWYLAIADIDHFKRVNDSYGHVIGDEVILLVARLLKNNFRLEDY 223
Cdd:cd01949    3 DPLTGLPNRRAFEERLERLLA--------RARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 224 VFRYGGEEFAVLFQTKTEAQAHIALNRLRSNIAEYPFP--QVGQLTISIGFLEL-ASIDTVSSIVNQADMALYHSKNSGR 300
Cdd:cd01949   75 VARLGGDEFAILLPGTDLEEAEALAERLREAIEEPFFIdgQEIRVTASIGIATYpEDGEDAEELLRRADEALYRAKRSGR 154


                 ...
gi 567930787 301 NKV 303
Cdd:cd01949  155 NRV 157
PRK09894 PRK09894
diguanylate cyclase; Provisional
 122-311 1.92e-39

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 140.59  E-value: 1.92e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 122 MLAVHILNIYANQLGllhkSRLDPLTELLNRQTFDKKvieivsgkgflLPRDDTN-EKRRWYLAIADIDHFKRVNDSYGH 200
Cdd:PRK09894 114 TAALTDYKIYLLTIR----SNMDVLTGLPGRRVLDES-----------FDHQLRNrEPQNLYLALLDIDRFKLVNDTYGH 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 201 VIGDEVILLVARLLKNNFRLEDYVFRYGGEEFAVLFQTKTEAQAHIALNRLRSNIAEYPFPQVG---QLTISIGFLELAS 277
Cdd:PRK09894 179 LIGDVVLRTLATYLASWTRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDgriNITATFGVSRAFP 258

                        170       180       190
                 ....*....|....*....|....*....|....
gi 567930787 278 IDTVSSIVNQADMALYHSKNSGRNKVTAYSELEV 311
Cdd:PRK09894 259 EETLDVVIGRADRAMYEGKQTGRNRVMFIDEQNV 292
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 144-302 2.31e-35

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: 125.83  E-value: 2.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787  144 DPLTELLNRQTFD---KKVIEIVSGKGFLLprddtnekrrwYLAIADIDHFKRVNDSYGHVIGDEVILLVARLLKNNFRL 220
Cdd:pfam00990   4 DPLTGLPNRRYFEeqlEQELQRALREGSPV-----------AVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787  221 EDYVFRYGGEEFAVLFQTKTEAQAHIALNRLRSNIAEYPFP-----QVGQLTISIGfleLASI----DTVSSIVNQADMA 291
Cdd:pfam00990  73 SDLVARLGGDEFAILLPETSLEGAQELAERIRRLLAKLKIPhtvsgLPLYVTISIG---IAAYpndgEDPEDLLKRADTA 149

                         170
                  ....*....|.
gi 567930787  292 LYHSKNSGRNK 302
Cdd:pfam00990 150 LYQAKQAGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 141-306 9.33e-35

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 124.28  E-value: 9.33e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787   141 SRLDPLTELLNRQTFDKKVIEIVSGKgfllprddTNEKRRWYLAIADIDHFKRVNDSYGHVIGDEVILLVARLLKNNFRL 220
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQELQRA--------QRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRP 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787   221 EDYVFRYGGEEFAVLFQTKTEAQAHIALNRLRSNIAEYPFP--QVGQLTISIGFLELA-SIDTVSSIVNQADMALYHSKN 297
Cdd:smart00267  75 GDLLARLGGDEFALLLPETSLEEAIALAERILQQLREPIIIhgIPLYLTISIGVAAYPnPGEDAEDLLKRADTALYQAKK 154


                   ....*....
gi 567930787   298 SGRNKVTAY 306
Cdd:smart00267 155 AGRNQVAVY 163
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 144-303 2.75e-32

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: 117.82  E-value: 2.75e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787  144 DPLTELLNRQTFDKKvIEIVSGKGFLLPRDDTnekrrwyLAIADIDHFKRVNDSYGHVIGDEVILLVARLLKNNFRLEDY 223
Cdd:TIGR00254   5 DPLTGLYNRRYLEEM-LDSELKRARRFQRSFS-------VLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787  224 VFRYGGEEFAVLFQTKTEAQAHIALNRLRSNIAEYPFP----QVGQLTISIGfleLASI----DTVSSIVNQADMALYHS 295
Cdd:TIGR00254  77 VGRYGGEEFVVILPGTPLEDALSKAERLRDAINSKPIEvagsETLTVTVSIG---VACYpghgLTLEELLKRADEALYQA 153


                  ....*...
gi 567930787  296 KNSGRNKV 303
Cdd:TIGR00254 154 KKAGRNRV 161
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
141-303 5.70e-30

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 114.31  E-value: 5.70e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 141 SRLDPLTELLNRQTFDKKVIEIV-----SGKGFLLprddtnekrrwylAIADIDHFKRVNDSYGHVIGDEVILLVARLLK 215
Cdd:NF038266  94 STRDPLTGLPNRRLLMERLREEVerarrSGRPFTL-------------AMLDVDHFKRINDRYGHEVGDRVLVEIARTLR 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 216 NNFRLEDYVFRYGGEEFAVLFQTKTEAQAHIALNRLRSNIAEYPFP---QVGQLTISIGFLEL-ASIDTVSSIVNQADMA 291
Cdd:NF038266 161 AELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRvgdDVLSVTASAGLAEHrPPEEGLSATLSRADQA 240

                        170
                 ....*....|..
gi 567930787 292 LYHSKNSGRNKV 303
Cdd:NF038266 241 LYQAKRAGRDRV 252
dguan_cyc_DgcA NF041606
diguanylate cyclase DgcA;
59-304 2.19e-27

diguanylate cyclase DgcA;


Pssm-ID: 469490 [Multi-domain]  Cd Length: 340  Bit Score: 109.45  E-value: 2.19e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787  59 THTRLEVLESNEALALLNKVTQNkIRVSRALGVV-----TTYVPVYYFGKVIGILLI-ETTKELAQTTTMLAVHILNIYA 132
Cdd:NF041606  85 NHPLLRLLDKENSCLSPEEIQKN-IKPDKIVESLfslnpSLFVPLKAKNHMVGFLLLgEQIEAGEEYTPYEKEIIMNIAS 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 133 ------NQLGLLHKSRLDPLTELLNRQTFdkkvieivsgKGFLLPRDDTNEKRRWYLAIA--DIDHFKRVNDSYGHVIGD 204
Cdd:NF041606 164 laaiaiNNALLLEMTTTDMMTHLKLKHYF----------YTVLMEKLDTINSQGEPLSILmlDIDFFKQINDTYGHACGD 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 205 EVILLVARLLKNNFRLEDYVFRYGGEEFAV-LFQTKTEAQAHIAlNRLRSNIAEYPFPQVGQ---LTISIGFLE-LASID 279
Cdd:NF041606 234 LVLQMVASIIQSCTRTQDMAARYGGEEFVVmLSNTSSKTAKKIA-ERIRKSIENLSILYDEQhirVTISIGVAEyNFDVE 312

                        250       260
                 ....*....|....*....|....*
gi 567930787 280 TVSSIVNQADMALYHSKNSGRNKVT 304
Cdd:NF041606 313 SAKSLVERADKALYESKQNGRNRVS 337
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 24-306 2.41e-51

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: 170.93  E-value: 2.41e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787  24 DASLVQIIGDLLEVENFAIYINKHFSAQLPPTLINTHTRLEVLESNEALALLNKVTQNKIRVSRALGVVTTYVPVYYFgk 103
Cdd:COG2199    1 VLLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLS-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 104 vIGILLIETTKELAQTTTMLAvHILNIYANQLGLLHKSRLDPLTELLNRQTFDKKVIEIVSgkgfllprDDTNEKRRWYL 183
Cdd:COG2199   79 -LVLELLLLLLALLLLLLALE-DITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELA--------RARREGRPLAL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 184 AIADIDHFKRVNDSYGHVIGDEVILLVARLLKNNFRLEDYVFRYGGEEFAVLFQTKTEAQAHIALNRLRSNIAEYPFPQV 263
Cdd:COG2199  149 LLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELE 228

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 567930787 264 GQ---LTISIGFLEL-ASIDTVSSIVNQADMALYHSKNSGRNKVTAY 306
Cdd:COG2199  229 GKelrVTVSIGVALYpEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 144-303 1.70e-50

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: 164.65  E-value: 1.70e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 144 DPLTELLNRQTFDKKVIEIVSgkgfllprDDTNEKRRWYLAIADIDHFKRVNDSYGHVIGDEVILLVARLLKNNFRLEDY 223
Cdd:cd01949    3 DPLTGLPNRRAFEERLERLLA--------RARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 224 VFRYGGEEFAVLFQTKTEAQAHIALNRLRSNIAEYPFP--QVGQLTISIGFLEL-ASIDTVSSIVNQADMALYHSKNSGR 300
Cdd:cd01949   75 VARLGGDEFAILLPGTDLEEAEALAERLREAIEEPFFIdgQEIRVTASIGIATYpEDGEDAEELLRRADEALYRAKRSGR 154


                 ...
gi 567930787 301 NKV 303
Cdd:cd01949  155 NRV 157
PRK09894 PRK09894
diguanylate cyclase; Provisional
 122-311 1.92e-39

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 140.59  E-value: 1.92e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 122 MLAVHILNIYANQLGllhkSRLDPLTELLNRQTFDKKvieivsgkgflLPRDDTN-EKRRWYLAIADIDHFKRVNDSYGH 200
Cdd:PRK09894 114 TAALTDYKIYLLTIR----SNMDVLTGLPGRRVLDES-----------FDHQLRNrEPQNLYLALLDIDRFKLVNDTYGH 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 201 VIGDEVILLVARLLKNNFRLEDYVFRYGGEEFAVLFQTKTEAQAHIALNRLRSNIAEYPFPQVG---QLTISIGFLELAS 277
Cdd:PRK09894 179 LIGDVVLRTLATYLASWTRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDgriNITATFGVSRAFP 258

                        170       180       190
                 ....*....|....*....|....*....|....
gi 567930787 278 IDTVSSIVNQADMALYHSKNSGRNKVTAYSELEV 311
Cdd:PRK09894 259 EETLDVVIGRADRAMYEGKQTGRNRVMFIDEQNV 292
pleD PRK09581
response regulator PleD; Reviewed
 144-305 5.95e-38

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 140.04  E-value: 5.95e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 144 DPLTELLNRQTFDKKVIEIVsgkgfllpRDDTNEKRRWYLAIADIDHFKRVNDSYGHVIGDEVILLVARLLKNNFRLEDY 223
Cdd:PRK09581 295 DGLTGLHNRRYFDMHLKNLI--------ERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDL 366

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 224 VFRYGGEEFAVLFQTKTEAQAHIALNRLRSNIAEYPFPQVGQ-----LTISIGFLELA-SIDTVSSIVNQADMALYHSKN 297
Cdd:PRK09581 367 IARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGkerlnVTVSIGVAELRpSGDTIEALIKRADKALYEAKN 446


                 ....*...
gi 567930787 298 SGRNKVTA 305
Cdd:PRK09581 447 TGRNRVVA 454
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 144-302 2.31e-35

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: 125.83  E-value: 2.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787  144 DPLTELLNRQTFD---KKVIEIVSGKGFLLprddtnekrrwYLAIADIDHFKRVNDSYGHVIGDEVILLVARLLKNNFRL 220
Cdd:pfam00990   4 DPLTGLPNRRYFEeqlEQELQRALREGSPV-----------AVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787  221 EDYVFRYGGEEFAVLFQTKTEAQAHIALNRLRSNIAEYPFP-----QVGQLTISIGfleLASI----DTVSSIVNQADMA 291
Cdd:pfam00990  73 SDLVARLGGDEFAILLPETSLEGAQELAERIRRLLAKLKIPhtvsgLPLYVTISIG---IAAYpndgEDPEDLLKRADTA 149

                         170
                  ....*....|.
gi 567930787  292 LYHSKNSGRNK 302
Cdd:pfam00990 150 LYQAKQAGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 141-306 9.33e-35

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 124.28  E-value: 9.33e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787   141 SRLDPLTELLNRQTFDKKVIEIVSGKgfllprddTNEKRRWYLAIADIDHFKRVNDSYGHVIGDEVILLVARLLKNNFRL 220
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQELQRA--------QRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRP 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787   221 EDYVFRYGGEEFAVLFQTKTEAQAHIALNRLRSNIAEYPFP--QVGQLTISIGFLELA-SIDTVSSIVNQADMALYHSKN 297
Cdd:smart00267  75 GDLLARLGGDEFALLLPETSLEEAIALAERILQQLREPIIIhgIPLYLTISIGVAAYPnPGEDAEDLLKRADTALYQAKK 154


                   ....*....
gi 567930787   298 SGRNKVTAY 306
Cdd:smart00267 155 AGRNQVAVY 163
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 8-322 1.57e-33

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: 130.28  E-value: 1.57e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787   8 HEWIISLTQQEEESDLDASLVQIIGDLLEVENFAIYINKHFSAQLPPTLINTHTRLEVLESNEALALLNKVTQNKIRVSR 87
Cdd:COG5001  118 ALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLL 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787  88 ALGVVTTYVPVYYFGKVIGILLIETTKELAQTTTMLAVHILNIYANQLGLLHKSRLDPLTELLNRQTFDKKVIEivsgkg 167
Cdd:COG5001  198 LLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQ------ 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 168 fLLPRDDTNEKRrwyLAIA--DIDHFKRVNDSYGHVIGDEVILLVARLLKNNFRLEDYVFRYGGEEFAVLFQ-TKTEAQA 244
Cdd:COG5001  272 -ALARARRSGRR---LALLfiDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPdLDDPEDA 347

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 245 HIALNRLRSNIAEyPFpQVGQLTISIGflelASI---------DTVSSIVNQADMALYHSKNSGRNKVTAYSElEVNEEV 315
Cdd:COG5001  348 EAVAERILAALAE-PF-ELDGHELYVS----ASIgialypddgADAEELLRNADLAMYRAKAAGRNRYRFFDP-EMDERA 420


                 ....*..
gi 567930787 316 TTDNSIE 322
Cdd:COG5001  421 RERLELE 427
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 144-303 2.75e-32

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: 117.82  E-value: 2.75e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787  144 DPLTELLNRQTFDKKvIEIVSGKGFLLPRDDTnekrrwyLAIADIDHFKRVNDSYGHVIGDEVILLVARLLKNNFRLEDY 223
Cdd:TIGR00254   5 DPLTGLYNRRYLEEM-LDSELKRARRFQRSFS-------VLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787  224 VFRYGGEEFAVLFQTKTEAQAHIALNRLRSNIAEYPFP----QVGQLTISIGfleLASI----DTVSSIVNQADMALYHS 295
Cdd:TIGR00254  77 VGRYGGEEFVVILPGTPLEDALSKAERLRDAINSKPIEvagsETLTVTVSIG---VACYpghgLTLEELLKRADEALYQA 153


                  ....*...
gi 567930787  296 KNSGRNKV 303
Cdd:TIGR00254 154 KKAGRNRV 161
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
141-303 5.70e-30

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 114.31  E-value: 5.70e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 141 SRLDPLTELLNRQTFDKKVIEIV-----SGKGFLLprddtnekrrwylAIADIDHFKRVNDSYGHVIGDEVILLVARLLK 215
Cdd:NF038266  94 STRDPLTGLPNRRLLMERLREEVerarrSGRPFTL-------------AMLDVDHFKRINDRYGHEVGDRVLVEIARTLR 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 216 NNFRLEDYVFRYGGEEFAVLFQTKTEAQAHIALNRLRSNIAEYPFP---QVGQLTISIGFLEL-ASIDTVSSIVNQADMA 291
Cdd:NF038266 161 AELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRvgdDVLSVTASAGLAEHrPPEEGLSATLSRADQA 240

                        170
                 ....*....|..
gi 567930787 292 LYHSKNSGRNKV 303
Cdd:NF038266 241 LYQAKRAGRDRV 252
dguan_cyc_DgcA NF041606
diguanylate cyclase DgcA;
59-304 2.19e-27

diguanylate cyclase DgcA;


Pssm-ID: 469490 [Multi-domain]  Cd Length: 340  Bit Score: 109.45  E-value: 2.19e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787  59 THTRLEVLESNEALALLNKVTQNkIRVSRALGVV-----TTYVPVYYFGKVIGILLI-ETTKELAQTTTMLAVHILNIYA 132
Cdd:NF041606  85 NHPLLRLLDKENSCLSPEEIQKN-IKPDKIVESLfslnpSLFVPLKAKNHMVGFLLLgEQIEAGEEYTPYEKEIIMNIAS 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 133 ------NQLGLLHKSRLDPLTELLNRQTFdkkvieivsgKGFLLPRDDTNEKRRWYLAIA--DIDHFKRVNDSYGHVIGD 204
Cdd:NF041606 164 laaiaiNNALLLEMTTTDMMTHLKLKHYF----------YTVLMEKLDTINSQGEPLSILmlDIDFFKQINDTYGHACGD 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 205 EVILLVARLLKNNFRLEDYVFRYGGEEFAV-LFQTKTEAQAHIAlNRLRSNIAEYPFPQVGQ---LTISIGFLE-LASID 279
Cdd:NF041606 234 LVLQMVASIIQSCTRTQDMAARYGGEEFVVmLSNTSSKTAKKIA-ERIRKSIENLSILYDEQhirVTISIGVAEyNFDVE 312

                        250       260
                 ....*....|....*....|....*
gi 567930787 280 TVSSIVNQADMALYHSKNSGRNKVT 304
Cdd:NF041606 313 SAKSLVERADKALYESKQNGRNRVS 337
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 137-306 1.96e-23

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 100.90  E-value: 1.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787  137 LLHKSRLDPLTELLNRQTFDKKVIEIVsgkgfllprDDTNEKR-RWYLAIADIDHFKRVNDSYGHVIGDEVILLVARLLK 215
Cdd:PRK09776  661 LSYSASHDALTHLANRASFEKQLRRLL---------QTVNSTHqRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLML 731

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787  216 NNFRLEDYVFRYGGEEFAVLFQTKTEAQAHIALNRLRSNIAEYPFPQVGQL---TISIGFLEL-ASIDTVSSIVNQADMA 291
Cdd:PRK09776  732 SMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPWEGRVyrvGASAGITLIdANNHQASEVMSQADIA 811

                         170
                  ....*....|....*
gi 567930787  292 LYHSKNSGRNKVTAY 306
Cdd:PRK09776  812 CYAAKNAGRGRVTVY 826
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 139-302 6.56e-23

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 97.59  E-value: 6.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 139 HKSRL------DPLTELLNRQTFDkkvieivsgkgfLLPRDDTNEKRRWY----LAIADIDHFKRVNDSYGHVIGDEVIL 208
Cdd:PRK10245 197 HKRRLqvmstrDGMTGVYNRRHWE------------TLLRNEFDNCRRHHrdatLLIIDIDHFKSINDTWGHDVGDEAIV 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 209 LVARLLKNNFRLEDYVFRYGGEEFAVLFqTKTEAQAHIA--------LNRLRSNIAeypfPQVgQLTISIGFLELAS-ID 279
Cdd:PRK10245 265 ALTRQLQITLRGSDVIGRFGGDEFAVIM-SGTPAESAITamsrvhegLNTLRLPNA----PQV-TLRISVGVAPLNPqMS 338

                        170       180
                 ....*....|....*....|...
gi 567930787 280 TVSSIVNQADMALYHSKNSGRNK 302
Cdd:PRK10245 339 HYREWLKSADLALYKAKNAGRNR 361
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
121-305 1.10e-21

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 95.47  E-value: 1.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 121 TMLAVHIL--NIYANQLGLLHKSRLDPLTELLNRQTFdkkvieivsgkgFLLPRDDTNEKRRWYLAIA----DIDHFKRV 194
Cdd:PRK15426 376 SWYVIRRMvsNMFVLQSSLQWQAWHDPLTRLYNRGAL------------FEKARALAKRCQRDQQPFSviqlDLDHFKSI 443

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 195 NDSYGHVIGDEVILLVARLLKNNFRLEDYVFRYGGEEFAVLFQTKTEAQAHIALNRLRSNIAEyPFPQVG-----QLTIS 269
Cdd:PRK15426 444 NDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINE-KEILVAksttiRISAS 522

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 567930787 270 IGFLELA-----SIDTVSSIvnqADMALYHSKNSGRNKVTA 305
Cdd:PRK15426 523 LGVSSAEedgdyDFEQLQSL---ADRRLYLAKQAGRNRVCA 560
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
144-315 1.54e-16

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 80.11  E-value: 1.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 144 DPLTELLNRQTFDKKVIEIVSgkgfllpRDDTNEKRRWYLaiaDIDHFKRVNDSYGHVIGDEVILLVARLLKNNFRLEDY 223
Cdd:PRK10060 240 DSITGLPNRNAIQELIDHAIN-------AADNNQVGIVYL---DLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQT 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 224 VFRYGGEEFAVLFQTKT----EAQAHIALNRLRSniaeyPFpqvgqltiSIGFLEL---ASI---------DTVSSIVNQ 287
Cdd:PRK10060 310 LARLGGDEFLVLASHTSqaalEAMASRILTRLRL-----PF--------RIGLIEVytgCSIgialapehgDDSESLIRS 376

                        170       180
                 ....*....|....*....|....*...
gi 567930787 288 ADMALYHSKNSGRNKVTAYSeLEVNEEV 315
Cdd:PRK10060 377 ADTAMYTAKEGGRGQFCVFS-PEMNQRV 403
PRK09966 PRK09966
diguanylate cyclase DgcN;
128-297 3.02e-13

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 69.65  E-value: 3.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 128 LNIYANQLGLLHKSRLDPLTELLNRQTFDKKVIEIVsgkgfllprDDTNEKRRWYLAIADIDHFKRVNDSYGHVIGDEVI 207
Cdd:PRK09966 235 LRLQAKNAQLLRTALHDPLTGLANRAAFRSGINTLM---------NNSDARKTSALLFLDGDNFKYINDTWGHATGDRVL 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 208 LLVARLLKNNFRLEDYVFRYGGEEFA-VLFQTKTEAQAHIALNRLrSNIAEYPFP----QVGQLTISIGF---LELASID 279
Cdd:PRK09966 306 IEIAKRLAEFGGLRHKAYRLGGDEFAmVLYDVQSESEVQQICSAL-TQIFNLPFDlhngHQTTMTLSIGYamtIEHASAE 384

                        170
                 ....*....|....*...
gi 567930787 280 TVSSIvnqADMALYHSKN 297
Cdd:PRK09966 385 KLQEL---ADHNMYQAKH 399
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 209-296 1.78e-10

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 59.15  E-value: 1.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 209 LVARLlknnfrleDYVFRYGGEEFAVLFQTKTEAQAHIALNRLRSNIAEYPFPQVgqlTISIGFlelasidTVSSIVNQA 288
Cdd:COG3706  111 LLARV--------DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAELPSLRV---TVSIGV-------AGDSLLKRA 172


                 ....*...
gi 567930787 289 DmALYHSK 296
Cdd:COG3706  173 D-ALYQAR 179
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 183-298 2.21e-10

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.


Pssm-ID: 143637 [Multi-domain]  Cd Length: 133  Bit Score: 57.75  E-value: 2.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 183 LAIADIDHFKRVNDSYGHVIGDEVILLVARLLKNN-FRLEDYVFRYGGEEFAVLFqTKTEAQAHIAL-NRLRSNIAEYPF 260
Cdd:cd07556    4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLiRRSGDLKIKTIGDEFMVVS-GLDHPAAAVAFaEDMREAVSALNQ 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 567930787 261 PQVGQLTISIG----------FLELASIDTVSSIVNQADMALYHSKNS 298
Cdd:cd07556   83 SEGNPVRVRIGihtgpvvvgvIGSRPQYDVWGALVNLASRMESQAKAG 130
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 102-271 4.44e-10

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 60.55  E-value: 4.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 102 GKVIGILLIETtKELAQTTTML------AVHI----LNIYANQLGLLHKSRLDPLTELLNRQTFDKKVIEIVsgkgfllp 171
Cdd:PRK11359 328 GAPAGTLQIKT-SSGAETSAFIervadiSQHLaalaLEQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLV-------- 398

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930787 172 rDDTNEKRRWYLaiaDIDHFKRVNDSYGHVIGDEVILLVARLLKNNFRLEDYVFRYGGEEFAVLFQTKTEAQAHIALNRL 251
Cdd:PRK11359 399 -DKAVSPVVYLI---GVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADEL 474

                        170       180
                 ....*....|....*....|....*.
gi 567930787 252 RS------NIAEYPFPqvgqLTISIG 271
Cdd:PRK11359 475 RNvvskpiMIDDKPFP----LTLSIG 496
 
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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