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Conserved domains on  [gi|494016764|ref|WP_006959103|]
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MULTISPECIES: GGDEF domain-containing protein [Vibrio]

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 ...
 67-332 3.27e-49

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: 165.92  E-value: 3.27e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764  67 YRPWHSALLISGLTALLIYSMAVADGYSVLVFWAFCFPALYHIFFNRYIASAITFAFYLVAISILASYPPLINSTPYTLI 146
Cdd:COG2199    4 LLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLEL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 147 NFTIPYFLIWAISFVHEDMQTKIKGKLSDAALLDPLTGAKNRLALEADTSDNPDLVHNH----YLVHFDLDHFKRVNDNY 222
Cdd:COG2199   84 LLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREgrplALLLIDLDHFKRINDTY 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 223 GHAAGDTVLKMVAKIVGQQVR-QDAFYRVGGEEFCTIFSAPDKESAFSIANALREKLSQTPISIGDQTLQVTLSGGLCel 301
Cdd:COG2199  164 GHAAGDEVLKEVARRLRASLReSDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVA-- 241

                        250       260       270
                 ....*....|....*....|....*....|.
gi 494016764 302 VVEEGTVRIDETMKITDAALYQAKAQGRNQV 332
Cdd:COG2199  242 LYPEDGDSAEELLRRADLALYRAKRAGRNRV 272
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 67-332 3.27e-49

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: 165.92  E-value: 3.27e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764  67 YRPWHSALLISGLTALLIYSMAVADGYSVLVFWAFCFPALYHIFFNRYIASAITFAFYLVAISILASYPPLINSTPYTLI 146
Cdd:COG2199    4 LLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLEL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 147 NFTIPYFLIWAISFVHEDMQTKIKGKLSDAALLDPLTGAKNRLALEADTSDNPDLVHNH----YLVHFDLDHFKRVNDNY 222
Cdd:COG2199   84 LLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREgrplALLLIDLDHFKRINDTY 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 223 GHAAGDTVLKMVAKIVGQQVR-QDAFYRVGGEEFCTIFSAPDKESAFSIANALREKLSQTPISIGDQTLQVTLSGGLCel 301
Cdd:COG2199  164 GHAAGDEVLKEVARRLRASLReSDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVA-- 241

                        250       260       270
                 ....*....|....*....|....*....|.
gi 494016764 302 VVEEGTVRIDETMKITDAALYQAKAQGRNQV 332
Cdd:COG2199  242 LYPEDGDSAEELLRRADLALYRAKRAGRNRV 272
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 180-333 1.81e-45

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: 152.33  E-value: 1.81e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 180 DPLTGAKNRLALEADTSDNPDLVHNH----YLVHFDLDHFKRVNDNYGHAAGDTVLKMVAKIVGQQVRQ-DAFYRVGGEE 254
Cdd:cd01949    3 DPLTGLPNRRAFEERLERLLARARRSgrplALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLREsDLVARLGGDE 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494016764 255 FCTIFSAPDKESAFSIANALREKLSQTPIsIGDQTLQVTLSGGLCELvvEEGTVRIDETMKITDAALYQAKAQGRNQVI 333
Cdd:cd01949   83 FAILLPGTDLEEAEALAERLREAIEEPFF-IDGQEIRVTASIGIATY--PEDGEDAEELLRRADEALYRAKRSGRNRVV 158
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 177-332 1.37e-37

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 131.99  E-value: 1.37e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764   177 ALLDPLTGAKNRLA----LEADTSDNPDLVHNHYLVHFDLDHFKRVNDNYGHAAGDTVLKMVAKIVGQQVRQDAF-YRVG 251
Cdd:smart00267   3 AFRDPLTGLPNRRYfeeeLEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLlARLG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764   252 GEEFCTIFSAPDKESAFSIANALREKLSQtPISIGDQTLQVTLSGGLCelVVEEGTVRIDETMKITDAALYQAKAQGRNQ 331
Cdd:smart00267  83 GDEFALLLPETSLEEAIALAERILQQLRE-PIIIHGIPLYLTISIGVA--AYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159


                   .
gi 494016764   332 V 332
Cdd:smart00267 160 V 160
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 177-331 1.88e-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: 126.21  E-value: 1.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764  177 ALLDPLTGAKNRLALE--ADTSDNPDLVHNH--YLVHFDLDHFKRVNDNYGHAAGDTVLKMVAKIVGQQVRQ-DAFYRVG 251
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEeqLEQELQRALREGSpvAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRsDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764  252 GEEFCTIFSAPDKESAFSIANALREKLSQ--TPISIGDQTLQVTLSGGLCelVVEEGTVRIDETMKITDAALYQAKAQGR 329
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKlkIPHTVSGLPLYVTISIGIA--AYPNDGEDPEDLLKRADTALYQAKQAGR 158


                  ..
gi 494016764  330 NQ 331
Cdd:pfam00990 159 NR 160
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
173-332 1.27e-34

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 127.02  E-value: 1.27e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 173 LSDAALLDPLTGAKNRLAL------EADTSD--NPDLVhnhyLVHFDLDHFKRVNDNYGHAAGDTVLKMVAKIVGQQVR- 243
Cdd:NF038266  90 LREASTRDPLTGLPNRRLLmerlreEVERARrsGRPFT----LAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELRe 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 244 QDAFYRVGGEEFCTIFSAPDKESAFSIANALREKLSQTPISIGDQTLQVTLSGGLCElvVEEGTVRIDETMKITDAALYQ 323
Cdd:NF038266 166 YDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAE--HRPPEEGLSATLSRADQALYQ 243


                 ....*....
gi 494016764 324 AKAQGRNQV 332
Cdd:NF038266 244 AKRAGRDRV 252
PRK09894 PRK09894
diguanylate cyclase; Provisional
 179-335 6.53e-34

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 126.33  E-value: 6.53e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 179 LDPLTGAKNRLALEADTSDNpdLV----HNHYLVHFDLDHFKRVNDNYGHAAGDTVLKMVAKIVGQQVRQ-DAFYRVGGE 253
Cdd:PRK09894 131 MDVLTGLPGRRVLDESFDHQ--LRnrepQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDyETVYRYGGE 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 254 EFCTIFSAPDKESAFSIANALREKLSQTPISIGDQTLQVTLSGGLCELVVEEgTVriDETMKITDAALYQAKAQGRNQVI 333
Cdd:PRK09894 209 EFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRAFPEE-TL--DVVIGRADRAMYEGKQTGRNRVM 285


                 ..
gi 494016764 334 AI 335
Cdd:PRK09894 286 FI 287
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 177-332 3.06e-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: 118.21  E-value: 3.06e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764  177 ALLDPLTGAKNRLALEADTSDNPDLV--HNH--YLVHFDLDHFKRVNDNYGHAAGDTVLKMVAKIVGQQVR-QDAFYRVG 251
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLDSELKRArrFQRsfSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRgSDVVGRYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764  252 GEEFCTIFSAPDKESAFSIANALREKLSQTPISI-GDQTLQVTLSGGLCELvvEEGTVRIDETMKITDAALYQAKAQGRN 330
Cdd:TIGR00254  82 GEEFVVILPGTPLEDALSKAERLRDAINSKPIEVaGSETLTVTVSIGVACY--PGHGLTLEELLKRADEALYQAKKAGRN 159


                  ..
gi 494016764  331 QV 332
Cdd:TIGR00254 160 RV 161
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 67-332 3.27e-49

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: 165.92  E-value: 3.27e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764  67 YRPWHSALLISGLTALLIYSMAVADGYSVLVFWAFCFPALYHIFFNRYIASAITFAFYLVAISILASYPPLINSTPYTLI 146
Cdd:COG2199    4 LLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLEL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 147 NFTIPYFLIWAISFVHEDMQTKIKGKLSDAALLDPLTGAKNRLALEADTSDNPDLVHNH----YLVHFDLDHFKRVNDNY 222
Cdd:COG2199   84 LLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREgrplALLLIDLDHFKRINDTY 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 223 GHAAGDTVLKMVAKIVGQQVR-QDAFYRVGGEEFCTIFSAPDKESAFSIANALREKLSQTPISIGDQTLQVTLSGGLCel 301
Cdd:COG2199  164 GHAAGDEVLKEVARRLRASLReSDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVA-- 241

                        250       260       270
                 ....*....|....*....|....*....|.
gi 494016764 302 VVEEGTVRIDETMKITDAALYQAKAQGRNQV 332
Cdd:COG2199  242 LYPEDGDSAEELLRRADLALYRAKRAGRNRV 272
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 180-333 1.81e-45

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: 152.33  E-value: 1.81e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 180 DPLTGAKNRLALEADTSDNPDLVHNH----YLVHFDLDHFKRVNDNYGHAAGDTVLKMVAKIVGQQVRQ-DAFYRVGGEE 254
Cdd:cd01949    3 DPLTGLPNRRAFEERLERLLARARRSgrplALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLREsDLVARLGGDE 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494016764 255 FCTIFSAPDKESAFSIANALREKLSQTPIsIGDQTLQVTLSGGLCELvvEEGTVRIDETMKITDAALYQAKAQGRNQVI 333
Cdd:cd01949   83 FAILLPGTDLEEAEALAERLREAIEEPFF-IDGQEIRVTASIGIATY--PEDGEDAEELLRRADEALYRAKRSGRNRVV 158
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 177-332 1.37e-37

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 131.99  E-value: 1.37e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764   177 ALLDPLTGAKNRLA----LEADTSDNPDLVHNHYLVHFDLDHFKRVNDNYGHAAGDTVLKMVAKIVGQQVRQDAF-YRVG 251
Cdd:smart00267   3 AFRDPLTGLPNRRYfeeeLEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLlARLG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764   252 GEEFCTIFSAPDKESAFSIANALREKLSQtPISIGDQTLQVTLSGGLCelVVEEGTVRIDETMKITDAALYQAKAQGRNQ 331
Cdd:smart00267  83 GDEFALLLPETSLEEAIALAERILQQLRE-PIIIHGIPLYLTISIGVA--AYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159


                   .
gi 494016764   332 V 332
Cdd:smart00267 160 V 160
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 177-331 1.88e-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: 126.21  E-value: 1.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764  177 ALLDPLTGAKNRLALE--ADTSDNPDLVHNH--YLVHFDLDHFKRVNDNYGHAAGDTVLKMVAKIVGQQVRQ-DAFYRVG 251
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEeqLEQELQRALREGSpvAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRsDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764  252 GEEFCTIFSAPDKESAFSIANALREKLSQ--TPISIGDQTLQVTLSGGLCelVVEEGTVRIDETMKITDAALYQAKAQGR 329
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKlkIPHTVSGLPLYVTISIGIA--AYPNDGEDPEDLLKRADTALYQAKQAGR 158


                  ..
gi 494016764  330 NQ 331
Cdd:pfam00990 159 NR 160
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
173-332 1.27e-34

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 127.02  E-value: 1.27e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 173 LSDAALLDPLTGAKNRLAL------EADTSD--NPDLVhnhyLVHFDLDHFKRVNDNYGHAAGDTVLKMVAKIVGQQVR- 243
Cdd:NF038266  90 LREASTRDPLTGLPNRRLLmerlreEVERARrsGRPFT----LAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELRe 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 244 QDAFYRVGGEEFCTIFSAPDKESAFSIANALREKLSQTPISIGDQTLQVTLSGGLCElvVEEGTVRIDETMKITDAALYQ 323
Cdd:NF038266 166 YDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAE--HRPPEEGLSATLSRADQALYQ 243


                 ....*....
gi 494016764 324 AKAQGRNQV 332
Cdd:NF038266 244 AKRAGRDRV 252
PRK09894 PRK09894
diguanylate cyclase; Provisional
 179-335 6.53e-34

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 126.33  E-value: 6.53e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 179 LDPLTGAKNRLALEADTSDNpdLV----HNHYLVHFDLDHFKRVNDNYGHAAGDTVLKMVAKIVGQQVRQ-DAFYRVGGE 253
Cdd:PRK09894 131 MDVLTGLPGRRVLDESFDHQ--LRnrepQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDyETVYRYGGE 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 254 EFCTIFSAPDKESAFSIANALREKLSQTPISIGDQTLQVTLSGGLCELVVEEgTVriDETMKITDAALYQAKAQGRNQVI 333
Cdd:PRK09894 209 EFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRAFPEE-TL--DVVIGRADRAMYEGKQTGRNRVM 285


                 ..
gi 494016764 334 AI 335
Cdd:PRK09894 286 FI 287
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 177-332 3.06e-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: 118.21  E-value: 3.06e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764  177 ALLDPLTGAKNRLALEADTSDNPDLV--HNH--YLVHFDLDHFKRVNDNYGHAAGDTVLKMVAKIVGQQVR-QDAFYRVG 251
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLDSELKRArrFQRsfSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRgSDVVGRYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764  252 GEEFCTIFSAPDKESAFSIANALREKLSQTPISI-GDQTLQVTLSGGLCELvvEEGTVRIDETMKITDAALYQAKAQGRN 330
Cdd:TIGR00254  82 GEEFVVILPGTPLEDALSKAERLRDAINSKPIEVaGSETLTVTVSIGVACY--PGHGLTLEELLKRADEALYQAKKAGRN 159


                  ..
gi 494016764  331 QV 332
Cdd:TIGR00254 160 RV 161
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 172-332 1.76e-31

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: 124.50  E-value: 1.76e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 172 KLSDAALLDPLTGAKNRLALEA------DTSDNPDlvHNHYLVHFDLDHFKRVNDNYGHAAGDTVLKMVAKIVGQQVR-Q 244
Cdd:COG5001  246 RLRHLAYHDPLTGLPNRRLFLDrleqalARARRSG--RRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLReG 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 245 DAFYRVGGEEFCTIFS-APDKESAFSIANALREKLSQtPISIGDQTLQVTLSGGLCeLVVEEGTvRIDETMKITDAALYQ 323
Cdd:COG5001  324 DTVARLGGDEFAVLLPdLDDPEDAEAVAERILAALAE-PFELDGHELYVSASIGIA-LYPDDGA-DAEELLRNADLAMYR 400


                 ....*....
gi 494016764 324 AKAQGRNQV 332
Cdd:COG5001  401 AKAAGRNRY 409
pleD PRK09581
response regulator PleD; Reviewed
 177-334 2.05e-31

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 122.70  E-value: 2.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 177 ALLDPLTGAKNR---------LALEADTSDNPdlvhnHYLVHFDLDHFKRVNDNYGHAAGDTVLKMVAKIVGQQVR-QDA 246
Cdd:PRK09581 292 AVTDGLTGLHNRryfdmhlknLIERANERGKP-----LSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRgTDL 366

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 247 FYRVGGEEFCTIFSAPDKESAFSIANALREKLSQTP--ISIGDQTLQVTLSGGLCELVVEEGTvrIDETMKITDAALYQA 324
Cdd:PRK09581 367 IARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPfiISDGKERLNVTVSIGVAELRPSGDT--IEALIKRADKALYEA 444

                        170
                 ....*....|
gi 494016764 325 KAQGRNQVIA 334
Cdd:PRK09581 445 KNTGRNRVVA 454
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
180-334 3.66e-28

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 114.73  E-value: 3.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 180 DPLTGAKNRLALEADTSDNPDLVHNH----YLVHFDLDHFKRVNDNYGHAAGDTVLKMVAKIVGQQVR-QDAFYRVGGEE 254
Cdd:PRK15426 401 DPLTRLYNRGALFEKARALAKRCQRDqqpfSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRaQDVAGRVGGEE 480

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 255 FCTIFSAPDKESAFSIANALREKLSQTPISIG-DQTLQVTLSGGLCElVVEEGTVRIDETMKITDAALYQAKAQGRNQVI 333
Cdd:PRK15426 481 FCVVLPGASLAEAAQVAERIRLRINEKEILVAkSTTIRISASLGVSS-AEEDGDYDFEQLQSLADRRLYLAKQAGRNRVC 559


                 .
gi 494016764 334 A 334
Cdd:PRK15426 560 A 560
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 172-332 1.47e-17

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 83.57  E-value: 1.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764  172 KLSDAALLDPLTGAKNRLALE----ADTSDNPDLVHNHYLVHFDLDHFKRVNDNYGHAAGDTVLKMVAKIVGQQVR-QDA 246
Cdd:PRK09776  660 QLSYSASHDALTHLANRASFEkqlrRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRsSDV 739

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764  247 FYRVGGEEF------CTIFSApdKESAFSIANALRE-------KLSQTPISIGdqtlqVTLsgglcelvVEEGTVRIDET 313
Cdd:PRK09776  740 LARLGGDEFglllpdCNVESA--RFIATRIISAINDyhfpwegRVYRVGASAG-----ITL--------IDANNHQASEV 804

                         170
                  ....*....|....*....
gi 494016764  314 MKITDAALYQAKAQGRNQV 332
Cdd:PRK09776  805 MSQADIACYAAKNAGRGRV 823
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 131-331 1.75e-16

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 79.49  E-value: 1.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 131 LASYPPLINSTPYTLInFTIPYFLIWAISFVHEDMQTKI-----KGKLSDAALLDPLTGAKNRLALEADTSDNPDLVHNH 205
Cdd:PRK10245 155 LTGITVSFNSAPLEWW-LSLPVIVIYPLLFAWVSYQTATklaehKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRH 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 206 Y----LVHFDLDHFKRVNDNYGHAAGDTVLKMVAKIVGQQVR-QDAFYRVGGEEFCTIFSAPDKESAFSIANALREKLSQ 280
Cdd:PRK10245 234 HrdatLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRgSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNT 313

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 494016764 281 TPISIGDQTLqVTLSGGLCELVVEEGTVRidETMKITDAALYQAKAQGRNQ 331
Cdd:PRK10245 314 LRLPNAPQVT-LRISVGVAPLNPQMSHYR--EWLKSADLALYKAKNAGRNR 361
PRK09966 PRK09966
diguanylate cyclase DgcN;
163-327 4.64e-14

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 72.35  E-value: 4.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 163 EDMQTKIKGK---LSDAALLDPLTGAKNRLALEADTS---DNPDLVHNHYLVHFDLDHFKRVNDNYGHAAGDTVLKMVAK 236
Cdd:PRK09966 231 EEWQLRLQAKnaqLLRTALHDPLTGLANRAAFRSGINtlmNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAK 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 237 IVGQ--QVRQDAfYRVGGEEFCTIFSAPDKESAFS-IANALREKLSQtPISIGD-QTLQVTLSGGLCeLVVEEGTVriDE 312
Cdd:PRK09966 311 RLAEfgGLRHKA-YRLGGDEFAMVLYDVQSESEVQqICSALTQIFNL-PFDLHNgHQTTMTLSIGYA-MTIEHASA--EK 385

                        170
                 ....*....|....*
gi 494016764 313 TMKITDAALYQAKAQ 327
Cdd:PRK09966 386 LQELADHNMYQAKHQ 400
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 180-298 1.23e-13

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 71.72  E-value: 1.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 180 DPLTGAKNRLALEA--DTSDNPDLVHNHYLVhfDLDHFKRVNDNYGHAAGDTVLKMVAKIVGQQVRQDAFY-RVGGEEFC 256
Cdd:PRK11359 379 DPLTGLPNRNNLHNylDDLVDKAVSPVVYLI--GVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLcRIEGTQFV 456

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 494016764 257 TIFSAPDKESAFSIANALREKLSQtPISIGDQTLQVTLSGGL 298
Cdd:PRK11359 457 LVSLENDVSNITQIADELRNVVSK-PIMIDDKPFPLTLSIGI 497
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
172-331 1.52e-13

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 71.25  E-value: 1.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 172 KLSDAALLDPLTGAKNRLAL-----EADTSDNPDLVHnhyLVHFDLDHFKRVNDNYGHAAGDTVLKMVAKIVGQQVRQDA 246
Cdd:PRK10060 232 RLRILANTDSITGLPNRNAIqelidHAINAADNNQVG---IVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQ 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 247 -FYRVGGEEFCTIFSAPDKESAFSIANALREKLsQTPISIGDQTLQVTLSGGLCeLVVEEGTVRiDETMKITDAALYQAK 325
Cdd:PRK10060 309 tLARLGGDEFLVLASHTSQAALEAMASRILTRL-RLPFRIGLIEVYTGCSIGIA-LAPEHGDDS-ESLIRSADTAMYTAK 385


                 ....*.
gi 494016764 326 AQGRNQ 331
Cdd:PRK10060 386 EGGRGQ 391
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 211-332 1.50e-08

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: 52.74  E-value: 1.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 211 DLDHFKRVNDNYGHAAGDTVLKMVAKIVGQQVR--QDAFYRVGGEEFCTIFSAPDKESAFSIANALREKLSQTPISIG-D 287
Cdd:cd07556    8 DIVGFTSLADALGPDEGDELLNELAGRFDSLIRrsGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSALNQSEGnP 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 494016764 288 QTLQVTLSGGLCELVVEEGTVRID---ETMKITDAALYQAKAqgrNQV 332
Cdd:cd07556   88 VRVRIGIHTGPVVVGVIGSRPQYDvwgALVNLASRMESQAKA---GQV 132
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 245-325 1.95e-06

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: 47.60  E-value: 1.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494016764 245 DAFYRVGGEEFCTIFSAPDKESAFSIANALREKLSQTPisigdqTLQVTLSGGLCElvveegtvriDETMKITDaALYQA 324
Cdd:COG3706  116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAELP------SLRVTVSIGVAG----------DSLLKRAD-ALYQA 178


                 .
gi 494016764 325 K 325
Cdd:COG3706  179 R 179
 
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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