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Conserved domains on  [gi|90111334|ref|NP_416308|]
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diguanylate cyclase DgcP [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

sensor domain-containing diguanylate cyclase( domain architecture ID 11250429)

diguanylate cyclase containing a GAF sensor domain catalyzes the condensation of two GTP molecules to the cyclic dinucleotide di-GMP (c-di-GMP), which acts as a secondary messenger

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
174-329 2.39e-51

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: 167.81  E-value: 2.39e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334   174 SYTDSLTGLPNRRAIFENLTTLFSLARHLNHKIMIAFIDLDNFKLINDRFGHNSGDLFLIQVGERLNTLQQNGEVIGRLG 253
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111334   254 GDEFLVVSLNNENADISSLRERIQQ--QIRGEYHLGDVDLYYPGASLGIVEVDPETTDADSALHAADIAMYQEKKHKQ 329
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRllAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGR 158
GAF COG2203
GAF domain [Signal transduction mechanisms];
4-340 1.06e-13

GAF domain [Signal transduction mechanisms];


:

Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 72.15  E-value: 1.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334   4 QIIARVSQSLAKEQSLESLVRQLLEMLEMVTDMESTYLTKVDVEARLQHIMFARNSQKMYIPEnftVSWDYSLCKRAIDE 83
Cdd:COG2203 193 ALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGR---LPLGEGLAGRALRT 269
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334  84 N--CFFSD-EVPDRWGDCI--AARNLGITTFLSTPIHLpDGSFYGTLCAASSEKRQWSERAEQVLQLFAGLIAQYIQKEA 158
Cdd:COG2203 270 GepVVVNDaSTDPRFAPSLreLLLALGIRSLLCVPLLV-DGRLIGVLALYSKEPRAFTEEDLELLEALADQAAIAIERAR 348
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334 159 LVEQLREANAAL------IAQSYTDSLTGLPNRRAIFENLTTLFSLARHLNHKIMIAFIDLDNFKLINDRFGHNSGDLFL 232
Cdd:COG2203 349 LYEALEAALAALlqelalLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDLLL 428
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334 233 IQVGERLNTLQQNGEVIGRLGGDEFLVVSLNNENADISSLRERIQQQIRGEYHLGDVDLYYPGASLGIVEVDPETTDADS 312
Cdd:COG2203 429 LLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLALSALAVLAS 508
                       330       340
                ....*....|....*....|....*...
gi 90111334 313 ALHAADIAMYQEKKHKQKTPFVAHPALH 340
Cdd:COG2203 509 LLLALLLLLLLLLLLLLLGLLAALAADL 536
 
Name Accession Description Interval E-value
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
174-329 2.39e-51

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: 167.81  E-value: 2.39e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334   174 SYTDSLTGLPNRRAIFENLTTLFSLARHLNHKIMIAFIDLDNFKLINDRFGHNSGDLFLIQVGERLNTLQQNGEVIGRLG 253
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111334   254 GDEFLVVSLNNENADISSLRERIQQ--QIRGEYHLGDVDLYYPGASLGIVEVDPETTDADSALHAADIAMYQEKKHKQ 329
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRllAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGR 158
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
175-326 1.16e-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: 165.81  E-value: 1.16e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334 175 YTDSLTGLPNRRAIFENLTTLFSLARHLNHKIMIAFIDLDNFKLINDRFGHNSGDLFLIQVGERLNTLQQNGEVIGRLGG 254
Cdd:cd01949   1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111334 255 DEFLVVSLNNENADISSLRERIQQQIRGEYHLGDVDLyYPGASLGIVEVDPETTDADSALHAADIAMYQEKK 326
Cdd:cd01949  81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEI-RVTASIGIATYPEDGEDAEELLRRADEALYRAKR 151
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
90-327 3.47e-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: 3.47e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334  90 EVPDRWGDCIAARNLGITTFLSTPIHLPDGSFYGTLCAASSEKRQWSERAEQVLQLFAGLIAQYIQKEALVEQLREANAA 169
Cdd:COG2199  30 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEER 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334 170 LIAQSYTDSLTGLPNRRAIFENLTTLFSLARHLNHKIMIAFIDLDNFKLINDRFGHNSGDLFLIQVGERLNTLQQNGEVI 249
Cdd:COG2199 110 LRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLV 189
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111334 250 GRLGGDEFLVVSLNNENADISSLRERIQQQIRG-EYHLGDVDLyYPGASLGIVEVDPETTDADSALHAADIAMYQEKKH 327
Cdd:COG2199 190 ARLGGDEFAVLLPGTDLEEAEALAERLREALEQlPFELEGKEL-RVTVSIGVALYPEDGDSAEELLRRADLALYRAKRA 267
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
173-326 7.82e-47

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 156.25  E-value: 7.82e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334    173 QSYTDSLTGLPNRRAIFENLTTLFSLARHLNHKIMIAFIDLDNFKLINDRFGHNSGDLFLIQVGERLNTLQQNGEVIGRL 252
Cdd:smart00267   2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111334    253 GGDEFLVVSLNNENADISSLRERIQQQIRGEYHLGDVDLyYPGASLGIVEVDPETTDADSALHAADIAMYQEKK 326
Cdd:smart00267  82 GGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPL-YLTISIGVAAYPNPGEDAEDLLKRADTALYQAKK 154
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
173-335 6.27e-35

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: 125.14  E-value: 6.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334   173 QSYTDSLTGLPNRRAIFENLTTLFSLARHLNHKIMIAFIDLDNFKLINDRFGHNSGDLFLIQVGERLNTLQQNGEVIGRL 252
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334   253 GGDEFLVVSLNNENADISSLRERIQQQIRGEY-HLGDVDLYYPGASLGIVEVDPETTDADSALHAADIAMYQEKKHKQKT 331
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPiEVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160

                  ....
gi 90111334   332 PFVA 335
Cdd:TIGR00254 161 VVVA 164
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
164-331 1.63e-28

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 115.93  E-value: 1.63e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334  164 REANAALIAQSYTDSLTGLPNRRAIFENLTTlfSLARHLNHKIMIAFIDLDNFKLINDRFGHNSGDLFLIQVGERLNTLQ 243
Cdd:PRK10060 227 RRAQERLRILANTDSITGLPNRNAIQELIDH--AINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCL 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334  244 QNGEVIGRLGGDEFLVVSLNNENADISSLRERIQQQIRGEYHLGDVDLyYPGASLGIVEVDPETTDADSALHAADIAMYQ 323
Cdd:PRK10060 305 EEDQTLARLGGDEFLVLASHTSQAALEAMASRILTRLRLPFRIGLIEV-YTGCSIGIALAPEHGDDSESLIRSADTAMYT 383

                 ....*...
gi 90111334  324 EKKHKQKT 331
Cdd:PRK10060 384 AKEGGRGQ 391
GAF COG2203
GAF domain [Signal transduction mechanisms];
4-340 1.06e-13

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 72.15  E-value: 1.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334   4 QIIARVSQSLAKEQSLESLVRQLLEMLEMVTDMESTYLTKVDVEARLQHIMFARNSQKMYIPEnftVSWDYSLCKRAIDE 83
Cdd:COG2203 193 ALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGR---LPLGEGLAGRALRT 269
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334  84 N--CFFSD-EVPDRWGDCI--AARNLGITTFLSTPIHLpDGSFYGTLCAASSEKRQWSERAEQVLQLFAGLIAQYIQKEA 158
Cdd:COG2203 270 GepVVVNDaSTDPRFAPSLreLLLALGIRSLLCVPLLV-DGRLIGVLALYSKEPRAFTEEDLELLEALADQAAIAIERAR 348
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334 159 LVEQLREANAAL------IAQSYTDSLTGLPNRRAIFENLTTLFSLARHLNHKIMIAFIDLDNFKLINDRFGHNSGDLFL 232
Cdd:COG2203 349 LYEALEAALAALlqelalLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDLLL 428
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334 233 IQVGERLNTLQQNGEVIGRLGGDEFLVVSLNNENADISSLRERIQQQIRGEYHLGDVDLYYPGASLGIVEVDPETTDADS 312
Cdd:COG2203 429 LLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLALSALAVLAS 508
                       330       340
                ....*....|....*....|....*...
gi 90111334 313 ALHAADIAMYQEKKHKQKTPFVAHPALH 340
Cdd:COG2203 509 LLLALLLLLLLLLLLLLLGLLAALAADL 536
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
19-164 1.81e-13

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 67.02  E-value: 1.81e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334     19 LESLVRQLLEMLEMVTDMESTYLTKVDVEARLQHIMFARNSQKMYIPEnFTVSWDYSLCKRAIDEN--CFFSDEVPD-RW 95
Cdd:smart00065   2 LEELLQTILEELRQLLGADRVLIYLVDENDRGELVLVAADGLTLPTLG-IRFPLDEGLAGRVAETGrpLNIPDVEADpLF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334     96 GDCIAARNLGITTFLSTPIHLpDGSFYGTLCAASSEK-RQWSERAEQVLQLFAGLIAQYIQKEALVEQLR 164
Cdd:smart00065  81 AEDLLGRYQGVRSFLAVPLVA-DGELVGVLALHNKKSpRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
16-155 4.63e-06

GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 45.54  E-value: 4.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334    16 EQSLESLVRQLLEMLEMVTDMESTYLTKVDVEARLqhimFARNSQKMYIPENFTVSWDYSLCKRAIDEN-CFFSDEVPDR 94
Cdd:pfam13185   1 AADLEELLDAVLEAAVELGASAVGFILLVDDDGRL----AAWGGAADELSAALDDPPGEGLVGEALRTGrPVIVNDLAAD 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111334    95 WGDC-IAARNLGITTFLSTPIHLpDGSFYGTLCAASSEKRQWSERAEQVLQLFAGLIAQYIQ 155
Cdd:pfam13185  77 PAKKgLPAGHAGLRSFLSVPLVS-GGRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAIE 137
 
Name Accession Description Interval E-value
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
174-329 2.39e-51

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: 167.81  E-value: 2.39e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334   174 SYTDSLTGLPNRRAIFENLTTLFSLARHLNHKIMIAFIDLDNFKLINDRFGHNSGDLFLIQVGERLNTLQQNGEVIGRLG 253
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111334   254 GDEFLVVSLNNENADISSLRERIQQ--QIRGEYHLGDVDLYYPGASLGIVEVDPETTDADSALHAADIAMYQEKKHKQ 329
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRllAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGR 158
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
175-326 1.16e-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: 165.81  E-value: 1.16e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334 175 YTDSLTGLPNRRAIFENLTTLFSLARHLNHKIMIAFIDLDNFKLINDRFGHNSGDLFLIQVGERLNTLQQNGEVIGRLGG 254
Cdd:cd01949   1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111334 255 DEFLVVSLNNENADISSLRERIQQQIRGEYHLGDVDLyYPGASLGIVEVDPETTDADSALHAADIAMYQEKK 326
Cdd:cd01949  81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEI-RVTASIGIATYPEDGEDAEELLRRADEALYRAKR 151
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
90-327 3.47e-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: 3.47e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334  90 EVPDRWGDCIAARNLGITTFLSTPIHLPDGSFYGTLCAASSEKRQWSERAEQVLQLFAGLIAQYIQKEALVEQLREANAA 169
Cdd:COG2199  30 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEER 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334 170 LIAQSYTDSLTGLPNRRAIFENLTTLFSLARHLNHKIMIAFIDLDNFKLINDRFGHNSGDLFLIQVGERLNTLQQNGEVI 249
Cdd:COG2199 110 LRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLV 189
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111334 250 GRLGGDEFLVVSLNNENADISSLRERIQQQIRG-EYHLGDVDLyYPGASLGIVEVDPETTDADSALHAADIAMYQEKKH 327
Cdd:COG2199 190 ARLGGDEFAVLLPGTDLEEAEALAERLREALEQlPFELEGKEL-RVTVSIGVALYPEDGDSAEELLRRADLALYRAKRA 267
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
173-326 7.82e-47

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 156.25  E-value: 7.82e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334    173 QSYTDSLTGLPNRRAIFENLTTLFSLARHLNHKIMIAFIDLDNFKLINDRFGHNSGDLFLIQVGERLNTLQQNGEVIGRL 252
Cdd:smart00267   2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111334    253 GGDEFLVVSLNNENADISSLRERIQQQIRGEYHLGDVDLyYPGASLGIVEVDPETTDADSALHAADIAMYQEKK 326
Cdd:smart00267  82 GGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPL-YLTISIGVAAYPNPGEDAEDLLKRADTALYQAKK 154
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
133-327 5.91e-44

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: 160.33  E-value: 5.91e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334 133 RQWSERAEQVLQLFAGLIAQYIQKEALVEQLREANAALIAQSYTDSLTGLPNRRAIFENLTTLFSLARHLNHKIMIAFID 212
Cdd:COG5001 210 LRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFID 289
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334 213 LDNFKLINDRFGHNSGDLFLIQVGERLNTLQQNGEVIGRLGGDEFLVVSLNNEN-ADISSLRERIQQQIRGEYHLGDVDL 291
Cdd:COG5001 290 LDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDpEDAEAVAERILAALAEPFELDGHEL 369
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 90111334 292 yYPGASLGIVEVDPETTDADSALHAADIAMYQEKKH 327
Cdd:COG5001 370 -YVSASIGIALYPDDGADAEELLRNADLAMYRAKAA 404
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
173-335 6.27e-35

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: 125.14  E-value: 6.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334   173 QSYTDSLTGLPNRRAIFENLTTLFSLARHLNHKIMIAFIDLDNFKLINDRFGHNSGDLFLIQVGERLNTLQQNGEVIGRL 252
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334   253 GGDEFLVVSLNNENADISSLRERIQQQIRGEY-HLGDVDLYYPGASLGIVEVDPETTDADSALHAADIAMYQEKKHKQKT 331
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPiEVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160

                  ....
gi 90111334   332 PFVA 335
Cdd:TIGR00254 161 VVVA 164
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
164-331 1.63e-28

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 115.93  E-value: 1.63e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334  164 REANAALIAQSYTDSLTGLPNRRAIFENLTTlfSLARHLNHKIMIAFIDLDNFKLINDRFGHNSGDLFLIQVGERLNTLQ 243
Cdd:PRK10060 227 RRAQERLRILANTDSITGLPNRNAIQELIDH--AINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCL 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334  244 QNGEVIGRLGGDEFLVVSLNNENADISSLRERIQQQIRGEYHLGDVDLyYPGASLGIVEVDPETTDADSALHAADIAMYQ 323
Cdd:PRK10060 305 EEDQTLARLGGDEFLVLASHTSQAALEAMASRILTRLRLPFRIGLIEV-YTGCSIGIALAPEHGDDSESLIRSADTAMYT 383

                 ....*...
gi 90111334  324 EKKHKQKT 331
Cdd:PRK10060 384 AKEGGRGQ 391
pleD PRK09581
response regulator PleD; Reviewed
171-326 4.48e-20

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 90.73  E-value: 4.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334  171 IAQSYTDSLTGLPNRRAIFENLTTLFSLARHLNHKIMIAFIDLDNFKLINDRFGHNSGDLFLIQVGERLNTLQQNGEVIG 250
Cdd:PRK09581 289 IEMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIA 368
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111334  251 RLGGDEFLVVSLNNENADISSLRERIQQQIRGE-YHLGDVDLYYP-GASLGIVEVDPETTDADSALHAADIAMYQEKK 326
Cdd:PRK09581 369 RYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEpFIISDGKERLNvTVSIGVAELRPSGDTIEALIKRADKALYEAKN 446
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
165-325 7.47e-20

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 90.89  E-value: 7.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334   165 EANAALIAQSYT---DSLTGLPNRrAIFEN-LTTLFSLARHLNHKIMIAFIDLDNFKLINDRFGHNSGDLFLIQVGERLN 240
Cdd:PRK09776  653 ESRKMLRQLSYSashDALTHLANR-ASFEKqLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLML 731
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334   241 TLQQNGEVIGRLGGDEF--LVVSLNNENA-DISSlreRIQQQIRGEYHLGDVDLYYPGASLGIVEVDPETTDADSALHAA 317
Cdd:PRK09776  732 SMLRSSDVLARLGGDEFglLLPDCNVESArFIAT---RIISAINDYHFPWEGRVYRVGASAGITLIDANNHQASEVMSQA 808

                  ....*...
gi 90111334   318 DIAMYQEK 325
Cdd:PRK09776  809 DIACYAAK 816
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
169-325 1.47e-19

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 89.30  E-value: 1.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334  169 ALIAQSYTDSLTGLPNRRAIFENLTTLFSLARHLNHKIMIAFIDLDNFKLINDRFGHNSGDLFLIQVGERLNTLQQNGEV 248
Cdd:PRK15426 393 SLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDV 472
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334  249 IGRLGGDEFLVVSLNNENADISSLRERIQQQIRGEYHL--GDVDLYYpGASLGIVEVDPETT-DADSALHAADIAMYQEK 325
Cdd:PRK15426 473 AGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILvaKSTTIRI-SASLGVSSAEEDGDyDFEQLQSLADRRLYLAK 551
PRK09894 PRK09894
diguanylate cyclase; Provisional
168-325 2.33e-18

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 83.96  E-value: 2.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334  168 AALIAQSYTDSLTGLPNRRAIFENLTTlfSLARHLNHKIMIAFIDLDNFKLINDRFGHNSGDLFLIQVGERLNTLQQNGE 247
Cdd:PRK09894 123 YLLTIRSNMDVLTGLPGRRVLDESFDH--QLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYE 200
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111334  248 VIGRLGGDEFLVVSLNNENADISSLRERIQQQI-RGEYHLGDVDLYYPgASLGIVEVDPETTDADSaLHAADIAMYQEK 325
Cdd:PRK09894 201 TVYRYGGEEFIICLKAATDEEACRAGERIRQLIaNHAITHSDGRINIT-ATFGVSRAFPEETLDVV-IGRADRAMYEGK 277
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
111-326 2.04e-17

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 83.28  E-value: 2.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334  111 STPIHLPDGSFYGTLCAASSEKRQWSERAEQVLQLFAGLIAQYIQKEA---LVEQLREanaaliaqsyTDSLTGLPNRRA 187
Cdd:PRK11359 320 SATIRQRDGAPAGTLQIKTSSGAETSAFIERVADISQHLAALALEQEKsrqHIEQLIQ----------FDPLTGLPNRNN 389
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334  188 IFENLTTLFSLArhlnHKIMIAFIDLDNFKLINDRFGHNSGDLFLIQVGERLNTLQQNGEVIGRLGGDEFLVVSLNNENA 267
Cdd:PRK11359 390 LHNYLDDLVDKA----VSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVS 465
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 90111334  268 DISSLRERIqQQIRGEYHLGDVDLYYPGASLGIVEvdPETTDADSALHAADIAMYQEKK 326
Cdd:PRK11359 466 NITQIADEL-RNVVSKPIMIDDKPFPLTLSIGISY--DVGKNRDYLLSTAHNAMDYIRK 521
adrA PRK10245
diguanylate cyclase AdrA; Provisional
162-326 9.41e-17

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 80.26  E-value: 9.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334  162 QLREANAALIAQSYTDSLTGLPNRRAIFENLTTLFSLARHLNHKIMIAFIDLDNFKLINDRFGHNSGDLFLIQVGERLNT 241
Cdd:PRK10245 193 KLAEHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQI 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334  242 LQQNGEVIGRLGGDEFLVV----SLNNENADISSLRERIQQqirgeyhlgdvdLYYPGA-------SLGIVEVDPETTDA 310
Cdd:PRK10245 273 TLRGSDVIGRFGGDEFAVImsgtPAESAITAMSRVHEGLNT------------LRLPNApqvtlriSVGVAPLNPQMSHY 340
                        170
                 ....*....|....*.
gi 90111334  311 DSALHAADIAMYQEKK 326
Cdd:PRK10245 341 REWLKSADLALYKAKN 356
PRK09966 PRK09966
diguanylate cyclase DgcN;
162-328 1.31e-14

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 74.27  E-value: 1.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334  162 QLREANAALIAQSYTDSLTGLPNRRAIFENLTTLF--SLARHLNhkiMIAFIDLDNFKLINDRFGHNSGDLFLIQVGERL 239
Cdd:PRK09966 236 RLQAKNAQLLRTALHDPLTGLANRAAFRSGINTLMnnSDARKTS---ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRL 312
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334  240 NTLQQNGEVIGRLGGDEFLVVSLN-NENADISSLRERIQQQIRGEYHLGDVDLYYPGASLGIVeVDPETTDADSALHAAD 318
Cdd:PRK09966 313 AEFGGLRHKAYRLGGDEFAMVLYDvQSESEVQQICSALTQIFNLPFDLHNGHQTTMTLSIGYA-MTIEHASAEKLQELAD 391
                        170
                 ....*....|
gi 90111334  319 IAMYQEKKHK 328
Cdd:PRK09966 392 HNMYQAKHQR 401
GAF COG2203
GAF domain [Signal transduction mechanisms];
4-340 1.06e-13

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 72.15  E-value: 1.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334   4 QIIARVSQSLAKEQSLESLVRQLLEMLEMVTDMESTYLTKVDVEARLQHIMFARNSQKMYIPEnftVSWDYSLCKRAIDE 83
Cdd:COG2203 193 ALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGR---LPLGEGLAGRALRT 269
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334  84 N--CFFSD-EVPDRWGDCI--AARNLGITTFLSTPIHLpDGSFYGTLCAASSEKRQWSERAEQVLQLFAGLIAQYIQKEA 158
Cdd:COG2203 270 GepVVVNDaSTDPRFAPSLreLLLALGIRSLLCVPLLV-DGRLIGVLALYSKEPRAFTEEDLELLEALADQAAIAIERAR 348
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334 159 LVEQLREANAAL------IAQSYTDSLTGLPNRRAIFENLTTLFSLARHLNHKIMIAFIDLDNFKLINDRFGHNSGDLFL 232
Cdd:COG2203 349 LYEALEAALAALlqelalLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDLLL 428
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334 233 IQVGERLNTLQQNGEVIGRLGGDEFLVVSLNNENADISSLRERIQQQIRGEYHLGDVDLYYPGASLGIVEVDPETTDADS 312
Cdd:COG2203 429 LLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLALSALAVLAS 508
                       330       340
                ....*....|....*....|....*...
gi 90111334 313 ALHAADIAMYQEKKHKQKTPFVAHPALH 340
Cdd:COG2203 509 LLLALLLLLLLLLLLLLLGLLAALAADL 536
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
19-164 1.81e-13

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 67.02  E-value: 1.81e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334     19 LESLVRQLLEMLEMVTDMESTYLTKVDVEARLQHIMFARNSQKMYIPEnFTVSWDYSLCKRAIDEN--CFFSDEVPD-RW 95
Cdd:smart00065   2 LEELLQTILEELRQLLGADRVLIYLVDENDRGELVLVAADGLTLPTLG-IRFPLDEGLAGRVAETGrpLNIPDVEADpLF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334     96 GDCIAARNLGITTFLSTPIHLpDGSFYGTLCAASSEK-RQWSERAEQVLQLFAGLIAQYIQKEALVEQLR 164
Cdd:smart00065  81 AEDLLGRYQGVRSFLAVPLVA-DGELVGVLALHNKKSpRPFTEEDEELLQALANQLAIALANAQLYEELR 149
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
208-261 1.16e-06

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: 47.35  E-value: 1.16e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 90111334 208 IAFIDLDNFKLINDRFGHNSGDLFLIQVGERLNTL-QQNGEVIGRLGGDEFLVVS 261
Cdd:cd07556   4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLiRRSGDLKIKTIGDEFMVVS 58
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
16-155 4.63e-06

GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 45.54  E-value: 4.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334    16 EQSLESLVRQLLEMLEMVTDMESTYLTKVDVEARLqhimFARNSQKMYIPENFTVSWDYSLCKRAIDEN-CFFSDEVPDR 94
Cdd:pfam13185   1 AADLEELLDAVLEAAVELGASAVGFILLVDDDGRL----AAWGGAADELSAALDDPPGEGLVGEALRTGrPVIVNDLAAD 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111334    95 WGDC-IAARNLGITTFLSTPIHLpDGSFYGTLCAASSEKRQWSERAEQVLQLFAGLIAQYIQ 155
Cdd:pfam13185  77 PAKKgLPAGHAGLRSFLSVPLVS-GGRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAIE 137
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
101-154 7.59e-05

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 42.08  E-value: 7.59e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 90111334   101 ARNLGITTFLSTPIHLpDGSFYGTLCAASSeKRQWSERAEQVLQLFAGLIAQYI 154
Cdd:pfam01590  82 LRNFGIRSLLAVPIID-DGELLGVLVLHHP-RPPFTEEELELLEVLADQVAIAL 133
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
247-323 1.33e-04

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: 42.20  E-value: 1.33e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111334 247 EVIGRLGGDEFLVVSLNNENADISSLRERIQQQIRGEYHLgdvdlyYPGASLGIVEvdpettdaDSALHAADiAMYQ 323
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAELPSL------RVTVSIGVAG--------DSLLKRAD-ALYQ 177
PRK11059 PRK11059
regulatory protein CsrD; Provisional
127-260 1.79e-03

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 40.23  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111334  127 AASSEKRQWSERAEQVL-QLFAGLiaQYIQKE-ALVEQLREANAALiaqsytDSLTGLPNrRAIFEN-LTTLfslarhLN 203
Cdd:PRK11059 187 AVAGSGYEWPRTASRALdHLLSEL--QDAREErSRFDTFIRSNAFQ------DAKTGLGN-RLFFDNqLATL------LE 251
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111334  204 HKIMIAF------IDLDNFKLINDRFGHNSGDLFLIQVGERLNTL--QQNGEVIGRLGGDEFLVV 260
Cdd:PRK11059 252 DQEMVGAhgvvmlIRLPDFDLLQEEWGESQVEELLFELINLLSTFvmRYPGALLARYSRSDFAVL 316
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
109-157 8.44e-03

FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];


Pssm-ID: 442823 [Multi-domain]  Cd Length: 338  Bit Score: 37.52  E-value: 8.44e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 90111334 109 FLSTPIHLpDGSFYGTLCAASSEKRQWSERAEQVLQLFAGLIAQYIQKE 157
Cdd:COG3604  76 FLGVPLRV-GGEVLGVLTLDSRRPGAFSEEDLRLLETLASLAAVAILGE 123
 
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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