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Conserved domains on  [gi|1024905951|ref|WP_063540052|]
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diguanylate cyclase [Stutzerimonas frequens]

Protein Classification

sensor domain-containing diguanylate cyclase( domain architecture ID 13413304)

sensor domain-containing diguanylate cyclase (GGDEF) with a GAF family sensor domain

CATH:  3.30.450.40|3.30.70.1230
EC:  2.7.7.65
Gene Ontology:  GO:0005525|GO:0005886|GO:0005515|GO:0046872|GO:0052621|GO:0007165
PubMed:  16166544|9433123
SCOP:  4001852|4001316

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 227-381 1.51e-55

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: 180.06  E-value: 1.51e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 227 RDPLTGVFSRGSGEEILRLQWDSAQRKDSALALAFIDLDHFKSINDNYGHEAGDQVLREAARRLVATLRSSDSLLRWGGE 306
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1024905951 307 EFLLIMPETDMEQAHKAIERI---VGEGLGVRPDGLALTASIGLAERRDDQvDDYRDLLELADRRMYLAKTGGRNRLC 381
Cdd:cd01949    82 EFAILLPGTDLEEAEALAERLreaIEEPFFIDGQEIRVTASIGIATYPEDG-EDAEELLRRADEALYRAKRSGRNRVV 158
COG5001 super family cl34859
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 25-398 5.18e-40

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


The actual alignment was detected with superfamily member COG5001:

Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 150.70  E-value: 5.18e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951  25 LRHLLDPRRHPVLLCQRRATLIVNRVRLFAFLFAVLTPLWSLIDLMVFEPKLWLALAGLRMMACLAFTGLLLFYRPSGNL 104
Cdd:COG5001    50 LLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 105 LDAYRAIAILFAIPTAFYIASHTLLGSYQLAQFSAVVGAGYAFLPFVLMAGLTIFPLTLVENLVLSSLLLLAQALAGYLS 184
Cdd:COG5001   130 AAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLA 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 185 WATLNWPSFAGAFWLLILIAGVASLASMSQLAFMIA-LVRQAIRDPLTGVFSRGSGEEILRLQWDSAQRKDSALALAFID 263
Cdd:COG5001   210 LRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEErLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFID 289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 264 LDHFKSINDNYGHEAGDQVLREAARRLVATLRSSDSLLRWGGEEFLLIMPE-TDMEQAHKAIERI---VGEGLGVRPDGL 339
Cdd:COG5001   290 LDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDlDDPEDAEAVAERIlaaLAEPFELDGHEL 369

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 340 ALTASIGLAERRDDQvDDYRDLLELADRRMYLAKTGGRNRLCAAESEKPQR-ERALALES 398
Cdd:COG5001   370 YVSASIGIALYPDDG-ADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERaRERLELEA 428
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 227-381 1.51e-55

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: 180.06  E-value: 1.51e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 227 RDPLTGVFSRGSGEEILRLQWDSAQRKDSALALAFIDLDHFKSINDNYGHEAGDQVLREAARRLVATLRSSDSLLRWGGE 306
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1024905951 307 EFLLIMPETDMEQAHKAIERI---VGEGLGVRPDGLALTASIGLAERRDDQvDDYRDLLELADRRMYLAKTGGRNRLC 381
Cdd:cd01949    82 EFAILLPGTDLEEAEALAERLreaIEEPFFIDGQEIRVTASIGIATYPEDG-EDAEELLRRADEALYRAKRSGRNRVV 158
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 110-383 4.05e-52

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: 175.17  E-value: 4.05e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 110 AIAILFAIPTAFYIASHTLLGSYQLAQFSAVVGAGYAFLPFVLMAGLTIFPLTLVENLVLSSLLLLAQALAGYLSWATLN 189
Cdd:COG2199     4 LLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLEL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 190 WPSFAGAFWLLILIAGVASLASMSQlafmiALVRQAIRDPLTGVFSRGSGEEILRLQWDSAQRKDSALALAFIDLDHFKS 269
Cdd:COG2199    84 LLLLLALLLLLLALEDITELRRLEE-----RLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 270 INDNYGHEAGDQVLREAARRLVATLRSSDSLLRWGGEEFLLIMPETDMEQAHKAIERIVG--EGLGVRPDG--LALTASI 345
Cdd:COG2199   159 INDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREalEQLPFELEGkeLRVTVSI 238

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1024905951 346 GLAERRDDQvDDYRDLLELADRRMYLAKTGGRNRLCAA 383
Cdd:COG2199   239 GVALYPEDG-DSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 225-379 1.30e-49

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: 164.73  E-value: 1.30e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 225 AIRDPLTGVFSRGSGEEILRLQWDSAQRKDSALALAFIDLDHFKSINDNYGHEAGDQVLREAARRLVATLRSSDSLLRWG 304
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 305 GEEFLLIMPETDMEQAHKAIERI------VGEGLGVRPDGLALTASIGLAERRDDQvDDYRDLLELADRRMYLAKTGGRN 378
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIrrllakLKIPHTVSGLPLYVTISIGIAAYPNDG-EDPEDLLKRADTALYQAKQAGRN 159


                  .
gi 1024905951 379 R 379
Cdd:pfam00990 160 R 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 224-384 2.91e-49

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: 164.05  E-value: 2.91e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 224 QAIRDPLTGVFSRGSGEEILRLQWDSAQRKDSALALAFIDLDHFKSINDNYGHEAGDQVLREAARRLVATLRSSDSLLRW 303
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 304 GGEEFLLIMPETDMEQAHKAIERIVgEGLGVRP------DGLALTASIGLAERRDDQvDDYRDLLELADRRMYLAKTGGR 377
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLR-DAINSKPievagsETLTVTVSIGVACYPGHG-LTLEELLKRADEALYQAKKAGR 158


                  ....*..
gi 1024905951 378 NRLCAAE 384
Cdd:TIGR00254 159 NRVVVAD 165
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 223-383 1.41e-46

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 157.02  E-value: 1.41e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951  223 RQAIRDPLTGVFSRGSGEEILRLQWDSAQRKDSALALAFIDLDHFKSINDNYGHEAGDQVLREAARRLVATLRSSDSLLR 302
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951  303 WGGEEFLLIMPETDMEQAHKAIERI---VGEGLGVRPDGLALTASIGLAERRDDqVDDYRDLLELADRRMYLAKTGGRNR 379
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERIlqqLREPIIIHGIPLYLTISIGVAAYPNP-GEDAEDLLKRADTALYQAKKAGRNQ 159


                   ....
gi 1024905951  380 LCAA 383
Cdd:smart00267 160 VAVY 163
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
220-380 8.82e-46

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 157.84  E-value: 8.82e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 220 ALVRQAIRDPLTGVFSRGSGEEILRLQWDSAQRKDSALALAFIDLDHFKSINDNYGHEAGDQVLREAARRLVATLRSSDS 299
Cdd:NF038266   89 ALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDL 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 300 LLRWGGEEFLLIMPETDMEQAHKAIERIVGE----GLGVRPDGLALTASIGLAERRDDQvDDYRDLLELADRRMYLAKTG 375
Cdd:NF038266  169 CGRWGGEEFLLLLPETGLEEAQVVLERLREAvralAVRVGDDVLSVTASAGLAEHRPPE-EGLSATLSRADQALYQAKRA 247


                  ....*
gi 1024905951 376 GRNRL 380
Cdd:NF038266  248 GRDRV 252
pleD PRK09581
response regulator PleD; Reviewed
 222-383 8.05e-42

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 152.75  E-value: 8.05e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 222 VRQAIRDPLTGVFSRGSGEEILRLQWDSAQRKDSALALAFIDLDHFKSINDNYGHEAGDQVLREAARRLVATLRSSDSLL 301
Cdd:PRK09581  289 IEMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIA 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 302 RWGGEEFLLIMPETDMEQAHKAIERI---VGEGLGVRPDG---LALTASIGLAERRdDQVDDYRDLLELADRRMYLAKTG 375
Cdd:PRK09581  369 RYGGEEFVVVMPDTDIEDAIAVAERIrrkIAEEPFIISDGkerLNVTVSIGVAELR-PSGDTIEALIKRADKALYEAKNT 447


                  ....*...
gi 1024905951 376 GRNRLCAA 383
Cdd:PRK09581  448 GRNRVVAL 455
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 25-398 5.18e-40

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: 150.70  E-value: 5.18e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951  25 LRHLLDPRRHPVLLCQRRATLIVNRVRLFAFLFAVLTPLWSLIDLMVFEPKLWLALAGLRMMACLAFTGLLLFYRPSGNL 104
Cdd:COG5001    50 LLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 105 LDAYRAIAILFAIPTAFYIASHTLLGSYQLAQFSAVVGAGYAFLPFVLMAGLTIFPLTLVENLVLSSLLLLAQALAGYLS 184
Cdd:COG5001   130 AAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLA 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 185 WATLNWPSFAGAFWLLILIAGVASLASMSQLAFMIA-LVRQAIRDPLTGVFSRGSGEEILRLQWDSAQRKDSALALAFID 263
Cdd:COG5001   210 LRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEErLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFID 289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 264 LDHFKSINDNYGHEAGDQVLREAARRLVATLRSSDSLLRWGGEEFLLIMPE-TDMEQAHKAIERI---VGEGLGVRPDGL 339
Cdd:COG5001   290 LDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDlDDPEDAEAVAERIlaaLAEPFELDGHEL 369

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 340 ALTASIGLAERRDDQvDDYRDLLELADRRMYLAKTGGRNRLCAAESEKPQR-ERALALES 398
Cdd:COG5001   370 YVSASIGIALYPDDG-ADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERaRERLELEA 428
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 227-381 1.51e-55

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: 180.06  E-value: 1.51e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 227 RDPLTGVFSRGSGEEILRLQWDSAQRKDSALALAFIDLDHFKSINDNYGHEAGDQVLREAARRLVATLRSSDSLLRWGGE 306
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1024905951 307 EFLLIMPETDMEQAHKAIERI---VGEGLGVRPDGLALTASIGLAERRDDQvDDYRDLLELADRRMYLAKTGGRNRLC 381
Cdd:cd01949    82 EFAILLPGTDLEEAEALAERLreaIEEPFFIDGQEIRVTASIGIATYPEDG-EDAEELLRRADEALYRAKRSGRNRVV 158
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 110-383 4.05e-52

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: 175.17  E-value: 4.05e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 110 AIAILFAIPTAFYIASHTLLGSYQLAQFSAVVGAGYAFLPFVLMAGLTIFPLTLVENLVLSSLLLLAQALAGYLSWATLN 189
Cdd:COG2199     4 LLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLEL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 190 WPSFAGAFWLLILIAGVASLASMSQlafmiALVRQAIRDPLTGVFSRGSGEEILRLQWDSAQRKDSALALAFIDLDHFKS 269
Cdd:COG2199    84 LLLLLALLLLLLALEDITELRRLEE-----RLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 270 INDNYGHEAGDQVLREAARRLVATLRSSDSLLRWGGEEFLLIMPETDMEQAHKAIERIVG--EGLGVRPDG--LALTASI 345
Cdd:COG2199   159 INDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREalEQLPFELEGkeLRVTVSI 238

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1024905951 346 GLAERRDDQvDDYRDLLELADRRMYLAKTGGRNRLCAA 383
Cdd:COG2199   239 GVALYPEDG-DSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 225-379 1.30e-49

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: 164.73  E-value: 1.30e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 225 AIRDPLTGVFSRGSGEEILRLQWDSAQRKDSALALAFIDLDHFKSINDNYGHEAGDQVLREAARRLVATLRSSDSLLRWG 304
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 305 GEEFLLIMPETDMEQAHKAIERI------VGEGLGVRPDGLALTASIGLAERRDDQvDDYRDLLELADRRMYLAKTGGRN 378
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIrrllakLKIPHTVSGLPLYVTISIGIAAYPNDG-EDPEDLLKRADTALYQAKQAGRN 159


                  .
gi 1024905951 379 R 379
Cdd:pfam00990 160 R 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 224-384 2.91e-49

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: 164.05  E-value: 2.91e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 224 QAIRDPLTGVFSRGSGEEILRLQWDSAQRKDSALALAFIDLDHFKSINDNYGHEAGDQVLREAARRLVATLRSSDSLLRW 303
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 304 GGEEFLLIMPETDMEQAHKAIERIVgEGLGVRP------DGLALTASIGLAERRDDQvDDYRDLLELADRRMYLAKTGGR 377
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLR-DAINSKPievagsETLTVTVSIGVACYPGHG-LTLEELLKRADEALYQAKKAGR 158


                  ....*..
gi 1024905951 378 NRLCAAE 384
Cdd:TIGR00254 159 NRVVVAD 165
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 223-383 1.41e-46

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 157.02  E-value: 1.41e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951  223 RQAIRDPLTGVFSRGSGEEILRLQWDSAQRKDSALALAFIDLDHFKSINDNYGHEAGDQVLREAARRLVATLRSSDSLLR 302
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951  303 WGGEEFLLIMPETDMEQAHKAIERI---VGEGLGVRPDGLALTASIGLAERRDDqVDDYRDLLELADRRMYLAKTGGRNR 379
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERIlqqLREPIIIHGIPLYLTISIGVAAYPNP-GEDAEDLLKRADTALYQAKKAGRNQ 159


                   ....
gi 1024905951  380 LCAA 383
Cdd:smart00267 160 VAVY 163
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
220-380 8.82e-46

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 157.84  E-value: 8.82e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 220 ALVRQAIRDPLTGVFSRGSGEEILRLQWDSAQRKDSALALAFIDLDHFKSINDNYGHEAGDQVLREAARRLVATLRSSDS 299
Cdd:NF038266   89 ALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDL 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 300 LLRWGGEEFLLIMPETDMEQAHKAIERIVGE----GLGVRPDGLALTASIGLAERRDDQvDDYRDLLELADRRMYLAKTG 375
Cdd:NF038266  169 CGRWGGEEFLLLLPETGLEEAQVVLERLREAvralAVRVGDDVLSVTASAGLAEHRPPE-EGLSATLSRADQALYQAKRA 247


                  ....*
gi 1024905951 376 GRNRL 380
Cdd:NF038266  248 GRDRV 252
pleD PRK09581
response regulator PleD; Reviewed
 222-383 8.05e-42

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 152.75  E-value: 8.05e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 222 VRQAIRDPLTGVFSRGSGEEILRLQWDSAQRKDSALALAFIDLDHFKSINDNYGHEAGDQVLREAARRLVATLRSSDSLL 301
Cdd:PRK09581  289 IEMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIA 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 302 RWGGEEFLLIMPETDMEQAHKAIERI---VGEGLGVRPDG---LALTASIGLAERRdDQVDDYRDLLELADRRMYLAKTG 375
Cdd:PRK09581  369 RYGGEEFVVVMPDTDIEDAIAVAERIrrkIAEEPFIISDGkerLNVTVSIGVAELR-PSGDTIEALIKRADKALYEAKNT 447


                  ....*...
gi 1024905951 376 GRNRLCAA 383
Cdd:PRK09581  448 GRNRVVAL 455
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 25-398 5.18e-40

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: 150.70  E-value: 5.18e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951  25 LRHLLDPRRHPVLLCQRRATLIVNRVRLFAFLFAVLTPLWSLIDLMVFEPKLWLALAGLRMMACLAFTGLLLFYRPSGNL 104
Cdd:COG5001    50 LLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 105 LDAYRAIAILFAIPTAFYIASHTLLGSYQLAQFSAVVGAGYAFLPFVLMAGLTIFPLTLVENLVLSSLLLLAQALAGYLS 184
Cdd:COG5001   130 AAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLA 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 185 WATLNWPSFAGAFWLLILIAGVASLASMSQLAFMIA-LVRQAIRDPLTGVFSRGSGEEILRLQWDSAQRKDSALALAFID 263
Cdd:COG5001   210 LRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEErLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFID 289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 264 LDHFKSINDNYGHEAGDQVLREAARRLVATLRSSDSLLRWGGEEFLLIMPE-TDMEQAHKAIERI---VGEGLGVRPDGL 339
Cdd:COG5001   290 LDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDlDDPEDAEAVAERIlaaLAEPFELDGHEL 369

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 340 ALTASIGLAERRDDQvDDYRDLLELADRRMYLAKTGGRNRLCAAESEKPQR-ERALALES 398
Cdd:COG5001   370 YVSASIGIALYPDDG-ADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERaRERLELEA 428
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
195-388 1.05e-37

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 143.23  E-value: 1.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 195 GAFWLLILIAGVASLASMSQL-AFMIALVR----QAIRDPLTGVFSRGSGEEILRLQWDSAQRKDSALALAFIDLDHFKS 269
Cdd:PRK15426  363 TLLWALFTAMLLISWYVIRRMvSNMFVLQSslqwQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKS 442

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 270 INDNYGHEAGDQVLREAARRLVATLRSSDSLLRWGGEEFLLIMPETDMEQAHKAIER----IVGEGLGVRPDG-LALTAS 344
Cdd:PRK15426  443 INDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERirlrINEKEILVAKSTtIRISAS 522

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1024905951 345 IGLAERRDDQVDDYRDLLELADRRMYLAKTGGRNRLCAAESEKP 388
Cdd:PRK15426  523 LGVSSAEEDGDYDFEQLQSLADRRLYLAKQAGRNRVCASDNAHE 566
PRK09894 PRK09894
diguanylate cyclase; Provisional
 215-379 1.58e-36

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 134.81  E-value: 1.58e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 215 LAFMIALVRQAI--------RDPLTGVFSR-GSGEEilrLQWDSAQRKDSALALAFIDLDHFKSINDNYGHEAGDQVLRE 285
Cdd:PRK09894  111 LSFTAALTDYKIylltirsnMDVLTGLPGRrVLDES---FDHQLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRT 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 286 AARRLVATLRSSDSLLRWGGEEFLLIMPETDMEQAHKAIERI---VGEGLGVRPDG-LALTASIGLAERRDDQVDDyrDL 361
Cdd:PRK09894  188 LATYLASWTRDYETVYRYGGEEFIICLKAATDEEACRAGERIrqlIANHAITHSDGrINITATFGVSRAFPEETLD--VV 265

                         170
                  ....*....|....*...
gi 1024905951 362 LELADRRMYLAKTGGRNR 379
Cdd:PRK09894  266 IGRADRAMYEGKQTGRNR 283
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 227-379 3.40e-27

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 111.07  E-value: 3.40e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 227 RDPLTGVFSRGSGEEILRLQWDSAQRKDSALALAFIDLDHFKSINDNYGHEAGDQVLREAARRLVATLRSSDSLLRWGGE 306
Cdd:PRK10245  207 RDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGD 286

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024905951 307 EFLLIMPETDMEQAHKAIERiVGEGLGVRPDGLA----LTASIGLAErRDDQVDDYRDLLELADRRMYLAKTGGRNR 379
Cdd:PRK10245  287 EFAVIMSGTPAESAITAMSR-VHEGLNTLRLPNApqvtLRISVGVAP-LNPQMSHYREWLKSADLALYKAKNAGRNR 361
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 216-395 1.58e-25

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 108.99  E-value: 1.58e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951  216 AFMIALVRQAIRDPLTGVFSRGSGEEILRLQWDSAQRKDSALALAFIDLDHFKSINDNYGHEAGDQVLREAARRLVATLR 295
Cdd:PRK09776   656 KMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLR 735

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951  296 SSDSLLRWGGEEFLLIMPETDMEQAHKAIERIVGEGLGVRP--DGLA--LTASIGLAErRDDQVDDYRDLLELADRRMYL 371
Cdd:PRK09776   736 SSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFpwEGRVyrVGASAGITL-IDANNHQASEVMSQADIACYA 814

                          170       180
                   ....*....|....*....|....
gi 1024905951  372 AKTGGRNRLCAAEsekPQRERALA 395
Cdd:PRK09776   815 AKNAGRGRVTVYE---PQQAAAHS 835
PRK09966 PRK09966
diguanylate cyclase DgcN;
221-373 1.77e-18

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 86.60  E-value: 1.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 221 LVRQAIRDPLTGVFSRGSGEE-ILRLQWDSAQRKDSALAlaFIDLDHFKSINDNYGHEAGDQVLREAARRLVATLRSSDS 299
Cdd:PRK09966  244 LLRTALHDPLTGLANRAAFRSgINTLMNNSDARKTSALL--FLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHK 321

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1024905951 300 LLRWGGEEFLLIM----PETDMEQAHKAIERIVGEGLGVRPDGLA-LTASIGLAERRDDQVDDyrDLLELADRRMYLAK 373
Cdd:PRK09966  322 AYRLGGDEFAMVLydvqSESEVQQICSALTQIFNLPFDLHNGHQTtMTLSIGYAMTIEHASAE--KLQELADHNMYQAK 398
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 222-376 1.76e-16

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 81.35  E-value: 1.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 222 VRQAIR-DPLTGVFSRGSgeeiLRLQWDSAQRKDSALALAFIDLDHFKSINDNYGHEAGDQVLREAARRLVATLRSSDSL 300
Cdd:PRK11359  372 IEQLIQfDPLTGLPNRNN----LHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYL 447

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 301 LRWGGEEFLLIMPETDMEQAHKAIE---RIVGEGLGVRPDGLALTASIGLAErrdDQVDDYRDLLELADRRM-YLAKTGG 376
Cdd:PRK11359  448 CRIEGTQFVLVSLENDVSNITQIADelrNVVSKPIMIDDKPFPLTLSIGISY---DVGKNRDYLLSTAHNAMdYIRKNGG 524
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
221-390 4.77e-16

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 80.11  E-value: 4.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 221 LVRQAIRDPLTGVFSRGSGEEilRLQWDSAQRKDSALALAFIDLDHFKSINDNYGHEAGDQVLREAARRLVATLRSSDSL 300
Cdd:PRK10060  233 LRILANTDSITGLPNRNAIQE--LIDHAINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTL 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 301 LRWGGEEFLLIMPETDMEQAHKAIERIVgeglgvrpDGLALTASIGLAE----------RRDDQVDDYRDLLELADRRMY 370
Cdd:PRK10060  311 ARLGGDEFLVLASHTSQAALEAMASRIL--------TRLRLPFRIGLIEvytgcsigiaLAPEHGDDSESLIRSADTAMY 382

                         170       180
                  ....*....|....*....|
gi 1024905951 371 LAKTGGRNRLCAAESEKPQR 390
Cdd:PRK10060  383 TAKEGGRGQFCVFSPEMNQR 402
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 259-375 1.68e-11

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: 61.22  E-value: 1.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024905951 259 LAFIDLDHFKSINDNYGHEAGDQVLREAARRLVATL-RSSDSLLRWGGEEFLLIMPETDMEQAHKAIERIVGEGLGVR-P 336
Cdd:cd07556     4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSALNqS 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1024905951 337 DGLALTASIGLA--------ERRDDQVDDYRDLLELADRRMYLAKTG 375
Cdd:cd07556    84 EGNPVRVRIGIHtgpvvvgvIGSRPQYDVWGALVNLASRMESQAKAG 130
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 298-373 9.27e-09

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: 54.53  E-value: 9.27e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1024905951 298 DSLLRWGGEEFLLIMPETDMEQAHKAIERIVGEGLgvRPDGLALTASIGLAErrddqvddyRDLLELADrRMYLAK 373
Cdd:COG3706   116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVA--ELPSLRVTVSIGVAG---------DSLLKRAD-ALYQAR 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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