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Conserved domains on  [gi|515666991|ref|WP_017099591|]
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MULTISPECIES: sensor domain-containing diguanylate cyclase [Vibrio]

Protein Classification

sensor domain-containing diguanylate cyclase( domain architecture ID 10005839)

sensor domain-containing diguanylate cyclase containing a GAF sensor domain, catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules

CATH:  3.30.70.1230
EC:  2.7.7.65
Gene Ontology:  GO:0046872|GO:0052621
PubMed:  11119645
SCOP:  4001316

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 ...
168-329 2.00e-41

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: 145.51  E-value: 2.00e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 168 EKYELENQLNFFANRDSLTHSLNRRALLREAEQVLTNRCFTEKVMACLFVDVDKFKSINDTFGHSFGDDVLLAVAKVLDE 247
Cdd:COG2199  102 ELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRA 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 248 ATTACAKIGRYGGDEFVVFSCFDDQESVLNFYRSLERTLEQA-LYIDGTQF--SVSVGLS-YDKDPESLEGLIAQADKNM 323
Cdd:COG2199  182 SLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLpFELEGKELrvTVSIGVAlYPEDGDSAEELLRRADLAL 261

                 ....*.
gi 515666991 324 YQIKQA 329
Cdd:COG2199  262 YRAKRA 267
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
24-168 9.63e-09

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: 53.24  E-value: 9.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991   24 LDRKELNRKIIQLTEQIFGQRMASILLLNPESNTLHLEYAPNLpdfynqQIEGVGVGAGIGSCGEAAALKKAVMVSNINA 103
Cdd:pfam13185   2 ADLEELLDAVLEAAVELGASAVGFILLVDDDGRLAAWGGAADE------LSAALDDPPGEGLVGEALRTGRPVIVNDLAA 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515666991  104 HPNWIPFLALtnQANLHACWSVPIISShGHVLGTFAIYSQYISEPHEFELEILELLASLYSVALE 168
Cdd:pfam13185  76 DPAKKGLPAG--HAGLRSFLSVPLVSG-GRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAIE 137
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
168-329 2.00e-41

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: 145.51  E-value: 2.00e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 168 EKYELENQLNFFANRDSLTHSLNRRALLREAEQVLTNRCFTEKVMACLFVDVDKFKSINDTFGHSFGDDVLLAVAKVLDE 247
Cdd:COG2199  102 ELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRA 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 248 ATTACAKIGRYGGDEFVVFSCFDDQESVLNFYRSLERTLEQA-LYIDGTQF--SVSVGLS-YDKDPESLEGLIAQADKNM 323
Cdd:COG2199  182 SLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLpFELEGKELrvTVSIGVAlYPEDGDSAEELLRRADLAL 261

                 ....*.
gi 515666991 324 YQIKQA 329
Cdd:COG2199  262 YRAKRA 267
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
181-330 4.16e-41

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: 140.77  E-value: 4.16e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 181 NRDSLTHSLNRRALLREAEQVLTNRCFTEKVMACLFVDVDKFKSINDTFGHSFGDDVLLAVAKVLDEATTACAKIGRYGG 260
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515666991 261 DEFVVFSCFDDQESVLNFYRSLERTLEQALYIDGTQF--SVSVGLS-YDKDPESLEGLIAQADKNMYQIKQAK 330
Cdd:cd01949   81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIrvTASIGIAtYPEDGEDAEELLRRADEALYRAKRSG 153
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
180-329 2.83e-32

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 118.12  E-value: 2.83e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991   180 ANRDSLTHSLNRRALLREAEQVLTNRCFTEKVMACLFVDVDKFKSINDTFGHSFGDDVLLAVAKVLDEATTACAKIGRYG 259
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515666991   260 GDEFVVFSCFDDQESVLNFYRSLERTLEQALYIDGTQF--SVSVGLS-YDKDPESLEGLIAQADKNMYQIKQA 329
Cdd:smart00267  83 GDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLylTISIGVAaYPNPGEDAEDLLKRADTALYQAKKA 155
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
180-330 9.10e-32

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: 116.58  E-value: 9.10e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991  180 ANRDSLTHSLNRRALLREAEQVLTNRCFTEKVMACLFVDVDKFKSINDTFGHSFGDDVLLAVAKVLDEATTACAKIGRYG 259
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515666991  260 GDEFVVF--SCFDDQESVLNfyRSLERTLEQ-----ALYIDGTQFSVSVGLS-YDKDPESLEGLIAQADKNMYQIKQAK 330
Cdd:pfam00990  81 GDEFAILlpETSLEGAQELA--ERIRRLLAKlkiphTVSGLPLYVTISIGIAaYPNDGEDPEDLLKRADTALYQAKQAG 157
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
180-330 4.16e-28

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: 107.04  E-value: 4.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991  180 ANRDSLTHSLNRRALLREAEQvLTNRCFTEKVMAC-LFVDVDKFKSINDTFGHSFGDDVLLAVAKVLDEATTACAKIGRY 258
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLDS-ELKRARRFQRSFSvLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515666991  259 GGDEFVVFSCFDDQESVLNFYRSLERTLEQ-ALYIDGTQ---FSVSVGLS-YDKDPESLEGLIAQADKNMYQIKQAK 330
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSkPIEVAGSEtltVTVSIGVAcYPGHGLTLEELLKRADEALYQAKKAG 157
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
121-329 2.88e-23

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 100.61  E-value: 2.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 121 ACWSVPIISSHGHVLGTFAIYSQYISEPHEFELEILELLASLYSVALEKYELENQLNFFANRDSLTHSLNRRALLREAEQ 200
Cdd:PRK11359 317 QSWSATIRQRDGAPAGTLQIKTSSGAETSAFIERVADISQHLAALALEQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDD 396
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 201 VLTNrcftEKVMACLFVDVDKFKSINDTFGHSFGDDVLLAVAKVLDEATTACAKIGRYGGDEFVVFSCFDDQESVLNFYR 280
Cdd:PRK11359 397 LVDK----AVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIAD 472
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515666991 281 SLERTLEQALYIDGTQF--SVSVGLSYD--KDPESlegLIAQADKNMYQIKQA 329
Cdd:PRK11359 473 ELRNVVSKPIMIDDKPFplTLSIGISYDvgKNRDY---LLSTAHNAMDYIRKN 522
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
24-168 9.63e-09

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: 53.24  E-value: 9.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991   24 LDRKELNRKIIQLTEQIFGQRMASILLLNPESNTLHLEYAPNLpdfynqQIEGVGVGAGIGSCGEAAALKKAVMVSNINA 103
Cdd:pfam13185   2 ADLEELLDAVLEAAVELGASAVGFILLVDDDGRLAAWGGAADE------LSAALDDPPGEGLVGEALRTGRPVIVNDLAA 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515666991  104 HPNWIPFLALtnQANLHACWSVPIISShGHVLGTFAIYSQYISEPHEFELEILELLASLYSVALE 168
Cdd:pfam13185  76 DPAKKGLPAG--HAGLRSFLSVPLVSG-GRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAIE 137
diguan_DgcJ NF040885
diguanylate cyclase DgcJ;
183-330 1.06e-08

diguanylate cyclase DgcJ;


Pssm-ID: 468821 [Multi-domain]  Cd Length: 490  Bit Score: 56.12  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 183 DSLTHSLNRRALLREAEQVLTNrcFTEKVMACLFV--DVDKFKSINDTFGHSFGDDVLLAVAKVLDEATTACAKIGRYGG 260
Cdd:NF040885 344 DSMTGLYNRKILTPTLEQRLQR--LTEKGIPVTFIalDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGIRLGG 421
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515666991 261 DEF-VVFSCFDDQESvlnfYRSLERTLEQALYIDGTQ-FSVSVGLSYDKDPESLEGLIAQADKNMYQIKQAK 330
Cdd:NF040885 422 DEFcIILIDYEEAEA----QNLIERIRQHLRTIDPDKrVSFSWGAYQMQPGDTLDDAYKAADERLYLNKKQK 489
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
25-177 1.37e-04

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: 41.60  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991    25 DRKELNRKIIQLTEQIFGQRMASILLLNPESNTLH-LEYAPNLPDFYnqqiEGVGVGAGIGSCGEAAALKKAVMVSNINA 103
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGELvLVAADGLTLPT----LGIRFPLDEGLAGRVAETGRPLNIPDVEA 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515666991   104 HPNWIPFLALTNQAnLHACWSVPIISsHGHVLGTFAIYSQYISEP-HEFELEILELLASLYSVALEKYELENQLN 177
Cdd:smart00065  77 DPLFAEDLLGRYQG-VRSFLAVPLVA-DGELVGVLALHNKKSPRPfTEEDEELLQALANQLAIALANAQLYEELR 149
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
168-329 2.00e-41

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: 145.51  E-value: 2.00e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 168 EKYELENQLNFFANRDSLTHSLNRRALLREAEQVLTNRCFTEKVMACLFVDVDKFKSINDTFGHSFGDDVLLAVAKVLDE 247
Cdd:COG2199  102 ELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRA 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 248 ATTACAKIGRYGGDEFVVFSCFDDQESVLNFYRSLERTLEQA-LYIDGTQF--SVSVGLS-YDKDPESLEGLIAQADKNM 323
Cdd:COG2199  182 SLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLpFELEGKELrvTVSIGVAlYPEDGDSAEELLRRADLAL 261

                 ....*.
gi 515666991 324 YQIKQA 329
Cdd:COG2199  262 YRAKRA 267
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
181-330 4.16e-41

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: 140.77  E-value: 4.16e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 181 NRDSLTHSLNRRALLREAEQVLTNRCFTEKVMACLFVDVDKFKSINDTFGHSFGDDVLLAVAKVLDEATTACAKIGRYGG 260
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515666991 261 DEFVVFSCFDDQESVLNFYRSLERTLEQALYIDGTQF--SVSVGLS-YDKDPESLEGLIAQADKNMYQIKQAK 330
Cdd:cd01949   81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIrvTASIGIAtYPEDGEDAEELLRRADEALYRAKRSG 153
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
168-329 1.42e-35

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: 136.44  E-value: 1.42e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 168 EKYELENQLNFFANRDSLTHSLNRRALLREAEQVLTNRCFTEKVMACLFVDVDKFKSINDTFGHSFGDDVLLAVAKVLDE 247
Cdd:COG5001  239 ERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRA 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 248 ATTACAKIGRYGGDEFVV-FSCFDDQESVLNFYRSLERTLEQALYIDGTQF--SVSVGLS-YDKDPESLEGLIAQADKNM 323
Cdd:COG5001  319 CLREGDTVARLGGDEFAVlLPDLDDPEDAEAVAERILAALAEPFELDGHELyvSASIGIAlYPDDGADAEELLRNADLAM 398

                 ....*.
gi 515666991 324 YQIKQA 329
Cdd:COG5001  399 YRAKAA 404
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
180-329 2.83e-32

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 118.12  E-value: 2.83e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991   180 ANRDSLTHSLNRRALLREAEQVLTNRCFTEKVMACLFVDVDKFKSINDTFGHSFGDDVLLAVAKVLDEATTACAKIGRYG 259
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515666991   260 GDEFVVFSCFDDQESVLNFYRSLERTLEQALYIDGTQF--SVSVGLS-YDKDPESLEGLIAQADKNMYQIKQA 329
Cdd:smart00267  83 GDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLylTISIGVAaYPNPGEDAEDLLKRADTALYQAKKA 155
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
180-330 9.10e-32

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: 116.58  E-value: 9.10e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991  180 ANRDSLTHSLNRRALLREAEQVLTNRCFTEKVMACLFVDVDKFKSINDTFGHSFGDDVLLAVAKVLDEATTACAKIGRYG 259
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515666991  260 GDEFVVF--SCFDDQESVLNfyRSLERTLEQ-----ALYIDGTQFSVSVGLS-YDKDPESLEGLIAQADKNMYQIKQAK 330
Cdd:pfam00990  81 GDEFAILlpETSLEGAQELA--ERIRRLLAKlkiphTVSGLPLYVTISIGIAaYPNDGEDPEDLLKRADTALYQAKQAG 157
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
180-330 4.16e-28

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: 107.04  E-value: 4.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991  180 ANRDSLTHSLNRRALLREAEQvLTNRCFTEKVMAC-LFVDVDKFKSINDTFGHSFGDDVLLAVAKVLDEATTACAKIGRY 258
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLDS-ELKRARRFQRSFSvLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515666991  259 GGDEFVVFSCFDDQESVLNFYRSLERTLEQ-ALYIDGTQ---FSVSVGLS-YDKDPESLEGLIAQADKNMYQIKQAK 330
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSkPIEVAGSEtltVTVSIGVAcYPGHGLTLEELLKRADEALYQAKKAG 157
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
121-329 2.88e-23

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 100.61  E-value: 2.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 121 ACWSVPIISSHGHVLGTFAIYSQYISEPHEFELEILELLASLYSVALEKYELENQLNFFANRDSLTHSLNRRALLREAEQ 200
Cdd:PRK11359 317 QSWSATIRQRDGAPAGTLQIKTSSGAETSAFIERVADISQHLAALALEQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDD 396
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 201 VLTNrcftEKVMACLFVDVDKFKSINDTFGHSFGDDVLLAVAKVLDEATTACAKIGRYGGDEFVVFSCFDDQESVLNFYR 280
Cdd:PRK11359 397 LVDK----AVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIAD 472
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515666991 281 SLERTLEQALYIDGTQF--SVSVGLSYD--KDPESlegLIAQADKNMYQIKQA 329
Cdd:PRK11359 473 ELRNVVSKPIMIDDKPFplTLSIGISYDvgKNRDY---LLSTAHNAMDYIRKN 522
PRK09894 PRK09894
diguanylate cyclase; Provisional
163-329 1.49e-20

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 89.74  E-value: 1.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 163 YSVALEKYELEnQLNFFANRDSLTHSLNRRALLREAEQVLTNRcfTEKVMACLFVDVDKFKSINDTFGHSFGDDVLLAVA 242
Cdd:PRK09894 113 FTAALTDYKIY-LLTIRSNMDVLTGLPGRRVLDESFDHQLRNR--EPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLA 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 243 KVLDEATTACAKIGRYGGDEFVVF--SCFDDQESvlnfyRSLERtLEQALYIDGTQFS-------VSVGLSYDKDPESLE 313
Cdd:PRK09894 190 TYLASWTRDYETVYRYGGEEFIIClkAATDEEAC-----RAGER-IRQLIANHAITHSdgrinitATFGVSRAFPEETLD 263
                        170
                 ....*....|....*.
gi 515666991 314 GLIAQADKNMYQIKQA 329
Cdd:PRK09894 264 VVIGRADRAMYEGKQT 279
pleD PRK09581
response regulator PleD; Reviewed
163-328 2.58e-18

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 85.34  E-value: 2.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 163 YSVALEKYeLENQLNFfANRDSLTHSLNRRALLREAEQVLTNRCFTEKVMACLFVDVDKFKSINDTFGHSFGDDVLLAVA 242
Cdd:PRK09581 277 YQDALRNN-LEQSIEM-AVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFA 354
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 243 KVLDEATTACAKIGRYGGDEFVVfscfddqesVLNfyrslERTLEQALY--------IDGTQFS-----------VSVGL 303
Cdd:PRK09581 355 KRLRNNIRGTDLIARYGGEEFVV---------VMP-----DTDIEDAIAvaerirrkIAEEPFIisdgkerlnvtVSIGV 420
                        170       180
                 ....*....|....*....|....*.
gi 515666991 304 S-YDKDPESLEGLIAQADKNMYQIKQ 328
Cdd:PRK09581 421 AeLRPSGDTIEALIKRADKALYEAKN 446
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
170-329 4.17e-18

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 85.07  E-value: 4.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 170 YELENQLNFFANRDSLTHSLNRRALlREAEQVLTNRCFTEKV-MACLFVDVDKFKSINDTFGHSFGDDVLLAVAKVLDEA 248
Cdd:PRK15426 388 FVLQSSLQWQAWHDPLTRLYNRGAL-FEKARALAKRCQRDQQpFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSS 466
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 249 TTACAKIGRYGGDEF-VVFSCFDDQESVLNFYRSLERTLEQALYIDGT---QFSVSVGLS--YDKDPESLEGLIAQADKN 322
Cdd:PRK15426 467 LRAQDVAGRVGGEEFcVVLPGASLAEAAQVAERIRLRINEKEILVAKSttiRISASLGVSsaEEDGDYDFEQLQSLADRR 546

                 ....*..
gi 515666991 323 MYQIKQA 329
Cdd:PRK15426 547 LYLAKQA 553
GAF COG2203
GAF domain [Signal transduction mechanisms];
11-329 2.62e-17

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 82.93  E-value: 2.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991  11 RAVNSLLRKLALGLDRKELNRKIIQLTEQIFGQRMASILLLNPESNTLHLEYAPNLPDFYNQQIEgvgvgAGIGSCGEAA 90
Cdd:COG2203  193 ALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRLP-----LGEGLAGRAL 267
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991  91 ALKKAVMVSNINAHPNWIPFL-ALTNQANLHACWSVPIISsHGHVLGTFAIYSQYISEPHEFELEILELLASLYSVALEK 169
Cdd:COG2203  268 RTGEPVVVNDASTDPRFAPSLrELLLALGIRSLLCVPLLV-DGRLIGVLALYSKEPRAFTEEDLELLEALADQAAIAIER 346
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 170 YELENQLNFFANR------------DSLTHSLNRRALLREAEQVLTNRCFTEKVMACLFVDVDKFKSINDTFGHSFGDDV 237
Cdd:COG2203  347 ARLYEALEAALAAllqelallrlllDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDL 426
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 238 LLAVAKVLDEATTACAKIGRYGGDEFVVFSCFDDQESVLNFYRSLERTLEQALYIDGTQFSVSVGLSYDKDPESLEGLIA 317
Cdd:COG2203  427 LLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLALSALAVL 506
                        330
                 ....*....|..
gi 515666991 318 QADKNMYQIKQA 329
Cdd:COG2203  507 ASLLLALLLLLL 518
PRK09966 PRK09966
diguanylate cyclase DgcN;
175-331 1.30e-15

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 76.97  E-value: 1.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 175 QLNFFANRDSLThSLNRRALLREAEQVLTNRCFTEKVMACLFVDVDKFKSINDTFGHSFGDDVLLAVAKVLDEATTACAK 254
Cdd:PRK09966 243 QLLRTALHDPLT-GLANRAAFRSGINTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHK 321
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 255 IGRYGGDEF--VVFSCFDDQEsVLNFYRSLERTLEQALYIDGTQ---FSVSVGLSYDKDPESLEGLIAQADKNMYQIKQA 329
Cdd:PRK09966 322 AYRLGGDEFamVLYDVQSESE-VQQICSALTQIFNLPFDLHNGHqttMTLSIGYAMTIEHASAEKLQELADHNMYQAKHQ 400

                 ..
gi 515666991 330 KS 331
Cdd:PRK09966 401 RA 402
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
176-328 2.36e-15

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 76.64  E-value: 2.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 176 LNFFANRDSLTHSLNRRALLREAEQVLTNRcfTEKVMACLFVDVDKFKSINDTFGHSFGD----DVLLAVAKVLDEATTa 251
Cdd:PRK10060 233 LRILANTDSITGLPNRNAIQELIDHAINAA--DNNQVGIVYLDLDNFKKVNDAYGHMFGDqllqDVSLAILSCLEEDQT- 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 252 cakIGRYGGDEFVVFSCFDDQEsvlnfyrSLERTLEQALYIDGTQFSV---------SVGLS-YDKDPESLEGLIAQADK 321
Cdd:PRK10060 310 ---LARLGGDEFLVLASHTSQA-------ALEAMASRILTRLRLPFRIglievytgcSIGIAlAPEHGDDSESLIRSADT 379

                 ....*..
gi 515666991 322 NMYQIKQ 328
Cdd:PRK10060 380 AMYTAKE 386
adrA PRK10245
diguanylate cyclase AdrA; Provisional
163-276 3.54e-15

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 75.25  E-value: 3.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 163 YSVALEKYELENQLNFFANRDSLTHSLNRR---ALLR-EAEQVLTNRCFTekvmACLFVDVDKFKSINDTFGHSFGDDVL 238
Cdd:PRK10245 188 YQTATKLAEHKRRLQVMSTRDGMTGVYNRRhweTLLRnEFDNCRRHHRDA----TLLIIDIDHFKSINDTWGHDVGDEAI 263
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 515666991 239 LAVAKVLDEATTACAKIGRYGGDEFVVFSCFDDQESVL 276
Cdd:PRK10245 264 VALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAI 301
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
175-329 4.25e-09

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 57.76  E-value: 4.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991  175 QLNFFANRDSLTHSLNRRALLREAEQVLTNRCFTEKVMACLFVDVDKFKSINDTFGHSFGDDVLLAVAKVLDEATTACAK 254
Cdd:PRK09776  660 QLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDV 739
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991  255 IGRYGGDEF--VVFSCFDDQ-----ESVLNFYRSLERTLEQALYidgtQFSVSVGLS-YDKDPESLEGLIAQADKNMYQI 326
Cdd:PRK09776  740 LARLGGDEFglLLPDCNVESarfiaTRIISAINDYHFPWEGRVY----RVGASAGITlIDANNHQASEVMSQADIACYAA 815

                  ...
gi 515666991  327 KQA 329
Cdd:PRK09776  816 KNA 818
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
24-168 9.63e-09

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: 53.24  E-value: 9.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991   24 LDRKELNRKIIQLTEQIFGQRMASILLLNPESNTLHLEYAPNLpdfynqQIEGVGVGAGIGSCGEAAALKKAVMVSNINA 103
Cdd:pfam13185   2 ADLEELLDAVLEAAVELGASAVGFILLVDDDGRLAAWGGAADE------LSAALDDPPGEGLVGEALRTGRPVIVNDLAA 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515666991  104 HPNWIPFLALtnQANLHACWSVPIISShGHVLGTFAIYSQYISEPHEFELEILELLASLYSVALE 168
Cdd:pfam13185  76 DPAKKGLPAG--HAGLRSFLSVPLVSG-GRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAIE 137
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
215-304 1.05e-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: 53.13  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 215 LFVDVDKFKSINDTFGHSFGDDVLLAVAKVLDEATTA--CAKIgRYGGDEFVVFSCFDDQESVLNFYRSLERTLEQALYI 292
Cdd:cd07556    5 LFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRsgDLKI-KTIGDEFMVVSGLDHPAAAVAFAEDMREAVSALNQS 83
                         90
                 ....*....|..
gi 515666991 293 DGTQFSVSVGLS 304
Cdd:cd07556   84 EGNPVRVRIGIH 95
diguan_DgcJ NF040885
diguanylate cyclase DgcJ;
183-330 1.06e-08

diguanylate cyclase DgcJ;


Pssm-ID: 468821 [Multi-domain]  Cd Length: 490  Bit Score: 56.12  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991 183 DSLTHSLNRRALLREAEQVLTNrcFTEKVMACLFV--DVDKFKSINDTFGHSFGDDVLLAVAKVLDEATTACAKIGRYGG 260
Cdd:NF040885 344 DSMTGLYNRKILTPTLEQRLQR--LTEKGIPVTFIalDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGIRLGG 421
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515666991 261 DEF-VVFSCFDDQESvlnfYRSLERTLEQALYIDGTQ-FSVSVGLSYDKDPESLEGLIAQADKNMYQIKQAK 330
Cdd:NF040885 422 DEFcIILIDYEEAEA----QNLIERIRQHLRTIDPDKrVSFSWGAYQMQPGDTLDDAYKAADERLYLNKKQK 489
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
25-143 3.20e-08

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: 51.71  E-value: 3.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991   25 DRKELNRKIIQLTEQIFGQRMASILLLNPESNTLHLEYAPNLPDFYNQQIEGVGVgagigscgEAAALKKAVMVSNINAH 104
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLEYLPPGARWLKAAGLEIPPGTGV--------TVLRTGRPLVVPDAAGD 72
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 515666991  105 PNWIPFLALTNQANLHACWSVPIIsSHGHVLGTFAIYSQ 143
Cdd:pfam01590  73 PRFLDPLLLLRNFGIRSLLAVPII-DDGELLGVLVLHHP 110
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
25-177 1.37e-04

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: 41.60  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515666991    25 DRKELNRKIIQLTEQIFGQRMASILLLNPESNTLH-LEYAPNLPDFYnqqiEGVGVGAGIGSCGEAAALKKAVMVSNINA 103
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGELvLVAADGLTLPT----LGIRFPLDEGLAGRVAETGRPLNIPDVEA 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515666991   104 HPNWIPFLALTNQAnLHACWSVPIISsHGHVLGTFAIYSQYISEP-HEFELEILELLASLYSVALEKYELENQLN 177
Cdd:smart00065  77 DPLFAEDLLGRYQG-VRSFLAVPLVA-DGELVGVLALHNKKSPRPfTEEDEELLQALANQLAIALANAQLYEELR 149
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
255-325 2.49e-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: 41.05  E-value: 2.49e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515666991 255 IGRYGGDEFVVFSCFDDQESVLNFYRSLERTLEQALYIdgtQFSVSVGLSYDKdpeslegLIAQADkNMYQ 325
Cdd:COG3706  118 VARYGGEEFAILLPGTDLEGALAVAERIREAVAELPSL---RVTVSIGVAGDS-------LLKRAD-ALYQ 177
 
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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