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Conserved domains on  [gi|852028170|ref|WP_048259573|]
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diguanylate cyclase [Pectobacterium peruviense]

Protein Classification

diguanylate cyclase( domain architecture ID 10201269)

diguanylate cyclase similar to DosC, an oxygen-sensing enzyme that catalyzes the synthesis of cyclic diguanylate (c-di-GMP) via the condensation of 2 GTP molecules

CATH:  3.30.70.1230|1.10.490.10
EC:  2.7.7.65
Gene Ontology:  GO:0046872|GO:0019825|GO:0020037|GO:0052621
PubMed:  32863222|16061809|19281958
SCOP:  4001316|4000551

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: ...
 310-465 1.56e-62

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: 200.09  E-value: 1.56e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 310 DTLTLLLNRRFLPTILRHEISLTMHSNTPLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVFRYGGEE 389
Cdd:cd01949    3 DPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 852028170 390 FLIVLIETPKVAAHTIIERLRKKIENHSIHlqNGESVKMTISAGIAVYSGHP-DYECLIKAADDALYQAKANGRNRI 465
Cdd:cd01949   83 FAILLPGTDLEEAEALAERLREAIEEPFFI--DGQEIRVTASIGIATYPEDGeDAEELLRRADEALYRAKRSGRNRV 157
GS_EcDosC-like_GGDEF cd14757
Globin sensor domain of Escherichia coli Direct Oxygen Sensing Cyclase and related proteins; ...
 20-167 2.22e-58

Globin sensor domain of Escherichia coli Direct Oxygen Sensing Cyclase and related proteins; coupled to a C-terminal GGDEF domain; Globin-coupled-sensors belonging to this subfamily have a C-terminal diguanylate cyclase (DGC/GGDEF) domain coupled to the globin sensor domain. DGC/GGDEF likely functions as a c-di-GMP cyclase in the synthesis of the second messenger cyclic-di-GMP (c-di-GMP). Members include Escherichia coli DosC (also known as YddV), the gene for which is found in a two-gene operon, dosCP. In DosC, the sensory globin domain is coupled to a GGDEF-class diguanylate cyclase, while in DosP, a heme-containing PAS domain is coupled to an EAL-class c-di-GMP phosphodiesterase. DosP and DosC associate in a di-GMP-responsive Escherichia coli RNA processing complex along with polynucleotide phosphorylase (PNPase), enolase, RNase E, and RNA.


:

Pssm-ID: 381271  Cd Length: 149  Bit Score: 188.98  E-value: 2.22e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170  20 QVITSEWTQLIATTSQQSFNLLRTLADQKASDFADEFYTYMLKDQEASLFLSSQQVHDRLHGSMSKWIAAILT-NTGDHL 98
Cdd:cd14757    1 ERLAAEWQALLQQVSPAVRALVAALVQAHADALAAEFYDTMLADPEASPFLSHEQVQTRLHASLQRWLIELFSaADDEDL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 852028170  99 ADLISHQKKIGQIHARIGIPVDLVERGARRLKWHLYEDIAQVADDKALCFDAMRFASISMDIAIEIMSK 167
Cdd:cd14757   81 EALVARQRKVGEVHARIGIPVHLVMRGARVLKRRLAELLAASALSRAELLQAVRYVSEVIDLAMEIMSR 149
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 310-465 1.56e-62

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: 200.09  E-value: 1.56e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 310 DTLTLLLNRRFLPTILRHEISLTMHSNTPLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVFRYGGEE 389
Cdd:cd01949    3 DPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 852028170 390 FLIVLIETPKVAAHTIIERLRKKIENHSIHlqNGESVKMTISAGIAVYSGHP-DYECLIKAADDALYQAKANGRNRI 465
Cdd:cd01949   83 FAILLPGTDLEEAEALAERLREAIEEPFFI--DGQEIRVTASIGIATYPEDGeDAEELLRRADEALYRAKRSGRNRV 157
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 310-468 8.27e-60

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: 197.51  E-value: 8.27e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 310 DTLTLLLNRRFLPTILRHEISLTMHSNTPLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVFRYGGEE 389
Cdd:COG2199  117 DPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDE 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 390 FLIVLIETPKVAAHTIIERLRKKIENHSIHLqNGESVKMTISAGIAVYSGHP-DYECLIKAADDALYQAKANGRNRIEYA 468
Cdd:COG2199  197 FAVLLPGTDLEEAEALAERLREALEQLPFEL-EGKELRVTVSIGVALYPEDGdSAEELLRRADLALYRAKRAGRNRVVVY 275
GS_EcDosC-like_GGDEF cd14757
Globin sensor domain of Escherichia coli Direct Oxygen Sensing Cyclase and related proteins; ...
 20-167 2.22e-58

Globin sensor domain of Escherichia coli Direct Oxygen Sensing Cyclase and related proteins; coupled to a C-terminal GGDEF domain; Globin-coupled-sensors belonging to this subfamily have a C-terminal diguanylate cyclase (DGC/GGDEF) domain coupled to the globin sensor domain. DGC/GGDEF likely functions as a c-di-GMP cyclase in the synthesis of the second messenger cyclic-di-GMP (c-di-GMP). Members include Escherichia coli DosC (also known as YddV), the gene for which is found in a two-gene operon, dosCP. In DosC, the sensory globin domain is coupled to a GGDEF-class diguanylate cyclase, while in DosP, a heme-containing PAS domain is coupled to an EAL-class c-di-GMP phosphodiesterase. DosP and DosC associate in a di-GMP-responsive Escherichia coli RNA processing complex along with polynucleotide phosphorylase (PNPase), enolase, RNase E, and RNA.


Pssm-ID: 381271  Cd Length: 149  Bit Score: 188.98  E-value: 2.22e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170  20 QVITSEWTQLIATTSQQSFNLLRTLADQKASDFADEFYTYMLKDQEASLFLSSQQVHDRLHGSMSKWIAAILT-NTGDHL 98
Cdd:cd14757    1 ERLAAEWQALLQQVSPAVRALVAALVQAHADALAAEFYDTMLADPEASPFLSHEQVQTRLHASLQRWLIELFSaADDEDL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 852028170  99 ADLISHQKKIGQIHARIGIPVDLVERGARRLKWHLYEDIAQVADDKALCFDAMRFASISMDIAIEIMSK 167
Cdd:cd14757   81 EALVARQRKVGEVHARIGIPVHLVMRGARVLKRRLAELLAASALSRAELLQAVRYVSEVIDLAMEIMSR 149
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 310-464 4.49e-56

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: 183.61  E-value: 4.49e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170  310 DTLTLLLNRRFLPTILRHEISLTMHSNTPLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVFRYGGEE 389
Cdd:pfam00990   4 DPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGGDE 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 852028170  390 FLIVLIETPKVAAHTIIERLRKKIENHSI-HLQNGESVKMTISAGIAVYS-GHPDYECLIKAADDALYQAKANGRNR 464
Cdd:pfam00990  84 FAILLPETSLEGAQELAERIRRLLAKLKIpHTVSGLPLYVTISIGIAAYPnDGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 310-468 7.53e-56

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: 183.31  E-value: 7.53e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170  310 DTLTLLLNRRFLPTILRHEISLTMHSNTPLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVFRYGGEE 389
Cdd:TIGR00254   5 DPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGEE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170  390 FLIVLIETPKVAAHTIIERLRKKIENHSIHLQNGESVKMTISAGIAVYSGHP-DYECLIKAADDALYQAKANGRNRIEYA 468
Cdd:TIGR00254  85 FVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYPGHGlTLEELLKRADEALYQAKKAGRNRVVVA 164
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 310-468 8.16e-51

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 169.74  E-value: 8.16e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170   310 DTLTLLLNRRFLPTILRHEISLTMHSNTPLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVFRYGGEE 389
Cdd:smart00267   6 DPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLGGDE 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170   390 FLIVLIETPKVAAHTIIERLRKKIENHSIhlQNGESVKMTISAGIAVYS-GHPDYECLIKAADDALYQAKANGRNRIEYA 468
Cdd:smart00267  86 FALLLPETSLEEAIALAERILQQLREPII--IHGIPLYLTISIGVAAYPnPGEDAEDLLKRADTALYQAKKAGRNQVAVY 163
pleD PRK09581
response regulator PleD; Reviewed
 309-465 6.71e-47

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 168.16  E-value: 6.71e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 309 KDTLTLLLNRRFLPTILRHEISLTMHSNTPLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVFRYGGE 388
Cdd:PRK09581 294 TDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGE 373

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 852028170 389 EFLIVLIETPKVAAHTIIERLRKKIENHSIHLQNG-ESVKMTISAGIAVYSGHPD-YECLIKAADDALYQAKANGRNRI 465
Cdd:PRK09581 374 EFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGkERLNVTVSIGVAELRPSGDtIEALIKRADKALYEAKNTGRNRV 452
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
307-465 1.63e-44

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 156.30  E-value: 1.63e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 307 SGKDTLTLLLNRRFLPTILRHEISLTMHSNTPLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVFRYG 386
Cdd:NF038266  94 STRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRWG 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 387 GEEFLIVLIETPKVAAHTIIERLRKKIENHSIHLqNGESVKMTISAGIAVY-SGHPDYECLIKAADDALYQAKANGRNRI 465
Cdd:NF038266 174 GEEFLLLLPETGLEEAQVVLERLREAVRALAVRV-GDDVLSVTASAGLAEHrPPEEGLSATLSRADQALYQAKRAGRDRV 252
dguan_cyc_DgcA NF041606
diguanylate cyclase DgcA;
310-465 1.24e-42

diguanylate cyclase DgcA;


Pssm-ID: 469490 [Multi-domain]  Cd Length: 340  Bit Score: 154.14  E-value: 1.24e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 310 DTLTLLLNRRFLPTILRHEISLTMHSNTPLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVFRYGGEE 389
Cdd:NF041606 181 DMMTHLKLKHYFYTVLMEKLDTINSQGEPLSILMLDIDFFKQINDTYGHACGDLVLQMVASIIQSCTRTQDMAARYGGEE 260

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 852028170 390 FLIVLIETPKVAAHTIIERLRKKIENHSIhLQNGESVKMTISAGIAVYSghPDYEC---LIKAADDALYQAKANGRNRI 465
Cdd:NF041606 261 FVVMLSNTSSKTAKKIAERIRKSIENLSI-LYDEQHIRVTISIGVAEYN--FDVESaksLVERADKALYESKQNGRNRV 336
diguan_DgcJ NF040885
diguanylate cyclase DgcJ;
310-462 1.16e-17

diguanylate cyclase DgcJ;


Pssm-ID: 468821 [Multi-domain]  Cd Length: 490  Bit Score: 85.40  E-value: 1.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 310 DTLTLLLNRRFLPTILRHEISLTMHSNTPLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVFRYGGEE 389
Cdd:NF040885 344 DSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGIRLGGDE 423

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 390 FLIVLIETPKVAAHTIIERLRKKIENH-----------SIHLQNGESVkmtisagiavysghpdyECLIKAADDALYQAK 458
Cdd:NF040885 424 FCIILIDYEEAEAQNLIERIRQHLRTIdpdkrvsfswgAYQMQPGDTL-----------------DDAYKAADERLYLNK 486


                 ....
gi 852028170 459 ANGR 462
Cdd:NF040885 487 KQKH 490
Protoglobin pfam11563
Protoglobin; This family includes protoglobin from Methanosarcina acetivorans C2A. It is also ...
 30-167 7.74e-11

Protoglobin; This family includes protoglobin from Methanosarcina acetivorans C2A. It is also found near the N-terminus of the Haem-based aerotactic transducer HemAT in Bacillus subtilis. It is part of the haemoglobin superfamily. Protoglobin has specific loops and an amino-terminal extension which leads to the burying of the haem within the matrix of the protein. Protoglobin-specific apolar tunnels allow the access of O2, CO and NO to the haem distal site. In HemAT it acts as an oxygen sensor domain. It can also recognize cyanide (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 431935 [Multi-domain]  Cd Length: 149  Bit Score: 60.29  E-value: 7.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170   30 IATTSQQSFNLLRTLADQKASDFADEFYTYMLKDQEASLFLSSQQVHDRLHGSMSKWIAAILTntGDHLADLISHQKKIG 109
Cdd:pfam11563  13 FTEEDLAALRALRPLIEPHIPAIVDAFYDKLLSFPETARIFTTSSQIERLKDTLKAYLLRLFS--GPYDEAYVEYRLKIG 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 852028170  110 QIHARIGIPVDLVERGARRLKWHLYEDIAQ-VADDKALCFDAMRFASISMDIAIEIMSK 167
Cdd:pfam11563  91 KMHVRLGLEPRWYIAAYALILEGLLEALLEkIKLSAAEKSALVRALSKLINLDQDLVLE 149
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 310-465 1.56e-62

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: 200.09  E-value: 1.56e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 310 DTLTLLLNRRFLPTILRHEISLTMHSNTPLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVFRYGGEE 389
Cdd:cd01949    3 DPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 852028170 390 FLIVLIETPKVAAHTIIERLRKKIENHSIHlqNGESVKMTISAGIAVYSGHP-DYECLIKAADDALYQAKANGRNRI 465
Cdd:cd01949   83 FAILLPGTDLEEAEALAERLREAIEEPFFI--DGQEIRVTASIGIATYPEDGeDAEELLRRADEALYRAKRSGRNRV 157
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 310-468 8.27e-60

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: 197.51  E-value: 8.27e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 310 DTLTLLLNRRFLPTILRHEISLTMHSNTPLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVFRYGGEE 389
Cdd:COG2199  117 DPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDE 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 390 FLIVLIETPKVAAHTIIERLRKKIENHSIHLqNGESVKMTISAGIAVYSGHP-DYECLIKAADDALYQAKANGRNRIEYA 468
Cdd:COG2199  197 FAVLLPGTDLEEAEALAERLREALEQLPFEL-EGKELRVTVSIGVALYPEDGdSAEELLRRADLALYRAKRAGRNRVVVY 275
GS_EcDosC-like_GGDEF cd14757
Globin sensor domain of Escherichia coli Direct Oxygen Sensing Cyclase and related proteins; ...
 20-167 2.22e-58

Globin sensor domain of Escherichia coli Direct Oxygen Sensing Cyclase and related proteins; coupled to a C-terminal GGDEF domain; Globin-coupled-sensors belonging to this subfamily have a C-terminal diguanylate cyclase (DGC/GGDEF) domain coupled to the globin sensor domain. DGC/GGDEF likely functions as a c-di-GMP cyclase in the synthesis of the second messenger cyclic-di-GMP (c-di-GMP). Members include Escherichia coli DosC (also known as YddV), the gene for which is found in a two-gene operon, dosCP. In DosC, the sensory globin domain is coupled to a GGDEF-class diguanylate cyclase, while in DosP, a heme-containing PAS domain is coupled to an EAL-class c-di-GMP phosphodiesterase. DosP and DosC associate in a di-GMP-responsive Escherichia coli RNA processing complex along with polynucleotide phosphorylase (PNPase), enolase, RNase E, and RNA.


Pssm-ID: 381271  Cd Length: 149  Bit Score: 188.98  E-value: 2.22e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170  20 QVITSEWTQLIATTSQQSFNLLRTLADQKASDFADEFYTYMLKDQEASLFLSSQQVHDRLHGSMSKWIAAILT-NTGDHL 98
Cdd:cd14757    1 ERLAAEWQALLQQVSPAVRALVAALVQAHADALAAEFYDTMLADPEASPFLSHEQVQTRLHASLQRWLIELFSaADDEDL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 852028170  99 ADLISHQKKIGQIHARIGIPVDLVERGARRLKWHLYEDIAQVADDKALCFDAMRFASISMDIAIEIMSK 167
Cdd:cd14757   81 EALVARQRKVGEVHARIGIPVHLVMRGARVLKRRLAELLAASALSRAELLQAVRYVSEVIDLAMEIMSR 149
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 310-464 4.49e-56

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: 183.61  E-value: 4.49e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170  310 DTLTLLLNRRFLPTILRHEISLTMHSNTPLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVFRYGGEE 389
Cdd:pfam00990   4 DPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGGDE 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 852028170  390 FLIVLIETPKVAAHTIIERLRKKIENHSI-HLQNGESVKMTISAGIAVYS-GHPDYECLIKAADDALYQAKANGRNR 464
Cdd:pfam00990  84 FAILLPETSLEGAQELAERIRRLLAKLKIpHTVSGLPLYVTISIGIAAYPnDGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 310-468 7.53e-56

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: 183.31  E-value: 7.53e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170  310 DTLTLLLNRRFLPTILRHEISLTMHSNTPLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVFRYGGEE 389
Cdd:TIGR00254   5 DPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGEE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170  390 FLIVLIETPKVAAHTIIERLRKKIENHSIHLQNGESVKMTISAGIAVYSGHP-DYECLIKAADDALYQAKANGRNRIEYA 468
Cdd:TIGR00254  85 FVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYPGHGlTLEELLKRADEALYQAKKAGRNRVVVA 164
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 310-468 8.16e-51

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 169.74  E-value: 8.16e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170   310 DTLTLLLNRRFLPTILRHEISLTMHSNTPLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVFRYGGEE 389
Cdd:smart00267   6 DPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLGGDE 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170   390 FLIVLIETPKVAAHTIIERLRKKIENHSIhlQNGESVKMTISAGIAVYS-GHPDYECLIKAADDALYQAKANGRNRIEYA 468
Cdd:smart00267  86 FALLLPETSLEEAIALAERILQQLREPII--IHGIPLYLTISIGVAAYPnPGEDAEDLLKRADTALYQAKKAGRNQVAVY 163
pleD PRK09581
response regulator PleD; Reviewed
 309-465 6.71e-47

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 168.16  E-value: 6.71e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 309 KDTLTLLLNRRFLPTILRHEISLTMHSNTPLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVFRYGGE 388
Cdd:PRK09581 294 TDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGE 373

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 852028170 389 EFLIVLIETPKVAAHTIIERLRKKIENHSIHLQNG-ESVKMTISAGIAVYSGHPD-YECLIKAADDALYQAKANGRNRI 465
Cdd:PRK09581 374 EFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGkERLNVTVSIGVAELRPSGDtIEALIKRADKALYEAKNTGRNRV 452
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
307-465 1.63e-44

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 156.30  E-value: 1.63e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 307 SGKDTLTLLLNRRFLPTILRHEISLTMHSNTPLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVFRYG 386
Cdd:NF038266  94 STRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRWG 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 387 GEEFLIVLIETPKVAAHTIIERLRKKIENHSIHLqNGESVKMTISAGIAVY-SGHPDYECLIKAADDALYQAKANGRNRI 465
Cdd:NF038266 174 GEEFLLLLPETGLEEAQVVLERLREAVRALAVRV-GDDVLSVTASAGLAEHrPPEEGLSATLSRADQALYQAKRAGRDRV 252
dguan_cyc_DgcA NF041606
diguanylate cyclase DgcA;
310-465 1.24e-42

diguanylate cyclase DgcA;


Pssm-ID: 469490 [Multi-domain]  Cd Length: 340  Bit Score: 154.14  E-value: 1.24e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 310 DTLTLLLNRRFLPTILRHEISLTMHSNTPLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVFRYGGEE 389
Cdd:NF041606 181 DMMTHLKLKHYFYTVLMEKLDTINSQGEPLSILMLDIDFFKQINDTYGHACGDLVLQMVASIIQSCTRTQDMAARYGGEE 260

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 852028170 390 FLIVLIETPKVAAHTIIERLRKKIENHSIhLQNGESVKMTISAGIAVYSghPDYEC---LIKAADDALYQAKANGRNRI 465
Cdd:NF041606 261 FVVMLSNTSSKTAKKIAERIRKSIENLSI-LYDEQHIRVTISIGVAEYN--FDVESaksLVERADKALYESKQNGRNRV 336
PRK09894 PRK09894
diguanylate cyclase; Provisional
 203-470 3.93e-41

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 148.68  E-value: 3.93e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 203 LLNWENAFIFSVATGTPLSSIQDLSDSDFGLWFNHKGKSSFSNIQGIRTIAT----IMTETDEYIRNYSHtALLTQQDYA 278
Cdd:PRK09894  26 LVSMFRSVVARDASKPEITDNHSHGLCQFGRWIDHLGPLDNDELPYVRLLDSahqhMHNCARELLLAIVE-GHWQDAHFD 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 279 pllkAVRSKIYKINMLLGSLFDEVQKLESGKDTLTLLLNRRFLPTILRHeiSLTMHSNTPLSIAMIDIDHFKSVNDTYGH 358
Cdd:PRK09894 105 ----AFQEGLLSFTAALTDYKIYLLTIRSNMDVLTGLPGRRVLDESFDH--QLRNREPQNLYLALLDIDRFKLVNDTYGH 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 359 AAGDNILKRIAEILYESTRNSDYVFRYGGEEFLIVLIETPKVAAHTIIERLRKKIENHSIHLQNGEsVKMTISAGIAVYS 438
Cdd:PRK09894 179 LIGDVVLRTLATYLASWTRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGR-INITATFGVSRAF 257

                        250       260       270
                 ....*....|....*....|....*....|..
gi 852028170 439 GHPDYECLIKAADDALYQAKANGRNRIEYAPE 470
Cdd:PRK09894 258 PEETLDVVIGRADRAMYEGKQTGRNRVMFIDE 289
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 310-470 3.00e-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: 153.39  E-value: 3.00e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 310 DTLTLLLNRRFLPTILRHEISLTMHSNTPLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVFRYGGEE 389
Cdd:COG5001  254 DPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDE 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 390 FLIVL--IETPKVA---AHTIIERLRK--KIENHSIHLqngesvkmTISAGIAVYSGH-PDYECLIKAADDALYQAKANG 461
Cdd:COG5001  334 FAVLLpdLDDPEDAeavAERILAALAEpfELDGHELYV--------SASIGIALYPDDgADAEELLRNADLAMYRAKAAG 405

                        170
                 ....*....|
gi 852028170 462 RNRIE-YAPE 470
Cdd:COG5001  406 RNRYRfFDPE 415
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
310-465 6.95e-36

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 139.76  E-value: 6.95e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 310 DTLTLLLNRRFLPTILRHEISLTMHSNTPLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVFRYGGEE 389
Cdd:PRK15426 401 DPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEE 480

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 852028170 390 FLIVLIETPKVAAHTIIERLRKKIENHSIHLQNGESVKMTISAGIAVYSGHPDY--ECLIKAADDALYQAKANGRNRI 465
Cdd:PRK15426 481 FCVVLPGASLAEAAQVAERIRLRINEKEILVAKSTTIRISASLGVSSAEEDGDYdfEQLQSLADRRLYLAKQAGRNRV 558
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 304-468 1.46e-29

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 118.78  E-value: 1.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 304 KLESGKDTLTLLLNRRFLPTILRHEISLTMHSNTPLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVF 383
Cdd:PRK10245 202 QVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIG 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 384 RYGGEEFLIVLIETPKVAAHTIIERLRKKIEnhSIHLQNGESVKMTISAGIAVYS---GHpdYECLIKAADDALYQAKAN 460
Cdd:PRK10245 282 RFGGDEFAVIMSGTPAESAITAMSRVHEGLN--TLRLPNAPQVTLRISVGVAPLNpqmSH--YREWLKSADLALYKAKNA 357


                 ....*...
gi 852028170 461 GRNRIEYA 468
Cdd:PRK10245 358 GRNRTEVA 365
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
310-462 2.36e-19

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 90.90  E-value: 2.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 310 DTLTLLLNRRFLPTILRHEISLTMhsNTPLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVFRYGGEE 389
Cdd:PRK10060 240 DSITGLPNRNAIQELIDHAINAAD--NNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDE 317

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 852028170 390 FlIVLIETPKVA-----AHTIIERLRKKIENHSIHLQNGESVkmtisaGIAVYSGH-PDYECLIKAADDALYQAKANGR 462
Cdd:PRK10060 318 F-LVLASHTSQAaleamASRILTRLRLPFRIGLIEVYTGCSI------GIALAPEHgDDSESLIRSADTAMYTAKEGGR 389
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 310-465 2.46e-18

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 88.19  E-value: 2.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170  310 DTLTLLLNRRFLPTILRHEISLTMHSNTPLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVFRYGGEE 389
Cdd:PRK09776  668 DALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDE 747

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 852028170  390 FLIVLIETPKVAAHTIIERLRKKIENHSIHLQnGESVKMTISAGIAVY--SGHPDYEcLIKAADDALYQAKANGRNRI 465
Cdd:PRK09776  748 FGLLLPDCNVESARFIATRIISAINDYHFPWE-GRVYRVGASAGITLIdaNNHQASE-VMSQADIACYAAKNAGRGRV 823
diguan_DgcJ NF040885
diguanylate cyclase DgcJ;
310-462 1.16e-17

diguanylate cyclase DgcJ;


Pssm-ID: 468821 [Multi-domain]  Cd Length: 490  Bit Score: 85.40  E-value: 1.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 310 DTLTLLLNRRFLPTILRHEISLTMHSNTPLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVFRYGGEE 389
Cdd:NF040885 344 DSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGIRLGGDE 423

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 390 FLIVLIETPKVAAHTIIERLRKKIENH-----------SIHLQNGESVkmtisagiavysghpdyECLIKAADDALYQAK 458
Cdd:NF040885 424 FCIILIDYEEAEAQNLIERIRQHLRTIdpdkrvsfswgAYQMQPGDTL-----------------DDAYKAADERLYLNK 486


                 ....
gi 852028170 459 ANGR 462
Cdd:NF040885 487 KQKH 490
PRK09966 PRK09966
diguanylate cyclase DgcN;
310-458 7.38e-17

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 82.36  E-value: 7.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 310 DTLTLLLNRrflpTILRHEISLTMHSNTPLS---IAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVFRYG 386
Cdd:PRK09966 251 DPLTGLANR----AAFRSGINTLMNNSDARKtsaLLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLG 326

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 852028170 387 GEEFLIVLIEtpkVAAHTIIERL---RKKIENHSIHLQNGESVKMTISAGIAVYSGHPDYECLIKAADDALYQAK 458
Cdd:PRK09966 327 GDEFAMVLYD---VQSESEVQQIcsaLTQIFNLPFDLHNGHQTTMTLSIGYAMTIEHASAEKLQELADHNMYQAK 398
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 338-460 1.11e-16

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: 76.24  E-value: 1.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 338 PLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYES-TRNSDYVFRYGGEEFLIVLIETPKVAAHTIIERLRKKIENH 416
Cdd:cd07556    1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLiRRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 852028170 417 SIHLQNGESVKMTISAGIA---VYSGHPDY---ECLIKAADDALYQAKAN 460
Cdd:cd07556   81 NQSEGNPVRVRIGIHTGPVvvgVIGSRPQYdvwGALVNLASRMESQAKAG 130
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 380-458 7.15e-15

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: 72.63  E-value: 7.15e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 852028170 380 DYVFRYGGEEFLIVLIETPKVAAHTIIERLRKKIENHsihlqngESVKMTISAGIAVYSghpdyecLIKAAdDALYQAK 458
Cdd:COG3706  116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAEL-------PSLRVTVSIGVAGDS-------LLKRA-DALYQAR 179
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 310-463 5.05e-12

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 68.26  E-value: 5.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170 310 DTLTLLLNRRFLptilRHEISLTMHSNTPLSIAMIDIDHFKSVNDTYGHAAGDNILKRIAEILYESTRNSDYVFRYGGEE 389
Cdd:PRK11359 379 DPLTGLPNRNNL----HNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQ 454

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 852028170 390 FLIVLIETPKVAAHTIIERLRkKIENHSIHLqNGESVKMTISAGIAvYSGHPDYECLIKAADDALYQAKANGRN 463
Cdd:PRK11359 455 FVLVSLENDVSNITQIADELR-NVVSKPIMI-DDKPFPLTLSIGIS-YDVGKNRDYLLSTAHNAMDYIRKNGGN 525
GS_GsGCS-like cd14761
Globin sensor domain of Geobacter sulfurreducens globin-coupled-sensor and related proteins; ...
 41-169 6.43e-12

Globin sensor domain of Geobacter sulfurreducens globin-coupled-sensor and related proteins; GsGCS is a GCS of unknown function, comprised of an N-terminal globin sensor domain and a C- terminal transmembrane signal-transduction domain. For GCSs in general, the first signal O2 binds to/dissociates from the heme iron complex inducing a structural change in the globin domain, which is then transduced to the functional domain, switching on (or off) the function of the latter. Ferric GsGCS is bis-histidyl hexa-coordinated (provided by a His residue located at the E11 topological site, as distinct from the E7 site). Ferrous GsGCS is a penta- and hexa-coordinated mixture. The C-terminal domains of other members of this subfamily include histidine kinase, and PsiE domains.


Pssm-ID: 381274  Cd Length: 149  Bit Score: 63.08  E-value: 6.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170  41 LRTLADQKASDFADEFYTYMLKDQEASLFLSSQQVHDRLHGSMSKWIAAILtnTGDHLADLISHQKKIGQIHARIGIPVD 120
Cdd:cd14761   23 LKPLMEKNKDRFVEDFYEYLFKFPDTAKFLKDDEVLKRHKEKLKVWFIRLF--SGKYDNQYFDYLQRIGQVHVRIGLPTH 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 852028170 121 LVERGARRLKWHLYEDIAQVADDKALCFDAMRFASISMDIAIEIMSKTY 169
Cdd:cd14761  101 YVNAAMNFVRRFFHEKIFQEFSDDEKRKKLLESVEKILDINLDIMTSSY 149
Protoglobin pfam11563
Protoglobin; This family includes protoglobin from Methanosarcina acetivorans C2A. It is also ...
 30-167 7.74e-11

Protoglobin; This family includes protoglobin from Methanosarcina acetivorans C2A. It is also found near the N-terminus of the Haem-based aerotactic transducer HemAT in Bacillus subtilis. It is part of the haemoglobin superfamily. Protoglobin has specific loops and an amino-terminal extension which leads to the burying of the haem within the matrix of the protein. Protoglobin-specific apolar tunnels allow the access of O2, CO and NO to the haem distal site. In HemAT it acts as an oxygen sensor domain. It can also recognize cyanide (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 431935 [Multi-domain]  Cd Length: 149  Bit Score: 60.29  E-value: 7.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170   30 IATTSQQSFNLLRTLADQKASDFADEFYTYMLKDQEASLFLSSQQVHDRLHGSMSKWIAAILTntGDHLADLISHQKKIG 109
Cdd:pfam11563  13 FTEEDLAALRALRPLIEPHIPAIVDAFYDKLLSFPETARIFTTSSQIERLKDTLKAYLLRLFS--GPYDEAYVEYRLKIG 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 852028170  110 QIHARIGIPVDLVERGARRLKWHLYEDIAQ-VADDKALCFDAMRFASISMDIAIEIMSK 167
Cdd:pfam11563  91 KMHVRLGLEPRWYIAAYALILEGLLEALLEkIKLSAAEKSALVRALSKLINLDQDLVLE 149
globin_sensor cd01068
Globin sensor domain of globin-coupled-sensors (GCSs), protoglobins (Pgbs), and sensor ...
 41-163 8.85e-11

Globin sensor domain of globin-coupled-sensors (GCSs), protoglobins (Pgbs), and sensor single-domain globins (SSDgbs); S family; This family includes sensor domains which binds porphyrins, and other non-heme cofactors. GCSs have an N-terminal sensor domain coupled to a functional domain. For heme-bound oxygen sensing/binding globin domains, O2 binds to/dissociates from the heme iron complex inducing a structural change in the sensor domain, which is then transduced to the functional domain, switching on (or off) the function of the latter. Functional domains include DGC/GGDEF, EAL, histidine kinase, MCP, PAS, and GAF domains. Characterized members include Bacillus subtilis heme-based aerotaxis transducer (HemAT-Bs) which has a sensor domain coupled to an MCP domain. HemAT-Bs mediates an aerophilic response, and may control the movement direction of bacteria and archaea. Its MCP domain interacts with the CheA histidine kinase, a component of the CheA/CheY signal transduction system that regulates the rotational direction of flagellar motors. Another GCS having the sensor domain coupled to an MCP domain is Caulobacter crescentus McpB. McpB is encoded by a gene which lies adjacent to the major chemotaxis operon. Like McpA (encoded on this operon), McpB has three potential methylation sites, a C-terminal CheBR docking motif, and a motif needed for proteolysis via a ClpX-dependent pathway during the swarmer-to-stalked cell transition. Also included is Geobacter sulfurreducens GCS, a GCS of unknown function, in which the sensor domain is coupled to a transmembrane signal-transduction domain. Pgbs are single-domain globins of unknown function. Methanosarcina acetivorans Pgbs is dimeric and has an N-terminal extension, which together with other Pgb-specific loops, buries the heme within the protein; small ligand molecules gain access to the heme via two orthogonal apolar tunnels. Pgbs and other single-domain globins can function as sensors, when coupled to an appropriate regulator domain.


Pssm-ID: 381256 [Multi-domain]  Cd Length: 146  Bit Score: 59.90  E-value: 8.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170  41 LRTLADQKASDFADEFYTYMLKDQEASLFLSSQQVHDRLHGSMSKWIAAILtnTGDHLADLISHQKKIGQIHARIGIPVD 120
Cdd:cd01068   19 LRPLIEPHLDEILDAFYDHLLSFPELAAIFDDHSTIERLKQTQRAHWLELF--SGDFDEAYVERRRRIGRVHVRIGLEPR 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 852028170 121 LVERGARRLKWHLYEDIAQ-VADDKALCFDAM----RFASISMDIAIE 163
Cdd:cd01068   97 WYIGAYALLLEELIEIIAEeLRKDPEELAELLlalvKALNLDMQLALE 144
SSDgbs_1 cd14763
Sensor single-domain globins; uncharacterized bacterial subgroup; This subfamily of sensor ...
 40-119 2.84e-08

Sensor single-domain globins; uncharacterized bacterial subgroup; This subfamily of sensor single-domain globins, belongs to a family that includes GCSs (globin-coupled-sensors) and single-domain protoglobins (Pgbs). For GCSs, an N-terminal heme-bound oxygen-sensing/binding globin domain is coupled to a C-terminal functional/signaling domain. The first signal O2 binds to/dissociates from the heme in its sensor domain inducing a conformational change in that domain and ultimately in the signaling domain. It has been demonstrated that the Pgbs and other single domain globins can function as sensors, when coupled to an appropriate regulatory domain.


Pssm-ID: 381276  Cd Length: 144  Bit Score: 52.77  E-value: 2.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170  40 LLRTL---ADQKASDFADEFYTYMLKDQEASLFLSSQQVH-DRLHGSMSKWIAAILTntGDHLADLISHQKKIGQIHARI 115
Cdd:cd14763   17 LLGSLapiAKEIAPQMADAFYDYLGRDPETAEILAAVPGRvERLHKTFANWFRELFS--GQYDAAYAERRLRIGLVHVRI 94


                 ....
gi 852028170 116 GIPV 119
Cdd:cd14763   95 GLPP 98
GS_GGDEF_1 cd14758
Globin sensor domain, coupled to DGC/GGDEF domains; uncharacterized subgroup; ...
 41-147 7.80e-07

Globin sensor domain, coupled to DGC/GGDEF domains; uncharacterized subgroup; Globin-coupled-sensors belonging to this subfamily have a sensor domain coupled to a C-terminal diguanylate cyclase (DGC/GGDEF) domain. DGC/GGDEF likely functions as a c-di-GMP cyclase in the synthesis of the second messenger cyclic-di-GMP (c-di-GMP).


Pssm-ID: 381272 [Multi-domain]  Cd Length: 148  Bit Score: 48.46  E-value: 7.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170  41 LRTLADQKASDFADEFYTYMLKDQEASLFLSSQQVHDRLHGSMSKWIAAILTNTGDhlADLISHQKKIGQIHARIGIPVD 120
Cdd:cd14758   22 LKPLIEPNLDDIVDEFYDHQTSVPEIALLIGDADTLQRLKNAQRQYVLDLFSGEYD--LEYVNNRLRIGLVHKRIGVEPK 99

                         90       100
                 ....*....|....*....|....*..
gi 852028170 121 LVERGARRLKWHLYEDIAQVADDKALC 147
Cdd:cd14758  100 LYLSAINTLKEILFEYIREYIEDCLPA 126
GS_PAS-GGDEF-EAL cd14760
Globin sensor domain; coupled to PAS, DGC/GGDEF and EAL domains; In addition to the N-terminal ...
 46-133 1.16e-05

Globin sensor domain; coupled to PAS, DGC/GGDEF and EAL domains; In addition to the N-terminal sensing domain, globin-coupled-sensors in this bacterial subfamily have a signal-sensing PAS domain, and diguanylate cyclase (DGC/GGDEF) and EAL domains. The latter two domains are involved in the synthesis and degradation of c-di-GMP, respectively, and may be involved in regulating cell surface adhesiveness, and in the transition between planktonic and biofilm growth modes.


Pssm-ID: 271293 [Multi-domain]  Cd Length: 148  Bit Score: 45.08  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170  46 DQKASDFADEFYTYMLKDQEASLFLSSQQVHDRLHGSMSKWIAAIltNTGDHLADLISHQKKIGQIHARIGIPvdlverg 125
Cdd:cd14760   26 SSFSPTFADSFYAHLLSFEETRRFLPDEDTLERLQRAQTAYFDSL--TAGRYDSDYIRERLRVGLTHQRIGLS------- 96


                 ....*...
gi 852028170 126 arrLKWHL 133
Cdd:cd14760   97 ---PQWYL 101
GS_STAS cd14762
Globin sensor domain; coupled to a STAS domain; Globin-coupled-sensors in this subfamily have ...
 22-163 6.51e-04

Globin sensor domain; coupled to a STAS domain; Globin-coupled-sensors in this subfamily have a C-terminal sulphate transporter and anti-sigma factor antagonist (STAT) domain coupled to the globin sensor domain.


Pssm-ID: 381275 [Multi-domain]  Cd Length: 143  Bit Score: 39.96  E-value: 6.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 852028170  22 ITSEWTQLIATTSQQSFnllrtlaDQKASDFaDEFYTYMLKDQEASLFLSSQQVH--DRLHGSMSKWIAAiltntGDHLA 99
Cdd:cd14762   10 ISDEDLELIRSAGQQIL-------DQKDWIF-DEFYDWMRSQPEYSEYFSEEVIKrlKSLQDIFWEDFLS-----GRVDD 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 852028170 100 DLISHQKKIGQIHARIGIPVDLVERGARRLKwHLYEDIAQvaDDKALCFDAM----RFASISMDIAIE 163
Cdd:cd14762   77 EYIERRRRIGEVHARIGLPLEAYLAGVAAFH-ELIEEAFR--RLGLASFELMqafkKFIQLDIAIVTD 141
 
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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