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Conserved domains on  [gi|521328933|gb|AGP83040|]
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diguanylate cyclase [Alteromonas mediterranea MED64]

Protein Classification

diguanylate cyclase( domain architecture ID 10542681)

diguanylate cyclase containing the transmembrane region and the extracellular 2 domain of 7TM-DISM (7TM Receptors with Diverse Intracellular Signaling Modules), catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules and may function as a membrane-associated receptor for various signaling molecules such as carbohydrates and their derivatives

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 ...
 274-544 2.57e-63

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: 208.68  E-value: 2.57e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 274 ALAVLIILVGSRSFAVMSQLVVLTTISLWMLAIGIFAYRNGDTLAKFFLPAVLCGTGGATVSSLATWGLVSYSKWAFRGI 353
Cdd:COG2199    2 LLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 354 EIGMVLEMSLLSISLAFNYKQVQQARLSAERDARLDPLTSLYNRRAFEDLVYPIWELGKRSNKHMSVLLIDLDWFKRIND 433
Cdd:COG2199   82 ELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIND 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 434 KFGHDMGDKVLQNVAKEIKGQVRGSDITFRWGGEEFLVFLPNTRANYAKQIAENLRLHLFSHDI---NKLVRVTVSIGVS 510
Cdd:COG2199  162 TYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFeleGKELRVTVSIGVA 241

                        250       260       270
                 ....*....|....*....|....*....|....
gi 521328933 511 GSYPGEDDLNVLIKEADQALYLAKAQGRNKVVLW 544
Cdd:COG2199  242 LYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
7TMR-DISM_7TM pfam07695
7TM diverse intracellular signalling; This entry represents the transmembrane region of the ...
 168-369 1.61e-27

7TM diverse intracellular signalling; This entry represents the transmembrane region of the 7TM-DISM (7TM Receptors with Diverse Intracellular Signalling Modules).


:

Pssm-ID: 429600 [Multi-domain]  Cd Length: 207  Bit Score: 109.67  E-value: 1.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933  168 YFYGALYGSLVILLVYNLVLYSYLKERRYLLYSLYLLSFLAFNFTYTGHGFWWVWSD-SVFLQQWLMPTLMFFYL-FSAV 245
Cdd:pfam07695   3 LLLGLFYGILLALALYNLFLFFSLRDRSYLYYVLYLLSFLLYQLSLNGLGFQYLWPNaPPWLNNKLLYLSLLLLLpFFAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933  246 RFTIEFLNTQLYLPKLYRNRKYIYGGLGALAVLIILVGSRSFAVMSQLVVLTTIsLWMLAIGIFAYRNGDTLAKFFLPAV 325
Cdd:pfam07695  83 LFARSFLELKKYLPRLLRLLLGLALLLALLLLLLPLFPYTLSLPLAQLLALLFI-LFLLLLGIIAWRKGYKPARYFLLAW 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 521328933  326 LCGTGGATVSSLATWGLVSYSKWAFRGIEIGMVLEMSLLSISLA 369
Cdd:pfam07695 162 LLLLIGALIDILSLLGLLPSNFFTNYLLQIGSALEVLLLSLALA 205
7TMR-DISMED2 pfam07696
7TMR-DISM extracellular 2; This entry represents one of two distinct types of extracellular ...
 8-150 4.46e-13

7TMR-DISM extracellular 2; This entry represents one of two distinct types of extracellular domain found in the 7TM-DISM (7TM Receptors with Diverse Intracellular Signalling Modules) bacterial transmembrane proteins. It is possible that this domain adopts a jelly roll fold and acts as a receptor for carbohydrates and their derivatives. It can also recognize Ca(II) (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


:

Pssm-ID: 429601  Cd Length: 127  Bit Score: 66.21  E-value: 4.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933    8 LWMLQESGSALTAEEVMAKYEGRllTKNTVGQVSYGFTNNTIWGVLPVDINTygepvtSDPhnlsesfpfLPLVIEIDNA 87
Cdd:pfam07696   1 VEYLEDPTGSLTIEDVLSADGRF--RPPEKGVPNFGYSSSAYWLRFTLENPT------DAP---------KDWLLELAYP 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521328933   88 WLDDIDVYFFENGERKHHVTLGDNQIHSARAERARMPSVFYRFTQQQTI-VVFRLSSQDPMTIP 150
Cdd:pfam07696  64 LLDEIDLYLPDGGGGYREQRLGDRLPFSQRPVAHRNFVFPLPLPPGETVtLYLRVKSSGSLLLP 127
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 274-544 2.57e-63

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: 208.68  E-value: 2.57e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 274 ALAVLIILVGSRSFAVMSQLVVLTTISLWMLAIGIFAYRNGDTLAKFFLPAVLCGTGGATVSSLATWGLVSYSKWAFRGI 353
Cdd:COG2199    2 LLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 354 EIGMVLEMSLLSISLAFNYKQVQQARLSAERDARLDPLTSLYNRRAFEDLVYPIWELGKRSNKHMSVLLIDLDWFKRIND 433
Cdd:COG2199   82 ELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIND 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 434 KFGHDMGDKVLQNVAKEIKGQVRGSDITFRWGGEEFLVFLPNTRANYAKQIAENLRLHLFSHDI---NKLVRVTVSIGVS 510
Cdd:COG2199  162 TYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFeleGKELRVTVSIGVA 241

                        250       260       270
                 ....*....|....*....|....*....|....
gi 521328933 511 GSYPGEDDLNVLIKEADQALYLAKAQGRNKVVLW 544
Cdd:COG2199  242 LYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 389-542 2.60e-61

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: 198.93  E-value: 2.60e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 389 DPLTSLYNRRAFEDLVYPIWELGKRSNKHMSVLLIDLDWFKRINDKFGHDMGDKVLQNVAKEIKGQVRGSDITFRWGGEE 468
Cdd:cd01949    3 DPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521328933 469 FLVFLPNTRANYAKQIAENLRLHLFSHDI--NKLVRVTVSIGVSGSYPGEDDLNVLIKEADQALYLAKAQGRNKVV 542
Cdd:cd01949   83 FAILLPGTDLEEAEALAERLREAIEEPFFidGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 386-540 1.64e-55

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: 183.99  E-value: 1.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933  386 ARLDPLTSLYNRRAFEDLVYPIWELGKRSNKHMSVLLIDLDWFKRINDKFGHDMGDKVLQNVAKEIKGQVRGSDITFRWG 465
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933  466 GEEFLVFLPNTRANYAKQIAE----NLRLHLFSHDINKLVR-VTVSIGVSGSYPGEDDLNVLIKEADQALYLAKAQGRNK 540
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAErirrLLAKLKIPHTVSGLPLyVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 389-543 9.55e-54

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: 179.46  E-value: 9.55e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933  389 DPLTSLYNRRAFEDLVYPIWELGKRSNKHMSVLLIDLDWFKRINDKFGHDMGDKVLQNVAKEIKGQVRGSDITFRWGGEE 468
Cdd:TIGR00254   5 DPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGEE 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521328933  469 FLVFLPNTRANYAKQIAENLRLHL----FSHDINKLVRVTVSIGVSGSYPGEDDLNVLIKEADQALYLAKAQGRNKVVL 543
Cdd:TIGR00254  85 FVVILPGTPLEDALSKAERLRDAInskpIEVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNRVVV 163
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 386-544 4.88e-52

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 174.74  E-value: 4.88e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933   386 ARLDPLTSLYNRRAFEDLVYPIWELGKRSNKHMSVLLIDLDWFKRINDKFGHDMGDKVLQNVAKEIKGQVRGSDITFRWG 465
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933   466 GEEFLVFLPNTRANYAKQIAENLRLHL----FSHDInkLVRVTVSIGVSGSYPGEDDLNVLIKEADQALYLAKAQGRNKV 541
Cdd:smart00267  83 GDEFALLLPETSLEEAIALAERILQQLrepiIIHGI--PLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQV 160


                   ...
gi 521328933   542 VLW 544
Cdd:smart00267 161 AVY 163
pleD PRK09581
response regulator PleD; Reviewed
 389-542 7.78e-47

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 170.08  E-value: 7.78e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 389 DPLTSLYNRRAFEDLVYPIWELGKRSNKHMSVLLIDLDWFKRINDKFGHDMGDKVLQNVAKEIKGQVRGSDITFRWGGEE 468
Cdd:PRK09581 295 DGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEE 374

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521328933 469 FLVFLPNTRANYAKQIAENLRLHL----FS-HDINKLVRVTVSIGVSGSYPGEDDLNVLIKEADQALYLAKAQGRNKVV 542
Cdd:PRK09581 375 FVVVMPDTDIEDAIAVAERIRRKIaeepFIiSDGKERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGRNRVV 453
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
367-541 3.29e-45

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 159.76  E-value: 3.29e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 367 SLAFNY-KQVQQ----ARLS-------AERDARL------DPLTSLYNRRAFEDLVYPIWELGKRSNKHMSVLLIDLDWF 428
Cdd:NF038266  57 SLAERYdRQLRRlekiVRISdryqrmmRDLNEALreastrDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHF 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 429 KRINDKFGHDMGDKVLQNVAKEIKGQVRGSDITFRWGGEEFLVFLPNTRANYAKQIAENLR-----LHLFshDINKLVRV 503
Cdd:NF038266 137 KRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLReavraLAVR--VGDDVLSV 214

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 521328933 504 TVSIGVSGSYPGEDDLNVLIKEADQALYLAKAQGRNKV 541
Cdd:NF038266 215 TASAGLAEHRPPEEGLSATLSRADQALYQAKRAGRDRV 252
7TMR-DISM_7TM pfam07695
7TM diverse intracellular signalling; This entry represents the transmembrane region of the ...
 168-369 1.61e-27

7TM diverse intracellular signalling; This entry represents the transmembrane region of the 7TM-DISM (7TM Receptors with Diverse Intracellular Signalling Modules).


Pssm-ID: 429600 [Multi-domain]  Cd Length: 207  Bit Score: 109.67  E-value: 1.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933  168 YFYGALYGSLVILLVYNLVLYSYLKERRYLLYSLYLLSFLAFNFTYTGHGFWWVWSD-SVFLQQWLMPTLMFFYL-FSAV 245
Cdd:pfam07695   3 LLLGLFYGILLALALYNLFLFFSLRDRSYLYYVLYLLSFLLYQLSLNGLGFQYLWPNaPPWLNNKLLYLSLLLLLpFFAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933  246 RFTIEFLNTQLYLPKLYRNRKYIYGGLGALAVLIILVGSRSFAVMSQLVVLTTIsLWMLAIGIFAYRNGDTLAKFFLPAV 325
Cdd:pfam07695  83 LFARSFLELKKYLPRLLRLLLGLALLLALLLLLLPLFPYTLSLPLAQLLALLFI-LFLLLLGIIAWRKGYKPARYFLLAW 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 521328933  326 LCGTGGATVSSLATWGLVSYSKWAFRGIEIGMVLEMSLLSISLA 369
Cdd:pfam07695 162 LLLLIGALIDILSLLGLLPSNFFTNYLLQIGSALEVLLLSLALA 205
7TMR-DISMED2 pfam07696
7TMR-DISM extracellular 2; This entry represents one of two distinct types of extracellular ...
 8-150 4.46e-13

7TMR-DISM extracellular 2; This entry represents one of two distinct types of extracellular domain found in the 7TM-DISM (7TM Receptors with Diverse Intracellular Signalling Modules) bacterial transmembrane proteins. It is possible that this domain adopts a jelly roll fold and acts as a receptor for carbohydrates and their derivatives. It can also recognize Ca(II) (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 429601  Cd Length: 127  Bit Score: 66.21  E-value: 4.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933    8 LWMLQESGSALTAEEVMAKYEGRllTKNTVGQVSYGFTNNTIWGVLPVDINTygepvtSDPhnlsesfpfLPLVIEIDNA 87
Cdd:pfam07696   1 VEYLEDPTGSLTIEDVLSADGRF--RPPEKGVPNFGYSSSAYWLRFTLENPT------DAP---------KDWLLELAYP 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521328933   88 WLDDIDVYFFENGERKHHVTLGDNQIHSARAERARMPSVFYRFTQQQTI-VVFRLSSQDPMTIP 150
Cdd:pfam07696  64 LLDEIDLYLPDGGGGYREQRLGDRLPFSQRPVAHRNFVFPLPLPPGETVtLYLRVKSSGSLLLP 127
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 274-544 2.57e-63

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: 208.68  E-value: 2.57e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 274 ALAVLIILVGSRSFAVMSQLVVLTTISLWMLAIGIFAYRNGDTLAKFFLPAVLCGTGGATVSSLATWGLVSYSKWAFRGI 353
Cdd:COG2199    2 LLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 354 EIGMVLEMSLLSISLAFNYKQVQQARLSAERDARLDPLTSLYNRRAFEDLVYPIWELGKRSNKHMSVLLIDLDWFKRIND 433
Cdd:COG2199   82 ELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIND 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 434 KFGHDMGDKVLQNVAKEIKGQVRGSDITFRWGGEEFLVFLPNTRANYAKQIAENLRLHLFSHDI---NKLVRVTVSIGVS 510
Cdd:COG2199  162 TYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFeleGKELRVTVSIGVA 241

                        250       260       270
                 ....*....|....*....|....*....|....
gi 521328933 511 GSYPGEDDLNVLIKEADQALYLAKAQGRNKVVLW 544
Cdd:COG2199  242 LYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 389-542 2.60e-61

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: 198.93  E-value: 2.60e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 389 DPLTSLYNRRAFEDLVYPIWELGKRSNKHMSVLLIDLDWFKRINDKFGHDMGDKVLQNVAKEIKGQVRGSDITFRWGGEE 468
Cdd:cd01949    3 DPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521328933 469 FLVFLPNTRANYAKQIAENLRLHLFSHDI--NKLVRVTVSIGVSGSYPGEDDLNVLIKEADQALYLAKAQGRNKVV 542
Cdd:cd01949   83 FAILLPGTDLEEAEALAERLREAIEEPFFidGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 386-540 1.64e-55

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: 183.99  E-value: 1.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933  386 ARLDPLTSLYNRRAFEDLVYPIWELGKRSNKHMSVLLIDLDWFKRINDKFGHDMGDKVLQNVAKEIKGQVRGSDITFRWG 465
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933  466 GEEFLVFLPNTRANYAKQIAE----NLRLHLFSHDINKLVR-VTVSIGVSGSYPGEDDLNVLIKEADQALYLAKAQGRNK 540
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAErirrLLAKLKIPHTVSGLPLyVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 389-543 9.55e-54

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: 179.46  E-value: 9.55e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933  389 DPLTSLYNRRAFEDLVYPIWELGKRSNKHMSVLLIDLDWFKRINDKFGHDMGDKVLQNVAKEIKGQVRGSDITFRWGGEE 468
Cdd:TIGR00254   5 DPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGEE 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521328933  469 FLVFLPNTRANYAKQIAENLRLHL----FSHDINKLVRVTVSIGVSGSYPGEDDLNVLIKEADQALYLAKAQGRNKVVL 543
Cdd:TIGR00254  85 FVVILPGTPLEDALSKAERLRDAInskpIEVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNRVVV 163
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 386-544 4.88e-52

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 174.74  E-value: 4.88e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933   386 ARLDPLTSLYNRRAFEDLVYPIWELGKRSNKHMSVLLIDLDWFKRINDKFGHDMGDKVLQNVAKEIKGQVRGSDITFRWG 465
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933   466 GEEFLVFLPNTRANYAKQIAENLRLHL----FSHDInkLVRVTVSIGVSGSYPGEDDLNVLIKEADQALYLAKAQGRNKV 541
Cdd:smart00267  83 GDEFALLLPETSLEEAIALAERILQQLrepiIIHGI--PLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQV 160


                   ...
gi 521328933   542 VLW 544
Cdd:smart00267 161 AVY 163
pleD PRK09581
response regulator PleD; Reviewed
 389-542 7.78e-47

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 170.08  E-value: 7.78e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 389 DPLTSLYNRRAFEDLVYPIWELGKRSNKHMSVLLIDLDWFKRINDKFGHDMGDKVLQNVAKEIKGQVRGSDITFRWGGEE 468
Cdd:PRK09581 295 DGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEE 374

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521328933 469 FLVFLPNTRANYAKQIAENLRLHL----FS-HDINKLVRVTVSIGVSGSYPGEDDLNVLIKEADQALYLAKAQGRNKVV 542
Cdd:PRK09581 375 FVVVMPDTDIEDAIAVAERIRRKIaeepFIiSDGKERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGRNRVV 453
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
367-541 3.29e-45

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 159.76  E-value: 3.29e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 367 SLAFNY-KQVQQ----ARLS-------AERDARL------DPLTSLYNRRAFEDLVYPIWELGKRSNKHMSVLLIDLDWF 428
Cdd:NF038266  57 SLAERYdRQLRRlekiVRISdryqrmmRDLNEALreastrDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHF 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 429 KRINDKFGHDMGDKVLQNVAKEIKGQVRGSDITFRWGGEEFLVFLPNTRANYAKQIAENLR-----LHLFshDINKLVRV 503
Cdd:NF038266 137 KRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLReavraLAVR--VGDDVLSV 214

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 521328933 504 TVSIGVSGSYPGEDDLNVLIKEADQALYLAKAQGRNKV 541
Cdd:NF038266 215 TASAGLAEHRPPEEGLSATLSRADQALYQAKRAGRDRV 252
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
386-542 7.72e-44

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 164.03  E-value: 7.72e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 386 ARLDPLTSLYNRRAFEDLVYPIWELGKRSNKHMSVLLIDLDWFKRINDKFGHDMGDKVLQNVAKEIKGQVRGSDITFRWG 465
Cdd:PRK15426 398 AWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVG 477

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 466 GEEFLVFLPNTRANYAKQIAENLRLHLFSHDI----NKLVRVTVSIGVSGSYPGED-DLNVLIKEADQALYLAKAQGRNK 540
Cdd:PRK15426 478 GEEFCVVLPGASLAEAAQVAERIRLRINEKEIlvakSTTIRISASLGVSSAEEDGDyDFEQLQSLADRRLYLAKQAGRNR 557


                 ..
gi 521328933 541 VV 542
Cdd:PRK15426 558 VC 559
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 274-546 1.34e-42

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: 161.87  E-value: 1.34e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 274 ALAVLIILVGSRSFAVMSQLVVLTTISLWMLAIGIFAYRNGDTLAKFFLPAVLCGTGGATVSSLATWGLVSYSKWAFRGI 353
Cdd:COG5001  136 LLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLG 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 354 EIGMVLEMSLLSISLAFNYKQVQQARLSAERDARL---DPLTSLYNRRAFEDLVYPIWELGKRSNKHMSVLLIDLDWFKR 430
Cdd:COG5001  216 LLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLayhDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKE 295

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 431 INDKFGHDMGDKVLQNVAKEIKGQVRGSDITFRWGGEEFLVFLPNTR-ANYAKQIAENLRLHL---FSHDiNKLVRVTVS 506
Cdd:COG5001  296 INDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDdPEDAEAVAERILAALaepFELD-GHELYVSAS 374

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 521328933 507 IGVSgSYPGE-DDLNVLIKEADQALYLAKAQGRNKVVLWNE 546
Cdd:COG5001  375 IGIA-LYPDDgADAEELLRNADLAMYRAKAAGRNRYRFFDP 414
PRK09894 PRK09894
diguanylate cyclase; Provisional
 388-546 1.42e-31

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 123.64  E-value: 1.42e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 388 LDPLTSLYNRRAF-EDLVYPIWELGKRSnkhMSVLLIDLDWFKRINDKFGHDMGDKVLQNVAKEIKGQVRGSDITFRWGG 466
Cdd:PRK09894 131 MDVLTGLPGRRVLdESFDHQLRNREPQN---LYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGG 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 467 EEFLVFLPNTRANYAKQIAENLRLHLFSHDI---NKLVRVTVSIGVSGSYPGEdDLNVLIKEADQALYLAKAQGRNKVVL 543
Cdd:PRK09894 208 EEFIICLKAATDEEACRAGERIRQLIANHAIthsDGRINITATFGVSRAFPEE-TLDVVIGRADRAMYEGKQTGRNRVMF 286


                 ...
gi 521328933 544 WNE 546
Cdd:PRK09894 287 IDE 289
7TMR-DISM_7TM pfam07695
7TM diverse intracellular signalling; This entry represents the transmembrane region of the ...
 168-369 1.61e-27

7TM diverse intracellular signalling; This entry represents the transmembrane region of the 7TM-DISM (7TM Receptors with Diverse Intracellular Signalling Modules).


Pssm-ID: 429600 [Multi-domain]  Cd Length: 207  Bit Score: 109.67  E-value: 1.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933  168 YFYGALYGSLVILLVYNLVLYSYLKERRYLLYSLYLLSFLAFNFTYTGHGFWWVWSD-SVFLQQWLMPTLMFFYL-FSAV 245
Cdd:pfam07695   3 LLLGLFYGILLALALYNLFLFFSLRDRSYLYYVLYLLSFLLYQLSLNGLGFQYLWPNaPPWLNNKLLYLSLLLLLpFFAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933  246 RFTIEFLNTQLYLPKLYRNRKYIYGGLGALAVLIILVGSRSFAVMSQLVVLTTIsLWMLAIGIFAYRNGDTLAKFFLPAV 325
Cdd:pfam07695  83 LFARSFLELKKYLPRLLRLLLGLALLLALLLLLLPLFPYTLSLPLAQLLALLFI-LFLLLLGIIAWRKGYKPARYFLLAW 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 521328933  326 LCGTGGATVSSLATWGLVSYSKWAFRGIEIGMVLEMSLLSISLA 369
Cdd:pfam07695 162 LLLLIGALIDILSLLGLLPSNFFTNYLLQIGSALEVLLLSLALA 205
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 326-540 8.31e-26

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 108.76  E-value: 8.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 326 LCGTGGATVSSLATWGLVSYSKwAFRGIEIGMVLEMSLLSI-SLAFNYKQVQQARLSAERDARL------DPLTSLYNRR 398
Cdd:PRK10245 139 VAGLVLMVVSCLVTLELTGITV-SFNSAPLEWWLSLPVIVIyPLLFAWVSYQTATKLAEHKRRLqvmstrDGMTGVYNRR 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 399 AFEDLVYPIWELGKRSNKHMSVLLIDLDWFKRINDKFGHDMGDKVLQNVAKEIKGQVRGSDITFRWGGEEFLVFLPNTRA 478
Cdd:PRK10245 218 HWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPA 297

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521328933 479 NYAkqIAENLRLHlfsHDINKL-------VRVTVSIGVSGSYPGEDDLNVLIKEADQALYLAKAQGRNK 540
Cdd:PRK10245 298 ESA--ITAMSRVH---EGLNTLrlpnapqVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKNAGRNR 361
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
377-540 3.42e-19

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 91.28  E-value: 3.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 377 QARLSAErdARLDPLTSLYNRRAFEDLVYPiwELGKRSNKHMSVLLIDLDWFKRINDKFGHDMGDKVLQNVAKEIKGQVR 456
Cdd:PRK10060 230 QERLRIL--ANTDSITGLPNRNAIQELIDH--AINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLE 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 457 GSDITFRWGGEEFLVFLPNTRAN----YAKQIAENLRL--HLfshdinKLVRV--TVSIGVSGSYPGEDDLNVLIKEADQ 528
Cdd:PRK10060 306 EDQTLARLGGDEFLVLASHTSQAaleaMASRILTRLRLpfRI------GLIEVytGCSIGIALAPEHGDDSESLIRSADT 379

                        170
                 ....*....|..
gi 521328933 529 ALYLAKAQGRNK 540
Cdd:PRK10060 380 AMYTAKEGGRGQ 391
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 351-549 1.08e-17

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 87.04  E-value: 1.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933  351 RGIEIGMVLEMSLLSISLAFnykqvqQARLSaeRDARLDPLTSLYNRRAFEDLVYPIWELGKRSNKHMSVLLIDLDWFKR 430
Cdd:PRK09776  638 DGENIGSVLVIQDVTESRKM------LRQLS--YSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKA 709

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933  431 INDKFGHDMGDKVLQNVAKEIKGQVRGSDITFRWGGEEFLVFLPNTRANYAKQIAENLrlhlfSHDIN--------KLVR 502
Cdd:PRK09776  710 VNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRI-----ISAINdyhfpwegRVYR 784

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 521328933  503 VTVSIGV----SGSYPGEDdlnvLIKEADQALYLAKAQGRNKVVLWNERKE 549
Cdd:PRK09776  785 VGASAGItlidANNHQASE----VMSQADIACYAAKNAGRGRVTVYEPQQA 831
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 419-542 1.20e-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: 76.63  E-value: 1.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 419 SVLLIDLDWFKRINDKFGHDMGDKVLQNVAKEIKGQV-RGSDITFRWGGEEFLVFLPNTRANYAKQIAENLRLHLFSHDI 497
Cdd:cd07556    3 TILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSALNQ 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 521328933 498 NKLVRVTVSIGVS---------GSYPGEDDLNVLIKEADQALYLAKAqgrNKVV 542
Cdd:cd07556   83 SEGNPVRVRIGIHtgpvvvgviGSRPQYDVWGALVNLASRMESQAKA---GQVL 133
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 459-534 1.14e-13

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: 69.17  E-value: 1.14e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521328933 459 DITFRWGGEEFLVFLPNTRANYAKQIAENLRLHLFSHdinKLVRVTVSIGVSGSypgeddlnVLIKEADqALYLAK 534
Cdd:COG3706  116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAEL---PSLRVTVSIGVAGD--------SLLKRAD-ALYQAR 179
7TMR-DISMED2 pfam07696
7TMR-DISM extracellular 2; This entry represents one of two distinct types of extracellular ...
 8-150 4.46e-13

7TMR-DISM extracellular 2; This entry represents one of two distinct types of extracellular domain found in the 7TM-DISM (7TM Receptors with Diverse Intracellular Signalling Modules) bacterial transmembrane proteins. It is possible that this domain adopts a jelly roll fold and acts as a receptor for carbohydrates and their derivatives. It can also recognize Ca(II) (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 429601  Cd Length: 127  Bit Score: 66.21  E-value: 4.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933    8 LWMLQESGSALTAEEVMAKYEGRllTKNTVGQVSYGFTNNTIWGVLPVDINTygepvtSDPhnlsesfpfLPLVIEIDNA 87
Cdd:pfam07696   1 VEYLEDPTGSLTIEDVLSADGRF--RPPEKGVPNFGYSSSAYWLRFTLENPT------DAP---------KDWLLELAYP 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521328933   88 WLDDIDVYFFENGERKHHVTLGDNQIHSARAERARMPSVFYRFTQQQTI-VVFRLSSQDPMTIP 150
Cdd:pfam07696  64 LLDEIDLYLPDGGGGYREQRLGDRLPFSQRPVAHRNFVFPLPLPPGETVtLYLRVKSSGSLLLP 127
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 376-537 5.97e-13

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 71.72  E-value: 5.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 376 QQARLSAERDARLDPLTSLYNR----RAFEDLVYPIWELgkrsnkhmSVLLIDLDWFKRINDKFGHDMGDKVLQNVAKEI 451
Cdd:PRK11359 366 EKSRQHIEQLIQFDPLTGLPNRnnlhNYLDDLVDKAVSP--------VVYLIGVDHFQDVIDSLGYAWADQALLEVVNRF 437

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 452 KGQVRGSDITFRWGGEEFLVFLPNTRANYAKQIAENLRlHLFSHDI---NKLVRVTVSIGVsgSYPGEDDLNVLIKEADQ 528
Cdd:PRK11359 438 REKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELR-NVVSKPImidDKPFPLTLSIGI--SYDVGKNRDYLLSTAHN 514

                        170
                 ....*....|
gi 521328933 529 AL-YLAKAQG 537
Cdd:PRK11359 515 AMdYIRKNGG 524
PRK09966 PRK09966
diguanylate cyclase DgcN;
377-542 1.30e-12

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 69.65  E-value: 1.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 377 QARLSAE-----RDARLDPLTSLYNRRAFEDLVYPIweLGKRSNKHMSVLL-IDLDWFKRINDKFGHDMGDKVLQNVAKE 450
Cdd:PRK09966 234 QLRLQAKnaqllRTALHDPLTGLANRAAFRSGINTL--MNNSDARKTSALLfLDGDNFKYINDTWGHATGDRVLIEIAKR 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 451 IkGQVRGSDI-TFRWGGEEFLVFLPNTRANY-AKQIAENLRLHL---FSHDINKLVRVTVSIG--VSGSYPGEDDLNVLi 523
Cdd:PRK09966 312 L-AEFGGLRHkAYRLGGDEFAMVLYDVQSESeVQQICSALTQIFnlpFDLHNGHQTTMTLSIGyaMTIEHASAEKLQEL- 389

                        170
                 ....*....|....*....
gi 521328933 524 keADQALYLAKAQGRNKVV 542
Cdd:PRK09966 390 --ADHNMYQAKHQRAEKLV 406
CdaR COG3835
Sugar diacid utilization regulator CdaR [Transcription, Signal transduction mechanisms];
375-543 3.89e-06

Sugar diacid utilization regulator CdaR [Transcription, Signal transduction mechanisms];


Pssm-ID: 443046 [Multi-domain]  Cd Length: 301  Bit Score: 48.87  E-value: 3.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 375 VQQARLSAERDARLdpltslynRRAF-EDLVYP-------IWELGKRS----NKHMSVLLIDLDwfkrindkfGHDMGDK 442
Cdd:COG3835   39 LEQAREQLEWERRL--------REEFlDDLLSGnledeeeLLERAKRLgidlDRPRVVLVIELD---------SEDDESK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 443 VLQNVAKEIKGqvRGSDITFRWGGEEFLVFLPNTRANYAKQIAEnlRLHLFSHDINKLVRVTVSIGVSGSYPGEDDLNVL 522
Cdd:COG3835  102 DLERLRRALRA--LRRDLLVALSGDRLVVLLPAESEWRDEELRE--LAERLLEELEREGGLRVRIGVGRPVPGLAGLARS 177

                        170       180
                 ....*....|....*....|.
gi 521328933 523 IKEADQALYLAKAQGRNKVVL 543
Cdd:COG3835  178 YREARRALELGRRLGPEGRVY 198
GGDEF_2 pfam17853
GGDEF-like domain; This domain is distantly related to the GGDEF domain, suggesting these may ...
 409-530 2.43e-04

GGDEF-like domain; This domain is distantly related to the GGDEF domain, suggesting these may by diguanylate cyclase enzymes.


Pssm-ID: 465533  Cd Length: 116  Bit Score: 40.77  E-value: 2.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933  409 ELGKRSNKHMSVLLIDLDwfkrindkfghDMGDKVLQNVAKEIKGqvRGSDITFRWGGEEFLVFLPNTRANYAKQIAENL 488
Cdd:pfam17853  14 RLGLDLDGPHVVVVVELD-----------EDADRLLRALERALRA--LGRGALVAVRGDRLVLLLPADDEADAEALLERL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 521328933  489 RlhlfshdiNKLVRVTVSIGVSGSYPGEDDLNVLIKEADQAL 530
Cdd:pfam17853  81 A--------RALGGLPVRVGVGRPAAGLAGLRRSYREARRAL 114
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 360-544 3.02e-03

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 40.31  E-value: 3.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 360 EMSLLSISLAFNYKQVQQARLSAERDARLDPLTSLYNRRAFEDLVYPIWELGKRSNkHMSVLLIDLDWFKRINDKFGHDM 439
Cdd:PRK11829 206 ELGVLVRNYNRNQQLLADAYADMGRISHRFPVTELPNRSLFISLLEKEIASSTRTD-HFHLLVIGIETLQEVSGAMSEAQ 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328933 440 GDKVLQNVAKEIKGQVRGSDITFRWGGEEFLVFLPNT-RANYAKQIAENLrLHLFSHDI---NKLVRVTVSIGVSGSYPG 515
Cdd:PRK11829 285 HQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVLARGTrRSFPAMQLARRI-MSQVTQPLffdEITLRPSASIGITRYQAQ 363

                        170       180
                 ....*....|....*....|....*....
gi 521328933 516 EDDLNVLIKEADQALYLAKAQGRNKVVLW 544
Cdd:PRK11829 364 QDTAESMMRNASTAMMAAHHEGRNQIMVF 392
 
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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