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Conserved domains on  [gi|489120894|ref|WP_003030727|]
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MULTISPECIES: sensor domain-containing diguanylate cyclase [Citrobacter]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
175-332 2.05e-44

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: 149.63  E-value: 2.05e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 175 YTDALTGLPNRRAIFENVETLFSLARHLRQKIVVAYIDLDDFKLINDRFGHEVGDQFLIQIGHRLLRKCSDNDILGRLGG 254
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 255 DEFLVarLSPEDDREQ------RVRlqqvkhqlqqQICGDYHLGDIHLFYPGASLGVVEIDPLETDVNCALHLADSAMYK 328
Cdd:cd01949   81 DEFAI--LLPGTDLEEaealaeRLR----------EAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYR 148

                 ....
gi 489120894 329 DKKR 332
Cdd:cd01949  149 AKRS 152
GAF COG2203
GAF domain [Signal transduction mechanisms];
5-334 1.07e-08

GAF domain [Signal transduction mechanisms];


:

Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 56.74  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894   5 ILARVSQSLATEQSVESLVRQLLEMLEVVTEMESTYLTKVDLDARLQHILYARNscqMQIPEGLSVPWDETLCKRAIEEN 84
Cdd:COG2203  194 LLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPG---LPEEELGRLPLGEGLAGRALRTG 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894  85 C-LYSDNVPA--RWPECT--AARALDITTFLSTPVHLpDGTFYGTLCATSRRQHALSERGEQVLHLFAGLIAQSIQKESL 159
Cdd:COG2203  271 EpVVVNDASTdpRFAPSLreLLLALGIRSLLCVPLLV-DGRLIGVLALYSKEPRAFTEEDLELLEALADQAAIAIERARL 349
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 160 VAQLREANAALIAHSYTDALTGLPNRRAIFENVETLFSLARHLRQKIVVAYIDLDDFKLINDRFGHEVGDQFLIQIGHRL 239
Cdd:COG2203  350 YEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDLLLL 429
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 240 LRKCSDNDILGRLGGDEFLVARLSPEDDREQRVRLQQVKHQLQQQICGDYHLGDIHLFYPGASLGVVEIDPLETDVNCAL 319
Cdd:COG2203  430 LLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLALSALAVLASL 509
                        330
                 ....*....|....*
gi 489120894 320 HLADSAMYKDKKRQD 334
Cdd:COG2203  510 LLALLLLLLLLLLLL 524
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
175-332 2.05e-44

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: 149.63  E-value: 2.05e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 175 YTDALTGLPNRRAIFENVETLFSLARHLRQKIVVAYIDLDDFKLINDRFGHEVGDQFLIQIGHRLLRKCSDNDILGRLGG 254
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 255 DEFLVarLSPEDDREQ------RVRlqqvkhqlqqQICGDYHLGDIHLFYPGASLGVVEIDPLETDVNCALHLADSAMYK 328
Cdd:cd01949   81 DEFAI--LLPGTDLEEaealaeRLR----------EAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYR 148

                 ....
gi 489120894 329 DKKR 332
Cdd:cd01949  149 AKRS 152
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
90-332 1.08e-43

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: 151.67  E-value: 1.08e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894  90 NVPARWPECTAARALDITTFLSTPVHLPDGTFYGTLCATSRRQHALSERGEQVLHLFAGLIAQSIQKESLVAQLREANAA 169
Cdd:COG2199   30 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEER 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 170 LIAHSYTDALTGLPNRRAIFENVETLFSLARHLRQKIVVAYIDLDDFKLINDRFGHEVGDQFLIQIGHRLLRKCSDNDIL 249
Cdd:COG2199  110 LRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLV 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 250 GRLGGDEFLVarLSPEDDREQRVRLQQVKHQLQQQICGDYHLGDIHLfypGASLGVVEIDPLETDVNCALHLADSAMYKD 329
Cdd:COG2199  190 ARLGGDEFAV--LLPGTDLEEAEALAERLREALEQLPFELEGKELRV---TVSIGVALYPEDGDSAEELLRRADLALYRA 264

                 ...
gi 489120894 330 KKR 332
Cdd:COG2199  265 KRA 267
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
174-332 5.95e-39

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: 135.46  E-value: 5.95e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894  174 SYTDALTGLPNRRAIFENVETLFSLARHLRQKIVVAYIDLDDFKLINDRFGHEVGDQFLIQIGHRLLRKCSDNDILGRLG 253
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489120894  254 GDEFLVarLSPEDDREQRVRLQQVKHQLQQQIcGDYHLGDIHLFYPGASLGVVEIDPLETDVNCALHLADSAMYKDKKR 332
Cdd:pfam00990  81 GDEFAI--LLPETSLEGAQELAERIRRLLAKL-KIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQA 156
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
174-332 1.35e-34

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 124.28  E-value: 1.35e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894   174 SYTDALTGLPNRRAIFENVETLFSLARHLRQKIVVAYIDLDDFKLINDRFGHEVGDQFLIQIGHRLLRKCSDNDILGRLG 253
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489120894   254 GDEFLVarLSPEDDREQRVRLQQVKHQLQQQicgdYHLGDIHLFYPGASLGVVEIDPLETDVNCALHLADSAMYKDKKR 332
Cdd:smart00267  83 GDEFAL--LLPETSLEEAIALAERILQQLRE----PIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKA 155
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
174-339 3.41e-26

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: 102.03  E-value: 3.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894  174 SYTDALTGLPNRRAIFENVETLFSLARHLRQKIVVAYIDLDDFKLINDRFGHEVGDQFLIQIGHRLLRKCSDNDILGRLG 253
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894  254 GDEFLVarLSPEDDREQRV----RLQQVKHQLQQQICGDYHLgdihlfYPGASLGVVEIDPLETDVNCALHLADSAMYKD 329
Cdd:TIGR00254  82 GEEFVV--ILPGTPLEDALskaeRLRDAINSKPIEVAGSETL------TVTVSIGVACYPGHGLTLEELLKRADEALYQA 153
                         170
                  ....*....|
gi 489120894  330 KKRQDKTAFV 339
Cdd:TIGR00254 154 KKAGRNRVVV 163
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
164-330 1.67e-20

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 92.44  E-value: 1.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 164 REANAALIAHSYTDALTGLPNRRAIFENVETlfSLARHLRQKIVVAYIDLDDFKLINDRFGHEVGDQFLIQIGHRLLRKC 243
Cdd:PRK10060 227 RRAQERLRILANTDSITGLPNRNAIQELIDH--AINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCL 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 244 SDNDILGRLGGDEFLVarLSPEDDRE------QRV--RLQQvkhqlqqqicgDYHLGDIHLfYPGASLGVVEIDPLETDV 315
Cdd:PRK10060 305 EEDQTLARLGGDEFLV--LASHTSQAaleamaSRIltRLRL-----------PFRIGLIEV-YTGCSIGIALAPEHGDDS 370
                        170
                 ....*....|....*
gi 489120894 316 NCALHLADSAMYKDK 330
Cdd:PRK10060 371 ESLIRSADTAMYTAK 385
GAF COG2203
GAF domain [Signal transduction mechanisms];
5-334 1.07e-08

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 56.74  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894   5 ILARVSQSLATEQSVESLVRQLLEMLEVVTEMESTYLTKVDLDARLQHILYARNscqMQIPEGLSVPWDETLCKRAIEEN 84
Cdd:COG2203  194 LLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPG---LPEEELGRLPLGEGLAGRALRTG 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894  85 C-LYSDNVPA--RWPECT--AARALDITTFLSTPVHLpDGTFYGTLCATSRRQHALSERGEQVLHLFAGLIAQSIQKESL 159
Cdd:COG2203  271 EpVVVNDASTdpRFAPSLreLLLALGIRSLLCVPLLV-DGRLIGVLALYSKEPRAFTEEDLELLEALADQAAIAIERARL 349
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 160 VAQLREANAALIAHSYTDALTGLPNRRAIFENVETLFSLARHLRQKIVVAYIDLDDFKLINDRFGHEVGDQFLIQIGHRL 239
Cdd:COG2203  350 YEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDLLLL 429
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 240 LRKCSDNDILGRLGGDEFLVARLSPEDDREQRVRLQQVKHQLQQQICGDYHLGDIHLFYPGASLGVVEIDPLETDVNCAL 319
Cdd:COG2203  430 LLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLALSALAVLASL 509
                        330
                 ....*....|....*
gi 489120894 320 HLADSAMYKDKKRQD 334
Cdd:COG2203  510 LLALLLLLLLLLLLL 524
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
19-164 1.54e-07

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


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 50.07  E-value: 1.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894    19 VESLVRQLLEMLEVVTEMESTYLTKVDLDARLQHILYARNScQMQIPEGLSVPWDETLCKRAIEEN-CLYSDNVPA--RW 95
Cdd:smart00065   2 LEELLQTILEELRQLLGADRVLIYLVDENDRGELVLVAADG-LTLPTLGIRFPLDEGLAGRVAETGrPLNIPDVEAdpLF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894    96 PECTAARALDITTFLSTPVHLpDGTFYGTLCATSR-RQHALSERGEQVLHLFAGLIAQSIQKESLVAQLR 164
Cdd:smart00065  81 AEDLLGRYQGVRSFLAVPLVA-DGELVGVLALHNKkSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
16-155 2.08e-06

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


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 46.69  E-value: 2.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894   16 EQSVESLVRQLLEMLEVVTEMESTYLTKVDLDARLQhilyARNSCQMQIPEGLSVPWDETLCKRAIEEN-CLYSDNVPAR 94
Cdd:pfam13185   1 AADLEELLDAVLEAAVELGASAVGFILLVDDDGRLA----AWGGAADELSAALDDPPGEGLVGEALRTGrPVIVNDLAAD 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489120894   95 WPECTA-ARALDITTFLSTPVHLpDGTFYGTLCATSRRQHALSERGEQVLHLFAGLIAQSIQ 155
Cdd:pfam13185  77 PAKKGLpAGHAGLRSFLSVPLVS-GGRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAIE 137
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
175-332 2.05e-44

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: 149.63  E-value: 2.05e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 175 YTDALTGLPNRRAIFENVETLFSLARHLRQKIVVAYIDLDDFKLINDRFGHEVGDQFLIQIGHRLLRKCSDNDILGRLGG 254
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 255 DEFLVarLSPEDDREQ------RVRlqqvkhqlqqQICGDYHLGDIHLFYPGASLGVVEIDPLETDVNCALHLADSAMYK 328
Cdd:cd01949   81 DEFAI--LLPGTDLEEaealaeRLR----------EAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYR 148

                 ....
gi 489120894 329 DKKR 332
Cdd:cd01949  149 AKRS 152
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
90-332 1.08e-43

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: 151.67  E-value: 1.08e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894  90 NVPARWPECTAARALDITTFLSTPVHLPDGTFYGTLCATSRRQHALSERGEQVLHLFAGLIAQSIQKESLVAQLREANAA 169
Cdd:COG2199   30 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEER 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 170 LIAHSYTDALTGLPNRRAIFENVETLFSLARHLRQKIVVAYIDLDDFKLINDRFGHEVGDQFLIQIGHRLLRKCSDNDIL 249
Cdd:COG2199  110 LRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLV 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 250 GRLGGDEFLVarLSPEDDREQRVRLQQVKHQLQQQICGDYHLGDIHLfypGASLGVVEIDPLETDVNCALHLADSAMYKD 329
Cdd:COG2199  190 ARLGGDEFAV--LLPGTDLEEAEALAERLREALEQLPFELEGKELRV---TVSIGVALYPEDGDSAEELLRRADLALYRA 264

                 ...
gi 489120894 330 KKR 332
Cdd:COG2199  265 KRA 267
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
174-332 5.95e-39

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: 135.46  E-value: 5.95e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894  174 SYTDALTGLPNRRAIFENVETLFSLARHLRQKIVVAYIDLDDFKLINDRFGHEVGDQFLIQIGHRLLRKCSDNDILGRLG 253
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489120894  254 GDEFLVarLSPEDDREQRVRLQQVKHQLQQQIcGDYHLGDIHLFYPGASLGVVEIDPLETDVNCALHLADSAMYKDKKR 332
Cdd:pfam00990  81 GDEFAI--LLPETSLEGAQELAERIRRLLAKL-KIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQA 156
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
130-332 1.33e-35

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


Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 136.83  E-value: 1.33e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 130 RRQHALSERGEQVLHLFAGLIAQSIQKESLVAQLREANAALIAHSYTDALTGLPNRRAIFENVETLFSLARHLRQKIVVA 209
Cdd:COG5001  207 RLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALL 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 210 YIDLDDFKLINDRFGHEVGDQFLIQIGHRLLRKCSDNDILGRLGGDEFLVarLSPEDDREQRV-----RLqqvkhqlQQQ 284
Cdd:COG5001  287 FIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAV--LLPDLDDPEDAeavaeRI-------LAA 357
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 489120894 285 ICGDYHLGDiHLFYPGASLGVVEIDPLETDVNCALHLADSAMYKDKKR 332
Cdd:COG5001  358 LAEPFELDG-HELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAA 404
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
174-332 1.35e-34

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 124.28  E-value: 1.35e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894   174 SYTDALTGLPNRRAIFENVETLFSLARHLRQKIVVAYIDLDDFKLINDRFGHEVGDQFLIQIGHRLLRKCSDNDILGRLG 253
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489120894   254 GDEFLVarLSPEDDREQRVRLQQVKHQLQQQicgdYHLGDIHLFYPGASLGVVEIDPLETDVNCALHLADSAMYKDKKR 332
Cdd:smart00267  83 GDEFAL--LLPETSLEEAIALAERILQQLRE----PIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKA 155
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
174-339 3.41e-26

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: 102.03  E-value: 3.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894  174 SYTDALTGLPNRRAIFENVETLFSLARHLRQKIVVAYIDLDDFKLINDRFGHEVGDQFLIQIGHRLLRKCSDNDILGRLG 253
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894  254 GDEFLVarLSPEDDREQRV----RLQQVKHQLQQQICGDYHLgdihlfYPGASLGVVEIDPLETDVNCALHLADSAMYKD 329
Cdd:TIGR00254  82 GEEFVV--ILPGTPLEDALskaeRLRDAINSKPIEVAGSETL------TVTVSIGVACYPGHGLTLEELLKRADEALYQA 153
                         170
                  ....*....|
gi 489120894  330 KKRQDKTAFV 339
Cdd:TIGR00254 154 KKAGRNRVVV 163
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
164-330 1.67e-20

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 92.44  E-value: 1.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 164 REANAALIAHSYTDALTGLPNRRAIFENVETlfSLARHLRQKIVVAYIDLDDFKLINDRFGHEVGDQFLIQIGHRLLRKC 243
Cdd:PRK10060 227 RRAQERLRILANTDSITGLPNRNAIQELIDH--AINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCL 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 244 SDNDILGRLGGDEFLVarLSPEDDRE------QRV--RLQQvkhqlqqqicgDYHLGDIHLfYPGASLGVVEIDPLETDV 315
Cdd:PRK10060 305 EEDQTLARLGGDEFLV--LASHTSQAaleamaSRIltRLRL-----------PFRIGLIEV-YTGCSIGIALAPEHGDDS 370
                        170
                 ....*....|....*
gi 489120894 316 NCALHLADSAMYKDK 330
Cdd:PRK10060 371 ESLIRSADTAMYTAK 385
PRK09894 PRK09894
diguanylate cyclase; Provisional
157-330 1.66e-17

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 81.65  E-value: 1.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 157 ESLVAQLREANAALIA-HSYTDALTGLPNRRAIFENVETlfSLARHLRQKIVVAYIDLDDFKLINDRFGHEVGDQFLIQI 235
Cdd:PRK09894 111 LSFTAALTDYKIYLLTiRSNMDVLTGLPGRRVLDESFDH--QLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTL 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 236 GHRLLRKCSDNDILGRLGGDEFLV--ARLSPEDDREQRVRLQQVKHQLQQQICGdyhlGDIHLfypGASLGVVEIDPLET 313
Cdd:PRK09894 189 ATYLASWTRDYETVYRYGGEEFIIclKAATDEEACRAGERIRQLIANHAITHSD----GRINI---TATFGVSRAFPEET 261
                        170
                 ....*....|....*..
gi 489120894 314 dVNCALHLADSAMYKDK 330
Cdd:PRK09894 262 -LDVVIGRADRAMYEGK 277
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
176-259 5.99e-17

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 81.60  E-value: 5.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 176 TDALTGLPNRRAIFENVETLFSLARHLRQKIVVAYIDLDDFKLINDRFGHEVGDQFLIQIGHRLLRKCSDNDILGRLGGD 255
Cdd:PRK15426 400 HDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGE 479

                 ....
gi 489120894 256 EFLV 259
Cdd:PRK15426 480 EFCV 483
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
161-330 1.12e-15

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 78.18  E-value: 1.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894  161 AQLREanaalIAHSYT-DALTGLPNRrAIFEN-VETLFSLARHLRQKIVVAYIDLDDFKLINDRFGHEVGDQFLIQIGHR 238
Cdd:PRK09776  656 KMLRQ-----LSYSAShDALTHLANR-ASFEKqLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASL 729
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894  239 LLRKCSDNDILGRLGGDEFlvARLSPEDDREQrvrlqqvkhqlQQQICG-------DYH---LGDIHLFypGASLGVVEI 308
Cdd:PRK09776  730 MLSMLRSSDVLARLGGDEF--GLLLPDCNVES-----------ARFIATriisainDYHfpwEGRVYRV--GASAGITLI 794
                         170       180
                  ....*....|....*....|..
gi 489120894  309 DPLETDVNCALHLADSAMYKDK 330
Cdd:PRK09776  795 DANNHQASEVMSQADIACYAAK 816
pleD PRK09581
response regulator PleD; Reviewed
176-331 2.72e-15

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 76.48  E-value: 2.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 176 TDALTGLPNRRAIFENVETLFSLARHLRQKIVVAYIDLDDFKLINDRFGHEVGDQFLIQIGHRLLRKCSDNDILGRLGGD 255
Cdd:PRK09581 294 TDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGE 373
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 256 EFLVarLSPEDDREQ------RVRLQQVKHqlqqqicgDYHL-GDIHLFYPGASLGVVEIDPLETDVNCALHLADSAMYK 328
Cdd:PRK09581 374 EFVV--VMPDTDIEDaiavaeRIRRKIAEE--------PFIIsDGKERLNVTVSIGVAELRPSGDTIEALIKRADKALYE 443

                 ...
gi 489120894 329 DKK 331
Cdd:PRK09581 444 AKN 446
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
111-267 8.65e-14

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 72.49  E-value: 8.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 111 STPVHLPDGTFYGTLCATSRRQHALSERGEQVLHLFAGLIAQSIQKEslvaQLREANAALIAHsytDALTGLPNRRAIFE 190
Cdd:PRK11359 320 SATIRQRDGAPAGTLQIKTSSGAETSAFIERVADISQHLAALALEQE----KSRQHIEQLIQF---DPLTGLPNRNNLHN 392
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489120894 191 NVETLFSLARhlrqKIVVAYIDLDDFKLINDRFGHEVGDQFLIQIGHRLLRKCSDNDILGRLGGDEFLVarLSPEDD 267
Cdd:PRK11359 393 YLDDLVDKAV----SPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVL--VSLEND 463
PRK09966 PRK09966
diguanylate cyclase DgcN;
129-257 1.04e-12

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 68.49  E-value: 1.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 129 SRRqhaLSERGEQVLHLFAgLIAQSIQKESLVAQLR--EANAALIAHSYTDALTGLPNRRAIFENVETLFSlARHLRQKI 206
Cdd:PRK09966 205 SRR---VSEERIAEFHRFA-LDFNSLLDEMEEWQLRlqAKNAQLLRTALHDPLTGLANRAAFRSGINTLMN-NSDARKTS 279
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489120894 207 VVAYIDLDDFKLINDRFGHEVGDQFLIQIGHRLLRKCSDNDILGRLGGDEF 257
Cdd:PRK09966 280 ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEF 330
adrA PRK10245
diguanylate cyclase AdrA; Provisional
162-259 1.70e-12

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 67.55  E-value: 1.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 162 QLREANAALIAHSYTDALTGLPNRRaifeNVETL----FSLARHLRQKIVVAYIDLDDFKLINDRFGHEVGDQFLIQIGH 237
Cdd:PRK10245 193 KLAEHKRRLQVMSTRDGMTGVYNRR----HWETLlrneFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTR 268
                         90       100
                 ....*....|....*....|..
gi 489120894 238 RLLRKCSDNDILGRLGGDEFLV 259
Cdd:PRK10245 269 QLQITLRGSDVIGRFGGDEFAV 290
GAF COG2203
GAF domain [Signal transduction mechanisms];
5-334 1.07e-08

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 56.74  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894   5 ILARVSQSLATEQSVESLVRQLLEMLEVVTEMESTYLTKVDLDARLQHILYARNscqMQIPEGLSVPWDETLCKRAIEEN 84
Cdd:COG2203  194 LLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPG---LPEEELGRLPLGEGLAGRALRTG 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894  85 C-LYSDNVPA--RWPECT--AARALDITTFLSTPVHLpDGTFYGTLCATSRRQHALSERGEQVLHLFAGLIAQSIQKESL 159
Cdd:COG2203  271 EpVVVNDASTdpRFAPSLreLLLALGIRSLLCVPLLV-DGRLIGVLALYSKEPRAFTEEDLELLEALADQAAIAIERARL 349
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 160 VAQLREANAALIAHSYTDALTGLPNRRAIFENVETLFSLARHLRQKIVVAYIDLDDFKLINDRFGHEVGDQFLIQIGHRL 239
Cdd:COG2203  350 YEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDLLLL 429
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894 240 LRKCSDNDILGRLGGDEFLVARLSPEDDREQRVRLQQVKHQLQQQICGDYHLGDIHLFYPGASLGVVEIDPLETDVNCAL 319
Cdd:COG2203  430 LLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLALSALAVLASL 509
                        330
                 ....*....|....*
gi 489120894 320 HLADSAMYKDKKRQD 334
Cdd:COG2203  510 LLALLLLLLLLLLLL 524
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
19-164 1.54e-07

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


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 50.07  E-value: 1.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894    19 VESLVRQLLEMLEVVTEMESTYLTKVDLDARLQHILYARNScQMQIPEGLSVPWDETLCKRAIEEN-CLYSDNVPA--RW 95
Cdd:smart00065   2 LEELLQTILEELRQLLGADRVLIYLVDENDRGELVLVAADG-LTLPTLGIRFPLDEGLAGRVAETGrPLNIPDVEAdpLF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894    96 PECTAARALDITTFLSTPVHLpDGTFYGTLCATSR-RQHALSERGEQVLHLFAGLIAQSIQKESLVAQLR 164
Cdd:smart00065  81 AEDLLGRYQGVRSFLAVPLVA-DGELVGVLALHNKkSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
16-155 2.08e-06

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


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 46.69  E-value: 2.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894   16 EQSVESLVRQLLEMLEVVTEMESTYLTKVDLDARLQhilyARNSCQMQIPEGLSVPWDETLCKRAIEEN-CLYSDNVPAR 94
Cdd:pfam13185   1 AADLEELLDAVLEAAVELGASAVGFILLVDDDGRLA----AWGGAADELSAALDDPPGEGLVGEALRTGrPVIVNDLAAD 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489120894   95 WPECTA-ARALDITTFLSTPVHLpDGTFYGTLCATSRRQHALSERGEQVLHLFAGLIAQSIQ 155
Cdd:pfam13185  77 PAKKGLpAGHAGLRSFLSVPLVS-GGRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAIE 137
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
206-260 3.88e-04

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: 40.03  E-value: 3.88e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489120894 206 IVVAYIDLDDFKLINDRFGHEVGDQFLIQIGHRLLRKCSDN-DILGRLGGDEFLVA 260
Cdd:cd07556    2 VTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSgDLKIKTIGDEFMVV 57
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
99-168 2.04e-03

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


Pssm-ID: 442823 [Multi-domain]  Cd Length: 338  Bit Score: 39.45  E-value: 2.04e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489120894  99 TAARALDITTFLSTPVHLpDGTFYGTLCATSRRQHALSERGEQVLHLFAGLIAQSIQKESLVAQLREANA 168
Cdd:COG3604   66 AALAARERQLFLGVPLRV-GGEVLGVLTLDSRRPGAFSEEDLRLLETLASLAAVAILGETGTGKELVANA 134
 
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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