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Conserved domains on  [gi|639310448|ref|WP_024592692|]
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MULTISPECIES: diguanylate cyclase [Pseudoalteromonas]

Protein Classification

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 ...
123-316 6.89e-69

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: 216.00  E-value: 6.89e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 123 EVSHICIILYDVTDVAVNKKELEELNKKLEQVSQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKIND 202
Cdd:COG2199   82 ELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIND 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 203 EYGHSCGDESLRHLSNLLRTTLRETDVAGRYGGEEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHFEITMTVSIGLA 282
Cdd:COG2199  162 TYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVA 241
                        170       180       190
                 ....*....|....*....|....*....|....
gi 639310448 283 GSSNDFKNHERWIEAADKALYQSKNTGRNKVIAY 316
Cdd:COG2199  242 LYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
PAS super family cl38023
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
16-134 2.16e-05

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


The actual alignment was detected with superfamily member pfam00989:

Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 43.17  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448   16 MFNTVDVGLVVLDRDYKVCVWNGFMENHSGLLPSAVKDKDLFDLFPAIDEKWFRSKSESVFVLKNRSFTIWeqqpYIFRF 95
Cdd:pfam00989   6 ILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFE----VSFRV 81
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 639310448   96 KNYRPItgkadYMYQNATfiPLTNTMGEVSHICIILYDV 134
Cdd:pfam00989  82 PDGRPR-----HVEVRAS--PVRDAGGEILGFLGVLRDI 113
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
123-316 6.89e-69

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: 216.00  E-value: 6.89e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 123 EVSHICIILYDVTDVAVNKKELEELNKKLEQVSQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKIND 202
Cdd:COG2199   82 ELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIND 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 203 EYGHSCGDESLRHLSNLLRTTLRETDVAGRYGGEEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHFEITMTVSIGLA 282
Cdd:COG2199  162 TYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVA 241
                        170       180       190
                 ....*....|....*....|....*....|....
gi 639310448 283 GSSNDFKNHERWIEAADKALYQSKNTGRNKVIAY 316
Cdd:COG2199  242 LYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
156-314 4.27e-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: 194.70  E-value: 4.27e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 156 QTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGRYGG 235
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639310448 236 EEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHfEITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKNTGRNKVI 314
Cdd:cd01949   81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQ-EIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
155-312 7.90e-57

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: 181.30  E-value: 7.90e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448  155 SQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGRYG 234
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448  235 GEEFAVTLLDTDKEGAFVFAERLRVLIETN--PVKYKHFEITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKNTGRNK 312
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLkiPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
155-313 3.93e-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: 179.46  E-value: 3.93e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448  155 SQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGRYG 234
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448  235 GEEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHFE-ITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKNTGRNKV 313
Cdd:TIGR00254  82 GEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSEtLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNRV 161
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
153-316 5.71e-53

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 171.28  E-value: 5.71e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448   153 QVSQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGR 232
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448   233 YGGEEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHfEITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKNTGRNK 312
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGI-PLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159

                   ....
gi 639310448   313 VIAY 316
Cdd:smart00267 160 VAVY 163
pleD PRK09581
response regulator PleD; Reviewed
157-315 1.45e-46

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 163.15  E-value: 1.45e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 157 TDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGRYGGE 236
Cdd:PRK09581 294 TDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGE 373
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 237 EFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHFE--ITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKNTGRNKVI 314
Cdd:PRK09581 374 EFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGKerLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGRNRVV 453

                 .
gi 639310448 315 A 315
Cdd:PRK09581 454 A 454
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
144-313 4.07e-44

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 151.29  E-value: 4.07e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 144 LEELNKKLEQVSQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTT 223
Cdd:NF038266  83 MRDLNEALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAE 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 224 LRETDVAGRYGGEEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHFEITMTVSIGLAGSSNDFKNHERWIEAADKALY 303
Cdd:NF038266 163 LREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAEHRPPEEGLSATLSRADQALY 242
                        170
                 ....*....|
gi 639310448 304 QSKNTGRNKV 313
Cdd:NF038266 243 QAKRAGRDRV 252
dguan_cyc_DgcA NF041606
diguanylate cyclase DgcA;
148-313 2.06e-42

diguanylate cyclase DgcA;


Pssm-ID: 469490 [Multi-domain]  Cd Length: 340  Bit Score: 149.51  E-value: 2.06e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 148 NKKLEQVSQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRET 227
Cdd:NF041606 171 NALLLEMTTTDMMTHLKLKHYFYTVLMEKLDTINSQGEPLSILMLDIDFFKQINDTYGHACGDLVLQMVASIIQSCTRTQ 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 228 DVAGRYGGEEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHFEITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKN 307
Cdd:NF041606 251 DMAARYGGEEFVVMLSNTSSKTAKKIAERIRKSIENLSILYDEQHIRVTISIGVAEYNFDVESAKSLVERADKALYESKQ 330

                 ....*.
gi 639310448 308 TGRNKV 313
Cdd:NF041606 331 NGRNRV 336
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
16-134 2.16e-05

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 43.17  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448   16 MFNTVDVGLVVLDRDYKVCVWNGFMENHSGLLPSAVKDKDLFDLFPAIDEKWFRSKSESVFVLKNRSFTIWeqqpYIFRF 95
Cdd:pfam00989   6 ILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFE----VSFRV 81
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 639310448   96 KNYRPItgkadYMYQNATfiPLTNTMGEVSHICIILYDV 134
Cdd:pfam00989  82 PDGRPR-----HVEVRAS--PVRDAGGEILGFLGVLRDI 113
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
6-164 3.22e-05

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 45.22  E-value: 3.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448   6 EMNEIH-WLMDMFNTVDVGLVVLDRDYKVCVWNGFMENHSGLLPSAVKDKDLFDLFPAIDEkwFRSKSESVfVLKNRSFT 84
Cdd:COG3852    1 ALRESEeLLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSP--LRELLERA-LAEGQPVT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448  85 IWEqqpYIFRFKNYRPITgkADYmyqnaTFIPLTNTMGEVsHICIILYDVTDvavnKKELEElnkKLEQVSQTDSLTQLA 164
Cdd:COG3852   78 ERE---VTLRRKDGEERP--VDV-----SVSPLRDAEGEG-GVLLVLRDITE----RKRLER---ELRRAEKLAAVGELA 139
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
11-69 9.85e-04

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 36.99  E-value: 9.85e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 639310448    11 HWLMDMFNTVDVGLVVLDRDYKVCVWNGFMENHSGLLPSAVKDKDLFDLFPAIDEKWFR 69
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQ 59
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
123-316 6.89e-69

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: 216.00  E-value: 6.89e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 123 EVSHICIILYDVTDVAVNKKELEELNKKLEQVSQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKIND 202
Cdd:COG2199   82 ELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIND 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 203 EYGHSCGDESLRHLSNLLRTTLRETDVAGRYGGEEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHFEITMTVSIGLA 282
Cdd:COG2199  162 TYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVA 241
                        170       180       190
                 ....*....|....*....|....*....|....
gi 639310448 283 GSSNDFKNHERWIEAADKALYQSKNTGRNKVIAY 316
Cdd:COG2199  242 LYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
156-314 4.27e-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: 194.70  E-value: 4.27e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 156 QTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGRYGG 235
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639310448 236 EEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHfEITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKNTGRNKVI 314
Cdd:cd01949   81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQ-EIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
155-312 7.90e-57

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: 181.30  E-value: 7.90e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448  155 SQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGRYG 234
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448  235 GEEFAVTLLDTDKEGAFVFAERLRVLIETN--PVKYKHFEITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKNTGRNK 312
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLkiPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
155-313 3.93e-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: 179.46  E-value: 3.93e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448  155 SQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGRYG 234
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448  235 GEEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHFE-ITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKNTGRNKV 313
Cdd:TIGR00254  82 GEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSEtLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNRV 161
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
153-316 5.71e-53

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 171.28  E-value: 5.71e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448   153 QVSQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGR 232
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448   233 YGGEEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHfEITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKNTGRNK 312
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGI-PLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159

                   ....
gi 639310448   313 VIAY 316
Cdd:smart00267 160 VAVY 163
pleD PRK09581
response regulator PleD; Reviewed
157-315 1.45e-46

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 163.15  E-value: 1.45e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 157 TDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGRYGGE 236
Cdd:PRK09581 294 TDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGE 373
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 237 EFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHFE--ITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKNTGRNKVI 314
Cdd:PRK09581 374 EFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGKerLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGRNRVV 453

                 .
gi 639310448 315 A 315
Cdd:PRK09581 454 A 454
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
144-313 4.07e-44

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 151.29  E-value: 4.07e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 144 LEELNKKLEQVSQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTT 223
Cdd:NF038266  83 MRDLNEALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAE 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 224 LRETDVAGRYGGEEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHFEITMTVSIGLAGSSNDFKNHERWIEAADKALY 303
Cdd:NF038266 163 LREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAEHRPPEEGLSATLSRADQALY 242
                        170
                 ....*....|
gi 639310448 304 QSKNTGRNKV 313
Cdd:NF038266 243 QAKRAGRDRV 252
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
129-318 2.26e-43

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: 158.01  E-value: 2.26e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 129 IILYDVTDVAVNKKELEELNKKLEQVSQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSC 208
Cdd:COG5001  225 LLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAA 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 209 GDESLRHLSNLLRTTLRETDVAGRYGGEEFAVTLLD-TDKEGAFVFAERLRVLIETnPVKYKHFEITMTVSIGLAGSSND 287
Cdd:COG5001  305 GDELLREVARRLRACLREGDTVARLGGDEFAVLLPDlDDPEDAEAVAERILAALAE-PFELDGHELYVSASIGIALYPDD 383
                        170       180       190
                 ....*....|....*....|....*....|.
gi 639310448 288 FKNHERWIEAADKALYQSKNTGRNKVIAYED 318
Cdd:COG5001  384 GADAEELLRNADLAMYRAKAAGRNRYRFFDP 414
dguan_cyc_DgcA NF041606
diguanylate cyclase DgcA;
148-313 2.06e-42

diguanylate cyclase DgcA;


Pssm-ID: 469490 [Multi-domain]  Cd Length: 340  Bit Score: 149.51  E-value: 2.06e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 148 NKKLEQVSQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRET 227
Cdd:NF041606 171 NALLLEMTTTDMMTHLKLKHYFYTVLMEKLDTINSQGEPLSILMLDIDFFKQINDTYGHACGDLVLQMVASIIQSCTRTQ 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 228 DVAGRYGGEEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHFEITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKN 307
Cdd:NF041606 251 DMAARYGGEEFVVMLSNTSSKTAKKIAERIRKSIENLSILYDEQHIRVTISIGVAEYNFDVESAKSLVERADKALYESKQ 330

                 ....*.
gi 639310448 308 TGRNKV 313
Cdd:NF041606 331 NGRNRV 336
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
147-315 1.85e-40

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 148.62  E-value: 1.85e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 147 LNKKLEQVSQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRE 226
Cdd:PRK15426 390 LQSSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRA 469
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 227 TDVAGRYGGEEFAVTLLDTDKEGAFVFAERLRVLIETNPV-KYKHFEITMTVSIGLAGSSNDFK-NHERWIEAADKALYQ 304
Cdd:PRK15426 470 QDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEIlVAKSTTIRISASLGVSSAEEDGDyDFEQLQSLADRRLYL 549
                        170
                 ....*....|.
gi 639310448 305 SKNTGRNKVIA 315
Cdd:PRK15426 550 AKQAGRNRVCA 560
adrA PRK10245
diguanylate cyclase AdrA; Provisional
144-312 5.69e-40

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 143.82  E-value: 5.69e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 144 LEELNKKLEQVSQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTT 223
Cdd:PRK10245 194 LAEHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQIT 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 224 LRETDVAGRYGGEEFAVTLLDTDKEGAFV----FAERLRVL-IETNPvkykhfEITMTVSIGLAGSSNDFKNHERWIEAA 298
Cdd:PRK10245 274 LRGSDVIGRFGGDEFAVIMSGTPAESAITamsrVHEGLNTLrLPNAP------QVTLRISVGVAPLNPQMSHYREWLKSA 347
                        170
                 ....*....|....
gi 639310448 299 DKALYQSKNTGRNK 312
Cdd:PRK10245 348 DLALYKAKNAGRNR 361
PRK09894 PRK09894
diguanylate cyclase; Provisional
155-318 7.69e-36

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 130.96  E-value: 7.69e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 155 SQTDSLTQLANR-GHWEGTLRQEFLRVKRsgGCStLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGRY 233
Cdd:PRK09894 129 SNMDVLTGLPGRrVLDESFDHQLRNREPQ--NLY-LALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRY 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 234 GGEEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHFEITMTVSIGLAGSSNDfKNHERWIEAADKALYQSKNTGRNKV 313
Cdd:PRK09894 206 GGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRAFPE-ETLDVVIGRADRAMYEGKQTGRNRV 284

                 ....*
gi 639310448 314 IAYED 318
Cdd:PRK09894 285 MFIDE 289
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
116-317 5.81e-23

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 99.75  E-value: 5.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448  116 PLTNTMGEVSHICIILYDVTdvavnkkELEELNKKLEQVSQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDID 195
Cdd:PRK09776  633 PLSTLDGENIGSVLVIQDVT-------ESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLD 705
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448  196 HFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGRYGGEEFAVTLLDTDKEGAFVFAERLrvlieTNPVKYKHFE--- 272
Cdd:PRK09776  706 RFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRI-----ISAINDYHFPweg 780
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 639310448  273 --ITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKNTGRNKVIAYE 317
Cdd:PRK09776  781 rvYRVGASAGITLIDANNHQASEVMSQADIACYAAKNAGRGRVTVYE 827
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
24-312 1.24e-20

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 92.44  E-value: 1.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448  24 LVVLDRDYKVCVWNGFMENHSGLLPSAVKDKDLFDLFPAIDEKWFRSKSESVFVLKNRSF-------TIWEQQPYIFRFK 96
Cdd:PRK10060 124 IVILDSRGNIQRFNRLCEEYTGLKEHDVIGQSVFKLFMSRREAAASRRNIRGFFRSGNAYeverwikTRKGQRLFLFRNK 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448  97 NYRPITGKadymyqNATFIpltntmgevshICiilyDVTDVAvnkkelEELN--KKLEQVSQTDSLTQLANRghwegTLR 174
Cdd:PRK10060 204 FVHSGSGK------NEIFL-----------IC----SGTDIT------EERRaqERLRILANTDSITGLPNR-----NAI 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 175 QEFLR---VKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGRYGGEEFAVTLLDTDKEG-- 249
Cdd:PRK10060 252 QELIDhaiNAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFLVLASHTSQAAle 331
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 639310448 250 --AFVFAERLRVlietnPVKYKHFEITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKNTGRNK 312
Cdd:PRK10060 332 amASRILTRLRL-----PFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSADTAMYTAKEGGRGQ 391
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
228-306 1.68e-16

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: 76.10  E-value: 1.68e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639310448 228 DVAGRYGGEEFAVTLLDTDKEGAFVFAERLRVLIEtnpvkyKHFEITMTVSIGLAGSSndfknherWIEAADkALYQSK 306
Cdd:COG3706  116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVA------ELPSLRVTVSIGVAGDS--------LLKRAD-ALYQAR 179
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
143-311 2.08e-15

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 76.73  E-value: 2.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 143 ELEELNKKLEQVSQTDSLTQLANRGHWEGTLrQEFLRVKRSggcSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRT 222
Cdd:PRK11359 364 EQEKSRQHIEQLIQFDPLTGLPNRNNLHNYL-DDLVDKAVS---PVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFRE 439
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 223 TLRETDVAGRYGGEEFAVTLLDTDKEGAFVFAERLRVLIeTNPVKYKHFEITMTVSIGLAGSSNdfKNHERWIEAADKAL 302
Cdd:PRK11359 440 KLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVV-SKPIMIDDKPFPLTLSIGISYDVG--KNRDYLLSTAHNAM 516

                 ....*....
gi 639310448 303 YQSKNTGRN 311
Cdd:PRK11359 517 DYIRKNGGN 525
PRK09966 PRK09966
diguanylate cyclase DgcN;
144-314 4.05e-14

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 72.35  E-value: 4.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 144 LEELNKKLEQVSQTDSLTQLANRGHWEGTLrQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTT 223
Cdd:PRK09966 237 LQAKNAQLLRTALHDPLTGLANRAAFRSGI-NTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEF 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 224 LRETDVAGRYGGEEFAVTLLDTDKEgafvfAERLRVLIETNPVKYKHFE------ITMTVSIGLAgSSNDFKNHERWIEA 297
Cdd:PRK09966 316 GGLRHKAYRLGGDEFAMVLYDVQSE-----SEVQQICSALTQIFNLPFDlhnghqTTMTLSIGYA-MTIEHASAEKLQEL 389
                        170
                 ....*....|....*..
gi 639310448 298 ADKALYQSKNTGRNKVI 314
Cdd:PRK09966 390 ADHNMYQAKHQRAEKLV 406
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
186-307 6.67e-12

Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.


Pssm-ID: 143637 [Multi-domain]  Cd Length: 133  Bit Score: 61.99  E-value: 6.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 186 CSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRET-DVAGRYGGEEFAVTLLDTDKEGAFVFAERLRVLIET- 263
Cdd:cd07556    1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSgDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAl 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 639310448 264 NPVKYKHFEI-----TMTVSIGLAGSSNDFKNHERWIEAADKALYQSKN 307
Cdd:cd07556   81 NQSEGNPVRVrigihTGPVVVGVIGSRPQYDVWGALVNLASRMESQAKA 129
PAS COG2202
PAS domain [Signal transduction mechanisms];
2-245 1.61e-08

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 54.65  E-value: 1.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448   2 AADLEMNEIHWLMDMFNTVDVGLVVLDRDYKVCVWNGFMENHSGLLPSAVKDKDLFDLFPAIDEKWFRsksesvfvlKNR 81
Cdd:COG2202    2 AEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFL---------ELL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448  82 SFTIWEQQPYIFRFKNYRPiTGKadYMYQNATFIPLTNTMGEVSHICIILYDVTDvavnKKELEELNKKLEQvsQTDSLT 161
Cdd:COG2202   73 RAALAGGGVWRGELRNRRK-DGS--LFWVELSISPVRDEDGEITGFVGIARDITE----RKRAEEALRESEE--RLRLLV 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 162 QLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGRYGGEEFAVT 241
Cdd:COG2202  144 ENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWV 223

                 ....
gi 639310448 242 LLDT 245
Cdd:COG2202  224 WVEA 227
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
16-134 2.16e-05

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 43.17  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448   16 MFNTVDVGLVVLDRDYKVCVWNGFMENHSGLLPSAVKDKDLFDLFPAIDEKWFRSKSESVFVLKNRSFTIWeqqpYIFRF 95
Cdd:pfam00989   6 ILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFE----VSFRV 81
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 639310448   96 KNYRPItgkadYMYQNATfiPLTNTMGEVSHICIILYDV 134
Cdd:pfam00989  82 PDGRPR-----HVEVRAS--PVRDAGGEILGFLGVLRDI 113
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
6-164 3.22e-05

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 45.22  E-value: 3.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448   6 EMNEIH-WLMDMFNTVDVGLVVLDRDYKVCVWNGFMENHSGLLPSAVKDKDLFDLFPAIDEkwFRSKSESVfVLKNRSFT 84
Cdd:COG3852    1 ALRESEeLLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSP--LRELLERA-LAEGQPVT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448  85 IWEqqpYIFRFKNYRPITgkADYmyqnaTFIPLTNTMGEVsHICIILYDVTDvavnKKELEElnkKLEQVSQTDSLTQLA 164
Cdd:COG3852   78 ERE---VTLRRKDGEERP--VDV-----SVSPLRDAEGEG-GVLLVLRDITE----RKRLER---ELRRAEKLAAVGELA 139
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
140-317 2.85e-04

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 42.62  E-value: 2.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 140 NKKELEELNKKLEQVSQTDSLTQLANRGHWEGTLRQEFL-RVKRSGGCstLLMFDIDHFKKINDEYGHSCGDESLRHLSN 218
Cdd:PRK11829 217 NQQLLADAYADMGRISHRFPVTELPNRSLFISLLEKEIAsSTRTDHFH--LLVIGIETLQEVSGAMSEAQHQQLLLTIVQ 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 219 LLRTTLRETDVAGRYGGEEFAVTLLDTDKEG-AFVFAERLRVLIeTNPVKYKHFEITMTVSIGLAGSSNDFKNHERWIEA 297
Cdd:PRK11829 295 RIEQCIDDSDLLAQLSKTEFAVLARGTRRSFpAMQLARRIMSQV-TQPLFFDEITLRPSASIGITRYQAQQDTAESMMRN 373
                        170       180
                 ....*....|....*....|
gi 639310448 298 ADKALYQSKNTGRNKVIAYE 317
Cdd:PRK11829 374 ASTAMMAAHHEGRNQIMVFE 393
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
2-153 3.11e-04

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


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 42.07  E-value: 3.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448   2 AADLEMNEIH-WLMDMFNTVDVGLVVLDRDYKVCVWNGFMENHSGLLPSAVKDKDLFDLFPaidekwfrsKSESVFVLKN 80
Cdd:COG3829    1 AEELELKELEeELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIP---------NSPLLEVLKT 71
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 639310448  81 RsftiweqQPYIFRFKNYRPitgkaDYMYQNATFIPLTNTmGEVSHICIILYDVTdvavnkkELEELNKKLEQ 153
Cdd:COG3829   72 G-------KPVTGVIQKTGG-----KGKTVIVTAIPIFED-GEVIGAVETFRDIT-------ELKRLERKLRE 124
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
11-69 9.85e-04

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 36.99  E-value: 9.85e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 639310448    11 HWLMDMFNTVDVGLVVLDRDYKVCVWNGFMENHSGLLPSAVKDKDLFDLFPAIDEKWFR 69
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQ 59
 
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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