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Conserved domains on  [gi|491008780|ref|WP_004870495|]
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MULTISPECIES: sensor domain-containing diguanylate cyclase [Klebsiella]

Protein Classification

sensor domain-containing diguanylate cyclase( domain architecture ID 13503960)

sensor domain-containing diguanylate cyclase with double PDC (PhoQ/DcuS/CitA) domain(s), catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
279-508 1.25e-48

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: 169.00  E-value: 1.25e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 279 LVNLTRHETDIVAWSFALAAIVIVLFGLYLRHASRTVLMNIINAIKTGDVQRAPRLEAMLSKAIESNKQRELTYVRQATI 358
Cdd:COG2199   37 LLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATH 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 359 DALTGCKNRRAFDSDIAALMND----HHPFSLALVDIDNFKTINDTWGHLNGDIVLRNVAREGLQILQPLQIsLYRYGGE 434
Cdd:COG2199  117 DPLTGLPNRRAFEERLERELARarreGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDL-VARLGGD 195
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491008780 435 EFAVIFSDEHIDNALRLLESWRASVAQRSWREEG--LTVTFSAGLGEW--NMEPLEQLVVRVDEALYKAKQQGKNRIV 508
Cdd:COG2199  196 EFAVLLPGTDLEEAEALAERLREALEQLPFELEGkeLRVTVSIGVALYpeDGDSAEELLRRADLALYRAKRAGRNRVV 273
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
54-273 2.12e-14

Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains. This domain when present in chemoreceptors recognize several signals such as proteinogenic amino acids, GABA, Histamine and polyamines, decanoic acid, Autoinducer-2, purine derivatives, quaternary amines, citrate and taurine, among others. When associated with histidine kinases, it recognizes C3/C4-dicarboxylic acids, Spermine, guanosine and Autoinducer-2 (Mantilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


:

Pssm-ID: 460673 [Multi-domain]  Cd Length: 237  Bit Score: 72.75  E-value: 2.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780   54 NMATNYTETLLRGNDFILTrattFFARNDELNNAVNVNPEKGLMQLMQLQNMMQTVSSISLADTNGHYLRAPEVLETEDS 133
Cdd:pfam02743  16 KQLAENIESYLDSLEEILE----LLASNPDLQDLLSAPAEEELAKLESLLRSNPGISSIYLVDADGRVLASSDESPSYPG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780  134 QsfDAKSRPWFIK--QAQASTFSLYTSPYIDYFTHHPTITLYKPIISPEGRLKGSLAFHLDLTSMGYALRQMVAPVQGEF 211
Cdd:pfam02743  92 L--DVSERPWYKEalKGGGGIIWVFSSPYPSSESGEPVLTIARPIYDDDGEVIGVLVADLDLDTLQELLSQIKLGEGGYV 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491008780  212 FVVQRDGKVVLHPDPGALF---KPYVSEALMDRMTSGEGQLYDAVTDG--WY-YYYSFTNPDWFVIYR 273
Cdd:pfam02743 170 FIVDSDGRILAHPLGKNLRsllAPFLGKSLADALPGSGITEIAVDLDGedYLvAYAPIPGTGWTLVVV 237
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
279-508 1.25e-48

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: 169.00  E-value: 1.25e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 279 LVNLTRHETDIVAWSFALAAIVIVLFGLYLRHASRTVLMNIINAIKTGDVQRAPRLEAMLSKAIESNKQRELTYVRQATI 358
Cdd:COG2199   37 LLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATH 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 359 DALTGCKNRRAFDSDIAALMND----HHPFSLALVDIDNFKTINDTWGHLNGDIVLRNVAREGLQILQPLQIsLYRYGGE 434
Cdd:COG2199  117 DPLTGLPNRRAFEERLERELARarreGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDL-VARLGGD 195
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491008780 435 EFAVIFSDEHIDNALRLLESWRASVAQRSWREEG--LTVTFSAGLGEW--NMEPLEQLVVRVDEALYKAKQQGKNRIV 508
Cdd:COG2199  196 EFAVLLPGTDLEEAEALAERLREALEQLPFELEGkeLRVTVSIGVALYpeDGDSAEELLRRADLALYRAKRAGRNRVV 273
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
357-508 8.17e-46

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: 157.33  E-value: 8.17e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 357 TIDALTGCKNRRAFDSDIAALMN----DHHPFSLALVDIDNFKTINDTWGHLNGDIVLRNVAreglQILQ---PLQISLY 429
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLArarrSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVA----ERLRsslRESDLVA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 430 RYGGEEFAVIFSDEHIDNALRLLESWRASVAQRSWREEG-LTVTFSAGLGEW--NMEPLEQLVVRVDEALYKAKQQGKNR 506
Cdd:cd01949   77 RLGGDEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQeIRVTASIGIATYpeDGEDAEELLRRADEALYRAKRSGRNR 156

                 ..
gi 491008780 507 IV 508
Cdd:cd01949  157 VV 158
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
354-508 6.16e-39

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 139.30  E-value: 6.16e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780   354 RQATIDALTGCKNRRAFDS----DIAALMNDHHPFSLALVDIDNFKTINDTWGHLNGDIVLRNVAREGLQILQPLQIsLY 429
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEeleqELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDL-LA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780   430 RYGGEEFAVIFSDEHIDNALRLLESWRASVAQR--SWREEgLTVTFSAGLGEWN--MEPLEQLVVRVDEALYKAKQQGKN 505
Cdd:smart00267  80 RLGGDEFALLLPETSLEEAIALAERILQQLREPiiIHGIP-LYLTISIGVAAYPnpGEDAEDLLKRADTALYQAKKAGRN 158

                   ...
gi 491008780   506 RIV 508
Cdd:smart00267 159 QVA 161
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
356-506 5.31e-38

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: 136.61  E-value: 5.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780  356 ATIDALTGCKNRRAFDSDIAALMN----DHHPFSLALVDIDNFKTINDTWGHLNGDIVLRNVAREGLQILQPLQIsLYRY 431
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQralrEGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDL-VARL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780  432 GGEEFAVIFSDEHIDNALRLLESWRASVAQRS----WREEGLTVTFSAGLGEW--NMEPLEQLVVRVDEALYKAKQQGKN 505
Cdd:pfam00990  80 GGDEFAILLPETSLEGAQELAERIRRLLAKLKiphtVSGLPLYVTISIGIAAYpnDGEDPEDLLKRADTALYQAKQAGRN 159

                  .
gi 491008780  506 R 506
Cdd:pfam00990 160 R 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
355-508 7.36e-34

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: 125.53  E-value: 7.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780  355 QATIDALTGCKNRRAF----DSDIAALMNDHHPFSLALVDIDNFKTINDTWGHLNGDIVLRNVAREglqilqpLQISLY- 429
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLeemlDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARI-------LQSSVRg 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780  430 -----RYGGEEFAVIFSDEHIDNALRLLESWRASVAQRSW---REEGLTVTFSAGLGEWN--MEPLEQLVVRVDEALYKA 499
Cdd:TIGR00254  74 sdvvgRYGGEEFVVILPGTPLEDALSKAERLRDAINSKPIevaGSETLTVTVSIGVACYPghGLTLEELLKRADEALYQA 153

                  ....*....
gi 491008780  500 KQQGKNRIV 508
Cdd:TIGR00254 154 KKAGRNRVV 162
pleD PRK09581
response regulator PleD; Reviewed
353-508 2.54e-33

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 131.56  E-value: 2.54e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 353 VRQATIDALTGCKNRRAFDSDIAALMND----HHPFSLALVDIDNFKTINDTWGHLNGDIVLRNVAReglQILQPLQIS- 427
Cdd:PRK09581 289 IEMAVTDGLTGLHNRRYFDMHLKNLIERanerGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAK---RLRNNIRGTd 365
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 428 -LYRYGGEEFAVIFSDEHIDNALRLLESWRASVAQRSWR----EEGLTVTFSAGLGEWN--MEPLEQLVVRVDEALYKAK 500
Cdd:PRK09581 366 lIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIisdgKERLNVTVSIGVAELRpsGDTIEALIKRADKALYEAK 445

                 ....*...
gi 491008780 501 QQGKNRIV 508
Cdd:PRK09581 446 NTGRNRVV 453
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
54-273 2.12e-14

Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains. This domain when present in chemoreceptors recognize several signals such as proteinogenic amino acids, GABA, Histamine and polyamines, decanoic acid, Autoinducer-2, purine derivatives, quaternary amines, citrate and taurine, among others. When associated with histidine kinases, it recognizes C3/C4-dicarboxylic acids, Spermine, guanosine and Autoinducer-2 (Mantilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460673 [Multi-domain]  Cd Length: 237  Bit Score: 72.75  E-value: 2.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780   54 NMATNYTETLLRGNDFILTrattFFARNDELNNAVNVNPEKGLMQLMQLQNMMQTVSSISLADTNGHYLRAPEVLETEDS 133
Cdd:pfam02743  16 KQLAENIESYLDSLEEILE----LLASNPDLQDLLSAPAEEELAKLESLLRSNPGISSIYLVDADGRVLASSDESPSYPG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780  134 QsfDAKSRPWFIK--QAQASTFSLYTSPYIDYFTHHPTITLYKPIISPEGRLKGSLAFHLDLTSMGYALRQMVAPVQGEF 211
Cdd:pfam02743  92 L--DVSERPWYKEalKGGGGIIWVFSSPYPSSESGEPVLTIARPIYDDDGEVIGVLVADLDLDTLQELLSQIKLGEGGYV 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491008780  212 FVVQRDGKVVLHPDPGALF---KPYVSEALMDRMTSGEGQLYDAVTDG--WY-YYYSFTNPDWFVIYR 273
Cdd:pfam02743 170 FIVDSDGRILAHPLGKNLRsllAPFLGKSLADALPGSGITEIAVDLDGedYLvAYAPIPGTGWTLVVV 237
diguan_DgcJ NF040885
diguanylate cyclase DgcJ;
359-504 5.29e-13

diguanylate cyclase DgcJ;


Pssm-ID: 468821 [Multi-domain]  Cd Length: 490  Bit Score: 71.14  E-value: 5.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 359 DALTGCKNR----RAFDSDIAALMNDHHPFSLALVDIDNFKTINDTWGHLNGDIVLRNVAReglQILQPLQISLY--RYG 432
Cdd:NF040885 344 DSMTGLYNRkiltPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQ---AISASIRKSDYgiRLG 420
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491008780 433 GEEFAVIFSDEHIDNALRLLESWRASVAQrswREEGLTVTFSAglGEWNMEP---LEQLVVRVDEALYKAKQQGK 504
Cdd:NF040885 421 GDEFCIILIDYEEAEAQNLIERIRQHLRT---IDPDKRVSFSW--GAYQMQPgdtLDDAYKAADERLYLNKKQKH 490
PDC1_HK_sensor cd18773
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase ...
73-193 4.12e-07

first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase and similar domains; Histidine kinase (HK) receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. HK receptors in this family contain double PDC (PhoQ/DcuS/CitA) sensor domains. Signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses. The HK family includes not just histidine kinase receptors but also sensors for chemotaxis proteins and diguanylate cyclase receptors, implying a combinatorial molecular evolution.


Pssm-ID: 350341 [Multi-domain]  Cd Length: 125  Bit Score: 49.10  E-value: 4.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780  73 RATTFFARNDELNNAVNVNPEKGLMQLM-QLQNMMQTVSSISLADTNGHYLRAPEVlETEDSQSFDAKSRPWFIKQAQAS 151
Cdd:cd18773    6 LLLRSLASALEALAALGSADREELQALLrRLLERNPEISGIYVVDADGRVVASSDR-DPGGGDDDDDRDRFWYQAAKATG 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 491008780 152 TFSLyTSPYIDYFTHHPTITLYKPIISPEGRLKGSLAFHLDL 193
Cdd:cd18773   85 KLVI-SEPYISRVTGKPVITLSRPIRDADGRFIGVVGADIDL 125
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
279-508 1.25e-48

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: 169.00  E-value: 1.25e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 279 LVNLTRHETDIVAWSFALAAIVIVLFGLYLRHASRTVLMNIINAIKTGDVQRAPRLEAMLSKAIESNKQRELTYVRQATI 358
Cdd:COG2199   37 LLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATH 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 359 DALTGCKNRRAFDSDIAALMND----HHPFSLALVDIDNFKTINDTWGHLNGDIVLRNVAREGLQILQPLQIsLYRYGGE 434
Cdd:COG2199  117 DPLTGLPNRRAFEERLERELARarreGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDL-VARLGGD 195
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491008780 435 EFAVIFSDEHIDNALRLLESWRASVAQRSWREEG--LTVTFSAGLGEW--NMEPLEQLVVRVDEALYKAKQQGKNRIV 508
Cdd:COG2199  196 EFAVLLPGTDLEEAEALAERLREALEQLPFELEGkeLRVTVSIGVALYpeDGDSAEELLRRADLALYRAKRAGRNRVV 273
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
357-508 8.17e-46

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: 157.33  E-value: 8.17e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 357 TIDALTGCKNRRAFDSDIAALMN----DHHPFSLALVDIDNFKTINDTWGHLNGDIVLRNVAreglQILQ---PLQISLY 429
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLArarrSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVA----ERLRsslRESDLVA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 430 RYGGEEFAVIFSDEHIDNALRLLESWRASVAQRSWREEG-LTVTFSAGLGEW--NMEPLEQLVVRVDEALYKAKQQGKNR 506
Cdd:cd01949   77 RLGGDEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQeIRVTASIGIATYpeDGEDAEELLRRADEALYRAKRSGRNR 156

                 ..
gi 491008780 507 IV 508
Cdd:cd01949  157 VV 158
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
354-508 6.16e-39

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 139.30  E-value: 6.16e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780   354 RQATIDALTGCKNRRAFDS----DIAALMNDHHPFSLALVDIDNFKTINDTWGHLNGDIVLRNVAREGLQILQPLQIsLY 429
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEeleqELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDL-LA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780   430 RYGGEEFAVIFSDEHIDNALRLLESWRASVAQR--SWREEgLTVTFSAGLGEWN--MEPLEQLVVRVDEALYKAKQQGKN 505
Cdd:smart00267  80 RLGGDEFALLLPETSLEEAIALAERILQQLREPiiIHGIP-LYLTISIGVAAYPnpGEDAEDLLKRADTALYQAKKAGRN 158

                   ...
gi 491008780   506 RIV 508
Cdd:smart00267 159 QVA 161
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
356-506 5.31e-38

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: 136.61  E-value: 5.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780  356 ATIDALTGCKNRRAFDSDIAALMN----DHHPFSLALVDIDNFKTINDTWGHLNGDIVLRNVAREGLQILQPLQIsLYRY 431
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQralrEGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDL-VARL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780  432 GGEEFAVIFSDEHIDNALRLLESWRASVAQRS----WREEGLTVTFSAGLGEW--NMEPLEQLVVRVDEALYKAKQQGKN 505
Cdd:pfam00990  80 GGDEFAILLPETSLEGAQELAERIRRLLAKLKiphtVSGLPLYVTISIGIAAYpnDGEDPEDLLKRADTALYQAKQAGRN 159

                  .
gi 491008780  506 R 506
Cdd:pfam00990 160 R 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
355-508 7.36e-34

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: 125.53  E-value: 7.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780  355 QATIDALTGCKNRRAF----DSDIAALMNDHHPFSLALVDIDNFKTINDTWGHLNGDIVLRNVAREglqilqpLQISLY- 429
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLeemlDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARI-------LQSSVRg 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780  430 -----RYGGEEFAVIFSDEHIDNALRLLESWRASVAQRSW---REEGLTVTFSAGLGEWN--MEPLEQLVVRVDEALYKA 499
Cdd:TIGR00254  74 sdvvgRYGGEEFVVILPGTPLEDALSKAERLRDAINSKPIevaGSETLTVTVSIGVACYPghGLTLEELLKRADEALYQA 153

                  ....*....
gi 491008780  500 KQQGKNRIV 508
Cdd:TIGR00254 154 KKAGRNRVV 162
pleD PRK09581
response regulator PleD; Reviewed
353-508 2.54e-33

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 131.56  E-value: 2.54e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 353 VRQATIDALTGCKNRRAFDSDIAALMND----HHPFSLALVDIDNFKTINDTWGHLNGDIVLRNVAReglQILQPLQIS- 427
Cdd:PRK09581 289 IEMAVTDGLTGLHNRRYFDMHLKNLIERanerGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAK---RLRNNIRGTd 365
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 428 -LYRYGGEEFAVIFSDEHIDNALRLLESWRASVAQRSWR----EEGLTVTFSAGLGEWN--MEPLEQLVVRVDEALYKAK 500
Cdd:PRK09581 366 lIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIisdgKERLNVTVSIGVAELRpsGDTIEALIKRADKALYEAK 445

                 ....*...
gi 491008780 501 QQGKNRIV 508
Cdd:PRK09581 446 NTGRNRVV 453
PRK09894 PRK09894
diguanylate cyclase; Provisional
318-509 1.55e-31

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 123.25  E-value: 1.55e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 318 NIINAIKTGDVQRAP------RLEAMLSKAieSNKQRELTYVRqATIDALTGCKNRRAFDSDI--AALMNDHHPFSLALV 389
Cdd:PRK09894  88 ELLLAIVEGHWQDAHfdafqeGLLSFTAAL--TDYKIYLLTIR-SNMDVLTGLPGRRVLDESFdhQLRNREPQNLYLALL 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 390 DIDNFKTINDTWGHLNGDIVLRNVAREGLQILQPLQiSLYRYGGEEFAVIFSDEHIDNALRLLESWRASVA--QRSWREE 467
Cdd:PRK09894 165 DIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYE-TVYRYGGEEFIICLKAATDEEACRAGERIRQLIAnhAITHSDG 243
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 491008780 468 GLTVTFSAGLGEWNM-EPLEQLVVRVDEALYKAKQQGKNRIVR 509
Cdd:PRK09894 244 RINITATFGVSRAFPeETLDVVIGRADRAMYEGKQTGRNRVMF 286
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
234-508 4.71e-27

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: 115.26  E-value: 4.71e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 234 VSEALMDRMTSGEGQLYDAVTDGWYYYYSFTNPDWFVIYRVDNSTLVNLTRHETDIVAWSFALAAIVIVLFGLYLRHASR 313
Cdd:COG5001  129 LAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRL 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 314 TVLMNIINAIKTGDVQRAPRLEAMLSKAIESNKQRELTYVRQATIDALTGCKNRRAF----DSDIAALMNDHHPFSLALV 389
Cdd:COG5001  209 ALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFldrlEQALARARRSGRRLALLFI 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 390 DIDNFKTINDTWGHLNGDIVLRNVAREGLQILQPLQIsLYRYGGEEFAVIFSD-EHIDNALRLLESWRASVAQR-SWREE 467
Cdd:COG5001  289 DLDRFKEINDTLGHAAGDELLREVARRLRACLREGDT-VARLGGDEFAVLLPDlDDPEDAEAVAERILAALAEPfELDGH 367
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 491008780 468 GLTVTFSAGLGEWNM--EPLEQLVVRVDEALYKAKQQGKNRIV 508
Cdd:COG5001  368 ELYVSASIGIALYPDdgADAEELLRNADLAMYRAKAAGRNRYR 410
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
68-508 4.04e-26

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 112.03  E-value: 4.04e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780  68 DFILTRaTTFFARNDE-LNNAVNVNPEKG-LMQLMQLQNMMQ-TVSSISladTNGHYLRAPEVLETED--SQSFDAKSRP 142
Cdd:PRK15426 131 DAFVSG-LTLLSRDDEdLANELTAALELGyLLRLAHNSSSLVeRAMYVS---RAGFYVSTYPTLFPSDvpTRYYQYVTQP 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 143 WFIKQAQASTFS---LYTSPYIDYFTH-HPTITLYKPIISpEGRLKGSLAFHLDLTSMGYALRQMVAPVQ-GEFFVVQRD 217
Cdd:PRK15426 207 WFIGQSQRRNPGrgvRWFTSQPDDASNtEPQVTASVPVDA-GNYWYGVLAMDIPVRSLQQFLRNAIDKDLdGEYQLYDSH 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 218 GKVVLHPDP----GALFKPYVSEALMDRMTS-GEGQLYdavTDGWYYYYSftnpdwfviyRVDNSTLVNLTRHETD-IVA 291
Cdd:PRK15426 286 LRLLTSSAPgvrtGNIFDPRELALLARAMEHdTRGGIR---MGSRYVSWE----------RLDHFDGVLVRVHTLReGVR 352
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 292 WSFALAAIVIVLFGLYLrhasrTVLMNIINAIKTGdvqraprleaMLSKAIEsnKQRELTYvrQATIDALTGCKNRRAFD 371
Cdd:PRK15426 353 GDFGSISIALTLLWALF-----TAMLLISWYVIRR----------MVSNMFV--LQSSLQW--QAWHDPLTRLYNRGALF 413
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 372 SDIAALMN----DHHPFSLALVDIDNFKTINDTWGHLNGDIVLRNVAREGLQILQPLQIsLYRYGGEEFAVIFSDEHIDN 447
Cdd:PRK15426 414 EKARALAKrcqrDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDV-AGRVGGEEFCVVLPGASLAE 492
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491008780 448 ALRLLESWRasvaQRSWREEGL-----TVTFSAGLGEWNMEP-----LEQLVVRVDEALYKAKQQGKNRIV 508
Cdd:PRK15426 493 AAQVAERIR----LRINEKEILvakstTIRISASLGVSSAEEdgdydFEQLQSLADRRLYLAKQAGRNRVC 559
PRK09966 PRK09966
diguanylate cyclase DgcN;
353-509 4.18e-20

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 92.38  E-value: 4.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 353 VRQATIDALTGCKNRRAFDSDIAALMNDHHPFS---LALVDIDNFKTINDTWGHLNGDIVLRNVAREgLQILQPLQISLY 429
Cdd:PRK09966 245 LRTALHDPLTGLANRAAFRSGINTLMNNSDARKtsaLLFLDGDNFKYINDTWGHATGDRVLIEIAKR-LAEFGGLRHKAY 323
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 430 RYGGEEFAVIFSDEHIDNALRLLESWRASVAQRSWREEG---LTVTFSAGLG-EWNMEPLEQLVVRVDEALYKAKQQGKN 505
Cdd:PRK09966 324 RLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNghqTTMTLSIGYAmTIEHASAEKLQELADHNMYQAKHQRAE 403

                 ....
gi 491008780 506 RIVR 509
Cdd:PRK09966 404 KLVR 407
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
343-507 2.38e-16

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 82.41  E-value: 2.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780  343 ESNK-QRELTYvrQATIDALTGCKNRRAFDSDIAALMND----HHPFSLALVDIDNFKTINDTWGHLNGDIVLRNVAREG 417
Cdd:PRK09776  653 ESRKmLRQLSY--SASHDALTHLANRASFEKQLRRLLQTvnstHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLM 730
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780  418 LQILQPLQIsLYRYGGEEFAVIFSDEHIDNALRLLESWRASVAQRSWREEG--LTVTFSAGLGEWNME--PLEQLVVRVD 493
Cdd:PRK09776  731 LSMLRSSDV-LARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPWEGrvYRVGASAGITLIDANnhQASEVMSQAD 809
                         170
                  ....*....|....
gi 491008780  494 EALYKAKQQGKNRI 507
Cdd:PRK09776  810 IACYAAKNAGRGRV 823
adrA PRK10245
diguanylate cyclase AdrA; Provisional
292-506 4.53e-15

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 76.79  E-value: 4.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 292 WSFALAAIVI--VLFGlYLRHASrtvlmniinAIKTGDVQRapRLEAMLSKaiesnkqreltyvrqatiDALTGCKNRRA 369
Cdd:PRK10245 169 WWLSLPVIVIypLLFA-WVSYQT---------ATKLAEHKR--RLQVMSTR------------------DGMTGVYNRRH 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 370 FDS----DIAALMNDHHPFSLALVDIDNFKTINDTWGHLNGDIVLRNVAREglqilqpLQISLY------RYGGEEFAVI 439
Cdd:PRK10245 219 WETllrnEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQ-------LQITLRgsdvigRFGGDEFAVI 291
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 440 FSDEHIDNAlrlleswrasVAQRSWREEGL-----------TVTFSAGLGEWN--MEPLEQLVVRVDEALYKAKQQGKNR 506
Cdd:PRK10245 292 MSGTPAESA----------ITAMSRVHEGLntlrlpnapqvTLRISVGVAPLNpqMSHYREWLKSADLALYKAKNAGRNR 361
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
54-273 2.12e-14

Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains. This domain when present in chemoreceptors recognize several signals such as proteinogenic amino acids, GABA, Histamine and polyamines, decanoic acid, Autoinducer-2, purine derivatives, quaternary amines, citrate and taurine, among others. When associated with histidine kinases, it recognizes C3/C4-dicarboxylic acids, Spermine, guanosine and Autoinducer-2 (Mantilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460673 [Multi-domain]  Cd Length: 237  Bit Score: 72.75  E-value: 2.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780   54 NMATNYTETLLRGNDFILTrattFFARNDELNNAVNVNPEKGLMQLMQLQNMMQTVSSISLADTNGHYLRAPEVLETEDS 133
Cdd:pfam02743  16 KQLAENIESYLDSLEEILE----LLASNPDLQDLLSAPAEEELAKLESLLRSNPGISSIYLVDADGRVLASSDESPSYPG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780  134 QsfDAKSRPWFIK--QAQASTFSLYTSPYIDYFTHHPTITLYKPIISPEGRLKGSLAFHLDLTSMGYALRQMVAPVQGEF 211
Cdd:pfam02743  92 L--DVSERPWYKEalKGGGGIIWVFSSPYPSSESGEPVLTIARPIYDDDGEVIGVLVADLDLDTLQELLSQIKLGEGGYV 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491008780  212 FVVQRDGKVVLHPDPGALF---KPYVSEALMDRMTSGEGQLYDAVTDG--WY-YYYSFTNPDWFVIYR 273
Cdd:pfam02743 170 FIVDSDGRILAHPLGKNLRsllAPFLGKSLADALPGSGITEIAVDLDGedYLvAYAPIPGTGWTLVVV 237
diguan_DgcJ NF040885
diguanylate cyclase DgcJ;
359-504 5.29e-13

diguanylate cyclase DgcJ;


Pssm-ID: 468821 [Multi-domain]  Cd Length: 490  Bit Score: 71.14  E-value: 5.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 359 DALTGCKNR----RAFDSDIAALMNDHHPFSLALVDIDNFKTINDTWGHLNGDIVLRNVAReglQILQPLQISLY--RYG 432
Cdd:NF040885 344 DSMTGLYNRkiltPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQ---AISASIRKSDYgiRLG 420
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491008780 433 GEEFAVIFSDEHIDNALRLLESWRASVAQrswREEGLTVTFSAglGEWNMEP---LEQLVVRVDEALYKAKQQGK 504
Cdd:NF040885 421 GDEFCIILIDYEEAEAQNLIERIRQHLRT---IDPDKRVSFSW--GAYQMQPgdtLDDAYKAADERLYLNKKQKH 490
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
343-504 6.24e-13

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 71.25  E-value: 6.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 343 ESNKQRELTyvRQATIDALTGCKNRRAFDSDIAALMNDHHPFSLALV--DIDNFKTINDTWGHLNGDIVLRNVAREGLQI 420
Cdd:PRK10060 226 ERRAQERLR--ILANTDSITGLPNRNAIQELIDHAINAADNNQVGIVylDLDNFKKVNDAYGHMFGDQLLQDVSLAILSC 303
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 421 LQPLQIsLYRYGGEEFAVIFSdehiDNALRLLEswraSVAQRSWreEGLTVTFSAGLGE--------WNMEP-----LEQ 487
Cdd:PRK10060 304 LEEDQT-LARLGGDEFLVLAS----HTSQAALE----AMASRIL--TRLRLPFRIGLIEvytgcsigIALAPehgddSES 372
                        170
                 ....*....|....*..
gi 491008780 488 LVVRVDEALYKAKQQGK 504
Cdd:PRK10060 373 LIRSADTAMYTAKEGGR 389
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
383-477 2.70e-10

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: 58.14  E-value: 2.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 383 PFSLALVDIDNFKTINDTWGHLNGDIVLRNVAREGLQILQPLQISLYRYGGEEFAVIFSDEHIDNALRLLESWRASVAQR 462
Cdd:cd07556    1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAL 80
                         90
                 ....*....|....*
gi 491008780 463 SWrEEGLTVTFSAGL 477
Cdd:cd07556   81 NQ-SEGNPVRVRIGI 94
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
343-461 2.10e-09

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 60.17  E-value: 2.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780 343 ESNKQRELTYVRqatIDALTGCKNRRAFDSDIAALMNDHHPFSLALVDIDNFKTINDTWGHLNGDIVLRNVAREGLQILQ 422
Cdd:PRK11359 366 EKSRQHIEQLIQ---FDPLTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLK 442
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 491008780 423 PLQIsLYRYGGEEFAVIFSDEHIDNALRLLESWRASVAQ 461
Cdd:PRK11359 443 PDQY-LCRIEGTQFVLVSLENDVSNITQIADELRNVVSK 480
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
428-500 6.65e-08

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: 52.60  E-value: 6.65e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491008780 428 LYRYGGEEFAVIFSDEHIDNALRLLESWRASVAQrswrEEGLTVTFSAGLGEwnmeplEQLVVRVDeALYKAK 500
Cdd:COG3706  118 VARYGGEEFAILLPGTDLEGALAVAERIREAVAE----LPSLRVTVSIGVAG------DSLLKRAD-ALYQAR 179
PDC1_HK_sensor cd18773
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase ...
73-193 4.12e-07

first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase and similar domains; Histidine kinase (HK) receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. HK receptors in this family contain double PDC (PhoQ/DcuS/CitA) sensor domains. Signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses. The HK family includes not just histidine kinase receptors but also sensors for chemotaxis proteins and diguanylate cyclase receptors, implying a combinatorial molecular evolution.


Pssm-ID: 350341 [Multi-domain]  Cd Length: 125  Bit Score: 49.10  E-value: 4.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780  73 RATTFFARNDELNNAVNVNPEKGLMQLM-QLQNMMQTVSSISLADTNGHYLRAPEVlETEDSQSFDAKSRPWFIKQAQAS 151
Cdd:cd18773    6 LLLRSLASALEALAALGSADREELQALLrRLLERNPEISGIYVVDADGRVVASSDR-DPGGGDDDDDRDRFWYQAAKATG 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 491008780 152 TFSLyTSPYIDYFTHHPTITLYKPIISPEGRLKGSLAFHLDL 193
Cdd:cd18773   85 KLVI-SEPYISRVTGKPVITLSRPIRDADGRFIGVVGADIDL 125
PDC1_DGC_like cd12914
first PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this ...
64-193 4.38e-06

first PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the first PDC domain of Diguanylate-cyclases (DGCs), Histidine kinases (HKs), and other similar domains. Many members of this subfamily contain a C-terminal DGC (also called GGDEF) domain. DGCs regulate the turnover of cyclic diguanosine monophosphate. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


Pssm-ID: 350339  Cd Length: 123  Bit Score: 45.84  E-value: 4.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008780  64 LRGNDFILTRAttffARNDELNNAVNVNPEKGLMQLMQLQNMMQTVSSISLADTNGHYLRAPEVLETEDsqsFDAKSRPW 143
Cdd:cd12914    1 LDEADLLLRSL----ADDLEARGAASADPAALQALLRRLLARLPEVRSIFVVDADGRVVASSGPGPAPG---LDVSDRDY 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491008780 144 FiKQAQASTFSLYTS-PYIDYFTHHPTITLYKPIISPEGRLKGSLAFHLDL 193
Cdd:cd12914   74 F-QAARAGGGGLFISePVISRVTGKPVIPLSRPIRDADGRFAGVVVASIDL 123
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
209-277 1.78e-05

second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the second PDC domain of Methyl-accepting chemotaxis proteins (MCPs), Histidine kinases (HKs), and other similar domains. Many members contain both HAMP (HK, Adenylyl cyclase, MCP, and Phosphatase) and MCP domains, which are signalling domains that interact with protein partners to relay a signal. MCPs are part of a transmembrane protein complex that controls bacterial chemotaxis. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


Pssm-ID: 350337 [Multi-domain]  Cd Length: 92  Bit Score: 43.14  E-value: 1.78e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491008780 209 GEFFVVQRDGKVVLHPDPGALFK-----PYVSEALMDRMTSGEGQLYDAVTDG---WYYYYSFTNPDWFVIYRVDNS 277
Cdd:cd12912   15 GYAFLVDKDGTIIAHPDKELVGKkisddEAAEEELAKKMLAGKSGSVEYTFNGekkYVAYAPIPGTGWSLVVVVPES 91
PDC2_HK_sensor cd18774
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, ...
208-275 3.44e-03

second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase and similar domains; Histidine kinase (HK) receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. HK receptors in this family contain double PDC (PhoQ/DcuS/CitA) sensor domains. Signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses. The HK family includes not just histidine kinase receptors but also sensors for chemotaxis proteins and diguanylate cyclase receptors, implying a combinatorial molecular evolution.


Pssm-ID: 350342 [Multi-domain]  Cd Length: 89  Bit Score: 36.65  E-value: 3.44e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491008780 208 QGEFFVVQRDGKVVLHPDPGALFK---PYVSEALMDRMTSGE-GQLYDAVTDG---WYYYYSFTNPDWFVIYRVD 275
Cdd:cd18774   14 TGYAFLVDSDGTILAHPPKELVGKgksLDDLALLAALLLAGEsGTFEYTSDDGverLVAYRPVPGTPWVVVVGVP 88
 
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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