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Conserved domains on  [gi|514970439|ref|WP_016658730|]
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MULTISPECIES: GGDEF domain-containing protein [Acinetobacter]

Protein Classification

GGDEF domain-containing protein( domain architecture ID 10005578)

GGDEF domain-containing protein may have diguanylate cyclase (DGC) activity, similar to Escherichia coli DgcT (YcdT) and to E. coli CdgI (YeaI), a c-di-GMP-binding effector with a degenerate GGDEF domain which binds c-di-GMP

CATH:  3.30.70.270
EC:  2.7.7.65
Gene Ontology:  GO:0005525|GO:0046872|GO:0052621|GO:0005886
PubMed:  11119645|15063857|15289546|15306016|16530465|16045609

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 ...
 124-388 1.92e-61

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: 199.43  E-value: 1.92e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 124 LVGVLSPATMVTYISLPTVGLVLFERRIVYSALIPATLYLVSCGYLSFFGQLTYAPLFLLTDFPYKNGFWVLSMLFFIVP 203
Cdd:COG2199    4 LLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLEL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 204 ILLTCLVLFEIL----LSQWRYREALIAHLSQVDPLTNTFNRRSINQCLEQL---NHKQAPSYAVILVDLDHFKQINDEH 276
Cdd:COG2199   84 LLLLLALLLLLLaledITELRRLEERLRRLATHDPLTGLPNRRAFEERLERElarARREGRPLALLLIDLDHFKRINDTY 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 277 GHHKGDEALVQVCHVLAGHIREQDVLGRFGGEEFILVLKQATAHQAKQVAERCRQAITQIELYDEhNQPIHFTASFGIA- 355
Cdd:COG2199  164 GHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELE-GKELRVTVSIGVAl 242

                        250       260       270
                 ....*....|....*....|....*....|...
gi 514970439 356 LSHHNTPYEKLLSQADQALYQAKAYGRNQVVLY 388
Cdd:COG2199  243 YPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 124-388 1.92e-61

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: 199.43  E-value: 1.92e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 124 LVGVLSPATMVTYISLPTVGLVLFERRIVYSALIPATLYLVSCGYLSFFGQLTYAPLFLLTDFPYKNGFWVLSMLFFIVP 203
Cdd:COG2199    4 LLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLEL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 204 ILLTCLVLFEIL----LSQWRYREALIAHLSQVDPLTNTFNRRSINQCLEQL---NHKQAPSYAVILVDLDHFKQINDEH 276
Cdd:COG2199   84 LLLLLALLLLLLaledITELRRLEERLRRLATHDPLTGLPNRRAFEERLERElarARREGRPLALLLIDLDHFKRINDTY 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 277 GHHKGDEALVQVCHVLAGHIREQDVLGRFGGEEFILVLKQATAHQAKQVAERCRQAITQIELYDEhNQPIHFTASFGIA- 355
Cdd:COG2199  164 GHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELE-GKELRVTVSIGVAl 242

                        250       260       270
                 ....*....|....*....|....*....|...
gi 514970439 356 LSHHNTPYEKLLSQADQALYQAKAYGRNQVVLY 388
Cdd:COG2199  243 YPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 233-386 2.27e-59

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: 189.69  E-value: 2.27e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 233 DPLTNTFNRRSINQCLEQL---NHKQAPSYAVILVDLDHFKQINDEHGHHKGDEALVQVCHVLAGHIREQDVLGRFGGEE 309
Cdd:cd01949    3 DPLTGLPNRRAFEERLERLlarARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514970439 310 FILVLKQATAHQAKQVAERCRQAITQieLYDEHNQPIHFTASFGIALSH-HNTPYEKLLSQADQALYQAKAYGRNQVV 386
Cdd:cd01949   83 FAILLPGTDLEEAEALAERLREAIEE--PFFIDGQEIRVTASIGIATYPeDGEDAEELLRRADEALYRAKRSGRNRVV 158
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 230-384 3.93e-53

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: 173.98  E-value: 3.93e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439  230 SQVDPLTNTFNRRSINQCLEQL---NHKQAPSYAVILVDLDHFKQINDEHGHHKGDEALVQVCHVLAGHIREQDVLGRFG 306
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQElqrALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439  307 GEEFILVLKQATAHQAKQVAERCRQAITQIELYDEHN-QPIHFTASFGIALSH-HNTPYEKLLSQADQALYQAKAYGRNQ 384
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSgLPLYVTISIGIAAYPnDGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 228-388 7.98e-49

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 162.80  E-value: 7.98e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439   228 HLSQVDPLTNTFNRRSINQCLEQ-LNHKQAP--SYAVILVDLDHFKQINDEHGHHKGDEALVQVCHVLAGHIREQDVLGR 304
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQeLQRAQRQgsPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439   305 FGGEEFILVLKQATAHQAKQVAERCRQAITQieLYDEHNQPIHFTASFGIALSH-HNTPYEKLLSQADQALYQAKAYGRN 383
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLRE--PIIIHGIPLYLTISIGVAAYPnPGEDAEDLLKRADTALYQAKKAGRN 158


                   ....*
gi 514970439   384 QVVLY 388
Cdd:smart00267 159 QVAVY 163
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 229-387 6.18e-46

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: 155.57  E-value: 6.18e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439  229 LSQVDPLTNTFNRRSINQCLEQLNHKQAP---SYAVILVDLDHFKQINDEHGHHKGDEALVQVCHVLAGHIREQDVLGRF 305
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRfqrSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439  306 GGEEFILVLKQATAHQAKQVAERCRQAITQIELYDEHNQPIHFTASFGIA-LSHHNTPYEKLLSQADQALYQAKAYGRNQ 384
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVAcYPGHGLTLEELLKRADEALYQAKKAGRNR 160


                  ...
gi 514970439  385 VVL 387
Cdd:TIGR00254 161 VVV 163
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
229-385 1.50e-44

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 154.75  E-value: 1.50e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 229 LSQVDPLTNTFNRRsinQCLEQLNHKQA------PSYAVILVDLDHFKQINDEHGHHKGDEALVQVCHVLAGHIREQDVL 302
Cdd:NF038266  93 ASTRDPLTGLPNRR---LLMERLREEVErarrsgRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLC 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 303 GRFGGEEFILVLKQATAHQAKQVAERCRQAITQIELYDEHNQPiHFTASFGIALshHNTPYEKL---LSQADQALYQAKA 379
Cdd:NF038266 170 GRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVL-SVTASAGLAE--HRPPEEGLsatLSRADQALYQAKR 246


                 ....*.
gi 514970439 380 YGRNQV 385
Cdd:NF038266 247 AGRDRV 252
PRK09894 PRK09894
diguanylate cyclase; Provisional
 211-390 1.85e-42

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 150.60  E-value: 1.85e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 211 LFEILLSQWRYREALIAHLSQVDPLTNTFNRRSINQCLE-QLNHKQAPSYAVILVDLDHFKQINDEHGHHKGDEALVQVC 289
Cdd:PRK09894 110 LLSFTAALTDYKIYLLTIRSNMDVLTGLPGRRVLDESFDhQLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLA 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 290 HVLAGHIREQDVLGRFGGEEFILVLKQATAHQAKQVAERCRQAI--TQIELYDEHnqpIHFTASFGIALSHHNTPYEKLL 367
Cdd:PRK09894 190 TYLASWTRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIanHAITHSDGR---INITATFGVSRAFPEETLDVVI 266

                        170       180
                 ....*....|....*....|...
gi 514970439 368 SQADQALYQAKAYGRNQVVLYQP 390
Cdd:PRK09894 267 GRADRAMYEGKQTGRNRVMFIDE 289
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 124-388 1.92e-61

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: 199.43  E-value: 1.92e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 124 LVGVLSPATMVTYISLPTVGLVLFERRIVYSALIPATLYLVSCGYLSFFGQLTYAPLFLLTDFPYKNGFWVLSMLFFIVP 203
Cdd:COG2199    4 LLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLEL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 204 ILLTCLVLFEIL----LSQWRYREALIAHLSQVDPLTNTFNRRSINQCLEQL---NHKQAPSYAVILVDLDHFKQINDEH 276
Cdd:COG2199   84 LLLLLALLLLLLaledITELRRLEERLRRLATHDPLTGLPNRRAFEERLERElarARREGRPLALLLIDLDHFKRINDTY 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 277 GHHKGDEALVQVCHVLAGHIREQDVLGRFGGEEFILVLKQATAHQAKQVAERCRQAITQIELYDEhNQPIHFTASFGIA- 355
Cdd:COG2199  164 GHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELE-GKELRVTVSIGVAl 242

                        250       260       270
                 ....*....|....*....|....*....|...
gi 514970439 356 LSHHNTPYEKLLSQADQALYQAKAYGRNQVVLY 388
Cdd:COG2199  243 YPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 233-386 2.27e-59

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: 189.69  E-value: 2.27e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 233 DPLTNTFNRRSINQCLEQL---NHKQAPSYAVILVDLDHFKQINDEHGHHKGDEALVQVCHVLAGHIREQDVLGRFGGEE 309
Cdd:cd01949    3 DPLTGLPNRRAFEERLERLlarARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514970439 310 FILVLKQATAHQAKQVAERCRQAITQieLYDEHNQPIHFTASFGIALSH-HNTPYEKLLSQADQALYQAKAYGRNQVV 386
Cdd:cd01949   83 FAILLPGTDLEEAEALAERLREAIEE--PFFIDGQEIRVTASIGIATYPeDGEDAEELLRRADEALYRAKRSGRNRVV 158
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 230-384 3.93e-53

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: 173.98  E-value: 3.93e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439  230 SQVDPLTNTFNRRSINQCLEQL---NHKQAPSYAVILVDLDHFKQINDEHGHHKGDEALVQVCHVLAGHIREQDVLGRFG 306
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQElqrALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439  307 GEEFILVLKQATAHQAKQVAERCRQAITQIELYDEHN-QPIHFTASFGIALSH-HNTPYEKLLSQADQALYQAKAYGRNQ 384
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSgLPLYVTISIGIAAYPnDGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 228-388 7.98e-49

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 162.80  E-value: 7.98e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439   228 HLSQVDPLTNTFNRRSINQCLEQ-LNHKQAP--SYAVILVDLDHFKQINDEHGHHKGDEALVQVCHVLAGHIREQDVLGR 304
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQeLQRAQRQgsPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439   305 FGGEEFILVLKQATAHQAKQVAERCRQAITQieLYDEHNQPIHFTASFGIALSH-HNTPYEKLLSQADQALYQAKAYGRN 383
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLRE--PIIIHGIPLYLTISIGVAAYPnPGEDAEDLLKRADTALYQAKKAGRN 158


                   ....*
gi 514970439   384 QVVLY 388
Cdd:smart00267 159 QVAVY 163
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 193-390 6.46e-47

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: 170.34  E-value: 6.46e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 193 WVLSMLFFIVPILLTCLVLFEILLSQWRYREALIAHLSQVDPLTNTFNRRSINQCLEQL---NHKQAPSYAVILVDLDHF 269
Cdd:COG5001  214 LGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQAlarARRSGRRLALLFIDLDRF 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 270 KQINDEHGHHKGDEALVQVCHVLAGHIREQDVLGRFGGEEFILVLKQ-ATAHQAKQVAERCRQAITQ-IELydeHNQPIH 347
Cdd:COG5001  294 KEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDlDDPEDAEAVAERILAALAEpFEL---DGHELY 370

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 514970439 348 FTASFGIALS-HHNTPYEKLLSQADQALYQAKAYGRNQVVLYQP 390
Cdd:COG5001  371 VSASIGIALYpDDGADAEELLRNADLAMYRAKAAGRNRYRFFDP 414
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 229-387 6.18e-46

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: 155.57  E-value: 6.18e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439  229 LSQVDPLTNTFNRRSINQCLEQLNHKQAP---SYAVILVDLDHFKQINDEHGHHKGDEALVQVCHVLAGHIREQDVLGRF 305
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRfqrSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439  306 GGEEFILVLKQATAHQAKQVAERCRQAITQIELYDEHNQPIHFTASFGIA-LSHHNTPYEKLLSQADQALYQAKAYGRNQ 384
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVAcYPGHGLTLEELLKRADEALYQAKKAGRNR 160


                  ...
gi 514970439  385 VVL 387
Cdd:TIGR00254 161 VVV 163
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
229-385 1.50e-44

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 154.75  E-value: 1.50e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 229 LSQVDPLTNTFNRRsinQCLEQLNHKQA------PSYAVILVDLDHFKQINDEHGHHKGDEALVQVCHVLAGHIREQDVL 302
Cdd:NF038266  93 ASTRDPLTGLPNRR---LLMERLREEVErarrsgRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLC 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 303 GRFGGEEFILVLKQATAHQAKQVAERCRQAITQIELYDEHNQPiHFTASFGIALshHNTPYEKL---LSQADQALYQAKA 379
Cdd:NF038266 170 GRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVL-SVTASAGLAE--HRPPEEGLsatLSRADQALYQAKR 246


                 ....*.
gi 514970439 380 YGRNQV 385
Cdd:NF038266 247 AGRDRV 252
PRK09894 PRK09894
diguanylate cyclase; Provisional
 211-390 1.85e-42

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 150.60  E-value: 1.85e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 211 LFEILLSQWRYREALIAHLSQVDPLTNTFNRRSINQCLE-QLNHKQAPSYAVILVDLDHFKQINDEHGHHKGDEALVQVC 289
Cdd:PRK09894 110 LLSFTAALTDYKIYLLTIRSNMDVLTGLPGRRVLDESFDhQLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLA 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 290 HVLAGHIREQDVLGRFGGEEFILVLKQATAHQAKQVAERCRQAI--TQIELYDEHnqpIHFTASFGIALSHHNTPYEKLL 367
Cdd:PRK09894 190 TYLASWTRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIanHAITHSDGR---INITATFGVSRAFPEETLDVVI 266

                        170       180
                 ....*....|....*....|...
gi 514970439 368 SQADQALYQAKAYGRNQVVLYQP 390
Cdd:PRK09894 267 GRADRAMYEGKQTGRNRVMFIDE 289
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
233-386 3.80e-42

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 155.56  E-value: 3.80e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 233 DPLTNTFNRRSIN---QCLEQLNHKQAPSYAVILVDLDHFKQINDEHGHHKGDEALVQVCHVLAGHIREQDVLGRFGGEE 309
Cdd:PRK15426 401 DPLTRLYNRGALFekaRALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEE 480

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514970439 310 FILVLKQATAHQAKQVAERCRQAITQIELYDEHNQPIHFTASFGIALSHHNTPY--EKLLSQADQALYQAKAYGRNQVV 386
Cdd:PRK15426 481 FCVVLPGASLAEAAQVAERIRLRINEKEILVAKSTTIRISASLGVSSAEEDGDYdfEQLQSLADRRLYLAKQAGRNRVC 559
pleD PRK09581
response regulator PleD; Reviewed
 220-386 5.00e-42

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 153.13  E-value: 5.00e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 220 RYREALIAHLSQ------VDPLTNTFNRR----SINQCLEQLNHKQAPsYAVILVDLDHFKQINDEHGHHKGDEALVQVC 289
Cdd:PRK09581 276 RYQDALRNNLEQsiemavTDGLTGLHNRRyfdmHLKNLIERANERGKP-LSLMMIDIDHFKKVNDTYGHDAGDEVLREFA 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 290 HVLAGHIREQDVLGRFGGEEFILVLKQATAHQAKQVAERCRQAITQIELYDEH-NQPIHFTASFGIA-LSHHNTPYEKLL 367
Cdd:PRK09581 355 KRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDgKERLNVTVSIGVAeLRPSGDTIEALI 434

                        170
                 ....*....|....*....
gi 514970439 368 SQADQALYQAKAYGRNQVV 386
Cdd:PRK09581 435 KRADKALYEAKNTGRNRVV 453
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 233-395 2.20e-25

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 108.61  E-value: 2.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439  233 DPLTNTFNRRSINQCLEQL---NHKQAPSYAVILVDLDHFKQINDEHGHHKGDEALVQVCHVLAGHIREQDVLGRFGGEE 309
Cdd:PRK09776  668 DALTHLANRASFEKQLRRLlqtVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDE 747

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439  310 FILVLKQATAHQAKQVAERCRQAITQI------ELYDehnqpihFTASFGI-ALSHHNTPYEKLLSQADQALYQAKAYGR 382
Cdd:PRK09776  748 FGLLLPDCNVESARFIATRIISAINDYhfpwegRVYR-------VGASAGItLIDANNHQASEVMSQADIACYAAKNAGR 820

                         170
                  ....*....|...
gi 514970439  383 NQVVLYQPLEPAA 395
Cdd:PRK09776  821 GRVTVYEPQQAAA 833
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 200-390 1.75e-21

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 96.76  E-value: 1.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 200 FIVPILLTCLVLFEILLSQWRYREAlIAHLSQVDPLTNTFNRRSINQCLEQLNHKQaPSYAVILVDLDHFKQINDEHGHH 279
Cdd:PRK11359 347 FIERVADISQHLAALALEQEKSRQH-IEQLIQFDPLTGLPNRNNLHNYLDDLVDKA-VSPVVYLIGVDHFQDVIDSLGYA 424

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 280 KGDEALVQVCHVLAGHIREQDVLGRFGGEEFILVLKQATAHQAKQVAERCRQAITQIELYDEHnqPIHFTASFGIalSHH 359
Cdd:PRK11359 425 WADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPIMIDDK--PFPLTLSIGI--SYD 500

                        170       180       190
                 ....*....|....*....|....*....|..
gi 514970439 360 -NTPYEKLLSQADQALYQAKAYGRNQVVLYQP 390
Cdd:PRK11359 501 vGKNRDYLLSTAHNAMDYIRKNGGNGWQFFSP 532
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 206-384 1.31e-20

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 92.20  E-value: 1.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 206 LTCLVLFEILLSQWRYREA--LIAH------LSQVDPLTNTFNRRSINQCLE------QLNHKQApsyAVILVDLDHFKQ 271
Cdd:PRK10245 173 LPVIVIYPLLFAWVSYQTAtkLAEHkrrlqvMSTRDGMTGVYNRRHWETLLRnefdncRRHHRDA---TLLIIDIDHFKS 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 272 INDEHGHHKGDEALVQVCHVLAGHIREQDVLGRFGGEEFILVLKQATAHQAKQVAERCRQAITQIELYDEHNQPIHFtaS 351
Cdd:PRK10245 250 INDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPQVTLRI--S 327

                        170       180       190
                 ....*....|....*....|....*....|....
gi 514970439 352 FGIA-LSHHNTPYEKLLSQADQALYQAKAYGRNQ 384
Cdd:PRK10245 328 VGVApLNPQMSHYREWLKSADLALYKAKNAGRNR 361
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
216-390 2.12e-20

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 93.21  E-value: 2.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 216 LSQWRYREaliahLSQVDPLTNTFNRRSINqclEQLNH--KQAPSYAVILV--DLDHFKQINDEHGHHKGDEALVQVCHV 291
Cdd:PRK10060 228 RAQERLRI-----LANTDSITGLPNRNAIQ---ELIDHaiNAADNNQVGIVylDLDNFKKVNDAYGHMFGDQLLQDVSLA 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 292 LAGHIREQDVLGRFGGEEFILVLKQATAHQ----AKQVAERCRQ--AITQIELYDehnqpihfTASFGIALS-HHNTPYE 364
Cdd:PRK10060 300 ILSCLEEDQTLARLGGDEFLVLASHTSQAAleamASRILTRLRLpfRIGLIEVYT--------GCSIGIALApEHGDDSE 371

                        170       180
                 ....*....|....*....|....*.
gi 514970439 365 KLLSQADQALYQAKAYGRNQVVLYQP 390
Cdd:PRK10060 372 SLIRSADTAMYTAKEGGRGQFCVFSP 397
PRK09966 PRK09966
diguanylate cyclase DgcN;
216-378 3.04e-18

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 85.83  E-value: 3.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 216 LSQWRYR-EALIAHLSQV---DPLTNTFNRRSINQCLEQL--NHKQAPSYAVILVDLDHFKQINDEHGHHKGDEALVQVC 289
Cdd:PRK09966 230 MEEWQLRlQAKNAQLLRTalhDPLTGLANRAAFRSGINTLmnNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIA 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 290 HVLA--GHIREQDVlgRFGGEEFILVLKQatAHQAKQVAERCrQAITQI--ELYDEHN-QPIHFTASFGIALSHHNTPYE 364
Cdd:PRK09966 310 KRLAefGGLRHKAY--RLGGDEFAMVLYD--VQSESEVQQIC-SALTQIfnLPFDLHNgHQTTMTLSIGYAMTIEHASAE 384

                        170
                 ....*....|....
gi 514970439 365 KLLSQADQALYQAK 378
Cdd:PRK09966 385 KLQELADHNMYQAK 398
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 300-378 7.10e-15

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 72.25  E-value: 7.10e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514970439 300 DVLGRFGGEEFILVLKQATAHQAKQVAERCRQAItqielydEHNQPIHFTASFGIAlshhntpYEKLLSQADqALYQAK 378
Cdd:COG3706  116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAV-------AELPSLRVTVSIGVA-------GDSLLKRAD-ALYQAR 179
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 261-386 1.96e-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: 1.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 261 VILVDLDHFKQINDEHGHHKGDEALVQVCHVLAGHIRE-QDVLGRFGGEEFILVLKQATAHQAKQVAERCRQAItqiely 339
Cdd:cd07556    4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRsGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAV------ 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 514970439 340 DEHNQP--IHFTASFGIA----------LSHHNTPYEKLLSQADQALYQAKAygrNQVV 386
Cdd:cd07556   78 SALNQSegNPVRVRIGIHtgpvvvgvigSRPQYDVWGALVNLASRMESQAKA---GQVL 133
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 224-390 1.97e-04

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 43.39  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 224 ALIAHLSQVDPLTNTFNRRSINQCLEQLNHKQAPS--YAVILVDLDHFKQINDEHGHHKGDEALVQVCHVLAGHIREQDV 301
Cdd:PRK11829 226 ADMGRISHRFPVTELPNRSLFISLLEKEIASSTRTdhFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDL 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 302 LGRFGGEEF-ILVLKQATAHQAKQVAERCRQAITQIELYDehNQPIHFTASFGIALSH-HNTPYEKLLSQADQALYQAKA 379
Cdd:PRK11829 306 LAQLSKTEFaVLARGTRRSFPAMQLARRIMSQVTQPLFFD--EITLRPSASIGITRYQaQQDTAESMMRNASTAMMAAHH 383

                        170
                 ....*....|.
gi 514970439 380 YGRNQVVLYQP 390
Cdd:PRK11829 384 EGRNQIMVFEP 394
Cas10 COG1353
CRISPR/Cas system-associated protein Cas10, large subunit of type III CRISPR-Cas systems, ...
 306-383 8.21e-04

CRISPR/Cas system-associated protein Cas10, large subunit of type III CRISPR-Cas systems, contains HD superfamily nuclease domain [Defense mechanisms]; CRISPR/Cas system-associated protein Cas10, large subunit of type III CRISPR-Cas systems, contains HD superfamily nuclease domain is part of the Pathway/BioSystem: CRISPR-Cas system


Pssm-ID: 440964 [Multi-domain]  Cd Length: 477  Bit Score: 41.28  E-value: 8.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970439 306 GGEEFILVLKqatAHQAKQVAERCRQAitqielYDEH--NQPIHFTASFGIALSHHNTPYEKLLSQADQALYQAKAY--- 380
Cdd:COG1353  308 GGDDVLAIGP---WDEALEFARELREA------FEEYtgNLNPEITLSAGIVIAHPKYPLYRALELAEELLKKAKKVsek 378


                 ...
gi 514970439 381 GRN 383
Cdd:COG1353  379 GKN 381
Cas10_III cd09679
CRISPR/Cas system-associated protein Cas10; CRISPR (Clustered Regularly Interspaced Short ...
 313-383 3.81e-03

CRISPR/Cas system-associated protein Cas10; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Multidomain protein with permuted HD nuclease domain, palm domain and Zn-ribbon; MTH326-like has inactivated polymerase catalytic domain; alr1562 and slr7011 - predicted only on the basis of size, presence of HD domain, and location with RAMPs in one operon; signature gene for type III; also known as Crm2 family


Pssm-ID: 187810 [Multi-domain]  Cd Length: 475  Bit Score: 39.36  E-value: 3.81e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514970439 313 VLKQATAHQAKQVAERCRQAITQIELY-DEHNQPIHFTASFGIALSHHNTPYEKLLSQADQALYQAKAYGRN 383
Cdd:cd09679  391 VLALLPVDKALDCAKKLRKAFSGILNKeIGEDMGEGPTMSAGIVIAHHKEPLQDALELARRAEKRAKKEGRN 462
 
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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