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Conserved domains on  [gi|492160285|ref|WP_005766730|]
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MULTISPECIES: GGDEF domain-containing protein [Pseudomonas]

Protein Classification

GGDEF domain-containing protein( domain architecture ID 10112692)

GGDEF domain-containing protein may function as a diguanylate cyclase and be involved in regulating cell surface adhesion in bacteria

CATH:  3.30.70.1230
Gene Ontology:  GO:0005525|GO:0005886|GO:0007165|GO:0046872|GO:0052621
PubMed:  16166544|17208514|11119645|15569936

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 148-303 1.68e-62

Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.


:

Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 195.08  E-value: 1.68e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 148 LRDPLTSTGNRIAMDQGLAREIEISSRHKQPLSLLMLDIDHFKKVNDEYGHHTGDDVLKTVAQSLKAQLRNIDRVFRYGG 227
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492160285 228 EEFVVILSNTGATAAELIGERLRQAVRNLEFrELDPALTMTVSLGCSTLLP-TETADSLLRRADNALYVAKREGRNR 303
Cdd:cd01949   81 DEFAILLPGTDLEEAEALAERLREAIEEPFF-IDGQEIRVTASIGIATYPEdGEDAEELLRRADEALYRAKRSGRNR 156
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 148-303 1.68e-62

Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.


Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 195.08  E-value: 1.68e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 148 LRDPLTSTGNRIAMDQGLAREIEISSRHKQPLSLLMLDIDHFKKVNDEYGHHTGDDVLKTVAQSLKAQLRNIDRVFRYGG 227
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492160285 228 EEFVVILSNTGATAAELIGERLRQAVRNLEFrELDPALTMTVSLGCSTLLP-TETADSLLRRADNALYVAKREGRNR 303
Cdd:cd01949   81 DEFAILLPGTDLEEAEALAERLREAIEEPFF-IDGQEIRVTASIGIATYPEdGEDAEELLRRADEALYRAKRSGRNR 156
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 38-307 1.21e-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: 197.12  E-value: 1.21e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285  38 LVYQLGRQLQTSLEAERILTLFFQGVQRFLPLSGLVYRHIESDLHLRLGEMSSDSASFHLRHEGKCIGELEFQGAKPFDT 117
Cdd:COG2199    2 LLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 118 RQLSDLESLLVCLVYPLLNALLYRIATQT---ALRDPLTSTGNRIAMDQGLAREIEISSRHKQPLSLLMLDIDHFKKVND 194
Cdd:COG2199   82 ELLLLLLALLLLLLALEDITELRRLEERLrrlATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIND 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 195 EYGHHTGDDVLKTVAQSLKAQLRNIDRVFRYGGEEFVVILSNTGATAAELIGERLRQAVRNLEFRELDPALTMTVSLGCS 274
Cdd:COG2199  162 TYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVA 241

                        250       260       270
                 ....*....|....*....|....*....|....
gi 492160285 275 TLLPT-ETADSLLRRADNALYVAKREGRNRLAMA 307
Cdd:COG2199  242 LYPEDgDSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 147-303 1.70e-55

Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.


Pssm-ID: 425976 [Multi-domain]  Cd Length: 160  Bit Score: 177.06  E-value: 1.70e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285  147 ALRDPLTSTGNRIAMDQGLAREIEISSRHKQPLSLLMLDIDHFKKVNDEYGHHTGDDVLKTVAQSLKAQLRNIDRVFRYG 226
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285  227 GEEFVVILSNTGATAAELIGERLRQAVRNLE--FRELDPALTMTVSLG-CSTLLPTETADSLLRRADNALYVAKREGRNR 303
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKipHTVSGLPLYVTISIGiAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 145-307 7.59e-53

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 170.51  E-value: 7.59e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285   145 QTALRDPLTSTGNRIAMDQGLAREIEISSRHKQPLSLLMLDIDHFKKVNDEYGHHTGDDVLKTVAQSLKAQLRNIDRVFR 224
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285   225 YGGEEFVVILSNTGATAAELIGERLRQAVRNLEFrELDPALTMTVSLG-CSTLLPTETADSLLRRADNALYVAKREGRNR 303
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPII-IHGIPLYLTISIGvAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159


                   ....
gi 492160285   304 LAMA 307
Cdd:smart00267 160 VAVY 163
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 147-307 1.08e-51

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: 167.51  E-value: 1.08e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285  147 ALRDPLTSTGNRIAMDQGLAREIEISSRHKQPLSLLMLDIDHFKKVNDEYGHHTGDDVLKTVAQSLKAQLRNIDRVFRYG 226
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285  227 GEEFVVILSNTGATAAELIGERLRQAVRNLEFR-ELDPALTMTVSLGCSTLLP-TETADSLLRRADNALYVAKREGRNRL 304
Cdd:TIGR00254  82 GEEFVVILPGTPLEDALSKAERLRDAINSKPIEvAGSETLTVTVSIGVACYPGhGLTLEELLKRADEALYQAKKAGRNRV 161


                  ...
gi 492160285  305 AMA 307
Cdd:TIGR00254 162 VVA 164
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
145-304 3.59e-50

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 166.70  E-value: 3.59e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 145 QTALRDPLTSTGNRIAMDQGLAREIEISSRHKQPLSLLMLDIDHFKKVNDEYGHHTGDDVLKTVAQSLKAQLRNIDRVFR 224
Cdd:NF038266  92 EASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGR 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 225 YGGEEFVVILSNTGATAAELIGERLRQAVRNLEFRELDPALTMTVSLGCSTL-LPTETADSLLRRADNALYVAKREGRNR 303
Cdd:NF038266 172 WGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAEHrPPEEGLSATLSRADQALYQAKRAGRDR 251


                 .
gi 492160285 304 L 304
Cdd:NF038266 252 V 252
pleD PRK09581
response regulator PleD; Reviewed
 130-307 5.15e-50

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 172.01  E-value: 5.15e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 130 LVYPL-LNALLYRIATQT-------------------ALRDPLTSTGNRIAMDQGLAREIEISSRHKQPLSLLMLDIDHF 189
Cdd:PRK09581 255 LMRPIdKNELLARVRTQIrrkryqdalrnnleqsiemAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHF 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 190 KKVNDEYGHHTGDDVLKTVAQSLKAQLRNIDRVFRYGGEEFVVILSNTGATAAELIGERLRQAVRNLEFR--ELDPALTM 267
Cdd:PRK09581 335 KKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIisDGKERLNV 414

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 492160285 268 TVSLGCSTLLP-TETADSLLRRADNALYVAKREGRNRLAMA 307
Cdd:PRK09581 415 TVSIGVAELRPsGDTIEALIKRADKALYEAKNTGRNRVVAL 455
dguan_cyc_DgcA NF041606
diguanylate cyclase DgcA;
165-307 1.67e-41

diguanylate cyclase DgcA;


Pssm-ID: 469490 [Multi-domain]  Cd Length: 340  Bit Score: 146.82  E-value: 1.67e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 165 LAREIEISSRHKQPLSLLMLDIDHFKKVNDEYGHHTGDDVLKTVAQSLKAQLRNIDRVFRYGGEEFVVILSNTGATAAEL 244
Cdd:NF041606 196 LMEKLDTINSQGEPLSILMLDIDFFKQINDTYGHACGDLVLQMVASIIQSCTRTQDMAARYGGEEFVVMLSNTSSKTAKK 275

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492160285 245 IGERLRQAVRNLEFRELDPALTMTVSLGCSTLLPT-ETADSLLRRADNALYVAKREGRNRLAMA 307
Cdd:NF041606 276 IAERIRKSIENLSILYDEQHIRVTISIGVAEYNFDvESAKSLVERADKALYESKQNGRNRVSIS 339
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 148-303 1.68e-62

Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.


Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 195.08  E-value: 1.68e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 148 LRDPLTSTGNRIAMDQGLAREIEISSRHKQPLSLLMLDIDHFKKVNDEYGHHTGDDVLKTVAQSLKAQLRNIDRVFRYGG 227
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492160285 228 EEFVVILSNTGATAAELIGERLRQAVRNLEFrELDPALTMTVSLGCSTLLP-TETADSLLRRADNALYVAKREGRNR 303
Cdd:cd01949   81 DEFAILLPGTDLEEAEALAERLREAIEEPFF-IDGQEIRVTASIGIATYPEdGEDAEELLRRADEALYRAKRSGRNR 156
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 38-307 1.21e-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: 197.12  E-value: 1.21e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285  38 LVYQLGRQLQTSLEAERILTLFFQGVQRFLPLSGLVYRHIESDLHLRLGEMSSDSASFHLRHEGKCIGELEFQGAKPFDT 117
Cdd:COG2199    2 LLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 118 RQLSDLESLLVCLVYPLLNALLYRIATQT---ALRDPLTSTGNRIAMDQGLAREIEISSRHKQPLSLLMLDIDHFKKVND 194
Cdd:COG2199   82 ELLLLLLALLLLLLALEDITELRRLEERLrrlATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIND 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 195 EYGHHTGDDVLKTVAQSLKAQLRNIDRVFRYGGEEFVVILSNTGATAAELIGERLRQAVRNLEFRELDPALTMTVSLGCS 274
Cdd:COG2199  162 TYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVA 241

                        250       260       270
                 ....*....|....*....|....*....|....
gi 492160285 275 TLLPT-ETADSLLRRADNALYVAKREGRNRLAMA 307
Cdd:COG2199  242 LYPEDgDSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 147-303 1.70e-55

Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.


Pssm-ID: 425976 [Multi-domain]  Cd Length: 160  Bit Score: 177.06  E-value: 1.70e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285  147 ALRDPLTSTGNRIAMDQGLAREIEISSRHKQPLSLLMLDIDHFKKVNDEYGHHTGDDVLKTVAQSLKAQLRNIDRVFRYG 226
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285  227 GEEFVVILSNTGATAAELIGERLRQAVRNLE--FRELDPALTMTVSLG-CSTLLPTETADSLLRRADNALYVAKREGRNR 303
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKipHTVSGLPLYVTISIGiAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 145-307 7.59e-53

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 170.51  E-value: 7.59e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285   145 QTALRDPLTSTGNRIAMDQGLAREIEISSRHKQPLSLLMLDIDHFKKVNDEYGHHTGDDVLKTVAQSLKAQLRNIDRVFR 224
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285   225 YGGEEFVVILSNTGATAAELIGERLRQAVRNLEFrELDPALTMTVSLG-CSTLLPTETADSLLRRADNALYVAKREGRNR 303
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPII-IHGIPLYLTISIGvAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159


                   ....
gi 492160285   304 LAMA 307
Cdd:smart00267 160 VAVY 163
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 147-307 1.08e-51

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: 167.51  E-value: 1.08e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285  147 ALRDPLTSTGNRIAMDQGLAREIEISSRHKQPLSLLMLDIDHFKKVNDEYGHHTGDDVLKTVAQSLKAQLRNIDRVFRYG 226
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285  227 GEEFVVILSNTGATAAELIGERLRQAVRNLEFR-ELDPALTMTVSLGCSTLLP-TETADSLLRRADNALYVAKREGRNRL 304
Cdd:TIGR00254  82 GEEFVVILPGTPLEDALSKAERLRDAINSKPIEvAGSETLTVTVSIGVACYPGhGLTLEELLKRADEALYQAKKAGRNRV 161


                  ...
gi 492160285  305 AMA 307
Cdd:TIGR00254 162 VVA 164
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
145-304 3.59e-50

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 166.70  E-value: 3.59e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 145 QTALRDPLTSTGNRIAMDQGLAREIEISSRHKQPLSLLMLDIDHFKKVNDEYGHHTGDDVLKTVAQSLKAQLRNIDRVFR 224
Cdd:NF038266  92 EASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGR 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 225 YGGEEFVVILSNTGATAAELIGERLRQAVRNLEFRELDPALTMTVSLGCSTL-LPTETADSLLRRADNALYVAKREGRNR 303
Cdd:NF038266 172 WGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAEHrPPEEGLSATLSRADQALYQAKRAGRDR 251


                 .
gi 492160285 304 L 304
Cdd:NF038266 252 V 252
pleD PRK09581
response regulator PleD; Reviewed
 130-307 5.15e-50

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 172.01  E-value: 5.15e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 130 LVYPL-LNALLYRIATQT-------------------ALRDPLTSTGNRIAMDQGLAREIEISSRHKQPLSLLMLDIDHF 189
Cdd:PRK09581 255 LMRPIdKNELLARVRTQIrrkryqdalrnnleqsiemAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHF 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 190 KKVNDEYGHHTGDDVLKTVAQSLKAQLRNIDRVFRYGGEEFVVILSNTGATAAELIGERLRQAVRNLEFR--ELDPALTM 267
Cdd:PRK09581 335 KKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIisDGKERLNV 414

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 492160285 268 TVSLGCSTLLP-TETADSLLRRADNALYVAKREGRNRLAMA 307
Cdd:PRK09581 415 TVSIGVAELRPsGDTIEALIKRADKALYEAKNTGRNRVVAL 455
PRK09894 PRK09894
diguanylate cyclase; Provisional
 140-308 7.70e-47

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 159.46  E-value: 7.70e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 140 YRIATQTAL--RDPLTSTGNRIAMDQGLAREIeiSSRHKQPLSLLMLDIDHFKKVNDEYGHHTGDDVLKTVAQSLKAQLR 217
Cdd:PRK09894 120 YKIYLLTIRsnMDVLTGLPGRRVLDESFDHQL--RNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTR 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 218 NIDRVFRYGGEEFVVILSNTGATAAELIGERLRQAVRNLEFRELDPALTMTVSLGCSTLLPTETADSLLRRADNALYVAK 297
Cdd:PRK09894 198 DYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRAFPEETLDVVIGRADRAMYEGK 277

                        170
                 ....*....|.
gi 492160285 298 REGRNRLAMAS 308
Cdd:PRK09894 278 QTGRNRVMFID 288
dguan_cyc_DgcA NF041606
diguanylate cyclase DgcA;
165-307 1.67e-41

diguanylate cyclase DgcA;


Pssm-ID: 469490 [Multi-domain]  Cd Length: 340  Bit Score: 146.82  E-value: 1.67e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 165 LAREIEISSRHKQPLSLLMLDIDHFKKVNDEYGHHTGDDVLKTVAQSLKAQLRNIDRVFRYGGEEFVVILSNTGATAAEL 244
Cdd:NF041606 196 LMEKLDTINSQGEPLSILMLDIDFFKQINDTYGHACGDLVLQMVASIIQSCTRTQDMAARYGGEEFVVMLSNTSSKTAKK 275

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492160285 245 IGERLRQAVRNLEFRELDPALTMTVSLGCSTLLPT-ETADSLLRRADNALYVAKREGRNRLAMA 307
Cdd:NF041606 276 IAERIRKSIENLSILYDEQHIRVTISIGVAEYNFDvESAKSLVERADKALYESKQNGRNRVSIS 339
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 147-306 1.61e-40

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: 149.54  E-value: 1.61e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 147 ALRDPLTSTGNRIAMDQGLAREIEISSRHKQPLSLLMLDIDHFKKVNDEYGHHTGDDVLKTVAQSLKAQLRNIDRVFRYG 226
Cdd:COG5001  251 AYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLG 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 227 GEEFVVILSN-TGATAAELIGERLRQAVRNlEFRELDPALTMTVSLGCStLLPT--ETADSLLRRADNALYVAKREGRNR 303
Cdd:COG5001  331 GDEFAVLLPDlDDPEDAEAVAERILAALAE-PFELDGHELYVSASIGIA-LYPDdgADAEELLRNADLAMYRAKAAGRNR 408


                 ...
gi 492160285 304 LAM 306
Cdd:COG5001  409 YRF 411
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
142-303 2.48e-40

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 147.85  E-value: 2.48e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 142 IATQTALR-----DPLTSTGNRIAMDQGLAREIEISSRHKQPLSLLMLDIDHFKKVNDEYGHHTGDDVLKTVAQSLKAQL 216
Cdd:PRK15426 388 FVLQSSLQwqawhDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSL 467

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 217 RNIDRVFRYGGEEFVVILSNTGATAAELIGERLRQAVrNLEFRELDPALTM--TVSLGCSTLLPTE--TADSLLRRADNA 292
Cdd:PRK15426 468 RAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRI-NEKEILVAKSTTIriSASLGVSSAEEDGdyDFEQLQSLADRR 546

                        170
                 ....*....|.
gi 492160285 293 LYVAKREGRNR 303
Cdd:PRK15426 547 LYLAKQAGRNR 557
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 103-308 1.45e-28

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 112.61  E-value: 1.45e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 103 CIGELEFQGAKP-FDTRQLSDLESLLVCLVYPLLNALL-YRIATQTA----------LRDPLTSTGNRIAMDQGLAREIE 170
Cdd:PRK10245 149 CLVTLELTGITVsFNSAPLEWWLSLPVIVIYPLLFAWVsYQTATKLAehkrrlqvmsTRDGMTGVYNRRHWETLLRNEFD 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 171 ISSRHKQPLSLLMLDIDHFKKVNDEYGHHTGDDVLKTVAQSLKAQLRNIDRVFRYGGEEFVVILSNTGATAAELIGERLR 250
Cdd:PRK10245 229 NCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVH 308

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 492160285 251 QAVRNLEFrELDPALTMTVSLGCSTLLPT-ETADSLLRRADNALYVAKREGRNRLAMAS 308
Cdd:PRK10245 309 EGLNTLRL-PNAPQVTLRISVGVAPLNPQmSHYREWLKSADLALYKAKNAGRNRTEVAA 366
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
144-301 1.94e-22

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 97.44  E-value: 1.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 144 TQTALRDPLTSTGNRIAMDQGLAreIEISSRHKQPLSLLMLDIDHFKKVNDEYGHHTGDDVLKTVAQSLKAQLRNIDRVF 223
Cdd:PRK10060 234 RILANTDSITGLPNRNAIQELID--HAINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLA 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 224 RYGGEEFVVILSNTGATA----AELIGERLRQAVR-NLefreldpaltMTVSLGCS---TLLPT--ETADSLLRRADNAL 293
Cdd:PRK10060 312 RLGGDEFLVLASHTSQAAleamASRILTRLRLPFRiGL----------IEVYTGCSigiALAPEhgDDSESLIRSADTAM 381


                 ....*...
gi 492160285 294 YVAKREGR 301
Cdd:PRK10060 382 YTAKEGGR 389
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 147-303 2.52e-18

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 85.49  E-value: 2.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285  147 ALRDPLTSTGNRIAMDQGLAREIEISSRHKQPLSLLMLDIDHFKKVNDEYGHHTGDDVLKTVAQSLKAQLRNIDRVFRYG 226
Cdd:PRK09776  665 ASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLG 744

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492160285  227 GEEFVVILSNTGATAAELIGERLRQAVRNLEFRELDPALTMTVSLGCSTL-LPTETADSLLRRADNALYVAKREGRNR 303
Cdd:PRK09776  745 GDEFGLLLPDCNVESARFIATRIISAINDYHFPWEGRVYRVGASAGITLIdANNHQASEVMSQADIACYAAKNAGRGR 822
PRK09966 PRK09966
diguanylate cyclase DgcN;
136-304 4.62e-17

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 80.82  E-value: 4.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 136 NALLYRiatqTALRDPLTSTGNRIAMDQGLAREIEISSRHKQPlSLLMLDIDHFKKVNDEYGHHTGDDVLKTVAQSLKAQ 215
Cdd:PRK09966 241 NAQLLR----TALHDPLTGLANRAAFRSGINTLMNNSDARKTS-ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEF 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 216 LRNIDRVFRYGGEEFVVILSNTGA-TAAELIGERLRQAVrNLEFrELDPA--LTMTVSLGCSTLLPTETADSLLRRADNA 292
Cdd:PRK09966 316 GGLRHKAYRLGGDEFAMVLYDVQSeSEVQQICSALTQIF-NLPF-DLHNGhqTTMTLSIGYAMTIEHASAEKLQELADHN 393

                        170
                 ....*....|..
gi 492160285 293 LYVAKREGRNRL 304
Cdd:PRK09966 394 MYQAKHQRAEKL 405
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 178-297 7.50e-16

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


Pssm-ID: 143637 [Multi-domain]  Cd Length: 133  Bit Score: 72.77  E-value: 7.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 178 PLSLLMLDIDHFKKVNDEYGHHTGDDVLKTVAQSLKAQL-RNIDRVFRYGGEEFVVILSNTGATAAELIGERLRQAVRNL 256
Cdd:cd07556    1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 492160285 257 EFRELDPaltMTVSLGCSTLLP----------TETADSLLRRADNALYVAK 297
Cdd:cd07556   81 NQSEGNP---VRVRIGIHTGPVvvgvigsrpqYDVWGALVNLASRMESQAK 128
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 219-297 2.40e-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: 72.63  E-value: 2.40e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492160285 219 IDRVFRYGGEEFVVILSNTGATAAELIGERLRQAVRNLefreldPALTMTVSLGCStllptetADSLLRRADnALYVAK 297
Cdd:COG3706  115 VDLVARYGGEEFAILLPGTDLEGALAVAERIREAVAEL------PSLRVTVSIGVA-------GDSLLKRAD-ALYQAR 179
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 150-302 8.66e-13

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 68.64  E-value: 8.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 150 DPLTSTGNRiamdQGLAREIEISSRHKQPLSLLMLDIDHFKKVNDEYGHHTGDDVLKTVAQSLKAQLRNIDRVFRYGGEE 229
Cdd:PRK11359 379 DPLTGLPNR----NNLHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQ 454

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492160285 230 FVVILSNTGATAAELIGERLrQAVRNLEFRELDPALTMTVSLGCSTLLPTETaDSLLRRADNALYVAKREGRN 302
Cdd:PRK11359 455 FVLVSLENDVSNITQIADEL-RNVVSKPIMIDDKPFPLTLSIGISYDVGKNR-DYLLSTAHNAMDYIRKNGGN 525
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 142-302 2.45e-05

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 45.62  E-value: 2.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 142 IATQTALrDPLTSTGNRIAMDQGLAREIEISSRHKQPLSLLMLDIDHFKKVNDEYGHHTGDDVLKTVAQSLKAQL-RNID 220
Cdd:PRK11059 224 IRSNAFQ-DAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVmRYPG 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 221 RVF-RYGGEEFVVILSNTGATAAELIGERLRQAVRNLEFRELDPALTMtVSLGCSTLLPTETADSLLRRADNALYVAKRE 299
Cdd:PRK11059 303 ALLaRYSRSDFAVLLPHRSLKEADSLASQLLKAVDALPPPKMLDRDDF-LHIGICAYRSGQSTEQVMEEAEMALRSAQLQ 381


                 ...
gi 492160285 300 GRN 302
Cdd:PRK11059 382 GGN 384
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 140-304 5.26e-04

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 41.47  E-value: 5.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 140 YRIATQTALRDPLTSTGNRIAMDQGLAREIEISSRHKQpLSLLMLDIDHFKKVNDEYGHHTGDDVLKTVAQSLKAQLRNI 219
Cdd:PRK11829 225 YADMGRISHRFPVTELPNRSLFISLLEKEIASSTRTDH-FHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDS 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492160285 220 DRVFRYGGEEFVVILSNTG--ATAAELIGERLRQAVRNLEFRELdpALTMTVSLGCSTLLPT-ETADSLLRRADNALYVA 296
Cdd:PRK11829 304 DLLAQLSKTEFAVLARGTRrsFPAMQLARRIMSQVTQPLFFDEI--TLRPSASIGITRYQAQqDTAESMMRNASTAMMAA 381


                 ....*...
gi 492160285 297 KREGRNRL 304
Cdd:PRK11829 382 HHEGRNQI 389
 
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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