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Conserved domains on  [gi|2418959376|ref|WP_269833774|]
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sensor domain-containing diguanylate cyclase [Agrobacterium salinitolerans]

Protein Classification

sensor domain-containing diguanylate cyclase( domain architecture ID 11812919)

sensor domain-containing diguanylate cyclase is a GGDEF domain-containing protein with PAS sensor domain(s)

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: ...
 166-319 2.48e-57

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: 182.37  E-value: 2.48e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 166 DELTGLGNRRYAMDTLNHLL--GPNKAQALAVIIMDIDHFKSVNDRFGHACGDLVLKDFAARLSSTAGRDDLLGRIGGEE 243
Cdd:cd01949     3 DPLTGLPNRRAFEERLERLLarARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2418959376 244 FLLVLSGARMHSAETLMRQLQVSLAdAAPLPDRPEFRYSCSAGIA-YASPGESASDVLRHADTALYEAKNTGRNRYV 319
Cdd:cd01949    83 FAILLPGTDLEEAEALAERLREAIE-EPFFIDGQEIRVTASIGIAtYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
PAS_7 super family cl26134
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 40-144 2.13e-03

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


The actual alignment was detected with superfamily member pfam12860:

Pssm-ID: 432837 [Multi-domain]  Cd Length: 115  Bit Score: 37.52  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376  40 QQGYALFDGHDEMRFANSAFRTALGVGPNVF---PSWVDLMRsgYQTATGtAIETSDFELWLRS--AKTRRGKLPFrtIE 114
Cdd:pfam12860   5 SQGLSVFDADLRLVAWNRRYRELLDLPEDLVqvgVPFEEIIR--YNAERG-EYGPGDVEAHVRRrlAAARAGSPHY--FE 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 2418959376 115 TSLKDGRWMLTTETTLPGGWMLCVITDVSE 144
Cdd:pfam12860  80 RERPDGRVIEIRGNPLPDGGFVTTFTDITE 109
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 166-319 2.48e-57

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: 182.37  E-value: 2.48e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 166 DELTGLGNRRYAMDTLNHLL--GPNKAQALAVIIMDIDHFKSVNDRFGHACGDLVLKDFAARLSSTAGRDDLLGRIGGEE 243
Cdd:cd01949     3 DPLTGLPNRRAFEERLERLLarARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2418959376 244 FLLVLSGARMHSAETLMRQLQVSLAdAAPLPDRPEFRYSCSAGIA-YASPGESASDVLRHADTALYEAKNTGRNRYV 319
Cdd:cd01949    83 FAILLPGTDLEEAEALAERLREAIE-EPFFIDGQEIRVTASIGIAtYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 88-321 1.81e-56

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: 184.41  E-value: 1.81e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376  88 AIETSDFELWLRSAKTRRGKLPFRTIETSLKDGRWMLTTETTLPGGWMLCVITDVSELgVELRDLRQERDRALKSALSDE 167
Cdd:COG2199    40 LLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLAL-EDITELRRLEERLRRLATHDP 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 168 LTGLGNRRYAMDTLNHLLGPNKA--QALAVIIMDIDHFKSVNDRFGHACGDLVLKDFAARLSSTAGRDDLLGRIGGEEFL 245
Cdd:COG2199   119 LTGLPNRRAFEERLERELARARRegRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFA 198

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2418959376 246 LVLSGARMHSAETLMRQLQVSLADAAPLPDRPEFRYSCSAGIA-YASPGESASDVLRHADTALYEAKNTGRNRYVVY 321
Cdd:COG2199   199 VLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVAlYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 163-317 2.33e-50

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: 164.73  E-value: 2.33e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 163 ALSDELTGLGNRRYAMDTLNHLL--GPNKAQALAVIIMDIDHFKSVNDRFGHACGDLVLKDFAARLSSTAGRDDLLGRIG 240
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELqrALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 241 GEEFLLVLSGARMHSAETLMRQLQVSLADAA-PLPDRPEFRY-SCSAGIAYASP-GESASDVLRHADTALYEAKNTGRNR 317
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKiPHTVSGLPLYvTISIGIAAYPNdGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 163-321 2.64e-49

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 162.03  E-value: 2.64e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376  163 ALSDELTGLGNRRYAMDTLNHLL--GPNKAQALAVIIMDIDHFKSVNDRFGHACGDLVLKDFAARLSSTAGRDDLLGRIG 240
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQELqrAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376  241 GEEFLLVLSGARMHSAETLMRQLQVSLaDAAPLPDRPEFRYSCSAGIAYAS-PGESASDVLRHADTALYEAKNTGRNRYV 319
Cdd:smart00267  83 GDEFALLLPETSLEEAIALAERILQQL-REPIIIHGIPLYLTISIGVAAYPnPGEDAEDLLKRADTALYQAKKAGRNQVA 161


                   ..
gi 2418959376  320 VY 321
Cdd:smart00267 162 VY 163
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 163-320 2.37e-40

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: 139.01  E-value: 2.37e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 163 ALSDELTGLGNRRYAMDTLNHLLGpnKAQ----ALAVIIMDIDHFKSVNDRFGHACGDLVLKDFAARLSSTAGRDDLLGR 238
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLDSELK--RARrfqrSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 239 IGGEEFLLVLSGARMHSAETLMRQLQ-VSLADAAPLPDRPEFRYSCSAGIA-YASPGESASDVLRHADTALYEAKNTGRN 316
Cdd:TIGR00254  80 YGGEEFVVILPGTPLEDALSKAERLRdAINSKPIEVAGSETLTVTVSIGVAcYPGHGLTLEELLKRADEALYQAKKAGRN 159


                  ....
gi 2418959376 317 RYVV 320
Cdd:TIGR00254 160 RVVV 163
pleD PRK09581
response regulator PleD; Reviewed
 152-319 4.10e-39

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 143.50  E-value: 4.10e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 152 LRQERDRALKSALSDELTGLGNRRYaMDT-LNHLLgpNKAQA----LAVIIMDIDHFKSVNDRFGHACGDLVLKDFAARL 226
Cdd:PRK09581  281 LRNNLEQSIEMAVTDGLTGLHNRRY-FDMhLKNLI--ERANErgkpLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRL 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 227 SSTAGRDDLLGRIGGEEFLLVLSGARMHSAETLMRQLQVSLADAaplpdrpEFRYS---------CSAGIA-YASPGESA 296
Cdd:PRK09581  358 RNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEE-------PFIISdgkerlnvtVSIGVAeLRPSGDTI 430

                         170       180
                  ....*....|....*....|...
gi 2418959376 297 SDVLRHADTALYEAKNTGRNRYV 319
Cdd:PRK09581  431 EALIKRADKALYEAKNTGRNRVV 453
PAS_7 pfam12860
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 40-144 2.13e-03

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 432837 [Multi-domain]  Cd Length: 115  Bit Score: 37.52  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376  40 QQGYALFDGHDEMRFANSAFRTALGVGPNVF---PSWVDLMRsgYQTATGtAIETSDFELWLRS--AKTRRGKLPFrtIE 114
Cdd:pfam12860   5 SQGLSVFDADLRLVAWNRRYRELLDLPEDLVqvgVPFEEIIR--YNAERG-EYGPGDVEAHVRRrlAAARAGSPHY--FE 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 2418959376 115 TSLKDGRWMLTTETTLPGGWMLCVITDVSE 144
Cdd:pfam12860  80 RERPDGRVIEIRGNPLPDGGFVTTFTDITE 109
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 166-319 2.48e-57

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: 182.37  E-value: 2.48e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 166 DELTGLGNRRYAMDTLNHLL--GPNKAQALAVIIMDIDHFKSVNDRFGHACGDLVLKDFAARLSSTAGRDDLLGRIGGEE 243
Cdd:cd01949     3 DPLTGLPNRRAFEERLERLLarARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2418959376 244 FLLVLSGARMHSAETLMRQLQVSLAdAAPLPDRPEFRYSCSAGIA-YASPGESASDVLRHADTALYEAKNTGRNRYV 319
Cdd:cd01949    83 FAILLPGTDLEEAEALAERLREAIE-EPFFIDGQEIRVTASIGIAtYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 88-321 1.81e-56

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: 184.41  E-value: 1.81e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376  88 AIETSDFELWLRSAKTRRGKLPFRTIETSLKDGRWMLTTETTLPGGWMLCVITDVSELgVELRDLRQERDRALKSALSDE 167
Cdd:COG2199    40 LLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLAL-EDITELRRLEERLRRLATHDP 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 168 LTGLGNRRYAMDTLNHLLGPNKA--QALAVIIMDIDHFKSVNDRFGHACGDLVLKDFAARLSSTAGRDDLLGRIGGEEFL 245
Cdd:COG2199   119 LTGLPNRRAFEERLERELARARRegRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFA 198

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2418959376 246 LVLSGARMHSAETLMRQLQVSLADAAPLPDRPEFRYSCSAGIA-YASPGESASDVLRHADTALYEAKNTGRNRYVVY 321
Cdd:COG2199   199 VLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVAlYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 163-317 2.33e-50

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: 164.73  E-value: 2.33e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 163 ALSDELTGLGNRRYAMDTLNHLL--GPNKAQALAVIIMDIDHFKSVNDRFGHACGDLVLKDFAARLSSTAGRDDLLGRIG 240
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELqrALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 241 GEEFLLVLSGARMHSAETLMRQLQVSLADAA-PLPDRPEFRY-SCSAGIAYASP-GESASDVLRHADTALYEAKNTGRNR 317
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKiPHTVSGLPLYvTISIGIAAYPNdGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 163-321 2.64e-49

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 162.03  E-value: 2.64e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376  163 ALSDELTGLGNRRYAMDTLNHLL--GPNKAQALAVIIMDIDHFKSVNDRFGHACGDLVLKDFAARLSSTAGRDDLLGRIG 240
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQELqrAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376  241 GEEFLLVLSGARMHSAETLMRQLQVSLaDAAPLPDRPEFRYSCSAGIAYAS-PGESASDVLRHADTALYEAKNTGRNRYV 319
Cdd:smart00267  83 GDEFALLLPETSLEEAIALAERILQQL-REPIIIHGIPLYLTISIGVAAYPnPGEDAEDLLKRADTALYQAKKAGRNQVA 161


                   ..
gi 2418959376  320 VY 321
Cdd:smart00267 162 VY 163
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 20-321 8.03e-49

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: 173.04  E-value: 8.03e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376  20 LIQGDMDVFIQQLMSLMEASQQGYALFDGHDEMRFANSAFRTALGVGPNVFPSWVDLMRSGYQTATGTAIETSDFELWLR 99
Cdd:COG5001   108 LLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLL 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 100 SAKTRRGKLPFRTIETSLKDGRWMLTTETTLPGGWMLCVITDVSELGVELRDLRQERDRALKSALSDELTGLGNRRYAMD 179
Cdd:COG5001   188 LLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLD 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 180 TLNHLLGPNKA--QALAVIIMDIDHFKSVNDRFGHACGDLVLKDFAARLSSTAGRDDLLGRIGGEEFLLVLSG-ARMHSA 256
Cdd:COG5001   268 RLEQALARARRsgRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDlDDPEDA 347

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2418959376 257 ETLMRQLQVSLADAAPLPDRpEFRYSCSAGIA-YASPGESASDVLRHADTALYEAKNTGRNRYVVY 321
Cdd:COG5001   348 EAVAERILAALAEPFELDGH-ELYVSASIGIAlYPDDGADAEELLRNADLAMYRAKAAGRNRYRFF 412
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 163-320 2.37e-40

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: 139.01  E-value: 2.37e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 163 ALSDELTGLGNRRYAMDTLNHLLGpnKAQ----ALAVIIMDIDHFKSVNDRFGHACGDLVLKDFAARLSSTAGRDDLLGR 238
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLDSELK--RARrfqrSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 239 IGGEEFLLVLSGARMHSAETLMRQLQ-VSLADAAPLPDRPEFRYSCSAGIA-YASPGESASDVLRHADTALYEAKNTGRN 316
Cdd:TIGR00254  80 YGGEEFVVILPGTPLEDALSKAERLRdAINSKPIEVAGSETLTVTVSIGVAcYPGHGLTLEELLKRADEALYQAKKAGRN 159


                  ....
gi 2418959376 317 RYVV 320
Cdd:TIGR00254 160 RVVV 163
pleD PRK09581
response regulator PleD; Reviewed
 152-319 4.10e-39

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 143.50  E-value: 4.10e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 152 LRQERDRALKSALSDELTGLGNRRYaMDT-LNHLLgpNKAQA----LAVIIMDIDHFKSVNDRFGHACGDLVLKDFAARL 226
Cdd:PRK09581  281 LRNNLEQSIEMAVTDGLTGLHNRRY-FDMhLKNLI--ERANErgkpLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRL 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 227 SSTAGRDDLLGRIGGEEFLLVLSGARMHSAETLMRQLQVSLADAaplpdrpEFRYS---------CSAGIA-YASPGESA 296
Cdd:PRK09581  358 RNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEE-------PFIISdgkerlnvtVSIGVAeLRPSGDTI 430

                         170       180
                  ....*....|....*....|...
gi 2418959376 297 SDVLRHADTALYEAKNTGRNRYV 319
Cdd:PRK09581  431 EALIKRADKALYEAKNTGRNRVV 453
PRK09894 PRK09894
diguanylate cyclase; Provisional
 138-321 1.73e-35

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 130.19  E-value: 1.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 138 VITDVSELGVELRDLRQERDRALKSAlsDELTGLGNRRYAMDTLNHLLGPNKAQALAVIIMDIDHFKSVNDRFGHACGDL 217
Cdd:PRK09894  106 FQEGLLSFTAALTDYKIYLLTIRSNM--DVLTGLPGRRVLDESFDHQLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDV 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 218 VLKDFAARLSSTAGRDDLLGRIGGEEFLLVLSGARMHSAETLMRQLQVSLADAAPLPDRPEFRYSCSAGIAYASPGESAS 297
Cdd:PRK09894  184 VLRTLATYLASWTRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRAFPEETLD 263

                         170       180
                  ....*....|....*....|....
gi 2418959376 298 DVLRHADTALYEAKNTGRNRYVVY 321
Cdd:PRK09894  264 VVIGRADRAMYEGKQTGRNRVMFI 287
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
163-324 1.17e-28

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 115.88  E-value: 1.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 163 ALSDELTGLGNRRYAMDTLNHLLGPNKAQA--LAVIIMDIDHFKSVNDRFGHACGDLVLKDFAARLSSTAGRDDLLGRIG 240
Cdd:PRK15426  398 AWHDPLTRLYNRGALFEKARALAKRCQRDQqpFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVG 477

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 241 GEEFLLVLSGARMHSAETLMRQLQVSLADAAPL--PDRPeFRYSCSAGIAYASPGESAS-DVLRH-ADTALYEAKNTGRN 316
Cdd:PRK15426  478 GEEFCVVLPGASLAEAAQVAERIRLRINEKEILvaKSTT-IRISASLGVSSAEEDGDYDfEQLQSlADRRLYLAKQAGRN 556


                  ....*...
gi 2418959376 317 RYVVYGTA 324
Cdd:PRK15426  557 RVCASDNA 564
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
134-321 6.06e-27

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 110.93  E-value: 6.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 134 WMLCVITDVSElgvELRdlRQERDRALksALSDELTGLGNRRYAMDTLNHLLGPNKAQALAVIIMDIDHFKSVNDRFGHA 213
Cdd:PRK10060  215 FLICSGTDITE---ERR--AQERLRIL--ANTDSITGLPNRNAIQELIDHAINAADNNQVGIVYLDLDNFKKVNDAYGHM 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 214 CGDLVLKDFAARLSSTAGRDDLLGRIGGEEFLLVLSGARMHSAETLMRQLQVSLAdaapLPDR---PEFRYSCSAGIA-Y 289
Cdd:PRK10060  288 FGDQLLQDVSLAILSCLEEDQTLARLGGDEFLVLASHTSQAALEAMASRILTRLR----LPFRiglIEVYTGCSIGIAlA 363

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2418959376 290 ASPGESASDVLRHADTALYEAKNTGRNRYVVY 321
Cdd:PRK10060  364 PEHGDDSESLIRSADTAMYTAKEGGRGQFCVF 395
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 138-321 2.86e-22

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 97.44  E-value: 2.86e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376  138 VITDVSELGVELRDLRQerdralkSALSDELTGLGNR-------RYAMDTLNhllgpNKAQALAVIIMDIDHFKSVNDRF 210
Cdd:PRK09776   647 VIQDVTESRKMLRQLSY-------SASHDALTHLANRasfekqlRRLLQTVN-----STHQRHALVFIDLDRFKAVNDSA 714

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376  211 GHACGDLVLKDFAARLSSTAGRDDLLGRIGGEEFLLVLSGARMHSAETLMRQLqVSLADAAPLP--DRpEFRYSCSAGI- 287
Cdd:PRK09776   715 GHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRI-ISAINDYHFPweGR-VYRVGASAGIt 792

                          170       180       190
                   ....*....|....*....|....*....|....
gi 2418959376  288 AYASPGESASDVLRHADTALYEAKNTGRNRYVVY 321
Cdd:PRK09776   793 LIDANNHQASEVMSQADIACYAAKNAGRGRVTVY 826
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 139-318 1.23e-21

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 95.61  E-value: 1.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 139 ITDVS----ELGVELRDLRQERDRALKSalsDELTGLGNRRYAMDTLNHLLGPnkAQALAVIIMDIDHFKSVNDRFGHAC 214
Cdd:PRK11359  351 VADISqhlaALALEQEKSRQHIEQLIQF---DPLTGLPNRNNLHNYLDDLVDK--AVSPVVYLIGVDHFQDVIDSLGYAW 425

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 215 GDLVLKDFAARLSSTAGRDDLLGRIGGEEFLLVLSGARMHSAETLMRQLQvSLADAAPLPDRPEFRYSCSAGIAYASpGE 294
Cdd:PRK11359  426 ADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELR-NVVSKPIMIDDKPFPLTLSIGISYDV-GK 503

                         170       180
                  ....*....|....*....|....
gi 2418959376 295 SASDVLRHADTALYEAKNTGRNRY 318
Cdd:PRK11359  504 NRDYLLSTAHNAMDYIRKNGGNGW 527
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 166-317 1.56e-21

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 93.74  E-value: 1.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 166 DELTGLGNRRYAMDTL----NHLLGPNKAQALavIIMDIDHFKSVNDRFGHACGDLVLKDFAARLSSTAGRDDLLGRIGG 241
Cdd:PRK10245  208 DGMTGVYNRRHWETLLrnefDNCRRHHRDATL--LIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGG 285

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2418959376 242 EEFLLVLSGARMHSAETLMRQLQVSLAdAAPLPDRPEFRYSCSAGIAYASPGESA-SDVLRHADTALYEAKNTGRNR 317
Cdd:PRK10245  286 DEFAVIMSGTPAESAITAMSRVHEGLN-TLRLPNAPQVTLRISVGVAPLNPQMSHyREWLKSADLALYKAKNAGRNR 361
PRK09966 PRK09966
diguanylate cyclase DgcN;
148-319 1.30e-17

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 82.75  E-value: 1.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 148 ELRdLRQERDRALKSALSDELTGLGNRRYAMDTLNHLLGPNKAQAL-AVIIMDIDHFKSVNDRFGHACGDLVLKDFAARL 226
Cdd:PRK09966  234 QLR-LQAKNAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTsALLFLDGDNFKYINDTWGHATGDRVLIEIAKRL 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 227 SSTAGRDDLLGRIGGEEFLLVLSGarMHSaETLMRQLQVSLADAAPLP----DRPEFRYSCSAGIAYASPGESASDVLRH 302
Cdd:PRK09966  313 AEFGGLRHKAYRLGGDEFAMVLYD--VQS-ESEVQQICSALTQIFNLPfdlhNGHQTTMTLSIGYAMTIEHASAEKLQEL 389

                         170
                  ....*....|....*..
gi 2418959376 303 ADTALYEAKNTGRNRYV 319
Cdd:PRK09966  390 ADHNMYQAKHQRAEKLV 406
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 234-311 7.26e-10

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: 57.23  E-value: 7.26e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2418959376 234 DLLGRIGGEEFLLVLSGARMHSAETLMRQLQVSLADAaplpdrPEFRYSCSAGIAyaspgesASDVLRHADtALYEAK 311
Cdd:COG3706   116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAEL------PSLRVTVSIGVA-------GDSLLKRAD-ALYQAR 179
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 152-317 8.97e-07

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 50.48  E-value: 8.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 152 LRQERDRALKSALSDELTGLGNRRYAMDTLNHLLgpNKAQALAVIIMDIDHFKSVNDRFGHACGDLVLKDFAARLSSTAG 231
Cdd:PRK13561  220 LQRQYEEQSRNATRFPVSDLPNKALLMALLEQVV--ARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLS 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 232 RDDLLGRIGGEEFLLVLSGAR--MHsAETLMRQLQVSLADAAPLPDRPeFRYSCSAGIAYASPGESASDVLRHADTALYE 309
Cdd:PRK13561  298 PRMVLAQISGYDFAIIANGVKepWH-AITLGQQVLTIINERLPIQRIQ-LRPSCSIGIAMFYGDLTAEQLYSRAISAAFT 375


                  ....*...
gi 2418959376 310 AKNTGRNR 317
Cdd:PRK13561  376 ARRKGKNQ 383
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 195-288 3.20e-06

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: 45.81  E-value: 3.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 195 VIIMDIDHFKSVNDRFGHACGDLVLKDFAARLSSTAGRD-DLLGRIGGEEFLLVLSGARMHSAETLMRQLQVSL-ADAAP 272
Cdd:cd07556     4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSgDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVsALNQS 83

                          90
                  ....*....|....*.
gi 2418959376 273 LPDRPEFRYSCSAGIA 288
Cdd:cd07556    84 EGNPVRVRIGIHTGPV 99
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 148-321 1.77e-05

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 46.39  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 148 ELRDLRQERDRA---LKS-ALSDELTGLGNRRYAMDTLNHLLgpNKAQALA----VIIMDIDHFKSVNDRFGHACGDLVL 219
Cdd:PRK11059  209 ELQDAREERSRFdtfIRSnAFQDAKTGLGNRLFFDNQLATLL--EDQEMVGahgvVMLIRLPDFDLLQEEWGESQVEELL 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 220 KDFAARLSSTAGR--DDLLGRIGGEEFLLVLSGARMHSAETLMRQLqVSLADAAPLP---DRPEFrysCSAGIAYASPGE 294
Cdd:PRK11059  287 FELINLLSTFVMRypGALLARYSRSDFAVLLPHRSLKEADSLASQL-LKAVDALPPPkmlDRDDF---LHIGICAYRSGQ 362

                         170       180
                  ....*....|....*....|....*..
gi 2418959376 295 SASDVLRHADTALYEAKNTGRNRYVVY 321
Cdd:PRK11059  363 STEQVMEEAEMALRSAQLQGGNGWFVY 389
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 144-321 5.53e-04

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 41.47  E-value: 5.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 144 ELGVELRDLRQ-----ERDRALKSALSDEL--TGLGNRRYAMDTL-NHLLGPNKAQALAVIIMDIDHFKSVNDRFGHACG 215
Cdd:PRK11829  206 ELGVLVRNYNRnqqllADAYADMGRISHRFpvTELPNRSLFISLLeKEIASSTRTDHFHLLVIGIETLQEVSGAMSEAQH 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376 216 DLVLKDFAARLSSTAGRDDLLGRIGGEEFLLVLSGA-----RMHSAETLMRQLqvsladAAPLP-DRPEFRYSCSAGIAY 289
Cdd:PRK11829  286 QQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVLARGTrrsfpAMQLARRIMSQV------TQPLFfDEITLRPSASIGITR 359

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2418959376 290 ASPG-ESASDVLRHADTALYEAKNTGRNRYVVY 321
Cdd:PRK11829  360 YQAQqDTAESMMRNASTAMMAAHHEGRNQIMVF 392
PAS_7 pfam12860
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 40-144 2.13e-03

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 432837 [Multi-domain]  Cd Length: 115  Bit Score: 37.52  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418959376  40 QQGYALFDGHDEMRFANSAFRTALGVGPNVF---PSWVDLMRsgYQTATGtAIETSDFELWLRS--AKTRRGKLPFrtIE 114
Cdd:pfam12860   5 SQGLSVFDADLRLVAWNRRYRELLDLPEDLVqvgVPFEEIIR--YNAERG-EYGPGDVEAHVRRrlAAARAGSPHY--FE 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 2418959376 115 TSLKDGRWMLTTETTLPGGWMLCVITDVSE 144
Cdd:pfam12860  80 RERPDGRVIEIRGNPLPDGGFVTTFTDITE 109
 
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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