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Conserved domains on  [gi|1542763058|gb|RTY51862|]
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cyclic-guanylate-specific phosphodiesterase [Enterobacter roggenkampii]

Protein Classification

cyclic-guanylate-specific phosphodiesterase( domain architecture ID 10013844)

cyclic-guanylate-specific phosphodiesterase catalyzes the hydrolysis of cyclic di-3',5'-guanylate to form 5'-phosphoguanylyl(3'->5')guanosine, and is involved in the control of the switch from cell motility to adhesion via regulation of cellular levels of cyclic-di-GMP (c-di-GMP)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
 2-257 7.33e-180

cyclic-di-GMP phosphodiesterase; Provisional


:

Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 494.13  E-value: 7.33e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058   2 KSEQVTQRLSTtPEASIENLQEHRYWLQCERAYTYQPIYRTDGRLMAIEILTVVTHPSNPTQRIAPDRYFAEVAVRQRLD 81
Cdd:PRK11596    1 MIRQVIQRISL-PEASIESLQERRYWLQCERAYTFQPIYRTSGRLMAIELLTAVTHPSNPSQRLSPERYFAEITVSHRLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058  82 VLEEQLRMLATKQPFFEQHDILASVNVDGPTLLALRQNAKLQALIATLPWVRFELVEHVRLPQDSSFASICEYGPLWLDD 161
Cdd:PRK11596   80 VVKEQLDLLAQWADFFVRHGLLASVNIDGPTLIALRQQPAILRLIERLPWLRFELVEHIRLPKDSPFASMCEFGPLWLDD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058 162 FGTGMANFSALSEVRYDYIKVARDLFIMLRQTPEGRNLFTLLLQLMNRYCQGVIVEGVETLEEWRDVQSSPAAAAQGYFL 241
Cdd:PRK11596  160 FGTGMANFSALSEVRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFL 239

                         250
                  ....*....|....*.
gi 1542763058 242 SRPVPMDRLDSVITTL 257
Cdd:PRK11596  240 SRPAPFETLETLPLAL 255
 
Name Accession Description Interval E-value
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
 2-257 7.33e-180

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 494.13  E-value: 7.33e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058   2 KSEQVTQRLSTtPEASIENLQEHRYWLQCERAYTYQPIYRTDGRLMAIEILTVVTHPSNPTQRIAPDRYFAEVAVRQRLD 81
Cdd:PRK11596    1 MIRQVIQRISL-PEASIESLQERRYWLQCERAYTFQPIYRTSGRLMAIELLTAVTHPSNPSQRLSPERYFAEITVSHRLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058  82 VLEEQLRMLATKQPFFEQHDILASVNVDGPTLLALRQNAKLQALIATLPWVRFELVEHVRLPQDSSFASICEYGPLWLDD 161
Cdd:PRK11596   80 VVKEQLDLLAQWADFFVRHGLLASVNIDGPTLIALRQQPAILRLIERLPWLRFELVEHIRLPKDSPFASMCEFGPLWLDD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058 162 FGTGMANFSALSEVRYDYIKVARDLFIMLRQTPEGRNLFTLLLQLMNRYCQGVIVEGVETLEEWRDVQSSPAAAAQGYFL 241
Cdd:PRK11596  160 FGTGMANFSALSEVRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFL 239

                         250
                  ....*....|....*.
gi 1542763058 242 SRPVPMDRLDSVITTL 257
Cdd:PRK11596  240 SRPAPFETLETLPLAL 255
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 29-248 5.37e-46

Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 153.91  E-value: 5.37e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058   29 QCERAYTYQPIY-RTDGRLMAIEILTVVTHPSNptQRIAPDRY---FAEVAVRQRLD--VLEEQLRMLATKQPFFeQHDI 102
Cdd:smart00052  10 NGQFLLYYQPIVsLRTGRLVGVEALIRWQHPEG--GIISPDEFiplAEETGLIVPLGrwVLEQACQQLAEWQAQG-PPPL 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058  103 LASVNVDGPTLLALRQNAKLQALIATLP----WVRFELVEHVRLPQDSS----FASICEYG-PLWLDDFGTGMANFSALS 173
Cdd:smart00052  87 LISINLSARQLISPDLVPRVLELLEETGlppqRLELEITESVLLDDDESavatLQRLRELGvRIALDDFGTGYSSLSYLK 166

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1542763058  174 EVRYDYIKVARDLFIMLRQTPEGRNLFTLLLQLMNRYCQGVIVEGVETLEEWRDVQSSPAAAAQGYFLSRPVPMD 248
Cdd:smart00052 167 RLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLD 241
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 36-249 1.24e-34

EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.


Pssm-ID: 238923 [Multi-domain]  Cd Length: 240  Bit Score: 124.20  E-value: 1.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058  36 YQPIYR-TDGRLMAIEILTVVTHPSNptQRIAPDRyFAEVAVRQRLD------VLEEQLRMLATKQPFfeQHDILASVNV 108
Cdd:cd01948    16 YQPIVDlRTGRIVGYEALLRWRHPEG--GLISPAE-FIPLAEETGLIvelgrwVLEEACRQLARWQAG--GPDLRLSVNL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058 109 DGPTLLALRQNAKLQALIATLP----WVRFELVEHVRLPQDSS----FASICEYG-PLWLDDFGTGMANFSALSEVRYDY 179
Cdd:cd01948    91 SARQLRDPDFLDRLLELLAETGlpprRLVLEITESALIDDLEEalatLRRLRALGvRIALDDFGTGYSSLSYLKRLPVDY 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058 180 IKVARDLFIMLRQTPEGRNLFTLLLQLMNRYCQGVIVEGVETLEEWRDVQSSPAAAAQGYFLSRPVPMDR 249
Cdd:cd01948   171 LKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 29-244 3.34e-32

EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.


Pssm-ID: 425752 [Multi-domain]  Cd Length: 235  Bit Score: 117.80  E-value: 3.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058  29 QCERAYTYQPIYR-TDGRLMAIEILTVVTHPSNPTqrIAPDRYFA---EVAVRQRLD--VLEEQLRMLATKQPFfeqHDI 102
Cdd:pfam00563  10 NGEFVLYYQPIVDlRTGRVVGYEALLRWQHPDGGL--ISPARFLPlaeELGLIAELDrwVLEQALADLAQLQLG---PDI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058 103 LASVNVDGPTL----LALRQNAKLQALIATLPWVRFELVEHVRLPQDSSFASICE----YG-PLWLDDFGTGMANFSALS 173
Cdd:pfam00563  85 KLSINLSPASLadpgFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKrlraLGiRIALDDFGTGYSSLSYLL 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1542763058 174 EVRYDYIKVARDLFIMLRQTPEGRNLFTLLLQLMNRYCQGVIVEGVETLEEWRDVQSSPAAAAQGYFLSRP 244
Cdd:pfam00563 165 RLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 36-254 2.03e-31

EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms];


Pssm-ID: 441802 [Multi-domain]  Cd Length: 576  Bit Score: 121.43  E-value: 2.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058  36 YQPIYRT-DGRLMAIEILTVVTHPSNptQRIAPDRYFAeVAVRQRLD------VLEEQLRMLATKQPffEQHDILASVNV 108
Cdd:COG2200   346 YQPIVDLrTGRVVGYEALLRWRHPDG--GLISPAEFIP-AAERSGLIveldrwVLERALRQLARWPE--RGLDLRLSVNL 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058 109 DGPTLLALRQNAKLQALIATLP----WVRFELVEHVRLPQDSSF----ASICEYG-PLWLDDFGTGMANFSALSEVRYDY 179
Cdd:COG2200   421 SARSLLDPDFLERLLELLAEYGlppeRLVLEITESALLEDLEAAiellARLRALGvRIALDDFGTGYSSLSYLKRLPPDY 500

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1542763058 180 IKVARDLFIMLRQTPEGRNLFTLLLQLMNRYCQGVIVEGVETLEEWRDVQSSPAAAAQGYFLSRPVPMDRLDSVI 254
Cdd:COG2200   501 LKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEALL 575
 
Name Accession Description Interval E-value
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
 2-257 7.33e-180

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 494.13  E-value: 7.33e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058   2 KSEQVTQRLSTtPEASIENLQEHRYWLQCERAYTYQPIYRTDGRLMAIEILTVVTHPSNPTQRIAPDRYFAEVAVRQRLD 81
Cdd:PRK11596    1 MIRQVIQRISL-PEASIESLQERRYWLQCERAYTFQPIYRTSGRLMAIELLTAVTHPSNPSQRLSPERYFAEITVSHRLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058  82 VLEEQLRMLATKQPFFEQHDILASVNVDGPTLLALRQNAKLQALIATLPWVRFELVEHVRLPQDSSFASICEYGPLWLDD 161
Cdd:PRK11596   80 VVKEQLDLLAQWADFFVRHGLLASVNIDGPTLIALRQQPAILRLIERLPWLRFELVEHIRLPKDSPFASMCEFGPLWLDD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058 162 FGTGMANFSALSEVRYDYIKVARDLFIMLRQTPEGRNLFTLLLQLMNRYCQGVIVEGVETLEEWRDVQSSPAAAAQGYFL 241
Cdd:PRK11596  160 FGTGMANFSALSEVRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFL 239

                         250
                  ....*....|....*.
gi 1542763058 242 SRPVPMDRLDSVITTL 257
Cdd:PRK11596  240 SRPAPFETLETLPLAL 255
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 29-248 5.37e-46

Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 153.91  E-value: 5.37e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058   29 QCERAYTYQPIY-RTDGRLMAIEILTVVTHPSNptQRIAPDRY---FAEVAVRQRLD--VLEEQLRMLATKQPFFeQHDI 102
Cdd:smart00052  10 NGQFLLYYQPIVsLRTGRLVGVEALIRWQHPEG--GIISPDEFiplAEETGLIVPLGrwVLEQACQQLAEWQAQG-PPPL 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058  103 LASVNVDGPTLLALRQNAKLQALIATLP----WVRFELVEHVRLPQDSS----FASICEYG-PLWLDDFGTGMANFSALS 173
Cdd:smart00052  87 LISINLSARQLISPDLVPRVLELLEETGlppqRLELEITESVLLDDDESavatLQRLRELGvRIALDDFGTGYSSLSYLK 166

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1542763058  174 EVRYDYIKVARDLFIMLRQTPEGRNLFTLLLQLMNRYCQGVIVEGVETLEEWRDVQSSPAAAAQGYFLSRPVPMD 248
Cdd:smart00052 167 RLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLD 241
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 36-249 1.24e-34

EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.


Pssm-ID: 238923 [Multi-domain]  Cd Length: 240  Bit Score: 124.20  E-value: 1.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058  36 YQPIYR-TDGRLMAIEILTVVTHPSNptQRIAPDRyFAEVAVRQRLD------VLEEQLRMLATKQPFfeQHDILASVNV 108
Cdd:cd01948    16 YQPIVDlRTGRIVGYEALLRWRHPEG--GLISPAE-FIPLAEETGLIvelgrwVLEEACRQLARWQAG--GPDLRLSVNL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058 109 DGPTLLALRQNAKLQALIATLP----WVRFELVEHVRLPQDSS----FASICEYG-PLWLDDFGTGMANFSALSEVRYDY 179
Cdd:cd01948    91 SARQLRDPDFLDRLLELLAETGlpprRLVLEITESALIDDLEEalatLRRLRALGvRIALDDFGTGYSSLSYLKRLPVDY 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058 180 IKVARDLFIMLRQTPEGRNLFTLLLQLMNRYCQGVIVEGVETLEEWRDVQSSPAAAAQGYFLSRPVPMDR 249
Cdd:cd01948   171 LKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 29-244 3.34e-32

EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.


Pssm-ID: 425752 [Multi-domain]  Cd Length: 235  Bit Score: 117.80  E-value: 3.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058  29 QCERAYTYQPIYR-TDGRLMAIEILTVVTHPSNPTqrIAPDRYFA---EVAVRQRLD--VLEEQLRMLATKQPFfeqHDI 102
Cdd:pfam00563  10 NGEFVLYYQPIVDlRTGRVVGYEALLRWQHPDGGL--ISPARFLPlaeELGLIAELDrwVLEQALADLAQLQLG---PDI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058 103 LASVNVDGPTL----LALRQNAKLQALIATLPWVRFELVEHVRLPQDSSFASICE----YG-PLWLDDFGTGMANFSALS 173
Cdd:pfam00563  85 KLSINLSPASLadpgFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKrlraLGiRIALDDFGTGYSSLSYLL 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1542763058 174 EVRYDYIKVARDLFIMLRQTPEGRNLFTLLLQLMNRYCQGVIVEGVETLEEWRDVQSSPAAAAQGYFLSRP 244
Cdd:pfam00563 165 RLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 36-254 2.03e-31

EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms];


Pssm-ID: 441802 [Multi-domain]  Cd Length: 576  Bit Score: 121.43  E-value: 2.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058  36 YQPIYRT-DGRLMAIEILTVVTHPSNptQRIAPDRYFAeVAVRQRLD------VLEEQLRMLATKQPffEQHDILASVNV 108
Cdd:COG2200   346 YQPIVDLrTGRVVGYEALLRWRHPDG--GLISPAEFIP-AAERSGLIveldrwVLERALRQLARWPE--RGLDLRLSVNL 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058 109 DGPTLLALRQNAKLQALIATLP----WVRFELVEHVRLPQDSSF----ASICEYG-PLWLDDFGTGMANFSALSEVRYDY 179
Cdd:COG2200   421 SARSLLDPDFLERLLELLAEYGlppeRLVLEITESALLEDLEAAiellARLRALGvRIALDDFGTGYSSLSYLKRLPPDY 500

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1542763058 180 IKVARDLFIMLRQTPEGRNLFTLLLQLMNRYCQGVIVEGVETLEEWRDVQSSPAAAAQGYFLSRPVPMDRLDSVI 254
Cdd:COG2200   501 LKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEALL 575
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 36-250 2.11e-11

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: 63.64  E-value: 2.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058  36 YQPIYRT-DGRLMAIEILTVVTHPsnptQR--IAPDRyFAEVAVR----QRLD--VLEEQLRMLATKQPFFEQHDILAsV 106
Cdd:COG5001   443 YQPQVDLaTGRIVGAEALLRWQHP----ERglVSPAE-FIPLAEEtgliVPLGewVLREACRQLAAWQDAGLPDLRVA-V 516

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058 107 NVDGptlLALRQN---AKLQALIAT--LP--WVRFELVEHVrLPQDSSFAS-----ICEYG-PLWLDDFGTGMANFSALS 173
Cdd:COG5001   517 NLSA---RQLRDPdlvDRVRRALAEtgLPpsRLELEITESA-LLEDPEEALetlraLRALGvRIALDDFGTGYSSLSYLK 592

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058 174 EVRYDYIKVARDlFIM-LRQTPEGRNLFTLLLQL---MNRycqGVIVEGVETLEEWRDVQSSPAAAAQGYFLSRPVPMDR 249
Cdd:COG5001   593 RLPVDTLKIDRS-FVRdLAEDPDDAAIVRAIIALahsLGL---EVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEE 668


                  .
gi 1542763058 250 L 250
Cdd:COG5001   669 L 669
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
159-251 2.35e-06

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 48.14  E-value: 2.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058 159 LDDFGTGMANFSALSEVRYDYIKVARDLFIMLRQTPEGRNLFTLLLQLMNRYCQGVIVEGVETLEEWRDVQSSPAAAAQG 238
Cdd:PRK10060  559 LDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQG 638

                          90
                  ....*....|...
gi 1542763058 239 YFLSRPVPMDRLD 251
Cdd:PRK10060  639 FLFAKPMPAVAFE 651
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
36-250 1.03e-05

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 46.14  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058  36 YQPIYRT-DGRLMAIEILTVVTHPSnpTQRIAPDRY--FAEVavrQRLDV-LEEQL-RMLATKQPFFEQH---DILASVN 107
Cdd:PRK10551  281 YQPVVDTqTLRVTGLEALLRWRHPT--AGEIPPDAFinYAEA---QKLIVpLTQHLfELIARDAAELQKVlpvGAKLGIN 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058 108 VDGPTLLALRQNAKLQALIATLPWVRFELV----------EHVRLPQdssFASICEYG-PLWLDDFGTGMANFSALSEVR 176
Cdd:PRK10551  356 ISPAHLHSDSFKADVQRLLASLPADHFQIVleiterdmvqEEEATKL---FAWLHSQGiEIAIDDFGTGHSALIYLERFT 432

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1542763058 177 YDYIKVARDlFImlrQTPeGRNLFT-----LLLQLMNRYCQGVIVEGVETLEEWRDVQSSPAAAAQGYFLSRPVPMDRL 250
Cdd:PRK10551  433 LDYLKIDRG-FI---QAI-GTETVTspvldAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPLEDF 506
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 82-248 3.12e-05

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 44.70  E-value: 3.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058  82 VLEEQLRMLATKQpffeQHDILA--SVNVdgpTLLALRQNAKLQALIATLPWVR-------FELVEHVRLpqDSSFASIC 152
Cdd:PRK13561  468 VLEESCRLLAAWQ----ERGIMLplSVNL---SALQLMHPNMVADMLELLTRYRiqpgtliLEVTESRRI--DDPHAAVA 538

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058 153 EYGPLW-------LDDFGTGMANFSALSEVR---YDYIKVARDLFIMLrqtPEGRNLFTLLLQLMNRYCQGVIVEGVETl 222
Cdd:PRK13561  539 ILRPLRnagvrvaLDDFGMGYAGLRQLQHMKslpIDVLKIDKMFVDGL---PEDDSMVAAIIMLAQSLNLQVIAEGVET- 614

                         170       180
                  ....*....|....*....|....*..
gi 1542763058 223 EEWRD-VQSSPAAAAQGYFLSRPVPMD 248
Cdd:PRK13561  615 EAQRDwLLKAGVGIAQGFLFARALPIE 641
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 157-246 6.36e-05

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 43.99  E-value: 6.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058 157 LWLDDFGTGMANFSALSEVRYDYIKVARDLFIMLRQTPEGRNLFTLLLQLMNRYCQGVIVEGVETLEEWRDVQSSPAAAA 236
Cdd:PRK11359  694 LSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVI 773

                          90
                  ....*....|
gi 1542763058 237 QGYFLSRPVP 246
Cdd:PRK11359  774 QGYFFSRPLP 783
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 159-250 3.41e-04

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 41.58  E-value: 3.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058  159 LDDFGTGMANFSALSEVRYDYIKVARDLFIMLRQTPEGRNLFTLLLQLMNRYcqgviveGVETLEEWRDVQSSPAA---- 234
Cdd:PRK09776   992 LSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRL-------GMKTIAGPVELPLVLDTlsgi 1064

                           90
                   ....*....|....*....
gi 1542763058  235 ---AAQGYFLSRPVPMDRL 250
Cdd:PRK09776  1065 gvdLAYGYAIARPQPLDLL 1083
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
 159-247 5.01e-03

c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 37.86  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542763058 159 LDDFgTGMANFSALseVRY-DYIKVarDLfimLRQTPEGrnlFTLLLQLMNRYCQGVIVEGVETLEEWRDVQSSPAAAAQ 237
Cdd:COG3434   116 LDDF-VLDPEWDPL--LPLaDIIKI--DV---LALDLEE---LAELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQ 184

                          90
                  ....*....|
gi 1542763058 238 GYFLSRPVPM 247
Cdd:COG3434   185 GYFFSKPEIL 194
 
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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