|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
2-257 |
0e+00 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 498.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 2 KSEQVIQRLSTtPEASIENLQEHRYWLQCERAYTYQPIYRTDGRLMAIEVLTVVTHPSNPSKRIAPDRYFAEVAVRQRID 81
Cdd:PRK11596 1 MIRQVIQRISL-PEASIESLQERRYWLQCERAYTFQPIYRTSGRLMAIELLTAVTHPSNPSQRLSPERYFAEITVSHRLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 82 VLEEQLRMLATKQAFFEQHGILASVNVDGPTLMALRQNATLQALIATLPWMRFELVEHVQLPQDSSFASMCEFGPLWLDD 161
Cdd:PRK11596 80 VVKEQLDLLAQWADFFVRHGLLASVNIDGPTLIALRQQPAILRLIERLPWLRFELVEHIRLPKDSPFASMCEFGPLWLDD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 162 FGTGMANFSALSEVRYDYIKVARDLFIMLRQTPEGRNLFTMLLQLMNRYCQGVIVEGVETLEEWRDVQNSPAAAAQGYFL 241
Cdd:PRK11596 160 FGTGMANFSALSEVRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFL 239
|
250
....*....|....*.
gi 1541808941 242 SRPVPMDTLEKVITSL 257
Cdd:PRK11596 240 SRPAPFETLETLPLAL 255
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
29-249 |
8.53e-45 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 150.83 E-value: 8.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 29 QCERAYTYQPIY-RTDGRLMAIEVLTVVTHPSNpsKRIAPDRYFAEVAVRQRIDVLEEQLRMLATKQAFFEQH----GIL 103
Cdd:smart00052 10 NGQFLLYYQPIVsLRTGRLVGVEALIRWQHPEG--GIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAqgppPLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 104 ASVNVDGPTLMALRQNATLQALIATLP----WMRFELVEHVQLPQDSS----FASMCEFG-PLWLDDFGTGMANFSALSE 174
Cdd:smart00052 88 ISINLSARQLISPDLVPRVLELLEETGlppqRLELEITESVLLDDDESavatLQRLRELGvRIALDDFGTGYSSLSYLKR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1541808941 175 VRYDYIKVARDLFIMLRQTPEGRNLFTMLLQLMNRYCQGVIVEGVETLEEWRDVQNSPAAAAQGYFLSRPVPMDT 249
Cdd:smart00052 168 LPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLDD 242
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
36-254 |
6.41e-34 |
|
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: 128.75 E-value: 6.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 36 YQPIYRT-DGRLMAIEVLTVVTHPSNpsKRIAPDRYFAEVAVRQRIDVLEEQLRMLATKQ-AFFEQHGILA--SVNVDGP 111
Cdd:COG2200 346 YQPIVDLrTGRVVGYEALLRWRHPDG--GLISPAEFIPAAERSGLIVELDRWVLERALRQlARWPERGLDLrlSVNLSAR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 112 TLMALRQNATLQALIATLP----WMRFELVEHVQLPQDSSF----ASMCEFG-PLWLDDFGTGMANFSALSEVRYDYIKV 182
Cdd:COG2200 424 SLLDPDFLERLLELLAEYGlppeRLVLEITESALLEDLEAAiellARLRALGvRIALDDFGTGYSSLSYLKRLPPDYLKI 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1541808941 183 ARDLFIMLRQTPEGRNLFTMLLQLMNRYCQGVIVEGVETLEEWRDVQNSPAAAAQGYFLSRPVPMDTLEKVI 254
Cdd:COG2200 504 DRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEALL 575
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
36-248 |
2.27e-33 |
|
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: 121.11 E-value: 2.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 36 YQPIYR-TDGRLMAIEVLTVVTHPSNPskRIAPDRyFAEVAVR----QRID--VLEEQLRMLATKQAFfeQHGILASVNV 108
Cdd:cd01948 16 YQPIVDlRTGRIVGYEALLRWRHPEGG--LISPAE-FIPLAEEtgliVELGrwVLEEACRQLARWQAG--GPDLRLSVNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 109 DGPTLMALRQNATLQALIATLP----WMRFELVEHVQLPQDSS----FASMCEFG-PLWLDDFGTGMANFSALSEVRYDY 179
Cdd:cd01948 91 SARQLRDPDFLDRLLELLAETGlpprRLVLEITESALIDDLEEalatLRRLRALGvRIALDDFGTGYSSLSYLKRLPVDY 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1541808941 180 IKVARDLFIMLRQTPEGRNLFTMLLQLMNRYCQGVIVEGVETLEEWRDVQNSPAAAAQGYFLSRPVPMD 248
Cdd:cd01948 171 LKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
29-244 |
1.15e-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: 118.96 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 29 QCERAYTYQPIYR-TDGRLMAIEVLTVVTHPSNPSkrIAPDRYFAEVAVRQRID-----VLEEQLRMLATKQAFfeqHGI 102
Cdd:pfam00563 10 NGEFVLYYQPIVDlRTGRVVGYEALLRWQHPDGGL--ISPARFLPLAEELGLIAeldrwVLEQALADLAQLQLG---PDI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 103 LASVNVDGPTL----MALRQNATLQALIATLPWMRFELVEHVQLPQDSSF-ASMCEFGPL----WLDDFGTGMANFSALS 173
Cdd:pfam00563 85 KLSINLSPASLadpgFLELLRALLKQAGPPPSRLVLEITESDLLARLEALrEVLKRLRALgiriALDDFGTGYSSLSYLL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1541808941 174 EVRYDYIKVARDLFIMLRQTPEGRNLFTMLLQLMNRYCQGVIVEGVETLEEWRDVQNSPAAAAQGYFLSRP 244
Cdd:pfam00563 165 RLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
2-257 |
0e+00 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 498.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 2 KSEQVIQRLSTtPEASIENLQEHRYWLQCERAYTYQPIYRTDGRLMAIEVLTVVTHPSNPSKRIAPDRYFAEVAVRQRID 81
Cdd:PRK11596 1 MIRQVIQRISL-PEASIESLQERRYWLQCERAYTFQPIYRTSGRLMAIELLTAVTHPSNPSQRLSPERYFAEITVSHRLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 82 VLEEQLRMLATKQAFFEQHGILASVNVDGPTLMALRQNATLQALIATLPWMRFELVEHVQLPQDSSFASMCEFGPLWLDD 161
Cdd:PRK11596 80 VVKEQLDLLAQWADFFVRHGLLASVNIDGPTLIALRQQPAILRLIERLPWLRFELVEHIRLPKDSPFASMCEFGPLWLDD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 162 FGTGMANFSALSEVRYDYIKVARDLFIMLRQTPEGRNLFTMLLQLMNRYCQGVIVEGVETLEEWRDVQNSPAAAAQGYFL 241
Cdd:PRK11596 160 FGTGMANFSALSEVRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFL 239
|
250
....*....|....*.
gi 1541808941 242 SRPVPMDTLEKVITSL 257
Cdd:PRK11596 240 SRPAPFETLETLPLAL 255
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
29-249 |
8.53e-45 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 150.83 E-value: 8.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 29 QCERAYTYQPIY-RTDGRLMAIEVLTVVTHPSNpsKRIAPDRYFAEVAVRQRIDVLEEQLRMLATKQAFFEQH----GIL 103
Cdd:smart00052 10 NGQFLLYYQPIVsLRTGRLVGVEALIRWQHPEG--GIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAqgppPLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 104 ASVNVDGPTLMALRQNATLQALIATLP----WMRFELVEHVQLPQDSS----FASMCEFG-PLWLDDFGTGMANFSALSE 174
Cdd:smart00052 88 ISINLSARQLISPDLVPRVLELLEETGlppqRLELEITESVLLDDDESavatLQRLRELGvRIALDDFGTGYSSLSYLKR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1541808941 175 VRYDYIKVARDLFIMLRQTPEGRNLFTMLLQLMNRYCQGVIVEGVETLEEWRDVQNSPAAAAQGYFLSRPVPMDT 249
Cdd:smart00052 168 LPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLDD 242
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
36-254 |
6.41e-34 |
|
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: 128.75 E-value: 6.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 36 YQPIYRT-DGRLMAIEVLTVVTHPSNpsKRIAPDRYFAEVAVRQRIDVLEEQLRMLATKQ-AFFEQHGILA--SVNVDGP 111
Cdd:COG2200 346 YQPIVDLrTGRVVGYEALLRWRHPDG--GLISPAEFIPAAERSGLIVELDRWVLERALRQlARWPERGLDLrlSVNLSAR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 112 TLMALRQNATLQALIATLP----WMRFELVEHVQLPQDSSF----ASMCEFG-PLWLDDFGTGMANFSALSEVRYDYIKV 182
Cdd:COG2200 424 SLLDPDFLERLLELLAEYGlppeRLVLEITESALLEDLEAAiellARLRALGvRIALDDFGTGYSSLSYLKRLPPDYLKI 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1541808941 183 ARDLFIMLRQTPEGRNLFTMLLQLMNRYCQGVIVEGVETLEEWRDVQNSPAAAAQGYFLSRPVPMDTLEKVI 254
Cdd:COG2200 504 DRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEALL 575
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
36-248 |
2.27e-33 |
|
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: 121.11 E-value: 2.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 36 YQPIYR-TDGRLMAIEVLTVVTHPSNPskRIAPDRyFAEVAVR----QRID--VLEEQLRMLATKQAFfeQHGILASVNV 108
Cdd:cd01948 16 YQPIVDlRTGRIVGYEALLRWRHPEGG--LISPAE-FIPLAEEtgliVELGrwVLEEACRQLARWQAG--GPDLRLSVNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 109 DGPTLMALRQNATLQALIATLP----WMRFELVEHVQLPQDSS----FASMCEFG-PLWLDDFGTGMANFSALSEVRYDY 179
Cdd:cd01948 91 SARQLRDPDFLDRLLELLAETGlpprRLVLEITESALIDDLEEalatLRRLRALGvRIALDDFGTGYSSLSYLKRLPVDY 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1541808941 180 IKVARDLFIMLRQTPEGRNLFTMLLQLMNRYCQGVIVEGVETLEEWRDVQNSPAAAAQGYFLSRPVPMD 248
Cdd:cd01948 171 LKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
29-244 |
1.15e-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: 118.96 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 29 QCERAYTYQPIYR-TDGRLMAIEVLTVVTHPSNPSkrIAPDRYFAEVAVRQRID-----VLEEQLRMLATKQAFfeqHGI 102
Cdd:pfam00563 10 NGEFVLYYQPIVDlRTGRVVGYEALLRWQHPDGGL--ISPARFLPLAEELGLIAeldrwVLEQALADLAQLQLG---PDI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 103 LASVNVDGPTL----MALRQNATLQALIATLPWMRFELVEHVQLPQDSSF-ASMCEFGPL----WLDDFGTGMANFSALS 173
Cdd:pfam00563 85 KLSINLSPASLadpgFLELLRALLKQAGPPPSRLVLEITESDLLARLEALrEVLKRLRALgiriALDDFGTGYSSLSYLL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1541808941 174 EVRYDYIKVARDLFIMLRQTPEGRNLFTMLLQLMNRYCQGVIVEGVETLEEWRDVQNSPAAAAQGYFLSRP 244
Cdd:pfam00563 165 RLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
36-256 |
3.09e-13 |
|
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: 69.03 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 36 YQPIYRT-DGRLMAIEVLTVVTHPSNPskRIAPDRyFAEVAVR----QRID--VLEEQLRMLATKQAFFEQHGILAsVNV 108
Cdd:COG5001 443 YQPQVDLaTGRIVGAEALLRWQHPERG--LVSPAE-FIPLAEEtgliVPLGewVLREACRQLAAWQDAGLPDLRVA-VNL 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 109 DGptlMALRQNATLQALIATL------P-WMRFELVEHVqLPQDSSFAS-----MCEFG-PLWLDDFGTGMANFSALSEV 175
Cdd:COG5001 519 SA---RQLRDPDLVDRVRRALaetglpPsRLELEITESA-LLEDPEEALetlraLRALGvRIALDDFGTGYSSLSYLKRL 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 176 RYDYIKVARDlFIM-LRQTPEGRNLFTMLLQL---MNRycqGVIVEGVETLEEWRDVQNSPAAAAQGYFLSRPVPMDTLE 251
Cdd:COG5001 595 PVDTLKIDRS-FVRdLAEDPDDAAIVRAIIALahsLGL---EVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELE 670
|
....*
gi 1541808941 252 KVITS 256
Cdd:COG5001 671 ALLRA 675
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
36-246 |
7.23e-08 |
|
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal transduction mechanisms];
Pssm-ID: 443970 [Multi-domain] Cd Length: 528 Bit Score: 52.61 E-value: 7.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 36 YQPIYR-TDGRLMAIEVLTVVTHPSNPSkrIAPDrYFAEVAVRQRidvLEEQLRMLATKQAFFEQHGILA-------SVN 107
Cdd:COG4943 289 YQPIVDlKTGRCVGAEALVRWRDPDGSV--ISPD-IFIPLAEQSG---LISPLTRQVIEQVFRDLGDLLAadpdfhiSIN 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 108 VDGPTLmalrQNATLQALIATLPWM--------RFELVEHVQLPQDSSFASMCEF---G-PLWLDDFGTGMANFSALSEV 175
Cdd:COG4943 363 LSASDL----LSPRFLDDLERLLARtgvapqqiVLEITERGFIDPAKARAVIAALreaGhRIAIDDFGTGYSSLSYLQTL 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1541808941 176 RYDYIKVARdLFIM-LRQTPEGRNLFTMLLQLMNRYCQGVIVEGVETLE--EW---RDVQnspaaAAQGYFLSRPVP 246
Cdd:COG4943 439 PVDILKIDK-SFVDaIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEqaDYlraRGVQ-----YGQGWLFAKPLP 509
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
82-252 |
9.52e-08 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 52.41 E-value: 9.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 82 VLEEQLRMLATKQaffeQHGILA--SVNVDGPTLMALRQNATLQALIA-------TLpwmRFELVEHVQLpqDSSFASMC 152
Cdd:PRK13561 468 VLEESCRLLAAWQ----ERGIMLplSVNLSALQLMHPNMVADMLELLTryriqpgTL---ILEVTESRRI--DDPHAAVA 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 153 EFGPLW-------LDDFGTGMANFSALSEVR---YDYIKVARDLFIMLrqtPEGRNLFTMLLQLMNRYCQGVIVEGVETl 222
Cdd:PRK13561 539 ILRPLRnagvrvaLDDFGMGYAGLRQLQHMKslpIDVLKIDKMFVDGL---PEDDSMVAAIIMLAQSLNLQVIAEGVET- 614
|
170 180 190
....*....|....*....|....*....|.
gi 1541808941 223 EEWRD-VQNSPAAAAQGYFLSRPVPMDTLEK 252
Cdd:PRK13561 615 EAQRDwLLKAGVGIAQGFLFARALPIEIFEE 645
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
36-252 |
2.04e-07 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 51.53 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 36 YQPIYRT-DGRLMAIEVLTVVTHPSnpSKRIAPDRY--FAEVavRQRIDVLEEQLRMLATKQAFFEQH----GILASVNV 108
Cdd:PRK10551 281 YQPVVDTqTLRVTGLEALLRWRHPT--AGEIPPDAFinYAEA--QKLIVPLTQHLFELIARDAAELQKvlpvGAKLGINI 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 109 DGPTLMALRQNATLQALIATLPWMRFELVEHVQ---LPQDSSFASMCEfgplWL---------DDFGTGMANFSALSEVR 176
Cdd:PRK10551 357 SPAHLHSDSFKADVQRLLASLPADHFQIVLEITerdMVQEEEATKLFA----WLhsqgieiaiDDFGTGHSALIYLERFT 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 177 YDYIKVARDlFImlrQTPeGRNLFT-----MLLQLMNRYCQGVIVEGVETLEEWRDVQNSPAAAAQGYFLSRPVPMDTLE 251
Cdd:PRK10551 433 LDYLKIDRG-FI---QAI-GTETVTspvldAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPLEDFV 507
|
.
gi 1541808941 252 K 252
Cdd:PRK10551 508 R 508
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
159-251 |
4.45e-07 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 50.45 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 159 LDDFGTGMANFSALSEVRYDYIKVARDLFIMLRQTPEGRNLFTMLLQLMNRYCQGVIVEGVETLEEWRDVQNSPAAAAQG 238
Cdd:PRK10060 559 LDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQG 638
|
90
....*....|...
gi 1541808941 239 YFLSRPVPMDTLE 251
Cdd:PRK10060 639 FLFAKPMPAVAFE 651
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
157-250 |
3.71e-05 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 44.76 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 157 LWLDDFGTGMANFSALSEVRYDYIKVARDLFIMLRQTPEGRNLFTMLLQLMNRYCQGVIVEGVETLEEWRDVQNSPAAAA 236
Cdd:PRK11359 694 LSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVI 773
|
90
....*....|....
gi 1541808941 237 QGYFLSRPVPMDTL 250
Cdd:PRK11359 774 QGYFFSRPLPAEEI 787
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
159-250 |
6.54e-04 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 40.81 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 159 LDDFGTGMANFSALSEVRYDYIKVARDLFIMLRQTPEGRNLFTMLLQLMNRYcqgviveGVETLEEWRDVQNSPAA---- 234
Cdd:PRK09776 992 LSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRL-------GMKTIAGPVELPLVLDTlsgi 1064
|
90
....*....|....*....
gi 1541808941 235 ---AAQGYFLSRPVPMDTL 250
Cdd:PRK09776 1065 gvdLAYGYAIARPQPLDLL 1083
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
159-249 |
2.95e-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: 38.63 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541808941 159 LDDFgTGMANFSALseVRY-DYIKVarDLfimLRQTPEGrnlFTMLLQLMNRYCQGVIVEGVETLEEWRDVQNSPAAAAQ 237
Cdd:COG3434 116 LDDF-VLDPEWDPL--LPLaDIIKI--DV---LALDLEE---LAELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQ 184
|
90
....*....|..
gi 1541808941 238 GYFLSRPVPMDT 249
Cdd:COG3434 185 GYFFSKPEILKG 196
|
|
| |
