|
Name |
Accession |
Description |
Interval |
E-value |
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
1-525 |
5.13e-173 |
|
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: 498.67 E-value: 5.13e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 1 MPLQILRTLHHRIGIYALSIVLTFGALYGAGLGVYYIYAHEKLEDYAESILARSNSLISQVKLIdgLRQEFAV-YEPCSA 79
Cdd:COG4943 1 MRMRRRRLLSLATLLALLAALLPLLLSLWLAQIQARRREREQLESYAQRALARAERVFDQARSA--LDELNALpGDPCSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 80 QYQQALRKRLWPYPLIKDIAYVEDEKIVCSAlWGKLNAPLSLNMFRNKVNRGSYTWVF-DAQIEENITADVFYTSNFAIT 158
Cdd:COG4943 79 AHLAALRRLVFSSRYVRDIGYVRDGRLLCSS-LGKLSKPVPLPPPDYVTADGYRLWLNvDNPLDPGRPMLIVGRGNYVVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 159 VSPFAFQRFWEEANkmDFDAIIGDFKHENHFFMIGKNTHLLESIEHNKAHSWL----YFTEHACNNTNDICVIAGTSLPL 234
Cdd:COG4943 158 IDPAAFIDVLSPQP--GISLALLATNGGHLFASSGNPDPALLSRLLRGPSSWFiqgdRLYASACSPQYPICVVAAAPLAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 235 FFKNNLYILISLFSASLIIGLLIGALYVNNVSHKESLLSRLKHAIENRELHFVYQPIYRLKDRQVTGVEVLLRWTDPQIG 314
Cdd:COG4943 236 LLALWRQLLLLLLPLGLLLSLLLGLLVLRLLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 315 RIGPDIFIPLAEKNGLINKISLYVVEHSIRECAPILL-NSDITLSINVSCADICSEEFREKLLSTLKDENVAGESIILEI 393
Cdd:COG4943 316 VISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDLLAaDPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 394 TERQSSGTEDIKRSMDLFKGTGIMFALDDFGTGYSNLNWLSLLDVGEIKIDKSITDSIGTESTNKDILPGLIEMFKNIPK 473
Cdd:COG4943 396 TERGFIDPAKARAVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNL 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1532594780 474 IVVFEGVETDIQYQFLKDNVPgGCAQGWYFAKAVPLSELRSVLTDPCGSLPA 525
Cdd:COG4943 476 DVVAEGVETEEQADYLRARGV-QYGQGWLFAKPLPAEEFIAWLAAQRAPASA 526
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
273-511 |
7.08e-76 |
|
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: 239.37 E-value: 7.08e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 273 SRLKHAIENRELHFVYQPIYRLKDRQVTGVEVLLRWTDPQIGRIGPDIFIPLAEKNGLINKISLYVVEHSIRECAPIL-L 351
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 352 NSDITLSINVSCADICSEEFREKLLSTLKDENVAGESIILEITERQS-SGTEDIKRSMDLFKGTGIMFALDDFGTGYSNL 430
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALiDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 431 NWLSLLDVGEIKIDKSITDSIGTESTNKDILPGLIEMFKNIPKIVVFEGVETDIQYQFLKDNvpgGC--AQGWYFAKAVP 508
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLREL---GCdyVQGYLFSRPLP 237
|
...
gi 1532594780 509 LSE 511
Cdd:cd01948 238 AEE 240
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
274-506 |
9.57e-63 |
|
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: 204.86 E-value: 9.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 274 RLKHAIENRELHFVYQPIYRLKDRQVTGVEVLLRWTDPQIGRIGPDIFIPLAEKNGLINKISLYVVEHSIRECAPILLNS 353
Cdd:pfam00563 3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 354 DITLSINVSCADICSEEFREKLLSTLKDENVAGESIILEITERQ-SSGTEDIKRSMDLFKGTGIMFALDDFGTGYSNLNW 432
Cdd:pfam00563 83 DIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDlLARLEALREVLKRLRALGIRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1532594780 433 LSLLDVGEIKIDKSITDSIGTESTNKDILPGLIEMFKNIPKIVVFEGVETDIQYQFLKDNvpgGC--AQGWYFAKA 506
Cdd:pfam00563 163 LLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALREL---GCdlVQGYYFSKP 235
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
274-509 |
3.44e-60 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 198.60 E-value: 3.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 274 RLKHAIENRELHFVYQPIYRLKDRQVTGVEVLLRWTDPQIGRIGPDIFIPLAEKNGLINKISLYVVEHSIRECAPI--LL 351
Cdd:smart00052 3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWqaQG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 352 NSDITLSINVSCADICSEEFREKLLSTLKDENVAGESIILEITERQSSGTEDIKRSM-DLFKGTGIMFALDDFGTGYSNL 430
Cdd:smart00052 83 PPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATlQRLRELGVRIALDDFGTGYSSL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 431 NWLSLLDVGEIKIDKSITDSIGTESTNKDILPGLIEMFKNIPKIVVFEGVETDIQYQFLKDNvpgGC--AQGWYFAKAVP 508
Cdd:smart00052 163 SYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSL---GCdyGQGYLFSRPLP 239
|
.
gi 1532594780 509 L 509
Cdd:smart00052 240 L 240
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
264-512 |
5.57e-40 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 154.54 E-value: 5.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 264 NVSHKESLL--SRLKHAIENRELHFVYQPIYRLKDRQVTGVEVLLRWTDPQIGRIGPDIFIPLAEKNGLINKISLYVVEH 341
Cdd:PRK11359 535 NEMVKERLVlgAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAE 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 342 SIRECAPI-LLNSDI-TLSINVSCADICSEEFREKLLSTLKDENVAGESIILEITERQS-SGTEDIKRSMDLFKGTGIMF 418
Cdd:PRK11359 615 ACRQLAEWrSQNIHIpALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMmEHDTEIFKRIQILRDMGVGL 694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 419 ALDDFGTGYSNLNWLSLLDVGEIKIDKSITDSIGTESTNKDILPGLIEMFKNIPKIVVFEGVETDIQYQFLKDNvpgGC- 497
Cdd:PRK11359 695 SVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKI---HCr 771
|
250
....*....|....*.
gi 1532594780 498 -AQGWYFAKAVPLSEL 512
Cdd:PRK11359 772 vIQGYFFSRPLPAEEI 787
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
1-525 |
5.13e-173 |
|
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: 498.67 E-value: 5.13e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 1 MPLQILRTLHHRIGIYALSIVLTFGALYGAGLGVYYIYAHEKLEDYAESILARSNSLISQVKLIdgLRQEFAV-YEPCSA 79
Cdd:COG4943 1 MRMRRRRLLSLATLLALLAALLPLLLSLWLAQIQARRREREQLESYAQRALARAERVFDQARSA--LDELNALpGDPCSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 80 QYQQALRKRLWPYPLIKDIAYVEDEKIVCSAlWGKLNAPLSLNMFRNKVNRGSYTWVF-DAQIEENITADVFYTSNFAIT 158
Cdd:COG4943 79 AHLAALRRLVFSSRYVRDIGYVRDGRLLCSS-LGKLSKPVPLPPPDYVTADGYRLWLNvDNPLDPGRPMLIVGRGNYVVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 159 VSPFAFQRFWEEANkmDFDAIIGDFKHENHFFMIGKNTHLLESIEHNKAHSWL----YFTEHACNNTNDICVIAGTSLPL 234
Cdd:COG4943 158 IDPAAFIDVLSPQP--GISLALLATNGGHLFASSGNPDPALLSRLLRGPSSWFiqgdRLYASACSPQYPICVVAAAPLAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 235 FFKNNLYILISLFSASLIIGLLIGALYVNNVSHKESLLSRLKHAIENRELHFVYQPIYRLKDRQVTGVEVLLRWTDPQIG 314
Cdd:COG4943 236 LLALWRQLLLLLLPLGLLLSLLLGLLVLRLLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 315 RIGPDIFIPLAEKNGLINKISLYVVEHSIRECAPILL-NSDITLSINVSCADICSEEFREKLLSTLKDENVAGESIILEI 393
Cdd:COG4943 316 VISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDLLAaDPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 394 TERQSSGTEDIKRSMDLFKGTGIMFALDDFGTGYSNLNWLSLLDVGEIKIDKSITDSIGTESTNKDILPGLIEMFKNIPK 473
Cdd:COG4943 396 TERGFIDPAKARAVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNL 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1532594780 474 IVVFEGVETDIQYQFLKDNVPgGCAQGWYFAKAVPLSELRSVLTDPCGSLPA 525
Cdd:COG4943 476 DVVAEGVETEEQADYLRARGV-QYGQGWLFAKPLPAEEFIAWLAAQRAPASA 526
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
273-511 |
7.08e-76 |
|
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: 239.37 E-value: 7.08e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 273 SRLKHAIENRELHFVYQPIYRLKDRQVTGVEVLLRWTDPQIGRIGPDIFIPLAEKNGLINKISLYVVEHSIRECAPIL-L 351
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 352 NSDITLSINVSCADICSEEFREKLLSTLKDENVAGESIILEITERQS-SGTEDIKRSMDLFKGTGIMFALDDFGTGYSNL 430
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALiDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 431 NWLSLLDVGEIKIDKSITDSIGTESTNKDILPGLIEMFKNIPKIVVFEGVETDIQYQFLKDNvpgGC--AQGWYFAKAVP 508
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLREL---GCdyVQGYLFSRPLP 237
|
...
gi 1532594780 509 LSE 511
Cdd:cd01948 238 AEE 240
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
265-516 |
2.08e-73 |
|
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: 243.54 E-value: 2.08e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 265 VSHKESLLSRLKHAIENRELHFVYQPIYRLKDRQVTGVEVLLRWTDPQIGRIGPDIFIPLAEKNGLINKISLYVVEHSIR 344
Cdd:COG2200 323 ARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALR 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 345 ECAPI-LLNSDITLSINVSCADICSEEFREKLLSTLKDENVAGESIILEITERQS-SGTEDIKRSMDLFKGTGIMFALDD 422
Cdd:COG2200 403 QLARWpERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALlEDLEAAIELLARLRALGVRIALDD 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 423 FGTGYSNLNWLSLLDVGEIKIDKSITDSIGTESTNKDILPGLIEMFKNIPKIVVFEGVETDIQYQFLKDNvpgGC--AQG 500
Cdd:COG2200 483 FGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALREL---GCdyAQG 559
|
250
....*....|....*.
gi 1532594780 501 WYFAKAVPLSELRSVL 516
Cdd:COG2200 560 YLFGRPLPLEELEALL 575
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
270-518 |
1.84e-71 |
|
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: 240.83 E-value: 1.84e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 270 SLLSRLKHAIENRELHFVYQPIYRLKDRQVTGVEVLLRWTDPQIGRIGPDIFIPLAEKNGLINKISLYVVEHSIRECA-- 347
Cdd:COG5001 425 ELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAaw 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 348 PILLNSDITLSINVSCADICSEEFREKLLSTLKDENVAGESIILEITERQ-SSGTEDIKRSMDLFKGTGIMFALDDFGTG 426
Cdd:COG5001 505 QDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESAlLEDPEEALETLRALRALGVRIALDDFGTG 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 427 YSNLNWLSLLDVGEIKIDKSITDSIGTESTNKDILPGLIEMFKNIPKIVVFEGVETDIQYQFLKDNvpgGC--AQGWYFA 504
Cdd:COG5001 585 YSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLREL---GCdyAQGYLFS 661
|
250
....*....|....
gi 1532594780 505 KAVPLSELRSVLTD 518
Cdd:COG5001 662 RPLPAEELEALLRA 675
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
274-506 |
9.57e-63 |
|
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: 204.86 E-value: 9.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 274 RLKHAIENRELHFVYQPIYRLKDRQVTGVEVLLRWTDPQIGRIGPDIFIPLAEKNGLINKISLYVVEHSIRECAPILLNS 353
Cdd:pfam00563 3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 354 DITLSINVSCADICSEEFREKLLSTLKDENVAGESIILEITERQ-SSGTEDIKRSMDLFKGTGIMFALDDFGTGYSNLNW 432
Cdd:pfam00563 83 DIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDlLARLEALREVLKRLRALGIRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1532594780 433 LSLLDVGEIKIDKSITDSIGTESTNKDILPGLIEMFKNIPKIVVFEGVETDIQYQFLKDNvpgGC--AQGWYFAKA 506
Cdd:pfam00563 163 LLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALREL---GCdlVQGYYFSKP 235
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
274-509 |
3.44e-60 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 198.60 E-value: 3.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 274 RLKHAIENRELHFVYQPIYRLKDRQVTGVEVLLRWTDPQIGRIGPDIFIPLAEKNGLINKISLYVVEHSIRECAPI--LL 351
Cdd:smart00052 3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWqaQG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 352 NSDITLSINVSCADICSEEFREKLLSTLKDENVAGESIILEITERQSSGTEDIKRSM-DLFKGTGIMFALDDFGTGYSNL 430
Cdd:smart00052 83 PPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATlQRLRELGVRIALDDFGTGYSSL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 431 NWLSLLDVGEIKIDKSITDSIGTESTNKDILPGLIEMFKNIPKIVVFEGVETDIQYQFLKDNvpgGC--AQGWYFAKAVP 508
Cdd:smart00052 163 SYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSL---GCdyGQGYLFSRPLP 239
|
.
gi 1532594780 509 L 509
Cdd:smart00052 240 L 240
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
264-512 |
5.57e-40 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 154.54 E-value: 5.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 264 NVSHKESLL--SRLKHAIENRELHFVYQPIYRLKDRQVTGVEVLLRWTDPQIGRIGPDIFIPLAEKNGLINKISLYVVEH 341
Cdd:PRK11359 535 NEMVKERLVlgAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAE 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 342 SIRECAPI-LLNSDI-TLSINVSCADICSEEFREKLLSTLKDENVAGESIILEITERQS-SGTEDIKRSMDLFKGTGIMF 418
Cdd:PRK11359 615 ACRQLAEWrSQNIHIpALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMmEHDTEIFKRIQILRDMGVGL 694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 419 ALDDFGTGYSNLNWLSLLDVGEIKIDKSITDSIGTESTNKDILPGLIEMFKNIPKIVVFEGVETDIQYQFLKDNvpgGC- 497
Cdd:PRK11359 695 SVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKI---HCr 771
|
250
....*....|....*.
gi 1532594780 498 -AQGWYFAKAVPLSEL 512
Cdd:PRK11359 772 vIQGYFFSRPLPAEEI 787
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
226-519 |
4.11e-38 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 146.68 E-value: 4.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 226 VIAGTSLPLFFKNNLY----ILISLFsASLIIGLLIGAL----YVNNVSHKESLLSrlkhAIENRELHFVYQPIYRLKDR 297
Cdd:PRK10551 216 TIPGYPLTIRLYADSWtandIWYALL-LGLLSGILVGLLcyylLSLRMRPGKEILT----GIKRGQFYVEYQPVVDTQTL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 298 QVTGVEVLLRWTDPQIGRIGPDIFIPLAEKNGLINKISLYVVEHSIREcAPILLNS---DITLSINVSCADICSEEFREK 374
Cdd:PRK10551 291 RVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARD-AAELQKVlpvGAKLGINISPAHLHSDSFKAD 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 375 LLSTLKDENVAGESIILEITERQSSGTEDIKRSMDLFKGTGIMFALDDFGTGYSNLNWLSLLDVGEIKIDKSITDSIGTE 454
Cdd:PRK10551 370 VQRLLASLPADHFQIVLEITERDMVQEEEATKLFAWLHSQGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTE 449
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1532594780 455 STNKDILPGLIEMFKNIPKIVVFEGVETDIQYQFLKDNvpgGCA--QGWYFAKAVPLSELRSVLTDP 519
Cdd:PRK10551 450 TVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRER---GVNflQGYWISRPLPLEDFVRWLKEP 513
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
275-512 |
3.28e-33 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 133.91 E-value: 3.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 275 LKHAIENRELHFVYQPIYRLKDRQVTGVEVLLRWTDPQIGRIGPDIFIPLAEKNGLINKISLYVVEHSIRecapILLN-- 352
Cdd:PRK11829 410 LLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACR----ILADwk 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 353 ---SDITLSINVSCADICSEEFREKLLSTLKDENVAGESIILEITErqSSGTEDIKRSMDL---FKGTGIMFALDDFGTG 426
Cdd:PRK11829 486 argVSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITE--TAQIQDLDEALRLlreLQGLGLLIALDDFGIG 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 427 YSNLNWL---SLLDVGEIKIDKSITDSIGTESTNKDILPGLIEMFKnipKIVVFEGVETDIQYQFLKDNvpgG--CAQGW 501
Cdd:PRK11829 564 YSSLRYLnhlKSLPIHMIKLDKSFVKNLPEDDAIARIISCVSDVLK---VRVMAEGVETEEQRQWLLEH---GiqCGQGF 637
|
250
....*....|.
gi 1532594780 502 YFAKAVPLSEL 512
Cdd:PRK11829 638 LFSPPLPRAEF 648
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
273-511 |
4.54e-30 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 124.44 E-value: 4.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 273 SRLKHAIENRELHFVYQPIYRLKDRQVTGVEVLLRWTDPQIGRIGPDIFIPLAEKNGLINKISLYVVEHSIRECAP---- 348
Cdd:PRK13561 403 SDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAwqer 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 349 -ILLnsdiTLSINVSCADICSEEFREKLLSTLKDENVAGESIILEITERQSSGteDIKRSMDLFKG---TGIMFALDDFG 424
Cdd:PRK13561 483 gIML----PLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRID--DPHAAVAILRPlrnAGVRVALDDFG 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 425 TGYSNLNWLS---LLDVGEIKIDKSITDSIGTESTnkdILPGLIEMFKNIPKIVVFEGVETDIQYQFLKdNVPGGCAQGW 501
Cdd:PRK13561 557 MGYAGLRQLQhmkSLPIDVLKIDKMFVDGLPEDDS---MVAAIIMLAQSLNLQVIAEGVETEAQRDWLL-KAGVGIAQGF 632
|
250
....*....|
gi 1532594780 502 YFAKAVPLSE 511
Cdd:PRK13561 633 LFARALPIEI 642
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
275-508 |
1.94e-25 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 110.54 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 275 LKHAIENRELHFVYQPIYRLKDRqVTGVEVLLRWTDPQIGRIGPDIFIPLAEKNGLINKISLYVVEHSIRECAP-----I 349
Cdd:PRK10060 413 LRKALENDQLVIHYQPKITWRGE-VRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKwrdkgI 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 350 llnsDITLSINVSCADICSEEFREKLLSTLKDENVAGESIILEITErqSSGTEDIKRSMDL---FKGTGIMFALDDFGTG 426
Cdd:PRK10060 492 ----NLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTE--SCLIENEELALSViqqFSQLGAQVHLDDFGTG 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 427 YSNLNWLSLLDVGEIKIDKSITDSIGTESTNKDILPGLIEMFKNIPKIVVFEGVETDIQYQFLKDNVPGGcAQGWYFAKA 506
Cdd:PRK10060 566 YSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNE-RQGFLFAKP 644
|
..
gi 1532594780 507 VP 508
Cdd:PRK10060 645 MP 646
|
|
| CSS-motif |
pfam12792 |
CSS motif domain associated with EAL; This family with its characteriztic highly conserved CSS ... |
41-243 |
1.93e-16 |
|
CSS motif domain associated with EAL; This family with its characteriztic highly conserved CSS sequence motif is found N-terminal to the EAL, pfam00563, domain in many cyclic diguanylate phosphodiesterases.
Pssm-ID: 463709 Cd Length: 209 Bit Score: 77.95 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 41 EKLEDYAESILARSNSLISQVKLIDGLRQEFAVyEPCSAQYQQALRKRLWPYPLIKDIAYVEDEKIVCSALWGKLNAPLS 120
Cdd:pfam12792 3 EQLDAFAERALRRLESVLDQADQALDRLLPLTG-QPCSPAHLAELRRIVAFSPYVRDVGLVKNGRLYCSSLWGELDTPLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 121 LNMFRNKVNRGSYTWVF-DAQIEENITADVFYTSNFAITVSPFAFqrfweeankMDFDAIIG-----DFKHENHFFMIGK 194
Cdd:pfam12792 82 LLPPDLTTPPGVRLWLLrGTPLVPGRPALVLRRGGYGVVIDPGVF---------IDVQYLPGllaavSQPDGRLLALVVG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1532594780 195 NTHL-----LESIEHNKAHSWL---YFTEHACNNTNDICVIAGTSLPLFFKNNLYIL 243
Cdd:pfam12792 153 DDALlfdgrLHSLAEPAPGTARsggALYARARSTRYPLTVVVYAPRASLLANWRQLL 209
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
266-446 |
1.04e-11 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 67.78 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 266 SHKE-SLLSRLKHAIENRELHFVYQPIYRLKDRQVTGVEVLLRWTDPQIGRIGPDIFIPLAEKNGLINKISLYVVEHSIR 344
Cdd:PRK09776 836 EHRAlSLAEQWRMIKENQLMMLAHGVASPRIPEARNHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFR 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 345 ECAPILLNSDITLSINVSCADICSEEFREKLLSTLKDENVAGESIILEITERQ-SSGTEDIKRSMDLFKGTGIMFALDDF 423
Cdd:PRK09776 916 QAAKAVASKGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETAlLNHAESASRLVQKLRLAGCRVVLSDF 995
|
170 180
....*....|....*....|...
gi 1532594780 424 GTGYSNLNWLSLLDVGEIKIDKS 446
Cdd:PRK09776 996 GRGLSSFNYLKAFMADYLKLDGE 1018
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
275-509 |
1.08e-07 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 54.48 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 275 LKHAIENRELHFVYQPIYrLKDRQVTGVEVLLRWTDPQIGRIGPDIFIPLAEKNGLINKISLYVVEHSIrecAPILLNSD 354
Cdd:PRK11059 408 LEQTLVRGGPRLYQQPAV-TRDGKVHHRELFCRIRDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVL---PLLRYWPE 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 355 ITLSINVSCADICSEEF----REKLLSTLKDENvagESIILEITERQ-SSGTEDIKRSMDLFKGTGIMFALDDFG----- 424
Cdd:PRK11059 484 ENLSINLSVDSLLSRAFqrwlRDTLLQCPRSQR---KRLIFELAEADvCQHISRLRPVLRMLRGLGCRLAVDQAGltvvs 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 425 TGYsnlnwLSLLDVGEIKIDKSITDSIGTESTNKDILPGLIEMFKNIPKIVVFEGVETDIQYQFLKDN-VPGGcaQGWYF 503
Cdd:PRK11059 561 TSY-----IKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFATGVESREEWQTLQELgVSGG--QGDFF 633
|
....*.
gi 1532594780 504 AKAVPL 509
Cdd:PRK11059 634 AESQPL 639
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
420-515 |
1.20e-07 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 53.08 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 420 LDDFGTGYSNLNWLSLLDVGEIKIDKSITDSIGTESTNKDILPGLIEMFKNIPKIVVFEGVETDIQYQFLKdNVPGGCAQ 499
Cdd:PRK11596 157 LDDFGTGMANFSALSEVRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQ-RSPAFAAQ 235
|
90
....*....|....*.
gi 1532594780 500 GWYFAKAVPLSELRSV 515
Cdd:PRK11596 236 GYFLSRPAPFETLETL 251
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
387-510 |
7.08e-07 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 51.73 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532594780 387 ESIILEITERqSSGTEDIKRSMDLFKGTGIMFALDDFGTGYSNLNWLSLLDVgeIKIDksitdsigTESTNKDILPGLIE 466
Cdd:COG3434 84 ERVVLEILED-VEPDEELLEALKELKEKGYRIALDDFVLDPEWDPLLPLADI--IKID--------VLALDLEELAELVA 152
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1532594780 467 MFKNIPKIVVFEGVETDIQYQFLKDNvpgGCA--QGWYFAKAVPLS 510
Cdd:COG3434 153 RLKRYGIKLLAEKVETREEFELCKEL---GFDlfQGYFFSKPEILK 195
|
|
|