|
Name |
Accession |
Description |
Interval |
E-value |
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
1-525 |
3.11e-178 |
|
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: 512.15 E-value: 3.11e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 1 MEAGRRSI----WIICLVWVFLGGICSLVIAEFIRNHSADEYVDYYGSDVFQNAVSVAETSLTVLRTLDRSDNAPCSAED 76
Cdd:COG4943 1 MRMRRRRLlslaTLLALLAALLPLLLSLWLAQIQARRREREQLESYAQRALARAERVFDQARSALDELNALPGDPCSPAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 77 LEAMRGVVFAAPYLTDVGRLRDGYLVCTGiWGELATPVKMPPRSQVVGvNAATLWKGARGIAPAGLAVDMSSFGNSVVMT 156
Cdd:COG4943 81 LAALRRLVFSSRYVRDIGYVRDGRLLCSS-LGKLSKPVPLPPPDYVTA-DGYRLWLNVDNPLDPGRPMLIVGRGNYVVVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 157 APTAFARYEDPAERLAALVLTSDASYSYQSFGDTEG--LAPLLGSNSDWYRIAQRRVYSRCNDKIDVCVVATYDAPALLK 234
Cdd:COG4943 159 DPAAFIDVLSPQPGISLALLATNGGHLFASSGNPDPalLSRLLRGPSSWFIQGDRLYASACSPQYPICVVAAAPLAGLLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 235 TAPLDFLLVLAGGVSAGACLGLWHAHLYREGRSWRQKLERALNDDRLTVHYQPIVRLSDNRICGAEALARLVDFDGTLIP 314
Cdd:COG4943 239 LWRQLLLLLLPLGLLLSLLLGLLVLRLLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVIS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 315 PDHFIPAAETCGFIGQITRSVVRRAFTDMAAHFAADPDFYVSINVASEDILSLEFLDFLETETRSHGLSAGQVALELTER 394
Cdd:COG4943 319 PDIFIPLAEQSGLISPLTRQVIEQVFRDLGDLLAADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITER 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 395 STASQDSLTQAMAAFSRRGYRILIDDFGTGYSNLAYIARMPIAGIKIDRMFTQALDQQAIGAVIVSKVCELAAVLEVTLI 474
Cdd:COG4943 399 GFIDPAKARAVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVV 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 516723119 475 CEGVETKGQADHLVAIYPDICiQGFLIGRPMPARQFSRAFPANHHAWTPSP 525
Cdd:COG4943 479 AEGVETEEQADYLRARGVQYG-QGWLFAKPLPAEEFIAWLAAQRAPASAPA 528
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
272-509 |
4.36e-82 |
|
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: 255.55 E-value: 4.36e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 272 LERALNDDRLTVHYQPIVRLSDNRICGAEALARLVDFDGTLIPPDHFIPAAETCGFIGQITRSVVRRAFTDMAAHFAADP 351
Cdd:cd01948 3 LRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAGGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 352 DFYVSINVASEDILSLEFLDFLETETRSHGLSAGQVALELTERSTASQ-DSLTQAMAAFSRRGYRILIDDFGTGYSNLAY 430
Cdd:cd01948 83 DLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDlEEALATLRRLRALGVRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516723119 431 IARMPIAGIKIDRMFTQALDQQAIGAVIVSKVCELAAVLEVTLICEGVETKGQADHLVAIYPDiCIQGFLIGRPMPARQ 509
Cdd:cd01948 163 LKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCD-YVQGYLFSRPLPAEE 240
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
269-504 |
7.40e-66 |
|
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: 213.33 E-value: 7.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 269 RQKLERALNDDRLTVHYQPIVRLSDNRICGAEALARLVDFDGTLIPPDHFIPAAETCGFIGQITRSVVRRAFTDMAAHfA 348
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQL-Q 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 349 ADPDFYVSINVASEDILSLEFLDFLETETRSHGLSAGQVALELTERS-TASQDSLTQAMAAFSRRGYRILIDDFGTGYSN 427
Cdd:pfam00563 80 LGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDlLARLEALREVLKRLRALGIRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516723119 428 LAYIARMPIAGIKIDRMFTQALDQQAIGAVIVSKVCELAAVLEVTLICEGVETKGQADHLVAIYPDiCIQGFLIGRP 504
Cdd:pfam00563 160 LSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCD-LVQGYYFSKP 235
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
272-509 |
8.68e-64 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 208.23 E-value: 8.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 272 LERALNDDRLTVHYQPIVRLSDNRICGAEALARLVDFDGTLIPPDHFIPAAETCGFIGQITRSVVRRAFTDMAAHFAA-D 350
Cdd:smart00052 4 LRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQgP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 351 PDFYVSINVASEDILSLEFLDFLETETRSHGLSAGQVALELTERSTASQDSLTQAM-AAFSRRGYRILIDDFGTGYSNLA 429
Cdd:smart00052 84 PPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATlQRLRELGVRIALDDFGTGYSSLS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 430 YIARMPIAGIKIDRMFTQALDQQAIGAVIVSKVCELAAVLEVTLICEGVETKGQADHLVAIYPDIcIQGFLIGRPMPARQ 509
Cdd:smart00052 164 YLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDY-GQGYLFSRPLPLDD 242
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
272-512 |
7.88e-40 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 153.30 E-value: 7.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 272 LERALNDDRLTVHYQPIVRLSdNRICGAEALARLVDFDGTLIPPDHFIPAAETCGFIGQITRSVVRRAFTDMAAHFAADP 351
Cdd:PRK10060 413 LRKALENDQLVIHYQPKITWR-GEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGI 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 352 DFYVSINVASEDILSLEFLDFLETETRSHGLSAGQVALELTERSTASQDSLTQA-MAAFSRRGYRILIDDFGTGYSNLAY 430
Cdd:PRK10060 492 NLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIENEELALSvIQQFSQLGAQVHLDDFGTGYSSLSQ 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 431 IARMPIAGIKIDRMFTQALDQQAIGAVIVSKVCELAAVLEVTLICEGVETKGQADHLVAIYPDIcIQGFLIGRPMPARQF 510
Cdd:PRK10060 572 LARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNE-RQGFLFAKPMPAVAF 650
|
..
gi 516723119 511 SR 512
Cdd:PRK10060 651 ER 652
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
1-525 |
3.11e-178 |
|
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: 512.15 E-value: 3.11e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 1 MEAGRRSI----WIICLVWVFLGGICSLVIAEFIRNHSADEYVDYYGSDVFQNAVSVAETSLTVLRTLDRSDNAPCSAED 76
Cdd:COG4943 1 MRMRRRRLlslaTLLALLAALLPLLLSLWLAQIQARRREREQLESYAQRALARAERVFDQARSALDELNALPGDPCSPAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 77 LEAMRGVVFAAPYLTDVGRLRDGYLVCTGiWGELATPVKMPPRSQVVGvNAATLWKGARGIAPAGLAVDMSSFGNSVVMT 156
Cdd:COG4943 81 LAALRRLVFSSRYVRDIGYVRDGRLLCSS-LGKLSKPVPLPPPDYVTA-DGYRLWLNVDNPLDPGRPMLIVGRGNYVVVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 157 APTAFARYEDPAERLAALVLTSDASYSYQSFGDTEG--LAPLLGSNSDWYRIAQRRVYSRCNDKIDVCVVATYDAPALLK 234
Cdd:COG4943 159 DPAAFIDVLSPQPGISLALLATNGGHLFASSGNPDPalLSRLLRGPSSWFIQGDRLYASACSPQYPICVVAAAPLAGLLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 235 TAPLDFLLVLAGGVSAGACLGLWHAHLYREGRSWRQKLERALNDDRLTVHYQPIVRLSDNRICGAEALARLVDFDGTLIP 314
Cdd:COG4943 239 LWRQLLLLLLPLGLLLSLLLGLLVLRLLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVIS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 315 PDHFIPAAETCGFIGQITRSVVRRAFTDMAAHFAADPDFYVSINVASEDILSLEFLDFLETETRSHGLSAGQVALELTER 394
Cdd:COG4943 319 PDIFIPLAEQSGLISPLTRQVIEQVFRDLGDLLAADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITER 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 395 STASQDSLTQAMAAFSRRGYRILIDDFGTGYSNLAYIARMPIAGIKIDRMFTQALDQQAIGAVIVSKVCELAAVLEVTLI 474
Cdd:COG4943 399 GFIDPAKARAVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVV 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 516723119 475 CEGVETKGQADHLVAIYPDICiQGFLIGRPMPARQFSRAFPANHHAWTPSP 525
Cdd:COG4943 479 AEGVETEEQADYLRARGVQYG-QGWLFAKPLPAEEFIAWLAAQRAPASAPA 528
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
272-509 |
4.36e-82 |
|
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: 255.55 E-value: 4.36e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 272 LERALNDDRLTVHYQPIVRLSDNRICGAEALARLVDFDGTLIPPDHFIPAAETCGFIGQITRSVVRRAFTDMAAHFAADP 351
Cdd:cd01948 3 LRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAGGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 352 DFYVSINVASEDILSLEFLDFLETETRSHGLSAGQVALELTERSTASQ-DSLTQAMAAFSRRGYRILIDDFGTGYSNLAY 430
Cdd:cd01948 83 DLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDlEEALATLRRLRALGVRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516723119 431 IARMPIAGIKIDRMFTQALDQQAIGAVIVSKVCELAAVLEVTLICEGVETKGQADHLVAIYPDiCIQGFLIGRPMPARQ 509
Cdd:cd01948 163 LKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCD-YVQGYLFSRPLPAEE 240
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
219-510 |
3.84e-76 |
|
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: 250.86 E-value: 3.84e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 219 IDVCVVATYDAPALLKTAPLDFLLVLAGGVSAGACLGLWHAHLYREGRSWRQKLERALNDDRLTVHYQPIVRLSDNRICG 298
Cdd:COG2200 280 GGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAEARARRRLALESELREALEEGELRLYYQPIVDLRTGRVVG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 299 AEALARLVDFDGTLIPPDHFIPAAETCGFIGQITRSVVRRAFTDMAAHFAADPDFYVSINVASEDILSLEFLDFLETETR 378
Cdd:COG2200 360 YEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPERGLDLRLSVNLSARSLLDPDFLERLLELLA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 379 SHGLSAGQVALELTERSTASQ-DSLTQAMAAFSRRGYRILIDDFGTGYSNLAYIARMPIAGIKIDRMFTQALDQQAIGAV 457
Cdd:COG2200 440 EYGLPPERLVLEITESALLEDlEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQA 519
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 516723119 458 IVSKVCELAAVLEVTLICEGVETKGQADHLVAIYPDIcIQGFLIGRPMPARQF 510
Cdd:COG2200 520 IVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDY-AQGYLFGRPLPLEEL 571
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
263-512 |
2.59e-70 |
|
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: 237.75 E-value: 2.59e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 263 REGRSWRQKLERALNDDRLTVHYQPIVRLSDNRICGAEALARLVDFDGTLIPPDHFIPAAETCGFIGQITRSVVRRAFTD 342
Cdd:COG5001 421 RERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQ 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 343 MAA-HFAADPDFYVSINVASEDILSLEFLDFLETETRSHGLSAGQVALELTERSTASQDSLT-QAMAAFSRRGYRILIDD 420
Cdd:COG5001 501 LAAwQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEAlETLRALRALGVRIALDD 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 421 FGTGYSNLAYIARMPIAGIKIDRMFTQALDQQAIGAVIVSKVCELAAVLEVTLICEGVETKGQADHLVAIYPDIcIQGFL 500
Cdd:COG5001 581 FGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDY-AQGYL 659
|
250
....*....|..
gi 516723119 501 IGRPMPARQFSR 512
Cdd:COG5001 660 FSRPLPAEELEA 671
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
269-504 |
7.40e-66 |
|
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: 213.33 E-value: 7.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 269 RQKLERALNDDRLTVHYQPIVRLSDNRICGAEALARLVDFDGTLIPPDHFIPAAETCGFIGQITRSVVRRAFTDMAAHfA 348
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQL-Q 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 349 ADPDFYVSINVASEDILSLEFLDFLETETRSHGLSAGQVALELTERS-TASQDSLTQAMAAFSRRGYRILIDDFGTGYSN 427
Cdd:pfam00563 80 LGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDlLARLEALREVLKRLRALGIRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516723119 428 LAYIARMPIAGIKIDRMFTQALDQQAIGAVIVSKVCELAAVLEVTLICEGVETKGQADHLVAIYPDiCIQGFLIGRP 504
Cdd:pfam00563 160 LSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCD-LVQGYYFSKP 235
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
272-509 |
8.68e-64 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 208.23 E-value: 8.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 272 LERALNDDRLTVHYQPIVRLSDNRICGAEALARLVDFDGTLIPPDHFIPAAETCGFIGQITRSVVRRAFTDMAAHFAA-D 350
Cdd:smart00052 4 LRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQgP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 351 PDFYVSINVASEDILSLEFLDFLETETRSHGLSAGQVALELTERSTASQDSLTQAM-AAFSRRGYRILIDDFGTGYSNLA 429
Cdd:smart00052 84 PPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATlQRLRELGVRIALDDFGTGYSSLS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 430 YIARMPIAGIKIDRMFTQALDQQAIGAVIVSKVCELAAVLEVTLICEGVETKGQADHLVAIYPDIcIQGFLIGRPMPARQ 509
Cdd:smart00052 164 YLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDY-GQGYLFSRPLPLDD 242
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
272-512 |
7.88e-40 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 153.30 E-value: 7.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 272 LERALNDDRLTVHYQPIVRLSdNRICGAEALARLVDFDGTLIPPDHFIPAAETCGFIGQITRSVVRRAFTDMAAHFAADP 351
Cdd:PRK10060 413 LRKALENDQLVIHYQPKITWR-GEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGI 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 352 DFYVSINVASEDILSLEFLDFLETETRSHGLSAGQVALELTERSTASQDSLTQA-MAAFSRRGYRILIDDFGTGYSNLAY 430
Cdd:PRK10060 492 NLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIENEELALSvIQQFSQLGAQVHLDDFGTGYSSLSQ 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 431 IARMPIAGIKIDRMFTQALDQQAIGAVIVSKVCELAAVLEVTLICEGVETKGQADHLVAIYPDIcIQGFLIGRPMPARQF 510
Cdd:PRK10060 572 LARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNE-RQGFLFAKPMPAVAF 650
|
..
gi 516723119 511 SR 512
Cdd:PRK10060 651 ER 652
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
275-514 |
7.00e-34 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 136.00 E-value: 7.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 275 ALNDDRLTVHYQPIVRLSDNRICGAEALARLVDFDGTLIPPDHFIPAAETCGFIGQITRSVVRRAFTDMAAHFAADPDFY 354
Cdd:PRK13561 408 ALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQERGIMLP 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 355 VSINVASEDILSLEFLDFLETETRSHGLSAGQVALELTErsTASQDSLTQAMAAFS---RRGYRILIDDFGTGYSNLAYI 431
Cdd:PRK13561 488 LSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTE--SRRIDDPHAAVAILRplrNAGVRVALDDFGMGYAGLRQL 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 432 ARM---PIAGIKIDRMFTQAL--DQQAIGAVIvskvcELAAVLEVTLICEGVETKGQADHLVAIYPDICiQGFLIGRPMP 506
Cdd:PRK13561 566 QHMkslPIDVLKIDKMFVDGLpeDDSMVAAII-----MLAQSLNLQVIAEGVETEAQRDWLLKAGVGIA-QGFLFARALP 639
|
....*...
gi 516723119 507 ARQFSRAF 514
Cdd:PRK13561 640 IEIFEERY 647
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
272-507 |
8.71e-31 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 127.19 E-value: 8.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 272 LERALNDDRLTVHYQPIVRLSDNRICGAEALARLVDFDGTLIPPDHFIPAAETCGFIGQITRSVVRRA------FTDMAA 345
Cdd:PRK11359 548 LKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEAcrqlaeWRSQNI 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 346 HFAAdpdfyVSINVASEDILSLEFLDFLETETRSHGLSAGQVALELTERSTAsqdSLTQAMAAFSRR----GYRILIDDF 421
Cdd:PRK11359 628 HIPA-----LSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMM---EHDTEIFKRIQIlrdmGVGLSVDDF 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 422 GTGYSNLAYIARMPIAGIKIDRMFTQALDQQAIGAVIVSKVCELAAVLEVTLICEGVETKGQADHLVAIYPDIcIQGFLI 501
Cdd:PRK11359 700 GTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRV-IQGYFF 778
|
....*.
gi 516723119 502 GRPMPA 507
Cdd:PRK11359 779 SRPLPA 784
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
258-520 |
2.72e-30 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 125.05 E-value: 2.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 258 HAHLYREgrswrQKLERALNDDRLTVHYQPIVRLSDNRICGAEALARLVDFDGTLIPPDHFIPAAETCGFIGQITRSVVR 337
Cdd:PRK11829 401 HKRLTQE-----NDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLE 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 338 RAFTDMAAHFAADPDFYVSINVASEDILSLEFLDFLETETRSHGLSAGQVALELTErsTASQDSLTQAMAAFSR---RGY 414
Cdd:PRK11829 476 EACRILADWKARGVSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITE--TAQIQDLDEALRLLRElqgLGL 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 415 RILIDDFGTGYSNLAYI---ARMPIAGIKIDRMFtqaLDQQAIGAVIVSKVCELAAVLEVTLICEGVETKGQADHLVA-- 489
Cdd:PRK11829 554 LIALDDFGIGYSSLRYLnhlKSLPIHMIKLDKSF---VKNLPEDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEhg 630
|
250 260 270
....*....|....*....|....*....|.
gi 516723119 490 IYpdiCIQGFLIGRPMPARQFSRAFPANHHA 520
Cdd:PRK11829 631 IQ---CGQGFLFSPPLPRAEFEAQYFSSAHH 658
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
283-515 |
2.55e-28 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 118.17 E-value: 2.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 283 VHYQPIVRLSDNRICGAEALARLVDFDGTLIPPDHFIPAAETCGFIGQITR---SVVRRAFTDMAAHFAADPDFyvSINV 359
Cdd:PRK10551 279 VEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQhlfELIARDAAELQKVLPVGAKL--GINI 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 360 ASEDILSLEFLD----FLETETRSHGlsagQVALELTERSTASQDSLTQAMAAFSRRGYRILIDDFGTGYSNLAYIARMP 435
Cdd:PRK10551 357 SPAHLHSDSFKAdvqrLLASLPADHF----QIVLEITERDMVQEEEATKLFAWLHSQGIEIAIDDFGTGHSALIYLERFT 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 436 IAGIKIDRMFTQALDQQAIGAVIVSKVCELAAVLEVTLICEGVETKGQA----DHLVAIypdicIQGFLIGRPMPARQFS 511
Cdd:PRK10551 433 LDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQArwlrERGVNF-----LQGYWISRPLPLEDFV 507
|
....
gi 516723119 512 RAFP 515
Cdd:PRK10551 508 RWLK 511
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
275-506 |
7.58e-24 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 106.30 E-value: 7.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 275 ALNDDRLTVHYQPIVRLSDNRICGAEALARLVDFDGTLIPPDHFIPAAETCGFIGQITRSVVRRAFTDMAAHFAAdPDFY 354
Cdd:PRK09776 849 IKENQLMMLAHGVASPRIPEARNHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFRQAAKAVAS-KGLS 927
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 355 VSINVASEDILSLEFLDFLETETRSHGLSAGQVALELTERSTASQDS-LTQAMAAFSRRGYRILIDDFGTGYSNLAYIAR 433
Cdd:PRK09776 928 IALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAEsASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKA 1007
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516723119 434 MPIAGIKIDRMFTQALDQQAIGAVIVSKVCELAAVLEVTLICEGVETKGQADHLVAIYPDIcIQGFLIGRPMP 506
Cdd:PRK09776 1008 FMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDL-AYGYAIARPQP 1079
|
|
| CSS-motif |
pfam12792 |
CSS motif domain associated with EAL; This family with its characteriztic highly conserved CSS ... |
37-233 |
2.07e-20 |
|
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: 89.51 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 37 EYVDYYGSDVFQNAVSVAETSLTVLRTLDRSDNAPCSAEDLEAMRGVVFAAPYLTDVGRLRDGYLVCTGIWGELATPVKM 116
Cdd:pfam12792 3 EQLDAFAERALRRLESVLDQADQALDRLLPLTGQPCSPAHLAELRRIVAFSPYVRDVGLVKNGRLYCSSLWGELDTPLPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 117 PPRSQVVGVNAAtLWKGARGIAPAGLAVDMSSFGNSVVMTAPTAFARYEDPAErLAALVLTSDASYSYQSFGDTEGLAP- 195
Cdd:pfam12792 83 LPPDLTTPPGVR-LWLLRGTPLVPGRPALVLRRGGYGVVIDPGVFIDVQYLPG-LLAAVSQPDGRLLALVVGDDALLFDg 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 516723119 196 ---LLGSNSD-WYRIAQRRVYSRCNDKIDVCVVATYDAPALL 233
Cdd:pfam12792 161 rlhSLAEPAPgTARSGGALYARARSTRYPLTVVVYAPRASLL 202
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
268-482 |
9.14e-10 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 61.03 E-value: 9.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 268 WRQKLERALNDDRLTVHYQPIVrLSDNRICGAEALARLVDFDGTLIPPDHFIPAAETCGFIGQITRSVVRRAFTDmaahF 347
Cdd:PRK11059 404 WRTLLEQTLVRGGPRLYQQPAV-TRDGKVHHRELFCRIRDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPL----L 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 348 AADPDFYVSINVASEDILSLEFLDFLETE----TRSHglsAGQVALELTERS-TASQDSLTQAMAAFSRRGYRILIDDFG 422
Cdd:PRK11059 479 RYWPEENLSINLSVDSLLSRAFQRWLRDTllqcPRSQ---RKRLIFELAEADvCQHISRLRPVLRMLRGLGCRLAVDQAG 555
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 423 TGYSNLAYIARMPIAGIKIDRMFTQALDQQAIGAVIVSKVCELAAVLEVTLICEGVETKG 482
Cdd:PRK11059 556 LTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFATGVESRE 615
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
357-520 |
8.07e-06 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 48.26 E-value: 8.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 357 INVaSEDILSLEFLDFLetetrshglSAGQVALELTERSTASQDsLTQAMAAFSRRGYRILIDDFGTGYSNLAYIARMPI 436
Cdd:COG3434 66 INF-TEELLLSDLPELL---------PPERVVLEILEDVEPDEE-LLEALKELKEKGYRIALDDFVLDPEWDPLLPLADI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 437 agIKIDrmfTQALDQQAIGAVIvskvcELAAVLEVTLICEGVETKGQADHLVAI---YpdicIQGFLIGRPMPARqfSRA 513
Cdd:COG3434 135 --IKID---VLALDLEELAELV-----ARLKRYGIKLLAEKVETREEFELCKELgfdL----FQGYFFSKPEILK--GKK 198
|
....*..
gi 516723119 514 FPANHHA 520
Cdd:COG3434 199 LPPSQLT 205
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
263-506 |
1.80e-05 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 46.53 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 263 REGRSWRQkLERALnddrltvHYQPIVRLSdNRICGAEALARLV--DFDGTLIPPDHF---IPAAETCGFIGQITRSVVR 337
Cdd:PRK11596 20 QERRYWLQ-CERAY-------TFQPIYRTS-GRLMAIELLTAVThpSNPSQRLSPERYfaeITVSHRLDVVKEQLDLLAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 338 RAFtdmaahFAADPDFYVSINVASEDILSLefldfletetRSHGLSAGQVA------LELTERSTASQDSLTQAMAAFSR 411
Cdd:PRK11596 91 WAD------FFVRHGLLASVNIDGPTLIAL----------RQQPAILRLIErlpwlrFELVEHIRLPKDSPFASMCEFGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516723119 412 rgyrILIDDFGTGYSNLAYIARMPIAGIKIDRMFTQALDQQAIGAVIVSKVCELAAVLEVTLICEGVETKgQADHLVAIY 491
Cdd:PRK11596 155 ----LWLDDFGTGMANFSALSEVRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETP-EEWRDVQRS 229
|
250
....*....|....*
gi 516723119 492 PDICIQGFLIGRPMP 506
Cdd:PRK11596 230 PAFAAQGYFLSRPAP 244
|
|
| |
