|
Name |
Accession |
Description |
Interval |
E-value |
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
7-527 |
0e+00 |
|
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: 683.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 7 HKALRLVGMGLVILLPVMLALWFAQLRAKAETIDQLHSFSQLALQKTEMVIREADQARFKASQYRGELCSAEHQRYLLHI 86
Cdd:COG4943 8 LLSLATLLALLAALLPLLLSLWLAQIQARRREREQLESYAQRALARAERVFDQARSALDELNALPGDPCSPAHLAALRRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 87 VRGLLYVEDLIYANGQRFICSTSAHPETGWRMPAANYTKKPDVAIYYYRDTPFYPGFAMNYMQKGPYVVVVNPYSFSSVI 166
Cdd:COG4943 88 VFSSRYVRDIGYVRDGRLLCSSLGKLSKPVPLPPPDYVTADGYRLWLNVDNPLDPGRPMLIVGRGNYVVVIDPAAFIDVL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 167 ASDRDLAYGVFDTKTNLFFSLSNNVEPAELQALIREGDAFFNQNGRVYTIARSAIRPIAVIMSTSRASYYHNFCDQASLT 246
Cdd:COG4943 168 SPQPGISLALLATNGGHLFASSGNPDPALLSRLLRGPSSWFIQGDRLYASACSPQYPICVVAAAPLAGLLALWRQLLLLL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 247 LPLGIICSILLVLVWTRTRRQYHSPRNMLQRALSCRQLRLHYQPIIDIKNNRCVGAEALLRWPGFDGPVMNPAEFIPLAE 326
Cdd:COG4943 248 LPLGLLLSLLLGLLVLRLLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 327 NEGMIAQITDYVVDELFYEMGEFLASHPQLYVAINLSASDFHSARLISQISEKAHSYAVCIGQIKIEVTERGFIDVAKTT 406
Cdd:COG4943 328 QSGLISPLTRQVIEQVFRDLGDLLAADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFIDPAKAR 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 407 PVIQAFREAGYEIAIDDFGTGYSNLHNLHALNVDILKIDKTFVDTLTTNNTSHLIAEHIIEMARGLRLKTIAEGVETPEQ 486
Cdd:COG4943 408 AVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQ 487
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 496082767 487 VSWLYKRGVQFCQGWLFAKAMPAREFMQWLANAPTPISRPQ 527
Cdd:COG4943 488 ADYLRARGVQYGQGWLFAKPLPAEEFIAWLAAQRAPASAPA 528
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
273-511 |
3.30e-92 |
|
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: 281.74 E-value: 3.30e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 273 NMLQRALSCRQLRLHYQPIIDIKNNRCVGAEALLRWPGFDGPVMNPAEFIPLAENEGMIAQITDYVVDELFYEMGEFLAS 352
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 353 HPQLYVAINLSASDFHSARLISQISEKAHSYAVCIGQIKIEVTERGFI-DVAKTTPVIQAFREAGYEIAIDDFGTGYSNL 431
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIdDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 432 HNLHALNVDILKIDKTFVDTLTTNNTSHLIAEHIIEMARGLRLKTIAEGVETPEQVSWLYKRGVQFCQGWLFAKAMPARE 511
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
273-511 |
4.76e-91 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 278.72 E-value: 4.76e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 273 NMLQRALSCRQLRLHYQPIIDIKNNRCVGAEALLRWPGFDGPVMNPAEFIPLAENEGMIAQITDYVVDELFYEMGEFLAS 352
Cdd:smart00052 2 RELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 353 HP-QLYVAINLSASDFHSARLISQISEKAHSYAVCIGQIKIEVTERGFIDVAKTT-PVIQAFREAGYEIAIDDFGTGYSN 430
Cdd:smart00052 82 GPpPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAvATLQRLRELGVRIALDDFGTGYSS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 431 LHNLHALNVDILKIDKTFVDTLTTNNTSHLIAEHIIEMARGLRLKTIAEGVETPEQVSWLYKRGVQFCQGWLFAKAMPAR 510
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLD 241
|
.
gi 496082767 511 E 511
Cdd:smart00052 242 D 242
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
272-506 |
1.13e-69 |
|
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: 223.35 E-value: 1.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 272 RNMLQRALSCRQLRLHYQPIIDIKNNRCVGAEALLRWPGFDGPVMNPAEFIPLAENEGMIAQITDYVVDELFYEMGEfLA 351
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQ-LQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 352 SHPQLYVAINLSASDFHSARLISQISEKAHSYAVCIGQIKIEVTERGFI-DVAKTTPVIQAFREAGYEIAIDDFGTGYSN 430
Cdd:pfam00563 80 LGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLaRLEALREVLKRLRALGIRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496082767 431 LHNLHALNVDILKIDKTFVDTLTTNNTSHLIAEHIIEMARGLRLKTIAEGVETPEQVSWLYKRGVQFCQGWLFAKA 506
Cdd:pfam00563 160 LSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
275-519 |
9.22e-52 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 186.84 E-value: 9.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 275 LQRALSCRQLRLHYQPIIDIKNNRCVGAEALLRWPGFDGPVMNPAEFIPLAENEGMIAQITDYVVDELFYEMGEFLASHP 354
Cdd:PRK13561 405 ILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQERGI 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 355 QLYVAINLSASDFHSARLISQISEKAHSYAVCIGQIKIEVTERGFIDVAKTTPVI-QAFREAGYEIAIDDFGTGYSNLHN 433
Cdd:PRK13561 485 MLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAIlRPLRNAGVRVALDDFGMGYAGLRQ 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 434 LH---ALNVDILKIDKTFVDTLTTNNTshlIAEHIIEMARGLRLKTIAEGVETPEQVSWLYKRGVQFCQGWLFAKAMPAR 510
Cdd:PRK13561 565 LQhmkSLPIDVLKIDKMFVDGLPEDDS---MVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIE 641
|
250
....*....|
gi 496082767 511 EF-MQWLANA 519
Cdd:PRK13561 642 IFeERYLEEK 651
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
7-527 |
0e+00 |
|
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: 683.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 7 HKALRLVGMGLVILLPVMLALWFAQLRAKAETIDQLHSFSQLALQKTEMVIREADQARFKASQYRGELCSAEHQRYLLHI 86
Cdd:COG4943 8 LLSLATLLALLAALLPLLLSLWLAQIQARRREREQLESYAQRALARAERVFDQARSALDELNALPGDPCSPAHLAALRRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 87 VRGLLYVEDLIYANGQRFICSTSAHPETGWRMPAANYTKKPDVAIYYYRDTPFYPGFAMNYMQKGPYVVVVNPYSFSSVI 166
Cdd:COG4943 88 VFSSRYVRDIGYVRDGRLLCSSLGKLSKPVPLPPPDYVTADGYRLWLNVDNPLDPGRPMLIVGRGNYVVVIDPAAFIDVL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 167 ASDRDLAYGVFDTKTNLFFSLSNNVEPAELQALIREGDAFFNQNGRVYTIARSAIRPIAVIMSTSRASYYHNFCDQASLT 246
Cdd:COG4943 168 SPQPGISLALLATNGGHLFASSGNPDPALLSRLLRGPSSWFIQGDRLYASACSPQYPICVVAAAPLAGLLALWRQLLLLL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 247 LPLGIICSILLVLVWTRTRRQYHSPRNMLQRALSCRQLRLHYQPIIDIKNNRCVGAEALLRWPGFDGPVMNPAEFIPLAE 326
Cdd:COG4943 248 LPLGLLLSLLLGLLVLRLLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 327 NEGMIAQITDYVVDELFYEMGEFLASHPQLYVAINLSASDFHSARLISQISEKAHSYAVCIGQIKIEVTERGFIDVAKTT 406
Cdd:COG4943 328 QSGLISPLTRQVIEQVFRDLGDLLAADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFIDPAKAR 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 407 PVIQAFREAGYEIAIDDFGTGYSNLHNLHALNVDILKIDKTFVDTLTTNNTSHLIAEHIIEMARGLRLKTIAEGVETPEQ 486
Cdd:COG4943 408 AVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQ 487
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 496082767 487 VSWLYKRGVQFCQGWLFAKAMPAREFMQWLANAPTPISRPQ 527
Cdd:COG4943 488 ADYLRARGVQYGQGWLFAKPLPAEEFIAWLAAQRAPASAPA 528
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
273-511 |
3.30e-92 |
|
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: 281.74 E-value: 3.30e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 273 NMLQRALSCRQLRLHYQPIIDIKNNRCVGAEALLRWPGFDGPVMNPAEFIPLAENEGMIAQITDYVVDELFYEMGEFLAS 352
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 353 HPQLYVAINLSASDFHSARLISQISEKAHSYAVCIGQIKIEVTERGFI-DVAKTTPVIQAFREAGYEIAIDDFGTGYSNL 431
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIdDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 432 HNLHALNVDILKIDKTFVDTLTTNNTSHLIAEHIIEMARGLRLKTIAEGVETPEQVSWLYKRGVQFCQGWLFAKAMPARE 511
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
273-511 |
4.76e-91 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 278.72 E-value: 4.76e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 273 NMLQRALSCRQLRLHYQPIIDIKNNRCVGAEALLRWPGFDGPVMNPAEFIPLAENEGMIAQITDYVVDELFYEMGEFLAS 352
Cdd:smart00052 2 RELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 353 HP-QLYVAINLSASDFHSARLISQISEKAHSYAVCIGQIKIEVTERGFIDVAKTT-PVIQAFREAGYEIAIDDFGTGYSN 430
Cdd:smart00052 82 GPpPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAvATLQRLRELGVRIALDDFGTGYSS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 431 LHNLHALNVDILKIDKTFVDTLTTNNTSHLIAEHIIEMARGLRLKTIAEGVETPEQVSWLYKRGVQFCQGWLFAKAMPAR 510
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLD 241
|
.
gi 496082767 511 E 511
Cdd:smart00052 242 D 242
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
273-520 |
1.93e-83 |
|
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: 272.80 E-value: 1.93e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 273 NMLQRALSCRQLRLHYQPIIDIKNNRCVGAEALLRW--PGFdGPVMnPAEFIPLAENEGMIAQITDYVVDELFYEMGEFL 350
Cdd:COG5001 428 ADLRRALERGELELHYQPQVDLATGRIVGAEALLRWqhPER-GLVS-PAEFIPLAEETGLIVPLGEWVLREACRQLAAWQ 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 351 AS-HPQLYVAINLSASDFHSARLISQISEKAHSYAVCIGQIKIEVTERGFI-DVAKTTPVIQAFREAGYEIAIDDFGTGY 428
Cdd:COG5001 506 DAgLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLeDPEEALETLRALRALGVRIALDDFGTGY 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 429 SNLHNLHALNVDILKIDKTFVDTLTTNNTSHLIAEHIIEMARGLRLKTIAEGVETPEQVSWLYKRGVQFCQGWLFAKAMP 508
Cdd:COG5001 586 SSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLP 665
|
250
....*....|..
gi 496082767 509 AREFMQWLANAP 520
Cdd:COG5001 666 AEELEALLRARA 677
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
272-517 |
1.03e-81 |
|
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: 265.88 E-value: 1.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 272 RNMLQRALSCRQLRLHYQPIIDIKNNRCVGAEALLRWPGFDGPVMNPAEFIPLAENEGMIAQITDYVVDELFYEMGEFLA 351
Cdd:COG2200 330 ESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 352 SHPQLYVAINLSASDFHSARLISQISEKAHSYAVCIGQIKIEVTERGFI-DVAKTTPVIQAFREAGYEIAIDDFGTGYSN 430
Cdd:COG2200 410 RGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLeDLEAAIELLARLRALGVRIALDDFGTGYSS 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 431 LHNLHALNVDILKIDKTFVDTLTTNNTSHLIAEHIIEMARGLRLKTIAEGVETPEQVSWLYKRGVQFCQGWLFAKAMPAR 510
Cdd:COG2200 490 LSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLE 569
|
....*..
gi 496082767 511 EFMQWLA 517
Cdd:COG2200 570 ELEALLR 576
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
272-506 |
1.13e-69 |
|
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: 223.35 E-value: 1.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 272 RNMLQRALSCRQLRLHYQPIIDIKNNRCVGAEALLRWPGFDGPVMNPAEFIPLAENEGMIAQITDYVVDELFYEMGEfLA 351
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQ-LQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 352 SHPQLYVAINLSASDFHSARLISQISEKAHSYAVCIGQIKIEVTERGFI-DVAKTTPVIQAFREAGYEIAIDDFGTGYSN 430
Cdd:pfam00563 80 LGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLaRLEALREVLKRLRALGIRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496082767 431 LHNLHALNVDILKIDKTFVDTLTTNNTSHLIAEHIIEMARGLRLKTIAEGVETPEQVSWLYKRGVQFCQGWLFAKA 506
Cdd:pfam00563 160 LSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
275-519 |
9.22e-52 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 186.84 E-value: 9.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 275 LQRALSCRQLRLHYQPIIDIKNNRCVGAEALLRWPGFDGPVMNPAEFIPLAENEGMIAQITDYVVDELFYEMGEFLASHP 354
Cdd:PRK13561 405 ILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQERGI 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 355 QLYVAINLSASDFHSARLISQISEKAHSYAVCIGQIKIEVTERGFIDVAKTTPVI-QAFREAGYEIAIDDFGTGYSNLHN 433
Cdd:PRK13561 485 MLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAIlRPLRNAGVRVALDDFGMGYAGLRQ 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 434 LH---ALNVDILKIDKTFVDTLTTNNTshlIAEHIIEMARGLRLKTIAEGVETPEQVSWLYKRGVQFCQGWLFAKAMPAR 510
Cdd:PRK13561 565 LQhmkSLPIDVLKIDKMFVDGLPEDDS---MVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIE 641
|
250
....*....|
gi 496082767 511 EF-MQWLANA 519
Cdd:PRK13561 642 IFeERYLEEK 651
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
275-518 |
5.51e-47 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 173.71 E-value: 5.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 275 LQRALSCRQLRLHYQPIIDIkNNRCVGAEALLRWPGFDGPVMNPAEFIPLAENEGMIAQITDYVVDELFYEMGEFLASHP 354
Cdd:PRK10060 413 LRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGI 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 355 QLYVAINLSASDFHSARLISQISEKAHSYAVCIGQIKIEVTERGFI-DVAKTTPVIQAFREAGYEIAIDDFGTGYSNLHN 433
Cdd:PRK10060 492 NLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIeNEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQ 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 434 LHALNVDILKIDKTFVDTLTTNNTSHLIAEHIIEMARGLRLKTIAEGVETPEQVSWLYKRGVQFCQGWLFAKAMPAREFM 513
Cdd:PRK10060 572 LARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFE 651
|
....*
gi 496082767 514 QWLAN 518
Cdd:PRK10060 652 RWYKR 656
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
245-522 |
1.95e-46 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 169.79 E-value: 1.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 245 LTLPLGIICSIL--LVLVWTRTRRQyhSPRNMLQRALSCRQLRLHYQPIIDIKNNRCVGAEALLRW--PgFDGPVmNPAE 320
Cdd:PRK10551 238 YALLLGLLSGILvgLLCYYLLSLRM--RPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWrhP-TAGEI-PPDA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 321 FIPLAENEGMIAQITDYVVdELFYEMGEFLASH--PQLYVAINLSASDFHSARLISQISEKAHSYAVCIGQIKIEVTERG 398
Cdd:PRK10551 314 FINYAEAQKLIVPLTQHLF-ELIARDAAELQKVlpVGAKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERD 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 399 FIDVAKTTPVIQAFREAGYEIAIDDFGTGYSNLHNLHALNVDILKIDKTFVDTLTTNNTSHLIAEHIIEMARGLRLKTIA 478
Cdd:PRK10551 393 MVQEEEATKLFAWLHSQGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVA 472
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 496082767 479 EGVETPEQVSWLYKRGVQFCQGWLFAKAMPAREFMQWLANAPTP 522
Cdd:PRK10551 473 EGVETPEQARWLRERGVNFLQGYWISRPLPLEDFVRWLKEPYTP 516
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
273-521 |
1.07e-44 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 167.43 E-value: 1.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 273 NMLQRALSCRQLRLHYQPIIDIKNNRCVGAEALLRWPGFDGPVMNPAEFIPLAENEGMIAQITDYVVDELFYEMGEFLAS 352
Cdd:PRK11829 408 NDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKAR 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 353 HPQLYVAINLSASDFHSARLISQISEKAHSYAVCIGQIKIEVTERGFI-DVAKTTPVIQAFREAGYEIAIDDFGTGYSNL 431
Cdd:PRK11829 488 GVSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIqDLDEALRLLRELQGLGLLIALDDFGIGYSSL 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 432 H---NLHALNVDILKIDKTFVDTLTTNNTshlIAEHIIEMARGLRLKTIAEGVETPEQVSWLYKRGVQFCQGWLFAKAMP 508
Cdd:PRK11829 568 RylnHLKSLPIHMIKLDKSFVKNLPEDDA---IARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLP 644
|
250
....*....|...
gi 496082767 509 AREFmqwLANAPT 521
Cdd:PRK11829 645 RAEF---EAQYFS 654
|
|
| CSS-motif |
pfam12792 |
CSS motif domain associated with EAL; This family with its characteriztic highly conserved CSS ... |
38-243 |
3.99e-43 |
|
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: 152.68 E-value: 3.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 38 TIDQLHSFSQLALQKTEMVIREADQARFKASQYRGELCSAEHQRYLLHIVRGLLYVEDLIYANGQRFICSTSAHP-ETGW 116
Cdd:pfam12792 1 EQEQLDAFAERALRRLESVLDQADQALDRLLPLTGQPCSPAHLAELRRIVAFSPYVRDVGLVKNGRLYCSSLWGElDTPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 117 RMPAANYTKKPDVAIYYYRDTPFYPGFAMNYMQKGPYVVVVNPYSFSSVIaSDRDLAYGVFDTKTNLFFSLSNN---VEP 193
Cdd:pfam12792 81 PLLPPDLTTPPGVRLWLLRGTPLVPGRPALVLRRGGYGVVIDPGVFIDVQ-YLPGLLAAVSQPDGRLLALVVGDdalLFD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496082767 194 AELQALIREGDAFFNQNGRVYTIARSAIRPIAVIMSTSRASYYHNFCDQA 243
Cdd:pfam12792 160 GRLHSLAEPAPGTARSGGALYARARSTRYPLTVVVYAPRASLLANWRQLL 209
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
275-519 |
4.02e-43 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 164.17 E-value: 4.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 275 LQRALSCRQLRLHYQPIIDIKNNRCVGAEALLRWPGFDGPVMNPAEFIPLAENEGMIAQITDYVVDELFYEMGEFLASHP 354
Cdd:PRK11359 548 LKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNI 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 355 QL-YVAINLSASDFHSARLISQISEKAHSYAVCIGQIKIEVTERGFIDV-AKTTPVIQAFREAGYEIAIDDFGTGYSNLH 432
Cdd:PRK11359 628 HIpALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHdTEIFKRIQILRDMGVGLSVDDFGTGFSGLS 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 433 NLHALNVDILKIDKTFVDTLTTNNTSHLIAEHIIEMARGLRLKTIAEGVETPEQVSWLYKRGVQFCQGWLFAKAMPAREF 512
Cdd:PRK11359 708 RLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEI 787
|
....*..
gi 496082767 513 MQWLANA 519
Cdd:PRK11359 788 PGWMSSV 794
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
258-519 |
2.76e-20 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 95.12 E-value: 2.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 258 VLVWTRTRRQYHSPRNMLQRALSCR-----QLRLHYQPIIDIKNNRCVGA-EALLRWPGFDGPVMNPAEFIPLAENEGMI 331
Cdd:PRK09776 823 VTVYEPQQAAAHSEHRALSLAEQWRmikenQLMMLAHGVASPRIPEARNHwLISLRLWDPEGEIIDEGAFRPAAEDPALM 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 332 AQITDYVVDELFYEMGEFLAShPQLYVAINLSASDFHSARLISQISEKAHSYAVCIGQIKIEVTERGFI-DVAKTTPVIQ 410
Cdd:PRK09776 903 HALDRRVIHEFFRQAAKAVAS-KGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLnHAESASRLVQ 981
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 411 AFREAGYEIAIDDFGTGYSNLHNLHALNVDILKIDKTFVDTLTTNNTSHLIAEHIIEMARGLRLKTIAEGVETPEQVSWL 490
Cdd:PRK09776 982 KLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTL 1061
|
250 260
....*....|....*....|....*....
gi 496082767 491 YKRGVQFCQGWLFAKAMPAREFMQWLANA 519
Cdd:PRK09776 1062 SGIGVDLAYGYAIARPQPLDLLLNSSYFA 1090
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
289-505 |
2.39e-11 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 65.59 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 289 QPIIDiKNNRCVGAEALLRwpgfdgpvMNPAEFIPLAENEgmiaQITDYVVDELFYEMG--EFLASHPqlyVAINLSASD 366
Cdd:COG3434 9 QPILD-RDQRVVGYELLFR--------SGLENSAPDVDGD----QATARVLLNAFLEIGldRLLGGKL---AFINFTEEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 367 FHSaRLISQISEKahsyavcigQIKIEVTERGFIDvAKTTPVIQAFREAGYEIAIDDFgTGYSNLHNLHALnVDILKIDk 446
Cdd:COG3434 73 LLS-DLPELLPPE---------RVVLEILEDVEPD-EELLEALKELKEKGYRIALDDF-VLDPEWDPLLPL-ADIIKID- 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496082767 447 tfvdtltTNNTSHLIAEHIIEMARGLRLKTIAEGVETPEQVSWLYKRGVQFCQGWLFAK 505
Cdd:COG3434 139 -------VLALDLEELAELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSK 190
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
272-504 |
1.10e-03 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 41.77 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 272 RNMLQRALSCRQLRLHYQPIIDIKNN---RCV------GAEALLRwpgfdgpvmnpAE-FIPLAENEGMIAQITDYVVDE 341
Cdd:PRK11059 405 RTLLEQTLVRGGPRLYQQPAVTRDGKvhhRELfcrirdGQGELLS-----------AElFMPMVQQLGLSEQYDRQVIER 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 342 LFYemgeFLASHPQLYVAINLSASDFHSARLISQI------SEKAHSyavciGQIKIEVTERgfiDV----AKTTPVIQA 411
Cdd:PRK11059 474 VLP----LLRYWPEENLSINLSVDSLLSRAFQRWLrdtllqCPRSQR-----KRLIFELAEA---DVcqhiSRLRPVLRM 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082767 412 FREAGYEIAIDDFG-----TGYsnlhnLHALNVDILKIDKTFVDTLTTNNTSHLIAEHIIEMARGLRLKTIAEGVETPEQ 486
Cdd:PRK11059 542 LRGLGCRLAVDQAGltvvsTSY-----IKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFATGVESREE 616
|
250
....*....|....*...
gi 496082767 487 VSWLYKRGVQFCQGWLFA 504
Cdd:PRK11059 617 WQTLQELGVSGGQGDFFA 634
|
|
| |
