|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
1-611 |
6.69e-178 |
|
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: 520.10 E-value: 6.69e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 1 MILAAIVLVALRLHEVAERHLEEEALRTARGWALQVGRVVPQPASLFGPAPAPRALLPLAGLRGTTAVYAFRLHAPDGRV 80
Cdd:COG5001 54 LLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAAS 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 81 TLASEGLPAAPAALATARVLDLVTGRSTHVVELQRQPDTRSAVHADVWLPVQGDGVLLGVAQVRVDLDESAAVTTRSAVR 160
Cdd:COG5001 134 AALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 161 AASATFAGLLGVGLAGLLLWRAYARAERSARARIDYLDQHDPLTGALNRESF---VAALRRAAARRAGHSAVLCMDLDRF 237
Cdd:COG5001 214 LGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFldrLEQALARARRSGRRLALLFIDLDRF 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 238 REFNEWLGRGAGDSLLRQVAARLRATVRSGDLVARLGSDEFAV-LADTGDAEALATLAQRIVEALRQPYDVGGRRCEIGA 316
Cdd:COG5001 294 KEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVlLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 317 SIGIALHGVDSREADRLLQQADLALARAKADGRGTFRFYDARLDDELQRRRRLGAELRDALAADALVLHFQPLMDAASGR 396
Cdd:COG5001 374 SIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGR 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 397 IVGYEALARWPHAERGWVPPASFIPLAEQTGLIEDLGAWVLRAACREAARWPA----PLSVAVNLSPAQFrRDGGIAEVV 472
Cdd:COG5001 454 IVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDaglpDLRVAVNLSARQL-RDPDLVDRV 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 473 AEALRDSGLAPERLELEITESLLMARTEPVLRALRELRGLGVSIAMDDFGTGYSSLAHLWRFPLDRVKLDREFTHSLADD 552
Cdd:COG5001 533 RRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAED 612
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 332111392 553 AKVGVIVGSVVSMAHALGMHVTAEGVETEAQRQALAAHGCDVLQGFLLGRPQPADRLPH 611
Cdd:COG5001 613 PDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEA 671
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
371-608 |
1.61e-104 |
|
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: 316.02 E-value: 1.61e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 371 AELRDALAADALVLHFQPLMDAASGRIVGYEALARWPHAERGWVPPASFIPLAEQTGLIEDLGAWVLRAACREAARWPA- 449
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 450 --PLSVAVNLSPAQFRRDGGIaEVVAEALRDSGLAPERLELEITESLLMARTEPVLRALRELRGLGVSIAMDDFGTGYSS 527
Cdd:cd01948 81 gpDLRLSVNLSARQLRDPDFL-DRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 528 LAHLWRFPLDRVKLDREFTHSLADDAKVGVIVGSVVSMAHALGMHVTAEGVETEAQRQALAAHGCDVLQGFLLGRPQPAD 607
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239
|
.
gi 332111392 608 R 608
Cdd:cd01948 240 E 240
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
201-616 |
3.75e-97 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 311.23 E-value: 3.75e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 201 DPLTGALNRESFVAALRRAAARRAGHS-AVLCMDLDRFREFNEWLGRGAGDSLLRQVAARLRATVRSGDLVARLGSDEFA 279
Cdd:PRK10060 240 DSITGLPNRNAIQELIDHAINAADNNQvGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 280 VLADTGDAEALATLAQRIVEALRQPYDVGGRRCEIGASIGIAL---HGvDSREAdrLLQQADLALARAKADGRGTFRFYD 356
Cdd:PRK10060 320 VLASHTSQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALapeHG-DDSES--LIRSADTAMYTAKEGGRGQFCVFS 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 357 ARLDDELQRRRRLGAELRDALAADALVLHFQPLMDAaSGRIVGYEALARWPHAERGWVPPASFIPLAEQTGLIEDLGAWV 436
Cdd:PRK10060 397 PEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWV 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 437 LRAACREAARWPAP---LSVAVNLSPAQFRrDGGIAEVVAEALRDSGLAPERLELEITESLLMARTEPVLRALRELRGLG 513
Cdd:PRK10060 476 MLDVVRQVAKWRDKginLRVAVNVSARQLA-DQTIFTALKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLG 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 514 VSIAMDDFGTGYSSLAHLWRFPLDRVKLDREFTHSLADDAKVGVIVGSVVSMAHALGMHVTAEGVETEAQRQALAAHGCD 593
Cdd:PRK10060 555 AQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVN 634
|
410 420
....*....|....*....|...
gi 332111392 594 VLQGFLLGRPQPADRLPHQSADT 616
Cdd:PRK10060 635 ERQGFLFAKPMPAVAFERWYKRY 657
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
372-607 |
9.82e-89 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 275.25 E-value: 9.82e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 372 ELRDALAADALVLHFQPLMDAASGRIVGYEALARWPHAERGWVPPASFIPLAEQTGLIEDLGAWVLRAACREAARWPA-- 449
Cdd:smart00052 3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAqg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 450 --PLSVAVNLSPAQFRRDGGIAEVVaEALRDSGLAPERLELEITESLLMARTEPVLRALRELRGLGVSIAMDDFGTGYSS 527
Cdd:smart00052 83 ppPLLISINLSARQLISPDLVPRVL-ELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 528 LAHLWRFPLDRVKLDREFTHSLADDAKVGVIVGSVVSMAHALGMHVTAEGVETEAQRQALAAHGCDVLQGFLLGRPQPAD 607
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLD 241
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
371-603 |
2.09e-76 |
|
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: 242.99 E-value: 2.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 371 AELRDALAADALVLHFQPLMDAASGRIVGYEALARWPHAERGWVPPASFIPLAEQTGLIEDLGAWVLRAACREAARW--P 448
Cdd:pfam00563 2 RALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLqlG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 449 APLSVAVNLSPAQFRrDGGIAEVVAEALRDSGLAPERLELEITESLLMARTEPVLRALRELRGLGVSIAMDDFGTGYSSL 528
Cdd:pfam00563 82 PDIKLSINLSPASLA-DPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332111392 529 AHLWRFPLDRVKLDREFTHSLADDAKVGVIVGSVVSMAHALGMHVTAEGVETEAQRQALAAHGCDVLQGFLLGRP 603
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
199-356 |
2.12e-24 |
|
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]
Pssm-ID: 272984 [Multi-domain] Cd Length: 165 Bit Score: 100.10 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 199 QHDPLTGALNRESFVAALRRAAARRAGHS---AVLCMDLDRFREFNEWLGRGAGDSLLRQVAARLRATVRSGDLVARLGS 275
Cdd:TIGR00254 3 VRDPLTGLYNRRYLEEMLDSELKRARRFQrsfSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 276 DEFAVLADTGDAEALATLAQRIVEALRQ-PYDVGGR-RCEIGASIGIALHGVDSREADRLLQQADLALARAKADGRGTFR 353
Cdd:TIGR00254 83 EEFVVILPGTPLEDALSKAERLRDAINSkPIEVAGSeTLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNRVV 162
|
...
gi 332111392 354 FYD 356
Cdd:TIGR00254 163 VAD 165
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
1-611 |
6.69e-178 |
|
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: 520.10 E-value: 6.69e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 1 MILAAIVLVALRLHEVAERHLEEEALRTARGWALQVGRVVPQPASLFGPAPAPRALLPLAGLRGTTAVYAFRLHAPDGRV 80
Cdd:COG5001 54 LLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAAS 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 81 TLASEGLPAAPAALATARVLDLVTGRSTHVVELQRQPDTRSAVHADVWLPVQGDGVLLGVAQVRVDLDESAAVTTRSAVR 160
Cdd:COG5001 134 AALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 161 AASATFAGLLGVGLAGLLLWRAYARAERSARARIDYLDQHDPLTGALNRESF---VAALRRAAARRAGHSAVLCMDLDRF 237
Cdd:COG5001 214 LGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFldrLEQALARARRSGRRLALLFIDLDRF 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 238 REFNEWLGRGAGDSLLRQVAARLRATVRSGDLVARLGSDEFAV-LADTGDAEALATLAQRIVEALRQPYDVGGRRCEIGA 316
Cdd:COG5001 294 KEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVlLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 317 SIGIALHGVDSREADRLLQQADLALARAKADGRGTFRFYDARLDDELQRRRRLGAELRDALAADALVLHFQPLMDAASGR 396
Cdd:COG5001 374 SIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGR 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 397 IVGYEALARWPHAERGWVPPASFIPLAEQTGLIEDLGAWVLRAACREAARWPA----PLSVAVNLSPAQFrRDGGIAEVV 472
Cdd:COG5001 454 IVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDaglpDLRVAVNLSARQL-RDPDLVDRV 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 473 AEALRDSGLAPERLELEITESLLMARTEPVLRALRELRGLGVSIAMDDFGTGYSSLAHLWRFPLDRVKLDREFTHSLADD 552
Cdd:COG5001 533 RRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAED 612
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 332111392 553 AKVGVIVGSVVSMAHALGMHVTAEGVETEAQRQALAAHGCDVLQGFLLGRPQPADRLPH 611
Cdd:COG5001 613 PDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEA 671
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
371-608 |
1.61e-104 |
|
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: 316.02 E-value: 1.61e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 371 AELRDALAADALVLHFQPLMDAASGRIVGYEALARWPHAERGWVPPASFIPLAEQTGLIEDLGAWVLRAACREAARWPA- 449
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 450 --PLSVAVNLSPAQFRRDGGIaEVVAEALRDSGLAPERLELEITESLLMARTEPVLRALRELRGLGVSIAMDDFGTGYSS 527
Cdd:cd01948 81 gpDLRLSVNLSARQLRDPDFL-DRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 528 LAHLWRFPLDRVKLDREFTHSLADDAKVGVIVGSVVSMAHALGMHVTAEGVETEAQRQALAAHGCDVLQGFLLGRPQPAD 607
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239
|
.
gi 332111392 608 R 608
Cdd:cd01948 240 E 240
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
201-616 |
3.75e-97 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 311.23 E-value: 3.75e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 201 DPLTGALNRESFVAALRRAAARRAGHS-AVLCMDLDRFREFNEWLGRGAGDSLLRQVAARLRATVRSGDLVARLGSDEFA 279
Cdd:PRK10060 240 DSITGLPNRNAIQELIDHAINAADNNQvGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 280 VLADTGDAEALATLAQRIVEALRQPYDVGGRRCEIGASIGIAL---HGvDSREAdrLLQQADLALARAKADGRGTFRFYD 356
Cdd:PRK10060 320 VLASHTSQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALapeHG-DDSES--LIRSADTAMYTAKEGGRGQFCVFS 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 357 ARLDDELQRRRRLGAELRDALAADALVLHFQPLMDAaSGRIVGYEALARWPHAERGWVPPASFIPLAEQTGLIEDLGAWV 436
Cdd:PRK10060 397 PEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWV 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 437 LRAACREAARWPAP---LSVAVNLSPAQFRrDGGIAEVVAEALRDSGLAPERLELEITESLLMARTEPVLRALRELRGLG 513
Cdd:PRK10060 476 MLDVVRQVAKWRDKginLRVAVNVSARQLA-DQTIFTALKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLG 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 514 VSIAMDDFGTGYSSLAHLWRFPLDRVKLDREFTHSLADDAKVGVIVGSVVSMAHALGMHVTAEGVETEAQRQALAAHGCD 593
Cdd:PRK10060 555 AQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVN 634
|
410 420
....*....|....*....|...
gi 332111392 594 VLQGFLLGRPQPADRLPHQSADT 616
Cdd:PRK10060 635 ERQGFLFAKPMPAVAFERWYKRY 657
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
70-611 |
8.42e-96 |
|
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: 305.17 E-value: 8.42e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 70 AFRLHAPDGRVTLASEGLPAAPAALATARVLDLVTGRSTHVVELQRQPDTRSAVHADVWLPVQGDGVLLGVAQVRVDLDE 149
Cdd:COG2200 29 LLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 150 SAAVTTRSAVRAASATFAGLLGVGLAGLLLWRAYARAERSARARIDYLDQHDPLTGALNRESFVAALRRAAARRAGHSAV 229
Cdd:COG2200 109 ALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLRRLLLLLLLLLLLLLLALALLALL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 230 LCMDLDRFREFNEWLGRGAGDSLLRQVAARLRATVRSGDLVARLGSDE--FAVLADTGDAEALATLAQRIVEALRQPYDV 307
Cdd:COG2200 189 LLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGgfLLLLLLLAAAAAAAAALRLLLLLLLEPLLL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 308 GGRRCEIGASIGIALHGVDSREADRLLQQADLALARAKADGRGTFRFYDARlDDELQRRRRLGAELRDALAADALVLHFQ 387
Cdd:COG2200 269 GGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAA-EARARRRLALESELREALEEGELRLYYQ 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 388 PLMDAASGRIVGYEALARWPHAERGWVPPASFIPLAEQTGLIEDLGAWVLRAACREAARWPA---PLSVAVNLSPAQFRr 464
Cdd:COG2200 348 PIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPErglDLRLSVNLSARSLL- 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 465 DGGIAEVVAEALRDSGLAPERLELEITESLLMARTEPVLRALRELRGLGVSIAMDDFGTGYSSLAHLWRFPLDRVKLDRE 544
Cdd:COG2200 427 DPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRS 506
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332111392 545 FTHSLADDAKVGVIVGSVVSMAHALGMHVTAEGVETEAQRQALAAHGCDVLQGFLLGRPQPADRLPH 611
Cdd:COG2200 507 FVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEA 573
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
194-610 |
5.44e-92 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 300.92 E-value: 5.44e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 194 IDYLDQHDPLTGALNReSFVAALRRAAARRAGHSAVLCMDLDRFREFNEWLGRGAGDSLLRQVAARLRATVRSGDLVARL 273
Cdd:PRK11359 372 IEQLIQFDPLTGLPNR-NNLHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRI 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 274 GSDEFAVLADTGDAEALATLAQRIVEALRQPYDVGGRRCEIGASIGIALHGvdSREADRLLQQADLALARAKADGRGTFR 353
Cdd:PRK11359 451 EGTQFVLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISYDV--GKNRDYLLSTAHNAMDYIRKNGGNGWQ 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 354 FYDARLDDELQRRRRLGAELRDALAADALVLHFQPLMDAASGRIVGYEALARWPHAERGWVPPASFIPLAEQTGLIEDLG 433
Cdd:PRK11359 529 FFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIG 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 434 AWVLRAACREAARW-------PAplsVAVNLSPAQFRRDGgIAEVVAEALRDSGLAPERLELEITESLLMARTEPVLRAL 506
Cdd:PRK11359 609 RWVIAEACRQLAEWrsqnihiPA---LSVNLSALHFRSNQ-LPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKRI 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 507 RELRGLGVSIAMDDFGTGYSSLAHLWRFPLDRVKLDREFTHSLADDAKVGVIVGSVVSMAHALGMHVTAEGVETEAQRQA 586
Cdd:PRK11359 685 QILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEM 764
|
410 420
....*....|....*....|....
gi 332111392 587 LAAHGCDVLQGFLLGRPQPADRLP 610
Cdd:PRK11359 765 LRKIHCRVIQGYFFSRPLPAEEIP 788
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
372-607 |
9.82e-89 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 275.25 E-value: 9.82e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 372 ELRDALAADALVLHFQPLMDAASGRIVGYEALARWPHAERGWVPPASFIPLAEQTGLIEDLGAWVLRAACREAARWPA-- 449
Cdd:smart00052 3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAqg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 450 --PLSVAVNLSPAQFRRDGGIAEVVaEALRDSGLAPERLELEITESLLMARTEPVLRALRELRGLGVSIAMDDFGTGYSS 527
Cdd:smart00052 83 ppPLLISINLSARQLISPDLVPRVL-ELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 528 LAHLWRFPLDRVKLDREFTHSLADDAKVGVIVGSVVSMAHALGMHVTAEGVETEAQRQALAAHGCDVLQGFLLGRPQPAD 607
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLD 241
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
371-603 |
2.09e-76 |
|
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: 242.99 E-value: 2.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 371 AELRDALAADALVLHFQPLMDAASGRIVGYEALARWPHAERGWVPPASFIPLAEQTGLIEDLGAWVLRAACREAARW--P 448
Cdd:pfam00563 2 RALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLqlG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 449 APLSVAVNLSPAQFRrDGGIAEVVAEALRDSGLAPERLELEITESLLMARTEPVLRALRELRGLGVSIAMDDFGTGYSSL 528
Cdd:pfam00563 82 PDIKLSINLSPASLA-DPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332111392 529 AHLWRFPLDRVKLDREFTHSLADDAKVGVIVGSVVSMAHALGMHVTAEGVETEAQRQALAAHGCDVLQGFLLGRP 603
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
363-610 |
1.32e-70 |
|
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: 237.51 E-value: 1.32e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 363 LQRRRRLGAELRDALAADALVLHFQPLMDAASGRIVGYEALARWPHAERGWVPPASFIPLAEQTGLIEDLGAWVLRAACR 442
Cdd:COG4943 266 LRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 443 EAARWPA---PLSVAVNLSPAQFRrDGGIAEVVAEALRDSGLAPERLELEITES--LLMARTEPVLRALRELrglGVSIA 517
Cdd:COG4943 346 DLGDLLAadpDFHISINLSASDLL-SPRFLDDLERLLARTGVAPQQIVLEITERgfIDPAKARAVIAALREA---GHRIA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 518 MDDFGTGYSSLAHLWRFPLDRVKLDREFTHSLADDAKVGVIVGSVVSMAHALGMHVTAEGVETEAQRQALAAHGCDVLQG 597
Cdd:COG4943 422 IDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQG 501
|
250
....*....|...
gi 332111392 598 FLLGRPQPADRLP 610
Cdd:COG4943 502 WLFAKPLPAEEFI 514
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
250-607 |
1.22e-63 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 221.51 E-value: 1.22e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 250 DSLLRQVAARLRATVRSGDLVARLGSDEFAVLADTGDAEALA-TLAQRIVEALRQPYDVGGRRCEIGASIGIAL-HGVDS 327
Cdd:PRK13561 282 EILLLTLVEKLKSVLSPRMVLAQISGYDFAIIANGVKEPWHAiTLGQQVLTIINERLPIQRIQLRPSCSIGIAMfYGDLT 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 328 reADRLLQQADLALARAKADGRGTFRFYDARLDDELQRRRRLGAELRDALAADALVLHFQPLMDAASGRIVGYEALARWP 407
Cdd:PRK13561 362 --AEQLYSRAISAAFTARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 408 HAERGWVPPASFIPLAEQTGLIEDLGAWVLRAACREAARWPA-----PLSvaVNLSPAQFRRDGGIAEVVaEALRDSGLA 482
Cdd:PRK13561 440 QPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQErgimlPLS--VNLSALQLMHPNMVADML-ELLTRYRIQ 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 483 PERLELEITESLLMARTEPVLRALRELRGLGVSIAMDDFGTGYSSLAHLWRF---PLDRVKLDREFTHSLADDAkvgVIV 559
Cdd:PRK13561 517 PGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMkslPIDVLKIDKMFVDGLPEDD---SMV 593
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 332111392 560 GSVVSMAHALGMHVTAEGVETEAQRQALAAHGCDVLQGFLLGRPQPAD 607
Cdd:PRK13561 594 AAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIE 641
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
200-613 |
5.65e-61 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 219.54 E-value: 5.65e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 200 HDPLTGALNRESFVAA--LRRAAARRAGHSAVLC-MDLDRFREFNEWLGRGAGDSLLRQVAARLRATVRSGDLVARLGSD 276
Cdd:PRK09776 667 HDALTHLANRASFEKQlrRLLQTVNSTHQRHALVfIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGD 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 277 EFAVLADTGDAEALATLAQRIVEALRQ---PYDvgGRRCEIGASIGIALHGVDSREADRLLQQADLALARAKADGRGTFR 353
Cdd:PRK09776 747 EFGLLLPDCNVESARFIATRIISAINDyhfPWE--GRVYRVGASAGITLIDANNHQASEVMSQADIACYAAKNAGRGRVT 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 354 FYDARlDDELQRRRR---LGAELRDALAADALvlhfqplmdaasgRIVGYEALARWPHAERGW-------------VPPA 417
Cdd:PRK09776 825 VYEPQ-QAAAHSEHRalsLAEQWRMIKENQLM-------------MLAHGVASPRIPEARNHWlislrlwdpegeiIDEG 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 418 SFIPLAEQTGLIEDLGAWVLRAACRE-AARWPAP-LSVAVNLSPAQFRRDGGIAEVVAEaLRDSGLAPERLELEITESLL 495
Cdd:PRK09776 891 AFRPAAEDPALMHALDRRVIHEFFRQaAKAVASKgLSIALPLSVAGLSSPTLLPFLLEQ-LENSPLPPRLLHLEITETAL 969
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 496 MARTEPVLRALRELRGLGVSIAMDDFGTGYSSLAHLWRFPLDRVKLDREFTHSLADDAKVGVIVGSVVSMAHALGMHVTA 575
Cdd:PRK09776 970 LNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIA 1049
|
410 420 430
....*....|....*....|....*....|....*...
gi 332111392 576 EGVETEAQRQALAAHGCDVLQGFLLGRPQPADRLPHQS 613
Cdd:PRK09776 1050 GPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLLLNSS 1087
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
202-605 |
4.35e-60 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 212.11 E-value: 4.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 202 PLTGALNRESFVAALRRAAARRAGHSA--VLCMDLDRFREFNEWLGRGAGDSLLRQVAARLRATVRSGDLVARLGSDEFA 279
Cdd:PRK11829 236 PVTELPNRSLFISLLEKEIASSTRTDHfhLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 280 VLA-DTGDAEALATLAQRIVEALRQPYDVGGRRCEIGASIGIALHGVDSREADRLLQQADLALARAKADGRGTFRFYDAR 358
Cdd:PRK11829 316 VLArGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQIMVFEPH 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 359 LDDELQRRRRLGAELRDALAADALVLHFQPLMDAASGRIVGYEALARWPHAERGWVPPASFIPLAEQTGLIEDLGAWVLR 438
Cdd:PRK11829 396 LIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLE 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 439 AACREAARWPA-----PLSvaVNLSPAQFrRDGGIAEVVAEALRDSGLAPERLELEITESLLMARTEPVLRALRELRGLG 513
Cdd:PRK11829 476 EACRILADWKArgvslPLS--VNISGLQV-QNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLG 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 514 VSIAMDDFGTGYSS---LAHLWRFPLDRVKLDREFTHSLADDAkvgVIVGSVVSMAHALGMHVTAEGVETEAQRQALAAH 590
Cdd:PRK11829 553 LLIALDDFGIGYSSlryLNHLKSLPIHMIKLDKSFVKNLPEDD---AIARIISCVSDVLKVRVMAEGVETEEQRQWLLEH 629
|
410
....*....|....*
gi 332111392 591 GCDVLQGFLLGRPQP 605
Cdd:PRK11829 630 GIQCGQGFLFSPPLP 644
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
199-353 |
3.74e-43 |
|
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.
Pssm-ID: 143635 [Multi-domain] Cd Length: 158 Bit Score: 151.94 E-value: 3.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 199 QHDPLTGALNRESF---VAALRRAAARRAGHSAVLCMDLDRFREFNEWLGRGAGDSLLRQVAARLRATVRSGDLVARLGS 275
Cdd:cd01949 1 YTDPLTGLPNRRAFeerLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332111392 276 DEFAVLADTGDAEALATLAQRIVEALRQPYDVGGRRCEIGASIGIALHGVDSREADRLLQQADLALARAKADGRGTFR 353
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
194-355 |
6.09e-38 |
|
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];
Pssm-ID: 441801 [Multi-domain] Cd Length: 275 Bit Score: 141.65 E-value: 6.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 194 IDYLDQHDPLTGALNRESF---VAALRRAAARRAGHSAVLCMDLDRFREFNEWLGRGAGDSLLRQVAARLRATVRSGDLV 270
Cdd:COG2199 110 LRRLATHDPLTGLPNRRAFeerLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLV 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 271 ARLGSDEFAVLADTGDAEALATLAQRIVEALRQ-PYDVGGRRCEIGASIGIALHGVDSREADRLLQQADLALARAKADGR 349
Cdd:COG2199 190 ARLGGDEFAVLLPGTDLEEAEALAERLREALEQlPFELEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAGR 269
|
....*.
gi 332111392 350 GTFRFY 355
Cdd:COG2199 270 NRVVVY 275
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
196-355 |
1.66e-36 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 133.91 E-value: 1.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 196 YLDQHDPLTGALNR---ESFVAALRRAAARRAGHSAVLCMDLDRFREFNEWLGRGAGDSLLRQVAARLRATVRSGDLVAR 272
Cdd:smart00267 1 RLAFRDPLTGLPNRryfEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 273 LGSDEFAVLADTGDAEALATLAQRIVEALRQPYDVGGRRCEIGASIGIALHGVDSREADRLLQQADLALARAKADGRGTF 352
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQV 160
|
...
gi 332111392 353 RFY 355
Cdd:smart00267 161 AVY 163
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
363-611 |
8.04e-36 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 141.28 E-value: 8.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 363 LQRRRRLGAELRDALAADALVLHFQPLMDAASGRIVGYEALARWPHAERGWVPPASFIPLAEQTGLIEDLGAWVLRAACR 442
Cdd:PRK10551 258 LSLRMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIAR 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 443 EAARW----PAPLSVAVNLSPAQFRRDGGIAEVvaEALRDSgLAPERLE--LEITESLlMARTEPVLRALRELRGLGVSI 516
Cdd:PRK10551 338 DAAELqkvlPVGAKLGINISPAHLHSDSFKADV--QRLLAS-LPADHFQivLEITERD-MVQEEEATKLFAWLHSQGIEI 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 517 AMDDFGTGYSSLAHLWRFPLDRVKLDREFTHSLADDAKVGVIVGSVVSMAHALGMHVTAEGVETEAQRQALAAHGCDVLQ 596
Cdd:PRK10551 414 AIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQ 493
|
250
....*....|....*
gi 332111392 597 GFLLGRPQPADRLPH 611
Cdd:PRK10551 494 GYWISRPLPLEDFVR 508
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
200-350 |
4.04e-35 |
|
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.
Pssm-ID: 425976 [Multi-domain] Cd Length: 160 Bit Score: 130.07 E-value: 4.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 200 HDPLTGALNR---ESFVAALRRAAARRAGHSAVLCMDLDRFREFNEWLGRGAGDSLLRQVAARLRATVRSGDLVARLGSD 276
Cdd:pfam00990 3 HDPLTGLPNRryfEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGGD 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332111392 277 EFAVL---ADTGDAEALATLAQRIVEALRQPYDVGGRRCEIGASIGIALHGVDSREADRLLQQADLALARAKADGRG 350
Cdd:pfam00990 83 EFAILlpeTSLEGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRN 159
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
199-356 |
2.12e-24 |
|
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]
Pssm-ID: 272984 [Multi-domain] Cd Length: 165 Bit Score: 100.10 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 199 QHDPLTGALNRESFVAALRRAAARRAGHS---AVLCMDLDRFREFNEWLGRGAGDSLLRQVAARLRATVRSGDLVARLGS 275
Cdd:TIGR00254 3 VRDPLTGLYNRRYLEEMLDSELKRARRFQrsfSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 276 DEFAVLADTGDAEALATLAQRIVEALRQ-PYDVGGR-RCEIGASIGIALHGVDSREADRLLQQADLALARAKADGRGTFR 353
Cdd:TIGR00254 83 EEFVVILPGTPLEDALSKAERLRDAINSkPIEVAGSeTLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNRVV 162
|
...
gi 332111392 354 FYD 356
Cdd:TIGR00254 163 VAD 165
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
201-349 |
1.85e-20 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 94.58 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 201 DPLTGALNRESFVA--ALRRAAARRAGHSAVLCM-DLDRFREFNEWLGRGAGDSLLRQVAARLRATVRSGDLVARLGSDE 277
Cdd:PRK09581 295 DGLTGLHNRRYFDMhlKNLIERANERGKPLSLMMiDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEE 374
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332111392 278 FA-VLADTGDAEALATlAQRIVEALRQ-PYDV--GGRRCEIGASIGIA--LHGVDSREAdrLLQQADLALARAKADGR 349
Cdd:PRK09581 375 FVvVMPDTDIEDAIAV-AERIRRKIAEePFIIsdGKERLNVTVSIGVAelRPSGDTIEA--LIKRADKALYEAKNTGR 449
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
200-349 |
2.00e-14 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 76.21 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 200 HDPLTGALNRESFVAALRRAAARRAGHS---AVLCMDLDRFREFNEWLGRGAGDSLLRQVAARLRATVRSGDLVARLGSD 276
Cdd:PRK15426 400 HDPLTRLYNRGALFEKARALAKRCQRDQqpfSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 277 EFAV-LADTGDAEALAtLAQRIVEAL-RQPYDVG-GRRCEIGASIGIAlhgvDSREA-----DRLLQQADLALARAKADG 348
Cdd:PRK15426 480 EFCVvLPGASLAEAAQ-VAERIRLRInEKEILVAkSTTIRISASLGVS----SAEEDgdydfEQLQSLADRRLYLAKQAG 554
|
.
gi 332111392 349 R 349
Cdd:PRK15426 555 R 555
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
201-356 |
1.33e-12 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 68.94 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 201 DPLTGALNRESFVAALRRAAARRAGHS-AVLCMDLDRFREFNEWLGRGAGDSLLRQVAARLRATVRSGDLVARLGSDEFA 279
Cdd:PRK09894 132 DVLTGLPGRRVLDESFDHQLRNREPQNlYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFI 211
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332111392 280 V-LADTGDAEAlATLAQRIVEAL-RQPYDVGGRRCEIGASIGIAlHGVDSREADRLLQQADLALARAKADGRGTFRFYD 356
Cdd:PRK09894 212 IcLKAATDEEA-CRAGERIRQLIaNHAITHSDGRINITATFGVS-RAFPEETLDVVIGRADRAMYEGKQTGRNRVMFID 288
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
200-345 |
1.68e-11 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 66.57 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 200 HDPLTGALNRESFVAALRRAAARRAGH--SAVLCMDLDRFREFNEWLGRGAGDSLLRQVAARLRATVRSGDLVARLGSDE 277
Cdd:PRK09966 250 HDPLTGLANRAAFRSGINTLMNNSDARktSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDE 329
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 278 FA-VLADTGDAEALATLAQRIVEALRQPYDV-GGRRCEIGASIGIALhGVDSREADRLLQQADLALARAK 345
Cdd:PRK09966 330 FAmVLYDVQSESEVQQICSALTQIFNLPFDLhNGHQTTMTLSIGYAM-TIEHASAEKLQELADHNMYQAK 398
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
201-350 |
1.42e-10 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 63.31 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 201 DPLTGALNR---ESFVAALRRAAARRAGHSAVLCMDLDRFREFNEWLGRGAGDSLLRQVAARLRATVRSGDLVARLGSDE 277
Cdd:PRK10245 208 DGMTGVYNRrhwETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDE 287
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332111392 278 FAVLADTGDAEALATLAQRIVEALRQPYDVGGRRCEIGASIGIALHGVDSREADRLLQQADLALARAKADGRG 350
Cdd:PRK10245 288 FAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPQVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKNAGRN 360
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
481-605 |
3.01e-10 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 62.51 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 481 LAPERLELEITESllMARTEPVLRALRELRGLGVSIAMDDFgTGYSSLAHLwrFPL-DRVKLDreFTHSLADDAKVGVIV 559
Cdd:COG3434 81 LPPERVVLEILED--VEPDEELLEALKELKEKGYRIALDDF-VLDPEWDPL--LPLaDIIKID--VLALDLEELAELVAR 153
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 332111392 560 gsvvsmAHALGMHVTAEGVETEAQRQALAAHGCDVLQGFLLGRPQP 605
Cdd:COG3434 154 ------LKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEI 193
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
201-607 |
1.23e-08 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 57.95 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 201 DPLTGALNRESF---VAALRRAAARRAGHSAVLCMDLDRFREFNEWLGRGAGDSLLRQVAARLRATVRS--GDLVARLGS 275
Cdd:PRK11059 231 DAKTGLGNRLFFdnqLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRypGALLARYSR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 276 DEFAVLA---DTGDAEALATLAQRIVEALrQPYDVGGRR--CEIGASigiALHGVDSREadRLLQQADLALARAKADGRG 350
Cdd:PRK11059 311 SDFAVLLphrSLKEADSLASQLLKAVDAL-PPPKMLDRDdfLHIGIC---AYRSGQSTE--QVMEEAEMALRSAQLQGGN 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 351 TFRFYDARLDDELQR---R-RRLgaeLRDALAADALVLHFQPLMDAaSGRIVGYEALARWPHAERGWVPPASFIPLAEQT 426
Cdd:PRK11059 385 GWFVYDKAQLPEKGRgsvRwRTL---LEQTLVRGGPRLYQQPAVTR-DGKVHHRELFCRIRDGQGELLSAELFMPMVQQL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 427 GLIEDLGAWVLRAACREAARWP-APLSVAVN----LSPAQFRRdggiaevvaeaLRDSGLAPE-----RLELEITESLLM 496
Cdd:PRK11059 461 GLSEQYDRQVIERVLPLLRYWPeENLSINLSvdslLSRAFQRW-----------LRDTLLQCPrsqrkRLIFELAEADVC 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 497 ARTEPVLRALRELRGLGVSIAMDDFGTGYSSLAHLWRFPLDRVKLDRE-------------FTHSLADDAKVGvivgsvv 563
Cdd:PRK11059 530 QHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSlvrnihkrtenqlFVRSLVGACAGT------- 602
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 332111392 564 smahalGMHVTAEGVETEAQRQALAAHGCDVLQGFLLGRPQPAD 607
Cdd:PRK11059 603 ------ETQVFATGVESREEWQTLQELGVSGGQGDFFAESQPLD 640
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
229-347 |
3.43e-07 |
|
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.
Pssm-ID: 143637 [Multi-domain] Cd Length: 133 Bit Score: 49.66 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 229 VLCMDLDRFREFNEWLGRGAGDSLLRQVAARLRATV-RSGDLVARLGSDEFAVLADTGDAEALATLAQRIVEALRQPYDV 307
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSALNQS 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 332111392 308 GGR--RCEIGASIGIALHGVDSREAD-----RLLQQADLALARAKAD 347
Cdd:cd07556 84 EGNpvRVRIGIHTGPVVVGVIGSRPQydvwgALVNLASRMESQAKAG 130
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
260-345 |
4.03e-07 |
|
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];
Pssm-ID: 442920 [Multi-domain] Cd Length: 179 Bit Score: 50.29 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 260 LRATVrsgDLVARLGSDEFAVLADTGDAEALATLAQRIVEALRQPYDVggrrcEIGASIGIAlhgvdsreADRLLQQADl 339
Cdd:COG3706 111 LLARV---DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAELPSL-----RVTVSIGVA--------GDSLLKRAD- 173
|
....*.
gi 332111392 340 ALARAK 345
Cdd:COG3706 174 ALYQAR 179
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
518-610 |
3.32e-04 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 42.68 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332111392 518 MDDFGTG---YSSLAhLWRFplDRVKLDRE-FTHSLADDAKVGVIVGSVVSMA-HALGmhVTAEGVETE-----AQRQ-A 586
Cdd:PRK11596 157 LDDFGTGmanFSALS-EVRY--DYIKVARElFIMLRQSEEGRNLFSQLLHLMNrYCRG--VIVEGVETPeewrdVQRSpA 231
|
90 100
....*....|....*....|....
gi 332111392 587 LAAhgcdvlQGFLLGRPQPADRLP 610
Cdd:PRK11596 232 FAA------QGYFLSRPAPFETLE 249
|
|
| |
