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Conserved domains on  [gi|332111392|gb|EGJ11375|]
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diguanylate cyclase/phosphodiesterase with pas/pac sensor(s) [Rubrivivax benzoatilyticus JA2 = ATCC BAA-35]

Protein Classification

putative bifunctional diguanylate cyclase/phosphodiesterase( domain architecture ID 11472025)

putative bifunctional diguanylate cyclase/phosphodiesterase may only contain one of the two functional domains (GGDEF diguanylate cyclase or EAL family cyclyc-guanylate-specific phosphodiesterase)

Graphical summary

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List of domain hits

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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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