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Conserved domains on  [gi|695713836|ref|WP_032644711|]
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MULTISPECIES: EAL domain-containing protein [Enterobacter cloacae complex]

Protein Classification

EAL domain-containing protein( domain architecture ID 11471819)

EAL domain-containing protein may act as a cyclic diguanylate phosphodiesterase, similar to Escherichia coli putative cyclic-di-GMP phosphodiesterases YjcC and YlaB

Gene Ontology:  GO:0007165

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 2-521 0e+00

Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal transduction mechanisms];


:

Pssm-ID: 443970 [Multi-domain]  Cd Length: 528  Bit Score: 693.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836   2 NRSARRKMLRVVGIIMVVMLPVMLALWFAQLRAVSETSAQLRTFAELALDKTELVIQQVDLARDEAEKYQGELCTPGHRQ 81
Cdd:COG4943    3 MRRRRLLSLATLLALLAALLPLLLSLWLAQIQARRREREQLESYAQRALARAERVFDQARSALDELNALPGDPCSPAHLA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836  82 YMLNVVRGRLFVADLIYAEGEHFLCSTVFTPDRPYAIPAANYTRKPDVAIYYYRDTPFYTGYKMTYMQRGNYVVVVNPLS 161
Cdd:COG4943   83 ALRRLVFSSRYVRDIGYVRDGRLLCSSLGKLSKPVPLPPPDYVTADGYRLWLNVDNPLDPGRPMLIVGRGNYVVVIDPAA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 162 YSEVMSADHSLSWGVYDTVTNAFFSVSQKANVSLLNSMIRDKESVFQKDNRFYTVVKSPKRPIAAIVSTSNKRFYETLYH 241
Cdd:COG4943  163 FIDVLSPQPGISLALLATNGGHLFASSGNPDPALLSRLLRGPSSWFIQGDRLYASACSPQYPICVVAAAPLAGLLALWRQ 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 242 QATLTLPLGMICSIIILLVWSRTHRELNSPGRLLHRALNKRQLCLHYQPIIDIKNNQCVGAEALLRWPGFNGQVMSPAEF 321
Cdd:COG4943  243 LLLLLLPLGLLLSLLLGLLVLRLLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIF 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 322 IPLAENEGMSERITDYVVEEVFNDLGHFLAEHPHLYISINLSATDFHSSRLIAMISDKARHYAVRAQQIKIEVTERGFID 401
Cdd:COG4943  323 IPLAEQSGLISPLTRQVIEQVFRDLGDLLAADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFID 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 402 VPKTTPVIQAFRQAGYEVAIDDFGTGYSNLHNLYSLNVDILKIDKSFIDTLTTNSTSHLIAEHIIEMAQSLRLKTIAEGV 481
Cdd:COG4943  403 PAKARAVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGV 482

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 695713836 482 ETAEQVSWLLKRGVQFCQGWHFAKAMPPQEFMTWQQQPLH 521
Cdd:COG4943  483 ETEEQADYLRARGVQYGQGWLFAKPLPAEEFIAWLAAQRA 522
 
Name Accession Description Interval E-value
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 2-521 0e+00

Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal transduction mechanisms];


Pssm-ID: 443970 [Multi-domain]  Cd Length: 528  Bit Score: 693.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836   2 NRSARRKMLRVVGIIMVVMLPVMLALWFAQLRAVSETSAQLRTFAELALDKTELVIQQVDLARDEAEKYQGELCTPGHRQ 81
Cdd:COG4943    3 MRRRRLLSLATLLALLAALLPLLLSLWLAQIQARRREREQLESYAQRALARAERVFDQARSALDELNALPGDPCSPAHLA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836  82 YMLNVVRGRLFVADLIYAEGEHFLCSTVFTPDRPYAIPAANYTRKPDVAIYYYRDTPFYTGYKMTYMQRGNYVVVVNPLS 161
Cdd:COG4943   83 ALRRLVFSSRYVRDIGYVRDGRLLCSSLGKLSKPVPLPPPDYVTADGYRLWLNVDNPLDPGRPMLIVGRGNYVVVIDPAA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 162 YSEVMSADHSLSWGVYDTVTNAFFSVSQKANVSLLNSMIRDKESVFQKDNRFYTVVKSPKRPIAAIVSTSNKRFYETLYH 241
Cdd:COG4943  163 FIDVLSPQPGISLALLATNGGHLFASSGNPDPALLSRLLRGPSSWFIQGDRLYASACSPQYPICVVAAAPLAGLLALWRQ 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 242 QATLTLPLGMICSIIILLVWSRTHRELNSPGRLLHRALNKRQLCLHYQPIIDIKNNQCVGAEALLRWPGFNGQVMSPAEF 321
Cdd:COG4943  243 LLLLLLPLGLLLSLLLGLLVLRLLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIF 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 322 IPLAENEGMSERITDYVVEEVFNDLGHFLAEHPHLYISINLSATDFHSSRLIAMISDKARHYAVRAQQIKIEVTERGFID 401
Cdd:COG4943  323 IPLAEQSGLISPLTRQVIEQVFRDLGDLLAADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFID 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 402 VPKTTPVIQAFRQAGYEVAIDDFGTGYSNLHNLYSLNVDILKIDKSFIDTLTTNSTSHLIAEHIIEMAQSLRLKTIAEGV 481
Cdd:COG4943  403 PAKARAVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGV 482

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 695713836 482 ETAEQVSWLLKRGVQFCQGWHFAKAMPPQEFMTWQQQPLH 521
Cdd:COG4943  483 ETEEQADYLRARGVQYGQGWLFAKPLPAEEFIAWLAAQRA 522
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 273-511 1.45e-97

Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 294.89  E-value: 1.45e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836   273 RLLHRALNKRQLCLHYQPIIDIKNNQCVGAEALLRWPGFNGQVMSPAEFIPLAENEGMSERITDYVVEEVFNDLGHFLAE 352
Cdd:smart00052   2 RELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQ 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836   353 HPH-LYISINLSATDFHSSRLIAMISDKARHYAVRAQQIKIEVTERGFIDVPKTT-PVIQAFRQAGYEVAIDDFGTGYSN 430
Cdd:smart00052  82 GPPpLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAvATLQRLRELGVRIALDDFGTGYSS 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836   431 LHNLYSLNVDILKIDKSFIDTLTTNSTSHLIAEHIIEMAQSLRLKTIAEGVETAEQVSWLLKRGVQFCQGWHFAKAMPPQ 510
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLD 241


                   .
gi 695713836   511 E 511
Cdd:smart00052 242 D 242
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 273-511 1.17e-96

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: 292.53  E-value: 1.17e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 273 RLLHRALNKRQLCLHYQPIIDIKNNQCVGAEALLRWPGFNGQVMSPAEFIPLAENEGMSERITDYVVEEVFNDLGHFLAE 352
Cdd:cd01948    1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 353 HPHLYISINLSATDFHSSRLIAMISDKARHYAVRAQQIKIEVTERGFI-DVPKTTPVIQAFRQAGYEVAIDDFGTGYSNL 431
Cdd:cd01948   81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIdDLEEALATLRRLRALGVRIALDDFGTGYSSL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 432 HNLYSLNVDILKIDKSFIDTLTTNSTSHLIAEHIIEMAQSLRLKTIAEGVETAEQVSWLLKRGVQFCQGWHFAKAMPPQE 511
Cdd:cd01948  161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 275-506 4.62e-75

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: 236.83  E-value: 4.62e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836  275 LHRALNKRQLCLHYQPIIDIKNNQCVGAEALLRWPGFNGQVMSPAEFIPLAENEGMSERITDYVVEEVFNDLGHfLAEHP 354
Cdd:pfam00563   4 LRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQ-LQLGP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836  355 HLYISINLSATDFHSSRLIAMISDKARHYAVRAQQIKIEVTERGFI-DVPKTTPVIQAFRQAGYEVAIDDFGTGYSNLHN 433
Cdd:pfam00563  83 DIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLaRLEALREVLKRLRALGIRIALDDFGTGYSSLSY 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695713836  434 LYSLNVDILKIDKSFIDTLTTNSTSHLIAEHIIEMAQSLRLKTIAEGVETAEQVSWLLKRGVQFCQGWHFAKA 506
Cdd:pfam00563 163 LLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 262-512 1.37e-50

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 183.38  E-value: 1.37e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 262 SRTHRELNSPGRLLHrALNKRQLCLHYQPIIDIKNNQCVGAEALLRWPGFNGQVMSPAEFIPLAENEGMSERITDYVVEE 341
Cdd:PRK13561 393 EAAQKRLTEESDILN-ALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEE 471

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 342 VFNDLGHFLAEHPHLYISINLSATDFHSSRLIAMISDKARHYAVRAQQIKIEVTERGFIDVPKTTPVI-QAFRQAGYEVA 420
Cdd:PRK13561 472 SCRLLAAWQERGIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAIlRPLRNAGVRVA 551

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 421 IDDFGTGYSNLHNLY---SLNVDILKIDKSFIDTLTTNSTshlIAEHIIEMAQSLRLKTIAEGVETAEQVSWLLKRGVQF 497
Cdd:PRK13561 552 LDDFGMGYAGLRQLQhmkSLPIDVLKIDKMFVDGLPEDDS---MVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGI 628

                        250
                 ....*....|....*
gi 695713836 498 CQGWHFAKAMPPQEF 512
Cdd:PRK13561 629 AQGFLFARALPIEIF 643
 
Name Accession Description Interval E-value
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 2-521 0e+00

Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal transduction mechanisms];


Pssm-ID: 443970 [Multi-domain]  Cd Length: 528  Bit Score: 693.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836   2 NRSARRKMLRVVGIIMVVMLPVMLALWFAQLRAVSETSAQLRTFAELALDKTELVIQQVDLARDEAEKYQGELCTPGHRQ 81
Cdd:COG4943    3 MRRRRLLSLATLLALLAALLPLLLSLWLAQIQARRREREQLESYAQRALARAERVFDQARSALDELNALPGDPCSPAHLA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836  82 YMLNVVRGRLFVADLIYAEGEHFLCSTVFTPDRPYAIPAANYTRKPDVAIYYYRDTPFYTGYKMTYMQRGNYVVVVNPLS 161
Cdd:COG4943   83 ALRRLVFSSRYVRDIGYVRDGRLLCSSLGKLSKPVPLPPPDYVTADGYRLWLNVDNPLDPGRPMLIVGRGNYVVVIDPAA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 162 YSEVMSADHSLSWGVYDTVTNAFFSVSQKANVSLLNSMIRDKESVFQKDNRFYTVVKSPKRPIAAIVSTSNKRFYETLYH 241
Cdd:COG4943  163 FIDVLSPQPGISLALLATNGGHLFASSGNPDPALLSRLLRGPSSWFIQGDRLYASACSPQYPICVVAAAPLAGLLALWRQ 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 242 QATLTLPLGMICSIIILLVWSRTHRELNSPGRLLHRALNKRQLCLHYQPIIDIKNNQCVGAEALLRWPGFNGQVMSPAEF 321
Cdd:COG4943  243 LLLLLLPLGLLLSLLLGLLVLRLLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIF 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 322 IPLAENEGMSERITDYVVEEVFNDLGHFLAEHPHLYISINLSATDFHSSRLIAMISDKARHYAVRAQQIKIEVTERGFID 401
Cdd:COG4943  323 IPLAEQSGLISPLTRQVIEQVFRDLGDLLAADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFID 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 402 VPKTTPVIQAFRQAGYEVAIDDFGTGYSNLHNLYSLNVDILKIDKSFIDTLTTNSTSHLIAEHIIEMAQSLRLKTIAEGV 481
Cdd:COG4943  403 PAKARAVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGV 482

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 695713836 482 ETAEQVSWLLKRGVQFCQGWHFAKAMPPQEFMTWQQQPLH 521
Cdd:COG4943  483 ETEEQADYLRARGVQYGQGWLFAKPLPAEEFIAWLAAQRA 522
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 273-511 1.45e-97

Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 294.89  E-value: 1.45e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836   273 RLLHRALNKRQLCLHYQPIIDIKNNQCVGAEALLRWPGFNGQVMSPAEFIPLAENEGMSERITDYVVEEVFNDLGHFLAE 352
Cdd:smart00052   2 RELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQ 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836   353 HPH-LYISINLSATDFHSSRLIAMISDKARHYAVRAQQIKIEVTERGFIDVPKTT-PVIQAFRQAGYEVAIDDFGTGYSN 430
Cdd:smart00052  82 GPPpLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAvATLQRLRELGVRIALDDFGTGYSS 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836   431 LHNLYSLNVDILKIDKSFIDTLTTNSTSHLIAEHIIEMAQSLRLKTIAEGVETAEQVSWLLKRGVQFCQGWHFAKAMPPQ 510
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLD 241


                   .
gi 695713836   511 E 511
Cdd:smart00052 242 D 242
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 273-511 1.17e-96

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: 292.53  E-value: 1.17e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 273 RLLHRALNKRQLCLHYQPIIDIKNNQCVGAEALLRWPGFNGQVMSPAEFIPLAENEGMSERITDYVVEEVFNDLGHFLAE 352
Cdd:cd01948    1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 353 HPHLYISINLSATDFHSSRLIAMISDKARHYAVRAQQIKIEVTERGFI-DVPKTTPVIQAFRQAGYEVAIDDFGTGYSNL 431
Cdd:cd01948   81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIdDLEEALATLRRLRALGVRIALDDFGTGYSSL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 432 HNLYSLNVDILKIDKSFIDTLTTNSTSHLIAEHIIEMAQSLRLKTIAEGVETAEQVSWLLKRGVQFCQGWHFAKAMPPQE 511
Cdd:cd01948  161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 275-515 3.46e-88

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: 284.74  E-value: 3.46e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 275 LHRALNKRQLCLHYQPIIDIKNNQCVGAEALLRWPGFNGQVMSPAEFIPLAENEGMSERITDYVVEEVFNDLGHFLAE-H 353
Cdd:COG5001  430 LRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAgL 509

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 354 PHLYISINLSATDFHSSRLIAMISDKARHYAVRAQQIKIEVTERGFI-DVPKTTPVIQAFRQAGYEVAIDDFGTGYSNLH 432
Cdd:COG5001  510 PDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLeDPEEALETLRALRALGVRIALDDFGTGYSSLS 589

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 433 NLYSLNVDILKIDKSFIDTLTTNSTSHLIAEHIIEMAQSLRLKTIAEGVETAEQVSWLLKRGVQFCQGWHFAKAMPPQEF 512
Cdd:COG5001  590 YLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEEL 669


                 ...
gi 695713836 513 MTW 515
Cdd:COG5001  670 EAL 672
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 273-515 3.15e-87

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: 279.75  E-value: 3.15e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 273 RLLHRALNKRQLCLHYQPIIDIKNNQCVGAEALLRWPGFNGQVMSPAEFIPLAENEGMSERITDYVVEEVFNDLGHFLAE 352
Cdd:COG2200  331 SELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPER 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 353 HPHLYISINLSATDFHSSRLIAMISDKARHYAVRAQQIKIEVTERGFI-DVPKTTPVIQAFRQAGYEVAIDDFGTGYSNL 431
Cdd:COG2200  411 GLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLeDLEAAIELLARLRALGVRIALDDFGTGYSSL 490

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 432 HNLYSLNVDILKIDKSFIDTLTTNSTSHLIAEHIIEMAQSLRLKTIAEGVETAEQVSWLLKRGVQFCQGWHFAKAMPPQE 511
Cdd:COG2200  491 SYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEE 570


                 ....
gi 695713836 512 FMTW 515
Cdd:COG2200  571 LEAL 574
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 275-506 4.62e-75

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: 236.83  E-value: 4.62e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836  275 LHRALNKRQLCLHYQPIIDIKNNQCVGAEALLRWPGFNGQVMSPAEFIPLAENEGMSERITDYVVEEVFNDLGHfLAEHP 354
Cdd:pfam00563   4 LRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQ-LQLGP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836  355 HLYISINLSATDFHSSRLIAMISDKARHYAVRAQQIKIEVTERGFI-DVPKTTPVIQAFRQAGYEVAIDDFGTGYSNLHN 433
Cdd:pfam00563  83 DIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLaRLEALREVLKRLRALGIRIALDDFGTGYSSLSY 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695713836  434 LYSLNVDILKIDKSFIDTLTTNSTSHLIAEHIIEMAQSLRLKTIAEGVETAEQVSWLLKRGVQFCQGWHFAKA 506
Cdd:pfam00563 163 LLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 262-512 1.37e-50

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 183.38  E-value: 1.37e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 262 SRTHRELNSPGRLLHrALNKRQLCLHYQPIIDIKNNQCVGAEALLRWPGFNGQVMSPAEFIPLAENEGMSERITDYVVEE 341
Cdd:PRK13561 393 EAAQKRLTEESDILN-ALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEE 471

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 342 VFNDLGHFLAEHPHLYISINLSATDFHSSRLIAMISDKARHYAVRAQQIKIEVTERGFIDVPKTTPVI-QAFRQAGYEVA 420
Cdd:PRK13561 472 SCRLLAAWQERGIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAIlRPLRNAGVRVA 551

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 421 IDDFGTGYSNLHNLY---SLNVDILKIDKSFIDTLTTNSTshlIAEHIIEMAQSLRLKTIAEGVETAEQVSWLLKRGVQF 497
Cdd:PRK13561 552 LDDFGMGYAGLRQLQhmkSLPIDVLKIDKMFVDGLPEDDS---MVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGI 628

                        250
                 ....*....|....*
gi 695713836 498 CQGWHFAKAMPPQEF 512
Cdd:PRK13561 629 AQGFLFARALPIEIF 643
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 263-513 1.41e-48

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 177.83  E-value: 1.41e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 263 RTHRELNSPGRLLHrALNKRQLCLHYQPIIDIKNNQCVGAEALLRWPGFNGQVMSPAEFIPLAENEGMSERITDYVVEEV 342
Cdd:PRK11829 399 KTHKRLTQENDLLQ-AIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEA 477

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 343 FNDLGHFLAEHPHLYISINLSATDFHSSRLIAMISDKARHYAVRAQQIKIEVTERGFI-DVPKTTPVIQAFRQAGYEVAI 421
Cdd:PRK11829 478 CRILADWKARGVSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIqDLDEALRLLRELQGLGLLIAL 557

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 422 DDFGTGYSNLH---NLYSLNVDILKIDKSFIDTLTTNSTshlIAEHIIEMAQSLRLKTIAEGVETAEQVSWLLKRGVQFC 498
Cdd:PRK11829 558 DDFGIGYSSLRylnHLKSLPIHMIKLDKSFVKNLPEDDA---IARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCG 634

                        250
                 ....*....|....*
gi 695713836 499 QGWHFAKAMPPQEFM 513
Cdd:PRK11829 635 QGFLFSPPLPRAEFE 649
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 272-521 7.60e-46

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 171.49  E-value: 7.60e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 272 GRLLHRALNKRQLCLHYQPIIDIKNNQCVGAEALLRWPGFNGQVMSPAEFIPLAENEGMSERITDYVVEEVFNDLGHFLA 351
Cdd:PRK11359 545 GAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRS 624

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 352 EHPHL-YISINLSATDFHSSRLIAMISDKARHYAVRAQQIKIEVTERGFIDV-PKTTPVIQAFRQAGYEVAIDDFGTGYS 429
Cdd:PRK11359 625 QNIHIpALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHdTEIFKRIQILRDMGVGLSVDDFGTGFS 704

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 430 NLHNLYSLNVDILKIDKSFIDTLTTNSTSHLIAEHIIEMAQSLRLKTIAEGVETAEQVSWLLKRGVQFCQGWHFAKAMPP 509
Cdd:PRK11359 705 GLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPA 784

                        250
                 ....*....|....
gi 695713836 510 QEFMTWQQ--QPLH 521
Cdd:PRK11359 785 EEIPGWMSsvLPLK 798
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
239-519 3.07e-45

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 166.32  E-value: 3.07e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 239 LYHQA------TLTLPLGMICSII-------ILLVWSRthrelnsPGRLLHRALNKRQLCLHYQPIIDIKNNQCVGAEAL 305
Cdd:PRK10551 226 LYADSwtandiWYALLLGLLSGILvgllcyyLLSLRMR-------PGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEAL 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 306 LRWPGFNGQVMSPAEFIPLAENEGMSERITDYVVEEVFNDlGHFLAEH--PHLYISINLSATDFHS-------SRLIAMI 376
Cdd:PRK10551 299 LRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARD-AAELQKVlpVGAKLGINISPAHLHSdsfkadvQRLLASL 377

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 377 SdkARHYavraqQIKIEVTERGFIDVPKTTPVIQAFRQAGYEVAIDDFGTGYSNLHNLYSLNVDILKIDKSFIDTLTTNS 456
Cdd:PRK10551 378 P--ADHF-----QIVLEITERDMVQEEEATKLFAWLHSQGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTET 450

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695713836 457 TSHLIAEHIIEMAQSLRLKTIAEGVETAEQVSWLLKRGVQFCQGWHFAKAMPPQEFMTWQQQP 519
Cdd:PRK10551 451 VTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPLEDFVRWLKEP 513
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
275-518 2.31e-43

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 163.31  E-value: 2.31e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 275 LHRALNKRQLCLHYQPIIDIKNNQCvGAEALLRW--PGfNGQVMsPAEFIPLAENEGMSERITDYVVEEVFNDLGHFLAE 352
Cdd:PRK10060 413 LRKALENDQLVIHYQPKITWRGEVR-SLEALVRWqsPE-RGLIP-PLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDK 489

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 353 HPHLYISINLSATDFHSSRLIAMISDKARHYAVRAQQIKIEVTERGFIDVPKTT-PVIQAFRQAGYEVAIDDFGTGYSNL 431
Cdd:PRK10060 490 GINLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIENEELAlSVIQQFSQLGAQVHLDDFGTGYSSL 569

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 432 HNLYSLNVDILKIDKSFIDTLTTNSTSHLIAEHIIEMAQSLRLKTIAEGVETAEQVSWLLKRGVQFCQGWHFAKAMPPQE 511
Cdd:PRK10060 570 SQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVA 649


                 ....*..
gi 695713836 512 FMTWQQQ 518
Cdd:PRK10060 650 FERWYKR 656
CSS-motif pfam12792
CSS motif domain associated with EAL; This family with its characteriztic highly conserved CSS ...
 38-243 2.02e-40

CSS motif domain associated with EAL; This family with its characteriztic highly conserved CSS sequence motif is found N-terminal to the EAL, pfam00563, domain in many cyclic diguanylate phosphodiesterases.


Pssm-ID: 463709  Cd Length: 209  Bit Score: 144.98  E-value: 2.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836   38 TSAQLRTFAELALDKTELVIQQVDLARDEAEKYQGELCTPGHRQYMLNVVRGRLFVADLIYAEGEHFLCSTVFTP-DRPY 116
Cdd:pfam12792   1 EQEQLDAFAERALRRLESVLDQADQALDRLLPLTGQPCSPAHLAELRRIVAFSPYVRDVGLVKNGRLYCSSLWGElDTPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836  117 AIPAANYTRKPDVAIYYYRDTPFYTGYKMTYMQRGNYVVVVNPLSYSEVMSaDHSLSWGVYDTVTNAFFSVSQKANVSLL 196
Cdd:pfam12792  81 PLLPPDLTTPPGVRLWLLRGTPLVPGRPALVLRRGGYGVVIDPGVFIDVQY-LPGLLAAVSQPDGRLLALVVGDDALLFD 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 695713836  197 NSMIRDKE---SVFQKDNRFYTVVKSPKRPIAAIVSTSNKRFYETLYHQA 243
Cdd:pfam12792 160 GRLHSLAEpapGTARSGGALYARARSTRYPLTVVVYAPRASLLANWRQLL 209
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 263-508 1.24e-21

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 98.98  E-value: 1.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836  263 RTHRELnSPGRLLHRALNKRQLCLHYQPIIDIKNNQCVGAEALLRWPGFNGQVMSPAEFIPLAENEGMSERITDYVVEEV 342
Cdd:PRK09776  835 SEHRAL-SLAEQWRMIKENQLMMLAHGVASPRIPEARNHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEF 913

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836  343 FNDLGHFLAEhPHLYISINLSATDFHSSRLIAMISDKARHYAVRAQQIKIEVTERGFI-DVPKTTPVIQAFRQAGYEVAI 421
Cdd:PRK09776  914 FRQAAKAVAS-KGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLnHAESASRLVQKLRLAGCRVVL 992

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836  422 DDFGTGYSNLHNLYSLNVDILKIDKSFIDTLTTNSTSHLIAEHIIEMAQSLRLKTIAEGVETAEQVSWLLKRGVQFCQGW 501
Cdd:PRK09776  993 SDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGY 1072


                  ....*..
gi 695713836  502 HFAKAMP 508
Cdd:PRK09776 1073 AIARPQP 1079
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
 289-505 1.03e-13

c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 72.91  E-value: 1.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 289 QPIIDiKNNQCVGAEALLRwpgfngqvMSPAEFIPLAEnegmSERITDYVVEEVFNDLG--HFLAEHPHLyisINLSAtD 366
Cdd:COG3434    9 QPILD-RDQRVVGYELLFR--------SGLENSAPDVD----GDQATARVLLNAFLEIGldRLLGGKLAF---INFTE-E 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 367 FHSSRLIAMISdkarhyavrAQQIKIEVTERGFIDvPKTTPVIQAFRQAGYEVAIDDFgTGYSNLHNLYSLnVDILKIDk 446
Cdd:COG3434   72 LLLSDLPELLP---------PERVVLEILEDVEPD-EELLEALKELKEKGYRIALDDF-VLDPEWDPLLPL-ADIIKID- 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 695713836 447 sfidtlTTNSTSHLIAEhIIEMAQSLRLKTIAEGVETAEQVSWLLKRGVQFCQGWHFAK 505
Cdd:COG3434  139 ------VLALDLEELAE-LVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSK 190
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 274-511 1.67e-06

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 50.63  E-value: 1.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 274 LLHRALNKRQLCLHYQPIID-------------IKNNQcvgaEALLRwpgfngqvmspAE-FIPLAENEGMSERITDYVV 339
Cdd:PRK11059 407 LLEQTLVRGGPRLYQQPAVTrdgkvhhrelfcrIRDGQ----GELLS-----------AElFMPMVQQLGLSEQYDRQVI 471

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 340 EEVFNDLGHFlaehPHLYISINLSATDFHSSRLIAMISDK----ARHYAvraQQIKIEVTERgfiDV----PKTTPVIQA 411
Cdd:PRK11059 472 ERVLPLLRYW----PEENLSINLSVDSLLSRAFQRWLRDTllqcPRSQR---KRLIFELAEA---DVcqhiSRLRPVLRM 541

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 412 FRQAGYEVAIDDFG-----TGYsnlhnLYSLNVDILKIDKSF---IDTLTTNstsHLIAEHIIEMAQSLRLKTIAEGVET 483
Cdd:PRK11059 542 LRGLGCRLAVDQAGltvvsTSY-----IKELNVELIKLHPSLvrnIHKRTEN---QLFVRSLVGACAGTETQVFATGVES 613

                        250       260
                 ....*....|....*....|....*...
gi 695713836 484 AEQVSWLLKRGVQFCQGWHFAkamPPQE 511
Cdd:PRK11059 614 REEWQTLQELGVSGGQGDFFA---ESQP 638
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
 421-521 3.70e-03

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 39.21  E-value: 3.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713836 421 IDDFGTGYSNLHNLYSLNVDILKIDKS-FIDTLTTNSTSHLIAEHIIEMAQSLRlKTIAEGVETAEQvsWLLKRGVQFC- 498
Cdd:PRK11596 157 LDDFGTGMANFSALSEVRYDYIKVARElFIMLRQSEEGRNLFSQLLHLMNRYCR-GVIVEGVETPEE--WRDVQRSPAFa 233

                         90       100
                 ....*....|....*....|....
gi 695713836 499 -QGWHFAKampPQEFMTWQQQPLH 521
Cdd:PRK11596 234 aQGYFLSR---PAPFETLETLPLA 254
 
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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