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Conserved domains on  [gi|446415521|ref|WP_000493376|]
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MULTISPECIES: cyclic di-GMP phosphodiesterase [Escherichia]

Protein Classification

cyclic di-GMP phosphodiesterase( domain architecture ID 11484791)

cyclic di-GMP phosphodiesterase such as Escherichia coli PdeN, a phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic-di-GMP (c-di-GMP) to 5'-pGpG; includes Escherichia coli Rtn, which is involved in resistance to phages N4 and lambda

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
1-518 0e+00

cyclic di-GMP phosphodiesterase;


:

Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 996.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521   1 MFTAANASGRKILLTCFITGLVVAVIISCLQFTVSWHKREVKYDTLITDIKTYLVHYFADLKTSTDKLQPLTLSSCKKAA 80
Cdd:PRK10551   1 MFTRAPSSGRKILLTSIVAGVMIALLFSCLQFLLLWHKREVKYDTLITDVQKYLDTYFADLKSTTDRLQPLTLDTCQQVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521  81 PELTAKAAFSLNVRTFLLVRDKKAFCSSATGNMDIPLAHLVPALDISKDVDIAILPGTPMMPGKPAMVIWYRNPLISNSG 160
Cdd:PRK10551  81 PELTSRAAFSLNVRAFLLVKDKKAFCSSATGEMNTPLSELIPAIDINKPVDMAILPGTPMMPNKPAIVIWYRNPLLKNSG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 161 VFTALNLNLTPYLLYTSRQEDFDGIAMIVGDTVLSTSSSHLLNINELSGPPARQVKVEGIPLTVRLYATEWTWNDLWYAL 240
Cdd:PRK10551 161 VFATLNLNLTPYLLYTSRQEDFDGIALIIGNTALSTFSSRLMNVNELPDMPLRETTIPGYPLTIRLYADSWTANDIWYAL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 241 LLGGMSGIAAGLLCFYILSVRLRPGREILTAIKRDQFYVVYQPAVDTQSLKVTGLEVLLRWRHPVAGEIPPDAFIHYAEA 320
Cdd:PRK10551 241 LLGLLSGILVGLLCYYLLSLRMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 321 QRMIVPLTQHLFELIRRDAHVLQRVLPVGVKFGINIAPDHLHGETFKKDIRQLVESLPAHHFQIVLEITERDMLKQHEAT 400
Cdd:PRK10551 321 QKLIVPLTQHLFELIARDAAELQKVLPVGAKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEEAT 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 401 QLFEWLHSVGVEIAIDDFGTGHSALIYLERFTLDYLKIDRGFINAIGTETVTSPVLDAVLTLSKRLNMLTVAEGVETPEQ 480
Cdd:PRK10551 401 KLFAWLHSQGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQ 480

                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 446415521 481 AKWLRDRGVNFLQGYWISRPLPLNEFVQWLKKPDTPQW 518
Cdd:PRK10551 481 ARWLRERGVNFLQGYWISRPLPLEDFVRWLKEPYTPQW 518
 
Name Accession Description Interval E-value
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
1-518 0e+00

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 996.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521   1 MFTAANASGRKILLTCFITGLVVAVIISCLQFTVSWHKREVKYDTLITDIKTYLVHYFADLKTSTDKLQPLTLSSCKKAA 80
Cdd:PRK10551   1 MFTRAPSSGRKILLTSIVAGVMIALLFSCLQFLLLWHKREVKYDTLITDVQKYLDTYFADLKSTTDRLQPLTLDTCQQVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521  81 PELTAKAAFSLNVRTFLLVRDKKAFCSSATGNMDIPLAHLVPALDISKDVDIAILPGTPMMPGKPAMVIWYRNPLISNSG 160
Cdd:PRK10551  81 PELTSRAAFSLNVRAFLLVKDKKAFCSSATGEMNTPLSELIPAIDINKPVDMAILPGTPMMPNKPAIVIWYRNPLLKNSG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 161 VFTALNLNLTPYLLYTSRQEDFDGIAMIVGDTVLSTSSSHLLNINELSGPPARQVKVEGIPLTVRLYATEWTWNDLWYAL 240
Cdd:PRK10551 161 VFATLNLNLTPYLLYTSRQEDFDGIALIIGNTALSTFSSRLMNVNELPDMPLRETTIPGYPLTIRLYADSWTANDIWYAL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 241 LLGGMSGIAAGLLCFYILSVRLRPGREILTAIKRDQFYVVYQPAVDTQSLKVTGLEVLLRWRHPVAGEIPPDAFIHYAEA 320
Cdd:PRK10551 241 LLGLLSGILVGLLCYYLLSLRMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 321 QRMIVPLTQHLFELIRRDAHVLQRVLPVGVKFGINIAPDHLHGETFKKDIRQLVESLPAHHFQIVLEITERDMLKQHEAT 400
Cdd:PRK10551 321 QKLIVPLTQHLFELIARDAAELQKVLPVGAKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEEAT 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 401 QLFEWLHSVGVEIAIDDFGTGHSALIYLERFTLDYLKIDRGFINAIGTETVTSPVLDAVLTLSKRLNMLTVAEGVETPEQ 480
Cdd:PRK10551 401 KLFAWLHSQGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQ 480

                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 446415521 481 AKWLRDRGVNFLQGYWISRPLPLNEFVQWLKKPDTPQW 518
Cdd:PRK10551 481 ARWLRERGVNFLQGYWISRPLPLEDFVRWLKEPYTPQW 518
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 10-517 1.60e-107

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: 330.73  E-value: 1.60e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521  10 RKILLTCFITGLVVAVIISCLQFTVSWH---KREVKY-DTLITDIKTYLVHYFADLKTSTDKLQPLTLSSCKKAAPELTA 85
Cdd:COG4943    6 RRLLSLATLLALLAALLPLLLSLWLAQIqarRREREQlESYAQRALARAERVFDQARSALDELNALPGDPCSPAHLAALR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521  86 KAAF-SLNVRTFLLVRDKKAFCSSA---TGNMDIPLAHLVPALDIS--KDVDIAILPGTPM--MPGKPAMVI----WYRN 153
Cdd:COG4943   86 RLVFsSRYVRDIGYVRDGRLLCSSLgklSKPVPLPPPDYVTADGYRlwLNVDNPLDPGRPMliVGRGNYVVVidpaAFID 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 154 PLISNSGVFTALNLNLTPYLLYTsrqedFDGIAMIVGDTVLSTSSSHLLNINELSgppaRQVKVEGIPLTV-------RL 226
Cdd:COG4943  166 VLSPQPGISLALLATNGGHLFAS-----SGNPDPALLSRLLRGPSSWFIQGDRLY----ASACSPQYPICVvaaaplaGL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 227 YATEWTWndLWYALLLGGMSGIAAGLLCFYILSVRLRPGREILTAIKRDQFYVVYQPAVDTQSLKVTGLEVLLRWRHPVA 306
Cdd:COG4943  237 LALWRQL--LLLLLPLGLLLSLLLGLLVLRLLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDG 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 307 GEIPPDAFIHYAEAQRMIVPLTQHLFELIRRDAHVLQRVLPvGVKFGINIAPDHLHGETFKKDIRQLVESLPAHHFQIVL 386
Cdd:COG4943  315 SVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDLLAADP-DFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVL 393

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 387 EITERDMLKQHEATQLFEWLHSVGVEIAIDDFGTGHSALIYLERFTLDYLKIDRGFINAIGTETVTSPVLDAVLTLSKRL 466
Cdd:COG4943  394 EITERGFIDPAKARAVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTL 473

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446415521 467 NMLTVAEGVETPEQAKWLRDRGVNFLQGYWISRPLPLNEFVQWLKKPDTPQ 517
Cdd:COG4943  474 NLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPLPAEEFIAWLAAQRAPA 524
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 266-505 1.18e-91

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 279.87  E-value: 1.18e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521   266 REILTAIKRDQFYVVYQPAVDTQSLKVTGLEVLLRWRHPVAGEIPPDAFIHYAEAQRMIVPLTQHLFELIRRDAHVLQRV 345
Cdd:smart00052   2 RELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQ 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521   346 LPVGVKFGINIAPDHLHGETFKKDIRQLVESLPAHHFQIVLEITERDMLKQ-HEATQLFEWLHSVGVEIAIDDFGTGHSA 424
Cdd:smart00052  82 GPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDdESAVATLQRLRELGVRIALDDFGTGYSS 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521   425 LIYLERFTLDYLKIDRGFINAIGTETVTSPVLDAVLTLSKRLNMLTVAEGVETPEQAKWLRDRGVNFLQGYWISRPLPLN 504
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLD 241


                   .
gi 446415521   505 E 505
Cdd:smart00052 242 D 242
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 266-505 1.74e-86

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: 266.33  E-value: 1.74e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 266 REILTAIKRDQFYVVYQPAVDTQSLKVTGLEVLLRWRHPVAGEIPPDAFIHYAEAQRMIVPLTQHLFELIRRDAHVLQRV 345
Cdd:cd01948    1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 346 LPvGVKFGINIAPDHLHGETFKKDIRQLVESLPAHHFQIVLEITERDMLKQ-HEATQLFEWLHSVGVEIAIDDFGTGHSA 424
Cdd:cd01948   81 GP-DLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDlEEALATLRRLRALGVRIALDDFGTGYSS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 425 LIYLERFTLDYLKIDRGFINAIGTETVTSPVLDAVLTLSKRLNMLTVAEGVETPEQAKWLRDRGVNFLQGYWISRPLPLN 504
Cdd:cd01948  160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239


                 .
gi 446415521 505 E 505
Cdd:cd01948  240 E 240
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 266-500 7.24e-78

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: 244.15  E-value: 7.24e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521  266 REILTAIKRDQFYVVYQPAVDTQSLKVTGLEVLLRWRHPVAGEIPPDAFIHYAEAQRMIVPLTQHLFELIRRDahVLQRV 345
Cdd:pfam00563   2 RALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALAD--LAQLQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521  346 LPVGVKFGINIAPDHLHGETFKKDIRQLVESLPAHHFQIVLEITERDMLKQ-HEATQLFEWLHSVGVEIAIDDFGTGHSA 424
Cdd:pfam00563  80 LGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARlEALREVLKRLRALGIRIALDDFGTGYSS 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446415521  425 LIYLERFTLDYLKIDRGFINAIGTETVTSPVLDAVLTLSKRLNMLTVAEGVETPEQAKWLRDRGVNFLQGYWISRP 500
Cdd:pfam00563 160 LSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
 
Name Accession Description Interval E-value
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
1-518 0e+00

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 996.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521   1 MFTAANASGRKILLTCFITGLVVAVIISCLQFTVSWHKREVKYDTLITDIKTYLVHYFADLKTSTDKLQPLTLSSCKKAA 80
Cdd:PRK10551   1 MFTRAPSSGRKILLTSIVAGVMIALLFSCLQFLLLWHKREVKYDTLITDVQKYLDTYFADLKSTTDRLQPLTLDTCQQVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521  81 PELTAKAAFSLNVRTFLLVRDKKAFCSSATGNMDIPLAHLVPALDISKDVDIAILPGTPMMPGKPAMVIWYRNPLISNSG 160
Cdd:PRK10551  81 PELTSRAAFSLNVRAFLLVKDKKAFCSSATGEMNTPLSELIPAIDINKPVDMAILPGTPMMPNKPAIVIWYRNPLLKNSG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 161 VFTALNLNLTPYLLYTSRQEDFDGIAMIVGDTVLSTSSSHLLNINELSGPPARQVKVEGIPLTVRLYATEWTWNDLWYAL 240
Cdd:PRK10551 161 VFATLNLNLTPYLLYTSRQEDFDGIALIIGNTALSTFSSRLMNVNELPDMPLRETTIPGYPLTIRLYADSWTANDIWYAL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 241 LLGGMSGIAAGLLCFYILSVRLRPGREILTAIKRDQFYVVYQPAVDTQSLKVTGLEVLLRWRHPVAGEIPPDAFIHYAEA 320
Cdd:PRK10551 241 LLGLLSGILVGLLCYYLLSLRMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 321 QRMIVPLTQHLFELIRRDAHVLQRVLPVGVKFGINIAPDHLHGETFKKDIRQLVESLPAHHFQIVLEITERDMLKQHEAT 400
Cdd:PRK10551 321 QKLIVPLTQHLFELIARDAAELQKVLPVGAKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEEAT 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 401 QLFEWLHSVGVEIAIDDFGTGHSALIYLERFTLDYLKIDRGFINAIGTETVTSPVLDAVLTLSKRLNMLTVAEGVETPEQ 480
Cdd:PRK10551 401 KLFAWLHSQGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQ 480

                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 446415521 481 AKWLRDRGVNFLQGYWISRPLPLNEFVQWLKKPDTPQW 518
Cdd:PRK10551 481 ARWLRERGVNFLQGYWISRPLPLEDFVRWLKEPYTPQW 518
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 10-517 1.60e-107

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: 330.73  E-value: 1.60e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521  10 RKILLTCFITGLVVAVIISCLQFTVSWH---KREVKY-DTLITDIKTYLVHYFADLKTSTDKLQPLTLSSCKKAAPELTA 85
Cdd:COG4943    6 RRLLSLATLLALLAALLPLLLSLWLAQIqarRREREQlESYAQRALARAERVFDQARSALDELNALPGDPCSPAHLAALR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521  86 KAAF-SLNVRTFLLVRDKKAFCSSA---TGNMDIPLAHLVPALDIS--KDVDIAILPGTPM--MPGKPAMVI----WYRN 153
Cdd:COG4943   86 RLVFsSRYVRDIGYVRDGRLLCSSLgklSKPVPLPPPDYVTADGYRlwLNVDNPLDPGRPMliVGRGNYVVVidpaAFID 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 154 PLISNSGVFTALNLNLTPYLLYTsrqedFDGIAMIVGDTVLSTSSSHLLNINELSgppaRQVKVEGIPLTV-------RL 226
Cdd:COG4943  166 VLSPQPGISLALLATNGGHLFAS-----SGNPDPALLSRLLRGPSSWFIQGDRLY----ASACSPQYPICVvaaaplaGL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 227 YATEWTWndLWYALLLGGMSGIAAGLLCFYILSVRLRPGREILTAIKRDQFYVVYQPAVDTQSLKVTGLEVLLRWRHPVA 306
Cdd:COG4943  237 LALWRQL--LLLLLPLGLLLSLLLGLLVLRLLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDG 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 307 GEIPPDAFIHYAEAQRMIVPLTQHLFELIRRDAHVLQRVLPvGVKFGINIAPDHLHGETFKKDIRQLVESLPAHHFQIVL 386
Cdd:COG4943  315 SVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDLLAADP-DFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVL 393

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 387 EITERDMLKQHEATQLFEWLHSVGVEIAIDDFGTGHSALIYLERFTLDYLKIDRGFINAIGTETVTSPVLDAVLTLSKRL 466
Cdd:COG4943  394 EITERGFIDPAKARAVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTL 473

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446415521 467 NMLTVAEGVETPEQAKWLRDRGVNFLQGYWISRPLPLNEFVQWLKKPDTPQ 517
Cdd:COG4943  474 NLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPLPAEEFIAWLAAQRAPA 524
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 266-505 1.18e-91

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 279.87  E-value: 1.18e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521   266 REILTAIKRDQFYVVYQPAVDTQSLKVTGLEVLLRWRHPVAGEIPPDAFIHYAEAQRMIVPLTQHLFELIRRDAHVLQRV 345
Cdd:smart00052   2 RELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQ 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521   346 LPVGVKFGINIAPDHLHGETFKKDIRQLVESLPAHHFQIVLEITERDMLKQ-HEATQLFEWLHSVGVEIAIDDFGTGHSA 424
Cdd:smart00052  82 GPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDdESAVATLQRLRELGVRIALDDFGTGYSS 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521   425 LIYLERFTLDYLKIDRGFINAIGTETVTSPVLDAVLTLSKRLNMLTVAEGVETPEQAKWLRDRGVNFLQGYWISRPLPLN 504
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLD 241


                   .
gi 446415521   505 E 505
Cdd:smart00052 242 D 242
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 266-505 1.74e-86

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: 266.33  E-value: 1.74e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 266 REILTAIKRDQFYVVYQPAVDTQSLKVTGLEVLLRWRHPVAGEIPPDAFIHYAEAQRMIVPLTQHLFELIRRDAHVLQRV 345
Cdd:cd01948    1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 346 LPvGVKFGINIAPDHLHGETFKKDIRQLVESLPAHHFQIVLEITERDMLKQ-HEATQLFEWLHSVGVEIAIDDFGTGHSA 424
Cdd:cd01948   81 GP-DLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDlEEALATLRRLRALGVRIALDDFGTGYSS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 425 LIYLERFTLDYLKIDRGFINAIGTETVTSPVLDAVLTLSKRLNMLTVAEGVETPEQAKWLRDRGVNFLQGYWISRPLPLN 504
Cdd:cd01948  160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239


                 .
gi 446415521 505 E 505
Cdd:cd01948  240 E 240
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 261-511 3.88e-78

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: 255.86  E-value: 3.88e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 261 RLRPGREILTAIKRDQFYVVYQPAVDTQSLKVTGLEVLLRWRHPVAGEIPPDAFIHYAEAQRMIVPLTQHLFELIRRDAH 340
Cdd:COG2200  326 RLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLA 405

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 341 VLQRVLPvGVKFGINIAPDHLHGETFKKDIRQLVESLPAHHFQIVLEITERDMLKQHE-ATQLFEWLHSVGVEIAIDDFG 419
Cdd:COG2200  406 RWPERGL-DLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEaAIELLARLRALGVRIALDDFG 484

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 420 TGHSALIYLERFTLDYLKIDRGFINAIGTETVTSPVLDAVLTLSKRLNMLTVAEGVETPEQAKWLRDRGVNFLQGYWISR 499
Cdd:COG2200  485 TGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGR 564

                        250
                 ....*....|..
gi 446415521 500 PLPLNEFVQWLK 511
Cdd:COG2200  565 PLPLEELEALLR 576
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 266-500 7.24e-78

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: 244.15  E-value: 7.24e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521  266 REILTAIKRDQFYVVYQPAVDTQSLKVTGLEVLLRWRHPVAGEIPPDAFIHYAEAQRMIVPLTQHLFELIRRDahVLQRV 345
Cdd:pfam00563   2 RALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALAD--LAQLQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521  346 LPVGVKFGINIAPDHLHGETFKKDIRQLVESLPAHHFQIVLEITERDMLKQ-HEATQLFEWLHSVGVEIAIDDFGTGHSA 424
Cdd:pfam00563  80 LGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARlEALREVLKRLRALGIRIALDDFGTGYSS 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446415521  425 LIYLERFTLDYLKIDRGFINAIGTETVTSPVLDAVLTLSKRLNMLTVAEGVETPEQAKWLRDRGVNFLQGYWISRP 500
Cdd:pfam00563 160 LSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 266-512 3.04e-77

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: 255.85  E-value: 3.04e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 266 REILTAIKRDQFYVVYQPAVDTQSLKVTGLEVLLRWRHPVAGEIPPDAFIHYAEAQRMIVPLTQHLFELIRRDAHVLQRV 345
Cdd:COG5001  428 ADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDA 507

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 346 LPVGVKFGINIAPDHLHGETFKKDIRQLVES--LPAHHfqIVLEITERDMLKQHEAT-QLFEWLHSVGVEIAIDDFGTGH 422
Cdd:COG5001  508 GLPDLRVAVNLSARQLRDPDLVDRVRRALAEtgLPPSR--LELEITESALLEDPEEAlETLRALRALGVRIALDDFGTGY 585

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 423 SALIYLERFTLDYLKIDRGFINAIGTETVTSPVLDAVLTLSKRLNMLTVAEGVETPEQAKWLRDRGVNFLQGYWISRPLP 502
Cdd:COG5001  586 SSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLP 665

                        250
                 ....*....|
gi 446415521 503 LNEFVQWLKK 512
Cdd:COG5001  666 AEELEALLRA 675
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
271-511 1.08e-42

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 161.39  E-value: 1.08e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 271 AIKRDQFYVVYQPAVDTQSlKVTGLEVLLRWRHPVAGEIPPDAFIHYAEAQRMIVPLTQHLFELIRRDAhVLQRVLPVGV 350
Cdd:PRK10060 416 ALENDQLVIHYQPKITWRG-EVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQV-AKWRDKGINL 493

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 351 KFGINIAPDHLHGETFKKDIRQLVESLPAHHFQIVLEITERDMLK-QHEATQLFEWLHSVGVEIAIDDFGTGHSALIYLE 429
Cdd:PRK10060 494 RVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIEnEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLA 573

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 430 RFTLDYLKIDRGFINAIGTETVTSPVLDAVLTLSKRLNMLTVAEGVETPEQAKWLRDRGVNFLQGYWISRPLPLNEFVQW 509
Cdd:PRK10060 574 RFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERW 653


                 ..
gi 446415521 510 LK 511
Cdd:PRK10060 654 YK 655
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 261-513 1.08e-40

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 155.64  E-value: 1.08e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 261 RLRPGREILTAIKRDQFYVVYQPAVDTQSLKVTGLEVLLRWRHPVAGEIPPDAFIHYAEAQRMIVPLTQHLF-ELIRRDA 339
Cdd:PRK13561 398 RLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLeESCRLLA 477

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 340 HVLQR--VLPVGVkfgiNIAPDHLHGETFKKDIRQLVESLPAHHFQIVLEITE-RDMLKQHEATQLFEWLHSVGVEIAID 416
Cdd:PRK13561 478 AWQERgiMLPLSV----NLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTEsRRIDDPHAAVAILRPLRNAGVRVALD 553

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 417 DFGTGHSALIYLERFT---LDYLKIDRGFINAIGTEtvtSPVLDAVLTLSKRLNMLTVAEGVETPEQAKWLRDRGVNFLQ 493
Cdd:PRK13561 554 DFGMGYAGLRQLQHMKslpIDVLKIDKMFVDGLPED---DSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQ 630

                        250       260
                 ....*....|....*....|.
gi 446415521 494 GYWISRPLPLNEF-VQWLKKP 513
Cdd:PRK13561 631 GFLFARALPIEIFeERYLEEK 651
CSS-motif pfam12792
CSS motif domain associated with EAL; This family with its characteriztic highly conserved CSS ...
 42-241 1.26e-38

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: 139.97  E-value: 1.26e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521   42 KYDTLITDIKTYLVHYFADLKTSTDKLQPLTLSSCKKAA-PELTAKAAFSLNVRTFLLVRDKKAFCSSATGNMDIPLAHL 120
Cdd:pfam12792   4 QLDAFAERALRRLESVLDQADQALDRLLPLTGQPCSPAHlAELRRIVAFSPYVRDVGLVKNGRLYCSSLWGELDTPLPLL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521  121 VPALDISKDVDIAILPGTPMMPGKPAMVIWYRNPLISNS-GVFtaLNLNLTPYLLYTSRQEDFDGIAMIVGDTVLStSSS 199
Cdd:pfam12792  84 PPDLTTPPGVRLWLLRGTPLVPGRPALVLRRGGYGVVIDpGVF--IDVQYLPGLLAAVSQPDGRLLALVVGDDALL-FDG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 446415521  200 HLLNINELSGPPAR-------QVKVEGIPLTVRLYATEWTWNDLWYALL 241
Cdd:pfam12792 161 RLHSLAEPAPGTARsggalyaRARSTRYPLTVVVYAPRASLLANWRQLL 209
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 261-511 5.40e-36

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 142.60  E-value: 5.40e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 261 RLRPGREILTAIKRDQFYVVYQPAVDTQSLKVTGLEVLLRWRHPVAGEIPPDAFIHYAEAQRMIVPLT--------QHLF 332
Cdd:PRK11359 541 RLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGrwviaeacRQLA 620

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 333 ELIRRDAHVlqrvlPVgvkFGINIAPDHLHGETFKKDIRQLVE--SLPAHhfQIVLEITERDMLKQheATQLFEWLHSV- 409
Cdd:PRK11359 621 EWRSQNIHI-----PA---LSVNLSALHFRSNQLPNQVSDAMQawGIDGH--QLTVEITESMMMEH--DTEIFKRIQILr 688

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 410 --GVEIAIDDFGTGHSALIYLERFTLDYLKIDRGFINAIGTETVTSPVLDAVLTLSKRLNMLTVAEGVETPEQAKWLRDR 487
Cdd:PRK11359 689 dmGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKI 768

                        250       260
                 ....*....|....*....|....
gi 446415521 488 GVNFLQGYWISRPLPLNEFVQWLK 511
Cdd:PRK11359 769 HCRVIQGYFFSRPLPAEEIPGWMS 792
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 261-506 1.30e-35

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 140.85  E-value: 1.30e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 261 RLRPGREILTAIKRDQFYVVYQPAVDTQSLKVTGLEVLLRWRHPVAGEIPPDAFIHYAEAQRMIVPLTQHLFELIRRDAH 340
Cdd:PRK11829 403 RLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILA 482

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 341 VLQRvLPVGVKFGINIAPDHLHGETFKkdirQLVESLPAHHF----QIVLEITERDMLKQ-HEATQLFEWLHSVGVEIAI 415
Cdd:PRK11829 483 DWKA-RGVSLPLSVNISGLQVQNKQFL----PHLKTLISHYHidpqQLLLEITETAQIQDlDEALRLLRELQGLGLLIAL 557

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 416 DDFGTGHSALIYL---ERFTLDYLKIDRGFINAIGTETVTSPVLDAVltlSKRLNMLTVAEGVETPEQAKWLRDRGVNFL 492
Cdd:PRK11829 558 DDFGIGYSSLRYLnhlKSLPIHMIKLDKSFVKNLPEDDAIARIISCV---SDVLKVRVMAEGVETEEQRQWLLEHGIQCG 634

                        250
                 ....*....|....
gi 446415521 493 QGYWISRPLPLNEF 506
Cdd:PRK11829 635 QGFLFSPPLPRAEF 648
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 268-507 3.47e-19

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 91.27  E-value: 3.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521  268 ILTAIKRDQFYVVYQPAVDTQSLKVTGLEVLLRWRHPVAGEIPPDAFIHYAEAQRMIVPLTQHLFELIRRDAhvLQRVLP 347
Cdd:PRK09776  846 WRMIKENQLMMLAHGVASPRIPEARNHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFRQA--AKAVAS 923

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521  348 VGVKFGINIAPDHLHGETFKKDIRQLVES--LPAHHfqIVLEITERDMLKQHEATQ-LFEWLHSVGVEIAIDDFGTGHSA 424
Cdd:PRK09776  924 KGLSIALPLSVAGLSSPTLLPFLLEQLENspLPPRL--LHLEITETALLNHAESASrLVQKLRLAGCRVVLSDFGRGLSS 1001

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521  425 LIYLERFTLDYLKIDRGFINAIGTETVTSPVLDAVLTLSKRLNMLTVAEGVETPEQAKWLRDRGVNFLQGYWISRPLPLN 504
Cdd:PRK09776 1002 FNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLD 1081


                  ...
gi 446415521  505 EFV 507
Cdd:PRK09776 1082 LLL 1084
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
 275-503 1.15e-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: 63.28  E-value: 1.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 275 DQFYVVYQPAVDTQsLKVTGLEVLLRwrhPVAGEIPPDAFIHYAEAQRmivpLTQHLFELirrdahVLQRVLPVGVKFgI 354
Cdd:COG3434    2 MDVFVARQPILDRD-QRVVGYELLFR---SGLENSAPDVDGDQATARV----LLNAFLEI------GLDRLLGGKLAF-I 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 355 NIAPDHLHGEtfkkdirqLVESLPAHhfQIVLEITERDmlkqhEATQlfEWLHSV------GVEIAIDDF--GTGHSALI 426
Cdd:COG3434   67 NFTEELLLSD--------LPELLPPE--RVVLEILEDV-----EPDE--ELLEALkelkekGYRIALDDFvlDPEWDPLL 129

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446415521 427 YLerftLDYLKIDrgfINAIGTETvtspvLDAVLTLSKRLNMLTVAEGVETPEQAKWLRDRGVNFLQGYWISRPLPL 503
Cdd:COG3434  130 PL----ADIIKID---VLALDLEE-----LAELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEIL 194
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
 281-506 1.53e-09

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 58.47  E-value: 1.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 281 YQPAVDTqSLKVTGLEVLLRWRHPVAGE--IPPDA-FIHYAEAQRMIVPLTQhlFELIRRDAHVLQRVlpvGVKFGINIA 357
Cdd:PRK11596  34 FQPIYRT-SGRLMAIELLTAVTHPSNPSqrLSPERyFAEITVSHRLDVVKEQ--LDLLAQWADFFVRH---GLLASVNID 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 358 PDHLHGETFKKDIRQLVESLPAHHFqivlEITERDMLKQHE-ATQLFE----WLhsvgveiaiDDFGTG---HSALIYLe 429
Cdd:PRK11596 108 GPTLIALRQQPAILRLIERLPWLRF----ELVEHIRLPKDSpFASMCEfgplWL---------DDFGTGmanFSALSEV- 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446415521 430 RFtlDYLKIDRG-FINAIGTETVTSpVLDAVLTLSKRLNMLTVAEGVETPEQAKWLRDRGVNFLQGYWISRPLPLNEF 506
Cdd:PRK11596 174 RY--DYIKVARElFIMLRQSEEGRN-LFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPAPFETL 248
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 259-504 1.53e-03

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 41.39  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 259 SVRLRPGREilTAIKRDQFYVVYQPAVDTQSlKVTGLEVLLRWRHPVAGEIPPDAFIhyaeaqrmivPLTQHLFELIRRD 338
Cdd:PRK11059 401 SVRWRTLLE--QTLVRGGPRLYQQPAVTRDG-KVHHRELFCRIRDGQGELLSAELFM----------PMVQQLGLSEQYD 467

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 339 AHVLQRVLP-----VGVKFGINIAPDHLHGETFkkdIRQLVESL---PAHHFQ-IVLEITErDMLKQHEA--TQLFEWLH 407
Cdd:PRK11059 468 RQVIERVLPllrywPEENLSINLSVDSLLSRAF---QRWLRDTLlqcPRSQRKrLIFELAE-ADVCQHISrlRPVLRMLR 543

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446415521 408 SVGVEIAIDDFG-----TGhsaliYLERFTLDYLKIDRGFINAIGTET-----VTSpVLDAVltlsKRLNMLTVAEGVET 477
Cdd:PRK11059 544 GLGCRLAVDQAGltvvsTS-----YIKELNVELIKLHPSLVRNIHKRTenqlfVRS-LVGAC----AGTETQVFATGVES 613

                        250       260
                 ....*....|....*....|....*..
gi 446415521 478 PEQAKWLRDRGVNFLQGYWISRPLPLN 504
Cdd:PRK11059 614 REEWQTLQELGVSGGQGDFFAESQPLD 640
 
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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