NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|504697483|ref|WP_014884585|]
View 

MULTISPECIES: cyclic di-GMP phosphodiesterase [Enterobacter]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
1-515 0e+00

cyclic di-GMP phosphodiesterase;


:

Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 938.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483   1 MLTRYFASHRKILFFSIITGLIAAILLGSLQFFWSYHKREIRFDTLIKDVSIYMENYFEELKTSIDVLQPLTLNNCQDVN 80
Cdd:PRK10551   1 MFTRAPSSGRKILLTSIVAGVMIALLFSCLQFLLLWHKREVKYDTLITDVQKYLDTYFADLKSTTDRLQPLTLDTCQQVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483  81 AELTSRAAFSINVRAFLLVRNKMAFCSSATGPMNTPMEELIPELHINKQIDIALLPGTPMLPNRPAIAIWYRNPLVKDGG 160
Cdd:PRK10551  81 PELTSRAAFSLNVRAFLLVKDKKAFCSSATGEMNTPLSELIPAIDINKPVDMAILPGTPMMPNKPAIVIWYRNPLLKNSG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 161 VFTSVNLNLTPYLLYTARQEEFAGIAIIIGDNALSTASSTLVRARDLHQTPARTATLTEVPLTIKLYAREWTSDEILFAL 240
Cdd:PRK10551 161 VFATLNLNLTPYLLYTSRQEDFDGIALIIGNTALSTFSSRLMNVNELPDMPLRETTIPGYPLTIRLYADSWTANDIWYAL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 241 FFGLLCGIAAGSLNFYILTLRLNPGKEILSAIKRGQFYVVYQPVVDTDALQMRGVEVLMRWKHPTMGEIPPDAFINFAEA 320
Cdd:PRK10551 241 LLGLLSGILVGLLCYYLLSLRMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 321 QKLIVPLTLHLFDLIIRDAPVLQTVLPPGAKLGINIAPGHLHAESFKDDMRTFKSLLPPDYFQIVLEITERDMLNHREAS 400
Cdd:PRK10551 321 QKLIVPLTQHLFELIARDAAELQKVLPVGAKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEEAT 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 401 SLFEWLHNEGFEIAIDDFGTGHSALIYLEHFTMDYLKIDRGFVNAIGTETVTSPVLDAVLTLARKLNMLTVAEGVETPEQ 480
Cdd:PRK10551 401 KLFAWLHSQGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQ 480
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 504697483 481 AAWLREHGVHFLQGYWISRPMPLEQFRTWQNKVSS 515
Cdd:PRK10551 481 ARWLRERGVNFLQGYWISRPLPLEDFVRWLKEPYT 515
 
Name Accession Description Interval E-value
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
1-515 0e+00

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 938.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483   1 MLTRYFASHRKILFFSIITGLIAAILLGSLQFFWSYHKREIRFDTLIKDVSIYMENYFEELKTSIDVLQPLTLNNCQDVN 80
Cdd:PRK10551   1 MFTRAPSSGRKILLTSIVAGVMIALLFSCLQFLLLWHKREVKYDTLITDVQKYLDTYFADLKSTTDRLQPLTLDTCQQVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483  81 AELTSRAAFSINVRAFLLVRNKMAFCSSATGPMNTPMEELIPELHINKQIDIALLPGTPMLPNRPAIAIWYRNPLVKDGG 160
Cdd:PRK10551  81 PELTSRAAFSLNVRAFLLVKDKKAFCSSATGEMNTPLSELIPAIDINKPVDMAILPGTPMMPNKPAIVIWYRNPLLKNSG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 161 VFTSVNLNLTPYLLYTARQEEFAGIAIIIGDNALSTASSTLVRARDLHQTPARTATLTEVPLTIKLYAREWTSDEILFAL 240
Cdd:PRK10551 161 VFATLNLNLTPYLLYTSRQEDFDGIALIIGNTALSTFSSRLMNVNELPDMPLRETTIPGYPLTIRLYADSWTANDIWYAL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 241 FFGLLCGIAAGSLNFYILTLRLNPGKEILSAIKRGQFYVVYQPVVDTDALQMRGVEVLMRWKHPTMGEIPPDAFINFAEA 320
Cdd:PRK10551 241 LLGLLSGILVGLLCYYLLSLRMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 321 QKLIVPLTLHLFDLIIRDAPVLQTVLPPGAKLGINIAPGHLHAESFKDDMRTFKSLLPPDYFQIVLEITERDMLNHREAS 400
Cdd:PRK10551 321 QKLIVPLTQHLFELIARDAAELQKVLPVGAKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEEAT 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 401 SLFEWLHNEGFEIAIDDFGTGHSALIYLEHFTMDYLKIDRGFVNAIGTETVTSPVLDAVLTLARKLNMLTVAEGVETPEQ 480
Cdd:PRK10551 401 KLFAWLHSQGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQ 480
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 504697483 481 AAWLREHGVHFLQGYWISRPMPLEQFRTWQNKVSS 515
Cdd:PRK10551 481 ARWLRERGVNFLQGYWISRPLPLEDFVRWLKEPYT 515
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
9-509 9.24e-109

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: 333.81  E-value: 9.24e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483   9 HRKILFFSIITGLIAAIL--LGSLQFFWSYHKREIRF--DTLIKDVSIYMENYFEELKTSIDVLQPLTLNNCQDVNAELT 84
Cdd:COG4943    5 RRRLLSLATLLALLAALLplLLSLWLAQIQARRREREqlESYAQRALARAERVFDQARSALDELNALPGDPCSPAHLAAL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483  85 SRAAFSI-NVRAFLLVRNKMAFCSSAtGPMNTPMEELIPELHINKQIDIALLPGTPMLPNRPAIAIWYRNPLVK-DGGVF 162
Cdd:COG4943   85 RRLVFSSrYVRDIGYVRDGRLLCSSL-GKLSKPVPLPPPDYVTADGYRLWLNVDNPLDPGRPMLIVGRGNYVVViDPAAF 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 163 TSVNLNLTPY---LLYTARQEEFAGIaiiigDNALSTASSTLVRARD--LHQTPARTATLTEVPLTIKLYARE------- 230
Cdd:COG4943  164 IDVLSPQPGIslaLLATNGGHLFASS-----GNPDPALLSRLLRGPSswFIQGDRLYASACSPQYPICVVAAAplaglla 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 231 -WTsDEILFALFFGLLCGIAAGSLNFYILTLRLNPGKEILSAIKRGQFYVVYQPVVDTDALQMRGVEVLMRWKHPTMGEI 309
Cdd:COG4943  239 lWR-QLLLLLLPLGLLLSLLLGLLVLRLLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVI 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 310 PPDAFINFAEAQKLIVPLTLHLFDLIIRD-APVLQTvlPPGAKLGINIAPGHLHAESFKDDMRTFKSLLPPDYFQIVLEI 388
Cdd:COG4943  318 SPDIFIPLAEQSGLISPLTRQVIEQVFRDlGDLLAA--DPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEI 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 389 TERDMLNHREASSLFEWLHNEGFEIAIDDFGTGHSALIYLEHFTMDYLKIDRGFVNAIGTETVTSPVLDAVLTLARKLNM 468
Cdd:COG4943  396 TERGFIDPAKARAVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNL 475
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 504697483 469 LTVAEGVETPEQAAWLREHGVHFLQGYWISRPMPLEQFRTW 509
Cdd:COG4943  476 DVVAEGVETEEQADYLRARGVQYGQGWLFAKPLPAEEFIAW 516
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
267-505 4.60e-87

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 267.93  E-value: 4.60e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483   267 EILSAIKRGQFYVVYQPVVDTDALQMRGVEVLMRWKHPTMGEIPPDAFINFAEAQKLIVPLTLHLFDLIIRDAPVLQTVL 346
Cdd:smart00052   3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483   347 PPGAKLGINIAPGHLHAESFKDDMRTFKSLLPPDYFQIVLEITERDMLNH-REASSLFEWLHNEGFEIAIDDFGTGHSAL 425
Cdd:smart00052  83 PPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDdESAVATLQRLRELGVRIALDDFGTGYSSL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483   426 IYLEHFTMDYLKIDRGFVNAIGTETVTSPVLDAVLTLARKLNMLTVAEGVETPEQAAWLREHGVHFLQGYWISRPMPLEQ 505
Cdd:smart00052 163 SYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLDD 242
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
267-505 2.68e-84

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: 260.94  E-value: 2.68e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 267 EILSAIKRGQFYVVYQPVVDTDALQMRGVEVLMRWKHPTMGEIPPDAFINFAEAQKLIVPLTLHLFDLIIRDAPVLQTVL 346
Cdd:cd01948    2 DLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 347 PPGaKLGINIAPGHLHAESFKDDMRTF--KSLLPPDyfQIVLEITERDMLNHRE-ASSLFEWLHNEGFEIAIDDFGTGHS 423
Cdd:cd01948   82 PDL-RLSVNLSARQLRDPDFLDRLLELlaETGLPPR--RLVLEITESALIDDLEeALATLRRLRALGVRIALDDFGTGYS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 424 ALIYLEHFTMDYLKIDRGFVNAIGTETVTSPVLDAVLTLARKLNMLTVAEGVETPEQAAWLREHGVHFLQGYWISRPMPL 503
Cdd:cd01948  159 SLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPA 238

                 ..
gi 504697483 504 EQ 505
Cdd:cd01948  239 EE 240
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
267-500 2.87e-71

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: 226.82  E-value: 2.87e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483  267 EILSAIKRGQFYVVYQPVVDTDALQMRGVEVLMRWKHPTMGEIPPDAFINFAEAQKLIVPLTLHLFDLIIRDapVLQTVL 346
Cdd:pfam00563   3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALAD--LAQLQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483  347 PPGAKLGINIAPGHLHAESFKDDMRTFKSLLPPDYFQIVLEITERDMLNHRE-ASSLFEWLHNEGFEIAIDDFGTGHSAL 425
Cdd:pfam00563  81 GPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEaLREVLKRLRALGIRIALDDFGTGYSSL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504697483  426 IYLEHFTMDYLKIDRGFVNAIGTETVTSPVLDAVLTLARKLNMLTVAEGVETPEQAAWLREHGVHFLQGYWISRP 500
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
 
Name Accession Description Interval E-value
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
1-515 0e+00

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 938.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483   1 MLTRYFASHRKILFFSIITGLIAAILLGSLQFFWSYHKREIRFDTLIKDVSIYMENYFEELKTSIDVLQPLTLNNCQDVN 80
Cdd:PRK10551   1 MFTRAPSSGRKILLTSIVAGVMIALLFSCLQFLLLWHKREVKYDTLITDVQKYLDTYFADLKSTTDRLQPLTLDTCQQVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483  81 AELTSRAAFSINVRAFLLVRNKMAFCSSATGPMNTPMEELIPELHINKQIDIALLPGTPMLPNRPAIAIWYRNPLVKDGG 160
Cdd:PRK10551  81 PELTSRAAFSLNVRAFLLVKDKKAFCSSATGEMNTPLSELIPAIDINKPVDMAILPGTPMMPNKPAIVIWYRNPLLKNSG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 161 VFTSVNLNLTPYLLYTARQEEFAGIAIIIGDNALSTASSTLVRARDLHQTPARTATLTEVPLTIKLYAREWTSDEILFAL 240
Cdd:PRK10551 161 VFATLNLNLTPYLLYTSRQEDFDGIALIIGNTALSTFSSRLMNVNELPDMPLRETTIPGYPLTIRLYADSWTANDIWYAL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 241 FFGLLCGIAAGSLNFYILTLRLNPGKEILSAIKRGQFYVVYQPVVDTDALQMRGVEVLMRWKHPTMGEIPPDAFINFAEA 320
Cdd:PRK10551 241 LLGLLSGILVGLLCYYLLSLRMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 321 QKLIVPLTLHLFDLIIRDAPVLQTVLPPGAKLGINIAPGHLHAESFKDDMRTFKSLLPPDYFQIVLEITERDMLNHREAS 400
Cdd:PRK10551 321 QKLIVPLTQHLFELIARDAAELQKVLPVGAKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEEAT 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 401 SLFEWLHNEGFEIAIDDFGTGHSALIYLEHFTMDYLKIDRGFVNAIGTETVTSPVLDAVLTLARKLNMLTVAEGVETPEQ 480
Cdd:PRK10551 401 KLFAWLHSQGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQ 480
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 504697483 481 AAWLREHGVHFLQGYWISRPMPLEQFRTWQNKVSS 515
Cdd:PRK10551 481 ARWLRERGVNFLQGYWISRPLPLEDFVRWLKEPYT 515
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
9-509 9.24e-109

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: 333.81  E-value: 9.24e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483   9 HRKILFFSIITGLIAAIL--LGSLQFFWSYHKREIRF--DTLIKDVSIYMENYFEELKTSIDVLQPLTLNNCQDVNAELT 84
Cdd:COG4943    5 RRRLLSLATLLALLAALLplLLSLWLAQIQARRREREqlESYAQRALARAERVFDQARSALDELNALPGDPCSPAHLAAL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483  85 SRAAFSI-NVRAFLLVRNKMAFCSSAtGPMNTPMEELIPELHINKQIDIALLPGTPMLPNRPAIAIWYRNPLVK-DGGVF 162
Cdd:COG4943   85 RRLVFSSrYVRDIGYVRDGRLLCSSL-GKLSKPVPLPPPDYVTADGYRLWLNVDNPLDPGRPMLIVGRGNYVVViDPAAF 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 163 TSVNLNLTPY---LLYTARQEEFAGIaiiigDNALSTASSTLVRARD--LHQTPARTATLTEVPLTIKLYARE------- 230
Cdd:COG4943  164 IDVLSPQPGIslaLLATNGGHLFASS-----GNPDPALLSRLLRGPSswFIQGDRLYASACSPQYPICVVAAAplaglla 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 231 -WTsDEILFALFFGLLCGIAAGSLNFYILTLRLNPGKEILSAIKRGQFYVVYQPVVDTDALQMRGVEVLMRWKHPTMGEI 309
Cdd:COG4943  239 lWR-QLLLLLLPLGLLLSLLLGLLVLRLLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVI 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 310 PPDAFINFAEAQKLIVPLTLHLFDLIIRD-APVLQTvlPPGAKLGINIAPGHLHAESFKDDMRTFKSLLPPDYFQIVLEI 388
Cdd:COG4943  318 SPDIFIPLAEQSGLISPLTRQVIEQVFRDlGDLLAA--DPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEI 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 389 TERDMLNHREASSLFEWLHNEGFEIAIDDFGTGHSALIYLEHFTMDYLKIDRGFVNAIGTETVTSPVLDAVLTLARKLNM 468
Cdd:COG4943  396 TERGFIDPAKARAVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNL 475
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 504697483 469 LTVAEGVETPEQAAWLREHGVHFLQGYWISRPMPLEQFRTW 509
Cdd:COG4943  476 DVVAEGVETEEQADYLRARGVQYGQGWLFAKPLPAEEFIAW 516
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
267-505 4.60e-87

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 267.93  E-value: 4.60e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483   267 EILSAIKRGQFYVVYQPVVDTDALQMRGVEVLMRWKHPTMGEIPPDAFINFAEAQKLIVPLTLHLFDLIIRDAPVLQTVL 346
Cdd:smart00052   3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483   347 PPGAKLGINIAPGHLHAESFKDDMRTFKSLLPPDYFQIVLEITERDMLNH-REASSLFEWLHNEGFEIAIDDFGTGHSAL 425
Cdd:smart00052  83 PPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDdESAVATLQRLRELGVRIALDDFGTGYSSL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483   426 IYLEHFTMDYLKIDRGFVNAIGTETVTSPVLDAVLTLARKLNMLTVAEGVETPEQAAWLREHGVHFLQGYWISRPMPLEQ 505
Cdd:smart00052 163 SYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLDD 242
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
267-505 2.68e-84

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: 260.94  E-value: 2.68e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 267 EILSAIKRGQFYVVYQPVVDTDALQMRGVEVLMRWKHPTMGEIPPDAFINFAEAQKLIVPLTLHLFDLIIRDAPVLQTVL 346
Cdd:cd01948    2 DLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 347 PPGaKLGINIAPGHLHAESFKDDMRTF--KSLLPPDyfQIVLEITERDMLNHRE-ASSLFEWLHNEGFEIAIDDFGTGHS 423
Cdd:cd01948   82 PDL-RLSVNLSARQLRDPDFLDRLLELlaETGLPPR--RLVLEITESALIDDLEeALATLRRLRALGVRIALDDFGTGYS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 424 ALIYLEHFTMDYLKIDRGFVNAIGTETVTSPVLDAVLTLARKLNMLTVAEGVETPEQAAWLREHGVHFLQGYWISRPMPL 503
Cdd:cd01948  159 SLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPA 238

                 ..
gi 504697483 504 EQ 505
Cdd:cd01948  239 EE 240
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
271-509 4.83e-75

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: 250.08  E-value: 4.83e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 271 AIKRGQFYVVYQPVVDTDALQMRGVEVLMRWKHPTMGEIPPDAFINFAEAQKLIVPLTLHLFDLIIRDAPVLQTVLPPGA 350
Cdd:COG5001  433 ALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPDL 512
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 351 KLGINIAPGHLHAESFKDDMRTF--KSLLPPDyfQIVLEITERDMLNHRE-ASSLFEWLHNEGFEIAIDDFGTGHSALIY 427
Cdd:COG5001  513 RVAVNLSARQLRDPDLVDRVRRAlaETGLPPS--RLELEITESALLEDPEeALETLRALRALGVRIALDDFGTGYSSLSY 590
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 428 LEHFTMDYLKIDRGFVNAIGTETVTSPVLDAVLTLARKLNMLTVAEGVETPEQAAWLREHGVHFLQGYWISRPMPLEQFR 507
Cdd:COG5001  591 LKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELE 670

                 ..
gi 504697483 508 TW 509
Cdd:COG5001  671 AL 672
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
266-509 1.05e-74

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: 246.62  E-value: 1.05e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 266 KEILSAIKRGQFYVVYQPVVDTDALQMRGVEVLMRWKHPTMGEIPPDAFINFAEAQKLIVPLTLHLFDLIIRDAPVLQTV 345
Cdd:COG2200  331 SELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPER 410
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 346 LPPGaKLGINIAPGHLHAESFKDDMRTFKSLLPPDYFQIVLEITERDMLNHRE-ASSLFEWLHNEGFEIAIDDFGTGHSA 424
Cdd:COG2200  411 GLDL-RLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEaAIELLARLRALGVRIALDDFGTGYSS 489
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 425 LIYLEHFTMDYLKIDRGFVNAIGTETVTSPVLDAVLTLARKLNMLTVAEGVETPEQAAWLREHGVHFLQGYWISRPMPLE 504
Cdd:COG2200  490 LSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLE 569

                 ....*
gi 504697483 505 QFRTW 509
Cdd:COG2200  570 ELEAL 574
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
267-500 2.87e-71

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: 226.82  E-value: 2.87e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483  267 EILSAIKRGQFYVVYQPVVDTDALQMRGVEVLMRWKHPTMGEIPPDAFINFAEAQKLIVPLTLHLFDLIIRDapVLQTVL 346
Cdd:pfam00563   3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALAD--LAQLQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483  347 PPGAKLGINIAPGHLHAESFKDDMRTFKSLLPPDYFQIVLEITERDMLNHRE-ASSLFEWLHNEGFEIAIDDFGTGHSAL 425
Cdd:pfam00563  81 GPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEaLREVLKRLRALGIRIALDDFGTGYSSL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504697483  426 IYLEHFTMDYLKIDRGFVNAIGTETVTSPVLDAVLTLARKLNMLTVAEGVETPEQAAWLREHGVHFLQGYWISRP 500
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
271-509 1.19e-40

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 155.61  E-value: 1.19e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 271 AIKRGQFYVVYQPVVDTDAlQMRGVEVLMRWKHPTMGEIPPDAFINFAEAQKLIVPLTLHlfdliirdapVLQTVLPPGA 350
Cdd:PRK10060 416 ALENDQLVIHYQPKITWRG-EVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRW----------VMLDVVRQVA 484
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 351 K-----LGINIAPgHLHAESFKDD--MRTFKSLLPP---DYFQIVLEITERDML-NHREASSLFEWLHNEGFEIAIDDFG 419
Cdd:PRK10060 485 KwrdkgINLRVAV-NVSARQLADQtiFTALKQALQElnfEYCPIDVELTESCLIeNEELALSVIQQFSQLGAQVHLDDFG 563
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 420 TGHSALIYLEHFTMDYLKIDRGFVNAIGTETVTSPVLDAVLTLARKLNMLTVAEGVETPEQAAWLREHGVHFLQGYWISR 499
Cdd:PRK10060 564 TGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAK 643
                        250
                 ....*....|
gi 504697483 500 PMPLEQFRTW 509
Cdd:PRK10060 644 PMPAVAFERW 653
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
261-506 3.55e-36

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 142.39  E-value: 3.55e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 261 RLNPGKEILSAIKRGQFYVVYQPVVDTDALQMRGVEVLMRWKHPTMGEIPPDAFINFAEAQKLIVPLTLHLFDLIIR--- 337
Cdd:PRK11829 403 RLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRila 482
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 338 DAPVLQTVLPpgakLGINIAPGHLHAESFKDDMRTFKSLLPPDYFQIVLEITERDMLNH-REASSLFEWLHNEGFEIAID 416
Cdd:PRK11829 483 DWKARGVSLP----LSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDlDEALRLLRELQGLGLLIALD 558
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 417 DFGTGHSALIYLEHFT---MDYLKIDRGFVNAIGTETVTSPVLDAVltlARKLNMLTVAEGVETPEQAAWLREHGVHFLQ 493
Cdd:PRK11829 559 DFGIGYSSLRYLNHLKslpIHMIKLDKSFVKNLPEDDAIARIISCV---SDVLKVRVMAEGVETEEQRQWLLEHGIQCGQ 635
                        250
                 ....*....|...
gi 504697483 494 GYWISRPMPLEQF 506
Cdd:PRK11829 636 GFLFSPPLPRAEF 648
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
261-506 5.56e-35

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 139.08  E-value: 5.56e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 261 RLNPGKEILSAIKRGQFYVVYQPVVDTDALQMRGVEVLMRWKHPTMGEIPPDAFINFAEAQKLIVPLTLHLFDLIIRDAP 340
Cdd:PRK13561 398 RLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLA 477
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 341 VLQ---TVLPpgakLGINIAPGHLHAESFKDDMrtfKSLLppDYFQI-----VLEITE-RDMLNHREASSLFEWLHNEGF 411
Cdd:PRK13561 478 AWQergIMLP----LSVNLSALQLMHPNMVADM---LELL--TRYRIqpgtlILEVTEsRRIDDPHAAVAILRPLRNAGV 548
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 412 EIAIDDFGTGHSALIYLEHFT---MDYLKIDRGFVNAIGTEtvtSPVLDAVLTLARKLNMLTVAEGVETPEQAAWLREHG 488
Cdd:PRK13561 549 RVALDDFGMGYAGLRQLQHMKslpIDVLKIDKMFVDGLPED---DSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAG 625
                        250
                 ....*....|....*...
gi 504697483 489 VHFLQGYWISRPMPLEQF 506
Cdd:PRK13561 626 VGIAQGFLFARALPIEIF 643
CSS-motif pfam12792
CSS motif domain associated with EAL; This family with its characteriztic highly conserved CSS ...
42-232 1.23e-33

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: 126.49  E-value: 1.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483   42 RFDTLIKDVSIYMENYFEELKTSIDVLQPLTLNNCQDVN-AELTSRAAFSINVRAFLLVRNKMAFCSSATGPMNTPMEEL 120
Cdd:pfam12792   4 QLDAFAERALRRLESVLDQADQALDRLLPLTGQPCSPAHlAELRRIVAFSPYVRDVGLVKNGRLYCSSLWGELDTPLPLL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483  121 IPELHINKQIDIALLPGTPMLPNRPAIAIWYRNPLVK-DGGVFtsVNLNLTPYLLYTARQEEFAGIAIIIGDNALStASS 199
Cdd:pfam12792  84 PPDLTTPPGVRLWLLRGTPLVPGRPALVLRRGGYGVViDPGVF--IDVQYLPGLLAAVSQPDGRLLALVVGDDALL-FDG 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 504697483  200 TLVRARDLHQTPAR-------TATLTEVPLTIKLYAREWT 232
Cdd:pfam12792 161 RLHSLAEPAPGTARsggalyaRARSTRYPLTVVVYAPRAS 200
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
261-514 1.84e-33

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 134.90  E-value: 1.84e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 261 RLNPGKEILSAIKRGQFYVVYQPVVDTDALQMRGVEVLMRWKHPTMGEIPPDAFINFAEAQKLIVPLTLHLFDLIIRDAP 340
Cdd:PRK11359 541 RLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLA 620
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 341 VLQTVLPPGAKLGINIAPGHLHAESFKDDMRTFKSLLPPDYFQIVLEITERDMLNH-REASSLFEWLHNEGFEIAIDDFG 419
Cdd:PRK11359 621 EWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHdTEIFKRIQILRDMGVGLSVDDFG 700
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 420 TGHSALIYLEHFTMDYLKIDRGFVNAIGTETVTSPVLDAVLTLARKLNMLTVAEGVETPEQAAWLREHGVHFLQGYWISR 499
Cdd:PRK11359 701 TGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSR 780
                        250
                 ....*....|....*
gi 504697483 500 PMPLEQFRTWQNKVS 514
Cdd:PRK11359 781 PLPAEEIPGWMSSVL 795
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
295-506 1.53e-19

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 92.43  E-value: 1.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483  295 VEVLMRWKHPTMGEIPPDAFINFAEAQKLIVPLTLHLFDLIIRDAPvlQTVLPPGAKLGINIAPGHLHAESFKDDM--RT 372
Cdd:PRK09776  873 WLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFRQAA--KAVASKGLSIALPLSVAGLSSPTLLPFLleQL 950
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483  373 FKSLLPPDyfQIVLEITERDMLNHRE-ASSLFEWLHNEGFEIAIDDFGTGHSALIYLEHFTMDYLKIDRGFVNAIGTETV 451
Cdd:PRK09776  951 ENSPLPPR--LLHLEITETALLNHAEsASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLM 1028
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 504697483  452 TSPVLDAVLTLARKLNMLTVAEGVETPEQAAWLREHGVHFLQGYWISRPMPLEQF 506
Cdd:PRK09776 1029 DEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLL 1083
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
276-505 4.58e-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: 70.99  E-value: 4.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 276 QFYVVYQPVVDTDaLQMRGVEVLMRwkhPTMGEIPPDAFINFAEAQkLIVPLTLHL-FDLIIRDAPVLqtvlppgaklgI 354
Cdd:COG3434    3 DVFVARQPILDRD-QRVVGYELLFR---SGLENSAPDVDGDQATAR-VLLNAFLEIgLDRLLGGKLAF-----------I 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 355 NIAPGHLHAESFkddmrtfkSLLPPDyfQIVLEITERDMLNHREASSLFEwLHNEGFEIAIDDF--GTGHSALIYLehft 432
Cdd:COG3434   67 NFTEELLLSDLP--------ELLPPE--RVVLEILEDVEPDEELLEALKE-LKEKGYRIALDDFvlDPEWDPLLPL---- 131
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504697483 433 MDYLKIDrgfVNAIGTETvtspvLDAVLTLARKLNMLTVAEGVETPEQAAWLREHGVHFLQGYWISRPMPLEQ 505
Cdd:COG3434  132 ADIIKID---VLALDLEE-----LAELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEILKG 196
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
281-508 1.61e-07

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 52.70  E-value: 1.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 281 YQPVVDTDALQMrGVEVLMRWKHPTMGE--IPPDA-FINFAEAQKL-IVPLTLHLF----DLIIRDapvlqtvlppGAKL 352
Cdd:PRK11596  34 FQPIYRTSGRLM-AIELLTAVTHPSNPSqrLSPERyFAEITVSHRLdVVKEQLDLLaqwaDFFVRH----------GLLA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 353 GINIAPGHLHAESFKDDMRTFKSLLPPDYFQIVLEIterDMLNHREASSLFE----WLhnegfeiaiDDFGTG---HSAL 425
Cdd:PRK11596 103 SVNIDGPTLIALRQQPAILRLIERLPWLRFELVEHI---RLPKDSPFASMCEfgplWL---------DDFGTGmanFSAL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697483 426 IYLEHftmDYLKIDRG-FVNAIGTETVTSpVLDAVLTLARKLNMLTVAEGVETPEQAAWLREHGVHFLQGYWISRPMPLE 504
Cdd:PRK11596 171 SEVRY---DYIKVARElFIMLRQSEEGRN-LFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPAPFE 246

                 ....
gi 504697483 505 QFRT 508
Cdd:PRK11596 247 TLET 250
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH