NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|491003105|ref|WP_004864826|]
View 

MULTISPECIES: cyclic di-GMP phosphodiesterase [Raoultella]

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;
1-513 0e+00

cyclic di-GMP phosphodiesterase;


:

Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 874.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105   1 MLTRYLSPRRNIWLTSILIGVIVALLAGSIQVMVIYHSRSERFDSIIDNVNVYLTDYFSQLEKTMADLQPLVDQKCENIA 80
Cdd:PRK10551   1 MFTRAPSSGRKILLTSIVAGVMIALLFSCLQFLLLWHKREVKYDTLITDVQKYLDTYFADLKSTTDRLQPLTLDTCQQVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105  81 SGLTARAAFSPNVRAFLLVKDGVAFCSSATGPMNTPLVQLIPHLDTHKAVDMLLLPGTPMMPGNAALAMWVRNPHGGNDG 160
Cdd:PRK10551  81 PELTSRAAFSLNVRAFLLVKDKKAFCSSATGEMNTPLSELIPAIDINKPVDMAILPGTPMMPNKPAIVIWYRNPLLKNSG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 161 VFVSINTNLTPYILYSARQNDFSSIALVVNDTALSTLTNRLIDPQSLHAEPIRQIQIKGVPLKVYLYANSWLSENTQFSL 240
Cdd:PRK10551 161 VFATLNLNLTPYLLYTSRQEDFDGIALIIGNTALSTFSSRLMNVNELPDMPLRETTIPGYPLTIRLYADSWTANDIWYAL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 241 LLGVMCGLLAGLVSYYVLTLKSDPRKAILLGIKNNQFYVVYQPVVKADTLRISGIEVLMRWRHPVAGEIPPDVFINLAET 320
Cdd:PRK10551 241 LLGLLSGILVGLLCYYLLSLRMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 321 QQVIVPLTHHLLALIARDAPALQKVLPAGSKLGLNISPSHLHADEFQDDLRQFAASMPANHFNVVLEITERAMIDKNKSL 400
Cdd:PRK10551 321 QKLIVPLTQHLFELIARDAAELQKVLPVGAKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEEAT 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 401 AIFDWLHEQGFEIAIDDFGTGHSALIYLERYKFDYLKIDRGFVQAIGTETVTSPVLDAVLTLSRRLQLMTVAEGVETPEQ 480
Cdd:PRK10551 401 KLFAWLHSQGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQ 480

                        490       500       510
                 ....*....|....*....|....*....|...
gi 491003105 481 AEWLRKHGVNFLQGYWLSRPLPLEELIAAHDEP 513
Cdd:PRK10551 481 ARWLRERGVNFLQGYWISRPLPLEDFVRWLKEP 513
 
Name Accession Description Interval E-value
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
1-513 0e+00

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 874.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105   1 MLTRYLSPRRNIWLTSILIGVIVALLAGSIQVMVIYHSRSERFDSIIDNVNVYLTDYFSQLEKTMADLQPLVDQKCENIA 80
Cdd:PRK10551   1 MFTRAPSSGRKILLTSIVAGVMIALLFSCLQFLLLWHKREVKYDTLITDVQKYLDTYFADLKSTTDRLQPLTLDTCQQVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105  81 SGLTARAAFSPNVRAFLLVKDGVAFCSSATGPMNTPLVQLIPHLDTHKAVDMLLLPGTPMMPGNAALAMWVRNPHGGNDG 160
Cdd:PRK10551  81 PELTSRAAFSLNVRAFLLVKDKKAFCSSATGEMNTPLSELIPAIDINKPVDMAILPGTPMMPNKPAIVIWYRNPLLKNSG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 161 VFVSINTNLTPYILYSARQNDFSSIALVVNDTALSTLTNRLIDPQSLHAEPIRQIQIKGVPLKVYLYANSWLSENTQFSL 240
Cdd:PRK10551 161 VFATLNLNLTPYLLYTSRQEDFDGIALIIGNTALSTFSSRLMNVNELPDMPLRETTIPGYPLTIRLYADSWTANDIWYAL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 241 LLGVMCGLLAGLVSYYVLTLKSDPRKAILLGIKNNQFYVVYQPVVKADTLRISGIEVLMRWRHPVAGEIPPDVFINLAET 320
Cdd:PRK10551 241 LLGLLSGILVGLLCYYLLSLRMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 321 QQVIVPLTHHLLALIARDAPALQKVLPAGSKLGLNISPSHLHADEFQDDLRQFAASMPANHFNVVLEITERAMIDKNKSL 400
Cdd:PRK10551 321 QKLIVPLTQHLFELIARDAAELQKVLPVGAKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEEAT 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 401 AIFDWLHEQGFEIAIDDFGTGHSALIYLERYKFDYLKIDRGFVQAIGTETVTSPVLDAVLTLSRRLQLMTVAEGVETPEQ 480
Cdd:PRK10551 401 KLFAWLHSQGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQ 480

                        490       500       510
                 ....*....|....*....|....*....|...
gi 491003105 481 AEWLRKHGVNFLQGYWLSRPLPLEELIAAHDEP 513
Cdd:PRK10551 481 ARWLRERGVNFLQGYWISRPLPLEDFVRWLKEP 513
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 4-515 1.54e-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: 1.54e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105   4 RYLSPRRNIWLTSILIGVIVALLAGSIQVMVIYHSRSERF-DSIIDNVNvyltDYFSQLEKTMADLQPLVDQKC--ENIA 80
Cdd:COG4943    7 RLLSLATLLALLAALLPLLLSLWLAQIQARRREREQLESYaQRALARAE----RVFDQARSALDELNALPGDPCspAHLA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105  81 SgLTARAAFSPNVRAFLLVKDGVAFCSSAtGPMNTPLVQLIPHLDTHKAVDMLLLPGTPMMPGNAALAMwvrnphgGNDG 160
Cdd:COG4943   83 A-LRRLVFSSRYVRDIGYVRDGRLLCSSL-GKLSKPVPLPPPDYVTADGYRLWLNVDNPLDPGRPMLIV-------GRGN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 161 VFVSINTNLtpYILYSARQNDFSSIALVVNDTALSTLTNR--LIDPQSLHAEPIRQIQIKGV----------PLKVYLYA 228
Cdd:COG4943  154 YVVVIDPAA--FIDVLSPQPGISLALLATNGGHLFASSGNpdPALLSRLLRGPSSWFIQGDRlyasacspqyPICVVAAA 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 229 NS--WLSENTQ---FSLLLGVMCGLLAG-LVSYYVLTLKSdPRKAILLGIKNNQFYVVYQPVVKADTLRISGIEVLMRWR 302
Cdd:COG4943  232 PLagLLALWRQlllLLLPLGLLLSLLLGlLVLRLLRRRLS-PRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWR 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 303 HPVAGEIPPDVFINLAETQQVIVPLTHHLLALIARDapaLQKVLPA--GSKLGLNISPSHLHADEFQDDLRQFAASMPAN 380
Cdd:COG4943  311 DPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRD---LGDLLAAdpDFHISINLSASDLLSPRFLDDLERLLARTGVA 387

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 381 HFNVVLEITERAMIDKNKSLAIFDWLHEQGFEIAIDDFGTGHSALIYLERYKFDYLKIDRGFVQAIGTETVTSPVLDAVL 460
Cdd:COG4943  388 PQQIVLEITERGFIDPAKARAVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHII 467

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491003105 461 TLSRRLQLMTVAEGVETPEQAEWLRKHGVNFLQGYWLSRPLPLEELIAAHDEPAK 515
Cdd:COG4943  468 EMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPLPAEEFIAWLAAQRA 522
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 267-505 1.33e-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: 266.72  E-value: 1.33e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 267 AILLGIKNNQFYVVYQPVVKADTLRISGIEVLMRWRHPVAGEIPPDVFINLAETQQVIVPLTHHLLALIARDAPALQKVL 346
Cdd:cd01948    2 DLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 347 PAGsKLGLNISPSHLHADEFQDDLRQFAASMPANHFNVVLEITERAMI-DKNKSLAIFDWLHEQGFEIAIDDFGTGHSAL 425
Cdd:cd01948   82 PDL-RLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIdDLEEALATLRRLRALGVRIALDDFGTGYSSL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 426 IYLERYKFDYLKIDRGFVQAIGTETVTSPVLDAVLTLSRRLQLMTVAEGVETPEQAEWLRKHGVNFLQGYWLSRPLPLEE 505
Cdd:cd01948  161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 267-505 3.81e-84

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 260.61  E-value: 3.81e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105   267 AILLGIKNNQFYVVYQPVVKADTLRISGIEVLMRWRHPVAGEIPPDVFINLAETQQVIVPLTHHLLALIARDAPALQKVL 346
Cdd:smart00052   3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105   347 PAGSKLGLNISPSHLHADEFQDDLRQFAASMPANHFNVVLEITERAMIDKNKS-LAIFDWLHEQGFEIAIDDFGTGHSAL 425
Cdd:smart00052  83 PPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESaVATLQRLRELGVRIALDDFGTGYSSL 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105   426 IYLERYKFDYLKIDRGFVQAIGTETVTSPVLDAVLTLSRRLQLMTVAEGVETPEQAEWLRKHGVNFLQGYWLSRPLPLEE 505
Cdd:smart00052 163 SYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLDD 242
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 265-500 9.21e-70

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: 222.96  E-value: 9.21e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105  265 RKAILLGIKNNQFYVVYQPVVKADTLRISGIEVLMRWRHPVAGEIPPDVFINLAETQQVIVPLTHHLLALIARDApaLQK 344
Cdd:pfam00563   1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADL--AQL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105  345 VLPAGSKLGLNISPSHLHADEFQDDLRQFAASMPANHFNVVLEITERAMIDKNKSL-AIFDWLHEQGFEIAIDDFGTGHS 423
Cdd:pfam00563  79 QLGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALrEVLKRLRALGIRIALDDFGTGYS 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491003105  424 ALIYLERYKFDYLKIDRGFVQAIGTETVTSPVLDAVLTLSRRLQLMTVAEGVETPEQAEWLRKHGVNFLQGYWLSRP 500
Cdd:pfam00563 159 SLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
 
Name Accession Description Interval E-value
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
1-513 0e+00

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 874.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105   1 MLTRYLSPRRNIWLTSILIGVIVALLAGSIQVMVIYHSRSERFDSIIDNVNVYLTDYFSQLEKTMADLQPLVDQKCENIA 80
Cdd:PRK10551   1 MFTRAPSSGRKILLTSIVAGVMIALLFSCLQFLLLWHKREVKYDTLITDVQKYLDTYFADLKSTTDRLQPLTLDTCQQVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105  81 SGLTARAAFSPNVRAFLLVKDGVAFCSSATGPMNTPLVQLIPHLDTHKAVDMLLLPGTPMMPGNAALAMWVRNPHGGNDG 160
Cdd:PRK10551  81 PELTSRAAFSLNVRAFLLVKDKKAFCSSATGEMNTPLSELIPAIDINKPVDMAILPGTPMMPNKPAIVIWYRNPLLKNSG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 161 VFVSINTNLTPYILYSARQNDFSSIALVVNDTALSTLTNRLIDPQSLHAEPIRQIQIKGVPLKVYLYANSWLSENTQFSL 240
Cdd:PRK10551 161 VFATLNLNLTPYLLYTSRQEDFDGIALIIGNTALSTFSSRLMNVNELPDMPLRETTIPGYPLTIRLYADSWTANDIWYAL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 241 LLGVMCGLLAGLVSYYVLTLKSDPRKAILLGIKNNQFYVVYQPVVKADTLRISGIEVLMRWRHPVAGEIPPDVFINLAET 320
Cdd:PRK10551 241 LLGLLSGILVGLLCYYLLSLRMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 321 QQVIVPLTHHLLALIARDAPALQKVLPAGSKLGLNISPSHLHADEFQDDLRQFAASMPANHFNVVLEITERAMIDKNKSL 400
Cdd:PRK10551 321 QKLIVPLTQHLFELIARDAAELQKVLPVGAKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEEAT 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 401 AIFDWLHEQGFEIAIDDFGTGHSALIYLERYKFDYLKIDRGFVQAIGTETVTSPVLDAVLTLSRRLQLMTVAEGVETPEQ 480
Cdd:PRK10551 401 KLFAWLHSQGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQ 480

                        490       500       510
                 ....*....|....*....|....*....|...
gi 491003105 481 AEWLRKHGVNFLQGYWLSRPLPLEELIAAHDEP 513
Cdd:PRK10551 481 ARWLRERGVNFLQGYWISRPLPLEDFVRWLKEP 513
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 4-515 1.54e-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: 1.54e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105   4 RYLSPRRNIWLTSILIGVIVALLAGSIQVMVIYHSRSERF-DSIIDNVNvyltDYFSQLEKTMADLQPLVDQKC--ENIA 80
Cdd:COG4943    7 RLLSLATLLALLAALLPLLLSLWLAQIQARRREREQLESYaQRALARAE----RVFDQARSALDELNALPGDPCspAHLA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105  81 SgLTARAAFSPNVRAFLLVKDGVAFCSSAtGPMNTPLVQLIPHLDTHKAVDMLLLPGTPMMPGNAALAMwvrnphgGNDG 160
Cdd:COG4943   83 A-LRRLVFSSRYVRDIGYVRDGRLLCSSL-GKLSKPVPLPPPDYVTADGYRLWLNVDNPLDPGRPMLIV-------GRGN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 161 VFVSINTNLtpYILYSARQNDFSSIALVVNDTALSTLTNR--LIDPQSLHAEPIRQIQIKGV----------PLKVYLYA 228
Cdd:COG4943  154 YVVVIDPAA--FIDVLSPQPGISLALLATNGGHLFASSGNpdPALLSRLLRGPSSWFIQGDRlyasacspqyPICVVAAA 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 229 NS--WLSENTQ---FSLLLGVMCGLLAG-LVSYYVLTLKSdPRKAILLGIKNNQFYVVYQPVVKADTLRISGIEVLMRWR 302
Cdd:COG4943  232 PLagLLALWRQlllLLLPLGLLLSLLLGlLVLRLLRRRLS-PRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWR 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 303 HPVAGEIPPDVFINLAETQQVIVPLTHHLLALIARDapaLQKVLPA--GSKLGLNISPSHLHADEFQDDLRQFAASMPAN 380
Cdd:COG4943  311 DPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRD---LGDLLAAdpDFHISINLSASDLLSPRFLDDLERLLARTGVA 387

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 381 HFNVVLEITERAMIDKNKSLAIFDWLHEQGFEIAIDDFGTGHSALIYLERYKFDYLKIDRGFVQAIGTETVTSPVLDAVL 460
Cdd:COG4943  388 PQQIVLEITERGFIDPAKARAVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHII 467

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491003105 461 TLSRRLQLMTVAEGVETPEQAEWLRKHGVNFLQGYWLSRPLPLEELIAAHDEPAK 515
Cdd:COG4943  468 EMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPLPAEEFIAWLAAQRA 522
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 267-505 1.33e-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: 266.72  E-value: 1.33e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 267 AILLGIKNNQFYVVYQPVVKADTLRISGIEVLMRWRHPVAGEIPPDVFINLAETQQVIVPLTHHLLALIARDAPALQKVL 346
Cdd:cd01948    2 DLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 347 PAGsKLGLNISPSHLHADEFQDDLRQFAASMPANHFNVVLEITERAMI-DKNKSLAIFDWLHEQGFEIAIDDFGTGHSAL 425
Cdd:cd01948   82 PDL-RLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIdDLEEALATLRRLRALGVRIALDDFGTGYSSL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 426 IYLERYKFDYLKIDRGFVQAIGTETVTSPVLDAVLTLSRRLQLMTVAEGVETPEQAEWLRKHGVNFLQGYWLSRPLPLEE 505
Cdd:cd01948  161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 267-505 3.81e-84

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 260.61  E-value: 3.81e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105   267 AILLGIKNNQFYVVYQPVVKADTLRISGIEVLMRWRHPVAGEIPPDVFINLAETQQVIVPLTHHLLALIARDAPALQKVL 346
Cdd:smart00052   3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105   347 PAGSKLGLNISPSHLHADEFQDDLRQFAASMPANHFNVVLEITERAMIDKNKS-LAIFDWLHEQGFEIAIDDFGTGHSAL 425
Cdd:smart00052  83 PPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESaVATLQRLRELGVRIALDDFGTGYSSL 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105   426 IYLERYKFDYLKIDRGFVQAIGTETVTSPVLDAVLTLSRRLQLMTVAEGVETPEQAEWLRKHGVNFLQGYWLSRPLPLEE 505
Cdd:smart00052 163 SYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLDD 242
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 258-508 2.31e-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: 250.85  E-value: 2.31e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 258 LTLKSDPRKAIllgiKNNQFYVVYQPVVKADTLRISGIEVLMRWRHPVAGEIPPDVFINLAETQQVIVPLTHHLLALIAR 337
Cdd:COG5001  424 LELEADLRRAL----ERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACR 499

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 338 DAPALQKVLPAGSKLGLNISPSHLHADEFQDDLRQFAAS--MPANHfnVVLEITERAMI-DKNKSLAIFDWLHEQGFEIA 414
Cdd:COG5001  500 QLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAEtgLPPSR--LELEITESALLeDPEEALETLRALRALGVRIA 577

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 415 IDDFGTGHSALIYLERYKFDYLKIDRGFVQAIGTETVTSPVLDAVLTLSRRLQLMTVAEGVETPEQAEWLRKHGVNFLQG 494
Cdd:COG5001  578 LDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQG 657

                        250
                 ....*....|....
gi 491003105 495 YWLSRPLPLEELIA 508
Cdd:COG5001  658 YLFSRPLPAEELEA 671
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 265-508 3.30e-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: 245.46  E-value: 3.30e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 265 RKAILLGIKNNQFYVVYQPVVKADTLRISGIEVLMRWRHPVAGEIPPDVFINLAETQQVIVPLTHHLLALIARDAPALQK 344
Cdd:COG2200  330 ESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPE 409

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 345 VLPAGsKLGLNISPSHLHADEFQDDLRQFAASMPANHFNVVLEITERAMI-DKNKSLAIFDWLHEQGFEIAIDDFGTGHS 423
Cdd:COG2200  410 RGLDL-RLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLeDLEAAIELLARLRALGVRIALDDFGTGYS 488

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 424 ALIYLERYKFDYLKIDRGFVQAIGTETVTSPVLDAVLTLSRRLQLMTVAEGVETPEQAEWLRKHGVNFLQGYWLSRPLPL 503
Cdd:COG2200  489 SLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPL 568


                 ....*
gi 491003105 504 EELIA 508
Cdd:COG2200  569 EELEA 573
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 265-500 9.21e-70

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: 222.96  E-value: 9.21e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105  265 RKAILLGIKNNQFYVVYQPVVKADTLRISGIEVLMRWRHPVAGEIPPDVFINLAETQQVIVPLTHHLLALIARDApaLQK 344
Cdd:pfam00563   1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADL--AQL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105  345 VLPAGSKLGLNISPSHLHADEFQDDLRQFAASMPANHFNVVLEITERAMIDKNKSL-AIFDWLHEQGFEIAIDDFGTGHS 423
Cdd:pfam00563  79 QLGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALrEVLKRLRALGIRIALDDFGTGYS 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491003105  424 ALIYLERYKFDYLKIDRGFVQAIGTETVTSPVLDAVLTLSRRLQLMTVAEGVETPEQAEWLRKHGVNFLQGYWLSRP 500
Cdd:pfam00563 159 SLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 272-506 1.52e-40

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 156.08  E-value: 1.52e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 272 IKNNQFYVVYQPVVKADTLRISGIEVLMRWRHPVAGEIPPDVFINLAETQQVIVPLTHHLLALIAR-----DAPALQkvL 346
Cdd:PRK11359 552 ISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRqlaewRSQNIH--I 629

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 347 PAgskLGLNISPSHLHADEFQDD----LRQFAasMPANHFNVvlEITERAMIDKNKS-LAIFDWLHEQGFEIAIDDFGTG 421
Cdd:PRK11359 630 PA---LSVNLSALHFRSNQLPNQvsdaMQAWG--IDGHQLTV--EITESMMMEHDTEiFKRIQILRDMGVGLSVDDFGTG 702

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 422 HSALIYLERYKFDYLKIDRGFVQAIGTETVTSPVLDAVLTLSRRLQLMTVAEGVETPEQAEWLRKHGVNFLQGYWLSRPL 501
Cdd:PRK11359 703 FSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPL 782


                 ....*
gi 491003105 502 PLEEL 506
Cdd:PRK11359 783 PAEEI 787
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
260-506 2.58e-37

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 145.98  E-value: 2.58e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 260 LKSDPRKAIllgiKNNQFYVVYQPVVKAdTLRISGIEVLMRWRHPVAGEIPPDVFINLAETQQVIVPLTHHLLALIARDA 339
Cdd:PRK10060 409 LDTNLRKAL----ENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQV 483

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 340 PALQKvlpAGSKL--GLNISPSHLhADefQDDLRQFAASMPANHFN---VVLEITERAMI-DKNKSLAIFDWLHEQGFEI 413
Cdd:PRK10060 484 AKWRD---KGINLrvAVNVSARQL-AD--QTIFTALKQALQELNFEycpIDVELTESCLIeNEELALSVIQQFSQLGAQV 557

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 414 AIDDFGTGHSALIYLERYKFDYLKIDRGFVQAIGTETVTSPVLDAVLTLSRRLQLMTVAEGVETPEQAEWLRKHGVNFLQ 493
Cdd:PRK10060 558 HLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQ 637

                        250
                 ....*....|...
gi 491003105 494 GYWLSRPLPLEEL 506
Cdd:PRK10060 638 GFLFAKPMPAVAF 650
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 258-514 5.00e-37

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 144.86  E-value: 5.00e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 258 LTLKSDprkaILLGIKNNQFYVVYQPVVKADTLRISGIEVLMRWRHPVAGEIPPDVFINLAETQQVIVPLTHHLLALIAR 337
Cdd:PRK13561 399 LTEESD----ILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCR 474

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 338 DAPALQK---VLPagskLGLNISPSHL-HAD---EFQDDLRQFAASmPANhfnVVLEITERAMIDK-NKSLAIFDWLHEQ 409
Cdd:PRK13561 475 LLAAWQErgiMLP----LSVNLSALQLmHPNmvaDMLELLTRYRIQ-PGT---LILEVTESRRIDDpHAAVAILRPLRNA 546

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 410 GFEIAIDDFGTGHSALIYLERYK---FDYLKIDRGFVQAIGTEtvtSPVLDAVLTLSRRLQLMTVAEGVETPEQAEWLRK 486
Cdd:PRK13561 547 GVRVALDDFGMGYAGLRQLQHMKslpIDVLKIDKMFVDGLPED---DSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLK 623

                        250       260
                 ....*....|....*....|....*...
gi 491003105 487 HGVNFLQGYWLSRPLPLEELIAAHDEPA 514
Cdd:PRK13561 624 AGVGIAQGFLFARALPIEIFEERYLEEK 651
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 268-519 5.64e-33

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 133.14  E-value: 5.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 268 ILLGIKNNQFYVVYQPVVKADTLRISGIEVLMRWRHPVAGEIPPDVFINLAETQQVIVPLTHHLLALIAR---DAPALQK 344
Cdd:PRK11829 410 LLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRilaDWKARGV 489

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 345 VLPagskLGLNISPSHLHADEFQDDLRQFAASMPANHFNVVLEITERAMI-DKNKSLAIFDWLHEQGFEIAIDDFGTGHS 423
Cdd:PRK11829 490 SLP----LSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIqDLDEALRLLRELQGLGLLIALDDFGIGYS 565

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 424 ALIYLERYK---FDYLKIDRGFVQAIGTETVTSPVLDAVltlSRRLQLMTVAEGVETPEQAEWLRKHGVNFLQGYWLSRP 500
Cdd:PRK11829 566 SLRYLNHLKslpIHMIKLDKSFVKNLPEDDAIARIISCV---SDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPP 642

                        250
                 ....*....|....*....
gi 491003105 501 LPLEELIaahdepAKYFAA 519
Cdd:PRK11829 643 LPRAEFE------AQYFSS 655
CSS-motif pfam12792
CSS motif domain associated with EAL; This family with its characteriztic highly conserved CSS ...
 39-241 6.63e-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: 124.56  E-value: 6.63e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105   39 RSERFDSIIDNVNVYLTDYFSQLEKTMADLQPLVDQKCENIA-SGLTARAAFSPNVRAFLLVKDGVAFCSSATGPMNTPL 117
Cdd:pfam12792   1 EQEQLDAFAERALRRLESVLDQADQALDRLLPLTGQPCSPAHlAELRRIVAFSPYVRDVGLVKNGRLYCSSLWGELDTPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105  118 VQLIPHLDTHKAVDMLLLPGTPMMPGNAALAMWVRNPHGGNDgVFVSINTNLTPYILYSARQNDFSSIALVVNDTALStL 197
Cdd:pfam12792  81 PLLPPDLTTPPGVRLWLLRGTPLVPGRPALVLRRGGYGVVID-PGVFIDVQYLPGLLAAVSQPDGRLLALVVGDDALL-F 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 491003105  198 TNRLIDPQSLHAEPIR-------QIQIKGVPLKVYLYANSWLSENTQFSLL 241
Cdd:pfam12792 159 DGRLHSLAEPAPGTARsggalyaRARSTRYPLTVVVYAPRASLLANWRQLL 209
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 274-520 7.89e-17

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 83.95  E-value: 7.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105  274 NNQFYVVYQPVVKADTLRISGIEVLMRWRHPVAGEIPPDVFINLAETQQvivpLTHHLLALIARDA--PALQKVLPAGSK 351
Cdd:PRK09776  852 NQLMMLAHGVASPRIPEARNHWLISLRLWDPEGEIIDEGAFRPAAEDPA----LMHALDRRVIHEFfrQAAKAVASKGLS 927

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105  352 LGLNISPSHLHADEFQDDL-RQFAASM-PANHFNvvLEITERAMIDKNKSLA-IFDWLHEQGFEIAIDDFGTGHSALIYL 428
Cdd:PRK09776  928 IALPLSVAGLSSPTLLPFLlEQLENSPlPPRLLH--LEITETALLNHAESASrLVQKLRLAGCRVVLSDFGRGLSSFNYL 1005

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105  429 ERYKFDYLKIDRGFVQAIGTETVTSPVLDAVLTLSRRLQLMTVAEGVETPEQAEWLRKHGVNFLQGYWLSRPLPLEELIA 508
Cdd:PRK09776 1006 KAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLLLN 1085

                         250
                  ....*....|..
gi 491003105  509 ahdepAKYFAAR 520
Cdd:PRK09776 1086 -----SSYFAIN 1092
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
 276-504 8.48e-16

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


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 79.46  E-value: 8.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 276 QFYVVYQPVVKADtLRISGIEVLmrWRHPvAGEIPPDVFINLAeTQQVIVpltHHLLALiardapALQKVLpaGSKLG-L 354
Cdd:COG3434    3 DVFVARQPILDRD-QRVVGYELL--FRSG-LENSAPDVDGDQA-TARVLL---NAFLEI------GLDRLL--GGKLAfI 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 355 NISPSHLHADefqddlrqFAASMPANhfNVVLEITERAMIDKnKSLAIFDWLHEQGFEIAIDDFgtghsalIYLERYK-- 432
Cdd:COG3434   67 NFTEELLLSD--------LPELLPPE--RVVLEILEDVEPDE-ELLEALKELKEKGYRIALDDF-------VLDPEWDpl 128

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491003105 433 ---FDYLKIDrgfVQAIGTETvtspvLDAVLTLSRRLQLMTVAEGVETPEQAEWLRKHGVNFLQGYWLSRPLPLE 504
Cdd:COG3434  129 lplADIIKID---VLALDLEE-----LAELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEILK 195
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
 281-506 1.18e-11

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 65.02  E-value: 1.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 281 YQPVVKADTlRISGIEVLMRWRHPVAGE--IPPDVF---INLAETQQVIVplthHLLALIARDAPALQKvlpAGSKLGLN 355
Cdd:PRK11596  34 FQPIYRTSG-RLMAIELLTAVTHPSNPSqrLSPERYfaeITVSHRLDVVK----EQLDLLAQWADFFVR---HGLLASVN 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 356 ISPSHLHADEFQDDLRQFAASMPANHFnvvlEITERAMIDKNKSLAIFD-----WLheqgfeiaiDDFGTG---HSALIY 427
Cdd:PRK11596 106 IDGPTLIALRQQPAILRLIERLPWLRF----ELVEHIRLPKDSPFASMCefgplWL---------DDFGTGmanFSALSE 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003105 428 LeryKFDYLKIDRG-FVQAIGTETVTSpVLDAVLTLSRRLQLMTVAEGVETPEQAEWLRKHGVNFLQGYWLSRPLPLEEL 506
Cdd:PRK11596 173 V---RYDYIKVARElFIMLRQSEEGRN-LFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPAPFETL 248
 
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