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Conserved domains on  [gi|1877448828|dbj|BBS06958|]
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phage resistance protein [Escherichia coli]

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: 989.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828   1 MFIRAPNSGRKLLLTCIVAGVMIAILVSCLQFLVAWHKHEVKYDTLITDVQKYLDTYFADLKSTTDRLQPLTLDTCQQAN 80
Cdd:PRK10551    1 MFTRAPSSGRKILLTSIVAGVMIALLFSCLQFLLLWHKREVKYDTLITDVQKYLDTYFADLKSTTDRLQPLTLDTCQQVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828  81 PELTARAAFSMNVRTFVLVKDKKTFCSSATGEMDIPLNELIPALDINKNVDMAILPGTPMVPNKPAIVIWYRNPLLKNSG 160
Cdd:PRK10551   81 PELTSRAAFSLNVRAFLLVKDKKAFCSSATGEMNTPLSELIPAIDINKPVDMAILPGTPMMPNKPAIVIWYRNPLLKNSG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 161 VFAALNLNLTPSLFYSSRQEDYDGVALIIGNTALSTFSSRLMNVNELTDMPVRETKIAGIPLTVRLYADDWTWNDVWYAF 240
Cdd:PRK10551  161 VFATLNLNLTPYLLYTSRQEDFDGIALIIGNTALSTFSSRLMNVNELPDMPLRETTIPGYPLTIRLYADSWTANDIWYAL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 241 LLGGMSGTVVGLLCYYLMSVRMRPGREIMTAIKREQFYVAYQPVVDTQALRVTGLEVLLRWRHPVAGEIPPDAFINFAES 320
Cdd:PRK10551  241 LLGLLSGILVGLLCYYLLSLRMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 321 QKMIVPLTQHLFELIARDAAELEKVLPVGVKFGINIAPDHLHSESFKADIQKLLTSLPAHHFQIVLEITERDMLKEQEAT 400
Cdd:PRK10551  321 QKLIVPLTQHLFELIARDAAELQKVLPVGAKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEEAT 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 401 QLFAWLHSVGVEIAIDDFGTGHSALIYLERFTLDYLKIDRGFINAIGTKTITSPVLDAVLTLAKRLNMLTVAEGVETPEQ 480
Cdd:PRK10551  401 KLFAWLHSQGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQ 480
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 1877448828 481 ARWLSERGVNFMQGYWISRPLPLDDFVRWLKKPYTPQW 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: 989.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828   1 MFIRAPNSGRKLLLTCIVAGVMIAILVSCLQFLVAWHKHEVKYDTLITDVQKYLDTYFADLKSTTDRLQPLTLDTCQQAN 80
Cdd:PRK10551    1 MFTRAPSSGRKILLTSIVAGVMIALLFSCLQFLLLWHKREVKYDTLITDVQKYLDTYFADLKSTTDRLQPLTLDTCQQVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828  81 PELTARAAFSMNVRTFVLVKDKKTFCSSATGEMDIPLNELIPALDINKNVDMAILPGTPMVPNKPAIVIWYRNPLLKNSG 160
Cdd:PRK10551   81 PELTSRAAFSLNVRAFLLVKDKKAFCSSATGEMNTPLSELIPAIDINKPVDMAILPGTPMMPNKPAIVIWYRNPLLKNSG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 161 VFAALNLNLTPSLFYSSRQEDYDGVALIIGNTALSTFSSRLMNVNELTDMPVRETKIAGIPLTVRLYADDWTWNDVWYAF 240
Cdd:PRK10551  161 VFATLNLNLTPYLLYTSRQEDFDGIALIIGNTALSTFSSRLMNVNELPDMPLRETTIPGYPLTIRLYADSWTANDIWYAL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 241 LLGGMSGTVVGLLCYYLMSVRMRPGREIMTAIKREQFYVAYQPVVDTQALRVTGLEVLLRWRHPVAGEIPPDAFINFAES 320
Cdd:PRK10551  241 LLGLLSGILVGLLCYYLLSLRMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 321 QKMIVPLTQHLFELIARDAAELEKVLPVGVKFGINIAPDHLHSESFKADIQKLLTSLPAHHFQIVLEITERDMLKEQEAT 400
Cdd:PRK10551  321 QKLIVPLTQHLFELIARDAAELQKVLPVGAKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEEAT 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 401 QLFAWLHSVGVEIAIDDFGTGHSALIYLERFTLDYLKIDRGFINAIGTKTITSPVLDAVLTLAKRLNMLTVAEGVETPEQ 480
Cdd:PRK10551  401 KLFAWLHSQGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQ 480
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 1877448828 481 ARWLSERGVNFMQGYWISRPLPLDDFVRWLKKPYTPQW 518
Cdd:PRK10551  481 ARWLRERGVNFLQGYWISRPLPLEDFVRWLKEPYTPQW 518
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
10-517 1.12e-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: 336.12  E-value: 1.12e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828  10 RKLLLTCIVAGVMIAILVSCLQFLVAWH---KHEVKY-DTLITDVQKYLDTYFADLKSTTDRLQPLTLDTCQQANPELTA 85
Cdd:COG4943     6 RRLLSLATLLALLAALLPLLLSLWLAQIqarRREREQlESYAQRALARAERVFDQARSALDELNALPGDPCSPAHLAALR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828  86 RAAFSM-NVRTFVLVKDKKTFCSSAtGEMDIPLNELIPALDINKNVDMAILPGTPMVPNKPAIVIWYRNpllknsgVFAA 164
Cdd:COG4943    86 RLVFSSrYVRDIGYVRDGRLLCSSL-GKLSKPVPLPPPDYVTADGYRLWLNVDNPLDPGRPMLIVGRGN-------YVVV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 165 LNlnltpSLFYSSRQEDYDGVALIIGNTALSTFSSRLMNVNELTDMPVRETKIAGIPLTVRLYA------DDWT------ 232
Cdd:COG4943   158 ID-----PAAFIDVLSPQPGISLALLATNGGHLFASSGNPDPALLSRLLRGPSSWFIQGDRLYAsacspqYPICvvaaap 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 233 --------WNDVWYAFLLGGMSGTVVGLLCYYLMSVRMRPGREIMTAIKREQFYVAYQPVVDTQALRVTGLEVLLRWRHP 304
Cdd:COG4943   233 lagllalwRQLLLLLLPLGLLLSLLLGLLVLRLLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDP 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 305 VAGEIPPDAFINFAESQKMIVPLTQHLFELIARDAAELEKVLPvGVKFGINIAPDHLHSESFKADIQKLLTSLPAHHFQI 384
Cdd:COG4943   313 DGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDLLAADP-DFHISINLSASDLLSPRFLDDLERLLARTGVAPQQI 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 385 VLEITERDMLKEQEATQLFAWLHSVGVEIAIDDFGTGHSALIYLERFTLDYLKIDRGFINAIGTKTITSPVLDAVLTLAK 464
Cdd:COG4943   392 VLEITERGFIDPAKARAVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAK 471
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1877448828 465 RLNMLTVAEGVETPEQARWLSERGVNFMQGYWISRPLPLDDFVRWLKKPYTPQ 517
Cdd:COG4943   472 TLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPLPAEEFIAWLAAQRAPA 524
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
266-505 2.33e-96

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 291.81  E-value: 2.33e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828  266 REIMTAIKREQFYVAYQPVVDTQALRVTGLEVLLRWRHPVAGEIPPDAFINFAESQKMIVPLTQHLFELIARDAAELEKV 345
Cdd:smart00052   2 RELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQ 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828  346 LPVGVKFGINIAPDHLHSESFKADIQKLLTSLPAHHFQIVLEITERDMLKEQEATQLFAW-LHSVGVEIAIDDFGTGHSA 424
Cdd:smart00052  82 GPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQrLRELGVRIALDDFGTGYSS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828  425 LIYLERFTLDYLKIDRGFINAIGTKTITSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLSERGVNFMQGYWISRPLPLD 504
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLD 241

                   .
gi 1877448828  505 D 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 7.08e-88

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: 270.19  E-value: 7.08e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 266 REIMTAIKREQFYVAYQPVVDTQALRVTGLEVLLRWRHPVAGEIPPDAFINFAESQKMIVPLTQHLFELIARDAAELEKV 345
Cdd:cd01948     1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 346 LPvGVKFGINIAPDHLHSESFKADIQKLLTSLPAHHFQIVLEITERDMLKE-QEATQLFAWLHSVGVEIAIDDFGTGHSA 424
Cdd:cd01948    81 GP-DLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDlEEALATLRRLRALGVRIALDDFGTGYSS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 425 LIYLERFTLDYLKIDRGFINAIGTKTITSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLSERGVNFMQGYWISRPLPLD 504
Cdd:cd01948   160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239

                  .
gi 1877448828 505 D 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 2.89e-79

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: 247.62  E-value: 2.89e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 266 REIMTAIKREQFYVAYQPVVDTQALRVTGLEVLLRWRHPVAGEIPPDAFINFAESQKMIVPLTQHLFELIARDAAELEkv 345
Cdd:pfam00563   2 RALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQ-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 346 LPVGVKFGINIAPDHLHSESFKADIQKLLTSLPAHHFQIVLEITERDMLKE-QEATQLFAWLHSVGVEIAIDDFGTGHSA 424
Cdd:pfam00563  80 LGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARlEALREVLKRLRALGIRIALDDFGTGYSS 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1877448828 425 LIYLERFTLDYLKIDRGFINAIGTKTITSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLSERGVNFMQGYWISRP 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: 989.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828   1 MFIRAPNSGRKLLLTCIVAGVMIAILVSCLQFLVAWHKHEVKYDTLITDVQKYLDTYFADLKSTTDRLQPLTLDTCQQAN 80
Cdd:PRK10551    1 MFTRAPSSGRKILLTSIVAGVMIALLFSCLQFLLLWHKREVKYDTLITDVQKYLDTYFADLKSTTDRLQPLTLDTCQQVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828  81 PELTARAAFSMNVRTFVLVKDKKTFCSSATGEMDIPLNELIPALDINKNVDMAILPGTPMVPNKPAIVIWYRNPLLKNSG 160
Cdd:PRK10551   81 PELTSRAAFSLNVRAFLLVKDKKAFCSSATGEMNTPLSELIPAIDINKPVDMAILPGTPMMPNKPAIVIWYRNPLLKNSG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 161 VFAALNLNLTPSLFYSSRQEDYDGVALIIGNTALSTFSSRLMNVNELTDMPVRETKIAGIPLTVRLYADDWTWNDVWYAF 240
Cdd:PRK10551  161 VFATLNLNLTPYLLYTSRQEDFDGIALIIGNTALSTFSSRLMNVNELPDMPLRETTIPGYPLTIRLYADSWTANDIWYAL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 241 LLGGMSGTVVGLLCYYLMSVRMRPGREIMTAIKREQFYVAYQPVVDTQALRVTGLEVLLRWRHPVAGEIPPDAFINFAES 320
Cdd:PRK10551  241 LLGLLSGILVGLLCYYLLSLRMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 321 QKMIVPLTQHLFELIARDAAELEKVLPVGVKFGINIAPDHLHSESFKADIQKLLTSLPAHHFQIVLEITERDMLKEQEAT 400
Cdd:PRK10551  321 QKLIVPLTQHLFELIARDAAELQKVLPVGAKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEEAT 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 401 QLFAWLHSVGVEIAIDDFGTGHSALIYLERFTLDYLKIDRGFINAIGTKTITSPVLDAVLTLAKRLNMLTVAEGVETPEQ 480
Cdd:PRK10551  401 KLFAWLHSQGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQ 480
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 1877448828 481 ARWLSERGVNFMQGYWISRPLPLDDFVRWLKKPYTPQW 518
Cdd:PRK10551  481 ARWLRERGVNFLQGYWISRPLPLEDFVRWLKEPYTPQW 518
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
10-517 1.12e-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: 336.12  E-value: 1.12e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828  10 RKLLLTCIVAGVMIAILVSCLQFLVAWH---KHEVKY-DTLITDVQKYLDTYFADLKSTTDRLQPLTLDTCQQANPELTA 85
Cdd:COG4943     6 RRLLSLATLLALLAALLPLLLSLWLAQIqarRREREQlESYAQRALARAERVFDQARSALDELNALPGDPCSPAHLAALR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828  86 RAAFSM-NVRTFVLVKDKKTFCSSAtGEMDIPLNELIPALDINKNVDMAILPGTPMVPNKPAIVIWYRNpllknsgVFAA 164
Cdd:COG4943    86 RLVFSSrYVRDIGYVRDGRLLCSSL-GKLSKPVPLPPPDYVTADGYRLWLNVDNPLDPGRPMLIVGRGN-------YVVV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 165 LNlnltpSLFYSSRQEDYDGVALIIGNTALSTFSSRLMNVNELTDMPVRETKIAGIPLTVRLYA------DDWT------ 232
Cdd:COG4943   158 ID-----PAAFIDVLSPQPGISLALLATNGGHLFASSGNPDPALLSRLLRGPSSWFIQGDRLYAsacspqYPICvvaaap 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 233 --------WNDVWYAFLLGGMSGTVVGLLCYYLMSVRMRPGREIMTAIKREQFYVAYQPVVDTQALRVTGLEVLLRWRHP 304
Cdd:COG4943   233 lagllalwRQLLLLLLPLGLLLSLLLGLLVLRLLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDP 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 305 VAGEIPPDAFINFAESQKMIVPLTQHLFELIARDAAELEKVLPvGVKFGINIAPDHLHSESFKADIQKLLTSLPAHHFQI 384
Cdd:COG4943   313 DGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDLLAADP-DFHISINLSASDLLSPRFLDDLERLLARTGVAPQQI 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 385 VLEITERDMLKEQEATQLFAWLHSVGVEIAIDDFGTGHSALIYLERFTLDYLKIDRGFINAIGTKTITSPVLDAVLTLAK 464
Cdd:COG4943   392 VLEITERGFIDPAKARAVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAK 471
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1877448828 465 RLNMLTVAEGVETPEQARWLSERGVNFMQGYWISRPLPLDDFVRWLKKPYTPQ 517
Cdd:COG4943   472 TLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPLPAEEFIAWLAAQRAPA 524
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
266-505 2.33e-96

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 291.81  E-value: 2.33e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828  266 REIMTAIKREQFYVAYQPVVDTQALRVTGLEVLLRWRHPVAGEIPPDAFINFAESQKMIVPLTQHLFELIARDAAELEKV 345
Cdd:smart00052   2 RELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQ 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828  346 LPVGVKFGINIAPDHLHSESFKADIQKLLTSLPAHHFQIVLEITERDMLKEQEATQLFAW-LHSVGVEIAIDDFGTGHSA 424
Cdd:smart00052  82 GPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQrLRELGVRIALDDFGTGYSS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828  425 LIYLERFTLDYLKIDRGFINAIGTKTITSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLSERGVNFMQGYWISRPLPLD 504
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLD 241

                   .
gi 1877448828  505 D 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 7.08e-88

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: 270.19  E-value: 7.08e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 266 REIMTAIKREQFYVAYQPVVDTQALRVTGLEVLLRWRHPVAGEIPPDAFINFAESQKMIVPLTQHLFELIARDAAELEKV 345
Cdd:cd01948     1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 346 LPvGVKFGINIAPDHLHSESFKADIQKLLTSLPAHHFQIVLEITERDMLKE-QEATQLFAWLHSVGVEIAIDDFGTGHSA 424
Cdd:cd01948    81 GP-DLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDlEEALATLRRLRALGVRIALDDFGTGYSS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 425 LIYLERFTLDYLKIDRGFINAIGTKTITSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLSERGVNFMQGYWISRPLPLD 504
Cdd:cd01948   160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239

                  .
gi 1877448828 505 D 505
Cdd:cd01948   240 E 240
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
261-511 4.77e-81

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: 263.57  E-value: 4.77e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 261 RMRPGREIMTAIKREQFYVAYQPVVDTQALRVTGLEVLLRWRHPVAGEIPPDAFINFAESQKMIVPLTQHLFELIARDAA 340
Cdd:COG2200   326 RLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLA 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 341 ELEKVLPvGVKFGINIAPDHLHSESFKADIQKLLTSLPAHHFQIVLEITERDMLKE-QEATQLFAWLHSVGVEIAIDDFG 419
Cdd:COG2200   406 RWPERGL-DLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDlEAAIELLARLRALGVRIALDDFG 484
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 420 TGHSALIYLERFTLDYLKIDRGFINAIGTKTITSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLSERGVNFMQGYWISR 499
Cdd:COG2200   485 TGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGR 564
                         250
                  ....*....|..
gi 1877448828 500 PLPLDDFVRWLK 511
Cdd:COG2200   565 PLPLEELEALLR 576
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
270-512 7.66e-81

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: 265.48  E-value: 7.66e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 270 TAIKREQFYVAYQPVVDTQALRVTGLEVLLRWRHPVAGEIPPDAFINFAESQKMIVPLTQHLFELIARDAAELEKVLPVG 349
Cdd:COG5001   432 RALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPD 511
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 350 VKFGINIAPDHLHSESFKADIQKLL--TSLPAHHfqIVLEITERDMLKEQEAT-QLFAWLHSVGVEIAIDDFGTGHSALI 426
Cdd:COG5001   512 LRVAVNLSARQLRDPDLVDRVRRALaeTGLPPSR--LELEITESALLEDPEEAlETLRALRALGVRIALDDFGTGYSSLS 589
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 427 YLERFTLDYLKIDRGFINAIGTKTITSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLSERGVNFMQGYWISRPLPLDDF 506
Cdd:COG5001   590 YLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEEL 669

                  ....*.
gi 1877448828 507 VRWLKK 512
Cdd:COG5001   670 EALLRA 675
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
266-500 2.89e-79

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: 247.62  E-value: 2.89e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 266 REIMTAIKREQFYVAYQPVVDTQALRVTGLEVLLRWRHPVAGEIPPDAFINFAESQKMIVPLTQHLFELIARDAAELEkv 345
Cdd:pfam00563   2 RALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQ-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 346 LPVGVKFGINIAPDHLHSESFKADIQKLLTSLPAHHFQIVLEITERDMLKE-QEATQLFAWLHSVGVEIAIDDFGTGHSA 424
Cdd:pfam00563  80 LGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARlEALREVLKRLRALGIRIALDDFGTGYSS 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1877448828 425 LIYLERFTLDYLKIDRGFINAIGTKTITSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLSERGVNFMQGYWISRP 500
Cdd:pfam00563 160 LSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
271-511 1.62e-46

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 172.17  E-value: 1.62e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 271 AIKREQFYVAYQPVVDTQAlRVTGLEVLLRWRHPVAGEIPPDAFINFAESQKMIVPLTQHLFELIARDAAELeKVLPVGV 350
Cdd:PRK10060  416 ALENDQLVIHYQPKITWRG-EVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKW-RDKGINL 493
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 351 KFGINIAPDHLHSESFKADIQKLLTSLPAHHFQIVLEITERDMLK-EQEATQLFAWLHSVGVEIAIDDFGTGHSALIYLE 429
Cdd:PRK10060  494 RVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIEnEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLA 573
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 430 RFTLDYLKIDRGFINAIGTKTITSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLSERGVNFMQGYWISRPLPLDDFVRW 509
Cdd:PRK10060  574 RFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERW 653

                  ..
gi 1877448828 510 LK 511
Cdd:PRK10060  654 YK 655
CSS-motif pfam12792
CSS motif domain associated with EAL; This family with its characteriztic highly conserved CSS ...
39-241 2.72e-42

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: 149.98  E-value: 2.72e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828  39 HEVKYDTLITDVQKYLDTYFADLKSTTDRLQPLTLDTCQQAN-PELTARAAFSMNVRTFVLVKDKKTFCSSATGEMDIPL 117
Cdd:pfam12792   1 EQEQLDAFAERALRRLESVLDQADQALDRLLPLTGQPCSPAHlAELRRIVAFSPYVRDVGLVKNGRLYCSSLWGELDTPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 118 NELIPALDINKNVDMAILPGTPMVPNKPAIVIWYRNPLLKNSgVFAALNLNLTPSLFYSSRQEDYDGVALIIGNTALStF 197
Cdd:pfam12792  81 PLLPPDLTTPPGVRLWLLRGTPLVPGRPALVLRRGGYGVVID-PGVFIDVQYLPGLLAAVSQPDGRLLALVVGDDALL-F 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1877448828 198 SSRLMNVNELTDMPVR-------ETKIAGIPLTVRLYADDWTWNDVWYAFL 241
Cdd:pfam12792 159 DGRLHSLAEPAPGTARsggalyaRARSTRYPLTVVVYAPRASLLANWRQLL 209
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
267-513 6.27e-42

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 159.11  E-value: 6.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 267 EIMTAIKREQFYVAYQPVVDTQALRVTGLEVLLRWRHPVAGEIPPDAFINFAESQKMIVPLTQHLFELIARDAAELEK-- 344
Cdd:PRK13561  404 DILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQErg 483
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 345 -VLPVGVkfgiNIAPDHLHSESFKADIQKLLtslpaHHFQI-----VLEITE-RDMLKEQEATQLFAWLHSVGVEIAIDD 417
Cdd:PRK13561  484 iMLPLSV----NLSALQLMHPNMVADMLELL-----TRYRIqpgtlILEVTEsRRIDDPHAAVAILRPLRNAGVRVALDD 554
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 418 FGTGHSALIYLERFT---LDYLKIDRGFINAIGTKtitSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLSERGVNFMQG 494
Cdd:PRK13561  555 FGMGYAGLRQLQHMKslpIDVLKIDKMFVDGLPED---DSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQG 631
                         250       260
                  ....*....|....*....|
gi 1877448828 495 YWISRPLPLDDF-VRWLKKP 513
Cdd:PRK13561  632 FLFARALPIEIFeERYLEEK 651
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
261-506 5.08e-36

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 142.00  E-value: 5.08e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 261 RMRPGREIMTAIKREQFYVAYQPVVDTQALRVTGLEVLLRWRHPVAGEIPPDAFINFAESQKMIVPLTQHLFELIARDAA 340
Cdd:PRK11829  403 RLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILA 482
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 341 ELEKvLPVGVKFGINIAPDHLHSESFkadIQKLLTSLPAHHF---QIVLEITERDMLKE-QEATQLFAWLHSVGVEIAID 416
Cdd:PRK11829  483 DWKA-RGVSLPLSVNISGLQVQNKQF---LPHLKTLISHYHIdpqQLLLEITETAQIQDlDEALRLLRELQGLGLLIALD 558
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 417 DFGTGHSALIYL---ERFTLDYLKIDRGFINAIgtktitsPVLDAVL----TLAKRLNMLTVAEGVETPEQARWLSERGV 489
Cdd:PRK11829  559 DFGIGYSSLRYLnhlKSLPIHMIKLDKSFVKNL-------PEDDAIAriisCVSDVLKVRVMAEGVETEEQRQWLLEHGI 631
                         250
                  ....*....|....*..
gi 1877448828 490 NFMQGYWISRPLPLDDF 506
Cdd:PRK11829  632 QCGQGFLFSPPLPRAEF 648
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
261-511 7.51e-33

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 133.36  E-value: 7.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 261 RMRPGREIMTAIKREQFYVAYQPVVDTQALRVTGLEVLLRWRHPVAGEIPPDAFINFAESQKMIVPLTQHLFELIARDAA 340
Cdd:PRK11359  541 RLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLA 620
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 341 ELEKV---LPVgvkFGINIAPDHLHSESFKADIQKLLT--SLPAHhfQIVLEITERDMLkeQEATQLFAWLHSV---GVE 412
Cdd:PRK11359  621 EWRSQnihIPA---LSVNLSALHFRSNQLPNQVSDAMQawGIDGH--QLTVEITESMMM--EHDTEIFKRIQILrdmGVG 693
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 413 IAIDDFGTGHSALIYLERFTLDYLKIDRGFINAIGTKTITSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLSERGVNFM 492
Cdd:PRK11359  694 LSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVI 773
                         250
                  ....*....|....*....
gi 1877448828 493 QGYWISRPLPLDDFVRWLK 511
Cdd:PRK11359  774 QGYFFSRPLPAEEIPGWMS 792
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
268-507 5.39e-20

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 93.97  E-value: 5.39e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828  268 IMTAIKREQFYVAYQPVVDTQALRVTGLEVLLRWRHPVAGEIPPDAFINFAESQKMIVPLTQHLFELIARDAAEleKVLP 347
Cdd:PRK09776   846 WRMIKENQLMMLAHGVASPRIPEARNHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFRQAAK--AVAS 923
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828  348 VGVKFGINIAPDHLHSESFKADIQKLL--TSLPAHHfqIVLEITERDMLKEQEATQ-LFAWLHSVGVEIAIDDFGTGHSA 424
Cdd:PRK09776   924 KGLSIALPLSVAGLSSPTLLPFLLEQLenSPLPPRL--LHLEITETALLNHAESASrLVQKLRLAGCRVVLSDFGRGLSS 1001
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828  425 LIYLERFTLDYLKIDRGFINAIGTKTITSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLSERGVNFMQGYWISRPLPLD 504
Cdd:PRK09776  1002 FNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLD 1081

                   ...
gi 1877448828  505 DFV 507
Cdd:PRK09776  1082 LLL 1084
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
276-503 3.44e-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: 71.37  E-value: 3.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 276 QFYVAYQPVVDTQaLRVTGLEVLLRwrhPVAGEIPPDAFINFAESQkMIVpltQHLFELiardaaELEKVLPVGVKFgIN 355
Cdd:COG3434     3 DVFVARQPILDRD-QRVVGYELLFR---SGLENSAPDVDGDQATAR-VLL---NAFLEI------GLDRLLGGKLAF-IN 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 356 IAPDHLHSEsfkadiqkLLTSLPAHhfQIVLEITE--------RDMLKEqeatqlfawLHSVGVEIAIDDF--GTGHSAL 425
Cdd:COG3434    68 FTEELLLSD--------LPELLPPE--RVVLEILEdvepdeelLEALKE---------LKEKGYRIALDDFvlDPEWDPL 128
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1877448828 426 IYLerftLDYLKIDrgfinaigTKTITSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLSERGVNFMQGYWISRPLPL 503
Cdd:COG3434   129 LPL----ADIIKID--------VLALDLEELAELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEIL 194
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
281-506 1.06e-09

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 59.24  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 281 YQPVVDTQAlRVTGLEVLLRWRHPVAGE--IPPDAFinFAE---SQKMIVPLTQhlFELIARDAAELEKVlpvGVKFGIN 355
Cdd:PRK11596   34 FQPIYRTSG-RLMAIELLTAVTHPSNPSqrLSPERY--FAEitvSHRLDVVKEQ--LDLLAQWADFFVRH---GLLASVN 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 356 IAPDHLHSESFKADIQKLLTSLPAHHFQIVLEIterDMLKEQEATQLFA----WLhsvgveiaiDDFGTG---HSALIYL 428
Cdd:PRK11596  106 IDGPTLIALRQQPAILRLIERLPWLRFELVEHI---RLPKDSPFASMCEfgplWL---------DDFGTGmanFSALSEV 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 429 eRFtlDYLKIDRG-FI----NAIGTKtitspVLDAVLTLAKRLNMLTVAEGVETPEQARWLSERGVNFMQGYWISRPLPL 503
Cdd:PRK11596  174 -RY--DYIKVARElFImlrqSEEGRN-----LFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPAPF 245

                  ...
gi 1877448828 504 DDF 506
Cdd:PRK11596  246 ETL 248
PRK11059 PRK11059
regulatory protein CsrD; Provisional
259-504 2.30e-04

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 43.70  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 259 SVRMRPGREimTAIKREQFYVAYQPVVDTQAlRVTGLEVLLRWRHPVAGEIPPDAFInfaesqkmivPLTQhLFELIAR- 337
Cdd:PRK11059  401 SVRWRTLLE--QTLVRGGPRLYQQPAVTRDG-KVHHRELFCRIRDGQGELLSAELFM----------PMVQ-QLGLSEQy 466
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 338 DAAELEKVLP-----VGVKFGINIAPDHLHSESFKADIQKLLTSLPAHHFQ-IVLEITERDMLKEQEATQ-LFAWLHSVG 410
Cdd:PRK11059  467 DRQVIERVLPllrywPEENLSINLSVDSLLSRAFQRWLRDTLLQCPRSQRKrLIFELAEADVCQHISRLRpVLRMLRGLG 546
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877448828 411 VEIAIDDFG-----TGhsaliYLERFTLDYLKIDRGFINAIGTKT-----ITSpvldavLTLA-KRLNMLTVAEGVETPE 479
Cdd:PRK11059  547 CRLAVDQAGltvvsTS-----YIKELNVELIKLHPSLVRNIHKRTenqlfVRS------LVGAcAGTETQVFATGVESRE 615
                         250       260
                  ....*....|....*....|....*
gi 1877448828 480 QARWLSERGVNFMQGYWISRPLPLD 504
Cdd:PRK11059  616 EWQTLQELGVSGGQGDFFAESQPLD 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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