NCBI Conserved Domain Search

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Conserved domains on [gi\|116624015\|ref\|YP_826171.1\|]
diguanylate phosphodiesterase [Solibacter usitatus Ellin6076]

Graphical summary show options »	Show site features Horizontal zoom: ×	?



List of domain hits		?

References:

Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.

Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.

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of the residues that compose this conserved feature have been mapped to the query sequence.

Click on the triangle to view details about the feature, including a multiple sequence alignment of your query sequence and the protein sequences used to curate the domain model, where hash marks (#) above the aligned sequences show the location of the conserved feature residues.

The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions. Click on the triangle for interactive 3D structure viewing options.

This image shows a graphical summary of conserved domains identified on the query sequence. The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits (labeled illustration) or all hits (labeled illustration).
Domains are color coded according to superfamilies to which they have been assigned. Hits with scores that pass a domain-specific threshold (specific hits) are drawn in bright colors. Others (non-specific hits) and superfamily placeholders are drawn in pastel colors.
if a domain or superfamily has been annotated with functional sites (conserved features), they are mapped to the query sequence and indicated through sets of triangles with the same color and shade of the domain or superfamily that provides the annotation.
Mouse over the colored bars or triangles to see descriptions of the domains and features. click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.

The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores. Click on the PssmId to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.

To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page, or click on the triangles, if present, that represent functional sites (conserved features) mapped to the query sequence.

Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence. (labeled illustration)
Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance. (labeled illustration)
Four types of hits can be shown, as available, for each region on the query sequence:

specific hits meet or exceed a domain-specific e-value threshold (illustrated example) and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the advanced search options)
the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains

The CD-Search help document provides more detail about the tool and its features.

Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool (CDART).

Modify your query to search against a different database and/or use advanced search options

30163

cd01948

EAL

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.

EAL domain. This domain is found in diverse bacterial signaling proteins. It is called...

true

false

true

240

7e-15

76.79

62.92

6,59,84,28,88,112,17,105,131,33,138,166,8,146,177,13,159,195,40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624015  60 FLEIGLAAVSPERPVFINHTRHLLALDPiLPADRCVVEVLEDVTAD--PDTVACLHRLKSLNYRIALDDFVYDDSLLPMI 137
cd01948       85 RLSVNLSARQLRDPDFLDRLLELLAETG-LPPRRLVLEITESALIDdlEEALATLRRLRALGVRIALDDFGTGYSSLSYL 163

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116624015 138 E--IADYIKLD---LLALGAGGFHEQM-----NLLHRFDVRIVAEKIESEAEFRWCRKIGCDLFQGYYLRRP 199
cd01948      164 KrlPVDYLKIDrsfVRDIETDPEDRAIvraiiALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235

cl00290

140582

EAL

EAL domain. This domain is found in diverse bacterial signaling proteins. It is called...

-1

109613

pfam00563

EAL

EAL domain

false

236

6e-19

90.17

96.61

12,8,8,16,24,25,13,37,46,16,53,64,10,63,79,14,77,103,17,94,121,6,100,128,27,127,156,12,139,169,7,146,178,13,159,196,40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624015   9 SEGNVYLGRQPIYGAR-REIRAYELLYRRH--------ASDTTASFQDPDQASA--DVMLKAFLEI-----GLAAVSPER 72
pfam00563      9 ENGEFSLYFQPIVDLRtGKVLGYEALLRWQhpdgglipPDEFLPLAERLGLIAEldRWVLEKALAQlaewrGNALLPPDL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624015  73 PVFIN----------HTRHLLALDPILPADRC-VVEVLE-DVTADPDTVACLHRLKSLNYRIALDDF-VYDDSLLPMIEI 139
pfam00563     89 PLSVNlspaslldpsFLEALLALKQGGLPPSRlVLEITEsDLDEDLRLLEALARLRSLGFRLALDDFgTGYSSLSYLSRL 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116624015 140 -ADYIKLD--LLALGAGGFHEQM-----NLLHRFDVRIVAEKIESEAEFRWCRKIGCDLFQGYYLRRP 199
pfam00563    169 pPDYIKIDrsFIKDLSDPESRALlraliALARELGIKVVAEGVETEEQLELLKELGIDYVQGYLFSKP 236

cl00290

140582

EAL

EAL domain. This domain is found in diverse bacterial signaling proteins. It is called...

-1

32382

COG2200

Rtn

c-di-GMP phosphodiesterase class I (EAL domain) [Signal transduction mechanisms]

false

256

3e-15

78.06

58.98

5,59,88,25,85,113,16,101,131,37,138,170,20,158,198,41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624015  60 FLEIGLAAVSPERPVFINHTRHLLAlDPILPADRCVVEVLED--VTADPDTVACLHRLKSLNYRIALDDFVYDDSLLPMI 137
COG2200       89 RLAVNLSPVQLRSPGLVDLLLRLLA-RLGLPPHRLVLEITESalIDDLDTALALLRQLRELGVRIALDDFGTGYSSLSYL 167

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116624015 138 E--IADYIKLDLLALGAGGFHEQ--------MNLLHRFDVRIVAEKIESEAEFRWCRKIGCDLFQGYYLRRP 199
COG2200      168 KrlPPDILKIDRSFVRDLETDARdqaivraiVALAHKLGLTVVAEGVETEEQLDLLRELGCDYLQGYLFSRP 239

cl00290

140582

EAL

EAL domain. This domain is found in diverse bacterial signaling proteins. It is called...

-1

128367

smart00052

EAL

Putative diguanylate phosphodiesterase

false

241

6e-15

77.25

51.04

6,88,113,19,107,134,23,130,158,9,139,168,7,152,175,7,159,196,40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624015  89 LPADRCVVEVLEDVTADPD--TVACLHRLKSLNYRIALDDFVYD-DSLLPMIEI-ADYIKLDllalgaGGFHEQM----- 159
smart00052   114 LPPQRLELEITESVLLDDDesAVATLQRLRELGVRIALDDFGTGySSLSYLKRLpVDLLKID------KSFVRDLqtdpe 187

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 116624015 160 ---------NLLHRFDVRIVAEKIESEAEFRWCRKIGCDLFQGYYLRRP 199
smart00052   188 deaivqsiiELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 236

cl00290

140582

EAL

EAL domain. This domain is found in diverse bacterial signaling proteins. It is called...

-1

117241

pfam08668

HDOD

HDOD domain

true

false

196

1e-14

76.50

64.80

3,206,0,78,284,85,34,318,120,7

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624015 207 IPSSQLSVLSLLAECADLESSAGVIAAIIARDAPLTYGLLRLANSALYRHRSEIRSPAQAVTLLGMDFVFRWATLLAL-- 284
pfam08668      1 LPTLPDVVLRILALLEDPDVSISDIAELISRDPALTARLLRLANSAYYGFRRKISSIEQAVARLGLRTVRNLVLSLSVkr 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 116624015 285 -----SGNDDCPAGYLEAALQRARMAELLGVHYRCSSQE-AYIAGLL 325
pfam08668     81 ifrgtPSLGFDLKGFWRHSLACALAARLLARRLGLDDPEeAFTAGLL 127

cl00076

140417

HDc

Metal dependent phosphohydrolases with conserved 'HD' motif

-1

31826

COG1639

Predicted signal transduction protein [Signal transduction mechanisms]

false

289

3e-10

61.51

43.94

4,206,22,66,272,92,21,293,116,19,312,136,13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624015 207 IPSSQLSVLSLLAECADLESSAGVIAAIIARDAPLTYGLLRLANSALYRHRSEIRSPAQAVTLLGM----DFVFRWATLL 282
COG1639       23 LPPLPDVVLKLQKACSDPNVSLSDIAELISQDPALTARLLRLANSPYFGFPREITTLNEAIVRLGIglviNLVLALAEQA 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 116624015 283 ALSGNDDCPAG---YLEAALQRARMAELLGVHY-RCSSQEAYIAGLL 325
COG1639      103 IQSVNSSSAEDrqlFWDTAIETAMIAEGLARALgRADSDEAYTAGLL 149

cl00076

140417

HDc

Metal dependent phosphohydrolases with conserved 'HD' motif

-1

33240

COG3434

Predicted signal transduction protein containing EAL and modified HD-GYP domains [Signal transduction mechanisms]

Predicted signal transduction protein containing EAL and modified HD-GYP domains [...

true

false

407

1e-57

218.99

91.65

5,12,2,71,83,75,48,131,125,155,286,281,26,312,308,67

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624015  13 VYLGRQPIYGARREIRAYELLYRRHASDTTASFQDPDQASADVMLKAFLEIGLAAVSPERPVFINHTRHLL--ALDPILP 90
COG3434        3 SFVARQPILDRNKEVFGYELLFREGEKNKYPEDVDNSRATYRIIIEEFVIQGIDKLANGKKCFINFPEELLisDLPELLP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624015  91 ADRCVVEVLEDVTADPDTVACLHRLKSLNYRIALDDFVYDD--SLLPMIEIADYIKLDLLALGAGGFHEQMNLLHRFDVR 168
COG3434       83 PDKVVIEILEDCPPTEKLLSAIKELKQKGYLLALDDFIFSNvsEWKPLLPLSDIVKIDFKRVTFDKARLFDRDLGYINKK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624015 169 IVAEKIESEAEFRWCRKIGCDLFQGYYLRRPEVLVGRRIPSSQLSVLSLLAECADLESSAGVIAAIIARDAPLTYGLLRL 248
COG3434      163 FLAEKVETEEEFEQAKKAGFDLFQGYFFSKPEIIKRGRLSPFLKTTIELLYEVIKPEVDVKRIENIIERDVGLSYKLLKF 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624015 249 ANSALYRHRSEIRSPAQAVTLLGMDFVFRWATLLALSG-NDDCPAGYLEAALQRARMAELLGVHY-RCSSQEAYIAGLLS 326
COG3434      243 VNSSYPRKSKKIQSIQQAVVYLGQENIRKFVSLLAMSElSDKKPEELYKLSLTRAKFCELLAKRYsPEYSEEAFLIGMFS 322

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 116624015 327 TLDAIFNAPLEELIVPLPIDIRFKRAILQREGALGGVLDAVLAYESGEFSGVD 379
COG3434      323 LLDELLDEDIESLVRELPISEEVVQALEKRYGELGQLLSLVELLENADWEEVL 375

-1

137515

PRK09776

putative sensor protein; Provisional

false

true

false

1116

4e-06

47.78

13.53

6,62,953,25,88,978,22,110,1002,28,138,1032,8,146,1042,13,159,1061,43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624015   63 IGLAAVSPERPVFINHTRHLLALDPiLPADRCVVEVLEDVTADPDTVA--CLHRLKSLNYRIALDDFVYDDSLLPMIE-- 138
PRK09776      954 IPLSVASLSSATLLPFLLEQLENSP-LPPRLLHLEITETALLNHAEAAsrLVQKLRLAGCRVVLDDFGRGLSSFNYLKaf 1032

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116624015  139 IADYIKLD--LLALGAGGFHEQM------NLLHRFDVRIVAEKIESEAEFRWCRKIGCDLFQGYYLRRPEVL 202
PRK09776     1033 MADYLKIDgeLCANLQGNLMDEMlvsiinGIAQRLGMKTIAGPVELPLTLDTLSGIGVDLAQGYVIGRPQPL 1104

-1

34551

COG4943

Predicted signal transduction protein containing sensor and EAL domains [Signal transduction mechanisms]

Predicted signal transduction protein containing sensor and EAL domains [Signal...

false

true

false

524

9e-06

46.49

28.63

5,59,354,31,91,385,19,110,405,29,139,436,23,162,467,37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624015  60 FLEIGLAAVSPERPVFINHTRHLLALDPILPaDRCVVEVLEDVTADPDTVA-CLHRLKSLNYRIALDDFVYDDSLLPMIE 138
COG4943      355 HVSINLSASDLASPRLIDRLNRKLAQYQVRP-QQIALELTERTFADPKKMTpIILRLREAGHEIYIDDFGTGYSNLHYLQ 433

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116624015 139 I--ADYIKLDLLALGAGGFHEQMNLL--------HRFDVRIVAEKIESEAEFRWCRKIGCDLFQGYYLRRP 199
COG4943      434 SlpVDALKIDKSFVDTLGTDSASHLIaphiiemaKSLGLKIVAEGVETEEQVDWLRKRGVHYGQGWLFSKA 504

-1

139666

PRK13561

putative phosphodiesterase; Provisional

false

true

false

651

1e-05

45.91

23.04

5,60,487,30,91,517,15,106,534,32,138,571,8,146,584,53

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624015  61 LEIGLAAVSPERPVFINHTRHLLALDPILPaDRCVVEVLEDVTADP--DTVACLHRLKSLNYRIALDDFVYDDSLLPMIE 138
PRK13561     488 LSVNLSALQLMHPNMVADMLELLTRYRIQP-GTLILEVTESRRIDDphAAVAILRPLRNAGVRIALDDFGMGYAGLRQLQ 566

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116624015 139 -----IADYIKLD-----LLALGAGGFHEQMNLLHRFDVRIVAEKIESEAEFRWCRKIGCDLFQGYYLRRP 199
PRK13561     567 hmkslPIDVLKIDkmfvdGLPEDSSMVAAIIMLAQSLNLQMIAEGVETEAQRDWLAKAGVGVAQGFLFARP 637

-1

137979

PRK10551

hypothetical protein; Provisional

false

true

false

518

2e-05

45.43

18.34

3,114,405,24,138,431,16,154,455,45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624015 115 LKSLNYRIALDDFVYDDSLLPMIE--IADYIKLDLLALGAGG--------FHEQMNLLHRFDVRIVAEKIESEAEFRWCR 184
PRK10551     406 LHSQGIEIAIDDFGTGHSALIYLErfTLDYLKIDRGFINAIGtetvtspvLDAVLTLAKRLNMLTVAEGVETPEQARWLR 485

                         90
                 ....*....|....*
gi 116624015 185 KIGCDLFQGYYLRRP 199
PRK10551     486 EHGVNFLQGYWISRP 500

-1

138538

PRK11359

cAMP phosphodiesterase; Provisional

false

true

false

799

2e-04

42.52

4.63

1,162,744,37

                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 116624015 163 HRFDVRIVAEKIESEAEFRWCRKIGCDLFQGYYLRRP 199
PRK11359     745 QSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRP 781

-1

34606

COG5001

Predicted signal transduction protein containing a membrane domain, an EAL and a GGDEF domain [Signal transduction mechanisms]

Predicted signal transduction protein containing a membrane domain, an EAL and a GGDEF...

false

true

false

663

0.001

39.62

20.06

4,78,503,22,100,530,15,118,545,40,158,595,41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624015  79 TRHLLALDPILPADRCVVEVLE-----DVTADPDTVACLHRLkslNYRIALDDFVYDDSLLPMIEIADYIKLDLLALGAG 153
COG5001      504 RLLAIVSESCIAPHRLDFEITEtaivcDFDQARDALAALHEL---GVRTALDDFGTGYSSLSHLRALPLDKIKIDRSFVS 580

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 116624015 154 GFHEQ----------MNLLHRFDVRIVAEKIESEAEFRWCRKIGCDLFQGYYLRRP 199
COG5001      581 DLEENptsedivrtvLQLGRNLRMECVVEGVETEAQRDRVAALGATVMQGYHYARP 636

-1