NCBI Conserved Domain Search

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Conserved domains on [gi\|117928819\|ref\|YP_873370.1\|]
diguanylate cyclase [Acidothermus cellulolyticus 11B]

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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

133472

cd01949

GGDEF

Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as domain of unknown function 1 (DUF1). It is widely present in bacteria and often links to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain has been suggested to be homologous to the adenylyl cyclase catalytic domain. This prediction correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesiveness in bacteria.

Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue...

true

false

true

157

2e-09

58.75

84.08

4,219,0,23,245,23,49,294,73,15,309,89,43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928819 220 HDAVTGLPNLAVFEQRLVRALARraaHQDGHREVAVILLQVLGVGRITDAHGATGVQAVLREIASRLLEIAPEHD-LGHL 298
cd01949        1 TDPLTGLPNRRAFEERLERLLAR---ARRSGRPLALLLIDLDHFKQINDTYGHAAGDEVLKEVARRLRSSLRESDlVARL 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 117928819 299 GASHFALIAHG-EPGAGIDLARTASEAVETPLVLPFGTVEVRCHLGVAVARDADT 352
cd01949       78 GGDEFAILLPGtDLEEAEELAERLRKAIEEPFFIDGEEIRVTASIGIAEYPEDGE 132

cl00291

140583

GGDEF

Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue...

128563

smart00267

GGDEF

diguanylate cyclase

false

163

1e-10

62.65

90.80

7,215,0,19,237,19,34,271,54,5,277,59,17,294,77,13,307,91,40,347,142,6

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928819 216 RRALHDAVTGLPNLAVFEQrlvRALARRAAHQDGHREVAVILLQVLGVGRITDAHG-ATGVQaVLREIASRLLEIAPEHD 294
smart00267     1 RLAFRDPLTGLPNRRYFEE---ELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGhAVGDE-LLQEVAQRLSSCLRPGD 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 117928819 295 -LGHLGASHFALIA-HGEPGAGIDLARTASEAVETPLVLPFGTVEVRCHLGVAVA-----------RDADTA 353
smart00267    77 lLARLGGDEFALLLpETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYpnpgedaedllKRADTA 148

cl00291

140583

GGDEF

Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue...

-1

32381

COG2199

c-di-GMP synthetase (diguanylate cyclase, GGDEF domain) [Signal transduction mechanisms]

c-di-GMP synthetase (diguanylate cyclase, GGDEF domain) [Signal transduction...

false

181

1e-09

58.98

75.69

4,214,16,28,245,44,49,294,94,20,314,115,38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928819 215 RRRALHDAVTGLPNLAVFEQRLVRALARraaHQDGHREVAVILLQVLGVGRITDAHGATGVQAVLREIASRLLEIAPEHD 294
COG2199       17 ERLALHDPLTGLPNRRAFEERLERALAR---ARRHGEPLALLLLDLDHFKQINDTYGHAAGDEVLREVARRLRSNLREGD 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928819 295 -LGHLGASHFALIAHGEPGAG-IDLARTASEAVETPLVLPFGTVEVRCHLGVAVARDADT 352
COG2199       94 lVARLGGDEFAVLLPGTSLEEaARLAERIRAALEEPFFLGGEELRVTVSIGVALYPEDGS 153

cl00291

140583

GGDEF

Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue...

-1

110022

pfam00990

GGDEF

GGDEF domain

false

160

4e-05

44.16

93.12

7,217,0,17,237,17,34,271,52,3,275,55,20,295,76,11,306,91,41,347,143,6

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928819 218 ALHDAVTGLPNLAVFEQrlvRALARRAAHQDGHREVAVILLQVLGVGRITDAHG-ATGvQAVLREIASRLLEIAPEHDL- 295
pfam00990      1 AAHDPLTGLPNRRYFEE---ELEQELQRAQRRQSPLALLLLDLDNFKRINDTYGhAVG-DEVLQEVAQRLSSSLRRSDLv 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117928819 296 GHLGASHFALI----AHGEPGAGIDLARTASEAVETPLVLPFGTVEVRCHLGVAVA-----------RDADTA 353
pfam00990     77 ARLGGDEFAILlpdtSLEGAQELAERIRRLLAALKIPHTLSGLPLYVTISIGIAAYpndgedaedllKRADQA 149

cl00291

140583

GGDEF

Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue...

-1

33501

COG3706

PleD

Response regulator containing a CheY-like receiver domain and a GGDEF domain [Signal transduction mechanisms]

Response regulator containing a CheY-like receiver domain and a GGDEF domain [Signal...

false

true

false

435

4e-04

41.06

30.57

5,214,266,33,250,299,38,288,338,19,307,358,19,326,378,21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928819 215 RRRALHDAVTGLPNLAVFEQRLVRALARRAAHQdghREVAVILLQVLGVGRITDAHGATGVQAVLREIASRLLE-IAPEH 293
COG3706      267 QELALVDGLTGLFNRRYFDEHLADLWKRALREG---RPLSLLMLDIDDFKEINDTYGHDVGDEVLRQVARRLRQtVRGLD 343

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 117928819 294 DLGHLGASHFALIA-HGEPGAGIDLARTASEAVE-TPLVLPFGTVEVRCHLGVAVA 347
COG3706      344 LVARYGGEEFAVVLpDTDLEAAIAIAERIRQKINeLPFVHELSREPLEVTISIGVA 399

-1

137662

PRK10060

RNase II stability modulator; Provisional

false

true

false

663

0.003

38.17

21.72

9,220,239,8,233,247,61,294,309,9,303,319,10,316,329,11,328,340,5,333,347,6,339,355,8,347,374,9

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928819 221 DAVTGLPNlavfeQRLVRALARRAAHQDGHREVAVILLQVLGVGRITDAHGATGVQAVLREIASRLLEIAPEHD-LGHLG 299
PRK10060     240 DSITGLPN-----RNAIQELIDHAIAQADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQtLARLG 314

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117928819 300 ASHF-ALIAHGEPGAgidLARTASEAVETpLVLPF--GTVEVR--CHLGVAVA-----------RDADTAGHV 356
PRK10060     315 GDEFlVLASHTSQAA---LEAMASRILTR-LRLPFriGLIEVYtgCSIGIALSpehgddsesliRSADTAMYT 383

-1

active site	0	10	10	true	133472	cd01949	GGDEF
I-site	1	3	3	true	133472	cd01949	GGDEF