NCBI Conserved Domain Search

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Conserved domains on [gi\|94968829\|ref\|YP_590877.1\|]
adenylate/guanylate cyclase [Candidatus Koribacter versatilis Ellin345]

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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

109276

pfam00211

Guanylate_cyc

Adenylate and Guanylate cyclase catalytic domain

true

false

185

2e-27

119.28

79.46

4,403,7,88,494,95,5,500,100,18,519,118,36

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968829 404 SVSILCSDIRGFTRMSATMDAEDVVAMLNDYFLALTDCIFRNDGTVDKFVGDAILAVFGSPDADPQHHHKAVKAAMEMQV 483
pfam00211     8 NVTILFADIVGFTALSSRHSPEELVRLLNDLYTRFDELLDKHGVYKVKTIGDAYMAASGLPPAAAHHAALLADMALDMVE 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 94968829 484 AMRELNQRrgaRGEPVcEIGIGVHTGDVLHGFIGSpERMEYTIIGDAVNRTSRFCDGAGAAEIVISPEIHQY 555
pfam00211    88 TIEEVNVG---HANGL-RVRIGIHTGPVVAGVIGA-RRPRYDVWGDTVNVASRMESTGVPGKIHVSEETYRL 154

cl00925

141019

Guanylate_cyc

Adenylate and Guanylate cyclase catalytic domain

-1

32297

COG2114

CyaA

Adenylate cyclase, family 3 (some proteins contain HAMP domain) [Signal transduction mechanisms]

Adenylate cyclase, family 3 (some proteins contain HAMP domain) [Signal transduction...

false

227

3e-26

114.89

78.41

5,359,8,35,401,43,68,473,111,18,494,129,24,523,153,33

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968829 360 RLQMKLQANATVMERLLTNFSPRIRKRLLERAQQGklrlggeRSSVSILCSDIRGFTRMSATMDAEDVVAMLNDYFLALT 439
COG2114       9 AKEAKVAAAGLRSDLVLRLYLARVVGRLLARGGAG-------DRRVTLLFADIVGSTELSESLGDEALVELLNLYFDAVA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968829 440 DCIFRNDGTVDKFVGDAILAVFGSPDADPQhhhkAVKAAMEMQVAMRELNQRrgaRGEPVCEIGIGVHTGDVLHGFIGSp 519
COG2114      82 EVVARHGGRVVKFIGDGFLAVFGRPSPLED----AVACALDLQLALRNPLAR---LRRESLRVRIGIHTGEVVVGNTGG- 153

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 94968829 520 ermeYTIIGDAVNRTSRFCDGAGAAEIVISPEIHQYV 556
COG2114     154 ----YTVVGSAVNQAARLESLAKPGQVLLSEATYDLV 186

cl00925

141019

Guanylate_cyc

Adenylate and Guanylate cyclase catalytic domain

-1

128359

smart00044

CYCc

Adenylyl- / guanylyl cyclase, catalytic domain

false

194

5e-25

111.22

91.75

8,371,5,11,385,16,13,398,30,66,464,97,28,494,125,5,500,130,18,520,148,2,522,151,32

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968829 372 MERLLTNFSPRirkRLLERAQQGKLRL-GGERSSVSILCSDIRGFTRMSATMDAEDVVAMLNDYFLALTDCIFRNDGTVD 450
smart00044    6 TDRLLDQLLPA---SVAESLKRGGSPVpAESYDNVTILFTDIVGFTTLSSEATPEQVVTLLNDLYSRFDRIIDRHGGYKV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968829 451 KFVGDAILAVFGSP-DADPQHHHKAVKAAMEMQVAMRELNQRRgaRGEPVcEIGIGVHTGDVLHGFIGSpeRM-EYTIIG 528
smart00044   83 KTIGDAYMVVSGLPtEALVDHAELAADEALDMVESLKTVLSQH--RGNGL-RVRIGIHTGPVVAGVVGI--TMpRYCLFG 157

                       170       180
                ....*....|....*....|....*.
gi 94968829 529 DAVNRTSRFCDGAGAAEIVISPEIHQ 554
smart00044  158 DTVNLASRMESVGDPGQILVSEETYS 183

cl00925

141019

Guanylate_cyc

Adenylate and Guanylate cyclase catalytic domain

-1