NCBI Conserved Domain Search

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Conserved domains on [gi\|94968372\|ref\|YP_590420.1\|]
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

113977

pfam05226

CHASE2

CHASE2 domain

true

false

243

1e-39

160.18

97.12

7,61,5,36,97,43,33,162,76,35,240,111,34,292,145,14,315,159,2,329,161,80

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968372  62 IELRSLDARFEMRGSRQTDLDIVIIGVDEKTLRKTG--YPIPRRAYASLVNKLASAGCKVIGFDLDFPTAEnnsaldvln 139
pfam05226     6 LELALYDLRLRLRPPEPPDPRIVIVAIDEASLAQALgrWPWPRSVLARLLDKLAAAQPKAIGLDIYFDEPS--------- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968372 140 rlkgqagahtspefmseidnqiaSSDNDAAFGEAVAKAGNVILGHVFLDSQQKAQSLSsqeaedyykllwdhpfpqthpy 219
pfam05226    77 -----------------------SPPGDEALAAALKRSPNLVVLPVLLEDNDGDGRGT---------------------- 111

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968372 220 pdganfspadafmrqkgntvfGVEPNIAKIAERAKSIGYLDTVFDADGTIRRVPLliyykdldfvppieiemlRYLENIS 299
pfam05226   112 ---------------------EVAPPPPALAAAAARIGFVDLVLDADGVVRRVLL------------------FEGSGCQ 152

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968372 300 IDDSNAFigqsgvheiRLgahaihpakdgtALINYAGPYKTYPHYSLADVLTGEVSPATFHNKIVFVGPTAKGMGDMRIT 379
pfam05226   153 TWPSFAL---------RL------------ALLNYRGPPGTFPTVSLADVLNGRVPPELLKDKIVLIGATAPGLGDLFPT 211

                       330       340       350
                ....*....|....*....|....*....|
gi 94968372 380 PFSTPEAAYMGVEIHANVLDNLLHSENPRR 409
pfam05226   212 PYSRSLELMPGVEIHANAVSQLLQGAALDG 241

cl01732

120848

CHASE2

CHASE2 domain

-1

109276

pfam00211

Guanylate_cyc

Adenylate and Guanylate cyclase catalytic domain

true

false

185

2e-29

126.21

96.76

7,532,6,79,614,85,10,625,95,24,650,119,27,679,146,11,690,161,15,706,176,9

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968372 533 RELTVMFSDIRGFTEISEGLTPDELVHLLNRYLGDMTGVIFESLGTLDKYIGDAIMAFWGSPVPQSDHAYRACETALKMs 612
pfam00211     7 DNVTILFADIVGFTALSSRHSPEELVRLLNDLYTRFDELLDKHGVYKVKTIGDAYMAASGLPPAAAHHAALLADMALDM- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968372 613 vaLNDLNQRLTHeGKKTLKIGIGINSGQMNVGNMGSEfRFAWTVMGDNVNLASRLEGQTKAYKTMrlITEFTYEEVKD-- 690
pfam00211    86 --VETIEEVNVG-HANGLRVRIGIHTGPVVAGVIGAR-RPRYDVWGDTVNVASRMESTGVPGKIH--VSEETYRLLKGee 159

                       170       180
                ....*....|....*....|....*..
gi 94968372 691 --QMVCRQLDVIRVQGKeKPVAIYELM 715
pfam00211   160 sfQFRLEPRGEVPVKGK-GPMETYFLN 185

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

5e-29

124.90

92.07

6,495,6,37,532,44,88,627,132,22,654,154,22,678,176,12,690,189,26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968372 496 EREKRKVRKTFERYVAPGVIKLIEENPEKYFRTGGEM-RELTVMFSDIRGFTEISEGLTPDELVHLLNRYLGDMTGVIFE 574
COG2114       7 LLAKEAKVAAAGLRSDLVLRLYLARVVGRLLARGGAGdRRVTLLFADIVGSTELSESLGDEALVELLNLYFDAVAEVVAR 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968372 575 SLGTLDKYIGDAIMAFWGSPVPQSDHAYRACETALKMSVALNDLNQrlthegkKTLKIGIGINSGQMNVGNMGSEfrfaw 654
COG2114      87 HGGRVVKFIGDGFLAVFGRPSPLEDAVACALDLQLALRNPLARLRR-------ESLRVRIGIHTGEVVVGNTGGY----- 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 94968372 655 TVMGDNVNLASRLEGQTKAYKTmrLITEFTYEEVKD-QMVCRQLDVIRVQGKEKPVAIYELMD 716
COG2114     155 TVVGSAVNQAARLESLAKPGQV--LLSEATYDLVRDlVDLFSGLGSHRLKGLARPVRVYQLCH 215

cl00925

141019

Guanylate_cyc

Adenylate and Guanylate cyclase catalytic domain

-1

33975

COG4252

Predicted transmembrane sensor domain [Signal transduction mechanisms]

false

400

3e-28

122.00

69.50

9,61,40,36,97,77,30,160,107,21,227,128,20,251,148,44,295,194,19,314,214,3,317,221,72,389,294,24

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968372  62 IELRSLDARFEMRGSRQTDLDIVIIGVDEKTLRKTG-YPIPRRAYASLVNKLASAGCKVIGFDLDFPtaennsaldvlnr 140
COG4252      41 LELAAFDQLLRLRPSEPPDDRILIVAIDEQDLESLGqWPWPRAALARLLDKLAAAQPRAIGLDIYRD------------- 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968372 141 lkgqagahtspefmseidnqIASSDNDAAFGEAVAKAGNVIlghvfldsqqkaqslssqeaedyykllwdhpfpqthpyp 220
COG4252     108 --------------------LPSSPGDRALAAVLQRAPNLI--------------------------------------- 128

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968372 221 dganfspADAFMRQKGNTVFGVEPNIAkiaeRAKSIGYLDTVFDADGTIRRVPLLIYYKDLDFVPPIEIEMLRYL--ENI 298
COG4252     129 -------GVEKLSGDPGIAVNPPPELP----RQAQIGFSDLILDSDGKVRRLLLAATPGPEPKYSLALKLALQYLasLGI 197

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968372 299 SIDDSNAFIGQSGVHE-IRL----GAHAIHPAKDGTALINYAGPYKTYPHYSLADVLTGEVSPATFHNKIVFVGPTAKGM 373
COG4252     198 SPKYPDPERLRLGKTTlPRLlgnsGGYQGADAGGYQILLNYRSSSSDFRTVSLRDVLNGKVPAELIRGRIVLIGATAPSL 277

                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 94968372 374 GDMRITPFSTPEAAYM-GVEIHANVLDNLLHSENPRRGFLK 413
COG4252     278 NDYFATPYSSSLKELVpGVEIHANIVSQILSALLDGRPLLP 318

cl01732

120848

CHASE2

CHASE2 domain

-1

128359

smart00044

CYCc

Adenylyl- / guanylyl cyclase, catalytic domain

false

194

6e-22

101.59

79.90

5,529,31,69,598,101,13,614,114,38,653,152,23,678,175,11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968372 530 GEMRELTVMFSDIRGFTEISEGLTPDELVHLLNRYLGDMTGVIFESLGTLDKYIGDAIMAFWGSPVPQS-DHAYRACETA 608
smart00044   32 ESYDNVTILFTDIVGFTTLSSEATPEQVVTLLNDLYSRFDRIIDRHGGYKVKTIGDAYMVVSGLPTEALvDHAELAADEA 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968372 609 LKMsvaLNDLNQRLTHEGKKTLKIGIGINSGQMNVGNMGSEFRFaWTVMGDNVNLASRLEGQTKAYKTmrLITEFTYEEV 688
smart00044  112 LDM---VESLKTVLSQHRGNGLRVRIGIHTGPVVAGVVGITMPR-YCLFGDTVNLASRMESVGDPGQI--LVSEETYSLL 185


                .
gi 94968372 689 K 689
smart00044  186 R 186

cl00925

141019

Guanylate_cyc

Adenylate and Guanylate cyclase catalytic domain

-1