NCBI Conserved Domain Search

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Conserved domains on [gi\|116620542\|ref\|YP_822698.1\|]
adenylate cyclase [Solibacter usitatus Ellin6076]

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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

28942

cd00060

FHA

Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain. FHA domains may bind phosphothreonine, phosphoserine and sometimes phosphotyrosine. In eukaryotes, many FHA domain-containing proteins localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. Members of the FHA family include: Dun1, Rad53, Cds1, Mek1, KAPP(kinase-associated protein phosphatase),and Ki-67 (a human nuclear protein related to cell proliferation).

Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins....

true

false

true

102

7e-16

79.72

87.25

3,13,10,23,36,34,42,78,78,21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620542  14 ANGRRFPLGEGQSWAIGRGDGCA-VMLDSRSVSRLHALIQRRDTGDLALVDLGSRNGSFVNGRRVS--FPVVLNDSDKLV 90
cd00060       11 ASGRRYYLDPGGTYTIGRDSDNCdIVLDDPSVSRRHAVIRYDGDGGVVLIDLGSTNGTFVNGQRVSpgEPVRLRDGDVIR 90


                 ....*....
gi 116620542  91 FGDQDLVFR 99
cd00060       91 LGNTSISFR 99

cl00062

140403

FHA

Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins....

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...

true

false

227

1e-16

82.15

79.30

5,127,45,58,194,103,26,220,131,20,240,152,20,262,172,53

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620542 128 LTTIMVVDIRDFTPLARTLPEALLSQTIGTWFLRSGQIVQRLGSWAQKYIGDAVMAVWvhdqreqlgADLVRVLRAVTEI 207
COG2114       46 RVTLLFADIVGSTELSESLGDEALVELLNLYFDAVAEVVARHGGRVVKFIGDGFLAVF---------GRPSPLEDAVACA 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620542 208 SAATAEISRTLEL--PVPLRIGAGVNTGLAILGGT-DYTVLGDTVNVAFRLESATKsiGLGVAIGAPSYLGLGETARAGF 284
COG2114      117 LDLQLALRNPLARlrRESLRVRIGIHTGEVVVGNTgGYTVVGSAVNQAARLESLAK--PGQVLLSEATYDLVRDLVDLFS 194

                        170       180       190
                 ....*....|....*....|....*....|.
gi 116620542 285 VRKEVELKGYEGSSIAWAISFEDLKNNLYRA 315
COG2114      195 GLGSHRLKGLARPVRVYQLCHRSLRRNLELR 225

cl00925

141019

Guanylate_cyc

Adenylate and Guanylate cyclase catalytic domain

-1

109549

pfam00498

FHA

FHA domain

false

4e-15

77.25

100.00

2,26,0,52,78,53,14

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116620542  27 WAIGRGDGCAVMLDSRSVSRLHALIQRRDTGDLALVDLGSRNGSFVNGRRVS-FPVVLNDSDKLVFG 92
pfam00498      1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDGGGRFYLEDLGSTNGTFVNGQRLGpEPVRLRDGDRIRLG 67

cl00062

140403

FHA

Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins....

-1

109276

pfam00211

Guanylate_cyc

Adenylate and Guanylate cyclase catalytic domain

false

185

6e-10

59.96

89.73

8,129,9,55,184,71,6,190,78,19,221,97,17,238,116,2,240,121,20,262,141,22,284,166,9

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620542 130 TIMVVDIRDFTPLARTLPEALLSQTIGTWFLRSGQIVQRLGSWAQKYIGDAVMAV-------WVHDQR-EQLGADLVRVL 201
pfam00211     10 TILFADIVGFTALSSRHSPEELVRLLNDLYTRFDELLDKHGVYKVKTIGDAYMAAsglppaaAHHAALlADMALDMVETI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620542 202 RAVTEISAataeisrtlelpVPLRIGAGVNTGLAILG--GT---DYTVLGDTVNVAFRLESATKsiGLGVAIGAPSYLGL 276
pfam00211     90 EEVNVGHA------------NGLRVRIGIHTGPVVAGviGArrpRYDVWGDTVNVASRMESTGV--PGKIHVSEETYRLL 155

                        170       180
                 ....*....|....*....|
gi 116620542 277 GETARAGF---VRKEVELKG 293
pfam00211    156 KGEESFQFrlePRGEVPVKG 175

cl00925

141019

Guanylate_cyc

Adenylate and Guanylate cyclase catalytic domain

-1

128536

smart00240

FHA

Forkhead associated domain

false

1e-09

59.12

100.00

2,26,0,6,32,7,45

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 116620542  27 WAIGRG-DGCAVMLDSRSVSRLHALIQRRDTGDLALVDLGSRNGSFVNGRRV 77
smart00240     1 VTIGRSsEDCDIQLPGPSISRRHAEIVYDGGGRFYLIDLGSTNGTFVNGKRI 52

cl00062

140403

FHA

Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins....

-1

128359

smart00044

CYCc

Adenylyl- / guanylyl cyclase, catalytic domain

false

194

1e-09

59.22

69.07

7,129,37,17,146,55,6,153,61,31,192,92,2,194,97,28,222,128,16,238,149,22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620542 130 TIMVVDIRDFTPLARTL-PEALLSqTIGTWFLRSGQIVQRLGSWAQKYIGDAVMAVwvhdqreqLG---ADLVRVLRAVT 205
smart00044    38 TILFTDIVGFTTLSSEAtPEQVVT-LLNDLYSRFDRIIDRHGGYKVKTIGDAYMVV--------SGlptEALVDHAELAA 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116620542 206 EISAATAEISRTLELPV---PLRIGAGVNTGLAILG-----GTDYTVLGDTVNVAFRLESATK 260
smart00044   109 DEALDMVESLKTVLSQHrgnGLRVRIGIHTGPVVAGvvgitMPRYCLFGDTVNLASRMESVGD 171

cl00925

141019

Guanylate_cyc

Adenylate and Guanylate cyclase catalytic domain

-1

31902

COG1716

FOG: FHA domain [Signal transduction mechanisms]

false

true

false

191

5e-10

60.36

45.03

2,10,74,41,52,115,45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620542  11 TVEANGRRFPLGEGQSWAIGRGDGCAVMLDSRSVSRLHALIqRRDTGDLALVDLGSRNGSFVNGRRVSFPVVLNDSDKLV 90
COG1716       75 TIGLDEGSVIVLGEPVTTIGRDPDNDIVLDDDVVSRRHAEL-RREGNEVFLEDLGSTNGTYVNGEKVRQRVLLQDGDVIR 153


                 ....*..
gi 116620542  91 FGDQDLV 97
COG1716      154 LGGTLAE 160

-1

132397

TIGR03354

VI_FHA

type VI secretion system FHA domain protein

false

true

false

396

3e-06

47.75

20.45

6,16,18,9,28,27,13,41,42,14,56,56,8,65,64,10,75,78,21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620542  17 RRFPLGEGQswaIGRGDGCAVMLDS--RSVSRLHALIQRRDtGDLALVDLgSRNGSFVNGR----RVSFPVVLNDSDKLV 90
TIGR03354     19 KTFGTNGGT---IGRSEDCDWVLPDpeRHVSGRHARIRYRD-GAYLLTDL-STNGVFLNGSgsplGRGNPVRLEQGDRLR 93


                 ....*.
gi 116620542  91 FGDQDL 96
TIGR03354     94 LGDYEI 99

-1

33259

COG3456

Predicted component of the type VI protein secretion system, contains a FHA domain [Intracellular trafficking, secretion, and vesicular transport; Signal transduction mechanisms]

Predicted component of the type VI protein secretion system, contains a FHA domain [...

false

true

false

430

0.002

38.83

23.26

7,7,0,6,13,7,14,27,28,13,40,43,15,56,58,8,65,66,12,77,81,19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620542   8 PFLTVE-ANGRRFPLGEGQSW-------AIGRGDGCAVMLD--SRSVSRLHALIQRRDtGDLALVDLgSRNGSFVNGRRV 77
COG3456        1 PTLSLQvTNAQKLESGKAAQKlfdrgggVIGRSPDCDWQIDdpERFVSKQHCTISYRD-GGFCLTDT-SNGGLLVNGSDL 78

                         90       100
                 ....*....|....*....|..
gi 116620542  78 ---SFPVVLNDSDKLVFGDQDL 96
COG3456       79 plgEGSARLQQGDEILIGRYII 100

-1

phosphopeptide binding site

true

28942

cd00060

FHA