NCBI Conserved Domain Search

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Conserved domains on [gi\|29829578\|ref\|NP_824212.1\|]
hypothetical protein SAV_3036 [Streptomyces avermitilis MA-4680]

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

28958

cd00077

HDc

Metal dependent phosphohydrolases with conserved 'HD' motif

true

false

true

145

1e-14

76.27

99.31

3,271,0,48,326,48,28,354,83,61

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29829578 272 GYTRGHSERVGQASMMIARELGMDDERAEVLRFAGILHDVGKLGVPTRllrkdgpLTPEERRIIELHPEYGHEMVRGIGF 351
cd00077       1 EHRFEHSLRVAQLARRLAEELGLSEEDIELLRLAALLHDIGKPGTPDA-------ITEEESELEKDHAIVGAEILRELLL 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29829578 352 LGE-------ARSAILHHHERLDGSGYPYGLTGAQIPEFARVVAVADAFDAMTSTRSYRRARPVAAALEEL 415
cd00077      74 EEViklidelILAVDASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRRDSREKRRRIAEEDLEEL 144

cl00076

140417

HDc

Metal dependent phosphohydrolases with conserved 'HD' motif

110919

pfam01966

HD domain

false

108

6e-11

63.80

87.96

5,276,3,19,298,22,15,315,37,8,328,45,23,351,69,29

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29829578 277 HSERVGQASMMIARELGMDderAEVLRFAGILHDVGKlgVPTRLLRKdgpltPEERRIIELHPEYGHEMVRGIGF-LGEA 355
pfam01966     4 HSLRVALLARELAEELGLD---PELLLLAALLHDIGK--DPFGFLEK-----LEDFGIFKSHSVVGAEILRELEKrLGVD 73

                        90       100
                ....*....|....*....|....*
gi 29829578 356 RSAILHHHERLDGSGYPYGLTGAQI 380
pfam01966    74 LELILEHHESWEGAGYEPISLEARI 98

cl00076

140417

HDc

Metal dependent phosphohydrolases with conserved 'HD' motif

-1

128747

smart00471

HDc

Metal dependent phosphohydrolases with conserved 'HD' motif.

false

124

3e-09

58.46

79.03

4,276,7,21,299,28,26,333,54,21,354,79,26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29829578 277 HSERVGQASMMIARELGMDDEraEVLRFAGILHDVGKLGVPTRLLRKDGpltpeerrIIELHPEYGHEMVRGIGFLGE-- 354
smart00471    8 HSLRVAQLAAALAEELGLLDI--ELLLLAALLHDIGKPGTPDSFLVKTS--------VLEDHHFIGAEILLEEEEPRIle 77

                        90       100
                ....*....|....*....|....*...
gi 29829578 355 --ARSAILHHHERLDGSGYPYGLTGAQI 380
smart00471   78 eiLATAILSHHERPDGLRGEPITLEARI 105

cl00076

140417

HDc

Metal dependent phosphohydrolases with conserved 'HD' motif

-1

129378

TIGR00277

HDIG

uncharacterized domain HDIG

false

3e-05

45.01

90.00

4,276,7,19,298,26,15,325,41,11,337,52,27

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29829578 277 HSERVGQASMMIARELGMDderAEVLRFAGILHDVGKlgvptrllrkdgPLTPEERRIIElHPEYGHEMVRGIGFLGEAR 356
TIGR00277     8 HSLEVAKLAEALARELGLD---VELARRGALLHDIGK------------PITREGVIFES-HAVVGAEIARKYGEPLEVI 71


                ....*...
gi 29829578 357 SAILHHHE 364
TIGR00277    72 DIIAEHHG 79

cl00076

140417

HDc

Metal dependent phosphohydrolases with conserved 'HD' motif

-1

117241

pfam08668

HDOD

HDOD domain

false

196

5e-05

44.53

50.00

5,276,97,20,296,118,5,304,123,10,314,144,23,337,168,27

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29829578 277 HSERVGQASMMIARELGMDD-ERAEVlrfAGILHDVGKL-----------GVPTRLLRKDGPLTPEERRIIEL-HPEYGH 343
pfam08668    98 HSLACALAARLLARRLGLDDpEEAFT---AGLLHDIGKLillsllpdeyeEILERVAAEGISLLEAERELLGTdHAEVGA 174

                        90       100
                ....*....|....*....|.
gi 29829578 344 EMVRGIGFLGEARSAILHHHE 364
pfam08668   175 ALLERWNLPEELVEAIAYHHD 195

cl00076

140417

HDc

Metal dependent phosphohydrolases with conserved 'HD' motif

-1

32388

COG2206

c-di-GMP phosphodiesterase class II (HD-GYP domain) [Signal transduction mechanisms]

false

true

false

344

1e-47

185.73

54.94

3,251,125,15,266,141,84,350,226,88

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29829578 252 ERAAHQATIRALVQA-VDIKDGYTRGHSERVGQASMMIARELGMDDERAEVLRFAGILHDVGKLGVPTRLLRKDGPLTPE 330
COG2206     126 AREIVKKALVALARGdIKAKDDYTYGHSVRVAELAEAIAKKLGLSEEKIEELALAGLLHDIGKIGIPDSILNKPGKLTEE 205

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29829578 331 ERRIIELHPEYGHEMVRGIG-FLGEARSAILHHHERLDGSGYPYGLTGAQIPEFARVVAVADAFDAMTSTRSYRRARPVA 409
COG2206     206 EFEIIKKHPIYGYDILKDLPeFLESVRAVALRHHERWDGTGYPRGLKGEEIPLEARIIAVADVYDALTSDRPYKKAKSPE 285

                       170       180
                ....*....|....*....|....*....
gi 29829578 410 AALEELERCAGAQFDPVMVGALVRALGRQ 438
COG2206     286 EALEELRKNSGGKFDPKVVDAFLKALSKY 314

-1

33243

COG3437

Response regulator containing a CheY-like receiver domain and an HD-GYP domain [Transcription / Signal transduction mechanisms]

Response regulator containing a CheY-like receiver domain and an HD-GYP domain [...

false

true

false

360

1e-37

153.15

51.94

2,247,159,102,349,262,84

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29829578 248 QYHRERAAHQATIRALVQAVDIKDGYTRGHSERVGQASMMIARELGMDDERAEVLRFAGILHDVGKLGVPTRLLRKDGPL 327
COG3437     160 ELAQIEDNLDETLEELAALLEVRDYETGDHLERVAQYSELLAELLGLSEEEVDLIKKAAPLHDIGKVAIPDSILLKPGKL 239

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29829578 328 TPEERRIIELHPEYGHEMVRGI-GFLGEARSAILHHHERLDGSGYPYGLTGAQIPEFARVVAVADAFDAMTSTRSYRRAR 406
COG3437     240 TSEEFEIMKGHPILGAEILKSSeRLMQVAAEIARHHHERWDGSGYPDGLKGDEIPLSARIVAIADVFDALVSGRPYKEAM 319

                       170       180
                ....*....|....*....|....*..
gi 29829578 407 PVAAALEELERCAGAQFDPVMVGALVR 433
COG3437     320 STEEALEIIRAQSGRLFDPKLVEAFIQ 346

-1

139166

PRK12705

hypothetical protein; Provisional

false

true

false

485

4e-05

44.71

14.23

4,276,302,19,298,321,15,314,336,2,330,338,33

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29829578 277 HSERVGQASMMIARELGMDderAEVLRFAGILHDVGKlGVptrllrkdgpltpeERRIIELHPEYGHEMVRGIGFLGEAR 356
PRK12705    303 HSLEVAFLAAILAALIGLD---PALAKKAGLLHDIGK-SV--------------DFESDGNHVEIGAELAKKFNEPDYVV 364


                ....*..
gi 29829578 357 SAILHHH 363
PRK12705    365 NAIASHH 371

-1

31608

COG1418

Predicted HD superfamily hydrolase [General function prediction only]

false

true

false

222

5e-05

44.29

31.53

3,276,39,19,298,58,15,328,73,36

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29829578 277 HSERVGQASMMIARELGMDderAEVLRFAGILHDVGKlgvptrllrkdgpltPEERRIIELHPEYGHEMVRGIGFLGEAR 356
COG1418      40 HSLRVAYLAYRIAEEEGVD---PDLALRAALLHDIGK---------------AIDHEPGGSHAEIGAEIARKFLEDPVVI 101


                ....*...
gi 29829578 357 SAILHHHE 364
COG1418     102 NAIEAHHG 109

-1

132362

TIGR03319

YmdA_YtgF

conserved hypothetical protein YmdA/YtgF

false

true

false

514

7e-05

43.76

13.62

5,276,332,23,302,355,11,314,366,6,323,372,3,337,375,27

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29829578 277 HSERVGQASMMIARELGMDDERAevlRFAGILHDVGKlGVPTRLlrkDGPltpeerriielHPEYGHEMVRGIGFLGEAR 356
TIGR03319   333 HSIEVAHLAGIMAAELGEDVKLA---KRAGLLHDIGK-AVDHEV---EGS-----------HVEIGAELAKKYKESPEVV 394


                ....*...
gi 29829578 357 SAILHHHE 364
TIGR03319   395 NAIAAHHG 402

-1

31899

COG1713

Predicted HD superfamily hydrolase involved in NAD metabolism [Coenzyme metabolism]

false

true

false

187

2e-04

42.16

35.29

4,276,20,25,304,45,18,322,66,11,337,77,9

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29829578 277 HSERVGQASMMIARELGMDDERAEVlrfAGILHDVGKLGVPTRLLR---KDGPLTPEERRiielHPEYGHEMV 346
COG1713      21 HCLGVAETAIELAEAYGLDPEKAYL---AGILHDIAKELPEQKLLKiakKYGLELDLERE----SPLLLHGKV 86

-1

31669

COG1480

Predicted membrane-associated HD superfamily hydrolase [General function prediction only]

false

true

false

700

0.002

39.54

13.57

5,273,489,22,298,511,23,321,536,5,326,546,5,331,552,32

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29829578 274 TRGHSERVGQASMMIARELGMDderAEVLRFAGILHDVGKLGVPTRLL--RKDGP-----LTPEE-RRIIELHPEYGHEM 345
COG1480     490 TYQHSVMVANLAEAAAEEIGAN---SLLARVGAYYHDIGKMKRPLFFIenQMGGKnphddLSPQLsALIIISHVKEGVEM 566

                        90
                ....*....|....*...
gi 29829578 346 VRGIGFLGEARSAILHHH 363
COG1480     567 AREYKLPQEIIDIIPEHH 584

-1

Zn2+ binding site	0	4	4	true	28958	cd00077	HDc
Mg2+ binding site	1	1	1	true	28958	cd00077	HDc