NCBI Conserved Domain Search

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Conserved domains on [gi\|117927754\|ref\|YP_872305.1\|]
metal dependent phosphohydrolase [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

28958

cd00077

HDc

Metal dependent phosphohydrolases with conserved 'HD' motif

true

false

true

145

1e-17

85.90

99.31

3,244,0,56,300,58,29,331,87,57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927754 245 YYTRGHSERVARAAVMIGRRLGMREDRLEMLRYAGMLHDVGKLGVPTRLLQKTGPL--DAAEFSAIKLHSVRGCEVIGDI 322
cd00077        1 EHRFEHSLRVAQLARRLAEELGLSEEDIELLRLAALLHDIGKPGTPDAITEEESELekDHAIVGAEILRELLLEEVIKLI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117927754 323 EFLGEAAkgIRHHHERMDGLGYPDGLAGDAIPEFARIIAVADAFDSMTSTRSYRAARSVEAAITEL 388
cd00077       81 DELILAV--DASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRRDSREKRRRIAEEDLEEL 144

cl00076

140417

HDc

Metal dependent phosphohydrolases with conserved 'HD' motif

128747

smart00471

HDc

Metal dependent phosphohydrolases with conserved 'HD' motif.

false

124

2e-13

72.32

97.58

5,243,1,29,274,30,26,300,57,22,327,79,11,344,90,32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927754 244 DYYTRGHSERVARAAVMIGRRLGMREDRLemLRYAGMLHDVGKLGVPTRLLQKTGPL-DAAEFSAIKLHSVRGCEVIGDI 322
smart00471     2 DYHVFEHSLRVAQLAAALAEELGLLDIEL--LLLAALLHDIGKPGTPDSFLVKTSVLeDHHFIGAEILLEEEEPRILEEI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 117927754 323 eflgeAAKGIRHHHERmdglgyPDGLAGDAIPEFARIIAVADAFDSMTSTRSYR 376
smart00471    80 -----LATAILSHHER------PDGLRGEPITLEARIVKVADRLDALRRDRRYR 122

cl00076

140417

HDc

Metal dependent phosphohydrolases with conserved 'HD' motif

-1

110919

pfam01966

HD domain

false

108

1e-12

69.19

97.22

6,249,3,25,277,28,9,288,37,10,303,47,21,324,69,20,350,89,19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927754 250 HSERVARAAVMIGRRLGMREDRLEMlryAGMLHDVGKlgVPTRLLQKTGpldaaEFSAIKLHSVRGCEVIGDIEF-LGEA 328
pfam01966      4 HSLRVALLARELAEELGLDPELLLL---AALLHDIGK--DPFGFLEKLE-----DFGIFKSHSVVGAEILRELEKrLGVD 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 117927754 329 AKGIRHHHERMDGLGYpdglagDAIPEFARIIAVADAFDSM 369
pfam01966     74 LELILEHHESWEGAGY------EPISLEARIVKLADRLDAL 108

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

4e-54

207.30

50.29

2,239,141,91,330,233,81

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927754 240 VETKDYYTRGHSERVARAAVMIGRRLGMREDRLEMLRYAGMLHDVGKLGVPTRLLQKTGPLDAAEFSAIKLHSVRGCEVI 319
COG2206      142 IKAKDDYTYGHSVRVAELAEAIAKKLGLSEEKIEELALAGLLHDIGKIGIPDSILNKPGKLTEEEFEIIKKHPIYGYDIL 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927754 320 GDIEFLGEAAK-GIRHHHERMDGLGYPDGLAGDAIPEFARIIAVADAFDSMTSTRSYRAARSVEAAITELRRWSGTQFDP 398
COG2206      222 KDLPEFLESVRaVALRHHERWDGTGYPRGLKGEEIPLEARIIAVADVYDALTSDRPYKKAKSPEEALEELRKNSGGKFDP 301

                        170
                 ....*....|...
gi 117927754 399 VMVEALIAALQEE 411
COG2206      302 KVVDAFLKALSKY 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-45

178.95

53.33

2,219,158,113,332,272,78

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927754 220 QQYGAQHAAYEATVASLIQAVETKDYYTRGHSERVARAAVMIGRRLGMREDRLEMLRYAGMLHDVGKLGVPTRLLQKTGP 299
COG3437      159 EELAQIEDNLDETLEELAALLEVRDYETGDHLERVAQYSELLAELLGLSEEEVDLIKKAAPLHDIGKVAIPDSILLKPGK 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927754 300 LDAAEFSAIKLHSVRGCEVIGDIEFLGEAAKGI-RHHHERMDGLGYPDGLAGDAIPEFARIIAVADAFDSMTSTRSYRAA 378
COG3437      239 LTSEEFEIMKGHPILGAEILKSSERLMQVAAEIaRHHHERWDGSGYPDGLKGDEIPLSARIVAIADVFDALVSGRPYKEA 318

                        170       180       190
                 ....*....|....*....|....*....|..
gi 117927754 379 RSVEAAITELRRWSGTQFDPVMVEALIAALQE 410
COG3437      319 MSTEEALEIIRAQSGRLFDPKLVEAFIQVEDE 350

-1

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