NCBI Conserved Domain Search

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Conserved domains on [gi\|94968207\|ref\|YP_590255.1\|]
metal dependent phosphohydrolase [Candidatus Koribacter versatilis Ellin345]

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

6e-17

84.36

87.59

3,362,2,45,414,47,29,443,83,46

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968207 363 TAGHSERVTVLATSIGRRMGLSPEELNIMHMGGLLHDIGKIGTPPdvldkpgKLTPDEMLTMMSHVQIGVRILEPIAGFR 442
cd00077       3 RFEHSLRVAQLARRLAEELGLSEEDIELLRLAALLHDIGKPGTPD-------AITEEESELEKDHAIVGAEILRELLLEE 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 94968207 443 K-------ALSIVSQHHEWYDGTGYPNKLKGEEISLHARIFAVADCFDALTSDR 489
cd00077      76 ViklidelILAVDASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRRDS 129

cl00076

140417

HDc

Metal dependent phosphohydrolases with conserved 'HD' motif

100122

cd06225

HAMP

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.

Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain...

true

false

true

7e-07

50.71

95.83

1,289,1,46

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 94968207 290 LGPLERLEEATKQIAGRDFKISLDVHSGDEFENLADSFNEMARQLE 335
cd06225       2 LRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLR 47

cl01054

141075

HAMP

Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain...

110919

pfam01966

HD domain

false

108

8e-14

73.81

100.00

5,362,0,26,391,26,17,415,43,28,443,72,17,466,89,19

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968207 363 TAGHSERVTVLATSIGRRMGLSPEELnimHMGGLLHDIGKIGTPPDvldkpgkLTPDEMLTMMSHVQIGVRILEPIAGFR 442
pfam01966     1 VLEHSLRVALLARELAEELGLDPELL---LLAALLHDIGKDPFGFL-------EKLEDFGIFKSHSVVGAEILRELEKRL 70

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 94968207 443 K-ALSIVSQHHEWYDGTGYpnklkgEEISLHARIFAVADCFDAL 485
pfam01966    71 GvDLELILEHHESWEGAGY------EPISLEARIVKLADRLDAL 108

cl00076

140417

HDc

Metal dependent phosphohydrolases with conserved 'HD' motif

-1

128747

smart00471

HDc

Metal dependent phosphohydrolases with conserved 'HD' motif.

false

124

8e-13

70.40

95.97

5,362,4,21,385,25,30,423,55,24,447,83,6,459,89,34

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968207 363 TAGHSERVTVLATSIGRRMGLspEELNIMHMGGLLHDIGKIGTPPDVLDKPGKltpdemltMMSHVQIGVRILEPIAGFR 442
smart00471    5 VFEHSLRVAQLAAALAEELGL--LDIELLLLAALLHDIGKPGTPDSFLVKTSV--------LEDHHFIGAEILLEEEEPR 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 94968207 443 KALSI----VSQHHEwydgtgYPNKLKGEEISLHARIFAVADCFDALTSDRPYRK 493
smart00471   75 ILEEIlataILSHHE------RPDGLRGEPITLEARIVKVADRLDALRRDRRYRR 123

cl00076

140417

HDc

Metal dependent phosphohydrolases with conserved 'HD' motif

-1

128599

smart00304

HAMP

HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain

false

9e-08

53.80

98.11

1,286,0,52

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 94968207 287 RRTLGPLERLEEATKQIAGRDFKISLDVHSGDEFENLADSFNEMARQLEMQF 338
smart00304    1 RRILRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETI 52

cl01054

141075

HAMP

Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain...

-1

109717

pfam00672

HAMP

HAMP domain

false

9e-08

53.77

71.43

1,285,19,50

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 94968207 286 IRRTLGPLERLEEATKQIAGRDFKISLDVHSGDEFENLADSFNEMARQLE 335
pfam00672    20 ARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLR 69

cl01054

141075

HAMP

Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain...

-1

117241

pfam08668

HDOD

HDOD domain

false

196

0.002

39.14

23.47

4,353,87,10,365,97,19,384,117,4,391,121,12

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 94968207 354 RAIDAKSDWTagHSERVTVLATSIGRRMGLS-PEELnimHMGGLLHDIGKI 403
pfam08668    88 LGFDLKGFWR--HSLACALAARLLARRLGLDdPEEA---FTAGLLHDIGKL 133

cl00076

140417

HDc

Metal dependent phosphohydrolases with conserved 'HD' motif

-1

129378

TIGR00277

HDIG

uncharacterized domain HDIG

false

0.003

38.85

90.00

5,365,7,21,389,28,17,419,45,19,439,64,7,446,72,7

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968207 366 HSERVTVLATSIGRRMGLSPEelnIMHMGGLLHDIGKIGTPpdvldkpgkltpdEMLTMMSHVQIGVRILEPIaGFRKAL 445
TIGR00277     8 HSLEVAKLAEALARELGLDVE---LARRGALLHDIGKPITR-------------EGVIFESHAVVGAEIARKY-GEPLEV 70


                ....*....
gi 94968207 446 S-IVSQHHE 453
TIGR00277    71 IdIIAEHHG 79

cl00076

140417

HDc

Metal dependent phosphohydrolases with conserved 'HD' motif

-1

32631

COG2770

ResE

FOG: HAMP domain [Signal transduction mechanisms]

false

0.003

38.85

67.47

2,286,27,48,337,75,8

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 94968207 287 RRTLGPLERLEEATKQIAGRDFKISLDVHSGDEFENLADSFNEMARQLemqFKAMEELH 345
COG2770      28 RRVTRPLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSL---QRALSALE 83

cl01054

141075

HAMP

Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain...

-1

32388

COG2206

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

false

true

false

344

1e-55

213.07

59.88

3,322,107,33,355,141,86,441,228,85

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968207 323 LADSFNEMARQLEMQFKAMEELHWGTLTALARA-IDAKSDWTAGHSERVTVLATSIGRRMGLSPEELNIMHMGGLLHDIG 401
COG2206     108 LIAKLDATLAVRIELSKVAREIVKKALVALARGdIKAKDDYTYGHSVRVAELAEAIAKKLGLSEEKIEELALAGLLHDIG 187

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968207 402 KIGTPPDVLDKPGKLTPDEMLTMMSHVQIGVRILEPIAGF-RKALSIVSQHHEWYDGTGYPNKLKGEEISLHARIFAVAD 480
COG2206     188 KIGIPDSILNKPGKLTEEEFEIIKKHPIYGYDILKDLPEFlESVRAVALRHHERWDGTGYPRGLKGEEIPLEARIIAVAD 267

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 94968207 481 CFDALTSDRPYRKGLPTVQTLAIMKSQSGTHFDPAVLIVFLEMMAE 526
COG2206     268 VYDALTSDRPYKKAKSPEEALEELRKNSGGKFDPKVVDAFLKALSK 313

-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-47

185.89

56.94

3,321,145,14,336,159,107,443,267,83

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968207 322 NLADSFNEMARQLEmQFKAMEELHWGTLTALARAIDAKSDWTAGHSERVTVLATSIGRRMGLSPEELNIMHMGGLLHDIG 401
COG3437     146 NLYLELQELRRRTE-ELAQIEDNLDETLEELAALLEVRDYETGDHLERVAQYSELLAELLGLSEEEVDLIKKAAPLHDIG 224

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968207 402 KIGTPPDVLDKPGKLTPDEMLTMMSHVQIGVRILEPIAGFRK-ALSIVSQHHEWYDGTGYPNKLKGEEISLHARIFAVAD 480
COG3437     225 KVAIPDSILLKPGKLTSEEFEIMKGHPILGAEILKSSERLMQvAAEIARHHHERWDGSGYPDGLKGDEIPLSARIVAIAD 304

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 94968207 481 CFDALTSDRPYRKGLPTVQTLAIMKSQSGTHFDPAVLIVFLEMMAE 526
COG3437     305 VFDALVSGRPYKEAMSTEEALEIIRAQSGRLFDPKLVEAFIQVEDE 350

-1

138290

PRK10935

nitrate/nitrite sensor protein NarQ; Provisional

false

true

false

568

8e-06

47.18

10.04

1,286,173,57

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 94968207 287 RRTLGPLERLEEATKQIAGRDFKISLDVHSGDEFENLADSFNEMARQLEMQFKAMEE 343
PRK10935    174 RQVVAPLNQLVTASQQIQKGQFDIPLDTTLPNELGLLAKAFNQMASELHKLYRSLES 230

-1

34605

COG5000

NtrY

Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms]

Signal transduction histidine kinase involved in nitrogen fixation and metabolism...

false

true

false

712

6e-05

44.56

8.15

2,286,302,35,321,338,22

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 94968207 287 RRTLGPLERLEEATKQIAGRDFKISLDVHSGDEFE-NLADSFNEMARQLEMQFKAMEE 343
COG5000     303 RRIVRPIRKLIEAADEVADGDLDVQVPVRRVDEDVgRLSKAFNKMTEQLSSQQEALER 360

-1

33640

COG3850

NarQ

Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms]

Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction...

false

true

false

574

1e-04

43.35

9.93

1,286,172,57

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 94968207 287 RRTLGPLERLEEATKQIAGRDFKISLDVHSGDEFENLADSFNEMARQLEMQFKAMEE 343
COG3850     173 RRVVRPLNQLTSAAQRIGRRQFDQRPTDTGRNELGLLGRAFNQMSGELKKLYADLEQ 229

-1

137977

PRK10549

signal transduction histidine-protein kinase BaeS; Provisional

false

true

false

467

2e-04

42.79

10.49

1,286,186,49

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 94968207 287 RRTLGPLERLEEATKQIAGRDFKISLDVHSGDEFENLADSFNEMARQLE 335
PRK10549    187 RGLLAPVKRLVEGTHKLAAGDFTTRVTPTSEDELGKLAQDFNQLASTLE 235

-1

31182

COG0840

Tar

Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction mechanisms]

Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction...

false

true

false

408

0.001

39.97

23.28

2,285,80,51,336,134,41

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968207 286 IRRTLGPLERLEEATKQIAGRDFKISLDVHSGDEFENLADSFNEMARQLEM---QFKAMEELHWGTLTALARAIDAKSDW 362
COG0840      81 LRAILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQiidAVQDNAEALSGASEEIAASATELSAR 160

                        90
                ....*....|....*
gi 94968207 363 TAGHSERVTVLATSI 377
COG0840     161 ADQQAESLEEVASAI 175

-1

Zn2+ binding site	0	4	4	true	28958	cd00077	HDc
Mg2+ binding site	1	1	1	true	28958	cd00077	HDc
dimerization interface	0	18	19	true	100122	cd06225	HAMP