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Conserved domains on  [gi|88195535|ref|YP_500341|]
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hypothetical protein SAOUHSC_01835 [Staphylococcus aureus subsp. aureus NCTC 8325]

Protein Classification

HAD family hydrolase( domain architecture ID 11425524)

HAD (haloacid dehalogenase) family hydrolase, part of a family of hydrolase that includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates; similar to

CATH:  3.30.1240.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  16889794|7966317

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
147-374 5.03e-22

Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];


:

Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 93.07  E-value: 5.03e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535 147 IYAALEEFATTELhvSDATLFSLKGalWTLAQEVYQewYLGSKLYEDVEKkiARTTFKTgyIYQEIIL---RPVDEVKVL 223
Cdd:COG0546  23 LNEALAELGLPPL--DLEELRALIG--LGLRELLRR--LLGEDPDEELEE--LLARFRE--LYEEELLdetRLFPGVREL 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535 224 LNDLKGAGFELGIATGRPYTETVVPFENLGLLPYFeaDFIATASDVleaenmyPQARPlgKPNPFSYIAALYGnnrdkye 303
Cdd:COG0546  93 LEALKARGIKLAVVTNKPREFAERLLEALGLDDYF--DAIVGGDDV-------PPAKP--KPEPLLEALERLG------- 154

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88195535 304 syinkqdniVNKDDVFIVGDSLADLLSAQKIGATFIGTLTGLKGKDaagELEAHHADYVINHLGELRGVLD 374
Cdd:COG0546 155 ---------LDPEEVLMVGDSPHDIEAARAAGVPFIGVTWGYGSAE---ELEAAGADYVIDSLAELLALLA 213
 
Name Accession Description Interval E-value
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
147-374 5.03e-22

Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 93.07  E-value: 5.03e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535 147 IYAALEEFATTELhvSDATLFSLKGalWTLAQEVYQewYLGSKLYEDVEKkiARTTFKTgyIYQEIIL---RPVDEVKVL 223
Cdd:COG0546  23 LNEALAELGLPPL--DLEELRALIG--LGLRELLRR--LLGEDPDEELEE--LLARFRE--LYEEELLdetRLFPGVREL 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535 224 LNDLKGAGFELGIATGRPYTETVVPFENLGLLPYFeaDFIATASDVleaenmyPQARPlgKPNPFSYIAALYGnnrdkye 303
Cdd:COG0546  93 LEALKARGIKLAVVTNKPREFAERLLEALGLDDYF--DAIVGGDDV-------PPAKP--KPEPLLEALERLG------- 154

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88195535 304 syinkqdniVNKDDVFIVGDSLADLLSAQKIGATFIGTLTGLKGKDaagELEAHHADYVINHLGELRGVLD 374
Cdd:COG0546 155 ---------LDPEEVLMVGDSPHDIEAARAAGVPFIGVTWGYGSAE---ELEAAGADYVIDSLAELLALLA 213
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
184-340 2.00e-12

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 64.91  E-value: 2.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535   184 WYLGSKlyEDVEKKIARTTFKTGYIYQEIILRPVDEVKVLLNDLKGAGFELGIATGRPYTETVVPFENLGLLPYFeaDFI 263
Cdd:pfam13419  50 RYLGVS--EDEEEKIEFYLRKYNEELHDKLVKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYF--DVI 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 88195535   264 ATASDVleaenmypqarPLGKPNPFSYIAALYGNNrdkyesyinkqdniVNKDDVFIVGDSLADLLSAQKIGATFIG 340
Cdd:pfam13419 126 VGGDDV-----------EGKKPDPDPILKALEQLG--------------LKPEEVIYVGDSPRDIEAAKNAGIKVIA 177
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 215-369 5.02e-09

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 55.75  E-value: 5.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535 215 RPVDEVKVLLNDLKGAGFELGIATGRpYTETVVPF-ENLGLLPYFeaDFIATASDVLEAenmypqarplgKPNPFSYIAA 293
Cdd:cd02616  80 KEYPGVYETLARLKSQGIKLGVVTTK-LRETALKGlKLLGLDKYF--DVIVGGDDVTHH-----------KPDPEPVLKA 145

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 88195535 294 LygnnrdkyesyinkQDNIVNKDDVFIVGDSLADLLSAQKIGATFIGTLTGLKGKDaagELEAHHADYVINHLGEL 369
Cdd:cd02616 146 L--------------ELLGAEPEEALMVGDSPHDILAGKNAGVKTVGVTWGYKGRE---YLKAFNPDFIIDKMSDL 204
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 203-335 6.14e-06

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions.The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)(D/E), (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 45.85  E-value: 6.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535   203 FKTGYIYQEIILRPVDEVkvlLNDLKGAGFELGIATGRPYTETVVPFENLGLLPYFeaDFIATASDvleaenmypqarPL 282
Cdd:TIGR01549  64 FWSEYDAEEAYIRGAADL---LARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYF--ELILVSDE------------PG 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 88195535   283 GKPNPFSYIAALygnnrdkyesyinkqDNIVNKDDVFIVGDSLADLLSAQKIG 335
Cdd:TIGR01549 127 SKPEPEIFLAAL---------------ESLGVPPEVLHVGDNLNDIEGARNAG 164
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 215-374 2.01e-03

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 39.24  E-value: 2.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535  215 RPVDEVKVLLNDLKGAGFELGIATGRPYTETVVPFENLGLLPYFeaDFIATASDVLEAenmypqarplgKPNPFSYIAAL 294
Cdd:PRK13288  82 TEYETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFF--DVVITLDDVEHA-----------KPDPEPVLKAL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535  295 ygnnrdkyesyiNKQDniVNKDDVFIVGDSLADLLSAQKIGATFIGTLTGLKGKDaagELEAHHADYVINHLGELRGVLD 374
Cdd:PRK13288 149 ------------ELLG--AKPEEALMVGDNHHDILAGKNAGTKTAGVAWTIKGRE---YLEQYKPDFMLDKMSDLLAIVG 211
 
Name Accession Description Interval E-value
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
147-374 5.03e-22

Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 93.07  E-value: 5.03e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535 147 IYAALEEFATTELhvSDATLFSLKGalWTLAQEVYQewYLGSKLYEDVEKkiARTTFKTgyIYQEIIL---RPVDEVKVL 223
Cdd:COG0546  23 LNEALAELGLPPL--DLEELRALIG--LGLRELLRR--LLGEDPDEELEE--LLARFRE--LYEEELLdetRLFPGVREL 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535 224 LNDLKGAGFELGIATGRPYTETVVPFENLGLLPYFeaDFIATASDVleaenmyPQARPlgKPNPFSYIAALYGnnrdkye 303
Cdd:COG0546  93 LEALKARGIKLAVVTNKPREFAERLLEALGLDDYF--DAIVGGDDV-------PPAKP--KPEPLLEALERLG------- 154

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88195535 304 syinkqdniVNKDDVFIVGDSLADLLSAQKIGATFIGTLTGLKGKDaagELEAHHADYVINHLGELRGVLD 374
Cdd:COG0546 155 ---------LDPEEVLMVGDSPHDIEAARAAGVPFIGVTWGYGSAE---ELEAAGADYVIDSLAELLALLA 213
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
208-369 3.80e-13

Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 67.93  E-value: 3.80e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535 208 IYQEII----LRPVDEVKVLLNDLKGAGFELGIATG--RPYTETVvpFENLGLLPYFeaDFIATASDVleaenmypqarP 281
Cdd:COG0637  75 LYRELLaeegLPLIPGVVELLEALKEAGIKIAVATSspRENAEAV--LEAAGLLDYF--DVIVTGDDV-----------A 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535 282 LGKPNPFSYIAAL--YGnnrdkyesyinkqdniVNKDDVFIVGDSLADLLSAQKIGATFIGTLTGlkgkdAAGELEAHHA 359
Cdd:COG0637 140 RGKPDPDIYLLAAerLG----------------VDPEECVVFEDSPAGIRAAKAAGMRVVGVPDG-----GTAEEELAGA 198

                       170
                ....*....|
gi 88195535 360 DYVINHLGEL 369
Cdd:COG0637 199 DLVVDDLAEL 208
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
184-340 2.00e-12

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 64.91  E-value: 2.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535   184 WYLGSKlyEDVEKKIARTTFKTGYIYQEIILRPVDEVKVLLNDLKGAGFELGIATGRPYTETVVPFENLGLLPYFeaDFI 263
Cdd:pfam13419  50 RYLGVS--EDEEEKIEFYLRKYNEELHDKLVKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYF--DVI 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 88195535   264 ATASDVleaenmypqarPLGKPNPFSYIAALYGNNrdkyesyinkqdniVNKDDVFIVGDSLADLLSAQKIGATFIG 340
Cdd:pfam13419 126 VGGDDV-----------EGKKPDPDPILKALEQLG--------------LKPEEVIYVGDSPRDIEAAKNAGIKVIA 177
Hydrolase_like pfam13242
HAD-hyrolase-like;
282-369 4.62e-12

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 61.09  E-value: 4.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535   282 LGKPNPFSYIAALYGNNrdkyesyinkqdniVNKDDVFIVGDSLA-DLLSAQKIGATFIGTLTGlKGKDAAGELEAHHAD 360
Cdd:pfam13242   2 CGKPNPGMLERALARLG--------------LDPERTVMIGDRLDtDILGAREAGARTILVLTG-VTRPADLEKAPIRPD 66


                  ....*....
gi 88195535   361 YVINHLGEL 369
Cdd:pfam13242  67 YVVDDLAEA 75
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 215-369 5.02e-09

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 55.75  E-value: 5.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535 215 RPVDEVKVLLNDLKGAGFELGIATGRpYTETVVPF-ENLGLLPYFeaDFIATASDVLEAenmypqarplgKPNPFSYIAA 293
Cdd:cd02616  80 KEYPGVYETLARLKSQGIKLGVVTTK-LRETALKGlKLLGLDKYF--DVIVGGDDVTHH-----------KPDPEPVLKA 145

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 88195535 294 LygnnrdkyesyinkQDNIVNKDDVFIVGDSLADLLSAQKIGATFIGTLTGLKGKDaagELEAHHADYVINHLGEL 369
Cdd:cd02616 146 L--------------ELLGAEPEEALMVGDSPHDILAGKNAGVKTVGVTWGYKGRE---YLKAFNPDFIIDKMSDL 204
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 220-340 5.80e-08

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 50.47  E-value: 5.80e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535 220 VKVLLNDLKGAGFELGIATGRPYTETVVPFENLGLLPYFeaDFIATASDVleaenmyPQARPLGKPNPFSYIAALygnnr 299
Cdd:cd01427  12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLF--DGIIGSDGG-------GTPKPKPKPLLLLLLKLG----- 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 88195535 300 dkyesyinkqdniVNKDDVFIVGDSLADLLSAQKIGATFIG 340
Cdd:cd01427  78 -------------VDPEEVLFVGDSENDIEAARAAGGRTVA 105
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 175-294 8.59e-08

uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized Bacillus subtilis YhcW; This subfamily includes the uncharacterized Bacillus subtilis YhcW. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319859 [Multi-domain]  Cd Length: 169  Bit Score: 51.49  E-value: 8.59e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535 175 TLAQEVYQEWyLGSKLYEDVEKKIARTTfktgyiyqeiILRPVDEVKVLLNDLKGAGFELGIATGRPYTETVVPFENLGL 254
Cdd:cd16423  15 PLWYEAWQEL-LNERRNELIKRQFSEKT----------DLPPIEGVKELLEFLKEKGIKLAVASSSPRRWIEPHLERLGL 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 88195535 255 LPYFEAdfIATASDVleaenmypqarPLGKPNPFSYIAAL 294
Cdd:cd16423  84 LDYFEV--IVTGDDV-----------EKSKPDPDLYLEAA 110
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 213-373 9.19e-08

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 52.34  E-value: 9.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535 213 ILRPVDEVKVLLNDLKGAGFELGIAT--GRPYTETVVpfENLGLLPYFEADFIAtasdvlEAENMYpqarplgKPNP--F 288
Cdd:COG1011  91 LVEPYPDALELLEALKARGYRLALLTngSAELQEAKL--RRLGLDDLFDAVVSS------EEVGVR-------KPDPeiF 155

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535 289 SYIAALYGnnrdkyesyinkqdniVNKDDVFIVGDSL-ADLLSAQKIGATFIgtltgLKGKDAAGELEAHHADYVINHLG 367
Cdd:COG1011 156 ELALERLG----------------VPPEEALFVGDSPeTDVAGARAAGMRTV-----WVNRSGEPAPAEPRPDYVISDLA 214


                ....*.
gi 88195535 368 ELRGVL 373
Cdd:COG1011 215 ELLELL 220
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 215-374 1.41e-06

haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter sphaeroides CbbZ; Phosphoglycolate phosphatase catalyzes the dephosphorylation of phosphoglycolate; its activity requires divalent cations, especially Mg++. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319815 [Multi-domain]  Cd Length: 214  Bit Score: 48.47  E-value: 1.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535 215 RPVDEVKVLLNDLKGAGFELGIATGRPYTETVVPFENLGLLPYFEAdfiATASDVLeaenmypqarPLGKPNPFSYIAAL 294
Cdd:cd07512  86 RPYPGVIEALERLRAAGWRLAICTNKPEAPARALLSALGLADLFAA---VVGGDTL----------PQRKPDPAPLRAAI 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535 295 YGNNRDkyesyinkqdnivnKDDVFIVGDSLADLLSAQKIGATFIGTLTGLKGKDAAgELEahhADYVINHLGELRGVLD 374
Cdd:cd07512 153 RRLGGD--------------VSRALMVGDSETDAATARAAGVPFVLVTFGYRHAPVA-ELP---HDAVFSDFDALPDLLA 214
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 223-373 2.11e-06

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; 5'-nucleotidases dephosphorylate nucleoside 5'-monophosphates to nucleosides and inorganic phosphate. Purified Pseudomonas aeruginosa PA0065 displayed high activity toward 5'-UMP and 5'-IMP, significant activity against 5'-XMP and 5'-TMP, and low activity against 5'-CMP. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319798 [Multi-domain]  Cd Length: 209  Bit Score: 47.97  E-value: 2.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535 223 LLNDLKGAGFELGIATGRP--YTETVVpfENLGLLPYFEAdfiatasdvleaenmypqarplgkpnpfsyiaaLYGNNRD 300
Cdd:cd04302  89 LLEKLKAAGYRLYVATSKPevFARRIL--EHFGLDEYFDG---------------------------------IAGASLD 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535 301 kyESYINKQDNI--------VNKDDVFIVGDSLADLLSAQKIGATFIGTLTGLKGKDaagELEAHHADYVINHLGELRGV 372
Cdd:cd04302 134 --GSRVHKADVIryaldtlgIAPEQAVMIGDRKHDIIGARANGIDSIGVLYGYGSED---ELEEAGATYIVETPAELLEL 208


                .
gi 88195535 373 L 373
Cdd:cd04302 209 L 209
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 203-335 6.14e-06

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions.The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)(D/E), (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 45.85  E-value: 6.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535   203 FKTGYIYQEIILRPVDEVkvlLNDLKGAGFELGIATGRPYTETVVPFENLGLLPYFeaDFIATASDvleaenmypqarPL 282
Cdd:TIGR01549  64 FWSEYDAEEAYIRGAADL---LARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYF--ELILVSDE------------PG 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 88195535   283 GKPNPFSYIAALygnnrdkyesyinkqDNIVNKDDVFIVGDSLADLLSAQKIG 335
Cdd:TIGR01549 127 SKPEPEIFLAAL---------------ESLGVPPEVLHVGDNLNDIEGARNAG 164
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 214-335 6.31e-06

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 46.43  E-value: 6.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535   214 LRPVDEVKVLLNDLKGAGFELGIATGRPYTETVVPFENLGLLPYFeaDFIATASDVleaenmypqarPLGKPNPFSYIAA 293
Cdd:pfam00702  97 LKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYF--DVVISGDDV-----------GVGKPKPEIYLAA 163

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 88195535   294 LygnnrDKYEsyinkqdniVNKDDVFIVGDSLADLLSAQKIG 335
Cdd:pfam00702 164 L-----ERLG---------VKPEEVLMVGDGVNDIPAAKAAG 191
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 145-369 3.49e-04

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to Parvibaculum lavamentivorans HAD-superfamily hydrolase, subfamily IA, variant 1; This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319835 [Multi-domain]  Cd Length: 207  Bit Score: 41.23  E-value: 3.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535 145 NNIYAALEE-FATTELHVSDATL------FSLKGALWTLAQEVYQEWYLGSKLYedveKKIARTTfktgYIYQEIILRPV 217
Cdd:cd07533  15 HNIVAAMTAaFADLGLPVPSAAEvrsiigLSLDEAIARLLPMATPALVAVAERY----KEAFDIL----RLLPEHAEPLF 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535 218 DEVKVLLNDLKGAGFELGIATGRPYTETVVPFENLGLLPYFEAdfIATASDvleaenmYPqarplGKPNPFSYIAALygn 297
Cdd:cd07533  87 PGVREALDALAAQGVLLAVATGKSRRGLDRVLEQHGLGGYFDA--TRTADD-------TP-----SKPHPEMLREIL--- 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 88195535 298 nrdkyesyinkQDNIVNKDDVFIVGDSLADLLSAQKIGATFIGTLTGLKGKDaagELEAHHADYVINHLGEL 369
Cdd:cd07533 150 -----------AELGVDPSRAVMVGDTAYDMQMAANAGAHAVGVAWGYHSLE---DLRSAGADAVVDHFSEL 207
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 207-340 7.91e-04

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 40.10  E-value: 7.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535   207 YIYQEIILRPVDEVKVLLNDLKGAGFELGIATGRPYTETVVpFENLGLLPYFeaDFIATASDVleaenmypqarPLGKPN 286
Cdd:TIGR01509  72 QIEEEAKLKPLPGVRALLEALRARGKKLALLTNSPRAHKLV-LALLGLRDLF--DVVIDSSDV-----------GLGKPD 137

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 88195535   287 PFSYIAAL--YGNNRDKYesyinkqdnivnkddVFIvGDSLADLLSAQKIGATFIG 340
Cdd:TIGR01509 138 PDIYLQALkaLGLEPSEC---------------VFV-DDSPAGIEAAKAAGMHTVG 177
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 215-374 2.01e-03

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 39.24  E-value: 2.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535  215 RPVDEVKVLLNDLKGAGFELGIATGRPYTETVVPFENLGLLPYFeaDFIATASDVLEAenmypqarplgKPNPFSYIAAL 294
Cdd:PRK13288  82 TEYETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFF--DVVITLDDVEHA-----------KPDPEPVLKAL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535  295 ygnnrdkyesyiNKQDniVNKDDVFIVGDSLADLLSAQKIGATFIGTLTGLKGKDaagELEAHHADYVINHLGELRGVLD 374
Cdd:PRK13288 149 ------------ELLG--AKPEEALMVGDNHHDILAGKNAGTKTAGVAWTIKGRE---YLEQYKPDFMLDKMSDLLAIVG 211
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 217-335 2.11e-03

human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases; N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 37.52  E-value: 2.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535 217 VDEVKVLLNDLKgAGFELGIATGRPYTETVVPFENLGLLPYFEADFIAtasdvleaenmypQARPLGKPNP--FSYIAAL 294
Cdd:cd04305  11 LPGAKELLEELK-KGYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVIS-------------EEVGVQKPNPeiFDYALNQ 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 88195535 295 YGnnrdkyesyinkqdniVNKDDVFIVGDSL-ADLLSAQKIG 335
Cdd:cd04305  77 LG----------------VKPEETLMVGDSLeSDILGAKNAG 102
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
316-369 4.08e-03

D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;


Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 37.88  E-value: 4.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 88195535  316 DDVFIVGDSLADLLSAQKIGATFIGTLTGlKGKDAAGELEAHHaDYVINHLGEL 369
Cdd:PRK08942 121 AGSPMVGDSLRDLQAAAAAGVTPVLVRTG-KGVTTLAEGAAPG-TWVLDSLADL 172
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 215-335 4.23e-03

Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGP; EC 3.1.3.18) catalyzes the conversion of 2-phosphoglycolate into glycolate and phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319854 [Multi-domain]  Cd Length: 212  Bit Score: 37.98  E-value: 4.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88195535 215 RPVDEVKVLLNDLKGAGFELGIATGRPYTETVVPFENLGLLPYFeadfiataSDVLEAENMypqarPLGKPNPfsyiAAL 294
Cdd:cd16417  87 HLYPGVKEGLAALKAQGYPLACVTNKPERFVAPLLEALGISDYF--------SLVLGGDSL-----PEKKPDP----APL 149

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 88195535 295 YgnnrdkyesYINKQDNIVNKDDVFiVGDSLADLLSAQKIG 335
Cdd:cd16417 150 L---------HACEKLGIAPAQMLM-VGDSRNDILAARAAG 180
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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