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Conserved domains on  [gi|515962626|ref|WP_017393209|]
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MULTISPECIES: Cof-type HAD-IIB family hydrolase [Acinetobacter]

Protein Classification

Cof-type HAD-IIB family hydrolase( domain architecture ID 11576316)

Cof-type haloacid dehalogenase (HAD)-IIB family hydrolase uses a nucleophilic aspartate in the phosphoryl transfer reaction and may function as a phosphatase; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

CATH:  3.30.1240.10
EC:  3.1.3.-|3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  16889794|15337123|33940035|37786806
SCOP:  3001890

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 4-263 2.73e-63

Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli YbiV can act as both a sugar phosphatase and as a phosphotransferase. 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, 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: 319820 [Multi-domain]  Cd Length: 184  Bit Score: 196.65  E-value: 2.73e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626   4 KILAVDMDGTFLNSKKQYNKARFLKQYEQLKQNNIHFVVASGNQLAKLVTYFPEINHEITFIAENGAHVVdagqelafah 83
Cdd:cd07518    1 KLIATDMDGTFLNDDKTYDHERFFAILDQLLKKGIKFVVASGRQYYQLISFFPEIKDEMSFVAENGAVVY---------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626  84 lskeqfskilkaidpaytstmvicgkqsayvhrsmnaenyakvaryfekltviddfyalddlvCKITFTAQENESFAIFE 163
Cdd:cd07518   71 ---------------------------------------------------------------FKFTLNVPDEAAPDIID 87

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626 164 HFQKQSfvaDKVLVPVSSGFGFIDLILPDQHKAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAGYGFAVENAIEALK 243
Cdd:cd07518   88 ELNQKF---GGILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEVK 164

                        250       260
                 ....*....|....*....|
gi 515962626 244 AVAPYTTRSNEREGALEVID 263
Cdd:cd07518  165 AAAKYVAPSNNENGVLQVIE 184
 
Name Accession Description Interval E-value
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 4-263 2.73e-63

Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli YbiV can act as both a sugar phosphatase and as a phosphotransferase. 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, 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: 319820 [Multi-domain]  Cd Length: 184  Bit Score: 196.65  E-value: 2.73e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626   4 KILAVDMDGTFLNSKKQYNKARFLKQYEQLKQNNIHFVVASGNQLAKLVTYFPEINHEITFIAENGAHVVdagqelafah 83
Cdd:cd07518    1 KLIATDMDGTFLNDDKTYDHERFFAILDQLLKKGIKFVVASGRQYYQLISFFPEIKDEMSFVAENGAVVY---------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626  84 lskeqfskilkaidpaytstmvicgkqsayvhrsmnaenyakvaryfekltviddfyalddlvCKITFTAQENESFAIFE 163
Cdd:cd07518   71 ---------------------------------------------------------------FKFTLNVPDEAAPDIID 87

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626 164 HFQKQSfvaDKVLVPVSSGFGFIDLILPDQHKAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAGYGFAVENAIEALK 243
Cdd:cd07518   88 ELNQKF---GGILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEVK 164

                        250       260
                 ....*....|....*....|
gi 515962626 244 AVAPYTTRSNEREGALEVID 263
Cdd:cd07518  165 AAAKYVAPSNNENGVLQVIE 184
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-262 5.88e-54

haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes.


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 175.12  E-value: 5.88e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626    6 LAVDMDGTFLNSKKQYNKaRFLKQYEQLKQNNIHFVVASGNQLAKLVTYFPEINHEITFIAENGAHVVDAGQELAFAH-L 84
Cdd:pfam08282   1 IASDLDGTLLNSDKKISE-KTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDENGKILYSNpI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626   85 SKEQFSKILKAIDPAYTSTMvICGKQSAYVHRSMNAENYAKVARYFEK--LTVIDDFYALDDLVCKITFTAQENESFAIF 162
Cdd:pfam08282  80 SKEAVKEIIEYLKENNLEIL-LYTDDGVYILNDNELEKILKELNYTKSfvPEIDDFELLEDEDINKILILLDEEDLDELE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626  163 EHFQKQSFvadKVLVPVSSGFGFIDLILPDQHKAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAGYGFAVENAIEAL 242
Cdd:pfam08282 159 KELKELFG---SLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEV 235

                         250       260
                  ....*....|....*....|
gi 515962626  243 KAVAPYTTRSNEREGALEVI 262
Cdd:pfam08282 236 KAAADYVTDSNNEDGVAKAL 255
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-262 3.42e-52

Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272905 [Multi-domain]  Cd Length: 256  Bit Score: 170.91  E-value: 3.42e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626    5 ILAVDMDGTFLNSKKqYNKARFLKQYEQLKQNNIHFVVASGNQLAKLVTYFPEINHEITFIAENGAHVVDAGQELAFAH- 83
Cdd:TIGR00099   1 LIFIDLDGTLLNDDH-TISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGEILYKKp 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626   84 LSKEQFSKILKAIDPAYTStMVICGKQSAYVHRSMNAENYAKVARYFEKLTVIDDFYALDDLVCKITFTAQENESFAIFE 163
Cdd:TIGR00099  80 LDLDLVEEILNFLKKHGLD-VILYGDDSIYASKNDPEYFTIFKKFLGEPKLEVVDIQYLPDDILKILLLFLDPEDLDLLI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626  164 HFQKQSFVADKVLVpVSSGFGFIDLILPDQHKAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAGYGFAVENAIEALK 243
Cdd:TIGR00099 159 EALNKLELEENVSV-VSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEELK 237

                         250
                  ....*....|....*....
gi 515962626  244 AVAPYTTRSNEREGALEVI 262
Cdd:TIGR00099 238 ALADYVTDSNNEDGVALAL 256
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 2-263 3.38e-50

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 163.38  E-value: 3.38e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626   2 TVKILAVDMDGTFLNSKKQYNkARFLKQYEQLKQNNIHFVVASGNQLAKLVTYFPEINHEITFIAENGAHVVDAGQELAF 81
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGEIS-PRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGEVLY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626  82 ahlskeqfskilkaidpaytstmvicgkqsayvHRSMNAENYAKVARYFEKLTViddfyalddlvckitftaqenesfai 161
Cdd:COG0561   80 ---------------------------------ERPLDPEDVREILELLREHGL-------------------------- 100

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626 162 fehfqkqsfvadKVLVPVSSGFGFIDLILPDQHKAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAGYGFAVENAIEA 241
Cdd:COG0561  101 ------------HLQVVVRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPE 168

                        250       260
                 ....*....|....*....|..
gi 515962626 242 LKAVAPYTTRSNEREGALEVID 263
Cdd:COG0561  169 VKAAADYVTGSNDEDGVAEALE 190
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 1-263 3.44e-23

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 95.53  E-value: 3.44e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626   1 MTVKILAVDMDGTFLNSKKQYNKArfLKQ-YEQLKQNNIHFVVASGNQLAKLVTYFPEINHEIT---FIAENGAHVVDA- 75
Cdd:PRK10513   1 MAIKLIAIDMDGTLLLPDHTISPA--VKQaIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPgdyCITNNGALVQKAa 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626  76 -GQELAFAHLSK------EQFSKIL----KAIDPA--YTSTMVIcgkqSAY-VHRSM---------NAENYAKVARyFEK 132
Cdd:PRK10513  79 dGETVAQTALSYddylylEKLSREVgvhfHALDRNtlYTANRDI----SYYtVHESFltgiplvfrEVEKMDPNLQ-FPK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626 133 LTVIDDFYALDDLVCKITftAQENESFAIFEhfqkqsfvadkvlvpvSSGFgFIDLILPDQHKAHGLKLLLQKWQIEASQ 212
Cdd:PRK10513 154 VMMIDEPEILDAAIARIP--AEVKERYTVLK----------------SAPY-FLEILDKRVNKGTGVKSLAEHLGIKPEE 214

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515962626 213 VVAIGDNNNDIQMIKAAGYGFAVENAIEALKAVAPYTTRSNEREGALEVID 263
Cdd:PRK10513 215 VMAIGDQENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIE 265
 
Name Accession Description Interval E-value
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 4-263 2.73e-63

Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli YbiV can act as both a sugar phosphatase and as a phosphotransferase. 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, 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: 319820 [Multi-domain]  Cd Length: 184  Bit Score: 196.65  E-value: 2.73e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626   4 KILAVDMDGTFLNSKKQYNKARFLKQYEQLKQNNIHFVVASGNQLAKLVTYFPEINHEITFIAENGAHVVdagqelafah 83
Cdd:cd07518    1 KLIATDMDGTFLNDDKTYDHERFFAILDQLLKKGIKFVVASGRQYYQLISFFPEIKDEMSFVAENGAVVY---------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626  84 lskeqfskilkaidpaytstmvicgkqsayvhrsmnaenyakvaryfekltviddfyalddlvCKITFTAQENESFAIFE 163
Cdd:cd07518   71 ---------------------------------------------------------------FKFTLNVPDEAAPDIID 87

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626 164 HFQKQSfvaDKVLVPVSSGFGFIDLILPDQHKAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAGYGFAVENAIEALK 243
Cdd:cd07518   88 ELNQKF---GGILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEVK 164

                        250       260
                 ....*....|....*....|
gi 515962626 244 AVAPYTTRSNEREGALEVID 263
Cdd:cd07518  165 AAAKYVAPSNNENGVLQVIE 184
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-262 5.88e-54

haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes.


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 175.12  E-value: 5.88e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626    6 LAVDMDGTFLNSKKQYNKaRFLKQYEQLKQNNIHFVVASGNQLAKLVTYFPEINHEITFIAENGAHVVDAGQELAFAH-L 84
Cdd:pfam08282   1 IASDLDGTLLNSDKKISE-KTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDENGKILYSNpI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626   85 SKEQFSKILKAIDPAYTSTMvICGKQSAYVHRSMNAENYAKVARYFEK--LTVIDDFYALDDLVCKITFTAQENESFAIF 162
Cdd:pfam08282  80 SKEAVKEIIEYLKENNLEIL-LYTDDGVYILNDNELEKILKELNYTKSfvPEIDDFELLEDEDINKILILLDEEDLDELE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626  163 EHFQKQSFvadKVLVPVSSGFGFIDLILPDQHKAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAGYGFAVENAIEAL 242
Cdd:pfam08282 159 KELKELFG---SLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEV 235

                         250       260
                  ....*....|....*....|
gi 515962626  243 KAVAPYTTRSNEREGALEVI 262
Cdd:pfam08282 236 KAAADYVTDSNNEDGVAKAL 255
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-262 3.42e-52

Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272905 [Multi-domain]  Cd Length: 256  Bit Score: 170.91  E-value: 3.42e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626    5 ILAVDMDGTFLNSKKqYNKARFLKQYEQLKQNNIHFVVASGNQLAKLVTYFPEINHEITFIAENGAHVVDAGQELAFAH- 83
Cdd:TIGR00099   1 LIFIDLDGTLLNDDH-TISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGEILYKKp 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626   84 LSKEQFSKILKAIDPAYTStMVICGKQSAYVHRSMNAENYAKVARYFEKLTVIDDFYALDDLVCKITFTAQENESFAIFE 163
Cdd:TIGR00099  80 LDLDLVEEILNFLKKHGLD-VILYGDDSIYASKNDPEYFTIFKKFLGEPKLEVVDIQYLPDDILKILLLFLDPEDLDLLI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626  164 HFQKQSFVADKVLVpVSSGFGFIDLILPDQHKAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAGYGFAVENAIEALK 243
Cdd:TIGR00099 159 EALNKLELEENVSV-VSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEELK 237

                         250
                  ....*....|....*....
gi 515962626  244 AVAPYTTRSNEREGALEVI 262
Cdd:TIGR00099 238 ALADYVTDSNNEDGVALAL 256
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 2-263 3.38e-50

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 163.38  E-value: 3.38e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626   2 TVKILAVDMDGTFLNSKKQYNkARFLKQYEQLKQNNIHFVVASGNQLAKLVTYFPEINHEITFIAENGAHVVDAGQELAF 81
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGEIS-PRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGEVLY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626  82 ahlskeqfskilkaidpaytstmvicgkqsayvHRSMNAENYAKVARYFEKLTViddfyalddlvckitftaqenesfai 161
Cdd:COG0561   80 ---------------------------------ERPLDPEDVREILELLREHGL-------------------------- 100

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626 162 fehfqkqsfvadKVLVPVSSGFGFIDLILPDQHKAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAGYGFAVENAIEA 241
Cdd:COG0561  101 ------------HLQVVVRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPE 168

                        250       260
                 ....*....|....*....|..
gi 515962626 242 LKAVAPYTTRSNEREGALEVID 263
Cdd:COG0561  169 VKAAADYVTGSNDEDGVAEALE 190
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 5-257 7.60e-37

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-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, 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: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 131.18  E-value: 7.60e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626   5 ILAVDMDGTFLNSKKQYNKARflKQY-EQLKQNNIHFVVASGNQLAKLVTYFPEINHEITFIAENGAHVVDAGQELAFAH 83
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRT--KEAiKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEILER 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626  84 LSKEQFSKILKAIDPAYTSTMVIcgkqsaYVHRSMNAENYA---KVARYFEKLTVIDDFYALDDLVCKITFTAQENEsfa 160
Cdd:cd07516   79 LISKEDVKELEEFLRKLGIGINI------YTNDDWADTIYEeneDDEIIKPAEILDDLLLPPDEDITKILFVGEDEE--- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626 161 IFEHFQKQSFVADKVLVPVSSGFGFIDLILPDQHKAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAGYGFAVENAIE 240
Cdd:cd07516  150 LDELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAID 229

                        250
                 ....*....|....*..
gi 515962626 241 ALKAVAPYTTRSNEREG 257
Cdd:cd07516  230 EVKEAADYVTLTNNEDG 246
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 1-263 3.44e-23

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 95.53  E-value: 3.44e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626   1 MTVKILAVDMDGTFLNSKKQYNKArfLKQ-YEQLKQNNIHFVVASGNQLAKLVTYFPEINHEIT---FIAENGAHVVDA- 75
Cdd:PRK10513   1 MAIKLIAIDMDGTLLLPDHTISPA--VKQaIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPgdyCITNNGALVQKAa 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626  76 -GQELAFAHLSK------EQFSKIL----KAIDPA--YTSTMVIcgkqSAY-VHRSM---------NAENYAKVARyFEK 132
Cdd:PRK10513  79 dGETVAQTALSYddylylEKLSREVgvhfHALDRNtlYTANRDI----SYYtVHESFltgiplvfrEVEKMDPNLQ-FPK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626 133 LTVIDDFYALDDLVCKITftAQENESFAIFEhfqkqsfvadkvlvpvSSGFgFIDLILPDQHKAHGLKLLLQKWQIEASQ 212
Cdd:PRK10513 154 VMMIDEPEILDAAIARIP--AEVKERYTVLK----------------SAPY-FLEILDKRVNKGTGVKSLAEHLGIKPEE 214

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515962626 213 VVAIGDNNNDIQMIKAAGYGFAVENAIEALKAVAPYTTRSNEREGALEVID 263
Cdd:PRK10513 215 VMAIGDQENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIE 265
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 4-257 3.18e-20

phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily; Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. 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, 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: 319819 [Multi-domain]  Cd Length: 213  Bit Score: 86.12  E-value: 3.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626   4 KILAVDMDGTFLNSKKQYNKARfLKQYEQLKQNNIHFVVASGNQLAklvtyfpEINHEI------TFIAENGAHVVDAGQ 77
Cdd:cd07517    1 KIVFFDIDGTLLDEDTTIPEST-KEAIAALKEKGILVVIATGRAPF-------EIQPIVkalgidSYVSYNGQYVFFEGE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626  78 ELAFAHLSKEQFSKILKAIDpaytstmvicGKQSAYVhrsmnaenyakvaryfekltviddFYALddlvckITFTAQENE 157
Cdd:cd07517   73 VIYKNPLPQELVERLTEFAK----------EQGHPVS------------------------FYGQ------LLLFEDEEE 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626 158 SFAIFEHFQKQSFVADKvlvPVSSgfgfiDLILPDQHKAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAGYGFAVEN 237
Cdd:cd07517  113 EQKYEELRPELRFVRWH---PLST-----DVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGN 184

                        250       260
                 ....*....|....*....|
gi 515962626 238 AIEALKAVAPYTTRSNEREG 257
Cdd:cd07517  185 AHEELKEIADYVTKDVDEDG 204
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 1-263 1.19e-19

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 85.02  E-value: 1.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626   1 MTVKILAVDMDGTFLNSKKQYN-KArfLKQYEQLKQNNIHFVVASGNQL------AKLvtyfpeINHEITFIAENGAHVv 73
Cdd:PRK01158   1 MKIKAIAIDIDGTITDKDRRLSlKA--VEAIRKAEKLGIPVILATGNVLcfaraaAKL------IGTSGPVIAENGGVI- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626  74 dagqelafaHLSKEQFSKILKAIDpaytstmvicGKQSAYVHRSmnaeNYAKVAryFEKLTVIDDFYALDDLVCKITFTA 153
Cdd:PRK01158  72 ---------SVGFDGKRIFLGDIE----------ECEKAYSELK----KRFPEA--STSLTKLDPDYRKTEVALRRTVPV 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626 154 QENEsfAIFEHFqkqsfvaDKVLVPVSSGFGfIDLILPDQHKAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAGYGF 233
Cdd:PRK01158 127 EEVR--ELLEEL-------GLDLEIVDSGFA-IHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGV 196

                        250       260       270
                 ....*....|....*....|....*....|
gi 515962626 234 AVENAIEALKAVAPYTTRSNEREGALEVID 263
Cdd:PRK01158 197 AVANADEELKEAADYVTEKSYGEGVAEAIE 226
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 195-266 1.26e-17

phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), and Pyrococcus horikoshii PH1421, a magnesium-dependent phosphatase; belongs to the haloacid dehalogenase-like superfamily; Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PGPase) catalyzes the magnesium-dependent dephosphorylation of phosphoglycolate. This family also includes Pyrococcus horikoshii OT3 PH1421, a magnesium-dependent phosphatase. 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: 319816 [Multi-domain]  Cd Length: 139  Bit Score: 77.24  E-value: 1.26e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515962626 195 KAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAGYGFAVENAIEALKAVAPYTTRSNEREGALEVIDLVL 266
Cdd:cd07514   68 KGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVLEAIDKLL 139
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 6-268 6.48e-17

sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP equivalog model (TIGR01485), encompassing plants and cyanobacteria, as well as those archaeal sequences which are the closest relatives (TIGR01487). It remains to be shown whether these archaeal sequences catalyze the same reaction as SPP.


Pssm-ID: 273650 [Multi-domain]  Cd Length: 225  Bit Score: 77.50  E-value: 6.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626    6 LAVDMDGTFLNSKKQYNKA--RFLKQYEQLKqnnIHFVVASGN------QLAKLVTYfPEInheitFIAENGAHVV--DA 75
Cdd:TIGR01482   1 IASDIDGTLTDPNRAINESalEAIRKAESKG---IPVVLVTGNsvqfarALAKLIGT-PDP-----VIAENGGEISynEG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626   76 GQELAFAHLSKEQFSKILKAIdpaytstmvicgkqsayvhRSMNAENYAKVARyfEKLTVIDDFYALDDLVCKITftaqe 155
Cdd:TIGR01482  72 LDDIFLAYLEEEWFLDIVIAK-------------------TFPFSRLKVQYPR--RASLVKMRYGIDVDTVREII----- 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626  156 nESFAIfehfqkqsfvadkVLVPVSSGFGfIDLILPDQHKAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAGYGFAV 235
Cdd:TIGR01482 126 -KELGL-------------NLVAVDSGFD-IHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAV 190

                         250       260       270
                  ....*....|....*....|....*....|...
gi 515962626  236 ENAIEALKAVAPYTTRSNEREGALEVIDLVLQH 268
Cdd:TIGR01482 191 ANAQPELKEWADYVTESPYGEGGAEAIGEILQA 223
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 5-235 6.88e-15

HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273651 [Multi-domain]  Cd Length: 207  Bit Score: 71.64  E-value: 6.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626    5 ILAVDMDGTFLNSKKQYNKARFLKQYEQLKQNNIHFVVASGNQLAKLVTYFPEINHEITFIAENGAHVVDAGQELAFAHL 84
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAHELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLPLPLIAENGALIFYPGEILYIEPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626   85 SKEQFskilkaidpaytstmvicgkQSAYVHRSMNAENYAKVARYFEKltvIDDFYALDDLvckITFTAQENESFAIFEH 164
Cdd:TIGR01484  81 DVFEE--------------------ILGIKFEEIGAELKSLSEHYVGT---FIEDKAIAVA---IHYVGAELGQELDSKM 134

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515962626  165 FQKQSFV--ADKVLVPVSSGFGFIDLILPDQHKAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAGYGFAV 235
Cdd:TIGR01484 135 RERLEKIgrNDLELEAIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 1-262 3.91e-12

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 64.66  E-value: 3.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626   1 MTVKILAVDMDGTFLNSKKQYNKARfLKQYEQLKQNNIHFVVASGNQLAKLVTYFPEINHEITFIAENGAHVVD--AGQE 78
Cdd:PRK10530   1 MTYRVIALDLDGTLLTPKKTILPES-LEALARAREAGYKVIIVTGRHHVAIHPFYQALALDTPAICCNGTYLYDyqAKKV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626  79 LAFAHLSKEQFSKILKAIDPA------YTSTMVICGKQSAYVHRSMN-AENYAKVARyfEKLTVIDDFYALDDLVCKITF 151
Cdd:PRK10530  80 LEADPLPVQQALQVIEMLDEHqihglmYVDDAMLYEHPTGHVIRTLNwAQTLPPEQR--PTFTQVDSLAQAARQVNAIWK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626 152 TAQENESFAIFEHFQKQsfVADKV-LVPVSSGFGFIDLILPDQHKAHglklLLQKWqIEA-----SQVVAIGDNNNDIQM 225
Cdd:PRK10530 158 FALTHEDLPQLQHFAKH--VEHELgLECEWSWHDQVDIARKGNSKGK----RLTQW-VEAqgwsmKNVVAFGDNFNDISM 230

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 515962626 226 IKAAGYGFAVENAIEALKAVAPYTTRSNEREGALEVI 262
Cdd:PRK10530 231 LEAAGLGVAMGNADDAVKARADLVIGDNTTPSIAEFI 267
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 3-262 4.83e-12

phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be phosphoglycolate phosphatases, is most closely related to the sucrose-phosphate phosphatases from plants and cyanobacteria (TIGR01485). Together, these two models comprise a subfamily model (TIGR01482). TIGR01482, in turn, is a member of the IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases.


Pssm-ID: 273652 [Multi-domain]  Cd Length: 215  Bit Score: 63.61  E-value: 4.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626    3 VKILAVDMDGTfLNSKKQYNKARFLKQYEQLKQNNIHFVVASGNQ---LAKLVTYfpeINHEITFIAENGAHVVDAGQEL 79
Cdd:TIGR01487   1 IKLVAIDIDGT-LTDPNRMISERAIEAIRKAEKKGIPVSLVTGNTvpfARALAVL---IGTSGPVVAENGGVIFYNKEDI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626   80 AFAHLSKEQFSKILKAIdpaytstmvicgkqsayvhRSMNAEnyaKVARYFEKLTVIDDFYALDDLVCKItftaqenesf 159
Cdd:TIGR01487  77 FLANMEEEWFLDEEKKK-------------------RFPRDR---LSNEYPRASLVIMREGKDVDEVREI---------- 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626  160 aifehfqkqsfVADKVLVPVSSGFGfIDLILPDQHKAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAGYGFAVENAI 239
Cdd:TIGR01487 125 -----------IKERGLNLVASGFA-IHIMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAVANAD 192

                         250       260
                  ....*....|....*....|...
gi 515962626  240 EALKAVAPYTTRSNEREGALEVI 262
Cdd:TIGR01487 193 DQLKEIADYVTSNPYGEGVVEVL 215
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 148-257 5.83e-11

sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3.1.3.24) catalyzes the dephosphorylation of sucrose-6(F)-phosphate (Suc6P)-the final step in the pathway of sucrose biosynthesis in plants and cyanobacteria. 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: 319792 [Multi-domain]  Cd Length: 245  Bit Score: 61.21  E-value: 5.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626 148 KITFTAQENESFAIFEHFQKQSFVADKVLVPVSSGFGFIDL-ILP-DQHKAHGLKLLLQKWQIEASQVVAIGDNNNDIQM 225
Cdd:cd02605  121 KISFYLDPQNDAAVIEQLEEMLLKAGLTVRIIYSSGLAYDLdILPlGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIAL 200

                         90       100       110
                 ....*....|....*....|....*....|..
gi 515962626 226 IKAAGYGFAVENAIEALKAVAPYTTRSNEREG 257
Cdd:cd02605  201 LSTGTRGVIVGNAQPELLKWADRVTRSRLAKG 232
PLN02887 PLN02887
hydrolase family protein
 186-262 1.49e-10

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 61.04  E-value: 1.49e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515962626 186 IDLILPDQHKAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAGYGFAVENAIEALKAVAPYTTRSNEREGALEVI 262
Cdd:PLN02887 499 LEIVPPGTSKGNGVKMLLNHLGVSPDEIMAIGDGENDIEMLQLASLGVALSNGAEKTKAVADVIGVSNDEDGVADAI 575
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 184-263 5.51e-10

haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) phosphatase KdsC, and rainbow trout N-acylneuraminate cytidylyltransferase; KDO 8-P phosphatase catalyzes the hydrolysis of KDO 8-P to KDO (3-deoxy-D-manno-octulosonate) and inorganic phosphate and is the last enzyme in the KDO biosynthetic pathway. KDO is an 8-carbon sugar that links the lipid A and polysaccharide moieties of the lipopolysaccharide region in Gram-negative bacteria. An interruption in KDO biosynthesis leads to the accumulation of lipid A precursors and subsequent arrest in cell growth. The KDO biosynthesis pathway involves five sequential enzymatic reactions. This family also includes rainbow trout CMP-sialic acid synthetase which effectively converts both deaminoneuraminic acid (KDN, 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid) and N-acetylneuraminic acid (Neu5Ac) to CMP-KDN and CMP-Neu5Ac, respectively. 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: 319769 [Multi-domain]  Cd Length: 146  Bit Score: 56.38  E-value: 5.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626 184 GFIDLILPDQHKAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAGYGFAVENAIEALKAVAPYTTRSNEREGAL-EVI 262
Cdd:cd01630   66 GIEDLFQGVKDKLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGRGAVrEVC 145


                 .
gi 515962626 263 D 263
Cdd:cd01630  146 E 146
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 193-264 6.84e-10

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 57.54  E-value: 6.84e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515962626 193 QHKAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAGYGFAVeNAIEALKAVAPyttrsneREGALEVIDL 264
Cdd:COG0560  154 EGKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAV-NPDPALREAAD-------RERGWPVLDL 217
serB PRK11133
phosphoserine phosphatase; Provisional
 193-234 8.01e-09

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 55.34  E-value: 8.01e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 515962626 193 QHKAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAGYGFA 234
Cdd:PRK11133 247 QYKADTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAGLGIA 288
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 178-255 1.85e-08

Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate phosphohydrolase proteins found in plants and cyanobacteria. Sucrose-6(F)-phosphate phosphohydrolase catalyzes the final step in the pathway of sucrose biosynthesis.


Pssm-ID: 428314 [Multi-domain]  Cd Length: 246  Bit Score: 53.81  E-value: 1.85e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515962626  178 PVSSGFGFIDLILPDQHKAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAGYGFAVENAIEALKAVAPYTTRSNER 255
Cdd:pfam05116 148 VIYSSGRDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTRGVVVGNAQPELLQWYLENARDNPR 225
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 189-262 3.83e-07

phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction 3-phospho-serine + H2O = L-serine + phosphate. It catalyzes the last of three steps in the biosynthesis of serine from D-3-phosphoglycerate. Note that this enzyme acts on free phosphoserine, not on phosphoserine residues of phosphoproteins. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273022 [Multi-domain]  Cd Length: 219  Bit Score: 49.66  E-value: 3.83e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515962626  189 ILPDQHKAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAGYGFAVeNAIEALKAVAPYTTRSNEREGALEVI 262
Cdd:TIGR00338 147 IVDASYKGKTLLILLRKEGISPENTVAVGDGANDLSMIKAAGLGIAF-NAKPKLQQKADICINKKDLTDILPLL 219
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 189-234 6.82e-07

phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p; This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. 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: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 48.31  E-value: 6.82e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 515962626 189 ILPDQHKAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAGYGFA 234
Cdd:cd07500  132 IVDAQRKAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIA 177
PRK09484 PRK09484
3-deoxy-manno-octulosonate-8-phosphatase KdsC;
202-269 3.66e-06

3-deoxy-manno-octulosonate-8-phosphatase KdsC;


Pssm-ID: 181898 [Multi-domain]  Cd Length: 183  Bit Score: 46.46  E-value: 3.66e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515962626 202 LLQKWQIEASQVVAIGDNNNDIQMIKAAGYGFAVENAIEALKAVAPYTTRSNEREGAL-EVIDLVLQHQ 269
Cdd:PRK09484 104 LLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYVTRIAGGRGAVrEVCDLLLLAQ 172
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
183-246 4.03e-06

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 46.46  E-value: 4.03e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515962626 183 FGFI---DLILPDQHKAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAG-------YGFAVENAIEALKAVA 246
Cdd:COG0546  127 FDAIvggDDVPPAKPKPEPLLEALERLGLDPEEVLMVGDSPHDIEAARAAGvpfigvtWGYGSAEELEAAGADY 200
SPP_plant-cyano TIGR01485
sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate ...
 180-242 1.89e-05

sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate phosphohydrolase from plants and cyanobacteria (SPP). SPP is a member of the Class IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. SPP catalyzes the final step in the biosynthesis of sucrose, a critically important molecule for plants. Sucrose phosphate synthase (SPS), the prior step in the biosynthesis of sucrose, contains a domain which exhibits considerable similarity to SPP albeit without conservation of the catalytic residues. The catalytic machinery of the synthase resides in another domain. It seems likely that the phosphatase-like domain is involved in substrate binding, possibly binding both substrates in a "product-like" orientation prior to ligation by the synthase catalytic domain.


Pssm-ID: 130549  Cd Length: 249  Bit Score: 44.80  E-value: 1.89e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515962626  180 SSGFGFiDLILPDQHKAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAG-YGFAVENAIEAL 242
Cdd:TIGR01485 154 SSGKDL-DILPQGSGKGQALQYLLQKLAMEPSQTLVCGDSGNDIELFEIGSvRGVIVSNAQEEL 216
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 195-235 2.73e-05

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: 42.38  E-value: 2.73e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 515962626 195 KAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAG-YGFAV 235
Cdd:cd01427   65 KPKPLLLLLLKLGVDPEEVLFVGDSENDIEAARAAGgRTVAV 106
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 190-246 1.08e-04

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: 42.22  E-value: 1.08e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515962626 190 LPDQhKAHGLKLL--LQKWQIEASQVVAIGDNNNDIQMIKAAG-------YGFAVENAIEALKAVA 246
Cdd:cd16417  139 LPEK-KPDPAPLLhaCEKLGIAPAQMLMVGDSRNDILAARAAGcpsvgltYGYNYGEDIAASGPDA 203
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 195-230 1.84e-04

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: 41.42  E-value: 1.84e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 515962626  195 KAHGLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAG 230
Cdd:pfam00702 156 KPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
COG4087 COG4087
Soluble P-type ATPase [General function prediction only];
207-235 5.77e-04

Soluble P-type ATPase [General function prediction only];


Pssm-ID: 443263 [Multi-domain]  Cd Length: 156  Bit Score: 39.37  E-value: 5.77e-04
                         10        20
                 ....*....|....*....|....*....
gi 515962626 207 QIEASQVVAIGDNNNDIQMIKAAGYGFAV 235
Cdd:COG4087   88 KLGAETTVAIGNGRNDVLMLKEAALGIAV 116
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
 9-237 5.97e-03

Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 37.50  E-value: 5.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626   9 DMDGTFLNSKK-QYNKAR-FLkqyEQLKQNNIHFVVASGNQLAKLVTYFPEINHEITFIAENGAHVVdagqelafahlsk 86
Cdd:COG3769    9 DLDGTLLDHDTySWAAALpAL---ARLKARGIPVILNTSKTAAEVEPLRQELGLSDPFIVENGAAIF------------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626  87 eqfskilkaIDPAYTSTMVICGKQSAYvHRSMNAENYAKVARYFEKL--TVIDDFYALDDL----VCKIT---------- 150
Cdd:COG3769   73 ---------IPKGYFAFPSGTADIDGY-WVIELGKPYAEIRAVLEQLreELGFKFTGFGDMsaeeVAELTglsleqaala 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515962626 151 ----FTaqE-------NESFAIF-EHFQKQSFvadKVLVpvssgfG--FIdLILPDQHKAHGLKLLLQKWQI---EASQV 213
Cdd:COG3769  143 kqreFS--EpllwlgsDEALERFiAALAALGL---TVLR------GgrFL-HLMGGADKGKAVRWLVEQYRQrfgKNVVT 210

                        250       260
                 ....*....|....*....|....
gi 515962626 214 VAIGDNNNDIQMIKAAGYGFAVEN 237
Cdd:COG3769  211 IALGDSPNDIPMLEAADIAVVIRS 234
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
193-230 7.11e-03

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 36.41  E-value: 7.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 515962626  193 QHKAH--GLKLLLQKWQIEASQVVAIGDNNNDIQMIKAAG 230
Cdd:pfam13419 133 GKKPDpdPILKALEQLGLKPEEVIYVGDSPRDIEAAKNAG 172
 
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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