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Conserved domains on  [gi|1327839098|ref|WP_102137520|]
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MULTISPECIES: Cof-type HAD-IIB family hydrolase [Providencia]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10530 super family cl32529
pyridoxal phosphate (PLP) phosphatase; Provisional
 2-272 7.55e-87

pyridoxal phosphate (PLP) phosphatase; Provisional


The actual alignment was detected with superfamily member PRK10530:

Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 259.96  E-value: 7.55e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098   2 YNVLALDLDGTVLTQEHTIHPAVKQAINNAAKQ-CHVMIVTGRHHTAARPYYDELGLTTPIICCNGTYIYDYQNEKVLTH 80
Cdd:PRK10530    3 YRVIALDLDGTLLTPKKTILPESLEALARAREAgYKVIIVTGRHHVAIHPFYQALALDTPAICCNGTYLYDYQAKKVLEA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098  81 NALTKENALTFIELAQQDKLKMVMYITDAMVYSKidPIDYMSAMEQWANNPTMAHPPKIYRIDSFEEQVQHADYIWKFVV 160
Cdd:PRK10530   83 DPLPVQQALQVIEMLDEHQIHGLMYVDDAMLYEH--PTGHVIRTLNWAQTLPPEQRPTFTQVDSLAQAARQVNAIWKFAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098 161 EGEpatlarflNLPWIKQtFNA----------EKSWSNRFDFAAKGNNKGTRLAEYLNSLGYDSNQVIAVGDNHNDISMI 230
Cdd:PRK10530  161 THE--------DLPQLQH-FAKhvehelglecEWSWHDQVDIARKGNSKGKRLTQWVEAQGWSMKNVVAFGDNFNDISML 231

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1327839098 231 ELAGLGVAMKNADDTVKSHADFVCAtDNNGDGLARLIHENIL 272
Cdd:PRK10530  232 EAAGLGVAMGNADDAVKARADLVIG-DNTTPSIAEFIYSHVL 272
 
Name Accession Description Interval E-value
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 2-272 7.55e-87

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 259.96  E-value: 7.55e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098   2 YNVLALDLDGTVLTQEHTIHPAVKQAINNAAKQ-CHVMIVTGRHHTAARPYYDELGLTTPIICCNGTYIYDYQNEKVLTH 80
Cdd:PRK10530    3 YRVIALDLDGTLLTPKKTILPESLEALARAREAgYKVIIVTGRHHVAIHPFYQALALDTPAICCNGTYLYDYQAKKVLEA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098  81 NALTKENALTFIELAQQDKLKMVMYITDAMVYSKidPIDYMSAMEQWANNPTMAHPPKIYRIDSFEEQVQHADYIWKFVV 160
Cdd:PRK10530   83 DPLPVQQALQVIEMLDEHQIHGLMYVDDAMLYEH--PTGHVIRTLNWAQTLPPEQRPTFTQVDSLAQAARQVNAIWKFAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098 161 EGEpatlarflNLPWIKQtFNA----------EKSWSNRFDFAAKGNNKGTRLAEYLNSLGYDSNQVIAVGDNHNDISMI 230
Cdd:PRK10530  161 THE--------DLPQLQH-FAKhvehelglecEWSWHDQVDIARKGNSKGKRLTQWVEAQGWSMKNVVAFGDNFNDISML 231

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1327839098 231 ELAGLGVAMKNADDTVKSHADFVCAtDNNGDGLARLIHENIL 272
Cdd:PRK10530  232 EAAGLGVAMGNADDAVKARADLVIG-DNTTPSIAEFIYSHVL 272
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 4-269 5.15e-74

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: 226.71  E-value: 5.15e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098   4 VLALDLDGTVLTQEHTIHPAVKQAINNAAKQ-CHVMIVTGRHHTAARPYYDELGLTTPIICCNGTYIYDYQNEKVLtHNA 82
Cdd:cd07516     1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKgIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEIL-ERL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098  83 LTKENALTFIELAQQDKLKMVMYITDAMvyskiDPIDYmsameqwanNPTMAHPPKIYRIDSFEEQVQHADYIWKFVVEG 162
Cdd:cd07516    80 ISKEDVKELEEFLRKLGIGINIYTNDDW-----ADTIY---------EENEDDEIIKPAEILDDLLLPPDEDITKILFVG 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098 163 EPA-TLARFLNLP-WIKQTFNAEKSWSNRFDFAAKGNNKGTRLAEYLNSLGYDSNQVIAVGDNHNDISMIELAGLGVAMK 240
Cdd:cd07516   146 EDEeLDELIAKLPeEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMG 225

                         250       260
                  ....*....|....*....|....*....
gi 1327839098 241 NADDTVKSHADFVCATdNNGDGLARLIHE 269
Cdd:cd07516   226 NAIDEVKEAADYVTLT-NNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 5-267 1.10e-62

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 197.85  E-value: 1.10e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098   5 LALDLDGTVLTQEHTIHPAVKQAINNA-AKQCHVMIVTGRHHTAARPYYDELGLTTPIICCNGTYIYDYqNEKVLTHNAL 83
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLkEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDE-NGKILYSNPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098  84 TKENALTFIELAQQDKLKMVMYITDAMVYSKIDPIDYMSameqwannpTMAHPPKIYRIDSFEEQVQHADYIWKFVVEGE 163
Cdd:pfam08282  80 SKEAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKIL---------KELNYTKSFVPEIDDFELLEDEDINKILILLD 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098 164 PATLARFLNlpWIKQTFN----AEKSWSNRFDFAAKGNNKGTRLAEYLNSLGYDSNQVIAVGDNHNDISMIELAGLGVAM 239
Cdd:pfam08282 151 EEDLDELEK--ELKELFGslitITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAM 228

                         250       260
                  ....*....|....*....|....*...
gi 1327839098 240 KNADDTVKSHADFVCATdNNGDGLARLI 267
Cdd:pfam08282 229 GNASPEVKAAADYVTDS-NNEDGVAKAL 255
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 4-267 5.62e-60

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: 190.94  E-value: 5.62e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098   4 VLALDLDGTVLTQEHTIHPAVKQAINNAAKQCH-VMIVTGRHHTAARPYYDELGLTTPIICCNGTYIYDYQNEkVLTHNA 82
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIkVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGE-ILYKKP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098  83 LTKENALTFIELAQQDKLKMVMYITDAMVYSKIDPIDYMsameqwANNPTMAHPPKIYR-IDSFEEQVQhadYIWKFVVE 161
Cdd:TIGR00099  80 LDLDLVEEILNFLKKHGLDVILYGDDSIYASKNDPEYFT------IFKKFLGEPKLEVVdIQYLPDDIL---KILLLFLD 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098 162 GEPATLAR-FLNLPWIKQTFNAEKSWSNRFDFAAKGNNKGTRLAEYLNSLGYDSNQVIAVGDNHNDISMIELAGLGVAMK 240
Cdd:TIGR00099 151 PEDLDLLIeALNKLELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMG 230

                         250       260
                  ....*....|....*....|....*..
gi 1327839098 241 NADDTVKSHADFVCAtDNNGDGLARLI 267
Cdd:TIGR00099 231 NADEELKALADYVTD-SNNEDGVALAL 256
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 1-269 3.14e-59

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: 186.88  E-value: 3.14e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098   1 MYNVLALDLDGTVLTQEHTIHPAVKQAINNAAKQ-CHVMIVTGRHHTAARPYYDELGLTTPIICCNGTYIYDYQNEkVLT 79
Cdd:COG0561     1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKgIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGE-VLY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098  80 HNALTKENALTFIELAQQDKLKMVMYItdamvyskidpidymsameqwannptmahppkiyridsfeeqvqhadyiwkfv 159
Cdd:COG0561    80 ERPLDPEDVREILELLREHGLHLQVVV----------------------------------------------------- 106

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098 160 vegepatlarflnlpwikqtfnaeKSWSNRFDFAAKGNNKGTRLAEYLNSLGYDSNQVIAVGDNHNDISMIELAGLGVAM 239
Cdd:COG0561   107 ------------------------RSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAM 162

                         250       260       270
                  ....*....|....*....|....*....|
gi 1327839098 240 KNADDTVKSHADFVCATdNNGDGLARLIHE 269
Cdd:COG0561   163 GNAPPEVKAAADYVTGS-NDEDGVAEALEK 191
 
Name Accession Description Interval E-value
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 2-272 7.55e-87

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 259.96  E-value: 7.55e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098   2 YNVLALDLDGTVLTQEHTIHPAVKQAINNAAKQ-CHVMIVTGRHHTAARPYYDELGLTTPIICCNGTYIYDYQNEKVLTH 80
Cdd:PRK10530    3 YRVIALDLDGTLLTPKKTILPESLEALARAREAgYKVIIVTGRHHVAIHPFYQALALDTPAICCNGTYLYDYQAKKVLEA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098  81 NALTKENALTFIELAQQDKLKMVMYITDAMVYSKidPIDYMSAMEQWANNPTMAHPPKIYRIDSFEEQVQHADYIWKFVV 160
Cdd:PRK10530   83 DPLPVQQALQVIEMLDEHQIHGLMYVDDAMLYEH--PTGHVIRTLNWAQTLPPEQRPTFTQVDSLAQAARQVNAIWKFAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098 161 EGEpatlarflNLPWIKQtFNA----------EKSWSNRFDFAAKGNNKGTRLAEYLNSLGYDSNQVIAVGDNHNDISMI 230
Cdd:PRK10530  161 THE--------DLPQLQH-FAKhvehelglecEWSWHDQVDIARKGNSKGKRLTQWVEAQGWSMKNVVAFGDNFNDISML 231

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1327839098 231 ELAGLGVAMKNADDTVKSHADFVCAtDNNGDGLARLIHENIL 272
Cdd:PRK10530  232 EAAGLGVAMGNADDAVKARADLVIG-DNTTPSIAEFIYSHVL 272
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 4-269 5.15e-74

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: 226.71  E-value: 5.15e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098   4 VLALDLDGTVLTQEHTIHPAVKQAINNAAKQ-CHVMIVTGRHHTAARPYYDELGLTTPIICCNGTYIYDYQNEKVLtHNA 82
Cdd:cd07516     1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKgIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEIL-ERL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098  83 LTKENALTFIELAQQDKLKMVMYITDAMvyskiDPIDYmsameqwanNPTMAHPPKIYRIDSFEEQVQHADYIWKFVVEG 162
Cdd:cd07516    80 ISKEDVKELEEFLRKLGIGINIYTNDDW-----ADTIY---------EENEDDEIIKPAEILDDLLLPPDEDITKILFVG 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098 163 EPA-TLARFLNLP-WIKQTFNAEKSWSNRFDFAAKGNNKGTRLAEYLNSLGYDSNQVIAVGDNHNDISMIELAGLGVAMK 240
Cdd:cd07516   146 EDEeLDELIAKLPeEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMG 225

                         250       260
                  ....*....|....*....|....*....
gi 1327839098 241 NADDTVKSHADFVCATdNNGDGLARLIHE 269
Cdd:cd07516   226 NAIDEVKEAADYVTLT-NNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 5-267 1.10e-62

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 197.85  E-value: 1.10e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098   5 LALDLDGTVLTQEHTIHPAVKQAINNA-AKQCHVMIVTGRHHTAARPYYDELGLTTPIICCNGTYIYDYqNEKVLTHNAL 83
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLkEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDE-NGKILYSNPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098  84 TKENALTFIELAQQDKLKMVMYITDAMVYSKIDPIDYMSameqwannpTMAHPPKIYRIDSFEEQVQHADYIWKFVVEGE 163
Cdd:pfam08282  80 SKEAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKIL---------KELNYTKSFVPEIDDFELLEDEDINKILILLD 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098 164 PATLARFLNlpWIKQTFN----AEKSWSNRFDFAAKGNNKGTRLAEYLNSLGYDSNQVIAVGDNHNDISMIELAGLGVAM 239
Cdd:pfam08282 151 EEDLDELEK--ELKELFGslitITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAM 228

                         250       260
                  ....*....|....*....|....*...
gi 1327839098 240 KNADDTVKSHADFVCATdNNGDGLARLI 267
Cdd:pfam08282 229 GNASPEVKAAADYVTDS-NNEDGVAKAL 255
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 4-267 5.62e-60

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: 190.94  E-value: 5.62e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098   4 VLALDLDGTVLTQEHTIHPAVKQAINNAAKQCH-VMIVTGRHHTAARPYYDELGLTTPIICCNGTYIYDYQNEkVLTHNA 82
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIkVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGE-ILYKKP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098  83 LTKENALTFIELAQQDKLKMVMYITDAMVYSKIDPIDYMsameqwANNPTMAHPPKIYR-IDSFEEQVQhadYIWKFVVE 161
Cdd:TIGR00099  80 LDLDLVEEILNFLKKHGLDVILYGDDSIYASKNDPEYFT------IFKKFLGEPKLEVVdIQYLPDDIL---KILLLFLD 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098 162 GEPATLAR-FLNLPWIKQTFNAEKSWSNRFDFAAKGNNKGTRLAEYLNSLGYDSNQVIAVGDNHNDISMIELAGLGVAMK 240
Cdd:TIGR00099 151 PEDLDLLIeALNKLELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMG 230

                         250       260
                  ....*....|....*....|....*..
gi 1327839098 241 NADDTVKSHADFVCAtDNNGDGLARLI 267
Cdd:TIGR00099 231 NADEELKALADYVTD-SNNEDGVALAL 256
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 1-269 3.14e-59

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: 186.88  E-value: 3.14e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098   1 MYNVLALDLDGTVLTQEHTIHPAVKQAINNAAKQ-CHVMIVTGRHHTAARPYYDELGLTTPIICCNGTYIYDYQNEkVLT 79
Cdd:COG0561     1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKgIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGE-VLY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098  80 HNALTKENALTFIELAQQDKLKMVMYItdamvyskidpidymsameqwannptmahppkiyridsfeeqvqhadyiwkfv 159
Cdd:COG0561    80 ERPLDPEDVREILELLREHGLHLQVVV----------------------------------------------------- 106

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098 160 vegepatlarflnlpwikqtfnaeKSWSNRFDFAAKGNNKGTRLAEYLNSLGYDSNQVIAVGDNHNDISMIELAGLGVAM 239
Cdd:COG0561   107 ------------------------RSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAM 162

                         250       260       270
                  ....*....|....*....|....*....|
gi 1327839098 240 KNADDTVKSHADFVCATdNNGDGLARLIHE 269
Cdd:COG0561   163 GNAPPEVKAAADYVTGS-NDEDGVAEALEK 191
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 5-272 1.14e-33

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 123.26  E-value: 1.14e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098   5 LALDLDGTVLTQEHTIHPAVKQAINNA-AKQCHVMIVTGRHHTAARPYYDELGLTTP---IICCNGTYIYDYQNEKVLTH 80
Cdd:PRK10513    6 IAIDMDGTLLLPDHTISPAVKQAIAAArAKGVNVVLTTGRPYAGVHRYLKELHMEQPgdyCITNNGALVQKAADGETVAQ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098  81 NALTKENALTFIELAQQ--------DKLKMVMYITDAMVYSKID------PIDYMSAMEQwanNPTMAHPpKIYRIDsfe 146
Cdd:PRK10513   86 TALSYDDYLYLEKLSREvgvhfhalDRNTLYTANRDISYYTVHEsfltgiPLVFREVEKM---DPNLQFP-KVMMID--- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098 147 eqvqhadyiwkfvvegEPATLARFL-NLPW-IKQTFNAEKSWSNRFDFAAKGNNKGT---RLAEYLnslGYDSNQVIAVG 221
Cdd:PRK10513  159 ----------------EPEILDAAIaRIPAeVKERYTVLKSAPYFLEILDKRVNKGTgvkSLAEHL---GIKPEEVMAIG 219

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1327839098 222 DNHNDISMIELAGLGVAMKNADDTVKSHADFVCATdNNGDGLARLIHENIL 272
Cdd:PRK10513  220 DQENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKS-NLEDGVAFAIEKYVL 269
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 4-265 6.51e-23

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: 93.44  E-value: 6.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098   4 VLALDLDGTVLTQEHTIHPAVKQAINNA-AKQCHVMIVTGRHHTAARPYYDELGLTTpIICCNGTYIYDyqNEKVLTHNA 82
Cdd:cd07517     2 IVFFDIDGTLLDEDTTIPESTKEAIAALkEKGILVVIATGRAPFEIQPIVKALGIDS-YVSYNGQYVFF--EGEVIYKNP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098  83 LTKENALTFIELAQQDKlkmvmyitdamvyskiDPIDYMSAMEqwannptmahppkiyridSFEeqvqHADYIWKFVVEG 162
Cdd:cd07517    79 LPQELVERLTEFAKEQG----------------HPVSFYGQLL------------------LFE----DEEEEQKYEELR 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098 163 EPATLARflnlpwikqtfnaeksWSNRF-DFAAKGNNKGTRLAEYLNSLGYDSNQVIAVGDNHNDISMIELAGLGVAMKN 241
Cdd:cd07517   121 PELRFVR----------------WHPLStDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGN 184

                         250       260
                  ....*....|....*....|....
gi 1327839098 242 ADDTVKSHADFVCAtDNNGDGLAR 265
Cdd:cd07517   185 AHEELKEIADYVTK-DVDEDGILK 207
PRK10976 PRK10976
putative hydrolase; Provisional
 1-247 1.28e-19

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 85.49  E-value: 1.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098   1 MYNVLALDLDGTVLTQEHTIHPAVKQAINN-AAKQCHVMIVTGRHHTAARPYYDELGLTTPIICCNGTYIYDYQNEKVLT 79
Cdd:PRK10976    1 MYQVVASDLDGTLLSPDHTLSPYAKETLKLlTARGIHFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDTDGNLIFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098  80 HN----------ALTKENALTFIELAQQDKLKMVMYITDAMVYSKIDPIDYmsameqwannptmahppKIYRIDSFEeqv 149
Cdd:PRK10976   81 HNldrdiasdlfGVVHDNPDIITNVYRDDEWFMNRHRPEEMRFFKEAVFKY-----------------QLYEPGLLE--- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098 150 qhADYIWK-FVVEGEPATLArflnlpWIKQTFNAEksWSNRFDFA----------AKGNNKGTRLAEYLNSLGYDSNQVI 218
Cdd:PRK10976  141 --PDGVSKvFFTCDSHEKLL------PLEQAINAR--WGDRVNVSfstltclevmAGGVSKGHALEAVAKKLGYSLKDCI 210

                         250       260
                  ....*....|....*....|....*....
gi 1327839098 219 AVGDNHNDISMIELAGLGVAMKNADDTVK 247
Cdd:PRK10976  211 AFGDGMNDAEMLSMAGKGCIMGNAHQRLK 239
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 195-268 2.60e-17

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 78.48  E-value: 2.60e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327839098 195 KGNNKGTRLAEYLNSLGYDSNQVIAVGDNHNDISMIELAGLGVAMKNADDTVKSHADFVCaTDNNGDGLARLIH 268
Cdd:PRK01158  154 PGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVANADEELKEAADYVT-EKSYGEGVAEAIE 226
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 5-267 3.28e-16

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: 75.16  E-value: 3.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098   5 LALDLDGTVLTQEHTIHPAVKQAINNAAKQCH-VMIVTGRHHTAARPYYDELGLTTPIICCNGTYIYDYQNEKVLthnAL 83
Cdd:TIGR01487   4 VAIDIDGTLTDPNRMISERAIEAIRKAEKKGIpVSLVTGNTVPFARALAVLIGTSGPVVAENGGVIFYNKEDIFL---AN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098  84 TKENAL-----TFIELAQQDKLKMVMYITDAMVYSKIdpIDYMSAMEQWANnptmahppkiyridsfeeqvqhadyiwkf 158
Cdd:TIGR01487  81 MEEEWFldeekKKRFPRDRLSNEYPRASLVIMREGKD--VDEVREIIKERG----------------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098 159 vvegepatlarfLNLpwikqtfnaeKSWSNRFDFAAKGNNKGTRLAEYLNSLGYDSNQVIAVGDNHNDISMIELAGLGVA 238
Cdd:TIGR01487 130 ------------LNL----------VASGFAIHIMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVA 187

                         250       260       270
                  ....*....|....*....|....*....|
gi 1327839098 239 MKNADDTVKSHADFVcaTDN-NGDGLARLI 267
Cdd:TIGR01487 188 VANADDQLKEIADYV--TSNpYGEGVVEVL 215
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 5-269 4.76e-16

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: 75.19  E-value: 4.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098   5 LALDLDGTVLTQEHTIHPAVKQAIN-NAAKQCHVMIVTGRHHTAARPYYDELGLTTPIICCNGTYIYDyqnekvlthnal 83
Cdd:TIGR01482   1 IASDIDGTLTDPNRAINESALEAIRkAESKGIPVVLVTGNSVQFARALAKLIGTPDPVIAENGGEISY------------ 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098  84 tkENALTFIELAQQDKlkmvMYITDAMVySKIDPIDYMSAmeQWannPTMAHPPKiyriDSFEEQVQHADYIWKFVVEGE 163
Cdd:TIGR01482  69 --NEGLDDIFLAYLEE----EWFLDIVI-AKTFPFSRLKV--QY---PRRASLVK----MRYGIDVDTVREIIKELGLNL 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098 164 PATLARFlnlpwikqtfnaekSWsnrfDFAAKGNNKGTRLAEYLNSLGYDSNQVIAVGDNHNDISMIELAGLGVAMKNAD 243
Cdd:TIGR01482 133 VAVDSGF--------------DI----HILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANAQ 194

                         250       260
                  ....*....|....*....|....*..
gi 1327839098 244 DTVKSHADFVcaTDN-NGDGLARLIHE 269
Cdd:TIGR01482 195 PELKEWADYV--TESpYGEGGAEAIGE 219
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 196-267 6.17e-16

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: 72.62  E-value: 6.17e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327839098 196 GNNKGTRLAEYLNSLGYDSNQVIAVGDNHNDISMIELAGLGVAMKNADDTVKSHADFVCaTDNNGDGLARLI 267
Cdd:cd07514    65 GVDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVT-DASYGDGVLEAI 135
PLN02887 PLN02887
hydrolase family protein
 8-269 1.65e-15

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 76.07  E-value: 1.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098   8 DLDGTVLTQEHTIHPAVKQAINNA-AKQCHVMIVTGRHHTAARPYYDELGLT---------TPIICCNGTYIYDYQNEKV 77
Cdd:PLN02887  314 DMDGTLLNSKSQISETNAKALKEAlSRGVKVVIATGKARPAVIDILKMVDLAgkdgiisesSPGVFLQGLLVYGRQGREI 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098  78 LTHN---ALTKENALTFIElaqqDKLKMVMYITDaMVYSKID-P-IDYMSameqwannpTMAHPPKIYRIDSFEEQVQHA 152
Cdd:PLN02887  394 YRSNldqEVCREACLYSLE----HKIPLIAFSQD-RCLTLFDhPlVDSLH---------TIYHEPKAEIMSSVDQLLAAA 459

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098 153 DyIWKFVVEGEPATLARFLNLPWIKQT---FNAEKSWSNRFDFAAKGNNKGTRLAEYLNSLGYDSNQVIAVGDNHNDISM 229
Cdd:PLN02887  460 D-IQKVIFLDTAEGVSSVLRPYWSEATgdrANVVQAQPDMLEIVPPGTSKGNGVKMLLNHLGVSPDEIMAIGDGENDIEM 538

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1327839098 230 IELAGLGVAMKNADDTVKSHADFVCATdNNGDGLARLIHE 269
Cdd:PLN02887  539 LQLASLGVALSNGAEKTKAVADVIGVS-NDEDGVADAIYR 577
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 191-267 2.16e-15

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: 72.23  E-value: 2.16e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327839098 191 DFAAKGNNKGTRLAEYLNSLGYDSNQVIAVGDNHNDISMIELAGLGVAMKNADDTVKSHADFVCAtDNNGDGLARLI 267
Cdd:cd07518   108 DIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEVKAAAKYVAP-SNNENGVLQVI 183
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 4-239 8.27e-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: 71.26  E-value: 8.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098   4 VLALDLDGTVLT-QEHTIHPAVKQAINNAAKQCH-VMIVTGRHHTAARPYYDELGLTTPIICCNGTYIYdYQNEKVLTHN 81
Cdd:TIGR01484   1 LLFFDLDGTLLDpNAHELSPETIEALERLREAGVkVVIVTGRSLAEIKELLKQLNLPLPLIAENGALIF-YPGEILYIEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098  82 ALTKEnaltFIELAQQDKLKMVMYitdamvyskidpidymSAMEQWANnptmahpPKIYRIDsfeeqvQHADYIWKFVVE 161
Cdd:TIGR01484  80 SDVFE----EILGIKFEEIGAELK----------------SLSEHYVG-------TFIEDKA------IAVAIHYVGAEL 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098 162 GEPATLARF--LNLPWI-KQTFNAEKSWSNRFDFAAKGNNKGTRLAEYLNSLGYDSNQVIAVGDNHNDISMIELAGLGVA 238
Cdd:TIGR01484 127 GQELDSKMRerLEKIGRnDLELEAIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVA 206


                  .
gi 1327839098 239 M 239
Cdd:TIGR01484 207 V 207
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 196-251 5.36e-13

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: 66.40  E-value: 5.36e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327839098 196 GNNKGTRLAEYLNSLGYDSNQVIAVGDNHNDISMIELAGLGVAMkNADDTVKSHAD 251
Cdd:COG0560   153 GEGKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAV-NPDPALREAAD 207
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 196-238 3.24e-08

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: 52.16  E-value: 3.24e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1327839098 196 GNNKGTRLAEYLNSLGYDSNQVIAVGDNHNDISMIELAGLGVA 238
Cdd:cd07500   135 AQRKAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIA 177
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 195-251 1.51e-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: 50.82  E-value: 1.51e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1327839098 195 KGNNKGTRLAEYLNSLGYDSNQVIAVGDNHNDISMIELAGLGVAMkNADDTVKSHAD 251
Cdd:TIGR00338 149 DASYKGKTLLILLRKEGISPENTVAVGDGANDLSMIKAAGLGIAF-NAKPKLQQKAD 204
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 198-265 2.36e-07

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: 49.06  E-value: 2.36e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327839098 198 NKGTRLAEYLNSLGYDSNQVIAVGDNHNDISMIELAGLGVAMKNADDTVKSHADFVCaTDNNGDGLAR 265
Cdd:cd01630    76 DKLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVT-RARGGRGAVR 142
PRK15126 PRK15126
HMP-PP phosphatase;
1-242 2.38e-07

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 50.85  E-value: 2.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098   1 MYNVLALDLDGTVLTQEHTIHPAVKQAINN-AAKQCHVMIVTGRHHTAARPYYDELGLTTPIICCNGTYIYDYQNEkVLT 79
Cdd:PRK15126    1 MARLAAFDMDGTLLMPDHHLGEKTLSTLARlRERDITLTFATGRHVLEMQHILGALSLDAYLITGNGTRVHSLEGE-LLH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098  80 HNALTKENALTFIELAQQDKLKMVMYITDAMVYSKIDPidymsAMEQwannptmAHppkiyRIDSFEEQVQH-----ADY 154
Cdd:PRK15126   80 RQDLPADVAELVLHQQWDTRASMHVFNDDGWFTGKEIP-----ALLQ-------AH-----VYSGFRYQLIDlkrlpAHG 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098 155 IWKFVVEGEPATLARflnlpwIKQTFNAEKSWSNRFDFAA--------KGNNKGTRLAEYLNSLGYDSNQVIAVGDNHND 226
Cdd:PRK15126  143 VTKICFCGDHDDLTR------LQIQLNEALGERAHLCFSAtdclevlpVGCNKGAALAVLSQHLGLSLADCMAFGDAMND 216

                         250
                  ....*....|....*.
gi 1327839098 227 ISMIELAGLGVAMKNA 242
Cdd:PRK15126  217 REMLGSVGRGFIMGNA 232
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 7-243 9.01e-07

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 49.17  E-value: 9.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098   7 LDLDGTVLTQEHTIHPAVKQAINN-AAKQCHVMIVTGRhhTAA--RPYYDELGLTTPIICCNGTYIYDYQNEKVLTHNAL 83
Cdd:PRK00192    9 TDLDGTLLDHHTYSYEPAKPALKAlKEKGIPVIPCTSK--TAAevEVLRKELGLEDPFIVENGAAIYIPKNYFPFQPDGE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098  84 TKENALTFIELAQQ-DKLKMVM-YITDAMVYsKIDPIDYMSAMEqwannptmahppkiyrIDSF----EEQVQHA---DY 154
Cdd:PRK00192   87 RLKGDYWVIELGPPyEELREILdEISDELGY-PLKGFGDLSAEE----------------VAELtglsGESARLAkdrEF 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098 155 IWKFVVEGEPATLARFLNlpwIKQTFNAEKSWSNRFDFAAKGNNKGT---RLAEYLNSLgyDSNQVIAVGDNHNDISMIE 231
Cdd:PRK00192  150 SEPFLWNGSEAAKERFEE---ALKRLGLKVTRGGRFLHLLGGGDKGKavrWLKELYRRQ--DGVETIALGDSPNDLPMLE 224

                         250
                  ....*....|..
gi 1327839098 232 LAGLGVAMKNAD 243
Cdd:PRK00192  225 AADIAVVVPGPD 236
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 4-244 1.23e-05

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: 45.42  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098   4 VLALDLDGTVLtqEHTIHPA----VKQAINNAAKQCHVMIV--TGRHHTAARPYYDELGLTTP--IICCNGTYIYdyqne 75
Cdd:cd02605     1 LLVSDLDETLV--GHDTNLQalerLQDLLEQLTADNDVILVyaTGRSPESVLELIKEVMLPKPdfIISDVGTEIY----- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098  76 kVLTHNALTKENALTFIeLAQQDKLKMVMYITDAMvyskidpidymsaMEQWANNPTMAHPPKI----------YRIDSF 145
Cdd:cd02605    74 -YGESGYLEPDTYWNEV-LSEGWERFLFEAIADLF-------------KQLKPQSELEQNPHKIsfyldpqndaAVIEQL 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098 146 EEQVQHADYIWKFVVEGEpatLARFLnlpwikqtfnaekswsnrfDFAAKGNNKGTRLAEYLNSLGYDSNQVIAVGDNHN 225
Cdd:cd02605   139 EEMLLKAGLTVRIIYSSG---LAYDL-------------------DILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGN 196

                         250
                  ....*....|....*....
gi 1327839098 226 DISMIELAGLGVAMKNADD 244
Cdd:cd02605   197 DIALLSTGTRGVIVGNAQP 215
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 4-243 2.72e-05

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: 44.56  E-value: 2.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098   4 VLALDLDGTVLTQEHTIHPAVKQAINNAAKQCHVMIVTGRHHTAARPYYDELGLTTP--IICCNGTYIYdYQNEKVLTHN 81
Cdd:pfam05116   4 LLVSDLDNTLVDGDNEALARLNQLLEAYRPDVGLVFATGRSLDSAKELLKEKPLPTPdyLITSVGTEIY-YGPSLVPDQS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098  82 ----------------ALTKENALTFIELAQQDKLKMVMYITDAMVYSKIDPIDYMsameqwannptmahppkiyridsF 145
Cdd:pfam05116  83 wqehldyhwdrqavveALAKFPGLTLQPEEEQRPHKVSYFLDPEAAAAVLAELEQL-----------------------L 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839098 146 EEQVQHADYIWkfvvegepatlarflnlpwikqtfnaekSWSNRFDFAAKGNNKGTRLAEYLNSLGYDSNQVIAVGDNHN 225
Cdd:pfam05116 140 RKRGLDVKVIY----------------------------SSGRDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGN 191

                         250
                  ....*....|....*...
gi 1327839098 226 DISMIELAGLGVAMKNAD 243
Cdd:pfam05116 192 DEELFIGGTRGVVVGNAQ 209
thrH PRK13582
bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;
207-267 5.33e-04

bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;


Pssm-ID: 237437 [Multi-domain]  Cd Length: 205  Bit Score: 40.30  E-value: 5.33e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327839098 207 LNSLGYDsnqVIAVGDNHNDISMIELAGLGVAMKNADDTVKSHADFVcATDNNGDGLARLI 267
Cdd:PRK13582  140 LKSLGYR---VIAAGDSYNDTTMLGEADAGILFRPPANVIAEFPQFP-AVHTYDELLAAID 196
COG4087 COG4087
Soluble P-type ATPase [General function prediction only];
204-272 6.89e-04

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


Pssm-ID: 443263 [Multi-domain]  Cd Length: 156  Bit Score: 39.37  E-value: 6.89e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327839098 204 AEYLNSLGydSNQVIAVGDNHNDISMIELAGLGVAMKNADDT-VKS--HADFVCATDNngDGLARLIHENIL 272
Cdd:COG4087    83 LEFVEKLG--AETTVAIGNGRNDVLMLKEAALGIAVIGPEGAsVKAllAADIVVKSIL--DALDLLLNPKRL 150
serB PRK11133
phosphoserine phosphatase; Provisional
 202-238 1.57e-03

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 39.16  E-value: 1.57e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1327839098 202 RLAEYLNslgYDSNQVIAVGDNHNDISMIELAGLGVA 238
Cdd:PRK11133  255 RLAQEYE---IPLAQTVAIGDGANDLPMIKAAGLGIA 288
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 195-233 2.50e-03

Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model represents a subfamily of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. Subfamily IA, B, C and D are distinguished from the rest of the superfamily by the presence of a variable domain between the first and second conserved catalytic motifs. In subfamilies IA and IB, this domain consists of an alpha-helical bundle. It was necessary to model these two subfamilies separately, breaking them at a an apparent phylogenetic bifurcation, so that the resulting model(s) are not so broadly defined that members of subfamily III (which lack the variable domain) are included. Subfamily IA includes the enzyme phosphoserine phosphatase (TIGR00338) as well as three hypothetical equivalogs. Many members of these hypothetical equivalogs have been annotated as PSPase-like or PSPase-family proteins. In particular, the hypothetical equivalog which appears to be most closely related to PSPase contains only Archaea (while TIGR00338 contains only eukaryotes and bacteria) of which some are annotated as PSPases. Although this is a reasonable conjecture, none of these sequences has sufficient evidence for this assignment. If such should be found, this model should be retired while the PSPase model should be broadened to include these sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273653 [Multi-domain]  Cd Length: 177  Bit Score: 37.72  E-value: 2.50e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1327839098 195 KGNNKGTRLAEYLNSLGYDSNQVIAVGDNHNDISMIELA 233
Cdd:TIGR01488 139 EGECKGKVLKELLEESKITLKKIIAVGDSVNDLPMLKLA 177
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 191-239 3.21e-03

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: 36.22  E-value: 3.21e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1327839098 191 DFAAKGNNKGTRLAEYLNSLGYDSNQVIAVGDNHNDISMIELAG-LGVAM 239
Cdd:cd01427    57 DGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSENDIEAARAAGgRTVAV 106
 
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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