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MULTISPECIES: Cof-type HAD-IIB family hydrolase [Mammaliicoccus]

Protein Classification

Cof-type HAD-IIB family hydrolase( domain architecture ID 11576297)

Cof-type HAD-IIB family hydrolase, part of the HAD (haloacid dehalogenase) family that includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

CATH:  3.30.1240.10
EC:  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_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 6-264 3.34e-70

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: 216.69  E-value: 3.34e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157   6 IVMDMDDTLLTSENKISEETHAYLLKKQQEGMKIILASGRPTAGMTKHAESLNLkqnGGYIVSYNGAIITDAaTNEVVFK 85
Cdd:cd07516     2 IALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGL---DSPLITFNGALVYDP-TGKEILE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157  86 QTIDKENAHKIIDFCRENNFFSLTYINDEIVYDsthEYMNIESELTGLPMVSVSDLKEVITEDVPKVMGIDYEENISKAN 165
Cdd:cd07516    78 RLISKEDVKELEEFLRKLGIGINIYTNDDWADT---IYEENEDDEIIKPAEILDDLLLPPDEDITKILFVGEDEELDELI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157 166 QSLNGQFNDHISSTTSKPYFLEFMNNEVSKGKSLQKLFDKIEADFSEVIAFGDSLNDSDMLEKAAIGVAMGNANYTIKEL 245
Cdd:cd07516   155 AKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDEVKEA 234

                         250
                  ....*....|....*....
gi 1337424157 246 ADVVTDDHDNNGIVTALEK 264
Cdd:cd07516   235 ADYVTLTNNEDGVAKAIEK 253
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 6-264 3.34e-70

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: 216.69  E-value: 3.34e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157   6 IVMDMDDTLLTSENKISEETHAYLLKKQQEGMKIILASGRPTAGMTKHAESLNLkqnGGYIVSYNGAIITDAaTNEVVFK 85
Cdd:cd07516     2 IALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGL---DSPLITFNGALVYDP-TGKEILE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157  86 QTIDKENAHKIIDFCRENNFFSLTYINDEIVYDsthEYMNIESELTGLPMVSVSDLKEVITEDVPKVMGIDYEENISKAN 165
Cdd:cd07516    78 RLISKEDVKELEEFLRKLGIGINIYTNDDWADT---IYEENEDDEIIKPAEILDDLLLPPDEDITKILFVGEDEELDELI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157 166 QSLNGQFNDHISSTTSKPYFLEFMNNEVSKGKSLQKLFDKIEADFSEVIAFGDSLNDSDMLEKAAIGVAMGNANYTIKEL 245
Cdd:cd07516   155 AKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDEVKEA 234

                         250
                  ....*....|....*....
gi 1337424157 246 ADVVTDDHDNNGIVTALEK 264
Cdd:cd07516   235 ADYVTLTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-262 1.28e-65

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 204.78  E-value: 1.28e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157   6 IVMDMDDTLLTSENKISEETHAYLLKKQQEGMKIILASGRPTAGMTKHAESLNLKQnggYIVSYNGAIITDAaTNEVVFK 85
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDD---PVICYNGALIYDE-NGKILYS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157  86 QTIDKENAHKIIDFCRENNFFSLTYINDEIVYDST--HEYMNIESELTGLPMVSVSDLKEVITEDVPKVMGIDYEENISK 163
Cdd:pfam08282  77 NPISKEAVKEIIEYLKENNLEILLYTDDGVYILNDneLEKILKELNYTKSFVPEIDDFELLEDEDINKILILLDEEDLDE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157 164 ANQSLNGQFNDHISSTTSKPYFLEFMNNEVSKGKSLQKLFDKIEADFSEVIAFGDSLNDSDMLEKAAIGVAMGNANYTIK 243
Cdd:pfam08282 157 LEKELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVK 236

                         250
                  ....*....|....*....
gi 1337424157 244 ELADVVTDDHDNNGIVTAL 262
Cdd:pfam08282 237 AAADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 2-265 5.29e-55

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: 175.71  E-value: 5.29e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157   2 TYKYIVMDMDDTLLTSENKISEETHAYLLKKQQEGMKIILASGRPTAGMTKHAESLNLKqngGYIVSYNGAIITDAAtNE 81
Cdd:COG0561     1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLD---DPLITSNGALIYDPD-GE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157  82 VVFKQTIDKENAHKIIDFCRENnffsltyindeivydstheymnieseltGLPMVSVsdlkevitedvpkvmgidyeeni 161
Cdd:COG0561    77 VLYERPLDPEDVREILELLREH----------------------------GLHLQVV----------------------- 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157 162 skanqslngqfndhissTTSKPYFLEFMNNEVSKGKSLQKLFDKIEADFSEVIAFGDSLNDSDMLEKAAIGVAMGNANYT 241
Cdd:COG0561   106 -----------------VRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPE 168

                         250       260
                  ....*....|....*....|....
gi 1337424157 242 IKELADVVTDDHDNNGIVTALEKL 265
Cdd:COG0561   169 VKAAADYVTGSNDEDGVAEALEKL 192
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-262 9.96e-54

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: 174.38  E-value: 9.96e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157   5 YIVMDMDDTLLTSENKISEETHAYLLKKQQEGMKIILASGRPTAGMTKHAESLNLKQnggYIVSYNGAIITDAATnEVVF 84
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDT---PFITANGAAVIDDQG-EILY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157  85 KQTIDKENAHKIIDFCRENNFfSLTYINDEIVY--DSTHEYMNIESELTGLPMVSVSDLKEVITEDVPKVMGIDYEENIS 162
Cdd:TIGR00099  77 KKPLDLDLVEEILNFLKKHGL-DVILYGDDSIYasKNDPEYFTIFKKFLGEPKLEVVDIQYLPDDILKILLLFLDPEDLD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157 163 KANQSLNGQFN-DHISSTTSKPYFLEFMNNEVSKGKSLQKLFDKIEADFSEVIAFGDSLNDSDMLEKAAIGVAMGNANYT 241
Cdd:TIGR00099 156 LLIEALNKLELeENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEE 235

                         250       260
                  ....*....|....*....|.
gi 1337424157 242 IKELADVVTDDHDNNGIVTAL 262
Cdd:TIGR00099 236 LKALADYVTDSNNEDGVALAL 256
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 1-264 3.59e-47

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 158.32  E-value: 3.59e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157   1 MTYKYIVMDMDDTLLTSENKISEETHAYLLKKQQEGMKIILASGRPTAGMTKHAESLNLKQNGGYIVSYNGAIITDAATN 80
Cdd:PRK10513    1 MAIKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPGDYCITNNGALVQKAADG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157  81 EVVFKQTIDKENAHKIIDFCRENN-------FFSLTYINDEIVYDSTHEymnieSELTGLPMV--SVSDLKEVITedVPK 151
Cdd:PRK10513   81 ETVAQTALSYDDYLYLEKLSREVGvhfhaldRNTLYTANRDISYYTVHE-----SFLTGIPLVfrEVEKMDPNLQ--FPK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157 152 VMGIDYEENISKANQSLNGQFNDHISSTTSKPYFLEFMNNEVSKGKSLQKLFDKIEADFSEVIAFGDSLNDSDMLEKAAI 231
Cdd:PRK10513  154 VMMIDEPEILDAAIARIPAEVKERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYAGV 233

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1337424157 232 GVAMGNANYTIKELADVVTDDHDNNGIVTALEK 264
Cdd:PRK10513  234 GVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIEK 266
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 6-264 3.34e-70

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: 216.69  E-value: 3.34e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157   6 IVMDMDDTLLTSENKISEETHAYLLKKQQEGMKIILASGRPTAGMTKHAESLNLkqnGGYIVSYNGAIITDAaTNEVVFK 85
Cdd:cd07516     2 IALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGL---DSPLITFNGALVYDP-TGKEILE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157  86 QTIDKENAHKIIDFCRENNFFSLTYINDEIVYDsthEYMNIESELTGLPMVSVSDLKEVITEDVPKVMGIDYEENISKAN 165
Cdd:cd07516    78 RLISKEDVKELEEFLRKLGIGINIYTNDDWADT---IYEENEDDEIIKPAEILDDLLLPPDEDITKILFVGEDEELDELI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157 166 QSLNGQFNDHISSTTSKPYFLEFMNNEVSKGKSLQKLFDKIEADFSEVIAFGDSLNDSDMLEKAAIGVAMGNANYTIKEL 245
Cdd:cd07516   155 AKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDEVKEA 234

                         250
                  ....*....|....*....
gi 1337424157 246 ADVVTDDHDNNGIVTALEK 264
Cdd:cd07516   235 ADYVTLTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-262 1.28e-65

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 204.78  E-value: 1.28e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157   6 IVMDMDDTLLTSENKISEETHAYLLKKQQEGMKIILASGRPTAGMTKHAESLNLKQnggYIVSYNGAIITDAaTNEVVFK 85
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDD---PVICYNGALIYDE-NGKILYS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157  86 QTIDKENAHKIIDFCRENNFFSLTYINDEIVYDST--HEYMNIESELTGLPMVSVSDLKEVITEDVPKVMGIDYEENISK 163
Cdd:pfam08282  77 NPISKEAVKEIIEYLKENNLEILLYTDDGVYILNDneLEKILKELNYTKSFVPEIDDFELLEDEDINKILILLDEEDLDE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157 164 ANQSLNGQFNDHISSTTSKPYFLEFMNNEVSKGKSLQKLFDKIEADFSEVIAFGDSLNDSDMLEKAAIGVAMGNANYTIK 243
Cdd:pfam08282 157 LEKELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVK 236

                         250
                  ....*....|....*....
gi 1337424157 244 ELADVVTDDHDNNGIVTAL 262
Cdd:pfam08282 237 AAADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 2-265 5.29e-55

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: 175.71  E-value: 5.29e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157   2 TYKYIVMDMDDTLLTSENKISEETHAYLLKKQQEGMKIILASGRPTAGMTKHAESLNLKqngGYIVSYNGAIITDAAtNE 81
Cdd:COG0561     1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLD---DPLITSNGALIYDPD-GE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157  82 VVFKQTIDKENAHKIIDFCRENnffsltyindeivydstheymnieseltGLPMVSVsdlkevitedvpkvmgidyeeni 161
Cdd:COG0561    77 VLYERPLDPEDVREILELLREH----------------------------GLHLQVV----------------------- 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157 162 skanqslngqfndhissTTSKPYFLEFMNNEVSKGKSLQKLFDKIEADFSEVIAFGDSLNDSDMLEKAAIGVAMGNANYT 241
Cdd:COG0561   106 -----------------VRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPE 168

                         250       260
                  ....*....|....*....|....
gi 1337424157 242 IKELADVVTDDHDNNGIVTALEKL 265
Cdd:COG0561   169 VKAAADYVTGSNDEDGVAEALEKL 192
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-262 9.96e-54

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: 174.38  E-value: 9.96e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157   5 YIVMDMDDTLLTSENKISEETHAYLLKKQQEGMKIILASGRPTAGMTKHAESLNLKQnggYIVSYNGAIITDAATnEVVF 84
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDT---PFITANGAAVIDDQG-EILY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157  85 KQTIDKENAHKIIDFCRENNFfSLTYINDEIVY--DSTHEYMNIESELTGLPMVSVSDLKEVITEDVPKVMGIDYEENIS 162
Cdd:TIGR00099  77 KKPLDLDLVEEILNFLKKHGL-DVILYGDDSIYasKNDPEYFTIFKKFLGEPKLEVVDIQYLPDDILKILLLFLDPEDLD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157 163 KANQSLNGQFN-DHISSTTSKPYFLEFMNNEVSKGKSLQKLFDKIEADFSEVIAFGDSLNDSDMLEKAAIGVAMGNANYT 241
Cdd:TIGR00099 156 LLIEALNKLELeENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEE 235

                         250       260
                  ....*....|....*....|.
gi 1337424157 242 IKELADVVTDDHDNNGIVTAL 262
Cdd:TIGR00099 236 LKALADYVTDSNNEDGVALAL 256
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 1-264 3.59e-47

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 158.32  E-value: 3.59e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157   1 MTYKYIVMDMDDTLLTSENKISEETHAYLLKKQQEGMKIILASGRPTAGMTKHAESLNLKQNGGYIVSYNGAIITDAATN 80
Cdd:PRK10513    1 MAIKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPGDYCITNNGALVQKAADG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157  81 EVVFKQTIDKENAHKIIDFCRENN-------FFSLTYINDEIVYDSTHEymnieSELTGLPMV--SVSDLKEVITedVPK 151
Cdd:PRK10513   81 ETVAQTALSYDDYLYLEKLSREVGvhfhaldRNTLYTANRDISYYTVHE-----SFLTGIPLVfrEVEKMDPNLQ--FPK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157 152 VMGIDYEENISKANQSLNGQFNDHISSTTSKPYFLEFMNNEVSKGKSLQKLFDKIEADFSEVIAFGDSLNDSDMLEKAAI 231
Cdd:PRK10513  154 VMMIDEPEILDAAIARIPAEVKERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYAGV 233

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1337424157 232 GVAMGNANYTIKELADVVTDDHDNNGIVTALEK 264
Cdd:PRK10513  234 GVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIEK 266
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 4-265 1.09e-35

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: 126.57  E-value: 1.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157   4 KYIVMDMDDTLLTSENKISEETHAYLLKKQQEGMKIILASGRPTAGMtkHAESLNLKQNGgyIVSYNGAIITDAatNEVV 83
Cdd:cd07517     1 KIVFFDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEI--QPIVKALGIDS--YVSYNGQYVFFE--GEVI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157  84 FKQTIDKENAHKIIDFCRENNFfsltyindEIVYdstheymnieseltGLPMVSVSDLKEVITedvpkvmgidYEENISk 163
Cdd:cd07517    75 YKNPLPQELVERLTEFAKEQGH--------PVSF--------------YGQLLLFEDEEEEQK----------YEELRP- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157 164 anqslngqfndHISSTTSKPYFLEFMNNEVSKGKSLQKLFDKIEADFSEVIAFGDSLNDSDMLEKAAIGVAMGNANYTIK 243
Cdd:cd07517   122 -----------ELRFVRWHPLSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELK 190

                         250       260
                  ....*....|....*....|..
gi 1337424157 244 ELADVVTDDHDNNGIVTALEKL 265
Cdd:cd07517   191 EIADYVTKDVDEDGILKALKHF 212
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 1-258 8.51e-24

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 97.02  E-value: 8.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157   1 MTYKYIVMDMDDTLLTSENKISEETHAYLLKKQQEGMKIILASGRPTAGMTKHAESLNLKQ-----NGGYIVSYNGAIIT 75
Cdd:PRK10530    1 MTYRVIALDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRHHVAIHPFYQALALDTpaiccNGTYLYDYQAKKVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157  76 DAatnevvfkQTIDKENAHKIIDFCRENNFFSLTYINDEIVYDstHEYMNIESELT---GLP------MVSVSDLKEVIt 146
Cdd:PRK10530   81 EA--------DPLPVQQALQVIEMLDEHQIHGLMYVDDAMLYE--HPTGHVIRTLNwaqTLPpeqrptFTQVDSLAQAA- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157 147 EDVpkvmgidyeENISKanqslngqFNDHISSTTSKPYFLEFMNNEV-------------------SKGKSLQKLFDKIE 207
Cdd:PRK10530  150 RQV---------NAIWK--------FALTHEDLPQLQHFAKHVEHELglecewswhdqvdiarkgnSKGKRLTQWVEAQG 212

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1337424157 208 ADFSEVIAFGDSLNDSDMLEKAAIGVAMGNANYTIKELADVVTDDHDNNGI 258
Cdd:PRK10530  213 WSMKNVVAFGDNFNDISMLEAAGLGVAMGNADDAVKARADLVIGDNTTPSI 263
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 1-266 1.44e-22

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 92.73  E-value: 1.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157   1 MTYKYIVMDMDDTLLTSENKISEETHAYLLKKQQEGMKIILASGRPTAGMtkHAESLnLKQNGGYIVSYNGAIITDAATN 80
Cdd:PRK01158    1 MKIKAIAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATGNVLCFA--RAAAK-LIGTSGPVIAENGGVISVGFDG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157  81 EVVFKQTIDKENAHKiidfcrenNFFSLTYINDEIVYDSTHEyMNIESELTGLPMVSVSDLKEVITEDVPKVMGIDyeen 160
Cdd:PRK01158   78 KRIFLGDIEECEKAY--------SELKKRFPEASTSLTKLDP-DYRKTEVALRRTVPVEEVRELLEELGLDLEIVD---- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157 161 iskanqslnGQFNDHIssttskpyflefMNNEVSKGKSLQKLFDKIEADFSEVIAFGDSLNDSDMLEKAAIGVAMGNANY 240
Cdd:PRK01158  145 ---------SGFAIHI------------KSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVANADE 203

                         250       260
                  ....*....|....*....|....*.
gi 1337424157 241 TIKELADVVTDDHDNNGIVTALEKLL 266
Cdd:PRK01158  204 ELKEAADYVTEKSYGEGVAEAIEHLL 229
PLN02887 PLN02887
hydrolase family protein
 3-262 8.76e-19

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 85.70  E-value: 8.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157   3 YKYIVMDMDDTLLTSENKISEETHAYLLKKQQEGMKIILASGRPTAGMTKHAESLNLKQNGGYI------VSYNGAIITD 76
Cdd:PLN02887  308 FSYIFCDMDGTLLNSKSQISETNAKALKEALSRGVKVVIATGKARPAVIDILKMVDLAGKDGIIsesspgVFLQGLLVYG 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157  77 AATNEVvFKQTIDKenahkiiDFCRENNFFSLTY--------------INDEIVYDSTHeymNIESELTGLPMVSVSDLK 142
Cdd:PLN02887  388 RQGREI-YRSNLDQ-------EVCREACLYSLEHkipliafsqdrcltLFDHPLVDSLH---TIYHEPKAEIMSSVDQLL 456

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157 143 EviTEDVPKVMGIDYEENISKA-----NQSLNGQFNdhisSTTSKPYFLEFMNNEVSKGKSLQKLFDKIEADFSEVIAFG 217
Cdd:PLN02887  457 A--AADIQKVIFLDTAEGVSSVlrpywSEATGDRAN----VVQAQPDMLEIVPPGTSKGNGVKMLLNHLGVSPDEIMAIG 530

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1337424157 218 DSLNDSDMLEKAAIGVAMGNANYTIKELADVVTDDHDNNGIVTAL 262
Cdd:PLN02887  531 DGENDIEMLQLASLGVALSNGAEKTKAVADVIGVSNDEDGVADAI 575
PRK10976 PRK10976
putative hydrolase; Provisional
 3-245 1.43e-17

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 79.71  E-value: 1.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157   3 YKYIVMDMDDTLLTSENKISEETHAYLLKKQQEGMKIILASGRPTAGMTKHAESLNLKqngGYIVSYNGAIITDAAtNEV 82
Cdd:PRK10976    2 YQVVASDLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRHHVDVGQIRDNLEIK---SYMITSNGARVHDTD-GNL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157  83 VFKQTIDKENAHkiidfcrenNFFSLTYINDEI---VYDSTHEYMNIES-ELTGLPMVSVSDLK-----EVITEDVPKVM 153
Cdd:PRK10976   78 IFSHNLDRDIAS---------DLFGVVHDNPDIitnVYRDDEWFMNRHRpEEMRFFKEAVFKYQlyepgLLEPDGVSKVF 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157 154 GI--DYEENISkANQSLNGQFNDHISSTTSKPYFLEFMNNEVSKGKSLQKLFDKIEADFSEVIAFGDSLNDSDMLEKAAI 231
Cdd:PRK10976  149 FTcdSHEKLLP-LEQAINARWGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGK 227

                         250
                  ....*....|....
gi 1337424157 232 GVAMGNANYTIKEL 245
Cdd:PRK10976  228 GCIMGNAHQRLKDL 241
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 151-263 1.96e-16

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: 74.93  E-value: 1.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157 151 KVMGIDYEENISKANQSLNGQFNDHISSTTSKPYFLEFMNNEVSKGKSLQKLFDKIEADFSEVIAFGDSLNDSDMLEKAA 230
Cdd:cd07518    72 KFTLNVPDEAAPDIIDELNQKFGGILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAG 151

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1337424157 231 IGVAMGNANYTIKELADVVTDDHDNNGIVTALE 263
Cdd:cd07518   152 YSYAMENAPEEVKAAAKYVAPSNNENGVLQVIE 184
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 180-266 4.46e-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: 73.01  E-value: 4.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157 180 TSKPYFLEfmNNEVSKGKSLQKLFDKIEADFSEVIAFGDSLNDSDMLEKAAIGVAMGNANYTIKELADVVTDDHDNNGIV 259
Cdd:cd07514    55 LSGPVVAE--NGGVDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVL 132


                  ....*..
gi 1337424157 260 TALEKLL 266
Cdd:cd07514   133 EAIDKLL 139
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 5-235 2.36e-14

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: 69.72  E-value: 2.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157   5 YIVMDMDDTLLTSEN-KISEETHAYLLKKQQEGMKIILASGRPTAGMTKHAESLNLKQNggyIVSYNGAIItdaatnevv 83
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAhELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLPLP---LIAENGALI--------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157  84 fkqtidkenahkiidfcrennffsltYINDEIVY----DSTHEYMNIESELTGLPMVS-VSDLKEVITEDVPKVMGIDY- 157
Cdd:TIGR01484  69 --------------------------FYPGEILYiepsDVFEEILGIKFEEIGAELKSlSEHYVGTFIEDKAIAVAIHYv 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157 158 -----EENISKANQSLN--GQFNDHISSTTSKPYFLEFMNNEVSKGKSLQKLFDKIEADFSEVIAFGDSLNDSDMLEKAA 230
Cdd:TIGR01484 123 gaelgQELDSKMRERLEkiGRNDLELEAIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAG 202


                  ....*
gi 1337424157 231 IGVAM 235
Cdd:TIGR01484 203 LAVAV 207
PRK15126 PRK15126
HMP-PP phosphatase;
9-238 6.29e-14

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 69.72  E-value: 6.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157   9 DMDDTLLTSENKISEETHAYLLKKQQEGMKIILASGRPTAGMTKHAESLNLKqngGYIVSYNGAIITDAaTNEVVFKQTI 88
Cdd:PRK15126    8 DMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHVLEMQHILGALSLD---AYLITGNGTRVHSL-EGELLHRQDL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157  89 DKENAHKI----------IDFCRENNFFSLTYINDEIvydSTHEYMNIESELTglpmvsvsDLKEVITEDVPKVMGIDYE 158
Cdd:PRK15126   84 PADVAELVlhqqwdtrasMHVFNDDGWFTGKEIPALL---QAHVYSGFRYQLI--------DLKRLPAHGVTKICFCGDH 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157 159 ENISKANQSLNGQFNDHISSTTSKPYFLEFMNNEVSKGKSLQKLFDKIEADFSEVIAFGDSLNDSDMLEKAAIGVAMGNA 238
Cdd:PRK15126  153 DDLTRLQIQLNEALGERAHLCFSATDCLEVLPVGCNKGAALAVLSQHLGLSLADCMAFGDAMNDREMLGSVGRGFIMGNA 232
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 6-266 4.34e-11

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: 60.94  E-value: 4.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157   6 IVMDMDDTLLTSENKISEETHAYLLKKQQEGMKIILASGRptagmTKH-AESLN-LKQNGGYIVSYNGAIITDAATNEVV 83
Cdd:TIGR01482   1 IASDIDGTLTDPNRAINESALEAIRKAESKGIPVVLVTGN-----SVQfARALAkLIGTPDPVIAENGGEISYNEGLDDI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157  84 FKQTIDKEnahkiidfCRENNFFSLTYINDEIvydsTHEYMNIESEltglpmVSVSDLKEVitEDVPKVmgidyeenISK 163
Cdd:TIGR01482  76 FLAYLEEE--------WFLDIVIAKTFPFSRL----KVQYPRRASL------VKMRYGIDV--DTVREI--------IKE 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157 164 ANQSLNgqfndhissTTSKPYFLEFMNNEVSKGKSLQKLFDKIEADFSEVIAFGDSLNDSDMLEKAAIGVAMGNANYTIK 243
Cdd:TIGR01482 128 LGLNLV---------AVDSGFDIHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANAQPELK 198

                         250       260
                  ....*....|....*....|....*..
gi 1337424157 244 ELADVVTDDHDNNG----IVTALEKLL 266
Cdd:TIGR01482 199 EWADYVTESPYGEGgaeaIGEILQAIG 225
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 184-265 3.29e-06

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: 46.96  E-value: 3.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157 184 YFLEFMNNEVSKGKSLQKLFDKIEADFSEVIAFGDSLNDSDMLEKAAIGVAMGNANYTIKELADVVTDDHDNN-----GI 258
Cdd:cd02605   159 YDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPELLKWADRVTRSRLAKgpyagGI 238


                  ....*..
gi 1337424157 259 VTALEKL 265
Cdd:cd02605   239 LEGLAHF 245
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 195-247 7.40e-06

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: 45.60  E-value: 7.40e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1337424157 195 KGKSLQKLFDKIEADFSEVIAFGDSLNDSDMLEKAAIGVAMgNANYTIKELAD 247
Cdd:COG0560   156 KAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAV-NPDPALREAAD 207
P-type_ATPase_SERCA cd02083
sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; ...
 209-263 4.46e-05

sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; SERCA is a transmembrane (Ca2+)-ATPase and a major regulator of Ca(2+) homeostasis and contractility in cardiac and skeletal muscle. It re-sequesters cytoplasmic Ca(2+) to the sarco/endoplasmic reticulum store, thereby also terminating Ca(2+)-induced signaling such as in muscle contraction. Three genes (ATP2A1-3/SERCA1-3) encode SERCA pumps in mammals, further isoforms exist due to alternative splicing of transcripts. The activity of SERCA is regulated by two small membrane proteins called phospholamban and sarcolipin. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319778 [Multi-domain]  Cd Length: 979  Bit Score: 44.59  E-value: 4.46e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1337424157 209 DFSEVIAF-GDSLNDSDMLEKAAIGVAMGNANYTIKELADVVTDDHDNNGIVTALE 263
Cdd:cd02083   683 SQGEITAMtGDGVNDAPALKKAEIGIAMGSGTAVAKSASDMVLADDNFATIVAAVE 738
P-type_ATPase_SPCA cd02085
golgi-associated secretory pathway Ca(2+) transport ATPases, similar to human ATPase secretory ...
 197-263 1.11e-04

golgi-associated secretory pathway Ca(2+) transport ATPases, similar to human ATPase secretory pathway Ca(2+) transporting 1/hSPCA1 and Saccharomyces cerevisiae Ca(2+)/Mn(2+)-transporting P-type ATPase, Pmr1p; SPCAs are Ca(2+) pumps important for the golgi-associated secretion pathway, in addition some function as Mn(2+) pumps in Mn(2+) detoxification. Saccharomyces cerevisiae Pmr1p is a high affinity Ca(2+)/Mn(2+) ATPase which transports Ca(2+) and Mn(2+) from the cytoplasm into the Golgi. Pmr1p also contributes to Cd(2+) detoxification. This subfamily includes human SPCA1 and SPCA2, encoded by the ATP2C1 and ATP2C2 genes; autosomal dominant Hailey-Hailey disease is caused by mutations in the human ATP2C1 gene. It also includes Strongylocentrotus purpuratus testis secretory pathway calcium transporting ATPase SPCA which plays an important role in fertilization. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319779 [Multi-domain]  Cd Length: 804  Bit Score: 43.16  E-value: 1.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1337424157 197 KSLQKLfdkieadfSEVIAF-GDSLNDSDMLEKAAIGVAMGNANYTI-KELADVVTDDHDNNGIVTALE 263
Cdd:cd02085   538 KALQKS--------GAVVAMtGDGVNDAVALKSADIGIAMGRTGTDVcKEAADMILVDDDFSTILAAIE 598
P-type_ATPase_Na-K_like cd02608
alpha-subunit of Na(+)/K(+)-ATPases and of gastric H(+)/K(+)-ATPase, similar to the human Na(+) ...
 217-263 1.21e-04

alpha-subunit of Na(+)/K(+)-ATPases and of gastric H(+)/K(+)-ATPase, similar to the human Na(+)/K(+)-ATPase alpha subunits 1-4; This subfamily includes the alpha subunit of Na(+)/K(+)-ATPase a heteromeric transmembrane protein composed of an alpha- and beta-subunit and an optional third subunit belonging to the FXYD proteins which are more tissue specific regulatory subunits of the enzyme. The alpha-subunit is the catalytic subunit responsible for transport activities of the enzyme. This subfamily includes all four isotopes of the human alpha subunit: (alpha1-alpha4, encoded by the ATP1A1- ATP1A4 genes). Na(+)/K(+)-ATPase functions chiefly as an ion pump, hydrolyzing one molecule of ATP to pump three Na(+) out of the cell in exchange for two K(+)entering the cell per pump cycle. In addition Na(+)/K(+)-ATPase acts as a signal transducer. This subfamily also includes Oreochromis mossambicus (tilapia) Na(+)/K(+)-ATPase alpha 1 and alpha 3 subunits, and gastric H(+)/K(+)-ATPase which exchanges hydronium ion with potassium and is responsible for gastric acid secretion. Gastric H(+)/K(+)-ATPase is an alpha,beta-heterodimeric enzyme. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319794 [Multi-domain]  Cd Length: 905  Bit Score: 43.11  E-value: 1.21e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1337424157 217 GDSLNDSDMLEKAAIGVAMGNANYTI-KELADVVTDDHDNNGIVTALE 263
Cdd:cd02608   601 GDGVNDSPALKKADIGVAMGIAGSDVsKQAADMILLDDNFASIVTGVE 648
ATPase-IIC_X-K TIGR01106
sodium or proton efflux -- potassium uptake antiporter, P-type ATPase, alpha subunit; This ...
 217-264 1.27e-04

sodium or proton efflux -- potassium uptake antiporter, P-type ATPase, alpha subunit; This model describes the P-type ATPases responsible for the exchange of either protons or sodium ions for potassium ions across the plasma membranes of eukaryotes. Unlike most other P-type ATPases, members of this subfamily require a beta subunit for activity. This model encompasses eukaryotes and consists of two functional types, a Na/K antiporter found widely distributed in eukaryotes and a H/K antiporter found only in vertebrates. The Na+ or H+/K+ antiporter P-type ATPases have been characterized as Type IIC based on a published phylogenetic analysis. Sequences from Blastocladiella emersonii (GP|6636502, GP|6636502 and PIR|T43025), C. elegans (GP|2315419, GP|6671808 and PIR|T31763) and Drosophila melanogaster (GP|7291424) score below trusted cutoff, apparently due to long branch length (excessive divergence from the last common ancestor) as evidenced by a phylogenetic tree. Experimental evidence is needed to determine whether these sequences represent ATPases with conserved function. Aside from fragments, other sequences between trusted and noise appear to be bacterial ATPases of unclear lineage, but most likely calcium pumps. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 273445 [Multi-domain]  Cd Length: 997  Bit Score: 43.24  E-value: 1.27e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1337424157 217 GDSLNDSDMLEKAAIGVAMGNANYTI-KELADVVTDDHDNNGIVTALEK 264
Cdd:TIGR01106 690 GDGVNDSPALKKADIGVAMGIAGSDVsKQAADMILLDDNFASIVTGVEE 738
ATPase-IB_hvy TIGR01525
heavy metal translocating P-type ATPase; This model encompasses two equivalog models for the ...
 205-264 1.68e-04

heavy metal translocating P-type ATPase; This model encompasses two equivalog models for the copper and cadmium-type heavy metal transporting P-type ATPases (TIGR01511 and TIGR01512) as well as those species which score ambiguously between both models. For more comments and references, see the files on TIGR01511 and 01512.


Pssm-ID: 273669 [Multi-domain]  Cd Length: 558  Bit Score: 42.62  E-value: 1.68e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157 205 KIEADFSEVIAFGDSLNDSDMLEKAAIGVAMGNANYTIKELADVVTDDHDNNGIVTALEK 264
Cdd:TIGR01525 445 KLQEEGGPVAMVGDGINDAPALAAADVGIAMGSGSDVAIEAADIVLLNDDLRSLPTAIDL 504
P-type_ATPase_cation cd02080
P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, ...
 212-263 2.32e-04

P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, and Synechocystis sp. PCC 6803 PMA1, a putative Ca(2+)-ATPase; This subfamily includes the P-type Na(+)-ATPase of an alkaliphilic bacterium Exiguobacterium aurantiacum Mna and cyanobacterium Synechocystis sp. PCC 6803 PMA1, a cation-transporting ATPase which may translocate calcium. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319775 [Multi-domain]  Cd Length: 819  Bit Score: 42.25  E-value: 2.32e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1337424157 212 EVIAF-GDSLNDSDMLEKAAIGVAMGNANYTI-KELADVVTDDHDNNGIVTALE 263
Cdd:cd02080   560 EVVAMtGDGVNDAPALKQADIGIAMGIKGTEVaKEAADMVLADDNFATIAAAVE 613
P-type_ATPase_Na_ENA cd02086
fungal-type Na(+)-ATPase, similar to the plasma membrane sodium transporters Saccharomyces ...
 217-263 3.80e-04

fungal-type Na(+)-ATPase, similar to the plasma membrane sodium transporters Saccharomyces cerevisiae Ena1p, Ena2p and Ustilago maydis Ena1, and the endoplasmic reticulum sodium transporter Ustilago maydis Ena2; Fungal-type Na(+)-ATPase (also called ENA ATPases). This subfamily includes the Saccharomyces cerevisiae plasma membrane transporters: Na(+)/Li(+)-exporting ATPase Ena1p which may also extrudes K(+), and Na(+)-exporting P-type ATPase Ena2p. It also includes Ustilago maydis plasma membrane Ena1, an K(+)/Na(+)-ATPase whose chief role is to pump Na(+) and K(+) out of the cytoplasm, especially at high pH values, and endoplasmic reticulum Ena2 ATPase which mediates Na(+) or K(+) fluxes in the ER or in other endomembranes. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319780 [Multi-domain]  Cd Length: 920  Bit Score: 41.67  E-value: 3.80e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1337424157 217 GDSLNDSDMLEKAAIGVAMG-NANYTIKELADVVTDDHDNNGIVTALE 263
Cdd:cd02086   628 GDGVNDSPSLKMADVGIAMGlNGSDVAKDASDIVLTDDNFASIVNAIE 675
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 194-238 4.91e-04

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: 40.71  E-value: 4.91e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1337424157 194 SKGKSLQKLFDKIEADFSEVIAFGDSLNDSDMLEKAAIGVAMGNA 238
Cdd:pfam05116 164 SKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTRGVVVGNA 208
ATPase-IID_K-Na TIGR01523
potassium and/or sodium efflux P-type ATPase, fungal-type; Initially described as a calcium ...
 217-264 7.08e-04

potassium and/or sodium efflux P-type ATPase, fungal-type; Initially described as a calcium efflux ATPase, more recent work has shown that the S. pombe CTA3 gene is in fact a potassium ion efflux pump. This model describes the clade of fungal P-type ATPases responsible for potassium and sodium efflux. The degree to which these pumps show preference for sodium or potassium varies. This group of ATPases has been classified by phylogentic analysis as type IID. The Leishmania sequence (GP|3192903), which falls between trusted and noise in this model, may very well turn out to be an active potassium pump.


Pssm-ID: 130586 [Multi-domain]  Cd Length: 1053  Bit Score: 40.77  E-value: 7.08e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1337424157  217 GDSLNDSDMLEKAAIGVAMG-NANYTIKELADVVTDDHDNNGIVTALEK 264
Cdd:TIGR01523  752 GDGVNDSPSLKMANVGIAMGiNGSDVAKDASDIVLSDDNFASILNAIEE 800
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 6-72 9.09e-04

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: 37.76  E-value: 9.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1337424157   6 IVMDMDDTLLTSEnkiseethayLLKK-QQEGMKIILASGRPTAGMTKHAESLNLKQNGGYIVSYNGA 72
Cdd:cd01427     2 VLFDLDGTLLAVE----------LLKRlRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGG 59
P-type_ATPases cd01431
ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, ...
 212-263 9.16e-04

ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids. They are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd(2+), and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine.


Pssm-ID: 319764 [Multi-domain]  Cd Length: 319  Bit Score: 40.13  E-value: 9.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1337424157 212 EVIAF-GDSLNDSDMLEKAAIGVAMGNANYTI-KELADVVTDDHDNNGIVTALE 263
Cdd:cd01431   207 EVVAMtGDGVNDAPALKQADVGIAMGSTGTDVaKEAADIVLLDDNFATIVEAVE 260
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 194-253 1.26e-03

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 39.54  E-value: 1.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1337424157 194 SKGKSLQKLFDKIEADFS-EVIAFGDSLNDSDMLEKAAIGVAMGNANYTIKELADVVTDDH 253
Cdd:PRK00192  190 DKGKAVRWLKELYRRQDGvETIALGDSPNDLPMLEAADIAVVVPGPDGPNPPLLPGIADGE 250
P-type_ATPase cd07538
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
 212-263 2.21e-03

uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase transporters of unknown function. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids. They are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd2+, and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine.


Pssm-ID: 319839 [Multi-domain]  Cd Length: 653  Bit Score: 39.35  E-value: 2.21e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1337424157 212 EVIAF-GDSLNDSDMLEKAAIGVAMGNANYTI-KELADVVTDDHDNNGIVTALE 263
Cdd:cd07538   506 EIVAMtGDGVNDAPALKAAHIGIAMGKRGTDVaREASDIVLLDDNFSSIVSTIR 559
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
 192-247 2.35e-03

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


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 38.66  E-value: 2.35e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1337424157 192 EVSKGKSLQKLFDKIEADFSE---VIAFGDSLNDSDMLEKAAIGVAMGNANYTIKELAD 247
Cdd:COG3769   186 GADKGKAVRWLVEQYRQRFGKnvvTIALGDSPNDIPMLEAADIAVVIRSPHGAPPELED 244
P-type_ATPase-Cd_Zn_Co_like cd07548
P-type heavy metal-transporting ATPase, similar to Bacillus subtilis CadA which appears to ...
 203-262 2.68e-03

P-type heavy metal-transporting ATPase, similar to Bacillus subtilis CadA which appears to transport cadmium, zinc and cobalt but not copper out of the cell; Bacillus subtilis CadA/YvgW appears to transport cadmium, zinc and cobalt but not copper, out of the cell. Functions in metal ion resistance and cellular metal ion homeostasis. CadA/YvgW is also important for sporulation in B. subtilis, the significant specific expression of the cadA/yvgW gene during the late stage of sporulation, is controlled by forespore-specific sigma factor, sigma G, and mother cell-specific sigma factor, sigma E. This subfamily also includes Helicobacter pylori CadA an essential resistance pump with ion specificity towards Cd(2+), Zn(2+) and Co(2+), and Zn-transporting ATPase, ZiaA(N) in Synechocystis PCC 6803. Transcription of ziaA is induced by Zn under the control of the Zn responsive repressor ZiaR. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319847 [Multi-domain]  Cd Length: 604  Bit Score: 38.76  E-value: 2.68e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1337424157 203 FDKIEADFSEVIAF-GDSLNDSDMLEKAAIGVAMGN-ANYTIKELADVVTDDHDNNGIVTAL 262
Cdd:cd07548   485 VEELKAESKGKVAFvGDGINDAPVLARADVGIAMGGlGSDAAIEAADVVLMNDEPSKVAEAI 546
PRK14501 PRK14501
putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional
 186-248 4.18e-03

putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional


Pssm-ID: 184712 [Multi-domain]  Cd Length: 726  Bit Score: 38.37  E-value: 4.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337424157 186 LEFMNNEVSKGKSLQKLFDKIEADFseVIAFGDSLNDSDM---LEKAAIGVAMGN----ANYTIKELADV 248
Cdd:PRK14501  649 VEVRPAGVNKGRAVRRLLEAGPYDF--VLAIGDDTTDEDMfraLPETAITVKVGPgesrARYRLPSQREV 716
COG4087 COG4087
Soluble P-type ATPase [General function prediction only];
211-268 4.24e-03

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


Pssm-ID: 443263 [Multi-domain]  Cd Length: 156  Bit Score: 37.06  E-value: 4.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1337424157 211 SEVIAFGDSLNDSDMLEKAAIGVA-MGNANYTIKEL--ADVVTddhdnNGIVTALEKLLKS 268
Cdd:COG4087    92 ETTVAIGNGRNDVLMLKEAALGIAvIGPEGASVKALlaADIVV-----KSILDALDLLLNP 147
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 194-234 4.82e-03

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: 37.14  E-value: 4.82e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1337424157 194 SKGKSLQKLFDKIEADFSEVIAFGDSLNDSDMLEKAAIGVA 234
Cdd:cd07500   137 RKAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIA 177
 
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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