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Conserved domains on  [gi|544824578|ref|WP_021240580|]
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MULTISPECIES: phosphoserine phosphatase [Enterobacter]

Protein Classification

phosphoserine phosphatase SerB( domain architecture ID 11485219)

phosphoserine phosphatase SerB is a HAD (haloacid dehalogenase) family hydrolase that catalyzes the dephosphorylation of phosphoserine (P-Ser); also catalyzes the hydrolysis of phosphothreonine (P-Thr)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
serB PRK11133
phosphoserine phosphatase; Provisional
 1-322 0e+00

phosphoserine phosphatase; Provisional


:

Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 655.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578   1 MPNITWCDLPTDVSLWPGLPLSLSGDEVMPLDYHAGRSGWLLYGRGLDKQRLTQYQTKLGAAMVIVAAWCVEDYQVIRLA 80
Cdd:PRK11133   1 MNNLTWCDLPEDVSLWPGLPLSLSGDEVMPLDYRAGRSGWLLYGRGLDKQRLTDFQRKLGAAMVIVAAWCVEDYQVVRLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578  81 GSLTQRATRLAHDAGLDVAPLGKIPHLKTPGLLVMDMDSTAIQIECIDEIAKLAGSGELVAEVTERAMRGELDFTASLRQ 160
Cdd:PRK11133  81 GSLTPRATRLAHELGLDVAPLGKIPHLRTPGLLVMDMDSTAIQIECIDEIAKLAGTGEEVAEVTERAMRGELDFEASLRQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 161 RVATLKGADANILRQVRDELPLMPGLTQLVLKLQSLGWKVAIASGGFTFFADYLREKLHLTTVVANELEIMDGKLTGQVI 240
Cdd:PRK11133 161 RVATLKGADANILQQVRENLPLMPGLTELVLKLQALGWKVAIASGGFTYFADYLRDKLRLDAAVANELEIMDGKLTGNVL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 241 GDIVDAQYKANTLTRLAEKYEIPVVQTVAIGDGANDLPMIKAAGLGIAYHAKPKVNEKTEVTIRHADLMGVFCILSGSLN 320
Cdd:PRK11133 241 GDIVDAQYKADTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAGLGIAYHAKPKVNEQAQVTIRHADLMGVLCILSGSLK 320


                 ..
gi 544824578 321 QK 322
Cdd:PRK11133 321 HK 322
 
Name Accession Description Interval E-value
serB PRK11133
phosphoserine phosphatase; Provisional
 1-322 0e+00

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 655.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578   1 MPNITWCDLPTDVSLWPGLPLSLSGDEVMPLDYHAGRSGWLLYGRGLDKQRLTQYQTKLGAAMVIVAAWCVEDYQVIRLA 80
Cdd:PRK11133   1 MNNLTWCDLPEDVSLWPGLPLSLSGDEVMPLDYRAGRSGWLLYGRGLDKQRLTDFQRKLGAAMVIVAAWCVEDYQVVRLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578  81 GSLTQRATRLAHDAGLDVAPLGKIPHLKTPGLLVMDMDSTAIQIECIDEIAKLAGSGELVAEVTERAMRGELDFTASLRQ 160
Cdd:PRK11133  81 GSLTPRATRLAHELGLDVAPLGKIPHLRTPGLLVMDMDSTAIQIECIDEIAKLAGTGEEVAEVTERAMRGELDFEASLRQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 161 RVATLKGADANILRQVRDELPLMPGLTQLVLKLQSLGWKVAIASGGFTFFADYLREKLHLTTVVANELEIMDGKLTGQVI 240
Cdd:PRK11133 161 RVATLKGADANILQQVRENLPLMPGLTELVLKLQALGWKVAIASGGFTYFADYLRDKLRLDAAVANELEIMDGKLTGNVL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 241 GDIVDAQYKANTLTRLAEKYEIPVVQTVAIGDGANDLPMIKAAGLGIAYHAKPKVNEKTEVTIRHADLMGVFCILSGSLN 320
Cdd:PRK11133 241 GDIVDAQYKADTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAGLGIAYHAKPKVNEQAQVTIRHADLMGVLCILSGSLK 320


                 ..
gi 544824578 321 QK 322
Cdd:PRK11133 321 HK 322
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 97-315 3.54e-118

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: 339.33  E-value: 3.54e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578   97 DVAPLGKIPHLKTPGLLVMDMDSTAIQIECIDEIAKLAGSGELVAEVTERAMRGELDFTASLRQRVATLKGADANILRQV 176
Cdd:TIGR00338   1 DIAHSELSPLLRSKKLVVFDMDSTLINAETIDEIAKIAGVEEEVSEITERAMRGELDFKASLRERVALLKGLPVELLKEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578  177 RDELPLMPGLTQLVLKLQSLGWKVAIASGGFTFFADYLREKLHLTTVVANELEIMDGKLTGQVIGDIVDAQYKANTLTRL 256
Cdd:TIGR00338  81 RENLPLTEGAEELVKTLKEKGYKVAVISGGFDLFAEHVKDKLGLDAAFANRLEVEDGKLTGLVEGPIVDASYKGKTLLIL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 544824578  257 AEKYEIPVVQTVAIGDGANDLPMIKAAGLGIAYHAKPKVNEKTEVTIRHADLMGVFCIL 315
Cdd:TIGR00338 161 LRKEGISPENTVAVGDGANDLSMIKAAGLGIAFNAKPKLQQKADICINKKDLTDILPLL 219
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 112-291 2.38e-95

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: 279.82  E-value: 2.38e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 112 LLVMDMDSTAIQIECIDEIAKLAGSGELVAEVTERAMRGELDFTASLRQRVATLKGADANILRQVRDELPLMPGLTQLVL 191
Cdd:cd07500    1 LIVFDMDSTLIQQEVIDELAAEAGVGEEVAAITERAMRGELDFEESLRERVALLKGLPESVLDEVYERLTLTPGAEELIQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 192 KLQSLGWKVAIASGGFTFFADYLREKLHLTTVVANELEIMDGKLTGQVIGDIVDAQYKANTLTRLAEKYEIPVVQTVAIG 271
Cdd:cd07500   81 TLKAKGYKTAVVSGGFTYFTDRLAEELGLDYAFANELEIKDGKLTGKVLGPIVDAQRKAETLQELAARLGIPLEQTVAVG 160

                        170       180
                 ....*....|....*....|
gi 544824578 272 DGANDLPMIKAAGLGIAYHA 291
Cdd:cd07500  161 DGANDLPMLKAAGLGIAFHA 180
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 110-298 5.73e-75

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: 229.72  E-value: 5.73e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 110 PGLLVMDMDSTAIQIECIDEIAKLAGS---------GELVAEVTERAMRGELDFTASLRQRVATLKGADANILRQVRDEL 180
Cdd:COG0560    3 MRLAVFDLDGTLIAGESIDELARFLGRrglvdrrevLEEVAAITERAMAGELDFEESLRFRVALLAGLPEEELEELAERL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 181 -----PLMPGLTQLVLKLQSLGWKVAIASGGFTFFADYLREKLHLTTVVANELEIMDGKLTGQVIGDIVDAQYKANTLTR 255
Cdd:COG0560   83 feevpRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDGRLTGEVVGPIVDGEGKAEALRE 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 544824578 256 LAEKYEIPVVQTVAIGDGANDLPMIKAAGLGIAYHAKPKVNEK 298
Cdd:COG0560  163 LAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREA 205
DUF5609 pfam18429
Domain of unknown function (DUF5609); This is a probable HAD-like (haloalkanoate dehalogenase) ...
 36-100 2.06e-24

Domain of unknown function (DUF5609); This is a probable HAD-like (haloalkanoate dehalogenase) domain found in bacterial phosphoserine phosphatases.


Pssm-ID: 436496  Cd Length: 65  Bit Score: 93.92  E-value: 2.06e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544824578   36 GRSGWLLYGRGLDKQRLTQYQTKLGAAMVIVAAWCVEDYQVIRLAGSLTQRATRLAHDAGLDVAP 100
Cdd:pfam18429   1 GKTGWLVYGRGLTKLRLDQIQQKLGEALVIVAAWKVGEYDVLLLRGELTDALETAAHALKLDCAD 65
 
Name Accession Description Interval E-value
serB PRK11133
phosphoserine phosphatase; Provisional
 1-322 0e+00

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 655.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578   1 MPNITWCDLPTDVSLWPGLPLSLSGDEVMPLDYHAGRSGWLLYGRGLDKQRLTQYQTKLGAAMVIVAAWCVEDYQVIRLA 80
Cdd:PRK11133   1 MNNLTWCDLPEDVSLWPGLPLSLSGDEVMPLDYRAGRSGWLLYGRGLDKQRLTDFQRKLGAAMVIVAAWCVEDYQVVRLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578  81 GSLTQRATRLAHDAGLDVAPLGKIPHLKTPGLLVMDMDSTAIQIECIDEIAKLAGSGELVAEVTERAMRGELDFTASLRQ 160
Cdd:PRK11133  81 GSLTPRATRLAHELGLDVAPLGKIPHLRTPGLLVMDMDSTAIQIECIDEIAKLAGTGEEVAEVTERAMRGELDFEASLRQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 161 RVATLKGADANILRQVRDELPLMPGLTQLVLKLQSLGWKVAIASGGFTFFADYLREKLHLTTVVANELEIMDGKLTGQVI 240
Cdd:PRK11133 161 RVATLKGADANILQQVRENLPLMPGLTELVLKLQALGWKVAIASGGFTYFADYLRDKLRLDAAVANELEIMDGKLTGNVL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 241 GDIVDAQYKANTLTRLAEKYEIPVVQTVAIGDGANDLPMIKAAGLGIAYHAKPKVNEKTEVTIRHADLMGVFCILSGSLN 320
Cdd:PRK11133 241 GDIVDAQYKADTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAGLGIAYHAKPKVNEQAQVTIRHADLMGVLCILSGSLK 320


                 ..
gi 544824578 321 QK 322
Cdd:PRK11133 321 HK 322
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 97-315 3.54e-118

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: 339.33  E-value: 3.54e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578   97 DVAPLGKIPHLKTPGLLVMDMDSTAIQIECIDEIAKLAGSGELVAEVTERAMRGELDFTASLRQRVATLKGADANILRQV 176
Cdd:TIGR00338   1 DIAHSELSPLLRSKKLVVFDMDSTLINAETIDEIAKIAGVEEEVSEITERAMRGELDFKASLRERVALLKGLPVELLKEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578  177 RDELPLMPGLTQLVLKLQSLGWKVAIASGGFTFFADYLREKLHLTTVVANELEIMDGKLTGQVIGDIVDAQYKANTLTRL 256
Cdd:TIGR00338  81 RENLPLTEGAEELVKTLKEKGYKVAVISGGFDLFAEHVKDKLGLDAAFANRLEVEDGKLTGLVEGPIVDASYKGKTLLIL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 544824578  257 AEKYEIPVVQTVAIGDGANDLPMIKAAGLGIAYHAKPKVNEKTEVTIRHADLMGVFCIL 315
Cdd:TIGR00338 161 LRKEGISPENTVAVGDGANDLSMIKAAGLGIAFNAKPKLQQKADICINKKDLTDILPLL 219
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 112-291 2.38e-95

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: 279.82  E-value: 2.38e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 112 LLVMDMDSTAIQIECIDEIAKLAGSGELVAEVTERAMRGELDFTASLRQRVATLKGADANILRQVRDELPLMPGLTQLVL 191
Cdd:cd07500    1 LIVFDMDSTLIQQEVIDELAAEAGVGEEVAAITERAMRGELDFEESLRERVALLKGLPESVLDEVYERLTLTPGAEELIQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 192 KLQSLGWKVAIASGGFTFFADYLREKLHLTTVVANELEIMDGKLTGQVIGDIVDAQYKANTLTRLAEKYEIPVVQTVAIG 271
Cdd:cd07500   81 TLKAKGYKTAVVSGGFTYFTDRLAEELGLDYAFANELEIKDGKLTGKVLGPIVDAQRKAETLQELAARLGIPLEQTVAVG 160

                        170       180
                 ....*....|....*....|
gi 544824578 272 DGANDLPMIKAAGLGIAYHA 291
Cdd:cd07500  161 DGANDLPMLKAAGLGIAFHA 180
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 110-298 5.73e-75

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: 229.72  E-value: 5.73e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 110 PGLLVMDMDSTAIQIECIDEIAKLAGS---------GELVAEVTERAMRGELDFTASLRQRVATLKGADANILRQVRDEL 180
Cdd:COG0560    3 MRLAVFDLDGTLIAGESIDELARFLGRrglvdrrevLEEVAAITERAMAGELDFEESLRFRVALLAGLPEEELEELAERL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 181 -----PLMPGLTQLVLKLQSLGWKVAIASGGFTFFADYLREKLHLTTVVANELEIMDGKLTGQVIGDIVDAQYKANTLTR 255
Cdd:COG0560   83 feevpRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDGRLTGEVVGPIVDGEGKAEALRE 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 544824578 256 LAEKYEIPVVQTVAIGDGANDLPMIKAAGLGIAYHAKPKVNEK 298
Cdd:COG0560  163 LAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREA 205
DUF5609 pfam18429
Domain of unknown function (DUF5609); This is a probable HAD-like (haloalkanoate dehalogenase) ...
 36-100 2.06e-24

Domain of unknown function (DUF5609); This is a probable HAD-like (haloalkanoate dehalogenase) domain found in bacterial phosphoserine phosphatases.


Pssm-ID: 436496  Cd Length: 65  Bit Score: 93.92  E-value: 2.06e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544824578   36 GRSGWLLYGRGLDKQRLTQYQTKLGAAMVIVAAWCVEDYQVIRLAGSLTQRATRLAHDAGLDVAP 100
Cdd:pfam18429   1 GKTGWLVYGRGLTKLRLDQIQQKLGEALVIVAAWKVGEYDVLLLRGELTDALETAAHALKLDCAD 65
HAD_PSP_eu cd04309
phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human ...
 116-289 2.28e-24

phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human PSP, EC 3.1.3.3, catalyzes the third and final of the L-serine biosynthesis pathway, the Mg2+-dependent hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, L-serine is a precursor for the biosynthesis of glycine. HPSP regulates the levels of glycine and D-serine (converted from L-serine), the putative co-agonists for the glycine site of the NMDA receptor in the brain. Plant 3-PSP catalyzes the conversion of 3-phosphoserine to serine in the last step of the plastidic pathway of serine biosynthesis. 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: 319801 [Multi-domain]  Cd Length: 202  Bit Score: 98.12  E-value: 2.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 116 DMDSTAIQIECIDEIAKLAGSGELVAEVTERAMRGELDFTASLRQRVATLKGADANIlRQVRDELP--LMPGLTQLVLKL 193
Cdd:cd04309    6 DVDSTVIQEEGIDELAKFCGVGDEVAELTRRAMGGSIPFRDALRKRLAIINPTKEQV-DEFLEEHPprLTPGVEELVSRL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 194 QSLGWKVAIASGGF----TFFADYLreKLHLTTVVANELeIMDGK----------LTGQVIGdivdaqyKANTLTRLAEK 259
Cdd:cd04309   85 KARGVEVYLISGGFreliEPVASQL--GIPLENVFANRL-LFDFNgeyagfdetqPTSRSGG-------KAKVIEQLKEK 154

                        170       180       190
                 ....*....|....*....|....*....|
gi 544824578 260 YEIPVVqtVAIGDGANDLPMIKAAGLGIAY 289
Cdd:cd04309  155 HHYKRV--IMIGDGATDLEACPPADAFIGF 182
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 112-283 5.84e-23

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: 93.57  E-value: 5.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578  112 LLVMDMDSTAIQIECIDEI-AKLAGSGELVAEVTERAMRGELDFTASLRQRVATLKGADANILRQ--VRDELPLMPGLTQ 188
Cdd:TIGR01488   1 LAIFDFDGTLTRQDSLIDLlAKLLGTNDEVIELTRLAPSGRISFEDALGRRLALLHRSRSEEVAKefLARQVALRPGARE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578  189 LVLKLQSLGWKVAIASGGFTFFADYLREKLHLTTVVANELEIMD-GKLTGQVIG-DIVDAQYKANTLTRLAEKYEIPVVQ 266
Cdd:TIGR01488  81 LISWLKERGIDTVIVSGGFDFFVEPVAEKLGIDDVFANRLEFDDnGLLTGPIEGqVNPEGECKGKVLKELLEESKITLKK 160

                         170
                  ....*....|....*..
gi 544824578  267 TVAIGDGANDLPMIKAA 283
Cdd:TIGR01488 161 IIAVGDSVNDLPMLKLA 177
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 112-284 5.42e-16

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


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 74.93  E-value: 5.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578  112 LLVMDMDSTAIQI-----ECIDE-----------IAKLAGSGELVAEVTERAMRGELDFTASL---RQRVATLKGADANI 172
Cdd:pfam00702   3 AVVFDLDGTLTDGepvvtEAIAElasehplakaiVAAAEDLPIPVEDFTARLLLGKRDWLEELdilRGLVETLEAEGLTV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578  173 LRQ-------VRDELPLMPGLTQLVLKLQSLGWKVAIASGGFTFFADYLREKLHLTTVVANeleimdgkltgqVIGDIVD 245
Cdd:pfam00702  83 VLVellgviaLADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDV------------VISGDDV 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 544824578  246 AQYKANT--LTRLAEKYEIPVVQTVAIGDGANDLPMIKAAG 284
Cdd:pfam00702 151 GVGKPKPeiYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD pfam12710
haloacid dehalogenase-like hydrolase;
113-281 9.83e-16

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 74.11  E-value: 9.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578  113 LVMDMDSTAIQIECIDEIAK-LAGSGELVAEVTERA--------MRGELDFTASLRQRVATLKGADANILRQVRDELP-- 181
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRaLLRRGGPDLWRALLVllllallrLLGRLSRAGARELLRALLAGLPEEDAAELERFVAev 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578  182 ----LMPGLTQLVLKLQSLGWKVAIASGGFTFFADYLREKLHLTTVVANELEIMDGKLTGQV--IGDIVDAQYKANTLTR 255
Cdd:pfam12710  81 alprLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATELEVDDGRFTGELrlIGPPCAGEGKVRRLRA 160

                         170       180
                  ....*....|....*....|....*...
gi 544824578  256 L--AEKYEIPVVQTVAIGDGANDLPMIK 281
Cdd:pfam12710 161 WlaARGLGLDLADSVAYGDSPSDLPMLR 188
PLN02954 PLN02954
phosphoserine phosphatase
 116-277 2.24e-15

phosphoserine phosphatase


Pssm-ID: 215514 [Multi-domain]  Cd Length: 224  Bit Score: 73.96  E-value: 2.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 116 DMDSTAIQIECIDEIAKLAGSGELVAEVTERAMRGELDFTASLRQRVATLKGADANILRQVRDELP-LMPGLTQLVLKLQ 194
Cdd:PLN02954  18 DVDSTVCVDEGIDELAEFCGAGEAVAEWTAKAMGGSVPFEEALAARLSLFKPSLSQVEEFLEKRPPrLSPGIPELVKKLR 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 195 SLGWKVAIASGGFTFFADYLREKLHL--TTVVANELEI-MDGKLTGqvigdiVDA-------QYKANTLTRLAEKYEIPV 264
Cdd:PLN02954  98 ARGTDVYLVSGGFRQMIAPVAAILGIppENIFANQILFgDSGEYAG------FDEneptsrsGGKAEAVQHIKKKHGYKT 171

                        170
                 ....*....|...
gi 544824578 265 VqtVAIGDGANDL 277
Cdd:PLN02954 172 M--VMIGDGATDL 182
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 112-284 1.25e-14

HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences modelled here are all bacterial. The IB subfamily includes the enzyme phosphoserine phosphatase (TIGR00338). Due to this relationship, several of these sequences have been annotated as "phosphoserine phosphatase related proteins," or "Phosphoserine phosphatase-family enzymes." There is presently no evidence that any of the enzymes in this model possess PSPase activity. OMNI|NTL01ML1250 is annotated as a "possible transferase," however this is due to the C-terminal domain found on this sequence which is homologous to a group of glycerol-phosphate acyltransferases (between trusted and noise to TIGR00530). A subset of these sequences including OMNI|CC1962, the Caulobacter crescentus CicA protein cluster together and may represent a separate equivalog. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273654 [Multi-domain]  Cd Length: 202  Bit Score: 71.22  E-value: 1.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578  112 LLVMDMDSTAIQIECIDEIAKLAGS------GELVAEVTERAM----RGELDFTASLRQRVATLKGADANILRQVRDEL- 180
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLASknilfeELRLPKVLARFEfflnRGLDYMAYYRAFALDALAGLLEEDVRAIVEEFv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578  181 -----PLM-PGLTQLVLKLQSLGWKVAIASGGFTFFADYLREKLHLTTVVANELEIM-DGKLTGQVIGDIVDAQYKANTL 253
Cdd:TIGR01490  81 nqkieSILyPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTRLEESeDGIYTGNIDGNNCKGEGKVHAL 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 544824578  254 TRLAEKYEIPVVQTVAIGDGANDLPMIKAAG 284
Cdd:TIGR01490 161 AELLAEEQIDLKDSYAYGDSISDLPLLSLVG 191
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 249-288 2.16e-11

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: 63.00  E-value: 2.16e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 544824578 249 KANTLTRLAEKYEIPVVQTVAIGDGANDLPMIKAAGLGIA 288
Cdd:cd07516  184 KGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVA 223
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 144-284 8.97e-11

phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). 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: 319796 [Multi-domain]  Cd Length: 195  Bit Score: 60.40  E-value: 8.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 144 TERAMRGELDF-TASLRQRVATL--KGADANILRQVRDElplmpglTQLVLK-LQSLGWKVAIASGGFTFFADYLREKLH 219
Cdd:cd02612   50 DGAGMEALLGFaTAGLAGELAALveEFVEEYILRVLYPE-------ARELIAwHKAAGHDVVLISASPEELVAPIARKLG 122

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544824578 220 LTTVVANELEIMDGKLTGQVIGDIVDAQYKANTLTRLAEKYEIPVVQTVAIGDGANDLPMIKAAG 284
Cdd:cd02612  123 IDNVLGTQLETEDGRYTGRIIGPPCYGEGKVKRLREWLAEEGIDLKDSYAYSDSINDLPMLEAVG 187
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 249-288 9.23e-11

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 61.10  E-value: 9.23e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 544824578  249 KANTLTRLAEKYEIPVVQTVAIGDGANDLPMIKAAGLGIA 288
Cdd:pfam08282 188 KGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVA 227
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 249-288 9.97e-11

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: 60.15  E-value: 9.97e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 544824578 249 KANTLTRLAEKYEIPVVQTVAIGDGANDLPMIKAAGLGIA 288
Cdd:COG0561  122 KGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVA 161
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 249-311 3.38e-10

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: 59.59  E-value: 3.38e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544824578  249 KANTLTRLAEKYEIPVVQTVAIGDGANDLPMIKAAGLGIAYH-AKPKVNEKTEVTIRHADLMGV 311
Cdd:TIGR00099 189 KGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGnADEELKALADYVTDSNNEDGV 252
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 242-298 2.03e-07

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: 50.68  E-value: 2.03e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 544824578 242 DIVDAQY-KANTLTRLAEKYEIPVVQTVAIGDGANDLPMIKAAGLGIAY-HAKPKVNEK 298
Cdd:cd07517  134 DVIPKGGsKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMgNAHEELKEI 192
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 188-289 2.66e-07

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: 48.16  E-value: 2.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 188 QLVLKLQSLGWKVAIASGGFTFFADYLREKLHLTtvvanelEIMDGKLTGqviGDIVDAQYKANTLTRLAEKYEIPVVQT 267
Cdd:cd01427   14 ELLKRLRAAGIKLAIVTNRSREALRALLEKLGLG-------DLFDGIIGS---DGGGTPKPKPKPLLLLLLKLGVDPEEV 83

                         90       100
                 ....*....|....*....|...
gi 544824578 268 VAIGDGANDLPMIKAAG-LGIAY 289
Cdd:cd01427   84 LFVGDSENDIEAARAAGgRTVAV 106
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 249-288 4.39e-07

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: 48.35  E-value: 4.39e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 544824578 249 KANTLTRLAEKYEIPVVQTVAIGDGANDLPMIKAAGLGIA 288
Cdd:cd07514   68 KGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVA 107
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 249-315 1.73e-06

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: 47.58  E-value: 1.73e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544824578 249 KANTLTRLAEKYEIPVVQTVAIGDGANDLPMIKAAGLGIAY-HAKPKVNEKTEVTIRHADLMGVFCIL 315
Cdd:cd07518  116 KATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMeNAPEEVKAAAKYVAPSNNENGVLQVI 183
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 242-288 1.85e-06

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 48.05  E-value: 1.85e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 544824578 242 DIVDAQY----------KANTLTRLAEKYEIPVVQTVAIGDGANDLPMIKAAGLGIA 288
Cdd:PRK01158 141 EIVDSGFaihikspgvnKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVA 197
thrH PRK13582
bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;
123-295 2.01e-06

bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;


Pssm-ID: 237437 [Multi-domain]  Cd Length: 205  Bit Score: 47.61  E-value: 2.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 123 QIECID-----------EIAKLAGSGELvaevtERAMRGELDFTASLRQRVATLK--GADANILRQVRDELPLMPGLTQL 189
Cdd:PRK13582   2 EIVCLDlegvlvpeiwiAFAEKTGIPEL-----RATTRDIPDYDVLMKQRLDILDehGLGLADIQEVIATLDPLPGAVEF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 190 VLKLQSLGwKVAIASGGFTFFADYLREKLHLTTVVANELEIM-DGKLTGQvigDIVDAQYKANTLTRLAEKYeipvVQTV 268
Cdd:PRK13582  77 LDWLRERF-QVVILSDTFYEFAGPLMRQLGWPTLFCHSLEVDeDGMITGY---DLRQPDGKRQAVKALKSLG----YRVI 148

                        170       180
                 ....*....|....*....|....*..
gi 544824578 269 AIGDGANDLPMIKAAGLGIAYHAKPKV 295
Cdd:PRK13582 149 AAGDSYNDTTMLGEADAGILFRPPANV 175
COG4087 COG4087
Soluble P-type ATPase [General function prediction only];
224-288 2.71e-05

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


Pssm-ID: 443263 [Multi-domain]  Cd Length: 156  Bit Score: 43.61  E-value: 2.71e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544824578 224 VANELEIMDGKLtgQVIGDIVDAQYKANTLTRLAEKyeipvvQTVAIGDGANDLPMIKAAGLGIA 288
Cdd:COG4087   59 VAKELAGLPVEL--HILPSGDQAEEKLEFVEKLGAE------TTVAIGNGRNDVLMLKEAALGIA 115
P-type_ATPase_APLT_Dnf-like cd02073
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
 267-288 6.65e-05

Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2, -10D, -11B, -11C; Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. Yeast Dnf1 and Dnf2 mediate the transport of phosphatidylethanolamine, phosphatidylserine, and phosphatidylcholine from the outer to the inner leaflet of the plasma membrane. This subfamily includes mammalian flippases such as ATP11C which may selectively transports PS and PE from the outer leaflet of the plasma membrane to the inner leaflet. It also includes Arabidopsis phospholipid flippases including ALA1, and Caenorhabditis elegans flippases, including TAT-1, the latter has been shown to facilitate the inward transport of phosphatidylserine. 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: 319770 [Multi-domain]  Cd Length: 836  Bit Score: 44.47  E-value: 6.65e-05
                         10        20
                 ....*....|....*....|....
gi 544824578 267 TVAIGDGANDLPMIKAA--GLGIA 288
Cdd:cd02073  673 TLAIGDGANDVSMIQEAhvGVGIS 696
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 249-300 1.10e-04

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 43.01  E-value: 1.10e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 544824578 249 KANTLTRLAEKYEIP-VVQTVAIGDGANDLPMIKAAGLGI----AYHAKPKVNEKTE 300
Cdd:PRK00192 191 KGKAVRWLKELYRRQdGVETIALGDSPNDLPMLEAADIAVvvpgPDGPNPPLLPGIA 247
HAD_ThrH_like cd02607
bifunctional phosphoserine phosphatase/phosphoserine:homoserine phosphotransferase, similar to ...
 130-291 2.60e-04

bifunctional phosphoserine phosphatase/phosphoserine:homoserine phosphotransferase, similar to Pseudomonas aeruginosa ThrH; This family includes Pseudomonas aeruginosa ThrH which is a duel activity enzyme having both phosphoserine phosphatase and phosphoserine:homoserine phosphotransferase activities, i.e. it can dephosphorylate phosphoserine, and can transfer phosphate from phosphoserine to homoserine. 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: 319793 [Multi-domain]  Cd Length: 195  Bit Score: 41.49  E-value: 2.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 130 IAKLAGSGELVAevTERAMRgelDFTASLRQRVATLK--GADANILRQVRDELPLMPGLTQLVLKLQSLGwKVAIASGGF 207
Cdd:cd02607   20 FAEKTGIDALKA--TTRDIP---DYDVLMKQRLRILDehGLKLADIQEVIATLKPLEGAVEFVDWLRERF-QVVILSDTF 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 208 TFFADYLREKLHLTTVVANELEIMDGKLTGqviGDIVDaQYKANTLTRLAEKYEIPVVqtVAIGDGANDLPMIKAAGLGI 287
Cdd:cd02607   94 YEFSQPLMRQLGFPTLLCHKLQTDDDDRVV---GYQLR-QKDPKRQSVIAVKSLYYRV--IAAGDSYNDTTMLSEAHAGI 167


                 ....
gi 544824578 288 AYHA 291
Cdd:cd02607  168 LFHA 171
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 228-297 4.29e-04

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 41.22  E-value: 4.29e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544824578 228 LEIMDGKLTgqvigdivdaqyKANTLTRLAEKYEIPVVQTVAIGDGANDLPMIKAAGLGIAY-HAKPKVNE 297
Cdd:PRK10513 188 LEILDKRVN------------KGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYAGVGVAMgNAIPSVKE 246
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
 249-310 1.02e-03

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


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 40.20  E-value: 1.02e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544824578 249 KANTLTRLAEKYEIPV---VQTVAIGDGANDLPMIKAAGLGI----AYHAKPKVNEKTEVtiRHADLMG 310
Cdd:COG3769  189 KGKAVRWLVEQYRQRFgknVVTIALGDSPNDIPMLEAADIAVvirsPHGAPPELEDKPRV--IRTPAPG 255
HAD_Pase cd07524
phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like ...
 116-288 1.23e-03

phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like superfamily; Bacillus subtilis recycles two toxic byproducts of polyamine metabolism, methylthioadenosine and methylthioribose, into methionine by a salvage pathway. The sixth reaction in this pathway is catalyzed by B. subtilis MtnX: the dephosphorylation of 2- hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HKMTP- 1-P) into 1,2-dihydroxy-3-keto-5-methylthiopentene. The hydrolysis of HK-MTP-1-P is a two-step mechanism involving the formation of a transiently phosphorylated aspartyl intermediate. 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: 319826 [Multi-domain]  Cd Length: 211  Bit Score: 39.62  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 116 DMDSTAIQIECIDEIAKLAGSGElvaEVTERAMRGELDFTASLRQRVATLKGA-----DANILRQVRDELPLMPGLTQLV 190
Cdd:cd07524    5 DFDGTITENDNIIYLMDEFAPPL---EEWEALKEGVLSQTLSFREGVGQMFELlpsslKDEIIEFLEKTAKIRPGFKEFV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 191 LKLQSLGWKVAIASGGFTFFADYLREKL--HLTTVVANELEIMDGKLTGQVIGDIVDAQYKANTLTRLAEKYEIPVVQTV 268
Cdd:cd07524   82 AFCQEHGIPFIIVSGGMDFFIEPLLEGLviEKIAIYCNGSDFSGEQIHIDWPHECDCTNGCGCCKSSIIRKYSKPRPFII 161

                        170       180
                 ....*....|....*....|
gi 544824578 269 AIGDGANDLPMIKAAGLGIA 288
Cdd:cd07524  162 VIGDSVTDLEAAKEADLVFA 181
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 249-288 1.28e-03

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: 39.29  E-value: 1.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 544824578  249 KANTLTRLAEKYEIPVVQTVAIGDGANDLPMIKAAGLGIA 288
Cdd:TIGR01484 167 KGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVA 206
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 127-288 1.43e-03

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: 39.37  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578  127 IDEIAKLAG-SGELVAEVTeramrGELDFTASLRQRVATL--KGADANILRQVRDELPLmpgltqlvLKLQSLG----WK 199
Cdd:TIGR01482  45 ARALAKLIGtPDPVIAENG-----GEISYNEGLDDIFLAYleEEWFLDIVIAKTFPFSR--------LKVQYPRraslVK 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578  200 VaiasgGFTFFADYLREklhlttvVANELEIM-DGKLTGQVIgDIVDAQY-KANTLTRLAEKYEIPVVQTVAIGDGANDL 277
Cdd:TIGR01482 112 M-----RYGIDVDTVRE-------IIKELGLNlVAVDSGFDI-HILPQGVnKGVAVKKLKEKLGIKPGETLVCGDSENDI 178

                         170
                  ....*....|.
gi 544824578  278 PMIKAAGLGIA 288
Cdd:TIGR01482 179 DLFEVPGFGVA 189
P-type_ATPases cd01431
ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, ...
 181-288 1.55e-03

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: 39.74  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824578 181 PLMPGLTQLVLKLQSLGWKVAIASGGFTFFADYLREKLHLTTVVANELEIMDGKLTGQVigDIVDAQYKANTLTRLAEKY 260
Cdd:cd01431  117 PPRPEVKEAIAKCRTAGIKVVMITGDNPLTAIAIAREIGIDTKASGVILGEEADEMSEE--ELLDLIAKVAVFARVTPEQ 194

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 544824578 261 EIPVVQ-------TVA-IGDGANDLPMIKAAGLGIA 288
Cdd:cd01431  195 KLRIVKalqargeVVAmTGDGVNDAPALKQADVGIA 230
ATPase-Plipid TIGR01652
phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase ...
 267-288 2.11e-03

phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase responsible for transporting phospholipids from one leaflet of bilayer membranes to the other. These ATPases are found only in eukaryotes.


Pssm-ID: 273734 [Multi-domain]  Cd Length: 1057  Bit Score: 40.06  E-value: 2.11e-03
                           10        20
                   ....*....|....*....|....
gi 544824578   267 TVAIGDGANDLPMIKAA--GLGIA 288
Cdd:TIGR01652  771 TLAIGDGANDVSMIQEAdvGVGIS 794
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 242-288 2.90e-03

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 38.85  E-value: 2.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 544824578 242 DIVDAQYKANT----LTRLAEKYEIPVVQTVAIGDGANDLPMIKAAGLGIA 288
Cdd:PRK10530 189 DQVDIARKGNSkgkrLTQWVEAQGWSMKNVVAFGDNFNDISMLEAAGLGVA 239
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 249-287 4.49e-03

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: 38.10  E-value: 4.49e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 544824578 249 KANTLTRLAEKYEIPVVQTVAIGDGANDLPMIKAAGLGI 287
Cdd:cd02605  170 KGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGV 208
 
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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