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Conserved domains on  [gi|663511222|gb|AIF01825|]
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Phosphoserine phosphatase (serB, PSPH) [uncultured marine group II/III euryarchaeote KM3_14_H03]

Protein Classification

HAD family hydrolase( domain architecture ID 10001729)

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

CATH:  3.30.1240.10
EC:  3.-.-.-
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
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 5-206 6.64e-33

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: 118.40  E-value: 6.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222   5 RAVVFDCDGVLTDnGSSWQNIHDY-----------FGTENLETLERFLNGEITDDEFMADDIRLWTavqpRIHRDDIMRC 73
Cdd:COG0560    4 RLAVFDLDGTLIA-GESIDELARFlgrrglvdrreVLEEVAAITERAMAGELDFEESLRFRVALLA----GLPEEELEEL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222  74 YSGI-----SLMEGARDVVEELRSRGIFVAIVSAGVDVFVGAIANMLSVDDWAANGFDWdDDGWLRG-PAPTRVNSHDKG 147
Cdd:COG0560   79 AERLfeevpRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEV-EDGRLTGeVVGPIVDGEGKA 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663511222 148 VMVEKLSRIKGIDPSGIVSVGDSSTDLSMMIPGSHFIGFNPARQRARDAFEQADTPLVD 206
Cdd:COG0560  158 EALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREAADRERGWPVLD 216
 
Name Accession Description Interval E-value
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 5-206 6.64e-33

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: 118.40  E-value: 6.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222   5 RAVVFDCDGVLTDnGSSWQNIHDY-----------FGTENLETLERFLNGEITDDEFMADDIRLWTavqpRIHRDDIMRC 73
Cdd:COG0560    4 RLAVFDLDGTLIA-GESIDELARFlgrrglvdrreVLEEVAAITERAMAGELDFEESLRFRVALLA----GLPEEELEEL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222  74 YSGI-----SLMEGARDVVEELRSRGIFVAIVSAGVDVFVGAIANMLSVDDWAANGFDWdDDGWLRG-PAPTRVNSHDKG 147
Cdd:COG0560   79 AERLfeevpRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEV-EDGRLTGeVVGPIVDGEGKA 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663511222 148 VMVEKLSRIKGIDPSGIVSVGDSSTDLSMMIPGSHFIGFNPARQRARDAFEQADTPLVD 206
Cdd:COG0560  158 EALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREAADRERGWPVLD 216
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 6-177 1.44e-26

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: 100.89  E-value: 1.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222    6 AVVFDCDGVLTDNGSSWQNIHDYFGT--ENLETLERFLNGEITDDEFMADDIRLWTAVQPRIHRDDIMRcySGISLMEGA 83
Cdd:TIGR01488   1 LAIFDFDGTLTRQDSLIDLLAKLLGTndEVIELTRLAPSGRISFEDALGRRLALLHRSRSEEVAKEFLA--RQVALRPGA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222   84 RDVVEELRSRGIFVAIVSAGVDVFVGAIANMLSVDDWAANGFDWDDDGWLRGP--APTRVNSHDKGVMVEKLSRIKGIDP 161
Cdd:TIGR01488  79 RELISWLKERGIDTVIVSGGFDFFVEPVAEKLGIDDVFANRLEFDDNGLLTGPieGQVNPEGECKGKVLKELLEESKITL 158

                         170
                  ....*....|....*.
gi 663511222  162 SGIVSVGDSSTDLSMM 177
Cdd:TIGR01488 159 KKIIAVGDSVNDLPML 174
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 73-177 1.03e-15

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: 72.20  E-value: 1.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222  73 CYSGISLMEGARDVVEELRSRGIFVAIVSAGVDVFVGAIANMLSVDDWAANGFDWDDD---GWLRGPAptrVNSHDKGVM 149
Cdd:cd07500   65 VYERLTLTPGAEELIQTLKAKGYKTAVVSGGFTYFTDRLAEELGLDYAFANELEIKDGkltGKVLGPI---VDAQRKAET 141

                         90       100
                 ....*....|....*....|....*...
gi 663511222 150 VEKLSRIKGIDPSGIVSVGDSSTDLSMM 177
Cdd:cd07500  142 LQELAARLGIPLEQTVAVGDGANDLPML 169
HAD pfam12710
haloacid dehalogenase-like hydrolase;
7-177 2.45e-13

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 66.02  E-value: 2.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222    7 VVFDCDGVLTDNGSSWQnIHDYFGTENLETLERFLNGEItdDEFMADDIRLWTAVQPRIHRDDIMRCYSGIS-------- 78
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFL-LIRALLRRGGPDLWRALLVLL--LLALLRLLGRLSRAGARELLRALLAGLPEEDaaelerfv 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222   79 -------LMEGARDVVEELRSRGIFVAIVSAGVDVFVGAIANMLSVDDWAANGFDWDDDGWLRGPAPTRVNSHDKGvmve 151
Cdd:pfam12710  78 aevalprLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATELEVDDGRFTGELRLIGPPCAGEG---- 153

                         170       180       190
                  ....*....|....*....|....*....|....
gi 663511222  152 KLSRIK--------GIDPSGIVSVGDSSTDLSMM 177
Cdd:pfam12710 154 KVRRLRawlaarglGLDLADSVAYGDSPSDLPML 187
PLN02954 PLN02954
phosphoserine phosphatase
 82-213 5.12e-09

phosphoserine phosphatase


Pssm-ID: 215514 [Multi-domain]  Cd Length: 224  Bit Score: 54.70  E-value: 5.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222  82 GARDVVEELRSRGIFVAIVSAGVDVFVGAIANMLSV--DDWAANGFDWDDDGWLRGPAPTRVNSHDKGvMVEKLSRIKGI 159
Cdd:PLN02954  88 GIPELVKKLRARGTDVYLVSGGFRQMIAPVAAILGIppENIFANQILFGDSGEYAGFDENEPTSRSGG-KAEAVQHIKKK 166

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 663511222 160 DPSG-IVSVGDSSTDLSMMIPG--SHFIGFNPARQRARDAfEQADTPLVDSKDLRDI 213
Cdd:PLN02954 167 HGYKtMVMIGDGATDLEARKPGgaDLFIGYGGVQVREAVA-AKADWFVTDFQDLIEV 222
 
Name Accession Description Interval E-value
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 5-206 6.64e-33

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: 118.40  E-value: 6.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222   5 RAVVFDCDGVLTDnGSSWQNIHDY-----------FGTENLETLERFLNGEITDDEFMADDIRLWTavqpRIHRDDIMRC 73
Cdd:COG0560    4 RLAVFDLDGTLIA-GESIDELARFlgrrglvdrreVLEEVAAITERAMAGELDFEESLRFRVALLA----GLPEEELEEL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222  74 YSGI-----SLMEGARDVVEELRSRGIFVAIVSAGVDVFVGAIANMLSVDDWAANGFDWdDDGWLRG-PAPTRVNSHDKG 147
Cdd:COG0560   79 AERLfeevpRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEV-EDGRLTGeVVGPIVDGEGKA 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663511222 148 VMVEKLSRIKGIDPSGIVSVGDSSTDLSMMIPGSHFIGFNPARQRARDAFEQADTPLVD 206
Cdd:COG0560  158 EALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREAADRERGWPVLD 216
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 6-177 1.44e-26

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: 100.89  E-value: 1.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222    6 AVVFDCDGVLTDNGSSWQNIHDYFGT--ENLETLERFLNGEITDDEFMADDIRLWTAVQPRIHRDDIMRcySGISLMEGA 83
Cdd:TIGR01488   1 LAIFDFDGTLTRQDSLIDLLAKLLGTndEVIELTRLAPSGRISFEDALGRRLALLHRSRSEEVAKEFLA--RQVALRPGA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222   84 RDVVEELRSRGIFVAIVSAGVDVFVGAIANMLSVDDWAANGFDWDDDGWLRGP--APTRVNSHDKGVMVEKLSRIKGIDP 161
Cdd:TIGR01488  79 RELISWLKERGIDTVIVSGGFDFFVEPVAEKLGIDDVFANRLEFDDNGLLTGPieGQVNPEGECKGKVLKELLEESKITL 158

                         170
                  ....*....|....*.
gi 663511222  162 SGIVSVGDSSTDLSMM 177
Cdd:TIGR01488 159 KKIIAVGDSVNDLPML 174
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 5-217 2.80e-24

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: 95.89  E-value: 2.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222    5 RAVVFDCDGVLTdNGSSWQNIHDYFGTENL--ETLERFLNGEITDDEFMADDIRLWTAVQprihRDDIMRCYSGISLMEG 82
Cdd:TIGR00338  15 KLVVFDMDSTLI-NAETIDEIAKIAGVEEEvsEITERAMRGELDFKASLRERVALLKGLP----VELLKEVRENLPLTEG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222   83 ARDVVEELRSRGIFVAIVSAGVDVFVGAIANMLSVDDWAANGFDWDDD---GWLRGPAptrVNSHDKGVMVEKLSRIKGI 159
Cdd:TIGR00338  90 AEELVKTLKEKGYKVAVISGGFDLFAEHVKDKLGLDAAFANRLEVEDGkltGLVEGPI---VDASYKGKTLLILLRKEGI 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222  160 DPSGIVSVGDSSTDLSMMIPGSHFIGFN--PARQRARDAfeqadtpLVDSKDLRDIWEHI 217
Cdd:TIGR00338 167 SPENTVAVGDGANDLSMIKAAGLGIAFNakPKLQQKADI-------CINKKDLTDILPLL 219
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 73-177 1.03e-15

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: 72.20  E-value: 1.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222  73 CYSGISLMEGARDVVEELRSRGIFVAIVSAGVDVFVGAIANMLSVDDWAANGFDWDDD---GWLRGPAptrVNSHDKGVM 149
Cdd:cd07500   65 VYERLTLTPGAEELIQTLKAKGYKTAVVSGGFTYFTDRLAEELGLDYAFANELEIKDGkltGKVLGPI---VDAQRKAET 141

                         90       100
                 ....*....|....*....|....*...
gi 663511222 150 VEKLSRIKGIDPSGIVSVGDSSTDLSMM 177
Cdd:cd07500  142 LQELAARLGIPLEQTVAVGDGANDLPML 169
HAD pfam12710
haloacid dehalogenase-like hydrolase;
7-177 2.45e-13

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 66.02  E-value: 2.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222    7 VVFDCDGVLTDNGSSWQnIHDYFGTENLETLERFLNGEItdDEFMADDIRLWTAVQPRIHRDDIMRCYSGIS-------- 78
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFL-LIRALLRRGGPDLWRALLVLL--LLALLRLLGRLSRAGARELLRALLAGLPEEDaaelerfv 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222   79 -------LMEGARDVVEELRSRGIFVAIVSAGVDVFVGAIANMLSVDDWAANGFDWDDDGWLRGPAPTRVNSHDKGvmve 151
Cdd:pfam12710  78 aevalprLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATELEVDDGRFTGELRLIGPPCAGEG---- 153

                         170       180       190
                  ....*....|....*....|....*....|....
gi 663511222  152 KLSRIK--------GIDPSGIVSVGDSSTDLSMM 177
Cdd:pfam12710 154 KVRRLRawlaarglGLDLADSVAYGDSPSDLPML 187
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
4-174 4.57e-13

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 65.72  E-value: 4.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222   4 VRAVVFDCDGVLTDNGSSW------------------QNIHDYFGTENLETLERFLNGEITDD-EFMADDIRlwtavqpR 64
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIaaalnealaelglppldlEELRALIGLGLRELLRRLLGEDPDEElEELLARFR-------E 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222  65 IHRDDIMRcysGISLMEGARDVVEELRSRGIFVAIVSAGVDVFVGAIANMLSVDDWaangFDW---DDDGWLRGPAPTrv 141
Cdd:COG0546   74 LYEEELLD---ETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDY----FDAivgGDDVPPAKPKPE-- 144

                        170       180       190
                 ....*....|....*....|....*....|...
gi 663511222 142 nshdkgvMVEKLSRIKGIDPSGIVSVGDSSTDL 174
Cdd:COG0546  145 -------PLLEALERLGLDPEEVLMVGDSPHDI 170
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 4-177 5.05e-11

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: 59.91  E-value: 5.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222    4 VRAVVFDCDGVLTDNGSSWQNIHDYFGTENLET---LERFLNGEITDDEF----MADDIRLWTAVQPRIHRDD------- 69
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPLAkaiVAAAEDLPIPVEDFtarlLLGKRDWLEELDILRGLVEtleaegl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222   70 ---------IMRCYSGISLMEGARDVVEELRSRGIFVAIVSAGVDVFVGAIANMLSVDDWAANGFDWDDDGwLRGPAPTr 140
Cdd:pfam00702  81 tvvlvellgVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVG-VGKPKPE- 158

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 663511222  141 vnshdkgvMVEKLSRIKGIDPSGIVSVGDSSTDLSMM 177
Cdd:pfam00702 159 --------IYLAALERLGVKPEEVLMVGDGVNDIPAA 187
HAD_PSP_eu cd04309
phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human ...
 6-192 1.07e-10

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: 58.83  E-value: 1.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222   6 AVVFDCDG-VLTDngsswqnihdyfgtENLETLERFLN-----GEITDdEFMADDIRLWTAVQPRIhrdDIMRC------ 73
Cdd:cd04309    2 AVCFDVDStVIQE--------------EGIDELAKFCGvgdevAELTR-RAMGGSIPFRDALRKRL---AIINPtkeqvd 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222  74 -YSGIS---LMEGARDVVEELRSRGIFVAIVSAGVDVFVGAIANMLSV--DDWAANGFDWDDDGWLRGPAPTRVN--SHD 145
Cdd:cd04309   64 eFLEEHpprLTPGVEELVSRLKARGVEVYLISGGFRELIEPVASQLGIplENVFANRLLFDFNGEYAGFDETQPTsrSGG 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 663511222 146 KGVMVEKLSriKGIDPSGIVSVGDSSTDLSMMIPGSHFIGFNPARQR 192
Cdd:cd04309  144 KAKVIEQLK--EKHHYKRVIMIGDGATDLEACPPADAFIGFGGNVIR 188
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 4-170 4.19e-09

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


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 54.65  E-value: 4.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222   4 VRAVVFDCDGVLTDNGSSW-----------------QNIHDYFGTENLETLERFLNGEITDDEFMADDIRLWTAVQPRIH 66
Cdd:COG1011    1 IKAVLFDLDGTLLDFDPVIaealralaerlglldeaEELAEAYRAIEYALWRRYERGEITFAELLRRLLEELGLDLAEEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222  67 RDDIMRCYSG-ISLMEGARDVVEELRSRGIFVAIVSAGVDVFVGAIANMLSVDDWaangFDwdddgwlrgpapTRVNSHD 145
Cdd:COG1011   81 AEAFLAALPElVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDL----FD------------AVVSSEE 144

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 663511222 146 KGV----------MVEKLsrikGIDPSGIVSVGDS 170
Cdd:COG1011  145 VGVrkpdpeifelALERL----GVPPEEALFVGDS 175
PLN02954 PLN02954
phosphoserine phosphatase
 82-213 5.12e-09

phosphoserine phosphatase


Pssm-ID: 215514 [Multi-domain]  Cd Length: 224  Bit Score: 54.70  E-value: 5.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222  82 GARDVVEELRSRGIFVAIVSAGVDVFVGAIANMLSV--DDWAANGFDWDDDGWLRGPAPTRVNSHDKGvMVEKLSRIKGI 159
Cdd:PLN02954  88 GIPELVKKLRARGTDVYLVSGGFRQMIAPVAAILGIppENIFANQILFGDSGEYAGFDENEPTSRSGG-KAEAVQHIKKK 166

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 663511222 160 DPSG-IVSVGDSSTDLSMMIPG--SHFIGFNPARQRARDAfEQADTPLVDSKDLRDI 213
Cdd:PLN02954 167 HGYKtMVMIGDGATDLEARKPGgaDLFIGYGGVQVREAVA-AKADWFVTDFQDLIEV 222
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
4-120 5.69e-09

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 54.06  E-value: 5.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222   4 VRAVVFDCDGVLTDNGS----SWQNIHDYFG----------------TENLETLERFLNGEITDDEFMAddiRLWTAVQP 63
Cdd:COG0637    2 IKAVIFDMDGTLVDSEPlharAWREAFAELGidlteeeyrrlmgrsrEDILRYLLEEYGLDLPEEELAA---RKEELYRE 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 663511222  64 RIHRDdimrcysGISLMEGARDVVEELRSRGIFVAIVSAGVDVFVGAIANMLSVDDW 120
Cdd:COG0637   79 LLAEE-------GLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDY 128
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 6-177 1.18e-07

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: 50.42  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222    6 AVVFDCDGVLTDNGS-----SWQ-----NIHDYFGTENLETLERFLNgEITDD-----EFMADDIRLWTAVQPRIHRDDI 70
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTlfiflKFLaskniLFEELRLPKVLARFEFFLN-RGLDYmayyrAFALDALAGLLEEDVRAIVEEF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222   71 MRCYSGISLMEGARDVVEELRSRGIFVAIVSAGVDVFVGAIANMLSVDDWAANGFDWDDDGWLRGpAPTRVNSHDKGvMV 150
Cdd:TIGR01490  80 VNQKIESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTRLEESEDGIYTG-NIDGNNCKGEG-KV 157

                         170       180       190
                  ....*....|....*....|....*....|
gi 663511222  151 EKLSR---IKGIDPSGIVSVGDSSTDLSMM 177
Cdd:TIGR01490 158 HALAEllaEEQIDLKDSYAYGDSISDLPLL 187
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 7-185 1.69e-06

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


Pssm-ID: 319835 [Multi-domain]  Cd Length: 207  Bit Score: 47.01  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222   7 VVFDCDGVLTDngsSWQNIHD-------YFGTENLETLE-RFLNGeITDDEFMAddiRLWTAVQPRIHRD--------DI 70
Cdd:cd07533    2 VIFDWDGTLAD---SQHNIVAamtaafaDLGLPVPSAAEvRSIIG-LSLDEAIA---RLLPMATPALVAVaerykeafDI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222  71 MRCYSG--ISLMEGARDVVEELRSRGIFVAIVS----AGVDvfvgaiaNMLSVDDWAanGFdWD-----DDGWLRgPAPT 139
Cdd:cd07533   75 LRLLPEhaEPLFPGVREALDALAAQGVLLAVATgksrRGLD-------RVLEQHGLG--GY-FDatrtaDDTPSK-PHPE 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 663511222 140 rvnshdkgvMVEKLSRIKGIDPSGIVSVGDSSTDLSMMI-PGSHFIG 185
Cdd:cd07533  144 ---------MLREILAELGVDPSRAVMVGDTAYDMQMAAnAGAHAVG 181
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 83-177 4.76e-06

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: 43.92  E-value: 4.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222  83 ARDVVEELRSRGIFVAIVSAGVDVFVGAIANMLSVDDWAANGFDWDDDGWlrgpaptrvnSHDKGVMVEKLSRIKGIDPS 162
Cdd:cd01427   12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGT----------PKPKPKPLLLLLLKLGVDPE 81

                         90
                 ....*....|....*
gi 663511222 163 GIVSVGDSSTDLSMM 177
Cdd:cd01427   82 EVLFVGDSENDIEAA 96
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 78-177 4.98e-06

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: 44.89  E-value: 4.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222  78 SLMEGARDVVEELRSRGIFVAIVSAGVDVFVGAIANMLSVDD--WAANGfdwdddgwlrgpaptrvnSHDKGVMVEKLSR 155
Cdd:cd07514   16 SIDLRAIEAIRKLEKAGIPVVLVTGNSLPVARALAKYLGLSGpvVAENG------------------GVDKGTGLEKLAE 77

                         90       100
                 ....*....|....*....|..
gi 663511222 156 IKGIDPSGIVSVGDSSTDLSMM 177
Cdd:cd07514   78 RLGIDPEEVLAIGDSENDIEMF 99
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 6-103 8.86e-06

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


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 44.72  E-value: 8.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222    6 AVVFDCDGVLTDNGSS-----WQNIHDYFGTE--------NLETLERFLNGEITDDEFMaddirLWTAVQPRIHRDDIMR 72
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAiakliNREELGLVPDElgvsavgrLELALRRFKAQYGRTISPE-----DAQLLYKQLFYEQIEE 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 663511222   73 cYSGISLMEGARDVVEELRSRGIFVAIVSAG 103
Cdd:TIGR01509  76 -EAKLKPLPGVRALLEALRARGKKLALLTNS 105
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 6-177 9.29e-06

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: 44.99  E-value: 9.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222   6 AVVFDCDGVLTDnGSSWqnIHdyFGTENLETLERFLNGEITDDEFMAD-----------DIRLWTAVQPRIHR-----DD 69
Cdd:cd02612    1 LAFFDLDGTLIA-GDSF--FA--FLRFKGIAERRAPLEELLLLRLMALyalgrldgagmEALLGFATAGLAGElaalvEE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222  70 IMRCYSGISLMEGARDVVEELRSRGIFVAIVSAGVDVFVGAIANMLSVDDWAANGFDWDDDGWLRGPAPTRVNSHDKGVM 149
Cdd:cd02612   76 FVEEYILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDNVLGTQLETEDGRYTGRIIGPPCYGEGKVKR 155

                        170       180
                 ....*....|....*....|....*...
gi 663511222 150 VEKLSRIKGIDPSGIVSVGDSSTDLSMM 177
Cdd:cd02612  156 LREWLAEEGIDLKDSYAYSDSINDLPML 183
HAD_Pase cd07524
phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like ...
 77-176 3.33e-05

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: 43.47  E-value: 3.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222  77 ISLMEGARDVVEELRSRGIFVAIVSAGVDVFVGAIANMLSVDDWA--ANGFDWDDDGW-LRGPAPTRVNS---HDKGVMV 150
Cdd:cd07524   71 AKIRPGFKEFVAFCQEHGIPFIIVSGGMDFFIEPLLEGLVIEKIAiyCNGSDFSGEQIhIDWPHECDCTNgcgCCKSSII 150

                         90       100
                 ....*....|....*....|....*.
gi 663511222 151 EKLSRIKGIdpsgIVSVGDSSTDLSM 176
Cdd:cd07524  151 RKYSKPRPF----IIVIGDSVTDLEA 172
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 4-101 3.53e-05

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. 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: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 43.10  E-value: 3.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222   4 VRAVVFDCDGVLTD-------------NGSSWQNIHDYFGTENLEtlERFLNGEITDDEFmaddIRLWTAVQPRIHRDDI 70
Cdd:cd02603    1 IRAVLFDFGGVLIDpdpaaavarfealTGEPSEFVLDTEGLAGAF--LELERGRITEEEF----WEELREELGRPLSAEL 74

                         90       100       110
                 ....*....|....*....|....*....|...
gi 663511222  71 MRCYS--GISLMEGARDVVEELRSRGIFVAIVS 101
Cdd:cd02603   75 FEELVlaAVDPNPEMLDLLEALRAKGYKVYLLS 107
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 6-103 5.84e-05

beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; This family represents the beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. Family members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. It 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: 319808 [Multi-domain]  Cd Length: 143  Bit Score: 41.83  E-value: 5.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222   6 AVVFDCDGVLTDNGSSWqnihdyfgtenletLERFLNGEITDDEFMaddirlwtavqpRIHRDDimrcysGISLMEGARD 85
Cdd:cd07505    1 AVIFDMDGVLIDTEPLH--------------RQAWQLLERKNALLL------------ELIASE------GLKLKPGVVE 48

                         90
                 ....*....|....*...
gi 663511222  86 VVEELRSRGIFVAIVSAG 103
Cdd:cd07505   49 LLDALKAAGIPVAVATSS 66
serB PRK11133
phosphoserine phosphatase; Provisional
 79-177 4.74e-04

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 40.32  E-value: 4.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222  79 LMEGARDVVEELRSRGIFVAIVSAGVDVFVGAIANMLSVDDWAANGFDWDD---DGWLRGPAptrVNSHDKGVMVEKLSR 155
Cdd:PRK11133 182 LMPGLTELVLKLQALGWKVAIASGGFTYFADYLRDKLRLDAAVANELEIMDgklTGNVLGDI---VDAQYKADTLTRLAQ 258

                         90       100
                 ....*....|....*....|..
gi 663511222 156 IKGIDPSGIVSVGDSSTDLSMM 177
Cdd:PRK11133 259 EYEIPLAQTVAIGDGANDLPMI 280
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
7-174 7.40e-04

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 39.10  E-value: 7.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222    7 VVFDCDGVLTDNGSSWQNIHDYfgtenleTLERFLNGEITDDE---FM---ADDIRLWTAVQPRIH--RDDIMRCYS--- 75
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNY-------LLEEFGYGELSEEEilkFIglpLREIFRYLGVSEDEEekIEFYLRKYNeel 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222   76 ---GISLMEGARDVVEELRSRGIFVAIVSAG----VDVFVgaiaNMLSVDDWaangFDW----DDDGwLRGPAPTrvnsh 144
Cdd:pfam13419  74 hdkLVKPYPGIKELLEELKEQGYKLGIVTSKsrenVEEFL----KQLGLEDY----FDVivggDDVE-GKKPDPD----- 139

                         170       180       190
                  ....*....|....*....|....*....|
gi 663511222  145 dkgvMVEKLSRIKGIDPSGIVSVGDSSTDL 174
Cdd:pfam13419 140 ----PILKALEQLGLKPEEVIYVGDSPRDI 165
P-type_ATPase_FixI-like cd02092
Rhizobium meliloti FixI and related proteins; belongs to P-type heavy metal-transporting ...
 68-123 7.55e-04

Rhizobium meliloti FixI and related proteins; belongs to P-type heavy metal-transporting ATPase subfamily; FixI may be a pump of a specific cation involved in symbiotic nitrogen fixation. The Rhizobium fixI gene is part of an operon conserved among rhizobia, fixGHIS. FixG, FixH, FixI, and FixS may participate in a membrane-bound complex coupling the FixI cation pump with a redox process catalyzed by FixG, an iron-sulfur protein. 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: 319782 [Multi-domain]  Cd Length: 605  Bit Score: 40.03  E-value: 7.55e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 663511222  68 DDIMRcysgislmEGARDVVEELRSRGIFVAIVSAGVDVFVGAIANMLSVDDWAAN 123
Cdd:cd02092  432 EDRPR--------PDAREAISALRALGLSVEILSGDREPAVRALARALGIEDWRAG 479
thrH PRK13582
bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;
10-199 1.14e-03

bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;


Pssm-ID: 237437 [Multi-domain]  Cd Length: 205  Bit Score: 38.75  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222  10 DCDGVLTDngSSWQNIHDYFGTENLETLERflngEITD-DEFMadDIRLWTAVQPRIHRDDIMRCYSGISLMEGARDVVE 88
Cdd:PRK13582   7 DLEGVLVP--EIWIAFAEKTGIPELRATTR----DIPDyDVLM--KQRLDILDEHGLGLADIQEVIATLDPLPGAVEFLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222  89 ELRSRGIFVaIVSAGVDVFVGAIANMLSVDDWAANGFDWDDDGW-----LRGPAPTRvnshdkgvmvEKLSRIKGIDpSG 163
Cdd:PRK13582  79 WLRERFQVV-ILSDTFYEFAGPLMRQLGWPTLFCHSLEVDEDGMitgydLRQPDGKR----------QAVKALKSLG-YR 146

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 663511222 164 IVSVGDSSTDLSMMIPGSHFIGFNPArQRARDAFEQ 199
Cdd:PRK13582 147 VIAAGDSYNDTTMLGEADAGILFRPP-ANVIAEFPQ 181
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 6-174 2.92e-03

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


Pssm-ID: 319798 [Multi-domain]  Cd Length: 209  Bit Score: 37.57  E-value: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222   6 AVVFDCDGVLTDNG----SSWQNIHDYFGTE--NLETLERFLNGEITD---DEFMADDIRLWTAVQprIHRDDIM-RCYS 75
Cdd:cd04302    1 TILFDLDGTLTDSAegitASVQYALEELGIPvpDESELRRFIGPPLEDsfrELLPFDEEEAQRAVD--AYREYYKeKGLF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222  76 GISLMEGARDVVEELRSRGIFVAIVSAGVDVFVGAIANMLSVDDWAANGFDWDDDGwlrgpapTRVNSHDkgVMVEKLSR 155
Cdd:cd04302   79 ENEVYPGIPELLEKLKAAGYRLYVATSKPEVFARRILEHFGLDEYFDGIAGASLDG-------SRVHKAD--VIRYALDT 149

                        170
                 ....*....|....*....
gi 663511222 156 IkGIDPSGIVSVGDSSTDL 174
Cdd:cd04302  150 L-GIAPEQAVMIGDRKHDI 167
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 145-177 2.95e-03

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 37.65  E-value: 2.95e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 663511222 145 DKGVMVEKLSRIKGIDPSGIVSVGDSSTDLSMM 177
Cdd:PRK01158 157 NKGTGLKKLAELMGIDPEEVAAIGDSENDLEMF 189
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 6-173 3.20e-03

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


Pssm-ID: 319799 [Multi-domain]  Cd Length: 201  Bit Score: 37.34  E-value: 3.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222   6 AVVFDCDGVLTDNG----SSWQNIHDYFGTENLETLER-FLNGEITDDEFMADDIRLWTavQPRIHRDDI---MRCYSGI 77
Cdd:cd04303    1 LIIFDFDGTLADSFpwflSILNQLAARHGFKTVDEEEIeQLRQLSSREILKQLGVPLWK--LPLIAKDFRrlmAEAAPEL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222  78 SLMEGARDVVEELRSRGIFVAIVS----AGVDVFVG--AIANMLSVDDwAANGFdwdddgwlrgpaptrvnshDKGVMVE 151
Cdd:cd04303   79 ALFPGVEDMLRALHARGVRLAVVSsnseENIRRVLGpeELISLFAVIE-GSSLF-------------------GKAKKIR 138

                        170       180
                 ....*....|....*....|..
gi 663511222 152 KLSRIKGIDPSGIVSVGDSSTD 173
Cdd:cd04303  139 RVLRRTKITAAQVIYVGDETRD 160
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 99-219 5.89e-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: 36.67  E-value: 5.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222   99 IVSAGVDV-FVGAIANMLSVD-DWAANGFDWDddgwlrgPAPTRVNshdKGVMVEKLSRIKGIDPSGIVSVGDSSTDLSM 176
Cdd:TIGR01482 111 KMRYGIDVdTVREIIKELGLNlVAVDSGFDIH-------ILPQGVN---KGVAVKKLKEKLGIKPGETLVCGDSENDIDL 180

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 663511222  177 M-IPgshfiGFNPARQRARDAFEQADTPLVDSKDLRDIWEHIFE 219
Cdd:TIGR01482 181 FeVP-----GFGVAVANAQPELKEWADYVTESPYGEGGAEAIGE 219
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 1-177 8.64e-03

3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily phosphatases [Cell wall/membrane/envelope biogenesis, General function prediction only];


Pssm-ID: 441384 [Multi-domain]  Cd Length: 170  Bit Score: 35.80  E-value: 8.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222   1 MAEVRAVVFDCDGVLTDNGSswqnihdYFGtENLETLERFlngeitddefmaddirlwtavqpriHRDDIMrcysGISLm 80
Cdd:COG1778    5 AKKIKLLIFDVDGVLTDGRI-------YYD-EDGEELKRF-------------------------NVRDGL----GIKL- 46

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222  81 egardvveeLRSRGIFVAIVSAGVDVFVGAIANMLSVDDwaangfdwdddgwlrgpapTRVNSHDKGVMVEKLSRIKGID 160
Cdd:COG1778   47 ---------LRKAGIKVAIITGRDSPAVRRRAEELGITH-------------------VYQGVKDKLEALEELLAKLGLS 98

                        170
                 ....*....|....*..
gi 663511222 161 PSGIVSVGDSSTDLSMM 177
Cdd:COG1778   99 PEEVAYIGDDLPDLPVM 115
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 4-101 9.09e-03

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


Pssm-ID: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 36.10  E-value: 9.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511222   4 VRAVVFDCDGVLTD------------------NGSSWQNIHDYFGTENLETLERFLNGEITD--DEFMADDirlwtavqp 63
Cdd:cd02616    1 ITTILFDLDGTLIDtneliiksfnhtlkeyglEGYTREEVLPFIGPPLRETFEKIDPDKLEDmvEEFRKYY--------- 71

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 663511222  64 RIHRDDIMRCYsgislmEGARDVVEELRSRGIFVAIVS 101
Cdd:cd02616   72 REHNDDLTKEY------PGVYETLARLKSQGIKLGVVT 103
 
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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