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Conserved domains on  [gi|516458049|ref|WP_017846889|]
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MULTISPECIES: HAD family phosphatase [Pseudomonas]

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 ...
 1-216 4.40e-81

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: 240.89  E-value: 4.40e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049   1 MALVIFDLDDTLIHGDCATLWSEQMGRLAWVDPESFMRKNNELMDAYSQGKLAMEEFMDFSLEPMIGRTPEEIEHLVEPW 80
Cdd:COG0560    3 MRLAVFDLDGTLIAGESIDELARFLGRRGLVDRREVLEEVAAITERAMAGELDFEESLRFRVALLAGLPEEELEELAERL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049  81 VEDViePLIYSDATRTIARHRANGDRVLVISASGTHLVTPIAARIGIDEVLGIELDVSHGVYSGRTVGVLTYREGKITRL 160
Cdd:COG0560   83 FEEV--PRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDGRLTGEVVGPIVDGEGKAEAL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 516458049 161 LEWLEQEGETLEGAYFYSDSRNDLPLLLKVDNPQVVNPDPVLREHA-EKAGWPVHRW 216
Cdd:COG0560  161 RELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREAAdRERGWPVLDL 217
 
Name Accession Description Interval E-value
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-216 4.40e-81

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: 240.89  E-value: 4.40e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049   1 MALVIFDLDDTLIHGDCATLWSEQMGRLAWVDPESFMRKNNELMDAYSQGKLAMEEFMDFSLEPMIGRTPEEIEHLVEPW 80
Cdd:COG0560    3 MRLAVFDLDGTLIAGESIDELARFLGRRGLVDRREVLEEVAAITERAMAGELDFEESLRFRVALLAGLPEEELEELAERL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049  81 VEDViePLIYSDATRTIARHRANGDRVLVISASGTHLVTPIAARIGIDEVLGIELDVSHGVYSGRTVGVLTYREGKITRL 160
Cdd:COG0560   83 FEEV--PRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDGRLTGEVVGPIVDGEGKAEAL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 516458049 161 LEWLEQEGETLEGAYFYSDSRNDLPLLLKVDNPQVVNPDPVLREHA-EKAGWPVHRW 216
Cdd:COG0560  161 RELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREAAdRERGWPVLDL 217
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 3-199 4.00e-57

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: 179.42  E-value: 4.00e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049   3 LVIFDLDDTLIHGDCATLWSEQMGRLAWVDPESfMRKNNELMDAYSQGKLAMEEfMDFSLEPMIGRTPEEIEHLVEPWVE 82
Cdd:cd02612    1 LAFFDLDGTLIAGDSFFAFLRFKGIAERRAPLE-ELLLLRLMALYALGRLDGAG-MEALLGFATAGLAGELAALVEEFVE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049  83 DVIEPLIYSDATRTIARHRANGDRVLVISASGTHLVTPIAARIGIDEVLGIELDVSHGVYSGRTVGVLTYREGKITRLLE 162
Cdd:cd02612   79 EYILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDNVLGTQLETEDGRYTGRIIGPPCYGEGKVKRLRE 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 516458049 163 WLEQEGETLEGAYFYSDSRNDLPLLLKVDNPQVVNPD 199
Cdd:cd02612  159 WLAEEGIDLKDSYAYSDSINDLPMLEAVGHPVAVNPD 195
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 3-200 5.95e-48

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: 155.96  E-value: 5.95e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049    3 LVIFDLDDTLIHGDCATLWSEQMGRLAWVDPESFMRKN-NELMDAYSQGKLAMEEFMDFSLEPMIGRTPEEIEHLVEPWV 81
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLASKNILFEELRLPKVlARFEFFLNRGLDYMAYYRAFALDALAGLLEEDVRAIVEEFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049   82 EDVIEPLIYSDATRTIARHRANGDRVLVISASGTHLVTPIAARIGIDEVLGIELDVSH-GVYSGRTVGVLTYREGKITRL 160
Cdd:TIGR01490  81 NQKIESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTRLEESEdGIYTGNIDGNNCKGEGKVHAL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 516458049  161 LEWLEQEGETLEGAYFYSDSRNDLPLLLKVDNPQVVNPDP 200
Cdd:TIGR01490 161 AELLAEEQIDLKDSYAYGDSISDLPLLSLVGHPYVVNPDK 200
HAD pfam12710
haloacid dehalogenase-like hydrolase;
4-187 2.35e-36

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 126.11  E-value: 2.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049    4 VIFDLDDTLIHGDCATLWSEQMGRLAWVDPESFMRKNNELMDAYSQGKLAMEEFMDFsLEPMIGRTPEEIEHLVEPWVED 83
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALLRRGGPDLWRALLVLLLLALLRLLGRLSRAGAREL-LRALLAGLPEEDAAELERFVAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049   84 VIEPLIYSDATRTIARHRANGDRVLVISASGTHLVTPIAARIGIDEVLGIELDVSHGVYSGRTV--GVLTYREGKITRLL 161
Cdd:pfam12710  80 VALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATELEVDDGRFTGELRliGPPCAGEGKVRRLR 159

                         170       180
                  ....*....|....*....|....*...
gi 516458049  162 EWLEQEGE--TLEGAYFYSDSRNDLPLL 187
Cdd:pfam12710 160 AWLAARGLglDLADSVAYGDSPSDLPML 187
 
Name Accession Description Interval E-value
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-216 4.40e-81

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: 240.89  E-value: 4.40e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049   1 MALVIFDLDDTLIHGDCATLWSEQMGRLAWVDPESFMRKNNELMDAYSQGKLAMEEFMDFSLEPMIGRTPEEIEHLVEPW 80
Cdd:COG0560    3 MRLAVFDLDGTLIAGESIDELARFLGRRGLVDRREVLEEVAAITERAMAGELDFEESLRFRVALLAGLPEEELEELAERL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049  81 VEDViePLIYSDATRTIARHRANGDRVLVISASGTHLVTPIAARIGIDEVLGIELDVSHGVYSGRTVGVLTYREGKITRL 160
Cdd:COG0560   83 FEEV--PRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDGRLTGEVVGPIVDGEGKAEAL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 516458049 161 LEWLEQEGETLEGAYFYSDSRNDLPLLLKVDNPQVVNPDPVLREHA-EKAGWPVHRW 216
Cdd:COG0560  161 RELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREAAdRERGWPVLDL 217
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 3-199 4.00e-57

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: 179.42  E-value: 4.00e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049   3 LVIFDLDDTLIHGDCATLWSEQMGRLAWVDPESfMRKNNELMDAYSQGKLAMEEfMDFSLEPMIGRTPEEIEHLVEPWVE 82
Cdd:cd02612    1 LAFFDLDGTLIAGDSFFAFLRFKGIAERRAPLE-ELLLLRLMALYALGRLDGAG-MEALLGFATAGLAGELAALVEEFVE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049  83 DVIEPLIYSDATRTIARHRANGDRVLVISASGTHLVTPIAARIGIDEVLGIELDVSHGVYSGRTVGVLTYREGKITRLLE 162
Cdd:cd02612   79 EYILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDNVLGTQLETEDGRYTGRIIGPPCYGEGKVKRLRE 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 516458049 163 WLEQEGETLEGAYFYSDSRNDLPLLLKVDNPQVVNPD 199
Cdd:cd02612  159 WLAEEGIDLKDSYAYSDSINDLPMLEAVGHPVAVNPD 195
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 3-200 5.95e-48

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: 155.96  E-value: 5.95e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049    3 LVIFDLDDTLIHGDCATLWSEQMGRLAWVDPESFMRKN-NELMDAYSQGKLAMEEFMDFSLEPMIGRTPEEIEHLVEPWV 81
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLASKNILFEELRLPKVlARFEFFLNRGLDYMAYYRAFALDALAGLLEEDVRAIVEEFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049   82 EDVIEPLIYSDATRTIARHRANGDRVLVISASGTHLVTPIAARIGIDEVLGIELDVSH-GVYSGRTVGVLTYREGKITRL 160
Cdd:TIGR01490  81 NQKIESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTRLEESEdGIYTGNIDGNNCKGEGKVHAL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 516458049  161 LEWLEQEGETLEGAYFYSDSRNDLPLLLKVDNPQVVNPDP 200
Cdd:TIGR01490 161 AELLAEEQIDLKDSYAYGDSISDLPLLSLVGHPYVVNPDK 200
HAD pfam12710
haloacid dehalogenase-like hydrolase;
4-187 2.35e-36

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 126.11  E-value: 2.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049    4 VIFDLDDTLIHGDCATLWSEQMGRLAWVDPESFMRKNNELMDAYSQGKLAMEEFMDFsLEPMIGRTPEEIEHLVEPWVED 83
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALLRRGGPDLWRALLVLLLLALLRLLGRLSRAGAREL-LRALLAGLPEEDAAELERFVAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049   84 VIEPLIYSDATRTIARHRANGDRVLVISASGTHLVTPIAARIGIDEVLGIELDVSHGVYSGRTV--GVLTYREGKITRLL 161
Cdd:pfam12710  80 VALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATELEVDDGRFTGELRliGPPCAGEGKVRRLR 159

                         170       180
                  ....*....|....*....|....*...
gi 516458049  162 EWLEQEGE--TLEGAYFYSDSRNDLPLL 187
Cdd:pfam12710 160 AWLAARGLglDLADSVAYGDSPSDLPML 187
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 3-190 9.50e-29

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: 105.90  E-value: 9.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049    3 LVIFDLDDTLIHGDCAT-LWSEQMGRLAWVDPESFMRKNNELMDAYSQGKLAMEEFMDFSLEpmigrtpeeiehlvepWV 81
Cdd:TIGR01488   1 LAIFDFDGTLTRQDSLIdLLAKLLGTNDEVIELTRLAPSGRISFEDALGRRLALLHRSRSEE----------------VA 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049   82 EDVI--EPLIYSDATRTIARHRANGDRVLVISASGTHLVTPIAARIGIDEVLGIELDVSH-GVYSGRTVGVL-TYREGKI 157
Cdd:TIGR01488  65 KEFLarQVALRPGARELISWLKERGIDTVIVSGGFDFFVEPVAEKLGIDDVFANRLEFDDnGLLTGPIEGQVnPEGECKG 144

                         170       180       190
                  ....*....|....*....|....*....|...
gi 516458049  158 TRLLEWLEQEGETLEGAYFYSDSRNDLPLLLKV 190
Cdd:TIGR01488 145 KVLKELLEESKITLKKIIAVGDSVNDLPMLKLA 177
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 3-207 1.19e-10

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: 58.91  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049    3 LVIFDLDDTLIHGDCAtlwsEQMGRLAWVDPESfmrknNELMDAYSQGKLAMEEfmdfSLEPMIGR---TPEEIehlvep 79
Cdd:TIGR00338  16 LVVFDMDSTLINAETI----DEIAKIAGVEEEV-----SEITERAMRGELDFKA----SLRERVALlkgLPVEL------ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049   80 wVEDVIEPL-IYSDATRTIARHRANGDRVLVISASGTHLVTPIAARIGIDEVLGIELDVSHGVYSGRTVGVLTYREGKIT 158
Cdd:TIGR00338  77 -LKEVRENLpLTEGAEELVKTLKEKGYKVAVISGGFDLFAEHVKDKLGLDAAFANRLEVEDGKLTGLVEGPIVDASYKGK 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 516458049  159 RLLEWLEQEGETLEGAYFYSDSRNDLPLLLKVDNPQVVNPDPVLREHAE 207
Cdd:TIGR00338 156 TLLILLRKEGISPENTVAVGDGANDLSMIKAAGLGIAFNAKPKLQQKAD 204
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 3-187 6.72e-09

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: 53.32  E-value: 6.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049   3 LVIFDLDDTLIHGDCAtlwsEQMGRLAWVDPESfmrknNELMDAYSQGKLAMEEfmdfSLEPMIGR---TPEEIehlvep 79
Cdd:cd07500    1 LIVFDMDSTLIQQEVI----DELAAEAGVGEEV-----AAITERAMRGELDFEE----SLRERVALlkgLPESV------ 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049  80 wVEDVIEPLIYSD-ATRTIARHRANGDRVLVISASGTHLVTPIAARIGIDEVLGIELDVSHGVYSGRTVGVLTYREGKIT 158
Cdd:cd07500   62 -LDEVYERLTLTPgAEELIQTLKAKGYKTAVVSGGFTYFTDRLAEELGLDYAFANELEIKDGKLTGKVLGPIVDAQRKAE 140

                        170       180
                 ....*....|....*....|....*....
gi 516458049 159 RLLEWLEQEGETLEGAYFYSDSRNDLPLL 187
Cdd:cd07500  141 TLQELAARLGIPLEQTVAVGDGANDLPML 169
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 1-129 6.78e-06

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: 45.40  E-value: 6.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049   1 MALVIFDLDDTLIHGD-----CATLWSEQMGRLAWVDP--ESFMRKNNELMDAYSQGKLAMEEFMDFSLEPM-IGRTPEE 72
Cdd:COG1011    1 IKAVLFDLDGTLLDFDpviaeALRALAERLGLLDEAEElaEAYRAIEYALWRRYERGEITFAELLRRLLEELgLDLAEEL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 516458049  73 IEHLVEPWvEDVIEPliYSDATRTIARHRANGDRVLVISASGTHLVTPIAARIGIDE 129
Cdd:COG1011   81 AEAFLAAL-PELVEP--YPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDD 134
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 1-185 2.14e-05

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: 43.73  E-value: 2.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049    1 MALVIFDLDDTLIHGdcATLWSEQMGRLAWVDP--ESFMRKNNELMDAYSQ-GKLAMEEFMDF--SLEPMIGRTPEEIEH 75
Cdd:pfam00702   1 IKAVVFDLDGTLTDG--EPVVTEAIAELASEHPlaKAIVAAAEDLPIPVEDfTARLLLGKRDWleELDILRGLVETLEAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049   76 LVEPWVEDVI-------EPLIYSDATRTIARHRANGDRVLVISASGTHLVTPIAARIGIDEVLGIELDVShgvysgrtvg 148
Cdd:pfam00702  79 GLTVVLVELLgvialadELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGD---------- 148

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 516458049  149 VLTYREGKITRLLEWLEQEGETLEGAYFYSDSRNDLP 185
Cdd:pfam00702 149 DVGVGKPKPEIYLAALERLGVKPEEVLMVGDGVNDIP 185
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 4-113 3.07e-04

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: 40.10  E-value: 3.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049    4 VIFDLDDTLIHGDCATLWSEQMGRLaWVDPESFMRKnnelmdAYSQGKLAMEEFMDFSLEPMIGRTPEEI-EHLVEPWVE 82
Cdd:TIGR01509   2 ILFDLDGVLVDTEFAIAKLINREEL-GLVPDELGVS------AVGRLELALRRFKAQYGRTISPEDAQLLyKQLFYEQIE 74

                          90       100       110
                  ....*....|....*....|....*....|.
gi 516458049   83 DVIEPLIYSDATRTIARHRANGDRVLVISAS 113
Cdd:TIGR01509  75 EEAKLKPLPGVRALLEALRARGKKLALLTNS 105
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
1-184 1.40e-03

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 38.37  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049   1 MALVIFDLDDTLIHgdcatlwSEQMGRLAWvdpesfmrknNELMDAYSQGKLAMEEfmdfsLEPMIGRT-PEEIEHLVEP 79
Cdd:COG0546    1 IKLVLFDLDGTLVD-------SAPDIAAAL----------NEALAELGLPPLDLEE-----LRALIGLGlRELLRRLLGE 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458049  80 WVEDVIEPLI-----------------YSDATRTIARHRANGDRVLVISASGTHLVTPIAARIGIDevlgielDVSHGVY 142
Cdd:COG0546   59 DPDEELEELLarfrelyeeelldetrlFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLD-------DYFDAIV 131

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 516458049 143 SGRTVgvlTYREGKITRLLEWLEQEGETLEGAYFYSDSRNDL 184
Cdd:COG0546  132 GGDDV---PPAKPKPEPLLEALERLGLDPEEVLMVGDSPHDI 170
KELK pfam15796
KELK-motif containing domain of MRCK Ser/Thr protein kinase; KELK is a domain of eukaryotic ...
 42-59 9.61e-03

KELK-motif containing domain of MRCK Ser/Thr protein kinase; KELK is a domain of eukaryotic proteins found in serine/threonine-protein kinase MRCK-type proteins. The region is low-complexity, but it is not a predicted disordered-binding domain. The name comes from a highly conserved sequence motif within the domain. The function is not known.


Pssm-ID: 464876 [Multi-domain]  Cd Length: 80  Bit Score: 34.14  E-value: 9.61e-03
                          10
                  ....*....|....*...
gi 516458049   42 ELMDAYSQGKLAMEEFMD 59
Cdd:pfam15796  36 ELKDAHSQRKLAMEEFSE 53
 
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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