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Conserved domains on  [gi|658548682|ref|WP_029741138|]
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phosphatidylglycerophosphatase C [Enterobacter asburiae]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

HAD (haloacid dehalogenase) family hydrolase; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

EC:  3.6.3.-
Gene Ontology:  GO:0005524|GO:0016887|GO:0005215

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
 2-211 8.03e-134

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member TIGR01545:

Pssm-ID: 473868  Cd Length: 210  Bit Score: 373.89  E-value: 8.03e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548682    2 ANHGRRVVFFDLDGTLHQQDMFGTFMRYLLRRQPLNALLVLPLLPVIGIALLVKGRAARWPMSLLLWGCTFGHSEARLKQ 81
Cdd:TIGR01545   1 AAGAKRIIFFDLDGTLHQQDMFGSFLRFLLRHLPLNALLVIPLLPIIAIALLIGGRAARWPMSLLLWACTFGHREAHLQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548682   82 LEKDFAHWFRGHVAAFPVVQARLTSYLDANDADIWLITGSPQTLVEQVYFDTPWLPRVNLIATQISRGYGGWVLTLRCLG 161
Cdd:TIGR01545  81 LEADFVAAFRDKVTAFPLVAERLRQYLESSDADIWLITGSPQPLVEAVYFDSNFIHRLNLIASQIERGNGGWVLPLRCLG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 658548682  162 HEKVVQLEKRIGTPLRLYSGYSDSKQDNPLLYFCQHRWRVTPSGELQQLE 211
Cdd:TIGR01545 161 HEKVAQLEQKIGSPLKLYSGYSDSKQDNPLLAFCEHRWRVSKRGELQQLE 210
 
Name Accession Description Interval E-value
YfhB_g-proteo TIGR01545
haloacid dehalogenase superfamily, subfamily IF hydrolase, YfhB; This model describes a clade ...
 2-211 8.03e-134

haloacid dehalogenase superfamily, subfamily IF hydrolase, YfhB; This model describes a clade of sequences limited to the gamma proteobacteria. This group is a member of the haloacid dehalogenase (HAD) superfamily of aspartate-dependent hydrolases and all of the conserved catalytic motifs are present. Although structurally similar to subfamily IA in that the variable domain is predicted to consist of five consecutive alpha helices (by PSI-PRED), it is sufficiently divergent to warrant being regarded as a separate sub-family (IF). The gene name comes from the E. coli gene. There is currently no information regarding the function of this gene.


Pssm-ID: 130608  Cd Length: 210  Bit Score: 373.89  E-value: 8.03e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548682    2 ANHGRRVVFFDLDGTLHQQDMFGTFMRYLLRRQPLNALLVLPLLPVIGIALLVKGRAARWPMSLLLWGCTFGHSEARLKQ 81
Cdd:TIGR01545   1 AAGAKRIIFFDLDGTLHQQDMFGSFLRFLLRHLPLNALLVIPLLPIIAIALLIGGRAARWPMSLLLWACTFGHREAHLQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548682   82 LEKDFAHWFRGHVAAFPVVQARLTSYLDANDADIWLITGSPQTLVEQVYFDTPWLPRVNLIATQISRGYGGWVLTLRCLG 161
Cdd:TIGR01545  81 LEADFVAAFRDKVTAFPLVAERLRQYLESSDADIWLITGSPQPLVEAVYFDSNFIHRLNLIASQIERGNGGWVLPLRCLG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 658548682  162 HEKVVQLEKRIGTPLRLYSGYSDSKQDNPLLYFCQHRWRVTPSGELQQLE 211
Cdd:TIGR01545 161 HEKVAQLEQKIGSPLKLYSGYSDSKQDNPLLAFCEHRWRVSKRGELQQLE 210
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 9-204 2.17e-38

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: 131.27  E-value: 2.17e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548682   9 VFFDLDGTLHQQDMFGTFMRY---LLRRQPLNALLVLPLlpvigIALLVKGRAARWPMSLLLWGCTFGHSEaRLKQLEKD 85
Cdd:cd02612    2 AFFDLDGTLIAGDSFFAFLRFkgiAERRAPLEELLLLRL-----MALYALGRLDGAGMEALLGFATAGLAG-ELAALVEE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548682  86 FAHWFRGHVaAFPVVQARLTSYLDANDaDIWLITGSPqTLVEQVYFDTPWLPrvNLIATQ--ISRGYGGWVLTLR-CLGH 162
Cdd:cd02612   76 FVEEYILRV-LYPEARELIAWHKAAGH-DVVLISASP-EELVAPIARKLGID--NVLGTQleTEDGRYTGRIIGPpCYGE 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 658548682 163 EKVVQLEKRI---GTPLRLYSGYSDSKQDNPLLYFCQHRWRVTPS 204
Cdd:cd02612  151 GKVKRLREWLaeeGIDLKDSYAYSDSINDLPMLEAVGHPVAVNPD 195
HAD pfam12710
haloacid dehalogenase-like hydrolase;
9-192 1.72e-10

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 57.93  E-value: 1.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548682    9 VFFDLDGTLHQQDMFGTFMRYLLRRQPLNALLVLPLLPVIGIALLVkGRAARWPMSLLLWGCTFGHSEARLKQLEKDFAH 88
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALLRRGGPDLWRALLVLLLLALLRLL-GRLSRAGARELLRALLAGLPEEDAAELERFVAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548682   89 WFRGhvAAFPVVQARLTSYLDANDAdIWLITGSPQTLVEqvyfdtPWLPRV---NLIATQISRGYGGWVLTLR-----CL 160
Cdd:pfam12710  80 VALP--RLHPGALELLAAHRAAGDR-VVVVTGGLRPLVE------PVLAELgfdEVLATELEVDDGRFTGELRligppCA 150

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 658548682  161 GHEKVVQLEKRIG------TPLRLYsGYSDSKQDNPLL 192
Cdd:pfam12710 151 GEGKVRRLRAWLAarglglDLADSV-AYGDSPSDLPML 187
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 6-192 1.62e-06

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 47.14  E-value: 1.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548682   6 RRVVFFDLDGTLHQQDMFGTFMRYLLRRQPLNALLVLPLLPVIgIALLVKGRAARWPMSLLLWGCTFGHSEARLKQLekd 85
Cdd:COG0560    3 MRLAVFDLDGTLIAGESIDELARFLGRRGLVDRREVLEEVAAI-TERAMAGELDFEESLRFRVALLAGLPEEELEEL--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548682  86 FAHWFRGHVAAFPVVQARLTSYLDANDaDIWLITGSPQTLVEqvyfdtPWLPRVNL---IATQ--ISRG-YGGWVLTLRC 159
Cdd:COG0560   79 AERLFEEVPRLYPGARELIAEHRAAGH-KVAIVSGGFTFFVE------PIAERLGIdhvIANEleVEDGrLTGEVVGPIV 151

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 658548682 160 LGHEKVVQLE---KRIGTPLRLYSGYSDSKQDNPLL 192
Cdd:COG0560  152 DGEGKAEALRelaAELGIDLEQSYAYGDSANDLPML 187
 
Name Accession Description Interval E-value
YfhB_g-proteo TIGR01545
haloacid dehalogenase superfamily, subfamily IF hydrolase, YfhB; This model describes a clade ...
 2-211 8.03e-134

haloacid dehalogenase superfamily, subfamily IF hydrolase, YfhB; This model describes a clade of sequences limited to the gamma proteobacteria. This group is a member of the haloacid dehalogenase (HAD) superfamily of aspartate-dependent hydrolases and all of the conserved catalytic motifs are present. Although structurally similar to subfamily IA in that the variable domain is predicted to consist of five consecutive alpha helices (by PSI-PRED), it is sufficiently divergent to warrant being regarded as a separate sub-family (IF). The gene name comes from the E. coli gene. There is currently no information regarding the function of this gene.


Pssm-ID: 130608  Cd Length: 210  Bit Score: 373.89  E-value: 8.03e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548682    2 ANHGRRVVFFDLDGTLHQQDMFGTFMRYLLRRQPLNALLVLPLLPVIGIALLVKGRAARWPMSLLLWGCTFGHSEARLKQ 81
Cdd:TIGR01545   1 AAGAKRIIFFDLDGTLHQQDMFGSFLRFLLRHLPLNALLVIPLLPIIAIALLIGGRAARWPMSLLLWACTFGHREAHLQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548682   82 LEKDFAHWFRGHVAAFPVVQARLTSYLDANDADIWLITGSPQTLVEQVYFDTPWLPRVNLIATQISRGYGGWVLTLRCLG 161
Cdd:TIGR01545  81 LEADFVAAFRDKVTAFPLVAERLRQYLESSDADIWLITGSPQPLVEAVYFDSNFIHRLNLIASQIERGNGGWVLPLRCLG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 658548682  162 HEKVVQLEKRIGTPLRLYSGYSDSKQDNPLLYFCQHRWRVTPSGELQQLE 211
Cdd:TIGR01545 161 HEKVAQLEQKIGSPLKLYSGYSDSKQDNPLLAFCEHRWRVSKRGELQQLE 210
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 9-204 2.17e-38

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: 131.27  E-value: 2.17e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548682   9 VFFDLDGTLHQQDMFGTFMRY---LLRRQPLNALLVLPLlpvigIALLVKGRAARWPMSLLLWGCTFGHSEaRLKQLEKD 85
Cdd:cd02612    2 AFFDLDGTLIAGDSFFAFLRFkgiAERRAPLEELLLLRL-----MALYALGRLDGAGMEALLGFATAGLAG-ELAALVEE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548682  86 FAHWFRGHVaAFPVVQARLTSYLDANDaDIWLITGSPqTLVEQVYFDTPWLPrvNLIATQ--ISRGYGGWVLTLR-CLGH 162
Cdd:cd02612   76 FVEEYILRV-LYPEARELIAWHKAAGH-DVVLISASP-EELVAPIARKLGID--NVLGTQleTEDGRYTGRIIGPpCYGE 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 658548682 163 EKVVQLEKRI---GTPLRLYSGYSDSKQDNPLLYFCQHRWRVTPS 204
Cdd:cd02612  151 GKVKRLREWLaeeGIDLKDSYAYSDSINDLPMLEAVGHPVAVNPD 195
HAD pfam12710
haloacid dehalogenase-like hydrolase;
9-192 1.72e-10

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 57.93  E-value: 1.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548682    9 VFFDLDGTLHQQDMFGTFMRYLLRRQPLNALLVLPLLPVIGIALLVkGRAARWPMSLLLWGCTFGHSEARLKQLEKDFAH 88
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALLRRGGPDLWRALLVLLLLALLRLL-GRLSRAGARELLRALLAGLPEEDAAELERFVAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548682   89 WFRGhvAAFPVVQARLTSYLDANDAdIWLITGSPQTLVEqvyfdtPWLPRV---NLIATQISRGYGGWVLTLR-----CL 160
Cdd:pfam12710  80 VALP--RLHPGALELLAAHRAAGDR-VVVVTGGLRPLVE------PVLAELgfdEVLATELEVDDGRFTGELRligppCA 150

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 658548682  161 GHEKVVQLEKRIG------TPLRLYsGYSDSKQDNPLL 192
Cdd:pfam12710 151 GEGKVRRLRAWLAarglglDLADSV-AYGDSPSDLPML 187
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 9-207 1.68e-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: 49.65  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548682    9 VFFDLDGTLHQQDMFGTFMRYLLRRQPLNALLVLPLLPVIGIALLVKGRAARWPMSLLLWGCTFGHSEARLKQLEKDFAH 88
Cdd:TIGR01490   2 AFFDFDGTLTAKDTLFIFLKFLASKNILFEELRLPKVLARFEFFLNRGLDYMAYYRAFALDALAGLLEEDVRAIVEEFVN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548682   89 -WFRGHVaaFPVVQARLTSYLDANDaDIWLITGSPQTLVEQVY----FDtpwlprvNLIATQISRG----YGGWVLTLRC 159
Cdd:TIGR01490  82 qKIESIL--YPEARDLIRWHKAEGH-TIVLVSASLTILVKPLArilgID-------NAIGTRLEESedgiYTGNIDGNNC 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 658548682  160 LGHEKVVQL-----EKRIgtPLRLYSGYSDSKQDNPLLYFCQHRWRVTPSGEL 207
Cdd:TIGR01490 152 KGEGKVHALaellaEEQI--DLKDSYAYGDSISDLPLLSLVGHPYVVNPDKKL 202
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 6-192 1.62e-06

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 47.14  E-value: 1.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548682   6 RRVVFFDLDGTLHQQDMFGTFMRYLLRRQPLNALLVLPLLPVIgIALLVKGRAARWPMSLLLWGCTFGHSEARLKQLekd 85
Cdd:COG0560    3 MRLAVFDLDGTLIAGESIDELARFLGRRGLVDRREVLEEVAAI-TERAMAGELDFEESLRFRVALLAGLPEEELEEL--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548682  86 FAHWFRGHVAAFPVVQARLTSYLDANDaDIWLITGSPQTLVEqvyfdtPWLPRVNL---IATQ--ISRG-YGGWVLTLRC 159
Cdd:COG0560   79 AERLFEEVPRLYPGARELIAEHRAAGH-KVAIVSGGFTFFVE------PIAERLGIdhvIANEleVEDGrLTGEVVGPIV 151

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 658548682 160 LGHEKVVQLE---KRIGTPLRLYSGYSDSKQDNPLL 192
Cdd:COG0560  152 DGEGKAEALRelaAELGIDLEQSYAYGDSANDLPML 187
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 7-129 9.35e-04

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: 38.72  E-value: 9.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548682    7 RVVFFDLDGTL-HQQDMFGTFMRYLLRRQPLNAllvLPLLPVIGIALLVKGRAARWPMSLLLWGCTFGHSEARLKQLEKD 85
Cdd:pfam00702   2 KAVVFDLDGTLtDGEPVVTEAIAELASEHPLAK---AIVAAAEDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 658548682   86 FAHWFRGHVAAFPVVQARLTSYLDANDA---------DIWLITGSPQTLVEQV 129
Cdd:pfam00702  79 GLTVVLVELLGVIALADELKLYPGAAEAlkalkergiKVAILTGDNPEAAEAL 131
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 8-193 7.86e-03

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


Pssm-ID: 273653 [Multi-domain]  Cd Length: 177  Bit Score: 35.79  E-value: 7.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548682    8 VVFFDLDGTLHQQDmfgTFMRYLLRRQPLNALLVLPLLPVIGIALLVKGRAARwPMSLLLWgctfghseARLKQLEKDFa 87
Cdd:TIGR01488   1 LAIFDFDGTLTRQD---SLIDLLAKLLGTNDEVIELTRLAPSGRISFEDALGR-RLALLHR--------SRSEEVAKEF- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548682   88 hwFRGHVAAFPVVQARLtSYLDANDADIWLITGSPQTLVEqvyfdtPWLPR---VNLIATQIS---RGY--GGWVLTLRC 159
Cdd:TIGR01488  68 --LARQVALRPGARELI-SWLKERGIDTVIVSGGFDFFVE------PVAEKlgiDDVFANRLEfddNGLltGPIEGQVNP 138

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 658548682  160 LGHEK---VVQLEKRIGTPLRLYSGYSDSKQDNPLLY 193
Cdd:TIGR01488 139 EGECKgkvLKELLEESKITLKKIIAVGDSVNDLPMLK 175
 
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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