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Conserved domains on  [gi|19173657|ref|NP_597460|]
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similarity to HYPOTHETICAL PROTEIN YGX4_yeast [Encephalitozoon cuniculi GB-M1]

Protein Classification

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 ...
105-279 1.69e-26

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 TIGR01993:

Pssm-ID: 354816 [Multi-domain]  Cd Length: 183  Bit Score: 102.81  E-value: 1.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657   105 FLYDIDDTLYHPSNNL-QEMERKflVEKFLSLKEGSTPEmfeeqlNVALLYSALFYKYG----------NLSLEEYWEMI 173
Cdd:TIGR01993   3 WFFDLDNTLYPHSAGIfLQIDRN--ITEFVAARLKLSPE------EARVLRKDYYKEYGttlaglmilhEIDADEYLRYV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657   174 SEFDYLQYLSPDMDLRNFLLSMKNvRKCCFTNGPRDRAENILTKIGILDCFEVVVCIGKYDKTFCCKPLSESYEFVTKVL 253
Cdd:TIGR01993  75 HGRLPYDKLKPDPELRNLLLRLPG-RKIIFTNGDRAHARRALRRLGIEDCFDGIFCFDTANPDLLPKPSPQAYEKALREA 153
                         170       180
                  ....*....|....*....|....*.
gi 19173657   254 GIEsPGNVYFFDDSENNIIKAREIGW 279
Cdd:TIGR01993 154 GVD-PERAIFFDDSARNIAAGKALGM 178
 
Name Accession Description Interval E-value
Pyr-5-nucltdase TIGR01993
pyrimidine 5'-nucleotidase; This family of proteins includes the SDT1/SSM1 gene from yeast ...
105-279 1.69e-26

pyrimidine 5'-nucleotidase; This family of proteins includes the SDT1/SSM1 gene from yeast which has been shown to code for a pyrimidine (UMP/CMP) 5'nucleotidase. The family spans plants, fungi and a small number of bacteria. These enzymes are members of the haloacid dehalogenase (HAD) superfamily of hydrolases, specifically the IA subfamily (variant 3, TIGR01509).


Pssm-ID: 273917 [Multi-domain]  Cd Length: 183  Bit Score: 102.81  E-value: 1.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657   105 FLYDIDDTLYHPSNNL-QEMERKflVEKFLSLKEGSTPEmfeeqlNVALLYSALFYKYG----------NLSLEEYWEMI 173
Cdd:TIGR01993   3 WFFDLDNTLYPHSAGIfLQIDRN--ITEFVAARLKLSPE------EARVLRKDYYKEYGttlaglmilhEIDADEYLRYV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657   174 SEFDYLQYLSPDMDLRNFLLSMKNvRKCCFTNGPRDRAENILTKIGILDCFEVVVCIGKYDKTFCCKPLSESYEFVTKVL 253
Cdd:TIGR01993  75 HGRLPYDKLKPDPELRNLLLRLPG-RKIIFTNGDRAHARRALRRLGIEDCFDGIFCFDTANPDLLPKPSPQAYEKALREA 153
                         170       180
                  ....*....|....*....|....*.
gi 19173657   254 GIEsPGNVYFFDDSENNIIKAREIGW 279
Cdd:TIGR01993 154 GVD-PERAIFFDDSARNIAAGKALGM 178
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
105-279 1.81e-26

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p and Sdt1p; This family includes Saccharomyces cerevisiae Phm8p (phosphate metabolism protein 8) and Sdt1p (Suppressor of disruption of TFIIS). Phm8p participates in the ribose salvage pathway, it catalyzes the dephosphorylation of nucleotide monophosphates to nucleosides, its preferred substrates are nucleotide monophosphates AMP, GMP, CMP, and UMP. Phm8p is also a lysophosphatidic acid phosphatase, dephosphorylating lysophosphatidic acids (LPAs) to monoacylglycerol in response to phosphate starvation. Sdt1p is a pyrimidine and pyridine-specific 5'-nucleotidase; it is an NMN/NaMN 5'-nucleotidases involved in the production of nicotinamide riboside and nicotinic acid riboside, and is a pyrimidine 5'-nucleotidase with high specificity for UMP and 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: 319791  Cd Length: 182  Bit Score: 102.71  E-value: 1.81e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657 105 FLYDIDDTLYHPSNNLQEMERKFLVEkFLSLKEGSTPEMFEEqlnvalLYSALFYKYG----------NLSLEEYWEM-I 173
Cdd:cd02604   2 WFFDLDNTLYPLSTGLFDQIQARITE-FVATKLGLSPEEARR------LRKSYYKEYGttlrglmaehGIDPDEFLDRvV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657 174 SEFDYlQYLSPDMDLRNFLLSMKNvRKCCFTNGPRDRAENILTKIGILDCFEVVVCIgKYDKtFCCKPLSESYEFVTKVL 253
Cdd:cd02604  75 HLILY-DHLKPDPKLRNLLLALPG-RKIIFTNASKNHAIRVLKRLGLADLFDGIFDI-EYAG-PDPKPHPAAFEKAIREA 150
                       170       180
                ....*....|....*....|....*.
gi 19173657 254 GIeSPGNVYFFDDSENNIIKAREIGW 279
Cdd:cd02604 151 GL-DPKRAAFFDDSIRNLLAAKALGM 175
YigB COG1011
FMN phosphatase YigB, HAD superfamily [Coenzyme transport and metabolism];
103-318 1.09e-17

FMN phosphatase YigB, HAD superfamily [Coenzyme transport and metabolism];


Pssm-ID: 223943 [Multi-domain]  Cd Length: 229  Bit Score: 80.33  E-value: 1.09e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657 103 ILFlyDIDDTLYHPSNNLQEMERKFLVEK----------FLSLKEGSTPEMF--EEQLNVALLYSALFYKYGNLSLEEYW 170
Cdd:COG1011   7 ILF--DLDGTLLDFDSAEFRAVLAEFAEIgvpetleelaLLKLIEKLEARFLrgEYTGEYGLTLERLLELLERLLGDEDA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657 171 EMISEFD--YLQYLSPDMDLRNFLLSMKN-VRKCCFTNGPRDRAENILTKIGILDCFEVVVCIGKYDktfCCKPLSESYE 247
Cdd:COG1011  85 ELVEELLaaLAKLLPDYPEALEALKELGKkYKLGILTNGARPHQERKLRQLGLLDYFDAVFISEDVG---VAKPDPEIFE 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19173657 248 FVTKVLGIEsPGNVYFFDDSENNIIK-AREIGWNG-WLITRDCNILDvssrlfQAICNDASSPHFQEVPPDIS 318
Cdd:COG1011 162 YALEKLGVP-PEEALFVGDSLENDILgARALGMKTvWINRGGKPLPD------ALEAPDYEISSLAELLDLLE 227
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
104-278 8.01e-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 Pseudomonas sp. (S)-2-haloacid dehalogenase 1. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteristic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 334216 [Multi-domain]  Cd Length: 190  Bit Score: 60.28  E-value: 8.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657   104 LFLYDIDDTLYHPSNNLQEMERK------------------FLVEKFLSLKEGSTPEMFEEQLNVALLYSALFYKYGNLS 165
Cdd:pfam00702   3 AVVFDLDGTLTDGEPVVTEAIAElraaglakaivaaaedlpIPVEDFTARLLLGKRDWLEELGILRGLVETLEAAGLTVV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657   166 LEEYWEMISEFDYLQyLSPDmdLRNFL--LSMKNVRKCCFTNGPRDRAENILTKIGILDCFEVVVCigkYDKTFCCKPLS 243
Cdd:pfam00702  83 LVELLGVIALADELK-LYPG--AAEALkaLKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVIS---GDDVGVGKPKP 156
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 19173657   244 ESYEFVTKVLGIEsPGNVYFFDDSENNIIKAREIG 278
Cdd:pfam00702 157 EIYLAALERLGVK-PEEVLMVGDGVNDIPAAKAAG 190
 
Name Accession Description Interval E-value
Pyr-5-nucltdase TIGR01993
pyrimidine 5'-nucleotidase; This family of proteins includes the SDT1/SSM1 gene from yeast ...
105-279 1.69e-26

pyrimidine 5'-nucleotidase; This family of proteins includes the SDT1/SSM1 gene from yeast which has been shown to code for a pyrimidine (UMP/CMP) 5'nucleotidase. The family spans plants, fungi and a small number of bacteria. These enzymes are members of the haloacid dehalogenase (HAD) superfamily of hydrolases, specifically the IA subfamily (variant 3, TIGR01509).


Pssm-ID: 273917 [Multi-domain]  Cd Length: 183  Bit Score: 102.81  E-value: 1.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657   105 FLYDIDDTLYHPSNNL-QEMERKflVEKFLSLKEGSTPEmfeeqlNVALLYSALFYKYG----------NLSLEEYWEMI 173
Cdd:TIGR01993   3 WFFDLDNTLYPHSAGIfLQIDRN--ITEFVAARLKLSPE------EARVLRKDYYKEYGttlaglmilhEIDADEYLRYV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657   174 SEFDYLQYLSPDMDLRNFLLSMKNvRKCCFTNGPRDRAENILTKIGILDCFEVVVCIGKYDKTFCCKPLSESYEFVTKVL 253
Cdd:TIGR01993  75 HGRLPYDKLKPDPELRNLLLRLPG-RKIIFTNGDRAHARRALRRLGIEDCFDGIFCFDTANPDLLPKPSPQAYEKALREA 153
                         170       180
                  ....*....|....*....|....*.
gi 19173657   254 GIEsPGNVYFFDDSENNIIKAREIGW 279
Cdd:TIGR01993 154 GVD-PERAIFFDDSARNIAAGKALGM 178
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
105-279 1.81e-26

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p and Sdt1p; This family includes Saccharomyces cerevisiae Phm8p (phosphate metabolism protein 8) and Sdt1p (Suppressor of disruption of TFIIS). Phm8p participates in the ribose salvage pathway, it catalyzes the dephosphorylation of nucleotide monophosphates to nucleosides, its preferred substrates are nucleotide monophosphates AMP, GMP, CMP, and UMP. Phm8p is also a lysophosphatidic acid phosphatase, dephosphorylating lysophosphatidic acids (LPAs) to monoacylglycerol in response to phosphate starvation. Sdt1p is a pyrimidine and pyridine-specific 5'-nucleotidase; it is an NMN/NaMN 5'-nucleotidases involved in the production of nicotinamide riboside and nicotinic acid riboside, and is a pyrimidine 5'-nucleotidase with high specificity for UMP and 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: 319791  Cd Length: 182  Bit Score: 102.71  E-value: 1.81e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657 105 FLYDIDDTLYHPSNNLQEMERKFLVEkFLSLKEGSTPEMFEEqlnvalLYSALFYKYG----------NLSLEEYWEM-I 173
Cdd:cd02604   2 WFFDLDNTLYPLSTGLFDQIQARITE-FVATKLGLSPEEARR------LRKSYYKEYGttlrglmaehGIDPDEFLDRvV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657 174 SEFDYlQYLSPDMDLRNFLLSMKNvRKCCFTNGPRDRAENILTKIGILDCFEVVVCIgKYDKtFCCKPLSESYEFVTKVL 253
Cdd:cd02604  75 HLILY-DHLKPDPKLRNLLLALPG-RKIIFTNASKNHAIRVLKRLGLADLFDGIFDI-EYAG-PDPKPHPAAFEKAIREA 150
                       170       180
                ....*....|....*....|....*.
gi 19173657 254 GIeSPGNVYFFDDSENNIIKAREIGW 279
Cdd:cd02604 151 GL-DPKRAAFFDDSIRNLLAAKALGM 175
YigB COG1011
FMN phosphatase YigB, HAD superfamily [Coenzyme transport and metabolism];
103-318 1.09e-17

FMN phosphatase YigB, HAD superfamily [Coenzyme transport and metabolism];


Pssm-ID: 223943 [Multi-domain]  Cd Length: 229  Bit Score: 80.33  E-value: 1.09e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657 103 ILFlyDIDDTLYHPSNNLQEMERKFLVEK----------FLSLKEGSTPEMF--EEQLNVALLYSALFYKYGNLSLEEYW 170
Cdd:COG1011   7 ILF--DLDGTLLDFDSAEFRAVLAEFAEIgvpetleelaLLKLIEKLEARFLrgEYTGEYGLTLERLLELLERLLGDEDA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657 171 EMISEFD--YLQYLSPDMDLRNFLLSMKN-VRKCCFTNGPRDRAENILTKIGILDCFEVVVCIGKYDktfCCKPLSESYE 247
Cdd:COG1011  85 ELVEELLaaLAKLLPDYPEALEALKELGKkYKLGILTNGARPHQERKLRQLGLLDYFDAVFISEDVG---VAKPDPEIFE 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19173657 248 FVTKVLGIEsPGNVYFFDDSENNIIK-AREIGWNG-WLITRDCNILDvssrlfQAICNDASSPHFQEVPPDIS 318
Cdd:COG1011 162 YALEKLGVP-PEEALFVGDSLENDILgARALGMKTvWINRGGKPLPD------ALEAPDYEISSLAELLDLLE 227
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
105-280 9.03e-17

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: 76.69  E-value: 9.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657   105 FLYDIDDTLYHPSNN---LQEMERKFLVEKFLSLKEGSTPEMFEEQLNVallysalfyKYGNLSLEEYWEMISEFDYLQY 181
Cdd:TIGR01509   2 ILFDLDGVLVDTEFAiakLINREELGLVPDELGVSAVGRLELALRRFKA---------QYGRTISPEDAQLLYKQLFYEQ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657   182 ------LSPDMDLRNFL--LSMKNVRKCCFTNGPRDRAENiLTKIGILDCFEVVVCIGKYDKtfcCKPLSESYEFVTKVL 253
Cdd:TIGR01509  73 ieeeakLKPLPGVRALLeaLRARGKKLALLTNSPRAHKLV-LALLGLRDLFDVVIDSSDVGL---GKPDPDIYLQALKAL 148
                         170       180
                  ....*....|....*....|....*..
gi 19173657   254 GIEsPGNVYFFDDSENNIIKAREIGWN 280
Cdd:TIGR01509 149 GLE-PSECVFVDDSPAGIEAAKAAGMH 174
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
104-278 8.01e-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 Pseudomonas sp. (S)-2-haloacid dehalogenase 1. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteristic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 334216 [Multi-domain]  Cd Length: 190  Bit Score: 60.28  E-value: 8.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657   104 LFLYDIDDTLYHPSNNLQEMERK------------------FLVEKFLSLKEGSTPEMFEEQLNVALLYSALFYKYGNLS 165
Cdd:pfam00702   3 AVVFDLDGTLTDGEPVVTEAIAElraaglakaivaaaedlpIPVEDFTARLLLGKRDWLEELGILRGLVETLEAAGLTVV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657   166 LEEYWEMISEFDYLQyLSPDmdLRNFL--LSMKNVRKCCFTNGPRDRAENILTKIGILDCFEVVVCigkYDKTFCCKPLS 243
Cdd:pfam00702  83 LVELLGVIALADELK-LYPG--AAEALkaLKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVIS---GDDVGVGKPKP 156
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 19173657   244 ESYEFVTKVLGIEsPGNVYFFDDSENNIIKAREIG 278
Cdd:pfam00702 157 EIYLAALERLGVK-PEEVLMVGDGVNDIPAAKAAG 190
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
106-285 5.17e-10

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: 57.74  E-value: 5.17e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657 106 LYDIDDTL--YHPSNNLQEMERKfLVEKFLSLKEGSTPEMFEEQLNVALLYSALFYK-----YG----NLSLEEYWEMIS 174
Cdd:cd02603   5 LFDFGGVLidPDPAAAVARFEAL-TGEPSEFVLDTEGLAGAFLELERGRITEEEFWEelreeLGrplsAELFEELVLAAV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657 175 EFDylqylsPDM-----DLRnfllsMKNVRKCCFTNGPRDRAENILTKI-GILDCFEVVV--C-IGkydktfCCKPLSES 245
Cdd:cd02603  84 DPN------PEMldlleALR-----AKGYKVYLLSNTWPDHFKFQLELLpRRGDLFDGVVesCrLG------VRKPDPEI 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 19173657 246 YEFVTKVLGIeSPGNVYFFDDSENNIIKAREIGWNGWLIT 285
Cdd:cd02603 147 YQLALERLGV-KPEEVLFIDDREENVEAARALGIHAILVT 185
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
185-284 3.28e-09

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: 53.55  E-value: 3.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657 185 DMD----LRNFL--LSMKNVRKCCFTNGPRDRAENILTKIGILDCFEVVVCigkYDKTFCCKPLSESYEFVTKVLGIeSP 258
Cdd:cd01427   5 DLDgtllAVELLkrLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIG---SDGGGTPKPKPKPLLLLLLKLGV-DP 80
                        90       100
                ....*....|....*....|....*.
gi 19173657 259 GNVYFFDDSENNIIKAREIGWNGWLI 284
Cdd:cd01427  81 EEVLFVGDSENDIEAARAAGGRTVAV 106
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
103-278 5.81e-07

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; 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/E), (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 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe 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 relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 48.55  E-value: 5.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657   103 ILFlyDIDDTLYHPSnnlqEMERKFLVEKFLslKEGSTPEMFEEQLNVALLYSALFYKYGNLSLEEYWEMI-SEFDYLQY 181
Cdd:TIGR01549   2 ILF--DIDGTLVDIK----FAIRRAFPQTFE--EFGLDPASFKALKQAGGLAEEEWYRIATSALEELQGRFwSEYDAEEA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657   182 LSPDM-DLRNFLLSmKNVRKCCFTNGPRDRAENILTKIGILDCFEVVVCIGKydktFCCKPLSESYEFVTKVLGIESPgn 260
Cdd:TIGR01549  74 YIRGAaDLLARLKS-AGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDE----PGSKPEPEIFLAALESLGVPPE-- 146
                         170
                  ....*....|....*...
gi 19173657   261 VYFFDDSENNIIKAREIG 278
Cdd:TIGR01549 147 VLHVGDNLNDIEGARNAG 164
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
103-278 2.46e-05

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


Pssm-ID: 223620 [Multi-domain]  Cd Length: 220  Bit Score: 44.37  E-value: 2.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657 103 ILFlyDIDDTL------YHPSnnLQEMERKFLV-----EKFLSLKEGSTPEMFEEqlnvallysalfyKYGNLSLEEYWE 171
Cdd:COG0546   7 ILF--DLDGTLvdsaedILRA--FNAALAELGLppldeEEIRQLIGLGLDELIER-------------LLGEADEEAAAE 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657 172 MISEFD--YLQYLSPDMDLRNF--------LLSMKNVRKCCFTNGPRDRAENILTKIGILDCFEVVVCigkYDKTFCCKP 241
Cdd:COG0546  70 LVERLReeFLTAYAELLESRLFpgvkellaALKSAGYKLGIVTNKPERELDILLKALGLADYFDVIVG---GDDVPPPKP 146
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 19173657 242 LSESYEFVTKVLGIEsPGNVYFFDDSENNIIKAREIG 278
Cdd:COG0546 147 DPEPLLLLLEKLGLD-PEEALMVGDSLNDILAAKAAG 182
YcjU COG0637
Beta-phosphoglucomutase or related phosphatase, HAD superfamily [Carbohydrate transport and ...
164-278 4.77e-05

Beta-phosphoglucomutase or related phosphatase, HAD superfamily [Carbohydrate transport and metabolism, General function prediction only];


Pssm-ID: 223710 [Multi-domain]  Cd Length: 221  Bit Score: 43.57  E-value: 4.77e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657 164 LSLEEYWEMISEFDYLQYLSPDMDLRNFLLSMK--NVRKCCFTNGPRDRAENILTKIGILDCFEVVVCIGKYDKTfccKP 241
Cdd:COG0637  67 LAELERLLYEAEALELEGLKPIPGVVELLEQLKarGIPLAVASSSPRRAAERVLARLGLLDYFDVIVTADDVARG---KP 143
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 19173657 242 LSESYEFVTKVLGIeSPGNVYFFDDSENNIIKAREIG 278
Cdd:COG0637 144 APDIYLLAAERLGV-DPEECVVVEDSPAGIQAAKAAG 179
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
103-278 5.75e-05

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 315982 [Multi-domain]  Cd Length: 178  Bit Score: 42.95  E-value: 5.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657   103 ILFlyDIDDTL-------YHPSNN-LQEMERKFLVEKFLSLKEGSTPEMFEEQLNVallysalfYKYGNLSLEEYWEMIS 174
Cdd:pfam13419   1 IIF--DFDGTLadteeliIKSFNYlLEEFGYGELSEEEILKFIGLTLREIFRYLGV--------SEDEDEKIEFYLRKYN 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657   175 EFDYLQYLSPDMDLRNFL--LSMKNVRKCCFTNGPRDRAENILTKIGILDCFEVVVCigkYDKTFCCKPLSESYEFVTKV 252
Cdd:pfam13419  71 EELHDKLVKPYPGIKELLeeLKEQGYKLGIVTSKSRENVEEGLEQLGLEDYFDVIVG---GDDVEGKKPDPDPILKALEQ 147
                         170       180
                  ....*....|....*....|....*.
gi 19173657   253 LGIEsPGNVYFFDDSENNIIKAREIG 278
Cdd:pfam13419 148 LGLK-PEEVIYVGDSPRDIEAAKNAG 172
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
203-292 8.85e-05

L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. 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: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 42.64  E-value: 8.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657 203 FTNGPRDRAENILTKIGILDCFEVVVC---IGKYdktfccKPLSESYEFVTKVLGIEsPGNVYFFDDSENNIIKAREIGW 279
Cdd:cd02588 113 LSNGSPDLIEDVVANAGLRDLFDAVLSaedVRAY------KPAPAVYELAAERLGVP-PDEILHVASHAWDLAGARALGL 185
                        90
                ....*....|...
gi 19173657 280 NGWLITRDCNILD 292
Cdd:cd02588 186 RTAWINRPGEVPD 198
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
196-278 5.09e-04

uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized Bacillus subtilis YhcW; This subfamily includes the uncharacterized Bacillus subtilis YhcW. It belongs to the beta-phosphoglucomutase-like family whose other 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. 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: 319859 [Multi-domain]  Cd Length: 169  Bit Score: 39.93  E-value: 5.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173657 196 KNVRKCCFTNGPRDRAENILTKIGILDCFEVVVCIGKYDKTfccKPLSESYEFVTKVLGIeSPGNVYFFDDSENNIIKAR 275
Cdd:cd16423  59 KGIKLAVASSSPRRWIEPHLERLGLLDYFEVIVTGDDVEKS---KPDPDLYLEAAERLGV-NPEECVVIEDSRNGVLAAK 134

                ...
gi 19173657 276 EIG 278
Cdd:cd16423 135 AAG 137
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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