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Conserved domains on  [gi|1002308657|ref|XP_015617720|]
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uncharacterized protein [Oryza sativa Japonica Group]

Protein Classification

HAD family hydrolase( domain architecture ID 11576243)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_MDP-1_like cd07501
eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to ...
 53-177 3.70e-46

eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to Bacillus cereus phosphonoacetaldehyde hydrolase and Streptomyces FkbH; This family includes eukaryotic magnesium-dependent phosphatase-1 (MDP-1) which is most likely a phosphotyrosine phosphatase catalyzing the dephosphorylation of tyrosine-phosphorylated proteins, Bacillus cereus phosphonoacetaldehyde hydrolase (phosphonatase)which catalyzes the hydrolysis of phosphonoacetaldehyde to acetaldehyde and phosphate using Mg(II) as cofactor, and sequences annotated as FkbH including BafAIV an FkbH-like protein from Streptomyces griseus encoded in ORF12 of the bafilomycin synthesis gene cluster. 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: 319804 [Multi-domain]  Cd Length: 129  Bit Score: 149.42  E-value: 3.70e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657  53 PRLVVFDLDHTLWPFQCD-------RLPKDEPPYLYPQARGILKALKDRGIEMAIASRASRKKGvAKAFLEKLGIHFMFG 125
Cdd:cd07501     1 PKCLVFDLDYTLWPGVVDehgippfKDRGGKEVSLYPDAQEILKELKERGILLAVASRNNEFDH-ANEVLEKLDLKELFD 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1002308657 126 AQEIFytWSPKNEHFQSIHRKTGVPFKSMLFFDDEARNIIATRKLGVSCVLV 177
Cdd:cd07501    80 AFEIY--PGSKSSHFRKIAKELGIGFDSMVFFDDEPRNREEVSEGGVTCILV 129
 
Name Accession Description Interval E-value
HAD_MDP-1_like cd07501
eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to ...
 53-177 3.70e-46

eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to Bacillus cereus phosphonoacetaldehyde hydrolase and Streptomyces FkbH; This family includes eukaryotic magnesium-dependent phosphatase-1 (MDP-1) which is most likely a phosphotyrosine phosphatase catalyzing the dephosphorylation of tyrosine-phosphorylated proteins, Bacillus cereus phosphonoacetaldehyde hydrolase (phosphonatase)which catalyzes the hydrolysis of phosphonoacetaldehyde to acetaldehyde and phosphate using Mg(II) as cofactor, and sequences annotated as FkbH including BafAIV an FkbH-like protein from Streptomyces griseus encoded in ORF12 of the bafilomycin synthesis gene cluster. 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: 319804 [Multi-domain]  Cd Length: 129  Bit Score: 149.42  E-value: 3.70e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657  53 PRLVVFDLDHTLWPFQCD-------RLPKDEPPYLYPQARGILKALKDRGIEMAIASRASRKKGvAKAFLEKLGIHFMFG 125
Cdd:cd07501     1 PKCLVFDLDYTLWPGVVDehgippfKDRGGKEVSLYPDAQEILKELKERGILLAVASRNNEFDH-ANEVLEKLDLKELFD 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1002308657 126 AQEIFytWSPKNEHFQSIHRKTGVPFKSMLFFDDEARNIIATRKLGVSCVLV 177
Cdd:cd07501    80 AFEIY--PGSKSSHFRKIAKELGIGFDSMVFFDDEPRNREEVSEGGVTCILV 129
Acid_PPase pfam12689
Acid Phosphatase; This family contains phosphatase enzymes and other proteins of the HAD ...
 52-196 1.50e-42

Acid Phosphatase; This family contains phosphatase enzymes and other proteins of the HAD superfamily. It includes MDP-1 which is a eukaryotic magnesium-dependent acid phosphatase.


Pssm-ID: 372256  Cd Length: 169  Bit Score: 141.21  E-value: 1.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657  52 LPRLVVFDLDHTLWPFQCDRLpkDEPPY------------------LYPQARGILKALKDRGIEMAIASRASRKKgVAKA 113
Cdd:pfam12689   2 LPKLIVFDLDYTLWPFWVDTH--VSPPFkkvsngsrvvdrrgeelsLYPDVPSILQELKTRGVTLAAASRTDAPD-WARE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657 114 FLEKLGI----------HFMFGAQEIFYtwSPKNEHFQSIHRKTGVPFKSMLFFDDEARNIIATRKLGVSCVLVDTGITL 183
Cdd:pfam12689  79 LLKLLHIndgpgdtvpaIDYFDDLEIYP--GSKTKHFTKILKKSGIPYSDMLFFDDESRNIDVVSRLGVTFVLVPDGLTR 156

                         170
                  ....*....|...
gi 1002308657 184 EKLRTGLSNYANR 196
Cdd:pfam12689 157 EEFERGLRKWRKR 169
HAD-SF-IIIC TIGR01681
HAD-superfamily phosphatase, subfamily IIIC; This model represents the IIIC subfamily of the ...
 54-171 8.37e-15

HAD-superfamily phosphatase, subfamily IIIC; This model represents the IIIC subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate nucleophile hydrolases. Subfamily III (also including IIIA - TIGR01662 and IIIB - pfam03767) contains sequences which do not contain either of the insert domains (between the 1st and 2nd conserved catalytic motifs, subfamily I - TIGR01493, TIGR01509, TIGR01549, TIGR01488, TIGR01494, TIGR01658, TIGR01544 and TIGR01545, or between the 2nd and 3rd, subfamily II - TIGR01460 and TIGR01484). Subfamily IIIC contains five relatively distantly related clades: a family of viral proteins (TIGR01684), a family of eukaryotic proteins called MDP-1 and a family of archaeal proteins most closely related to MDP-1 (TIGR01685), a family of bacteria including the Streptomyces FkbH protein (TIGR01686), and a small clade including the Pasteurella BcbF and EcbF proteins. The overall lack of species overlap among these clades may indicate a conserved function, but the degree of divergence between the clades and the differences in archetecture outside of the domain in some clades warns against such a conclusion. No member of this subfamily is characterized with respect to function, however the MDP-1 protein is a characterized phosphatase. All of the characterized enzymes within subfamily III are phosphatases, and all of the active site residues characteristic of HAD-superfamily phosphatases are present in subfamily IIIC.


Pssm-ID: 273752 [Multi-domain]  Cd Length: 128  Bit Score: 68.23  E-value: 8.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657  54 RLVVFDLDHTLWPFQCD---RLPKDEPPYLYPQARGILKALKDRGIEMAIASRASRKKgVAKAFLeKLGIHF-------- 122
Cdd:TIGR01681   1 KVIVFDLDNTLWTGENIvvgEDPIIDLEVTIKEIRDKLQTLKKNGFLLALASYNDDPH-VAYELL-KIFEDFgiifplae 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1002308657 123 MFGAQEIFYtWSPKNEHFQSIHRKTGVP--FKSMLFFDDEARNIIATRKLG 171
Cdd:TIGR01681  79 YFDPLTIGY-WLPKSPRLVEIALKLNGVlkPKSILFVDDRPDNNEEVDYYL 128
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
80-180 3.04e-11

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 60.33  E-value: 3.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657  80 LYPQARGILKALKDRGIEMAIASRASRKkgVAKAFLEKLGIHFMFGA---QEIFYTWSPKNEHFQSIHRKTGVPFKSMLF 156
Cdd:COG0546    85 LFPGVRELLEALKARGIKLAVVTNKPRE--FAERLLEALGLDDYFDAivgGDDVPPAKPKPEPLLEALERLGLDPEEVLM 162

                          90       100
                  ....*....|....*....|....
gi 1002308657 157 FDDEARNIIATRKLGVSCVLVDTG 180
Cdd:COG0546   163 VGDSPHDIEAARAAGVPFIGVTWG 186
PRK13225 PRK13225
phosphoglycolate phosphatase; Provisional
 80-180 1.80e-03

phosphoglycolate phosphatase; Provisional


Pssm-ID: 106187 [Multi-domain]  Cd Length: 273  Bit Score: 38.54  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657  80 LYPQARGILKALKDRGIEMAIASRASRKKgvAKAFLEKLGIHFMFGAQEIFYTWSPKNEHFQSIHRKTGVPFKSMLFFDD 159
Cdd:PRK13225  143 LFPGVADLLAQLRSRSLCLGILSSNSRQN--IEAFLQRQGLRSLFSVVQAGTPILSKRRALSQLVAREGWQPAAVMYVGD 220

                          90       100
                  ....*....|....*....|.
gi 1002308657 160 EARNIIATRKLGVSCVLVDTG 180
Cdd:PRK13225  221 ETRDVEAARQVGLIAVAVTWG 241
 
Name Accession Description Interval E-value
HAD_MDP-1_like cd07501
eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to ...
 53-177 3.70e-46

eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to Bacillus cereus phosphonoacetaldehyde hydrolase and Streptomyces FkbH; This family includes eukaryotic magnesium-dependent phosphatase-1 (MDP-1) which is most likely a phosphotyrosine phosphatase catalyzing the dephosphorylation of tyrosine-phosphorylated proteins, Bacillus cereus phosphonoacetaldehyde hydrolase (phosphonatase)which catalyzes the hydrolysis of phosphonoacetaldehyde to acetaldehyde and phosphate using Mg(II) as cofactor, and sequences annotated as FkbH including BafAIV an FkbH-like protein from Streptomyces griseus encoded in ORF12 of the bafilomycin synthesis gene cluster. 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: 319804 [Multi-domain]  Cd Length: 129  Bit Score: 149.42  E-value: 3.70e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657  53 PRLVVFDLDHTLWPFQCD-------RLPKDEPPYLYPQARGILKALKDRGIEMAIASRASRKKGvAKAFLEKLGIHFMFG 125
Cdd:cd07501     1 PKCLVFDLDYTLWPGVVDehgippfKDRGGKEVSLYPDAQEILKELKERGILLAVASRNNEFDH-ANEVLEKLDLKELFD 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1002308657 126 AQEIFytWSPKNEHFQSIHRKTGVPFKSMLFFDDEARNIIATRKLGVSCVLV 177
Cdd:cd07501    80 AFEIY--PGSKSSHFRKIAKELGIGFDSMVFFDDEPRNREEVSEGGVTCILV 129
Acid_PPase pfam12689
Acid Phosphatase; This family contains phosphatase enzymes and other proteins of the HAD ...
 52-196 1.50e-42

Acid Phosphatase; This family contains phosphatase enzymes and other proteins of the HAD superfamily. It includes MDP-1 which is a eukaryotic magnesium-dependent acid phosphatase.


Pssm-ID: 372256  Cd Length: 169  Bit Score: 141.21  E-value: 1.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657  52 LPRLVVFDLDHTLWPFQCDRLpkDEPPY------------------LYPQARGILKALKDRGIEMAIASRASRKKgVAKA 113
Cdd:pfam12689   2 LPKLIVFDLDYTLWPFWVDTH--VSPPFkkvsngsrvvdrrgeelsLYPDVPSILQELKTRGVTLAAASRTDAPD-WARE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657 114 FLEKLGI----------HFMFGAQEIFYtwSPKNEHFQSIHRKTGVPFKSMLFFDDEARNIIATRKLGVSCVLVDTGITL 183
Cdd:pfam12689  79 LLKLLHIndgpgdtvpaIDYFDDLEIYP--GSKTKHFTKILKKSGIPYSDMLFFDDESRNIDVVSRLGVTFVLVPDGLTR 156

                         170
                  ....*....|...
gi 1002308657 184 EKLRTGLSNYANR 196
Cdd:pfam12689 157 EEFERGLRKWRKR 169
HAD-SF-IIIC TIGR01681
HAD-superfamily phosphatase, subfamily IIIC; This model represents the IIIC subfamily of the ...
 54-171 8.37e-15

HAD-superfamily phosphatase, subfamily IIIC; This model represents the IIIC subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate nucleophile hydrolases. Subfamily III (also including IIIA - TIGR01662 and IIIB - pfam03767) contains sequences which do not contain either of the insert domains (between the 1st and 2nd conserved catalytic motifs, subfamily I - TIGR01493, TIGR01509, TIGR01549, TIGR01488, TIGR01494, TIGR01658, TIGR01544 and TIGR01545, or between the 2nd and 3rd, subfamily II - TIGR01460 and TIGR01484). Subfamily IIIC contains five relatively distantly related clades: a family of viral proteins (TIGR01684), a family of eukaryotic proteins called MDP-1 and a family of archaeal proteins most closely related to MDP-1 (TIGR01685), a family of bacteria including the Streptomyces FkbH protein (TIGR01686), and a small clade including the Pasteurella BcbF and EcbF proteins. The overall lack of species overlap among these clades may indicate a conserved function, but the degree of divergence between the clades and the differences in archetecture outside of the domain in some clades warns against such a conclusion. No member of this subfamily is characterized with respect to function, however the MDP-1 protein is a characterized phosphatase. All of the characterized enzymes within subfamily III are phosphatases, and all of the active site residues characteristic of HAD-superfamily phosphatases are present in subfamily IIIC.


Pssm-ID: 273752 [Multi-domain]  Cd Length: 128  Bit Score: 68.23  E-value: 8.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657  54 RLVVFDLDHTLWPFQCD---RLPKDEPPYLYPQARGILKALKDRGIEMAIASRASRKKgVAKAFLeKLGIHF-------- 122
Cdd:TIGR01681   1 KVIVFDLDNTLWTGENIvvgEDPIIDLEVTIKEIRDKLQTLKKNGFLLALASYNDDPH-VAYELL-KIFEDFgiifplae 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1002308657 123 MFGAQEIFYtWSPKNEHFQSIHRKTGVP--FKSMLFFDDEARNIIATRKLG 171
Cdd:TIGR01681  79 YFDPLTIGY-WLPKSPRLVEIALKLNGVlkPKSILFVDDRPDNNEEVDYYL 128
MDP-1 TIGR01685
magnesium-dependent phosphatase-1; This model represents two closely related clades of ...
 52-193 1.09e-11

magnesium-dependent phosphatase-1; This model represents two closely related clades of sequences from eukaryotes and archaea. The mouse enzyme has been characterized as a phosphatase and has been positively identified as a member of the haloacid dehalogenase (HAD) superfamily by site-directed mutagenesis of the active site residues.


Pssm-ID: 273756  Cd Length: 174  Bit Score: 61.02  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657  52 LPRLVVFDLDHTLWPFQCDRLPKdePPY-------------------LYPQARGILKALKDRGIEMAIASRASRKKgVAK 112
Cdd:TIGR01685   1 LPRVIVFDLDGTLWDHYMISLLG--GPFkpvkqnnsiiidksgtevtLIKEVRDVLQTLKDAGTYLATASWNDVPE-WAY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657 113 AFLEKLGIHF---MFGAQEIF--YTWSPKNEHF-------QSIHRKTGVPFKS--MLFFDDEARNIIATRKLGVSCVLVD 178
Cdd:TIGR01685  78 EILGTFEITYagkTVPMHSLFddRIEIYKPNKAkqlemilQKVNKVDPSVLKPaqILFFDDRTDNVREVWGYGVTSCYCP 157

                         170
                  ....*....|....*
gi 1002308657 179 TGITLEKLRTGLSNY 193
Cdd:TIGR01685 158 SGMDKGTFKKILEMW 172
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
80-180 3.04e-11

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 60.33  E-value: 3.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657  80 LYPQARGILKALKDRGIEMAIASRASRKkgVAKAFLEKLGIHFMFGA---QEIFYTWSPKNEHFQSIHRKTGVPFKSMLF 156
Cdd:COG0546    85 LFPGVRELLEALKARGIKLAVVTNKPRE--FAERLLEALGLDDYFDAivgGDDVPPAKPKPEPLLEALERLGLDPEEVLM 162

                          90       100
                  ....*....|....*....|....
gi 1002308657 157 FDDEARNIIATRKLGVSCVLVDTG 180
Cdd:COG0546   163 VGDSPHDIEAARAAGVPFIGVTWG 186
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 55-177 5.55e-11

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: 57.41  E-value: 5.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657  55 LVVFDLDHTLWpfqcdrlpkdeppylypqARGILKALKDRGIEMAIASRASRKkgVAKAFLEKLGIHFMFGAQ---EIFY 131
Cdd:cd01427     1 AVLFDLDGTLL------------------AVELLKRLRAAGIKLAIVTNRSRE--ALRALLEKLGLGDLFDGIigsDGGG 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1002308657 132 TWSPKNEHFQSIHRKTGVPFKSMLFFDDEARNIIATRKLGVSCVLV 177
Cdd:cd01427    61 TPKPKPKPLLLLLLKLGVDPEEVLFVGDSENDIEAARAAGGRTVAV 106
FkbH COG3882
Predicted enzyme involved in methoxymalonyl-ACP biosynthesis [Lipid transport and metabolism];
40-178 2.98e-09

Predicted enzyme involved in methoxymalonyl-ACP biosynthesis [Lipid transport and metabolism];


Pssm-ID: 443090 [Multi-domain]  Cd Length: 375  Bit Score: 56.04  E-value: 2.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657  40 AEALALMAAHPVLPR-LVVFDLDHTLWpfqcD-----------RLPKDEPPYLYPQARGILKALKDRGIEMAIASRASRK 107
Cdd:COG3882     5 REIARLVAALRGKTRkCLVLDLDNTLW----GgvlgedgidgiRLGQGAPGEAFLAFQEVIKTLDRRGILLAIASKNDEE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002308657 108 kgVAKAFLEKLgiHFMFGAQEIFYT----WSPKNEHFQSIHRKTGVPFKSMLFFDDEA--RNIIATRKLGVSCVLVD 178
Cdd:COG3882    81 --DALEVLEEH--PDMVLKEEDFAApqinWNPKSENIREIAKELNIGLDSFVFIDDNPfeREEVRAALPEVLVIDAP 153
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
74-177 6.62e-07

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 47.58  E-value: 6.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657  74 KDEPPYLYPQARGILKALKDRGIEMAIASraSRKKGVAKAFLEKLGIHFMF----GAQEIFytwsPKNEHFQSIH---RK 146
Cdd:pfam13419  74 HDKLVKPYPGIKELLEELKEQGYKLGIVT--SKSRENVEEFLKQLGLEDYFdvivGGDDVE----GKKPDPDPILkalEQ 147

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1002308657 147 TGVPFKSMLFFDDEARNIIATRKLGVSCVLV 177
Cdd:pfam13419 148 LGLKPEEVIYVGDSPRDIEAAKNAGIKVIAV 178
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 76-171 1.35e-06

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: 47.20  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657  76 EPPYLYPQARGILKALKDRGIEMAIASRASRKkgVAKAFLEKLGIHFMFG---AQEIFYTWSPKNEHFQSIHRKTGVPFK 152
Cdd:pfam00702  95 DELKLYPGAAEALKALKERGIKVAILTGDNPE--AAEALLRLLGLDDYFDvviSGDDVGVGKPKPEIYLAALERLGVKPE 172

                          90
                  ....*....|....*....
gi 1002308657 153 SMLFFDDEARNIIATRKLG 171
Cdd:pfam00702 173 EVLMVGDGVNDIPAAKAAG 191
Pyr-5-nucltdase TIGR01993
pyrimidine 5'-nucleotidase; This family of proteins includes the SDT1/SSM1 gene from yeast ...
 82-177 2.82e-06

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: 46.19  E-value: 2.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657  82 PQARGILKALKDRGIemaIASRASRKKgvAKAFLEKLGIH------FMFGAQEIFYTWSPKNEHFQSIHRKTGVPFKSML 155
Cdd:TIGR01993  87 PELRNLLLRLPGRKI---IFTNGDRAH--ARRALRRLGIEdcfdgiFCFDTANPDLLPKPSPQAYEKALREAGVDPERAI 161

                          90       100
                  ....*....|....*....|..
gi 1002308657 156 FFDDEARNIIATRKLGVSCVLV 177
Cdd:TIGR01993 162 FFDDSARNIAAGKALGMKTVLV 183
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 45-179 2.96e-06

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 [Multi-domain]  Cd Length: 182  Bit Score: 46.09  E-value: 2.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657  45 LMAAHPVLP----RLVVFDLDHtlwpfqcDRLPKDeppylyPQARGILKALKDRGIemaIASRASrkKGVAKAFLEKLGI 120
Cdd:cd02604    58 LMAEHGIDPdeflDRVVHLILY-------DHLKPD------PKLRNLLLALPGRKI---IFTNAS--KNHAIRVLKRLGL 119

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002308657 121 --HF--MFGAQEIFYTWSPKNEHFQSIHRKTGVPFKSMLFFDDEARNIIATRKLGVSCVLVDT 179
Cdd:cd02604   120 adLFdgIFDIEYAGPDPKPHPAAFEKAIREAGLDPKRAAFFDDSIRNLLAAKALGMKTVLVGP 182
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 67-180 4.01e-06

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


Pssm-ID: 319799 [Multi-domain]  Cd Length: 201  Bit Score: 45.81  E-value: 4.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657  67 FQCDRLPKDEPPYLYPQARGILKALKDRGIEMAIASRASRKkgVAKAFLEKLGIHFMFG---AQEIFytwsPKNEHFQSI 143
Cdd:cd04303    67 FRRLMAEAAPELALFPGVEDMLRALHARGVRLAVVSSNSEE--NIRRVLGPEELISLFAvieGSSLF----GKAKKIRRV 140

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1002308657 144 HRKTGVPFKSMLFFDDEARNIIATRKLGVSCVLVDTG 180
Cdd:cd04303   141 LRRTKITAAQVIYVGDETRDIEAARKVGLAFAAVSWG 177
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 44-178 4.25e-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: 45.79  E-value: 4.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657  44 ALMAAHPVLPRLVVFDLDHTLWPfqcdrlpkdEPPYLYPQARGILKALKDRGIEMAIASRASRKkgVAKAFLEKLGIHFM 123
Cdd:COG1011    67 RLLEELGLDLAEELAEAFLAALP---------ELVEPYPDALELLEALKARGYRLALLTNGSAE--LQEAKLRRLGLDDL 135

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002308657 124 FgaQEIFYTWS-----PKNEHFQSIHRKTGVPFKSMLFFDD-EARNIIATRKLGVSCVLVD 178
Cdd:COG1011   136 F--DAVVSSEEvgvrkPDPEIFELALERLGVPPEEALFVGDsPETDVAGARAAGMRTVWVN 194
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 54-126 9.73e-06

HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class III subfamilies are characterized by the lack of any domains located between either between the first and second conserved catalytic motifs (as in the Class I subfamilies, TIGR01493, TIGR01509, TIGR01488 and TIGR01494) or between the second and third conserved catalytic motifs (as in the Class II subfamilies, TIGR01460 and TIGR01484) of the superfamily domain. The IIIA subfamily contains five major clades: histidinol-phosphatase (TIGR01261) and histidinol-phosphatase-related protein (TIGR00213) which together form a subfamily (TIGR01656), DNA 3'-phosphatase (TIGR01663, TIGR01664), YqeG (TIGR01668) and YrbI (TIGR01670). In the case of histidinol phosphatase and PNK-3'-phosphatase, this model represents a domain of a bifunctional system. In the histidinol phosphatase HisB, a C-terminal domain is an imidazoleglycerol-phosphate dehydratase which catalyzes a related step in histidine biosynthesis. In PNK-3'-phosphatase, N- and C-terminal domains constitute the polynucleotide kinase and DNA-binding components of the enzyme. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273742 [Multi-domain]  Cd Length: 135  Bit Score: 43.93  E-value: 9.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657  54 RLVVFDLDHTLwpfQCDRLPKDEPP--YLYPQARGILKALKDRGIEMAIASRAS---------RKKGVAKAFLEKLGIHF 122
Cdd:TIGR01662   1 KAVVLDLDGTL---TDDVPYVSDEDerILYPEVPDALAELKEAGYKVVIVTNQSgigrgyfsrSFSGRVARRLEELGVPI 77


                  ....
gi 1002308657 123 MFGA 126
Cdd:TIGR01662  78 DILY 81
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 80-177 1.55e-05

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: 43.95  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657  80 LYPQARGILKALKDRGIEMAIASRASRkkgVAKAFLEKLGI--HFmfgaqEIFYTWS------PKNEHFQSIHRKTGVPF 151
Cdd:TIGR01509  81 PLPGVRALLEALRARGKKLALLTNSPR---AHKLVLALLGLrdLF-----DVVIDSSdvglgkPDPDIYLQALKALGLEP 152

                          90       100
                  ....*....|....*....|....*.
gi 1002308657 152 KSMLFFDDEARNIIATRKLGVSCVLV 177
Cdd:TIGR01509 153 SECVFVDDSPAGIEAAKAAGMHTVGV 178
FkbH TIGR01686
FkbH-like domain; This model describes a domain of a family of proteins of unknown overall ...
 53-159 5.75e-05

FkbH-like domain; This model describes a domain of a family of proteins of unknown overall function. One of these, however, is a modular polyketide synthase 4800 amino acids in length from Streptomyces avermilitis in which this domain is the C-terminal segment. By contrast, the FkbH protein from Streptomyces hygroscopicus aparently contains only this domain. The remaining members of the family all contain an additional N-terminal domain of between 200 and 275 amino acids which show less than 20% identity to one another. It seems likely then that these proteins are involved in disparate functions, probably the biosynthesis of different natural products. For instance, the FkbH gene is found in a gene cluster believed to be responsible for the biosynthesis of unususal "PKS extender units" in the ascomycin pathway. This domain is composed of two parts, the first of which is a member of subfamily IIIC (TIGR01681) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. All of the characterized enzymes within subfamily III are phosphatases, and all of the active site residues characteristic of HAD-superfamily phosphatases are present in this domain. The C-terminal portion of this domain is unique to this family (by BLAST).


Pssm-ID: 273757 [Multi-domain]  Cd Length: 320  Bit Score: 42.92  E-value: 5.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657  53 PRLVVFDLDHTLW--------PFQCDRLPkdeppyLYPQARGILKALKDRGIEMAIASRASRKkgVAKAFLEK----LGI 120
Cdd:TIGR01686   3 LKVLVLDLDNTLWggvlgedgIDNLNLSP------LHKTLQEKIKTLKKQGFLLALASKNDED--DAKKVFERrkdfILQ 74

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1002308657 121 HFMFGAQEIfyTWSPKNEHFQSIHRKTGVPFKSMLFFDD 159
Cdd:TIGR01686  75 AEDFDARSI--NWGPKSESLRKIAKKLNLGTDSFLFIDD 111
COG4996 COG4996
Predicted phosphatase [General function prediction only];
52-102 3.20e-04

Predicted phosphatase [General function prediction only];


Pssm-ID: 444020  Cd Length: 165  Bit Score: 39.97  E-value: 3.20e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657  52 LPRLVVFDLDHTLWpfqcDRL--PKDEPPY-----------------LYPQARGILKALKDRGIEMAIAS 102
Cdd:COG4996     2 MIKLLVLDLDGTLW----DHHniSELKPPFkrisensivdsygrevrLFPDVREFLEWAKERGAILSTAS 67
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 53-177 5.80e-04

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 39.35  E-value: 5.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657  53 PRLVVFDLDHTLwpfqcdrLPKDEppYLYPQARGILKALKDRGIEMAIASraSRKKGVAKAFLEKLGIHFMF----GAqe 128
Cdd:COG0561     2 IKLIALDLDGTL-------LNDDG--EISPRTKEALRRLREKGIKVVIAT--GRPLRSALPLLEELGLDDPLitsnGA-- 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002308657 129 ifYTWSPKNEhfqsIHRKTGVPfksmlffDDEARNIIAT-RKLGVSCVLV 177
Cdd:COG0561    69 --LIYDPDGE----VLYERPLD-------PEDVREILELlREHGLHLQVV 105
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
80-126 1.32e-03

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 38.65  E-value: 1.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1002308657  80 LYPQARGILKALKDRGIEMAIASRASRKKgvAKAFLEKLGIHFMFGA 126
Cdd:COG0637    87 LIPGVVELLEALKEAGIKIAVATSSPREN--AEAVLEAAGLLDYFDV 131
PRK13225 PRK13225
phosphoglycolate phosphatase; Provisional
 80-180 1.80e-03

phosphoglycolate phosphatase; Provisional


Pssm-ID: 106187 [Multi-domain]  Cd Length: 273  Bit Score: 38.54  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002308657  80 LYPQARGILKALKDRGIEMAIASRASRKKgvAKAFLEKLGIHFMFGAQEIFYTWSPKNEHFQSIHRKTGVPFKSMLFFDD 159
Cdd:PRK13225  143 LFPGVADLLAQLRSRSLCLGILSSNSRQN--IEAFLQRQGLRSLFSVVQAGTPILSKRRALSQLVAREGWQPAAVMYVGD 220

                          90       100
                  ....*....|....*....|.
gi 1002308657 160 EARNIIATRKLGVSCVLVDTG 180
Cdd:PRK13225  221 ETRDVEAARQVGLIAVAVTWG 241
PRK09456 PRK09456
?-D-glucose-1-phosphatase; Provisional
 135-177 5.09e-03

?-D-glucose-1-phosphatase; Provisional


Pssm-ID: 181872 [Multi-domain]  Cd Length: 199  Bit Score: 36.55  E-value: 5.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1002308657 135 PKNEHFQSIHRKTGVPFKSMLFFDDEARNIIATRKLGVSCVLV 177
Cdd:PRK09456  142 PEARIYQHVLQAEGFSAADAVFFDDNADNIEAANALGITSILV 184
 
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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