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Conserved domains on  [gi|671554405|ref|WP_031536957|]
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MULTISPECIES: HAD family acid phosphatase [Bacillaceae]

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
YqfW super family cl42550
Uncharacterized conserved protein YqfW, HAD superfamily [General function prediction only];
1-184 2.07e-50

Uncharacterized conserved protein YqfW, HAD superfamily [General function prediction only];


The actual alignment was detected with superfamily member COG5663:

Pssm-ID: 444382 [Multi-domain]  Cd Length: 187  Bit Score: 160.78  E-value: 2.07e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671554405   1 MKFGFDIDDTLINLRQHAFNIYNKKLKKNIPLAsfhALKTVEIHEPFGLNAIEGKQLWDSLREEIYfTDCSPFPGAVEAL 80
Cdd:COG5663    1 MRIGIDIDGTITDPYPYFIPLLNKYFGKNITLE---DITTYDLHEVLGLTEEEFDKFFEENEEEIY-TEAPPVPGAKEVL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671554405  81 NELvHNGHQVYYITARNKQFATKTKEWMKEIGFPVVDHHFycgMEDHEKITIIQNLKLDYYFDDKPAVLETLIDHSTQLY 160
Cdd:COG5663   77 NKL-KDQHELYYITARPKHLEEVTENWLEKHGIPYDELIL---LGSHDKVEAAKELGIDLFIEDKPDNALQLAEEGIPVL 152

                        170       180
                 ....*....|....*....|....*..
gi 671554405 161 VKDHLYNEHLEWN---RIKDWKELKQL 184
Cdd:COG5663  153 LFDTPYNRGPLPEgviRVNNWQEIKQI 179
 
Name Accession Description Interval E-value
YqfW COG5663
Uncharacterized conserved protein YqfW, HAD superfamily [General function prediction only];
1-184 2.07e-50

Uncharacterized conserved protein YqfW, HAD superfamily [General function prediction only];


Pssm-ID: 444382 [Multi-domain]  Cd Length: 187  Bit Score: 160.78  E-value: 2.07e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671554405   1 MKFGFDIDDTLINLRQHAFNIYNKKLKKNIPLAsfhALKTVEIHEPFGLNAIEGKQLWDSLREEIYfTDCSPFPGAVEAL 80
Cdd:COG5663    1 MRIGIDIDGTITDPYPYFIPLLNKYFGKNITLE---DITTYDLHEVLGLTEEEFDKFFEENEEEIY-TEAPPVPGAKEVL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671554405  81 NELvHNGHQVYYITARNKQFATKTKEWMKEIGFPVVDHHFycgMEDHEKITIIQNLKLDYYFDDKPAVLETLIDHSTQLY 160
Cdd:COG5663   77 NKL-KDQHELYYITARPKHLEEVTENWLEKHGIPYDELIL---LGSHDKVEAAKELGIDLFIEDKPDNALQLAEEGIPVL 152

                        170       180
                 ....*....|....*....|....*..
gi 671554405 161 VKDHLYNEHLEWN---RIKDWKELKQL 184
Cdd:COG5663  153 LFDTPYNRGPLPEgviRVNNWQEIKQI 179
NT5C pfam06941
5' nucleotidase, deoxy (Pyrimidine), cytosolic type C protein (NT5C); This family consists of ...
 1-184 1.10e-10

5' nucleotidase, deoxy (Pyrimidine), cytosolic type C protein (NT5C); This family consists of several 5' nucleotidase, deoxy (Pyrimidine), cytosolic type C (NT5C) proteins. 5'(3')-Deoxyribonucleotidase is a ubiquitous enzyme in mammalian cells whose physiological function is not known.


Pssm-ID: 284381 [Multi-domain]  Cd Length: 180  Bit Score: 57.62  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671554405    1 MKFGFDIDDTLINLRQHAFNIYNKKLKKNIPLASFHALKTVEIHEPFglnaiEGKQLWDSLREEIYFTDCSPFPGAVEAL 80
Cdd:pfam06941   2 SIIGVDLDGVCADFYGRMRQIANEWFERPLLPEEVSSWGWSEWTNPE-----QYDSLHRFVTQPGFFSDLEPIPGAREYL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671554405   81 NELVHNGHQVyYITARNKQFATKTKE---WMKEiGFPVVdhHFYCGMEDHEKitiiQNLKLDYYFDDKPavlETLIDHST 157
Cdd:pfam06941  77 RQLSDEGRIV-IITHRLFQHYTAVQQkvnWLDS-HLPGI--PYWNLCFVKEK----TQVRGDIYIDDSP---ENLAQLRG 145

                         170       180
                  ....*....|....*....|....*...
gi 671554405  158 QLYVKDHLYNEHLE-WNRIKDWKELKQL 184
Cdd:pfam06941 146 RGILFGNPTNRHIEdELRAASWQEVYDM 173
HAD_5-3dNT cd02587
5'(3')-deoxyribonucleotidase; This family includes cytosolic 5'(3')-deoxyribonucleotidase (cdN) ...
 1-150 3.68e-07

5'(3')-deoxyribonucleotidase; This family includes cytosolic 5'(3')-deoxyribonucleotidase (cdN) and mitochondrial 5'(3')-deoxyribonucleotidase (mdN). cdN and mdN specifically dephosphorylate the deoxyribo form of nucleoside monophosphates helps maintain homeostasis of deoxynucleosides required for mitochondrial DNA synthesis. Their preferred substrates are dUMP and dTMP. cdN also dephosphorylates dGMP and dIMP efficiently. They can also dephosphorylate the 5'- or 3'-phosphates of pyrimidine ribonucleotides. 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: 319786  Cd Length: 161  Bit Score: 47.77  E-value: 3.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671554405   1 MKFGFDIDDTLINLrQHAFNIYNKKLKKNIPLASFHALKTVEIHEPFGLNAIEGKqLWDSLREEIYFTDCSPFPGAVEAL 80
Cdd:cd02587    1 IVILVDMDGVLADF-EGALVRAIRERFPDEPHVLLESRRGFWVIEQYKAPELSRK-AADILEEPGFFRNLEPIPGAVEAL 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 671554405  81 NELVHNGHQVYYITARNKQFAT---KTKEWMKE-IGFPVVDHHFYCgmedHEKiTIIQnlkLDYYFDDKPAVLE 150
Cdd:cd02587   79 RELSDEGTDVYICTSPLNKYPTcveEKYEWVEEhFPPLFYQRIVLT----RDK-TVVL---ADILIDDNPENLE 144
lipo_e_P4 TIGR01533
5'-nucleotidase, lipoprotein e(P4) family; This model represents a set of bacterial ...
 69-140 1.25e-04

5'-nucleotidase, lipoprotein e(P4) family; This model represents a set of bacterial lipoproteins belonging to a larger acid phosphatase family (pfam03767), which in turn belongs to the haloacid dehalogenase (HAD) superfamily of aspartate-dependent hydrolases. Members are found on the outer membrane of Gram-negative bacteria and the cytoplasmic membrane of Gram-positive bacteria. Most members have classic lipoprotein signal sequences. A critical role of this 5'-nucleotidase in Haemophilus influenzae is the degradation of external riboside in order to allow transport into the cell. An earlier suggested role in hemin transport is no longer current. This enzyme may also have other physiologically significant roles. [Transport and binding proteins, Other, Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]


Pssm-ID: 273674  Cd Length: 266  Bit Score: 41.35  E-value: 1.25e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 671554405   69 DCSPFPGAVEALNELVHNGHQVYYITARNKQFATKTKEWMKEIGFPVVDH-HFYCGMEDHEKITIIQNLKLDY 140
Cdd:TIGR01533 116 QAKPVAGALDFLNYANSKGVKIFYVSNRSEKEKAATLKNLKRFGFPQADEeHLLLKKDKSSKESRRQKVQKDY 188
 
Name Accession Description Interval E-value
YqfW COG5663
Uncharacterized conserved protein YqfW, HAD superfamily [General function prediction only];
1-184 2.07e-50

Uncharacterized conserved protein YqfW, HAD superfamily [General function prediction only];


Pssm-ID: 444382 [Multi-domain]  Cd Length: 187  Bit Score: 160.78  E-value: 2.07e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671554405   1 MKFGFDIDDTLINLRQHAFNIYNKKLKKNIPLAsfhALKTVEIHEPFGLNAIEGKQLWDSLREEIYfTDCSPFPGAVEAL 80
Cdd:COG5663    1 MRIGIDIDGTITDPYPYFIPLLNKYFGKNITLE---DITTYDLHEVLGLTEEEFDKFFEENEEEIY-TEAPPVPGAKEVL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671554405  81 NELvHNGHQVYYITARNKQFATKTKEWMKEIGFPVVDHHFycgMEDHEKITIIQNLKLDYYFDDKPAVLETLIDHSTQLY 160
Cdd:COG5663   77 NKL-KDQHELYYITARPKHLEEVTENWLEKHGIPYDELIL---LGSHDKVEAAKELGIDLFIEDKPDNALQLAEEGIPVL 152

                        170       180
                 ....*....|....*....|....*..
gi 671554405 161 VKDHLYNEHLEWN---RIKDWKELKQL 184
Cdd:COG5663  153 LFDTPYNRGPLPEgviRVNNWQEIKQI 179
YorC COG4502
5'(3')-deoxyribonucleotidase [Nucleotide transport and metabolism];
1-184 6.81e-13

5'(3')-deoxyribonucleotidase [Nucleotide transport and metabolism];


Pssm-ID: 443586 [Multi-domain]  Cd Length: 177  Bit Score: 63.35  E-value: 6.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671554405   1 MKFGFDIDDTLINLRQHAFNIYNKKLKKNIPLASFHALKTVEIHEPfglnaIEGKQLWDSLREEIYFTDCSPFPGAVEAL 80
Cdd:COG4502    3 PRIAVDMDGVLADFYAAFLDIYNKEYGTNLTLEDLDGWDLWELVPP-----EHRERIREFLNEPGFFRDLPPIPGAQEVL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671554405  81 NELVHNgHQVYYITAR--NKQFATKTKEWMKEiGFPVVDHHFYCgmEDHEKiTIIQnlkLDYYFDDKPAVLETLIDHsTQ 158
Cdd:COG4502   78 KELSDK-YEVYIVTAAmeFPNSLEEKYEWLDE-HFPFIPWQNII--FCGDK-SLVG---GDYLIDDNPKNLEEFKGK-GI 148

                        170       180
                 ....*....|....*....|....*..
gi 671554405 159 LYvkDHLYNEHLEW-NRIKDWKELKQL 184
Cdd:COG4502  149 LF--DAPHNRHITGyPRVNNWKEVEAL 173
NT5C pfam06941
5' nucleotidase, deoxy (Pyrimidine), cytosolic type C protein (NT5C); This family consists of ...
 1-184 1.10e-10

5' nucleotidase, deoxy (Pyrimidine), cytosolic type C protein (NT5C); This family consists of several 5' nucleotidase, deoxy (Pyrimidine), cytosolic type C (NT5C) proteins. 5'(3')-Deoxyribonucleotidase is a ubiquitous enzyme in mammalian cells whose physiological function is not known.


Pssm-ID: 284381 [Multi-domain]  Cd Length: 180  Bit Score: 57.62  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671554405    1 MKFGFDIDDTLINLRQHAFNIYNKKLKKNIPLASFHALKTVEIHEPFglnaiEGKQLWDSLREEIYFTDCSPFPGAVEAL 80
Cdd:pfam06941   2 SIIGVDLDGVCADFYGRMRQIANEWFERPLLPEEVSSWGWSEWTNPE-----QYDSLHRFVTQPGFFSDLEPIPGAREYL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671554405   81 NELVHNGHQVyYITARNKQFATKTKE---WMKEiGFPVVdhHFYCGMEDHEKitiiQNLKLDYYFDDKPavlETLIDHST 157
Cdd:pfam06941  77 RQLSDEGRIV-IITHRLFQHYTAVQQkvnWLDS-HLPGI--PYWNLCFVKEK----TQVRGDIYIDDSP---ENLAQLRG 145

                         170       180
                  ....*....|....*....|....*...
gi 671554405  158 QLYVKDHLYNEHLE-WNRIKDWKELKQL 184
Cdd:pfam06941 146 RGILFGNPTNRHIEdELRAASWQEVYDM 173
COG2503 COG2503
Predicted secreted acid phosphatase [General function prediction only];
72-129 3.24e-08

Predicted secreted acid phosphatase [General function prediction only];


Pssm-ID: 441997 [Multi-domain]  Cd Length: 269  Bit Score: 51.89  E-value: 3.24e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 671554405  72 PFPGAVEALNELVHNGHQVYYITARNKQFATKTKEWMKEIGFPVVDH-HFYCGMEDHEK 129
Cdd:COG2503  124 AVPGAVEFLNYANSKGVTVFYISNRKAEEKAATLANLKALGFPVVDEdHLLLKTDGSDK 182
HAD_5-3dNT cd02587
5'(3')-deoxyribonucleotidase; This family includes cytosolic 5'(3')-deoxyribonucleotidase (cdN) ...
 1-150 3.68e-07

5'(3')-deoxyribonucleotidase; This family includes cytosolic 5'(3')-deoxyribonucleotidase (cdN) and mitochondrial 5'(3')-deoxyribonucleotidase (mdN). cdN and mdN specifically dephosphorylate the deoxyribo form of nucleoside monophosphates helps maintain homeostasis of deoxynucleosides required for mitochondrial DNA synthesis. Their preferred substrates are dUMP and dTMP. cdN also dephosphorylates dGMP and dIMP efficiently. They can also dephosphorylate the 5'- or 3'-phosphates of pyrimidine ribonucleotides. 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: 319786  Cd Length: 161  Bit Score: 47.77  E-value: 3.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671554405   1 MKFGFDIDDTLINLrQHAFNIYNKKLKKNIPLASFHALKTVEIHEPFGLNAIEGKqLWDSLREEIYFTDCSPFPGAVEAL 80
Cdd:cd02587    1 IVILVDMDGVLADF-EGALVRAIRERFPDEPHVLLESRRGFWVIEQYKAPELSRK-AADILEEPGFFRNLEPIPGAVEAL 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 671554405  81 NELVHNGHQVYYITARNKQFAT---KTKEWMKE-IGFPVVDHHFYCgmedHEKiTIIQnlkLDYYFDDKPAVLE 150
Cdd:cd02587   79 RELSDEGTDVYICTSPLNKYPTcveEKYEWVEEhFPPLFYQRIVLT----RDK-TVVL---ADILIDDNPENLE 144
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
5-155 6.89e-05

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 41.84  E-value: 6.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671554405   5 FDIDDTLINLRQHAFNIYNKKLKK-NIPLASFHALKTVeIHEP--------FGLNAIEG-KQLWDSLRE---EIYFTDCS 71
Cdd:COG0546    6 FDLDGTLVDSAPDIAAALNEALAElGLPPLDLEELRAL-IGLGlrellrrlLGEDPDEElEELLARFRElyeEELLDETR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671554405  72 PFPGAVEALNELVHNGHQVYYITARNKQFATKTkewMKEIGFpvvDHHF---YCGMEDHEKitiiqnlkldyyfDDKPAV 148
Cdd:COG0546   85 LFPGVRELLEALKARGIKLAVVTNKPREFAERL---LEALGL---DDYFdaiVGGDDVPPA-------------KPKPEP 145


                 ....*..
gi 671554405 149 LETLIDH 155
Cdd:COG0546  146 LLEALER 152
lipo_e_P4 TIGR01533
5'-nucleotidase, lipoprotein e(P4) family; This model represents a set of bacterial ...
 69-140 1.25e-04

5'-nucleotidase, lipoprotein e(P4) family; This model represents a set of bacterial lipoproteins belonging to a larger acid phosphatase family (pfam03767), which in turn belongs to the haloacid dehalogenase (HAD) superfamily of aspartate-dependent hydrolases. Members are found on the outer membrane of Gram-negative bacteria and the cytoplasmic membrane of Gram-positive bacteria. Most members have classic lipoprotein signal sequences. A critical role of this 5'-nucleotidase in Haemophilus influenzae is the degradation of external riboside in order to allow transport into the cell. An earlier suggested role in hemin transport is no longer current. This enzyme may also have other physiologically significant roles. [Transport and binding proteins, Other, Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]


Pssm-ID: 273674  Cd Length: 266  Bit Score: 41.35  E-value: 1.25e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 671554405   69 DCSPFPGAVEALNELVHNGHQVYYITARNKQFATKTKEWMKEIGFPVVDH-HFYCGMEDHEKITIIQNLKLDY 140
Cdd:TIGR01533 116 QAKPVAGALDFLNYANSKGVKIFYVSNRSEKEKAATLKNLKRFGFPQADEeHLLLKKDKSSKESRRQKVQKDY 188
HAD_CAP cd07534
molecular class C acid phosphatases, similar to Haemophilus influenzae e (P4) acid phosphatase; ...
 72-129 3.03e-04

molecular class C acid phosphatases, similar to Haemophilus influenzae e (P4) acid phosphatase; belongs to the haloacid dehalogenase-like hydrolase superfamily; Molecular class C acid phosphatases (CAPs) are nonspecific acid phosphatases with generally broad substrate specificity and optimum activity at neutral to acidic pH. Members include Haemophilus influenzae lipoprotein e (P4), Elizabethkingia meningosepticum OlpA, Helicobacter pylori HppA, Enterobacter sp. 4 acid phosphatase PhoI, and Streptococcus pyogenes M1 GAS LppC. Lipoprotein e (P4) exhibits phosphomonoesterase activity with aryl phosphate substrates including nicotinamide mononucleotide (NMN), tyrosine phosphate, phenyl phosphate, p-nitrophenyl phosphate, and 4-methylumbelliferyl phosphate. The role of P4 in NAD+ uptake appears to be the dephosphorylation of NMN to nicotinamide riboside, which is then taken up by the organism. Elizabethkingia meningosepticum OlpA is a broad-spectrum nucleotidase with preference for 5'-nucleotides, it efficiently hydrolyzes nucleotide monophosphates, with a strong preference for 5'-nucleotides and for 3'-AMP; OlpA can also hydrolyze sugar phosphates and beta-glycerol phosphate, although with a lower efficiency. Helicobacter pylori HppA is also a 5' nucleotidase. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319836 [Multi-domain]  Cd Length: 196  Bit Score: 39.62  E-value: 3.03e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 671554405  72 PFPGAVEALNELVHNGHQVYYITARNKQFATKTKEWMKEIGFPVV-DHHFYCGMEDHEK 129
Cdd:cd07534   75 PIPGAVDFLNYANAKGVTIFYVSNRDQKLKAATLKNLKRLGFPQAsDDHLLLKTDKSSK 133
Acid_phosphat_B pfam03767
HAD superfamily, subfamily IIIB (Acid phosphatase); This family proteins includes acid ...
 3-118 3.75e-04

HAD superfamily, subfamily IIIB (Acid phosphatase); This family proteins includes acid phosphatases and a number of vegetative storage proteins.


Pssm-ID: 397712  Cd Length: 213  Bit Score: 39.66  E-value: 3.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671554405    3 FGFDIDDTLINlrqhafniynkklkkNIPLASFHALKTveihEPFGlnaiegKQLWDSLREEiyfTDCSPFPGAVEALNE 82
Cdd:pfam03767  63 VVFDIDETVLS---------------NSPYYAYHGYGG----EPFD------PEKFDEWVNK---GEAPALPGALELYNY 114

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 671554405   83 LVHNGHQVYYITARNKQFATKTKEWMKEIGFPVVDH 118
Cdd:pfam03767 115 LVELGVKIFFVSGRSEDLRAATVENLKKAGFHGWEK 150
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 72-122 1.76e-03

Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.


Pssm-ID: 433132  Cd Length: 101  Bit Score: 36.29  E-value: 1.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 671554405   72 PFPGAVEALNELVHNGHQVYYIT----ARNKQFATKtkewMKEIGFPVVDHHFYC 122
Cdd:pfam13344  15 PIPGAAEALRALRAAGKPVVFVTnnssRSREEYAEK----LRKLGFDIDEDEIIT 65
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
72-121 3.24e-03

Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 37.01  E-value: 3.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 671554405  72 PFPGAVEALNELVHNGHQVYYIT----ARNKQFATKtkewMKEIGFPVVDHHFY 121
Cdd:COG0647   25 PIPGAVEALARLRAAGKPVLFLTnnssRTPEDVAEK----LRRLGIPVAEDEIV 74
 
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.
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