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Conserved domains on  [gi|83754294]
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Chain A, class B acid phosphatase

Protein Classification

AphA family protein( domain architecture ID 10007848)

AphA family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AphA COG3700
Acid phosphatase, class B [Inorganic ion transport and metabolism, General function prediction ...
 1-211 1.91e-165

Acid phosphatase, class B [Inorganic ion transport and metabolism, General function prediction only];


:

Pssm-ID: 442914  Cd Length: 237  Bit Score: 454.84  E-value: 1.91e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83754294   1 SPSPLNPGTNVARLAEQAPIHWVSVAQIENSLAGRPPMAVGFDIDDTVLFSSPGFWRGKKTFSPESEDYLKNPVFWEKMN 80
Cdd:COG3700  27 KVPYTQEGTTVAQLAQQAPIHWVSVEQIENSLKGKPPMAVGFDIDDTVLFSSPGFYYGKQKFSPGSYSYLKNQKFWDKMN 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83754294  81 NGWDEFSIPKEVARQLIDMHVRRGDAIFFVTGRSPTKTETVSKTLADNFHIPATNMNPVIFAGDKPGQNTKSQWLQDKNI 160
Cdd:COG3700 107 NGWDEFSIPKEVARALIAMHLKRGDQIYFITGRTATKTETVTKTLQKDFNIPAKNMNPVIFAGDKPGQYDKTQWIKKHNI 186

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 83754294 161 RIFYGDSDNDITAARDVGARGIRILRASNSTYKPLPQAGAFGEEVIVNSEY 211
Cdd:COG3700 187 KIHYGDSDDDILAAREAGIRGIRVLRASNSTYQPLPQAGGYGEEVIVNSEY 237
 
Name Accession Description Interval E-value
AphA COG3700
Acid phosphatase, class B [Inorganic ion transport and metabolism, General function prediction ...
 1-211 1.91e-165

Acid phosphatase, class B [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 442914  Cd Length: 237  Bit Score: 454.84  E-value: 1.91e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83754294   1 SPSPLNPGTNVARLAEQAPIHWVSVAQIENSLAGRPPMAVGFDIDDTVLFSSPGFWRGKKTFSPESEDYLKNPVFWEKMN 80
Cdd:COG3700  27 KVPYTQEGTTVAQLAQQAPIHWVSVEQIENSLKGKPPMAVGFDIDDTVLFSSPGFYYGKQKFSPGSYSYLKNQKFWDKMN 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83754294  81 NGWDEFSIPKEVARQLIDMHVRRGDAIFFVTGRSPTKTETVSKTLADNFHIPATNMNPVIFAGDKPGQNTKSQWLQDKNI 160
Cdd:COG3700 107 NGWDEFSIPKEVARALIAMHLKRGDQIYFITGRTATKTETVTKTLQKDFNIPAKNMNPVIFAGDKPGQYDKTQWIKKHNI 186

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 83754294 161 RIFYGDSDNDITAARDVGARGIRILRASNSTYKPLPQAGAFGEEVIVNSEY 211
Cdd:COG3700 187 KIHYGDSDDDILAAREAGIRGIRVLRASNSTYQPLPQAGGYGEEVIVNSEY 237
AphA TIGR01672
HAD superfamily (subfamily IIIB) phosphatase, TIGR01672; This family of proteins is a member ...
 1-211 3.33e-144

HAD superfamily (subfamily IIIB) phosphatase, TIGR01672; This family of proteins is a member of the IIIB subfamily (pfam02767) of the haloacid dehalogenase (HAD) superfamily of hydrolases. All characterized members of subfamily III and most characterized members of the HAD superfamily are phosphatases. HAD superfamily phosphatases contain active site residues in several conserved catalytic motifs, all of which are found conserved here. The AphA gene from E. coli has been characterized and shown to be an active phosphatase enzyme. This family has been previously described as the "class B non-specific bacterial acid phosphatase" (B-NSAP) family, where it is noted that the enzyme is secreted and has a broad substrate range. The possibility exists, however, that the enzyme is specific for an as yet undefined substrate. Supporting evidence for the inclusion in the HAD superfamily, whose phosphatase members are magnesium dependent, is the inhibition by EDTA and calcium ions, and stimulation by magnesium ion.


Pssm-ID: 273747  Cd Length: 237  Bit Score: 401.22  E-value: 3.33e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83754294     1 SPSPLNPGTNVARLAEQAPIHWVSVAQIENSLAGRPPMAVGFDIDDTVLFSSPGFWRGKKTFSPESEDYLKNPVFWEKMN 80
Cdd:TIGR01672  27 SPPYTQPGTNAARLAEQAPIHWISVAQIENSLEGRPPIAVSFDIDDTVLFSSPGFWRGKKTFSPGSEDYLKNQVFWEKVN 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83754294    81 NGWDEFSIPKEVARQLIDMHVRRGDAIFFVTGRSPTKTETVSKTLADNFHIPatNMNPVIFAGDKPG--QNTKSQWLQDK 158
Cdd:TIGR01672 107 NGWDEFSIPKEVARQLIDMHQRRGDAIFFVTGRTPGKTDTVSKTLAKNFHIP--AMNPVIFAGDKPGqyQYTKTQWIQDK 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 83754294   159 NIRIFYGDSDNDITAARDVGARGIRILRASNSTYKPLPQAGAFGEEVIVNSEY 211
Cdd:TIGR01672 185 NIRIHYGDSDNDITAAKEAGARGIRILRASNSTYKPLPQAGGYGEEVLVNSEY 237
HAD_CBAP cd07499
molecular class B acid phosphatases, similar to Escherichia coli AphA; class B acid ...
 25-211 1.80e-130

molecular class B acid phosphatases, similar to Escherichia coli AphA; class B acid phosphatases (CBAPs) have been detected in a minority of bacterial species which include a number of major pathogens such as Escherichia coli, Haemophilus influenzae, and Streptococcus pyogenes. This family includes the CBAP Escherichia coli AphA. The purified enzyme is a broad-spectrum nucleotidase highly active against both 3'- and 5'-mononucleotides and monodeoxynucleotides, which can also act as a phosphotransferase. 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: 319802  Cd Length: 185  Bit Score: 364.43  E-value: 1.80e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83754294  25 VAQIENSLAGRPPMAVGFDIDDTVLFSSPGFWRGKKTFSPESEDYLKNPVFWEKMNNGWDEFSIPKEVARQLIDMHVRRG 104
Cdd:cd07499   1 VAQIAKSLEGKAPIAVGFDIDDTVLFSSPCFYYGKQTFSPDSFDYLKNQKFWDKVNNGWDEFSIPKEIAKQLIDMHQKRG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83754294 105 DAIFFVTGRSPTKTETVSKTLADNFHIpaTNMNPVIFAGDKPGQNTKSQWLQDKNIRIFYGDSDNDITAARDVGARGIRI 184
Cdd:cd07499  81 DQIYFITGRTPGKTDTVTKTLAKDFHI--KNMNPVIFAGDKPVQYTKTQYIQKNNISIHYGDSDNDILAAREAGARGIRV 158

                       170       180
                ....*....|....*....|....*..
gi 83754294 185 LRASNSTYKPLPQAGAFGEEVIVNSEY 211
Cdd:cd07499 159 LRAANSTYKPLPKNGGYGEEVLVNSQY 185
Acid_phosphat_B pfam03767
HAD superfamily, subfamily IIIB (Acid phosphatase); This family proteins includes acid ...
 1-195 4.89e-40

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: 135.96  E-value: 4.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83754294     1 SPSPLNPGTNVARLAEQAP-------------IHWVS-----VAQIENSLAGRP-----PMAVGFDIDDTVLFSSPGF-- 55
Cdd:pfam03767   1 ASWRLAVETNNIRPFKTIPaecvdyvkdymngQQYSSdskavVDQAYNYAKERElhgdkKDAVVFDIDETVLSNSPYYay 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83754294    56 -WRGKKTFSPESedylknpvFWEKMNNGWDeFSIPKEVarQLIDMHVRRGDAIFFVTGRSPT-KTETVSKTLADNFHipa 133
Cdd:pfam03767  81 hGYGGEPFDPEK--------FDEWVNKGEA-PALPGAL--ELYNYLVELGVKIFFVSGRSEDlRAATVENLKKAGFH--- 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83754294   134 tNMNPVIFAGDKPGQNT-------KSQWLQDK--NIRIFYGDSDNDITaarDVGARGIRILRASNSTYKPL 195
Cdd:pfam03767 147 -GWEKLILRGKKDSNKSatsykseRRKKLVKKgyNIVGNIGDQWSDFL---GNGARGIRTFKLPNPMYYIW 213
 
Name Accession Description Interval E-value
AphA COG3700
Acid phosphatase, class B [Inorganic ion transport and metabolism, General function prediction ...
 1-211 1.91e-165

Acid phosphatase, class B [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 442914  Cd Length: 237  Bit Score: 454.84  E-value: 1.91e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83754294   1 SPSPLNPGTNVARLAEQAPIHWVSVAQIENSLAGRPPMAVGFDIDDTVLFSSPGFWRGKKTFSPESEDYLKNPVFWEKMN 80
Cdd:COG3700  27 KVPYTQEGTTVAQLAQQAPIHWVSVEQIENSLKGKPPMAVGFDIDDTVLFSSPGFYYGKQKFSPGSYSYLKNQKFWDKMN 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83754294  81 NGWDEFSIPKEVARQLIDMHVRRGDAIFFVTGRSPTKTETVSKTLADNFHIPATNMNPVIFAGDKPGQNTKSQWLQDKNI 160
Cdd:COG3700 107 NGWDEFSIPKEVARALIAMHLKRGDQIYFITGRTATKTETVTKTLQKDFNIPAKNMNPVIFAGDKPGQYDKTQWIKKHNI 186

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 83754294 161 RIFYGDSDNDITAARDVGARGIRILRASNSTYKPLPQAGAFGEEVIVNSEY 211
Cdd:COG3700 187 KIHYGDSDDDILAAREAGIRGIRVLRASNSTYQPLPQAGGYGEEVIVNSEY 237
AphA TIGR01672
HAD superfamily (subfamily IIIB) phosphatase, TIGR01672; This family of proteins is a member ...
 1-211 3.33e-144

HAD superfamily (subfamily IIIB) phosphatase, TIGR01672; This family of proteins is a member of the IIIB subfamily (pfam02767) of the haloacid dehalogenase (HAD) superfamily of hydrolases. All characterized members of subfamily III and most characterized members of the HAD superfamily are phosphatases. HAD superfamily phosphatases contain active site residues in several conserved catalytic motifs, all of which are found conserved here. The AphA gene from E. coli has been characterized and shown to be an active phosphatase enzyme. This family has been previously described as the "class B non-specific bacterial acid phosphatase" (B-NSAP) family, where it is noted that the enzyme is secreted and has a broad substrate range. The possibility exists, however, that the enzyme is specific for an as yet undefined substrate. Supporting evidence for the inclusion in the HAD superfamily, whose phosphatase members are magnesium dependent, is the inhibition by EDTA and calcium ions, and stimulation by magnesium ion.


Pssm-ID: 273747  Cd Length: 237  Bit Score: 401.22  E-value: 3.33e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83754294     1 SPSPLNPGTNVARLAEQAPIHWVSVAQIENSLAGRPPMAVGFDIDDTVLFSSPGFWRGKKTFSPESEDYLKNPVFWEKMN 80
Cdd:TIGR01672  27 SPPYTQPGTNAARLAEQAPIHWISVAQIENSLEGRPPIAVSFDIDDTVLFSSPGFWRGKKTFSPGSEDYLKNQVFWEKVN 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83754294    81 NGWDEFSIPKEVARQLIDMHVRRGDAIFFVTGRSPTKTETVSKTLADNFHIPatNMNPVIFAGDKPG--QNTKSQWLQDK 158
Cdd:TIGR01672 107 NGWDEFSIPKEVARQLIDMHQRRGDAIFFVTGRTPGKTDTVSKTLAKNFHIP--AMNPVIFAGDKPGqyQYTKTQWIQDK 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 83754294   159 NIRIFYGDSDNDITAARDVGARGIRILRASNSTYKPLPQAGAFGEEVIVNSEY 211
Cdd:TIGR01672 185 NIRIHYGDSDNDITAAKEAGARGIRILRASNSTYKPLPQAGGYGEEVLVNSEY 237
HAD_CBAP cd07499
molecular class B acid phosphatases, similar to Escherichia coli AphA; class B acid ...
 25-211 1.80e-130

molecular class B acid phosphatases, similar to Escherichia coli AphA; class B acid phosphatases (CBAPs) have been detected in a minority of bacterial species which include a number of major pathogens such as Escherichia coli, Haemophilus influenzae, and Streptococcus pyogenes. This family includes the CBAP Escherichia coli AphA. The purified enzyme is a broad-spectrum nucleotidase highly active against both 3'- and 5'-mononucleotides and monodeoxynucleotides, which can also act as a phosphotransferase. 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: 319802  Cd Length: 185  Bit Score: 364.43  E-value: 1.80e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83754294  25 VAQIENSLAGRPPMAVGFDIDDTVLFSSPGFWRGKKTFSPESEDYLKNPVFWEKMNNGWDEFSIPKEVARQLIDMHVRRG 104
Cdd:cd07499   1 VAQIAKSLEGKAPIAVGFDIDDTVLFSSPCFYYGKQTFSPDSFDYLKNQKFWDKVNNGWDEFSIPKEIAKQLIDMHQKRG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83754294 105 DAIFFVTGRSPTKTETVSKTLADNFHIpaTNMNPVIFAGDKPGQNTKSQWLQDKNIRIFYGDSDNDITAARDVGARGIRI 184
Cdd:cd07499  81 DQIYFITGRTPGKTDTVTKTLAKDFHI--KNMNPVIFAGDKPVQYTKTQYIQKNNISIHYGDSDNDILAAREAGARGIRV 158

                       170       180
                ....*....|....*....|....*..
gi 83754294 185 LRASNSTYKPLPQAGAFGEEVIVNSEY 211
Cdd:cd07499 159 LRAANSTYKPLPKNGGYGEEVLVNSQY 185
Acid_phosphat_B pfam03767
HAD superfamily, subfamily IIIB (Acid phosphatase); This family proteins includes acid ...
 1-195 4.89e-40

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: 135.96  E-value: 4.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83754294     1 SPSPLNPGTNVARLAEQAP-------------IHWVS-----VAQIENSLAGRP-----PMAVGFDIDDTVLFSSPGF-- 55
Cdd:pfam03767   1 ASWRLAVETNNIRPFKTIPaecvdyvkdymngQQYSSdskavVDQAYNYAKERElhgdkKDAVVFDIDETVLSNSPYYay 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83754294    56 -WRGKKTFSPESedylknpvFWEKMNNGWDeFSIPKEVarQLIDMHVRRGDAIFFVTGRSPT-KTETVSKTLADNFHipa 133
Cdd:pfam03767  81 hGYGGEPFDPEK--------FDEWVNKGEA-PALPGAL--ELYNYLVELGVKIFFVSGRSEDlRAATVENLKKAGFH--- 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83754294   134 tNMNPVIFAGDKPGQNT-------KSQWLQDK--NIRIFYGDSDNDITaarDVGARGIRILRASNSTYKPL 195
Cdd:pfam03767 147 -GWEKLILRGKKDSNKSatsykseRRKKLVKKgyNIVGNIGDQWSDFL---GNGARGIRTFKLPNPMYYIW 213
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 92-184 2.65e-07

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: 47.39  E-value: 2.65e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83754294  92 VARQLIDMHVRRGDAIFFVTGRSPTKTETVSKTLADNFHIPatnmnPVIFAGD--------KPGQNTKSQWLQDKNIRIF 163
Cdd:cd01427  11 LAVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFD-----GIIGSDGggtpkpkpKPLLLLLLKLGVDPEEVLF 85

                        90       100
                ....*....|....*....|.
gi 83754294 164 YGDSDNDITAARDVGARGIRI 184
Cdd:cd01427  86 VGDSENDIEAARAAGGRTVAV 106
HAD_CAP cd07534
molecular class C acid phosphatases, similar to Haemophilus influenzae e (P4) acid phosphatase; ...
 26-211 1.89e-05

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: 43.86  E-value: 1.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83754294  26 AQIENSLAGRPPmAVGFDIDDTVLFSSP-GFWRGK--KTFSPESedylknpvfwekmnngWDEFSIPKEV-----ARQLI 97
Cdd:cd07534  21 HALKKEKTDKKP-AVVLDLDETVLDNSPyQARQVKngKPFSPET----------------WDKWVQEAQAkpipgAVDFL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83754294  98 DMHVRRGDAIFFVTGRsptKTETVSKTLAD--NFHIPATNMNPVIFAGDKPGQNTKSQWLQDK-NIRIFYGDSDNDITAA 174
Cdd:cd07534  84 NYANAKGVTIFYVSNR---DQKLKAATLKNlkRLGFPQASDDHLLLKTDKSSKESRRQLVKEKyNIVLLFGDNLGDFGDF 160

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 83754294 175 RDVGARGIRilRASNSTYkplpqAGAFGEEVIV--NSEY 211
Cdd:cd07534 161 TYKKENEDR--RALVEKN-----AEEFGEKFIIlpNPMY 192
COG2503 COG2503
Predicted secreted acid phosphatase [General function prediction only];
26-174 2.38e-04

Predicted secreted acid phosphatase [General function prediction only];


Pssm-ID: 441997 [Multi-domain]  Cd Length: 269  Bit Score: 41.10  E-value: 2.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83754294  26 AQIENSLAGRPPmAVGFDIDDTVLFSSPgFW----RGKKTFSPESedylknpvfWEKmnngWDEFSIPKEV--ARQLIDM 99
Cdd:COG2503  70 AALAQPSGGKPP-AVVLDLDETVLDNSP-YQawliKNGKSFDPKT---------WDE----WVKEAQATAVpgAVEFLNY 134

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83754294 100 HVRRGDAIFFVTGRsptKTETVSKTLAD--NFHIPATNMNPVIFAGDKPGQNTKSQWLQDK-NIRIFYGDSDNDITAA 174
Cdd:COG2503 135 ANSKGVTVFYISNR---KAEEKAATLANlkALGFPVVDEDHLLLKTDGSDKEARRQAVAKRyRIVMLVGDNLGDFADA 209
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 93-171 5.73e-04

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


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 39.43  E-value: 5.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83754294  93 ARQLIDMHVRRGDAIFFVTGrSPtkTETVSKtLADNFHIP---ATNM------------NPVIFAGDKPgQNTKsQWLQD 157
Cdd:COG0560  93 ARELIAEHRAAGHKVAIVSG-GF--TFFVEP-IAERLGIDhviANELevedgrltgevvGPIVDGEGKA-EALR-ELAAE 166

                        90
                ....*....|....*...
gi 83754294 158 KNIR----IFYGDSDNDI 171
Cdd:COG0560 167 LGIDleqsYAYGDSANDL 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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