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Conserved domains on  [gi|15233504|ref|NP_194655|]
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HAD superfamily, subfamily IIIB acid phosphatase [Arabidopsis thaliana]

Protein Classification

HAD_VSP domain-containing protein( domain architecture ID 11576411)

HAD_VSP domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HAD_VSP cd07535
vegetative storage proteins similar to soybean VSPalpha and VSPbeta proteins; belongs to the ...
69-254 4.76e-112

vegetative storage proteins similar to soybean VSPalpha and VSPbeta proteins; belongs to the haloacid dehalogenase-like superfamily; Soybean [Glycine max (L.) Merr.] vegetative storage protein VSPalpha and VSPbeta levels were identified as storage proteins due to their abundance and pattern of expression in plant tissues, they accumulate to almost one-half the amount of soluble leaf protein when soybean plants are continually depodded. They possess acid phosphatase activity which appears to be low compared to several other plant acid phosphatases, it increases in the leaves of depodded soybean plants, but to no more than 0.1% of the total acid phosphatase activity in these leaves. This acid phosphatase activity has maximal activity at pH 5.0 - 5.5, and can liberate Pi from different substrates such as napthyl acid phosphate, carboxyphenyl phosphate, sugar-phosphates, glyceraldehyde 3-phosphate, dihydroxyacetone phosphate, phosphoenolpyruvate, ATP, ADP, PPi, and short chain polyphosphates; they cleave phosphoenolpyruvate, ATP, ADP, PPI, and polyphosphates most efficiently. 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. Soybean VSPalpha and VSPbeta lack this active site aspartate, other members of this family have this aspartate and may be more active. 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: 319837  Cd Length: 186  Bit Score: 319.71  E-value: 4.76e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504  69 VAEYLNGDQFLSDYSVIVDYALAFAKSVEISGDGKDVWIFDIDETLLTNIDYYKAHGYGSEPYDDNKFSEWVEQGTAPAF 148
Cdd:cd07535   1 VEDYMKGGQYLRDSSVKTVNALAYAYSKVLAGDGMDVWIFDIDDTLLSNIPYYKKHGYGGEKFDSTAFDEWVEKGKAPAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504 149 DASLRLYNALKKLGFTIILLTGRDEHQRTSTETNLRDAGYSGWERLLLRGPNDQGKSATNYKSEQRSKLIEEGFKIRGNS 228
Cdd:cd07535  81 PESLKLYNKLLELGFKIFLLSGRDETLRNATVENLKKAGYHGWEHLILRGPDDQGKSAVVYKSEQRKELEEKGYRIVGNI 160
                       170       180
                ....*....|....*....|....*.
gi 15233504 229 GDQWSDLQGFAVADRSFKVPNPMYYI 254
Cdd:cd07535 161 GDQWSDLLGDPEGDRTFKLPNPMYYI 186
 
Name Accession Description Interval E-value
HAD_VSP cd07535
vegetative storage proteins similar to soybean VSPalpha and VSPbeta proteins; belongs to the ...
69-254 4.76e-112

vegetative storage proteins similar to soybean VSPalpha and VSPbeta proteins; belongs to the haloacid dehalogenase-like superfamily; Soybean [Glycine max (L.) Merr.] vegetative storage protein VSPalpha and VSPbeta levels were identified as storage proteins due to their abundance and pattern of expression in plant tissues, they accumulate to almost one-half the amount of soluble leaf protein when soybean plants are continually depodded. They possess acid phosphatase activity which appears to be low compared to several other plant acid phosphatases, it increases in the leaves of depodded soybean plants, but to no more than 0.1% of the total acid phosphatase activity in these leaves. This acid phosphatase activity has maximal activity at pH 5.0 - 5.5, and can liberate Pi from different substrates such as napthyl acid phosphate, carboxyphenyl phosphate, sugar-phosphates, glyceraldehyde 3-phosphate, dihydroxyacetone phosphate, phosphoenolpyruvate, ATP, ADP, PPi, and short chain polyphosphates; they cleave phosphoenolpyruvate, ATP, ADP, PPI, and polyphosphates most efficiently. 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. Soybean VSPalpha and VSPbeta lack this active site aspartate, other members of this family have this aspartate and may be more active. 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: 319837  Cd Length: 186  Bit Score: 319.71  E-value: 4.76e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504  69 VAEYLNGDQFLSDYSVIVDYALAFAKSVEISGDGKDVWIFDIDETLLTNIDYYKAHGYGSEPYDDNKFSEWVEQGTAPAF 148
Cdd:cd07535   1 VEDYMKGGQYLRDSSVKTVNALAYAYSKVLAGDGMDVWIFDIDDTLLSNIPYYKKHGYGGEKFDSTAFDEWVEKGKAPAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504 149 DASLRLYNALKKLGFTIILLTGRDEHQRTSTETNLRDAGYSGWERLLLRGPNDQGKSATNYKSEQRSKLIEEGFKIRGNS 228
Cdd:cd07535  81 PESLKLYNKLLELGFKIFLLSGRDETLRNATVENLKKAGYHGWEHLILRGPDDQGKSAVVYKSEQRKELEEKGYRIVGNI 160
                       170       180
                ....*....|....*....|....*.
gi 15233504 229 GDQWSDLQGFAVADRSFKVPNPMYYI 254
Cdd:cd07535 161 GDQWSDLLGDPEGDRTFKLPNPMYYI 186
Acid_phosphat_B pfam03767
HAD superfamily, subfamily IIIB (Acid phosphatase); This family proteins includes acid ...
44-255 2.71e-104

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: 301.21  E-value: 2.71e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504    44 DSWRLAAETNNVGTWDLIPSICVDSVAEYLNGDQFLSDYSVIVDYALAFAKSVEISGDGKDVWIFDIDETLLTNIDYYKA 123
Cdd:pfam03767   1 ASWRLAVETNNIRPFKTIPAECVDYVKDYMNGQQYSSDSKAVVDQAYNYAKERELHGDKKDAVVFDIDETVLSNSPYYAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504   124 HGYGSEPYDDNKFSEWVEQGTAPAFDASLRLYNALKKLGFTIILLTGRDEHQRTSTETNLRDAGYSGWERLLLRGPNDQG 203
Cdd:pfam03767  81 HGYGGEPFDPEKFDEWVNKGEAPALPGALELYNYLVELGVKIFFVSGRSEDLRAATVENLKKAGFHGWEKLILRGKKDSN 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15233504   204 KSATNYKSEQRSKLIEEGFKIRGNSGDQWSDLQG-FAVADRSFKVPNPMYYIP 255
Cdd:pfam03767 161 KSATSYKSERRKKLVKKGYNIVGNIGDQWSDFLGnGARGIRTFKLPNPMYYIW 213
plant-AP TIGR01675
plant acid phosphatase; This model represents a family of acid phosphatase from plants which ...
36-255 7.47e-98

plant acid phosphatase; This model represents a family of acid phosphatase from plants which are most closely related to the (so called) class B non-specific acid phosphatase OlpA (TIGR01533, which is believed to be a 5'-nucleotide phosphatase) and somewhat more distantly to another class B phosphatase, AphA (TIGR01672). Together these three clades define a subfamily (pfam03767) which corresponds to the IIIB subfamily of the haloacid dehalogenase (HAD) superfamily of aspartate nucleophile hydrolases. It has been reported that the best substrate for this enzyme that could be found was purine 5'-nucleoside phosphates. This is in concordance with the assignment of the H. influenzae hel protein (from TIGR01533) as a 5'-nucleotidase, however there is presently no other evidence to support this specific function for these plant phosphatases. Many genes from this family have been annotated as vegetative storage proteins due to their close homology with these earlier-characterized gene products, which are highly expressed in leaves. There are significant differences however, including expression levels and distribution. The most important difference is the lack in authentic VSPs of the nucleophilic aspartate residue, which is instead replaced by serine, glycine or asparagine. Thus these proteins can not be expected to be active phosphatases. This issue was confused by the publication in 1992 of an article claiming activity for the Glycine max VSP. In 1994 this assertion was refuted by the separation of the activity from the VSP. This model explicitly excludes the VSPs which lack the nucleophilc aspartate. The possibility exists, however, that some members of this family may, while containing all of the conserved HAD-superfamily catalytic residues, lack activity and have a function related to the function of the VSPs rather than the acid phosphatases.


Pssm-ID: 273749  Cd Length: 228  Bit Score: 285.49  E-value: 7.47e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504    36 GSDGSRYCDSWRLAAETNNVGTWDLIPSICVDSVAEYLNGDQFLSDYSVIVDYALAFAKSVEISGDGKDVWIFDIDETLL 115
Cdd:TIGR01675   9 LSIDYGYCRSWRLGVETNNIRKWDTVPAECKDYVEDYMTSKQYKRDSKRVVDEAYFYAKSLALSGDGMDAWIFDVDDTLL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504   116 TNIDYYKAHGYGSEPYDDNKFSEWVEQGTAPAFDASLRLYNALKKLGFTIILLTGRDEHQRTSTETNLRDAGYSGWERLL 195
Cdd:TIGR01675  89 SNIPYYKKHGYGTEKTDPTAFWDWLEKGEAPALPETLKLYQKLLELGIKIFLLSGRWEELRSATVENLINAGFTGWKHLI 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504   196 LRGPNDQGKSATNYKSEQRSKLIEEGFKIRGNSGDQWSDLQGFAVADRSFKVPNPMYYIP 255
Cdd:TIGR01675 169 LRGLEDSQKTVVTYKSEVRKSLVEEGYRIVGNIGDQWSDLLGSPPGRRTFKLPNPMYYVP 228
COG2503 COG2503
Predicted secreted acid phosphatase [General function prediction only];
99-252 6.57e-14

Predicted secreted acid phosphatase [General function prediction only];


Pssm-ID: 441997 [Multi-domain]  Cd Length: 269  Bit Score: 69.61  E-value: 6.57e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504  99 SGDGKDVWIFDIDETLLTNIDYYkahGY---GSEPYDDNKFSEWVEQGTAPAFDASLRLYNALKKLGFTIILLTGRDEHQ 175
Cdd:COG2503  76 SGGKPPAVVLDLDETVLDNSPYQ---AWlikNGKSFDPKTWDEWVKEAQATAVPGAVEFLNYANSKGVTVFYISNRKAEE 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504 176 RTSTETNLRDAG--YSGWERLLLRgpndQGKSAtnyKSEQRsKLIEEGFKIRGNSGDQWSD----LQGFAVADRSFKV-- 247
Cdd:COG2503 153 KAATLANLKALGfpVVDEDHLLLK----TDGSD---KEARR-QAVAKRYRIVMLVGDNLGDfadaFDKKSNAERRALVeq 224
                       170
                ....*....|....*..
gi 15233504 248 ------------PNPMY 252
Cdd:COG2503 225 naakfgtkwivlPNPMY 241
 
Name Accession Description Interval E-value
HAD_VSP cd07535
vegetative storage proteins similar to soybean VSPalpha and VSPbeta proteins; belongs to the ...
69-254 4.76e-112

vegetative storage proteins similar to soybean VSPalpha and VSPbeta proteins; belongs to the haloacid dehalogenase-like superfamily; Soybean [Glycine max (L.) Merr.] vegetative storage protein VSPalpha and VSPbeta levels were identified as storage proteins due to their abundance and pattern of expression in plant tissues, they accumulate to almost one-half the amount of soluble leaf protein when soybean plants are continually depodded. They possess acid phosphatase activity which appears to be low compared to several other plant acid phosphatases, it increases in the leaves of depodded soybean plants, but to no more than 0.1% of the total acid phosphatase activity in these leaves. This acid phosphatase activity has maximal activity at pH 5.0 - 5.5, and can liberate Pi from different substrates such as napthyl acid phosphate, carboxyphenyl phosphate, sugar-phosphates, glyceraldehyde 3-phosphate, dihydroxyacetone phosphate, phosphoenolpyruvate, ATP, ADP, PPi, and short chain polyphosphates; they cleave phosphoenolpyruvate, ATP, ADP, PPI, and polyphosphates most efficiently. 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. Soybean VSPalpha and VSPbeta lack this active site aspartate, other members of this family have this aspartate and may be more active. 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: 319837  Cd Length: 186  Bit Score: 319.71  E-value: 4.76e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504  69 VAEYLNGDQFLSDYSVIVDYALAFAKSVEISGDGKDVWIFDIDETLLTNIDYYKAHGYGSEPYDDNKFSEWVEQGTAPAF 148
Cdd:cd07535   1 VEDYMKGGQYLRDSSVKTVNALAYAYSKVLAGDGMDVWIFDIDDTLLSNIPYYKKHGYGGEKFDSTAFDEWVEKGKAPAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504 149 DASLRLYNALKKLGFTIILLTGRDEHQRTSTETNLRDAGYSGWERLLLRGPNDQGKSATNYKSEQRSKLIEEGFKIRGNS 228
Cdd:cd07535  81 PESLKLYNKLLELGFKIFLLSGRDETLRNATVENLKKAGYHGWEHLILRGPDDQGKSAVVYKSEQRKELEEKGYRIVGNI 160
                       170       180
                ....*....|....*....|....*.
gi 15233504 229 GDQWSDLQGFAVADRSFKVPNPMYYI 254
Cdd:cd07535 161 GDQWSDLLGDPEGDRTFKLPNPMYYI 186
Acid_phosphat_B pfam03767
HAD superfamily, subfamily IIIB (Acid phosphatase); This family proteins includes acid ...
44-255 2.71e-104

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: 301.21  E-value: 2.71e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504    44 DSWRLAAETNNVGTWDLIPSICVDSVAEYLNGDQFLSDYSVIVDYALAFAKSVEISGDGKDVWIFDIDETLLTNIDYYKA 123
Cdd:pfam03767   1 ASWRLAVETNNIRPFKTIPAECVDYVKDYMNGQQYSSDSKAVVDQAYNYAKERELHGDKKDAVVFDIDETVLSNSPYYAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504   124 HGYGSEPYDDNKFSEWVEQGTAPAFDASLRLYNALKKLGFTIILLTGRDEHQRTSTETNLRDAGYSGWERLLLRGPNDQG 203
Cdd:pfam03767  81 HGYGGEPFDPEKFDEWVNKGEAPALPGALELYNYLVELGVKIFFVSGRSEDLRAATVENLKKAGFHGWEKLILRGKKDSN 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15233504   204 KSATNYKSEQRSKLIEEGFKIRGNSGDQWSDLQG-FAVADRSFKVPNPMYYIP 255
Cdd:pfam03767 161 KSATSYKSERRKKLVKKGYNIVGNIGDQWSDFLGnGARGIRTFKLPNPMYYIW 213
plant-AP TIGR01675
plant acid phosphatase; This model represents a family of acid phosphatase from plants which ...
36-255 7.47e-98

plant acid phosphatase; This model represents a family of acid phosphatase from plants which are most closely related to the (so called) class B non-specific acid phosphatase OlpA (TIGR01533, which is believed to be a 5'-nucleotide phosphatase) and somewhat more distantly to another class B phosphatase, AphA (TIGR01672). Together these three clades define a subfamily (pfam03767) which corresponds to the IIIB subfamily of the haloacid dehalogenase (HAD) superfamily of aspartate nucleophile hydrolases. It has been reported that the best substrate for this enzyme that could be found was purine 5'-nucleoside phosphates. This is in concordance with the assignment of the H. influenzae hel protein (from TIGR01533) as a 5'-nucleotidase, however there is presently no other evidence to support this specific function for these plant phosphatases. Many genes from this family have been annotated as vegetative storage proteins due to their close homology with these earlier-characterized gene products, which are highly expressed in leaves. There are significant differences however, including expression levels and distribution. The most important difference is the lack in authentic VSPs of the nucleophilic aspartate residue, which is instead replaced by serine, glycine or asparagine. Thus these proteins can not be expected to be active phosphatases. This issue was confused by the publication in 1992 of an article claiming activity for the Glycine max VSP. In 1994 this assertion was refuted by the separation of the activity from the VSP. This model explicitly excludes the VSPs which lack the nucleophilc aspartate. The possibility exists, however, that some members of this family may, while containing all of the conserved HAD-superfamily catalytic residues, lack activity and have a function related to the function of the VSPs rather than the acid phosphatases.


Pssm-ID: 273749  Cd Length: 228  Bit Score: 285.49  E-value: 7.47e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504    36 GSDGSRYCDSWRLAAETNNVGTWDLIPSICVDSVAEYLNGDQFLSDYSVIVDYALAFAKSVEISGDGKDVWIFDIDETLL 115
Cdd:TIGR01675   9 LSIDYGYCRSWRLGVETNNIRKWDTVPAECKDYVEDYMTSKQYKRDSKRVVDEAYFYAKSLALSGDGMDAWIFDVDDTLL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504   116 TNIDYYKAHGYGSEPYDDNKFSEWVEQGTAPAFDASLRLYNALKKLGFTIILLTGRDEHQRTSTETNLRDAGYSGWERLL 195
Cdd:TIGR01675  89 SNIPYYKKHGYGTEKTDPTAFWDWLEKGEAPALPETLKLYQKLLELGIKIFLLSGRWEELRSATVENLINAGFTGWKHLI 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504   196 LRGPNDQGKSATNYKSEQRSKLIEEGFKIRGNSGDQWSDLQGFAVADRSFKVPNPMYYIP 255
Cdd:TIGR01675 169 LRGLEDSQKTVVTYKSEVRKSLVEEGYRIVGNIGDQWSDLLGSPPGRRTFKLPNPMYYVP 228
Veg_Stor_Prot TIGR01680
vegetative storage protein; The proteins represented by this model are close relatives of the ...
36-250 1.37e-72

vegetative storage protein; The proteins represented by this model are close relatives of the plant acid phosphatases (TIGR01675), are limited to members of the Phaseoleae including Glycine max (soybean) and Phaseolus vulgaris (kidney bean). These proteins are highly expressed in the leaves of repeatedly depodded plants. VSP differs most strinkingly from the acid phosphatases in the lack of the conserved nucleophilic aspartate residue in the N-terminus, thus, they should be inactive as phosphatases. This issue was confused by the publication in 1992 of an article claiming activity for the Glycine max VSP. In 1994 this assertion was refuted by the separation of the activity from the VSP.


Pssm-ID: 130741  Cd Length: 275  Bit Score: 223.07  E-value: 1.37e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504    36 GSDGSRYCDSWRLAAETNNVGTWDLIPSICVDSVAEYLNGDQFLSDYSVIVDYALAFAKSVEISGdgKDVWIFDIDETLL 115
Cdd:TIGR01680  36 ARDPEVKCASWRLAVEAHNIFGFETIPEECVDATAEYIEGEQYRSDSKTVNQQAYFFARDLEVHE--KDTFLFNIDGTAL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504   116 TNIDYYKAHGYGSEPYDDNKF-SEWVEQGTAPAFDASLRLYNALKKLGFTIILLTGRDEHQRTSTETNLRDAGYSGWERL 194
Cdd:TIGR01680 114 SNIPYYKKHGYGSEKFDSELYdEEFVNKGEAPALPETLKNYNKLVSLGFKIIFLSGRLKDKQAVTEANLKKAGYHTWEKL 193
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15233504   195 LLRGPND-QGKSATNYKSEQRSKLIEEGFKIRGNSGDQWSDLQG-FAVADRSFKVPNP 250
Cdd:TIGR01680 194 ILKDPQDnSAENAVEYKTAARAKLIQEGYNIVGIIGDQWNDLKGeHRGAIRSFKLPNP 251
HAD_VSP_like cd01624
vegetative storage proteins and related proteins, similar to soybean VSPalpha and VSPbeta ...
101-252 6.80e-40

vegetative storage proteins and related proteins, similar to soybean VSPalpha and VSPbeta proteins; belongs to the haloacid dehalogenase-like superfamily; Soybean [Glycine max (L.) Merr.] vegetative storage protein VSPalpha and VSPbeta levels were identified as storage proteins due to their abundance and pattern of expression in plant tissues, they accumulate to almost one-half the amount of soluble leaf protein when soybean plants are continually depodded. They possess acid phosphatase activity which appears to be low compared to several other plant acid phosphatases; it increases in the leaves of depodded soybean plants, but to no more than 0.1% of the total acid phosphatase activity in these leaves. This acid phosphatase activity has maximal activity at pH 5.0 - 5.5, and can liberate Pi from different substrates such as napthyl acid phosphate, carboxyphenyl phosphate, sugar-phosphates, glyceraldehyde 3-phosphate, dihydroxyacetone phosphate, phosphoenolpyruvate, ATP, ADP, PPi, and short chain polyphosphates; they cleave phosphoenolpyruvate, ATP, ADP, PPI, and polyphosphates most efficiently. 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. Soybean VSPalpha and VSPbeta lack this active site aspartate, other members of this family have this aspartate and may be more active. 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: 319765 [Multi-domain]  Cd Length: 160  Bit Score: 135.36  E-value: 6.80e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504 101 DGKDVWIFDIDETLLTNIDYYKAHGyGSEPYDDNKFSEWVEQGTAPAFDASLRLYNALKKLGFTIILLTGRDEHQRTSTE 180
Cdd:cd01624  11 DTVNAWVFDIDDTLLSSIDYLKKYG-GTEGTAPGIWNSWLERGDSPPVPETLELAEYALEKGVEVFFISDRWEKLREPTV 89
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15233504 181 TNLRDAGYSGWERLLLRGPNDQGKSATNYKSEQRSKLIEEGFKIRGNSGDQWSDLQGfAVADRSFKVPNPMY 252
Cdd:cd01624  90 ENLKAAGYTVWSHLFLKPNGNKSKTVVVYKAKVRASIESKGYTIVANIGDQWSDLVG-GYAERTFKLPNYLY 160
COG2503 COG2503
Predicted secreted acid phosphatase [General function prediction only];
99-252 6.57e-14

Predicted secreted acid phosphatase [General function prediction only];


Pssm-ID: 441997 [Multi-domain]  Cd Length: 269  Bit Score: 69.61  E-value: 6.57e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504  99 SGDGKDVWIFDIDETLLTNIDYYkahGY---GSEPYDDNKFSEWVEQGTAPAFDASLRLYNALKKLGFTIILLTGRDEHQ 175
Cdd:COG2503  76 SGGKPPAVVLDLDETVLDNSPYQ---AWlikNGKSFDPKTWDEWVKEAQATAVPGAVEFLNYANSKGVTVFYISNRKAEE 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504 176 RTSTETNLRDAG--YSGWERLLLRgpndQGKSAtnyKSEQRsKLIEEGFKIRGNSGDQWSD----LQGFAVADRSFKV-- 247
Cdd:COG2503 153 KAATLANLKALGfpVVDEDHLLLK----TDGSD---KEARR-QAVAKRYRIVMLVGDNLGDfadaFDKKSNAERRALVeq 224
                       170
                ....*....|....*..
gi 15233504 248 ------------PNPMY 252
Cdd:COG2503 225 naakfgtkwivlPNPMY 241
HAD_CAP cd07534
molecular class C acid phosphatases, similar to Haemophilus influenzae e (P4) acid phosphatase; ...
100-252 1.01e-12

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: 65.05  E-value: 1.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504 100 GDGKDVWIFDIDETLLTNIDYYKAHGYGSEPYDDNKFSEWVEQGTAPAFDASLRLYNALKKLGFTIILLTGRDEHQRTST 179
Cdd:cd07534  28 TDKKPAVVLDLDETVLDNSPYQARQVKNGKPFSPETWDKWVQEAQAKPIPGAVDFLNYANAKGVTIFYVSNRDQKLKAAT 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504 180 ETNLRDAG--YSGWERLLLRGpndqGKSAtnykSEQRSKLIEEGFKIRGNSGDQWSDLQGFA----VADRSFKV------ 247
Cdd:cd07534 108 LKNLKRLGfpQASDDHLLLKT----DKSS----KESRRQLVKEKYNIVLLFGDNLGDFGDFTykkeNEDRRALVeknaee 179
                       170
                ....*....|...
gi 15233504 248 --------PNPMY 252
Cdd:cd07534 180 fgekfiilPNPMY 192
HAD_PNKP-C cd07502
C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related ...
107-225 3.06e-06

C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related phosphatases; This family includes the C-terminal domain of the bifunctional enzyme T4 polynucleotide kinase/phosphatase, PNKP. The PNKP phosphatase domain can catalyze the hydrolytic removal of the 3'-phosphoryl of DNA, RNA and deoxynucleoside 3'-monophosphates. 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: 319805  Cd Length: 145  Bit Score: 45.60  E-value: 3.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233504 107 IFDIDETLlTNIDyykahgyGSEPYDDNKFSEWVEQGTAPAFDASLR----LYNALKKLGFTIILLTGRDEHQRTSTETN 182
Cdd:cd07502   5 IFDLDGTL-ADTN-------GRQPYLERRPRDWDAFFEAADHDPPNApvieLVKESALTGYEIVYLSGRPERYRRDTLRW 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15233504 183 LRDAGYSgWERLLLRGPNDQGKsATNYKSEQRSKLIEEGFKIR 225
Cdd:cd07502  77 LAKHGIP-DDALHMRGNADRRK-DRRVKLEILRRLIRTRFEVR 117
 
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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