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Conserved domains on  [gi|744594755|ref|XP_010988447|]
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haloacid dehalogenase-like hydrolase domain-containing protein 2 isoform X1 [Camelus dromedarius]

Protein Classification

HAD-IIA family hydrolase( domain architecture ID 11576289)

HAD (haloacid dehalogenase)-IIA family hydrolase such as vertebrate haloacid dehalogenase-like hydrolase domain-containing protein 2 and phospholysine phosphohistidine inorganic pyrophosphate phosphatase, which hydrolyzes imidodiphosphate, 3-phosphohistidine and 6-phospholysine, as well as inorganic diphosphate with lower efficiency

CATH:  3.30.1240.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  16889794|15337123|33940035|37786806

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 8-255 1.12e-158

inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP); LHPP hydrolyzes nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate as well as oxygen-phosphorus bonds in inorganic pyrophosphate in vitro. This family also includes human haloacid dehalogenase like hydrolase domain containing 2 protine (HDHD2) a phosphatase which may be involved in polygenic hypertension. 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: 319812 [Multi-domain]  Cd Length: 248  Bit Score: 440.18  E-value: 1.12e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755   8 KAVLVDLNGTLHIEDAAVPGAQEALKRLRATSVVVKFVTNTTKESKQDLMERLKKLEFDISEDEIFTSLTAARNLVEQKQ 87
Cdd:cd07509    1 KAVLLDLSGTLYISGAAIPGAAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQRLGFDVSEEEIFTSLTAARQYLEEKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  88 VRPMLLVDDRALPDFKGIQTSDPNAVVIGLAPEHFHYQILNQAFRLLLDGAPLIAIHKARYYKRKDGLALGPGPFVTALE 167
Cdd:cd07509   81 LRPHLLVDDDALEDFIGIDTSDPNAVVIGDAGEHFNYQTLNRAFRLLLDGAPLIALHKGRYYKRKDGLALDPGAFVTGLE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755 168 FATDTKATVVGKPAQTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQNVGMRGILVKTGKYRAADEEKINPAPYLTCESF 247
Cdd:cd07509  161 YATGIKATVVGKPSPEFFLSALRSLGVDPEEAVMIGDDLRDDVGGAQACGMRGILVRTGKYRPSDEKKPNVPPDLTADSF 240


                 ....*...
gi 744594755 248 PHAVDHIL 255
Cdd:cd07509  241 ADAVDHIL 248
 
Name Accession Description Interval E-value
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 8-255 1.12e-158

inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP); LHPP hydrolyzes nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate as well as oxygen-phosphorus bonds in inorganic pyrophosphate in vitro. This family also includes human haloacid dehalogenase like hydrolase domain containing 2 protine (HDHD2) a phosphatase which may be involved in polygenic hypertension. 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: 319812 [Multi-domain]  Cd Length: 248  Bit Score: 440.18  E-value: 1.12e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755   8 KAVLVDLNGTLHIEDAAVPGAQEALKRLRATSVVVKFVTNTTKESKQDLMERLKKLEFDISEDEIFTSLTAARNLVEQKQ 87
Cdd:cd07509    1 KAVLLDLSGTLYISGAAIPGAAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQRLGFDVSEEEIFTSLTAARQYLEEKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  88 VRPMLLVDDRALPDFKGIQTSDPNAVVIGLAPEHFHYQILNQAFRLLLDGAPLIAIHKARYYKRKDGLALGPGPFVTALE 167
Cdd:cd07509   81 LRPHLLVDDDALEDFIGIDTSDPNAVVIGDAGEHFNYQTLNRAFRLLLDGAPLIALHKGRYYKRKDGLALDPGAFVTGLE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755 168 FATDTKATVVGKPAQTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQNVGMRGILVKTGKYRAADEEKINPAPYLTCESF 247
Cdd:cd07509  161 YATGIKATVVGKPSPEFFLSALRSLGVDPEEAVMIGDDLRDDVGGAQACGMRGILVRTGKYRPSDEKKPNVPPDLTADSF 240


                 ....*...
gi 744594755 248 PHAVDHIL 255
Cdd:cd07509  241 ADAVDHIL 248
HAD-SF-IIA-hyp3 TIGR01458
HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of ...
 7-257 3.11e-149

HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of the IIA subfamily (TIGR01460) of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. One sequence (GP|10716807) has been annotated as a "phospholysine phosphohistidine inorganic pyrophosphatase," probably in reference to studies on similarly described (but unsequenced) enzymes from bovine and rat tissues. However, the supporting information for this annotation has never been published. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 162372 [Multi-domain]  Cd Length: 257  Bit Score: 416.96  E-value: 3.11e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755    7 LKAVLVDLNGTLHIEDA----AVPGAQEALKRLRATSVVVKFVTNTTKESKQDLMERLKKLEFDISEDEIFTSLTAARNL 82
Cdd:TIGR01458   1 VKGVLLDISGVLYISDAgggtAVPGSQEAVKRLRGASVKVRFVTNTTKESKQDLLERLQRLGFDISEDEVFTPAPAARQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755   83 VEQKQVRPMLLVDDRALPDFKGIQTSDPNAVVIGLAPEHFHYQILNQAFRLLLDGAP--LIAIHKARYYKRKDGLALGPG 160
Cdd:TIGR01458  81 LEEKQLRPMLLVDDRVLPDFDGIDTSDPNCVVMGLAPEHFSYQILNQAFRLLLDGAKpvLIAIGKGRYYKRKDGLALDVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  161 PFVTALEFATDTKATVVGKPAQTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQNVGMRGILVKTGKYRAADEEKINPAP 240
Cdd:TIGR01458 161 PFVTALEYATDTKATVVGKPSKTFFLEALRATGCEPEEAVMIGDDCRDDVGGAQDCGMRGIQVRTGKYRPSDEEKINVPP 240

                         250
                  ....*....|....*..
gi 744594755  241 YLTCESFPHAVDHILQH 257
Cdd:TIGR01458 241 DLTCDSLPHAVDLILQH 257
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
8-247 1.46e-74

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 227.68  E-value: 1.46e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755   8 KAVLVDLNGTLHIEDAAVPGAQEALKRLRATSVVVKFVTNTTKESKQDLMERLKKLEFDISEDEIFTSLTAARNLVEQKQ 87
Cdd:COG0647    9 DAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATAAYLAERH 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  88 V--RPMLLVDDRALPDFKGI-----QTSDPNAVVIGLAPEhFHYQILNQAFRLLLDGAPLIAIHKARYYKRKDGLALGPG 160
Cdd:COG0647   89 PgaRVYVIGEEGLREELEEAgltlvDDEEPDAVVVGLDRT-FTYEKLAEALRAIRRGAPFIATNPDRTVPTEDGLIPGAG 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755 161 PFVTALEFATDTKATVVGKPAQTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQNVGMRGILVKTGKYRAADEEKINPAP 240
Cdd:COG0647  168 ALAAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAGLDTLLVLTGVTTAEDLEAAPIRP 247


                 ....*..
gi 744594755 241 YLTCESF 247
Cdd:COG0647  248 DYVLDSL 254
Hydrolase_like pfam13242
HAD-hyrolase-like;
176-250 2.60e-23

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 89.98  E-value: 2.60e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 744594755  176 VVGKPAQTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQNVGMRGILVKTGKYRAADEEKINPAPYLTCESFPHA 250
Cdd:pfam13242   1 VCGKPNPGMLERALARLGLDPERTVMIGDRLDTDILGAREAGARTILVLTGVTRPADLEKAPIRPDYVVDDLAEA 75
PRK10444 PRK10444
HAD-IIA family hydrolase;
7-252 3.68e-16

HAD-IIA family hydrolase;


Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 75.60  E-value: 3.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755   7 LKAVLVDLNGTLHIEDAAVPGAQEALKRLRATSVVVKFVTNTTKESKQDLMERLKKLEFDISEDEIFTSLTAARNLVEQK 86
Cdd:PRK10444   1 IKNVICDIDGVLMHDNVAVPGAAEFLHRILDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFLRRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  87 QVRPMLLVDDRALPD--FKG---IQTSDPNAVVIGlAPEHFHYQILNQAFRLLLDGAPLIAIHKARYykrkdGLALGP-- 159
Cdd:PRK10444  81 EGKKAYVIGEGALIHelYKAgftITDINPDFVIVG-ETRSYNWDMMHKAAYFVANGARFIATNPDTH-----GRGFYPac 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755 160 GPFVTALEFATDTKATVVGKPAQTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQNVGMRGILVKTGKYRAADeekINPA 239
Cdd:PRK10444 155 GALCAGIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILVLSGVSTLDD---IDSM 231

                        250
                 ....*....|...
gi 744594755 240 PYLTCESFPHAVD 252
Cdd:PRK10444 232 PFRPSWIYPSVAD 244
 
Name Accession Description Interval E-value
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 8-255 1.12e-158

inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP); LHPP hydrolyzes nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate as well as oxygen-phosphorus bonds in inorganic pyrophosphate in vitro. This family also includes human haloacid dehalogenase like hydrolase domain containing 2 protine (HDHD2) a phosphatase which may be involved in polygenic hypertension. 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: 319812 [Multi-domain]  Cd Length: 248  Bit Score: 440.18  E-value: 1.12e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755   8 KAVLVDLNGTLHIEDAAVPGAQEALKRLRATSVVVKFVTNTTKESKQDLMERLKKLEFDISEDEIFTSLTAARNLVEQKQ 87
Cdd:cd07509    1 KAVLLDLSGTLYISGAAIPGAAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQRLGFDVSEEEIFTSLTAARQYLEEKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  88 VRPMLLVDDRALPDFKGIQTSDPNAVVIGLAPEHFHYQILNQAFRLLLDGAPLIAIHKARYYKRKDGLALGPGPFVTALE 167
Cdd:cd07509   81 LRPHLLVDDDALEDFIGIDTSDPNAVVIGDAGEHFNYQTLNRAFRLLLDGAPLIALHKGRYYKRKDGLALDPGAFVTGLE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755 168 FATDTKATVVGKPAQTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQNVGMRGILVKTGKYRAADEEKINPAPYLTCESF 247
Cdd:cd07509  161 YATGIKATVVGKPSPEFFLSALRSLGVDPEEAVMIGDDLRDDVGGAQACGMRGILVRTGKYRPSDEKKPNVPPDLTADSF 240


                 ....*...
gi 744594755 248 PHAVDHIL 255
Cdd:cd07509  241 ADAVDHIL 248
HAD-SF-IIA-hyp3 TIGR01458
HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of ...
 7-257 3.11e-149

HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of the IIA subfamily (TIGR01460) of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. One sequence (GP|10716807) has been annotated as a "phospholysine phosphohistidine inorganic pyrophosphatase," probably in reference to studies on similarly described (but unsequenced) enzymes from bovine and rat tissues. However, the supporting information for this annotation has never been published. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 162372 [Multi-domain]  Cd Length: 257  Bit Score: 416.96  E-value: 3.11e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755    7 LKAVLVDLNGTLHIEDA----AVPGAQEALKRLRATSVVVKFVTNTTKESKQDLMERLKKLEFDISEDEIFTSLTAARNL 82
Cdd:TIGR01458   1 VKGVLLDISGVLYISDAgggtAVPGSQEAVKRLRGASVKVRFVTNTTKESKQDLLERLQRLGFDISEDEVFTPAPAARQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755   83 VEQKQVRPMLLVDDRALPDFKGIQTSDPNAVVIGLAPEHFHYQILNQAFRLLLDGAP--LIAIHKARYYKRKDGLALGPG 160
Cdd:TIGR01458  81 LEEKQLRPMLLVDDRVLPDFDGIDTSDPNCVVMGLAPEHFSYQILNQAFRLLLDGAKpvLIAIGKGRYYKRKDGLALDVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  161 PFVTALEFATDTKATVVGKPAQTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQNVGMRGILVKTGKYRAADEEKINPAP 240
Cdd:TIGR01458 161 PFVTALEYATDTKATVVGKPSKTFFLEALRATGCEPEEAVMIGDDCRDDVGGAQDCGMRGIQVRTGKYRPSDEEKINVPP 240

                         250
                  ....*....|....*..
gi 744594755  241 YLTCESFPHAVDHILQH 257
Cdd:TIGR01458 241 DLTCDSLPHAVDLILQH 257
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
8-247 1.46e-74

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 227.68  E-value: 1.46e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755   8 KAVLVDLNGTLHIEDAAVPGAQEALKRLRATSVVVKFVTNTTKESKQDLMERLKKLEFDISEDEIFTSLTAARNLVEQKQ 87
Cdd:COG0647    9 DAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATAAYLAERH 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  88 V--RPMLLVDDRALPDFKGI-----QTSDPNAVVIGLAPEhFHYQILNQAFRLLLDGAPLIAIHKARYYKRKDGLALGPG 160
Cdd:COG0647   89 PgaRVYVIGEEGLREELEEAgltlvDDEEPDAVVVGLDRT-FTYEKLAEALRAIRRGAPFIATNPDRTVPTEDGLIPGAG 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755 161 PFVTALEFATDTKATVVGKPAQTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQNVGMRGILVKTGKYRAADEEKINPAP 240
Cdd:COG0647  168 ALAAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAGLDTLLVLTGVTTAEDLEAAPIRP 247


                 ....*..
gi 744594755 241 YLTCESF 247
Cdd:COG0647  248 DYVLDSL 254
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 8-232 1.21e-37

UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase and Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase; Escherichia coli UmpH/NagD is a ribonucleoside tri-, di-, and monophosphatase with a preference for purines, it shows peak activity with UMP and functions in UMP-degradation. It is also an effective phosphatase with AMP, GMP and CMP. Mycobacterium tuberculosis phosphatase, Rv1692 is a glycerol 3-phosphate phosphatase. Rv1692 is the final enzyme involved in glycerophospholipid recycling/catabolism. This subfamily belongs to the UmpH/NagD phosphatase family, and 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: 319832 [Multi-domain]  Cd Length: 247  Bit Score: 132.33  E-value: 1.21e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755   8 KAVLVDLNGTLHIEDAAVPGAQEALKRLRATSVVVKFVTNTTKESKQDLMERLKKLEFDISEDEIFTS-LTAARNLVEQK 86
Cdd:cd07530    1 KGYLIDLDGTVYRGGTAIPGAVEFIERLREKGIPFLFLTNNSTRTPEDVAAKLAEMGIDVPEEDVYTSaLATAQYLAEQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  87 QVRPMLLVDDRALPD------FKGIQTsDPNAVVIGLAPeHFHYQILNQAFRLLLDGAPLIAIHKARYYKRKDGLALGPG 160
Cdd:cd07530   81 PGAKVYVIGEEGLRTalheagLTLTDE-NPDYVVVGLDR-DLTYEKLAEATLAIRNGAKFIATNPDLTLPTERGLLPGNG 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 744594755 161 PFVTALEFATDTKATVVGKPAQTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQNVGMRGILVKTGKYRAAD 232
Cdd:cd07530  159 SVVAALEAATGVKPLFIGKPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAAGIAAGIDTLLVLTGVTTRED 230
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 10-226 1.20e-34

Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural subclass of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The classes 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. Class I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Class II consists of sequences in which the capping domain is found between the second and third motifs. Class III sequences have no capping domain in iether of these positions. The Class IIA capping domain is predicted by PSI-PRED to consist of a mixed alpha-beta fold with the basic pattern: Helix-Helix-Helix-Sheet-Helix-Loop-Sheet-Helix-Sheet-Helix. Presently, this subfamily encompasses a single equivalog model (TIGR01452) for the eukaryotic phosphoglycolate phosphatase, as well as four hypothetical equivalogs covering closely related sequences (TIGR01456 and TIGR01458 in eukaryotes, TIGR01457 in gram positive bacteria and TIGR01459 in gram negative bacteria). The Escherishia coli NagD gene and the Bacillus subtilus AraL gene are members of this subfamily but are not members of the any of the presently defined equivalogs within it. NagD is part of the NAG operon responsible for N-acetylglucosamine metabolism. The function of this gene is unknown. Genes from several organisms have been annotated as NagD, or NagD-like. However, without data on the presence of other members of this pathway, (such as in the case of Yersinia pestis) these assignments should not be given great weight. The AraL gene is similar: it is part of the L-arabinose operon, but the function is unknown. A gene from Halobacterium has been annotated as AraL, but no other Ara operon genes have been annotated. Many of the genes in this subfamily have been annotated as "pNPPase" "4-nitrophenyl phosphatase" or "NPPase". These all refer to the same activity versus a common lab test compound used to determine phosphatase activity. There is no evidence that this activity is physiologically relevant. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273637 [Multi-domain]  Cd Length: 236  Bit Score: 124.36  E-value: 1.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755   10 VLVDLNGTLHIEDAAVPGAQEALKRLRATSVVVKFVTNTTKESKQDLMERLKKLEF-DISEDEIFTSLTAARNLVEQKQV 88
Cdd:TIGR01460   1 FLFDIDGVLWLGHKPIPGAAEALNRLRAKGKPVVFLTNNSSRSEEDYAEKLSSLLGvDVSPDQIITSGSVTKDLLRQRFE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755   89 R-PMLLV--------------DDRALPDFKGIQTSDPNAVVIGLAPEHFHYQILNQAFRLLLDG-APLIAIHKARYYKRK 152
Cdd:TIGR01460  81 GeKVYVIgvgelresleglgfRNDFFDDIDHLAIEKIPAAVIVGEPSDFSYDELAKAAYLLAEGdVPFIAANRDDLVRLG 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 744594755  153 DG-LALGPGPFVTALEFATDTKATVVGKPAQTFFLEALRGTGCEPEE-AVMIGDDCRDDVGGAQNVGMRGILVKTG 226
Cdd:TIGR01460 161 DGrFRPGAGAIAAGIKELSGREPTVVGKPSPAIYRAALNLLQARPERrDVMVGDNLRTDILGAKNAGFDTLLVLTG 236
HAD_Pase_UmpH-like cd07531
UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar ...
 8-235 5.55e-32

UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar phosphatase; Bacillus subtilis AraL is a phosphatase displaying activity towards different sugar phosphate substrates; it is encoded by the arabinose metabolic operon araABDLMNPQ-abfA and may play a role in the dephosphorylation of substrates related to l-arabinose metabolism. This subfamily belongs to the UmpH/NagD phosphatase family, and 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: 319833 [Multi-domain]  Cd Length: 252  Bit Score: 118.06  E-value: 5.55e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755   8 KAVLVDLNGTLHIEDAAVPGAQEALKRLRATSVVVKFVTNTTKESKQDLMERLKKLEFDISEDEIFTSLTA-ARNLVEQK 86
Cdd:cd07531    1 KGYIIDLDGTIGKGVTLIPGAVEGVKTLRRLGKKIIFLSNNSTRSRRILLERLRSFGIEVGEDEILVSSYVtARFLAREK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  87 QVRPMLLVDDRALPD---FKGIQTSDP---NAVVIGLAPEHFHYQILNQAFRLLLDGAPLIAIHKARYYKRKDGLALGPG 160
Cdd:cd07531   81 PNAKVFVTGEEGLIEelrLAGLEIVDKydeAEYVVVGSNRKITYELLTKAFRACLRGARYIATNPDRIFPAEDGPIPDTA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 744594755 161 PFVTALEFATDTKA-TVVGKPAQTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQNVGMRGILVKTGKYRAADEEK 235
Cdd:cd07531  161 AIIGAIEWCTGREPeVVVGKPSEVMAREALDILGLDAKDCAIVGDQIDVDIAMGKAIGMETALVLTGVTTRENLDR 236
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
 10-226 6.67e-26

haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this UmpH/NagD family include Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase , Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase, human PGP phosphoglycolate phosphatase, Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase, Bacillus AraL a putative sugar phosphatase, and Plasmodium falciparum para nitrophenyl phosphate phosphatase PNPase. 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: 319811 [Multi-domain]  Cd Length: 270  Bit Score: 102.44  E-value: 6.67e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  10 VLVDLNGTLHIEDAAVPGAQEALKRLRATSVVVKFVTNTTKESKQDLMERLKKLEFDISEDEIFTS-LTAARNLVEQK-- 86
Cdd:cd07508    2 VISDCDGVLWHDERAIPGAAEFLEALKEAGKKIVFVSNNSSRSRQDYAEKFRKFGVDVPEDQIVTSaKATARFLRSRKfg 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  87 --------------------QVRPMLLVDDRALPDFKGIQTSDPN--AVVIGLApEHFHYQILNQAFRLLLD-GAPLIAI 143
Cdd:cd07508   82 kkvyvlgeeglkeelraagfRIAGGPSKGIETYAELVEHLEDDENvdAVIVGSD-FKLNFAKLRKACRYLRNpGCLFIAT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755 144 HKARYYK-RKDGLALGPGPFVTALEFATDTKATVVGKPAQTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQNVGMRGIL 222
Cdd:cd07508  161 APDRIHPlKDGGPIPGTGAFAAAVEAATGRQPLVLGKPSPWLGELALEKFGIDPERVLFVGDRLATDVLFGKACGFQTLL 240


                 ....
gi 744594755 223 VKTG 226
Cdd:cd07508  241 VLTG 244
Hydrolase_like pfam13242
HAD-hyrolase-like;
176-250 2.60e-23

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 89.98  E-value: 2.60e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 744594755  176 VVGKPAQTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQNVGMRGILVKTGKYRAADEEKINPAPYLTCESFPHA 250
Cdd:pfam13242   1 VCGKPNPGMLERALARLGLDPERTVMIGDRLDTDILGAREAGARTILVLTGVTRPADLEKAPIRPDYVVDDLAEA 75
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
 10-226 5.36e-23

UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase; This subfamily includes the phosphoglycolate phosphatases (human PGP and Arabidopsis thaliana PGLP2) and p-nitrophenylphosphatases (Schizosaccharomyces pombe PHO2 and Saccharomyces PHO13p). It belongs to the UmpH/NagD phosphatase family, and 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: 319813 [Multi-domain]  Cd Length: 282  Bit Score: 94.76  E-value: 5.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  10 VLVDLNGTLHIEDAAVPGAQEALKRLRATSVVVKFVTNTTKESKQDLMERLKKLEFD-ISEDEIFTS-LTAARNLveqKQ 87
Cdd:cd07510    4 FLFDCDGVLWNGEKAIPGAPETLNLLRSLGKRLVFVTNNSTKSREAYAKKFARLGFTgLKEEEIFSSaYCAARYL---RQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  88 VRPmLLVDDRA-------------LPDFKGIQTSDPN-------------------AVVIGLAPeHFHYQILNQAFRLLL 135
Cdd:cd07510   81 RLP-GPADGKVyvlggeglraeleAAGVAHLGGPDDGlrraapkdwllagldpdvgAVLVGLDE-HVNYLKLAKATQYLR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755 136 D-GAPLIAIHKARYYKRKDGLAL-GPGPFVTALEFATDTKATVVGKPAQTFFLEALRGTGCEPEEAVMIGDDCRDDVGGA 213
Cdd:cd07510  159 DpGCLFVATNRDPWHPLSDGSFIpGTGSLVAALETASGRQAIVVGKPSRFMFDCISSKFSIDPARTCMVGDRLDTDILFG 238

                        250
                 ....*....|...
gi 744594755 214 QNVGMRGILVKTG 226
Cdd:cd07510  239 QNCGLKTLLVLTG 251
HAD_Pase_UmpH-like cd16422
uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid ...
 11-246 6.80e-23

uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid dehalogenase-like superfamily; This uncharacterized subfamily belongs to the UmpH/NagD phosphatase family and 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: 319858 [Multi-domain]  Cd Length: 247  Bit Score: 93.66  E-value: 6.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  11 LVDLNGTLHIEDAAVPGAQEALKRLRATSVVVKFVTNTTKESKQDLMERLKKLEFDISEDEIFTSLTAARNLVEQKQVRP 90
Cdd:cd16422    3 IFDMDGTIYLGDDLIPGTLEFLERLHEKKRRYIFLTNNSSKNLADYVEKLNRLGIDAGLDRVFTSGEATIDHLKKEFIKP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  91 MLLVddRALPDFKG--------IQTSDPNAVVIGLAPEhFHYQILNQAFRLLLDGAPLIAIHKARYYKRKDGLALGPGPF 162
Cdd:cd16422   83 KIFL--LGTKSLREefekagftLDGDDIDVVVLGFDTE-LTYEKLRTACLLLRRGIPYIATHPDINCPSEEGPIPDAGSI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755 163 VTALEFATDTKA-TVVGKPAQTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQNVGMRGILVKTGKYRAADEEKINPAPY 241
Cdd:cd16422  160 IALIETSTGRRPdLVIGKPNPIILDPVLEKFDYSKEETVMVGDRLYTDIVLGINAGVDSILVLSGETTREDLEDLERKPT 239


                 ....*
gi 744594755 242 LTCES 246
Cdd:cd16422  240 YVFDN 244
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
 10-236 1.58e-22

UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium falciparum PNPase; Plasmodium falciparum para nitrophenyl phosphate phosphatase (PNPase) catalyzes the dephosphorylation of thiamine monophosphate to thiamine, other substrates on which its active are nucleotides, phosphorylated sugars, pyridoxal-5-phosphate, and paranitrophenyl phosphate. This subfamily belongs to the UmpH/NagD phosphatase family, and 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: 319834 [Multi-domain]  Cd Length: 286  Bit Score: 93.52  E-value: 1.58e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  10 VLVDLNGTLHIEDAAVPGAQEALKRLRATSVVVKFVTNTTKESKQDLMERLKKLEFDISEDEIFTSLTA-ARNLVEQKQV 88
Cdd:cd07532    9 VIFDADGVLWTGDKPIPGAVEVFNALLDKGKKVFIVTNNSTKTREELAKKAKKLGFNVKENNILSSAAViADYLKEKGFK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  89 RPMLLVDDRALP---DFKGIQT-----------------------SDPNAVVIGLaPEHFHYQILNQAFRLLLDgaPLI- 141
Cdd:cd07532   89 KKVYVIGEEGIRkelEEAGIVScggdgedekddsmgdfahnleldPDVGAVVVGR-DEHFSYPKLMKACNYLRN--PDVl 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755 142 -------AIHKARYYKRkdglALGPGPFVTALEFATDTKATVVGKPAQTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQ 214
Cdd:cd07532  166 flatnmdATFPGPVGRV----IPGAGAMVAAIEAVSGRKPLVLGKPNPQILNFLMKSGVIKPERTLMIGDRLKTDILFAN 241

                        250       260
                 ....*....|....*....|..
gi 744594755 215 NVGMRGILVKTGKYRAADEEKI 236
Cdd:cd07532  242 NCGFQSLLVGTGVNSLEDAEKI 263
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 10-86 3.89e-21

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 84.82  E-value: 3.89e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 744594755   10 VLVDLNGTLHIEDAAVPGAQEALKRLRATSVVVKFVTNTTKESKQDLMERLKKLEFDISEDEIFTSLTAARNLVEQK 86
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGFDIDEDEIITSGTAAADYLKER 77
PGP_euk TIGR01452
phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the ...
 10-242 4.65e-21

phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the glycolate salvage pathway in higher organisms (photorespiration in plants). Phosphoglycolate results from the oxidase activity of RubisCO in the Calvin cycle when concentrations of carbon dioxide are low relative to oxygen. In mammals, PGP is found in many tissues, notably in red blood cells where P-glycolate is and important activator of the hydrolysis of 2,3-bisphosphoglycerate, a major modifier of the oxygen affinity of hemoglobin. Pyridoxal phosphate (PLP, Vitamin B6) phosphatase is involved in the degradation of PLP in mammals and is widely distributed in human tissues including erythrocyes. The enzymes described here are members of the Haloacid dehalogenase superfamily of hydrolase enzymes (pfam00702). Unlike the bacterial PGP equivalog (TIGR01449), which is a member of class (subfamily) I, these enzymes are members of class (subfamily) II. These two families have almost certainly arisen from convergent evolution (although these two ancestors may themselves have diverged from a more distant HAD superfamily progenitor). The primary seed sequence for this model comes from Chlamydomonas reinhardtii, a photosynthetic alga. The enzyme has been purified and characterized and these data are fully consistent with the assignment of function as a PGPase involved in photorespiration. The second seed, from Homo sapiens chromosome 22 has been characterized as a pyridoxal phosphatase. Biochemical characterization of partially purified PGP's from various tissues including red blood cells have been performed while one gene for PGP has been localized to chromosome 16p13.3. The sequence used here maps to chromosome 22. There is indeed a related gene on chromosome 16 (and it is expressed, since EST's are found) which shows 46% identity. The chromosome 16 gene is not in evidence in nraa but translated from the genomic sequence. The third seed, from C. elegans, is only supported by sequence similarity. This model is limited to eukaryotic species including S. pombe and S. cerevisiae, although several archaea score between the trusted and noise cutoffs. This model is closely related to a family of bacterial sequences including the E. coli NagD and B. subtilus AraL genes which are characterized by the ability to hydrolyze para-nitrophenylphosphate (pNPPases or NPPases). The chlamydomonas PGPase d


Pssm-ID: 273635 [Multi-domain]  Cd Length: 279  Bit Score: 89.54  E-value: 4.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755   10 VLVDLNGTLHIEDAAVPGAQEALKRLRATSVVVKFVTNTTKESKQDLMERLKKLEFDISEDEIFTSLTAARNLVEQ---- 85
Cdd:TIGR01452   5 FIFDCDGVLWLGERVVPGAPELLDRLARAGKQILFVTNNSTKSRAEYALKFARLGFNGLAEQLFSSALCAARLLRQppda 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755   86 -KQVRPMLLVDDRALPDFKGIQ--------------------TSDPN--AVVIGLaPEHFHYQILNQAFRLLLD-GAPLI 141
Cdd:TIGR01452  85 gKAVYVIGEEGLRAELDAAGIRlagdpgekkqdeadgfmydiKLDERvgAVVVGY-DEHFSYVKLMEACAHLREpGCLFV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  142 AIHKARYYKRKDGLAL-GPGPFVTALEFATDTKATVVGKPAQTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQNVGMRG 220
Cdd:TIGR01452 164 ATNRDPWHPLSDGSRTpGTGSLVAAIETASGRQPLVVGKPSPYMFNCITEKFSIDPARTLMVGDRLETDILFGHRCGMTT 243

                         250       260       270
                  ....*....|....*....|....*....|...
gi 744594755  221 ILVKTG--------KYRAADEEKINP---APYL 242
Cdd:TIGR01452 244 VLVLSGvsqleeaqEYLMAGQDDLVPdyvVESL 276
PRK10444 PRK10444
HAD-IIA family hydrolase;
7-252 3.68e-16

HAD-IIA family hydrolase;


Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 75.60  E-value: 3.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755   7 LKAVLVDLNGTLHIEDAAVPGAQEALKRLRATSVVVKFVTNTTKESKQDLMERLKKLEFDISEDEIFTSLTAARNLVEQK 86
Cdd:PRK10444   1 IKNVICDIDGVLMHDNVAVPGAAEFLHRILDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFLRRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  87 QVRPMLLVDDRALPD--FKG---IQTSDPNAVVIGlAPEHFHYQILNQAFRLLLDGAPLIAIHKARYykrkdGLALGP-- 159
Cdd:PRK10444  81 EGKKAYVIGEGALIHelYKAgftITDINPDFVIVG-ETRSYNWDMMHKAAYFVANGARFIATNPDTH-----GRGFYPac 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755 160 GPFVTALEFATDTKATVVGKPAQTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQNVGMRGILVKTGKYRAADeekINPA 239
Cdd:PRK10444 155 GALCAGIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILVLSGVSTLDD---IDSM 231

                        250
                 ....*....|...
gi 744594755 240 PYLTCESFPHAVD 252
Cdd:PRK10444 232 PFRPSWIYPSVAD 244
HAD_like cd07525
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 8-234 2.27e-13

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The haloacid dehalogenase-like (HAD) hydrolases are 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 include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members 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: 319827 [Multi-domain]  Cd Length: 253  Bit Score: 67.74  E-value: 2.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755   8 KAVLVDLNGTLHIEDAAVPGAQEALKRLRATSVVVKFVTNTTKeSKQDLMERLKKLEF-DISEDEIFTSLTAARNLVEQK 86
Cdd:cd07525    1 DAFLLDLWGVLHDGNEPYPGAVEALAALRAAGKTVVLVTNAPR-PAESVVRQLAKLGVpPSTYDAIITSGEVTRELLARE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  87 QVRP---MLLVDDRALPDFKGIQ---TSDPNA----VVIGLAPEHF----HYQ-ILNQAFRlllDGAPLIAIHKARYYKR 151
Cdd:cd07525   80 AGLGrkvYHLGPERDANVLEGLDvvaTDDAEKaefiLCTGLYDDETetpeDYRkLLKAAAA---RGLPLICANPDLVVPR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755 152 KDGLALGPGPFVTALEfATDTKATVVGKP-AQTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQNVGMRGILVKTGKYRA 230
Cdd:cd07525  157 GGKLIYCAGALAELYE-ELGGEVIYFGKPhPPIYDLALARLGRPAKARILAVGDGLHTDILGANAAGLDSLFVTGGIHRR 235


                 ....
gi 744594755 231 ADEE 234
Cdd:cd07525  236 LAAE 239
PLN02645 PLN02645
phosphoglycolate phosphatase
 1-226 7.69e-12

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 63.96  E-value: 7.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755   1 MAARRALKAV---LVDLNGTLHIEDAAVPGAQEALKRLRATSVVVKFVTNTTKESKQDLMERLKKLEFDISEDEIFTSLT 77
Cdd:PLN02645  19 ENADELIDSVetfIFDCDGVIWKGDKLIEGVPETLDMLRSMGKKLVFVTNNSTKSRAQYGKKFESLGLNVTEEEIFSSSF 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  78 AAR------NLVEQKQVRPM---LLVDDRALPDFKGI-------------------QTSDPNAVVIGLAPEHFHYQIlnQ 129
Cdd:PLN02645  99 AAAaylksiNFPKDKKVYVIgeeGILEELELAGFQYLggpedgdkkielkpgflmeHDKDVGAVVVGFDRYINYYKI--Q 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755 130 AFRLLL---DGAPLIAIHK-ARYYKRKDGLALGPGPFVTALEFATDTKATVVGKPAqTFFLEALRGT-GCEPEEAVMIGD 204
Cdd:PLN02645 177 YATLCIrenPGCLFIATNRdAVTHLTDAQEWAGAGSMVGAIKGSTEREPLVVGKPS-TFMMDYLANKfGIEKSQICMVGD 255

                        250       260
                 ....*....|....*....|..
gi 744594755 205 DCRDDVGGAQNVGMRGILVKTG 226
Cdd:PLN02645 256 RLDTDILFGQNGGCKTLLVLSG 277
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 179-257 1.85e-11

Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino acid transport and metabolism]; Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 440011 [Multi-domain]  Cd Length: 176  Bit Score: 60.88  E-value: 1.85e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 744594755 179 KPAQTFFLEALRGTGCEPEEAVMIGDDCRdDVGGAQNVGMRGILVKTGKyraADEEKINPAPYLTCESFPHAVDHILQH 257
Cdd:COG0241  102 KPKPGMLLQAAERLGIDLSNSYMIGDRLS-DLQAAKAAGCKGILVLTGK---GAEELAEALPDTVADDLAEAVDYLLAE 176
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 177-224 6.91e-11

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: 60.43  E-value: 6.91e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 744594755 177 VGKPAQTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQNVGMRGILVK 224
Cdd:COG1011  147 VRKPDPEIFELALERLGVPPEEALFVGDSPETDVAGARAAGMRTVWVN 194
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 179-223 1.76e-09

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to uncharacterized Drosophila melanogaster rhythmically expressed gene 2 protein and human haloacid dehalogenase-like hydrolase domain-containing protein 3; The haloacid dehalogenase-like (HAD) hydrolases are 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 include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members 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: 319852 [Multi-domain]  Cd Length: 128  Bit Score: 54.60  E-value: 1.76e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 744594755 179 KPAQTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQNVGMRGILV 223
Cdd:cd16415   62 KPDPRIFQKALERLGVSPEEALHVGDDLKNDYLGARAVGWHALLV 106
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 177-221 1.98e-08

human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases; N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. 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: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 51.00  E-value: 1.98e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 744594755 177 VGKPAQTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQNVGMRGI 221
Cdd:cd04305   62 VQKPNPEIFDYALNQLGVKPEETLMVGDSLESDILGAKNAGIKTV 106
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
178-256 6.74e-08

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 51.47  E-value: 6.74e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 744594755 178 GKPAQTFFLEALRGTGCEPEEAVMIGDDcRDDVGGAQNVGMRGILVKTGkYRAADEEKINPAPYLtCESFPHAVDHILQ 256
Cdd:COG0546  139 AKPKPEPLLEALERLGLDPEEVLMVGDS-PHDIEAARAAGVPFIGVTWG-YGSAEELEAAGADYV-IDSLAELLALLAE 214
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 9-223 4.62e-06

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: 45.87  E-value: 4.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755    9 AVLVDLNGTLHieDAAVPGAQEALKRLRATSVVVKFVTnttKESKQDLMERLKKLEF-DISEDEIFtsltaaRNLVEQKQ 87
Cdd:TIGR01509   1 AILFDLDGVLV--DTEFAIAKLINREELGLVPDELGVS---AVGRLELALRRFKAQYgRTISPEDA------QLLYKQLF 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755   88 VRPMLLVDDralpdfkgiqtSDPNAVVIGLApehfhYQILNQAFRL-LLDGAPLIAIHKARYYkrkdglalgpgPFVTAL 166
Cdd:TIGR01509  70 YEQIEEEAK-----------LKPLPGVRALL-----EALRARGKKLaLLTNSPRAHKLVLALL-----------GLRDLF 122

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 744594755  167 EFATDTKATVVGKPAQTFFLEALRGTGCEPEEAVMIgDDCRDDVGGAQNVGMRGILV 223
Cdd:TIGR01509 123 DVVIDSSDVGLGKPDPDIYLQALKALGLEPSECVFV-DDSPAGIEAAKAAGMHTVGV 178
COG2503 COG2503
Predicted secreted acid phosphatase [General function prediction only];
23-112 1.01e-05

Predicted secreted acid phosphatase [General function prediction only];


Pssm-ID: 441997 [Multi-domain]  Cd Length: 269  Bit Score: 45.72  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  23 AAVPGAQEALKRLRATSVVVKFVTNTTKESKQDLMERLKKLEF-DISEDEIF-----TSLTAARNLVEQKQvRPMLLVDD 96
Cdd:COG2503  123 TAVPGAVEFLNYANSKGVTVFYISNRKAEEKAATLANLKALGFpVVDEDHLLlktdgSDKEARRQAVAKRY-RIVMLVGD 201

                         90
                 ....*....|....*.
gi 744594755  97 RaLPDFKGIQTSDPNA 112
Cdd:COG2503  202 N-LGDFADAFDKKSNA 216
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 175-223 1.17e-05

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: 43.15  E-value: 1.17e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 744594755 175 TVVGKPAQTFFLEALRGTGCEPEEAVMIGDDcRDDVGGAQNVGMRGILV 223
Cdd:cd01427   59 GGTPKPKPKPLLLLLLKLGVDPEEVLFVGDS-ENDIEAARAAGGRTVAV 106
CECR5 TIGR01456
HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member ...
 9-255 2.34e-05

HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all eukaryotes. One sequence (GP|13344995) is called "Cat Eye Syndrome critical region protein 5" (CECR5). This gene has been cloned from a pericentromere region of human chromosome 22 believed to be the location of the gene or genes responsible for Cat Eye Syndrome. This is one of a number of candidate genes. The Schizosaccharomyces pombe sequence (EGAD|138276) is annotated as "phosphatidyl synthase," however this is due entirely to a C-terminal region of the protein (outside the region of similarity of this model) which is highly homologous to a family of CDP-alcohol phosphatidyltransferases. (Thus, the annotation of GP|4226073 from C. elegans as similar to phosphatidyl synthase, is a mistake as this gene does not contain the C-terminal portion). The physical connection of the phosphatidyl synthase and the HAD-superfamily hydrolase domain in S. pombe may, however, be an important clue to the substrate for the hydrolases in this equivalog.


Pssm-ID: 200106 [Multi-domain]  Cd Length: 321  Bit Score: 44.87  E-value: 2.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755    9 AVLVDLNGTLHIEDAAVPGAQEALKRLRATSVVVK----FVTNTTKESKQDLMERLK-KLEFDISEDEIFTSLTAARNLV 83
Cdd:TIGR01456   2 GFAFDIDGVLFRGKKPIAGASDALRRLNRNQGQLKipyiFLTNGGGFSERARAEEISsLLGVDVSPLQVIQSHSPYKSLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755   84 EQKQVR--------PM-----------LLVDD-----------------------RALPD--FKGIQT----SDP----- 110
Cdd:TIGR01456  82 NKYEKRilavgtgsVRgvaegygfqnvVHQDEivryfrdidpfsgmsdeqvmeysRDIPDltTKRFDAvlvfNDPvdwaa 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  111 ------------NAVVIGLAPEHFHYQILNQ----------------AFRLLLD-------GAPLiaihkaRYYkrkdgl 155
Cdd:TIGR01456 162 diqiisdalnseGLPGEKSGKPSIPIYFSNQdllwaneyklnrfgqgAFRLLLEriylelnGKPL------QYY------ 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  156 ALG-PGPFVtaLEFATDTKATVVGKPAQTfflealRGTGCEPEEAVMIGDDCRDDVGGAQNVGMRGILVKTGKYRAADEE 234
Cdd:TIGR01456 230 TLGkPTKLT--YDFAEDVLIDWEKRLSGT------KPSTSPFHALYMVGDNPASDIIGAQNYGWFSCLVKTGVYNGGDDL 301

                         330       340
                  ....*....|....*....|.
gi 744594755  235 KINPaPYLTCESFPHAVDHIL 255
Cdd:TIGR01456 302 KECK-PTLIVNDVFDAVTKIL 321
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 178-223 2.35e-05

Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the uncharacterized protein Bacillus subtilis YqeG; The haloacid dehalogenase-like (HAD) hydrolases are 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 include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members 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: 319853 [Multi-domain]  Cd Length: 108  Bit Score: 42.26  E-value: 2.35e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 744594755 178 GKPAQTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQNVGMRGILV 223
Cdd:cd16416   63 GKPRPRAFRRALKEMDLPPEQVAMVGDQLFTDILGGNRAGLYTILV 108
YqeG COG2179
Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];
178-224 2.92e-05

Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];


Pssm-ID: 441782  Cd Length: 164  Bit Score: 43.20  E-value: 2.92e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 744594755 178 GKPAQTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQNVGMRGILVK 224
Cdd:COG2179   90 KKPLPRGFRKALKLMGLPPEETAVVGDQLFTDVLGGNRAGLYTILVK 136
YqeG_hyp_ppase TIGR01668
HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins ...
 177-226 3.40e-05

HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins is a member of the IIIA subfamily of the haloacid dehalogenase (HAD) superfamily of hydrolases. All characterized members of this subfamily (TIGR01662) 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. This family consists of sequences from fungi, plants, cyanobacteria, gram-positive bacteria and Deinococcus. There is presently no characterization of any sequence in this family.


Pssm-ID: 273744  Cd Length: 170  Bit Score: 43.16  E-value: 3.40e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 744594755  177 VGKPAQTFFlEALRGTGCEPEEAVMIGDDCRDDVGGAQNVGMRGILVKTG 226
Cdd:TIGR01668  90 VKPPGCAFR-RAHPEMGLTSEQVAVVGDRLFTDVMGGNRNGSYTILVEPL 138
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 177-224 1.41e-04

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 41.56  E-value: 1.41e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 744594755 177 VGKPAQTFFLEALRGTGCEPEEAVMIgDDCRDDVGGAQNVGMRGILVK 224
Cdd:cd02603  139 VRKPDPEIYQLALERLGVKPEEVLFI-DDREENVEAARALGIHAILVT 185
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
179-223 1.97e-04

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 41.03  E-value: 1.97e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 744594755  179 KPAQTFFLEALRGTGCEPEEAVMIGDDCRdDVGGAQNVGMRGILV 223
Cdd:pfam13419 135 KPDPDPILKALEQLGLKPEEVIYVGDSPR-DIEAAKNAGIKVIAV 178
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 7-217 4.06e-04

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: 40.26  E-value: 4.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755    7 LKAVLVDLNGTLHIedaAVPGAQEALKRLRATSVVVKfvtnttkeskqDLMERLKKLEFDISEdeiftsLTAARNLVEQK 86
Cdd:pfam00702   1 IKAVVFDLDGTLTD---GEPVVTEAIAELASEHPLAK-----------AIVAAAEDLPIPVED------FTARLLLGKRD 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755   87 QVR--PMLLVDDRALPDFKGIQTSDPNAVVIGLAPEHFHYQILNQAFRLLLD-GAPLIAI-HKARYYKRKDGLALGPGPF 162
Cdd:pfam00702  61 WLEelDILRGLVETLEAEGLTVVLVELLGVIALADELKLYPGAAEALKALKErGIKVAILtGDNPEAAEALLRLLGLDDY 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 744594755  163 VTALEFATDTKatvVGKPAQTFFLEALRGTGCEPEEAVMIGDDcRDDVGGAQNVG 217
Cdd:pfam00702 141 FDVVISGDDVG---VGKPKPEIYLAALERLGVKPEEVLMVGDG-VNDIPAAKAAG 191
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 158-226 4.92e-04

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to Parvibaculum lavamentivorans HAD-superfamily hydrolase, subfamily IA, variant 1; 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: 319835 [Multi-domain]  Cd Length: 207  Bit Score: 40.07  E-value: 4.92e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 744594755 158 GPGPFVTALEFATDTKatvvGKPAQTFFLEALRGTGCEPEEAVMIGDDCRdDVGGAQNVGMRGILVKTG 226
Cdd:cd07533  122 GLGGYFDATRTADDTP----SKPHPEMLREILAELGVDPSRAVMVGDTAY-DMQMAANAGAHAVGVAWG 185
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
179-257 5.12e-04

D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;


Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 39.80  E-value: 5.12e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 744594755 179 KPAQTFFLEALRGTGCEPEEAVMIGDDcRDDVGGAQNVGMRGILVKTGKYRAADEEKiNPAPYLTCESFPHAVDHILQH 257
Cdd:PRK08942 103 KPKPGMLLSIAERLNIDLAGSPMVGDS-LRDLQAAAAAGVTPVLVRTGKGVTTLAEG-AAPGTWVLDSLADLPQALKKQ 179
HAD_CAP cd07534
molecular class C acid phosphatases, similar to Haemophilus influenzae e (P4) acid phosphatase; ...
 23-127 7.05e-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: 7.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755  23 AAVPGAQEALKRLRATSVVVKFVTNTTKESKQDLMERLKKLEFDISEDEIF-----TSLTAARNLVEQKQVRPMLLVDDR 97
Cdd:cd07534   74 KPIPGAVDFLNYANAKGVTIFYVSNRDQKLKAATLKNLKRLGFPQASDDHLllktdKSSKESRRQLVKEKYNIVLLFGDN 153

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 744594755  98 aLPDFKGIQTSDPNA---VVIGLAPEHF--HYQIL 127
Cdd:cd07534  154 -LGDFGDFTYKKENEdrrALVEKNAEEFgeKFIIL 187
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 9-75 2.33e-03

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: 36.60  E-value: 2.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 744594755   9 AVLVDLNGTLHiedaavpgAQEALKRLRATSVVVKFVTNTTKESkqdLMERLKKLEFDISEDEIFTS 75
Cdd:cd01427    1 AVLFDLDGTLL--------AVELLKRLRAAGIKLAIVTNRSREA---LRALLEKLGLGDLFDGIIGS 56
HAD_like cd07511
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 9-90 2.48e-03

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to the uncharacterized human CECR5 (cat eye syndrome critical region protein 5); 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: 319814  Cd Length: 136  Bit Score: 37.37  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755   9 AVLVDLNGTLHIEDAAVPGAQEALKRLRATSVVVKFVTNTTKESKQDLMERL-KKLEFDISEDEI-----------FTSL 76
Cdd:cd07511    2 GFAFDIDGVLVRGKKPIPGAPKALKFLNDNKIPFIFLTNGGGFPESKRADFLsKLLGVEVSPDQViqshspgkpteLTYD 81

                         90
                 ....*....|....
gi 744594755  77 TAARNLVEQKQVRP 90
Cdd:cd07511   82 FAEHVLQRQAKRLG 95
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 179-236 3.23e-03

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 37.70  E-value: 3.23e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 744594755 179 KPAQTFFLEALRGTGCEPEEAVMIGDDCRDDVGGaQNVGmrgilVKTG--KYRAADEEKI 236
Cdd:PRK13288 138 KPDPEPVLKALELLGAKPEEALMVGDNHHDILAG-KNAG-----TKTAgvAWTIKGREYL 191
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 187-258 4.22e-03

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; 5'-nucleotidases dephosphorylate nucleoside 5'-monophosphates to nucleosides and inorganic phosphate. Purified Pseudomonas aeruginosa PA0065 displayed high activity toward 5'-UMP and 5'-IMP, significant activity against 5'-XMP and 5'-TMP, and low activity against 5'-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: 319798 [Multi-domain]  Cd Length: 209  Bit Score: 37.57  E-value: 4.22e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 744594755 187 EALRGTGCEPEEAVMIGDDcRDDVGGAQNVGMRGILVKTGkYRAADEEKINPAPYLTcesfpHAVDHILQHL 258
Cdd:cd04302  145 YALDTLGIAPEQAVMIGDR-KHDIIGARANGIDSIGVLYG-YGSEDELEEAGATYIV-----ETPAELLELL 209
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 179-223 8.17e-03

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: 35.84  E-value: 8.17e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 744594755  179 KPAQTFFLEAL-RGTGCEPEEAVMIGDDCRDDVGGAQNVGMRGILV 223
Cdd:TIGR01662  88 KPKPGMFLEALkRFNEIDPEESVYVGDQDLTDLQAAKRVGLATILV 133
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 179-223 8.43e-03

2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Belongs to the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases (pfam00702), class (subfamily) I. Note that the Type I HAD enzymes have not yet been fully characterized, but clearly utilize a substantially different catalytic mechanism and are thus unlikely to be related.


Pssm-ID: 130495 [Multi-domain]  Cd Length: 198  Bit Score: 36.55  E-value: 8.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 744594755  179 KPAQTFFLEALRGTGCEPEEAVMIGDDcRDDVGGAQNVGMRGILV 223
Cdd:TIGR01428 148 KPAPQVYQLALEALGVPPDEVLFVASN-PWDLGGAKKFGFKTAWI 191
 
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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