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Conserved domains on  [gi|917292859|ref|WP_051899571|]
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6-phosphogluconate phosphatase [Ewingella americana]

Protein Classification

6-phosphogluconate phosphatase( domain architecture ID 10793419)

6-phosphogluconate phosphatase catalyzes strongly the dephosphorylation of 6-phosphogluconate (6P-Glu) and slightly the dephosphorylation of dihydroxyacetone phosphate (DHAP) and phosphoenolpyruvate (PEP); also hydrolyzes both purines (GMP and IMP) and pyrimidines as secondary substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 13-232 1.05e-139

6-phosphogluconate phosphatase; Provisional


:

Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 390.21  E-value: 1.05e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  13 SPIDCVLFDCDGTLVDSELLCCEAYVEMFAHFGVTVSFDEMYKTYKGVKLYEIIAIINKQHGLDVPKEEMEVVFRQHVAR 92
Cdd:PRK10563   2 SQIEAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLSLEEVFKRFKGVKLYEIIDIISKEHGVTLAKAELEPVYRAEVAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  93 LFDSKLTAIDGVHQLLEQIQVPMCVVSNGPVSKMQLSLGKTGLLPFMGDNLFSGYDLQRWKPDPAVLYKAAEVMQVDIKR 172
Cdd:PRK10563  82 LFDSELEPIAGANALLESITVPMCVVSNGPVSKMQHSLGKTGMLHYFPDKLFSGYDIQRWKPDPALMFHAAEAMNVNVEN 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859 173 CILVEDSVAGAQAGIAAGIPVFYYCADPHNPPLDNPLVTTFYDMRELPALWHAKGYAITA 232
Cdd:PRK10563 162 CILVDDSSAGAQSGIAAGMEVFYFCADPHNKPIDHPLVTTFTDLAQLPELWKARGWDITR 221
 
Name Accession Description Interval E-value
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 13-232 1.05e-139

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 390.21  E-value: 1.05e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  13 SPIDCVLFDCDGTLVDSELLCCEAYVEMFAHFGVTVSFDEMYKTYKGVKLYEIIAIINKQHGLDVPKEEMEVVFRQHVAR 92
Cdd:PRK10563   2 SQIEAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLSLEEVFKRFKGVKLYEIIDIISKEHGVTLAKAELEPVYRAEVAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  93 LFDSKLTAIDGVHQLLEQIQVPMCVVSNGPVSKMQLSLGKTGLLPFMGDNLFSGYDLQRWKPDPAVLYKAAEVMQVDIKR 172
Cdd:PRK10563  82 LFDSELEPIAGANALLESITVPMCVVSNGPVSKMQHSLGKTGMLHYFPDKLFSGYDIQRWKPDPALMFHAAEAMNVNVEN 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859 173 CILVEDSVAGAQAGIAAGIPVFYYCADPHNPPLDNPLVTTFYDMRELPALWHAKGYAITA 232
Cdd:PRK10563 162 CILVDDSSAGAQSGIAAGMEVFYFCADPHNKPIDHPLVTTFTDLAQLPELWKARGWDITR 221
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
14-181 2.01e-53

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 170.78  E-value: 2.01e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  14 PIDCVLFDCDGTLVDSELLCCEAYVEMFAHFGVTVSfDEMYKTYKGVKLYEIIAIINKQHGLDVPKEEMEVVFRQHVARL 93
Cdd:COG0637    1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLT-EEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYREL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  94 FDS-KLTAIDGVHQLLEQIQ---VPMCVVSNGPVSKMQLSLGKTGLLPFMgDNLFSGYDLQRWKPDPAVLYKAAEVMQVD 169
Cdd:COG0637   80 LAEeGLPLIPGVVELLEALKeagIKIAVATSSPRENAEAVLEAAGLLDYF-DVIVTGDDVARGKPDPDIYLLAAERLGVD 158

                        170
                 ....*....|..
gi 917292859 170 IKRCILVEDSVA 181
Cdd:COG0637  159 PEECVVFEDSPA 170
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 16-180 6.89e-50

subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli 6-phosphogluconate phosphatase YieH; This subfamily includes Escherichia coli YieH/HAD3 an 6-phosphogluconate phosphatase, which can hydrolyzed purines and pyrimidines as secondary substrates. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate, and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate. 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: 319828 [Multi-domain]  Cd Length: 141  Bit Score: 159.79  E-value: 6.89e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  16 DCVLFDCDGTLVDSELLCCEAYVEMFAHFGVTVsfdemyktykgvklyeiiaiinkqhgldvpkeemevvfrqhvARLFD 95
Cdd:cd07526    1 DLVIFDCDGVLVDSEVIAARVLVEVLAELGARV------------------------------------------LAAFE 38

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  96 SKLTAIDGVHQLLEQIQVPMCVVSNGPVSKMQLSLGKTGLLPFMGDNLFSGYDLQRWKPDPAVLYKAAEVMQVDIKRCIL 175
Cdd:cd07526   39 AELQPIPGAAAALSALTLPFCVASNSSRERLTHSLGLAGLLAYFEGRIFSASDVGRGKPAPDLFLHAAAQMGVAPERCLV 118


                 ....*
gi 917292859 176 VEDSV 180
Cdd:cd07526  119 IEDSP 123
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 18-179 1.29e-20

beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: the characterized beta-phosphoglucomutases (including those from E.coli, B.subtilus and L.lactis, TIGR01990), a clade of putative bPGM's from mycobacteria and a clade including the uncharacterized E.coli and H.influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the "variant 3" glu-asp version of the third conserved HAD domain (TIGR01509).


Pssm-ID: 213673 [Multi-domain]  Cd Length: 185  Bit Score: 85.47  E-value: 1.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859   18 VLFDCDGTLVDSELLCCEAYVEMFAHFGVtvSFDEMYKTY-KGVKLYEIIAIINKQHGLDVPKEEMEVVF---RQHVARL 93
Cdd:TIGR02009   4 VIFDMDGVITDTAPLHAQAWKHIAAKYGI--SFDKQYNESlKGLSREDILRAILKLRGDGLSLEEIHQLAerkNELYREL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859   94 FDSKLTAI-DGVHQLLEQIQ---VPMCVVSNGPVSKMqlSLGKTGLLPFMgDNLFSGYDLQRWKPDPAVLYKAAEVMQVD 169
Cdd:TIGR02009  82 LRLTGVAVlPGIRNLLKRLKakgIAVGLGSSSKNAPR--ILAKLGLRDYF-DAIVDASEVKNGKPHPETFLLAAELLGVP 158

                         170
                  ....*....|
gi 917292859  170 IKRCILVEDS 179
Cdd:TIGR02009 159 PNECIVFEDA 168
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
18-179 2.70e-18

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 79.17  E-value: 2.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859   18 VLFDCDGTLVDSELLCCEAYVEMFAHFGVTVSFDEMYKTYKGVKLYEIIAIINKQHGLDvpkEEMEVVFRQHVARLFDSK 97
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYGELSEEEILKFIGLPLREIFRYLGVSEDEE---EKIEFYLRKYNEELHDKL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859   98 LTAIDGVHQLLEQIQ---VPMCVVSNGPVSKMQLSLGKTGLLPFMgDNLFSGYDLQRWKPDPAVLYKAAEVMQVDIKRCI 174
Cdd:pfam13419  78 VKPYPGIKELLEELKeqgYKLGIVTSKSRENVEEFLKQLGLEDYF-DVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVI 156


                  ....*
gi 917292859  175 LVEDS 179
Cdd:pfam13419 157 YVGDS 161
 
Name Accession Description Interval E-value
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 13-232 1.05e-139

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 390.21  E-value: 1.05e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  13 SPIDCVLFDCDGTLVDSELLCCEAYVEMFAHFGVTVSFDEMYKTYKGVKLYEIIAIINKQHGLDVPKEEMEVVFRQHVAR 92
Cdd:PRK10563   2 SQIEAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLSLEEVFKRFKGVKLYEIIDIISKEHGVTLAKAELEPVYRAEVAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  93 LFDSKLTAIDGVHQLLEQIQVPMCVVSNGPVSKMQLSLGKTGLLPFMGDNLFSGYDLQRWKPDPAVLYKAAEVMQVDIKR 172
Cdd:PRK10563  82 LFDSELEPIAGANALLESITVPMCVVSNGPVSKMQHSLGKTGMLHYFPDKLFSGYDIQRWKPDPALMFHAAEAMNVNVEN 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859 173 CILVEDSVAGAQAGIAAGIPVFYYCADPHNPPLDNPLVTTFYDMRELPALWHAKGYAITA 232
Cdd:PRK10563 162 CILVDDSSAGAQSGIAAGMEVFYFCADPHNKPIDHPLVTTFTDLAQLPELWKARGWDITR 221
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
14-181 2.01e-53

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 170.78  E-value: 2.01e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  14 PIDCVLFDCDGTLVDSELLCCEAYVEMFAHFGVTVSfDEMYKTYKGVKLYEIIAIINKQHGLDVPKEEMEVVFRQHVARL 93
Cdd:COG0637    1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLT-EEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYREL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  94 FDS-KLTAIDGVHQLLEQIQ---VPMCVVSNGPVSKMQLSLGKTGLLPFMgDNLFSGYDLQRWKPDPAVLYKAAEVMQVD 169
Cdd:COG0637   80 LAEeGLPLIPGVVELLEALKeagIKIAVATSSPRENAEAVLEAAGLLDYF-DVIVTGDDVARGKPDPDIYLLAAERLGVD 158

                        170
                 ....*....|..
gi 917292859 170 IKRCILVEDSVA 181
Cdd:COG0637  159 PEECVVFEDSPA 170
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 16-180 6.89e-50

subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli 6-phosphogluconate phosphatase YieH; This subfamily includes Escherichia coli YieH/HAD3 an 6-phosphogluconate phosphatase, which can hydrolyzed purines and pyrimidines as secondary substrates. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate, and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate. 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: 319828 [Multi-domain]  Cd Length: 141  Bit Score: 159.79  E-value: 6.89e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  16 DCVLFDCDGTLVDSELLCCEAYVEMFAHFGVTVsfdemyktykgvklyeiiaiinkqhgldvpkeemevvfrqhvARLFD 95
Cdd:cd07526    1 DLVIFDCDGVLVDSEVIAARVLVEVLAELGARV------------------------------------------LAAFE 38

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  96 SKLTAIDGVHQLLEQIQVPMCVVSNGPVSKMQLSLGKTGLLPFMGDNLFSGYDLQRWKPDPAVLYKAAEVMQVDIKRCIL 175
Cdd:cd07526   39 AELQPIPGAAAALSALTLPFCVASNSSRERLTHSLGLAGLLAYFEGRIFSASDVGRGKPAPDLFLHAAAQMGVAPERCLV 118


                 ....*
gi 917292859 176 VEDSV 180
Cdd:cd07526  119 IEDSP 123
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
15-180 5.41e-29

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 108.09  E-value: 5.41e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  15 IDCVLFDCDGTLVDSELLCCEAYVEMFAHFGVTVSFDEMYKTYKGVKLYEIIAIINkQHGLDVPKEEMEVVFRQHVARLF 94
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEELRALIGLGLRELLRRLL-GEDPDEELEELLARFRELYEEEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  95 DSKLTAIDGVHQLLEQIQ---VPMCVVSNGPVSKMQLSLGKTGLLPFMgDNLFSGYDLQRWKPDPAVLYKAAEVMQVDIK 171
Cdd:COG0546   80 LDETRLFPGVRELLEALKargIKLAVVTNKPREFAERLLEALGLDDYF-DAIVGGDDVPPAKPKPEPLLEALERLGLDPE 158


                 ....*....
gi 917292859 172 RCILVEDSV 180
Cdd:COG0546  159 EVLMVGDSP 167
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 15-179 3.32e-25

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: 98.56  E-value: 3.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  15 IDCVLFDCDGTLVDSELLCCEAYVEMFAHFGVTVSFDEMYKTYKGVK-------------LYEIIAIINKQHGLDVPKEE 81
Cdd:COG1011    1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELAEAYRAIEyalwrryergeitFAELLRRLLEELGLDLAEEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  82 MEvVFRQHVARLFDskltAIDGVHQLLEQIQ---VPMCVVSNGPVSKMQLSLGKTGLLPFMgDNLFSGYDLQRWKPDPAV 158
Cdd:COG1011   81 AE-AFLAALPELVE----PYPDALELLEALKargYRLALLTNGSAELQEAKLRRLGLDDLF-DAVVSSEEVGVRKPDPEI 154

                        170       180
                 ....*....|....*....|.
gi 917292859 159 LYKAAEVMQVDIKRCILVEDS 179
Cdd:COG1011  155 FELALERLGVPPEEALFVGDS 175
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 18-179 1.29e-20

beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: the characterized beta-phosphoglucomutases (including those from E.coli, B.subtilus and L.lactis, TIGR01990), a clade of putative bPGM's from mycobacteria and a clade including the uncharacterized E.coli and H.influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the "variant 3" glu-asp version of the third conserved HAD domain (TIGR01509).


Pssm-ID: 213673 [Multi-domain]  Cd Length: 185  Bit Score: 85.47  E-value: 1.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859   18 VLFDCDGTLVDSELLCCEAYVEMFAHFGVtvSFDEMYKTY-KGVKLYEIIAIINKQHGLDVPKEEMEVVF---RQHVARL 93
Cdd:TIGR02009   4 VIFDMDGVITDTAPLHAQAWKHIAAKYGI--SFDKQYNESlKGLSREDILRAILKLRGDGLSLEEIHQLAerkNELYREL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859   94 FDSKLTAI-DGVHQLLEQIQ---VPMCVVSNGPVSKMqlSLGKTGLLPFMgDNLFSGYDLQRWKPDPAVLYKAAEVMQVD 169
Cdd:TIGR02009  82 LRLTGVAVlPGIRNLLKRLKakgIAVGLGSSSKNAPR--ILAKLGLRDYF-DAIVDASEVKNGKPHPETFLLAAELLGVP 158

                         170
                  ....*....|
gi 917292859  170 IKRCILVEDS 179
Cdd:TIGR02009 159 PNECIVFEDA 168
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
18-179 2.70e-18

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 79.17  E-value: 2.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859   18 VLFDCDGTLVDSELLCCEAYVEMFAHFGVTVSFDEMYKTYKGVKLYEIIAIINKQHGLDvpkEEMEVVFRQHVARLFDSK 97
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYGELSEEEILKFIGLPLREIFRYLGVSEDEE---EKIEFYLRKYNEELHDKL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859   98 LTAIDGVHQLLEQIQ---VPMCVVSNGPVSKMQLSLGKTGLLPFMgDNLFSGYDLQRWKPDPAVLYKAAEVMQVDIKRCI 174
Cdd:pfam13419  78 VKPYPGIKELLEELKeqgYKLGIVTSKSRENVEEFLKQLGLEDYF-DVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVI 156


                  ....*
gi 917292859  175 LVEDS 179
Cdd:pfam13419 157 YVGDS 161
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 15-181 1.57e-17

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: 77.63  E-value: 1.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859   15 IDCVLFDCDGTLVDSELLCCEAYVEMFAHF-----------GVTVSFDEMYKTY-KGVKLYEIIAIINKQHGLDVPKEEM 82
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHplakaivaaaeDLPIPVEDFTARLlLGKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859   83 EVVFRQHVARLF-DSKLTAIDGVHQLLEQIQ---VPMCVVSNGPVSKMQLSLGKTGLLPFMgDNLFSGYDLQRWKPDPAV 158
Cdd:pfam00702  81 TVVLVELLGVIAlADELKLYPGAAEALKALKergIKVAILTGDNPEAAEALLRLLGLDDYF-DVVISGDDVGVGKPKPEI 159

                         170       180
                  ....*....|....*....|...
gi 917292859  159 LYKAAEVMQVDIKRCILVEDSVA 181
Cdd:pfam00702 160 YLAALERLGVKPEEVLMVGDGVN 182
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 18-180 1.16e-16

beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; This family represents the beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. Family members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. It 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: 319808 [Multi-domain]  Cd Length: 143  Bit Score: 73.80  E-value: 1.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  18 VLFDCDGTLVDSELLCCEAYVEMfahfgvtvsfdemyktykgvKLYEiiaiinkqhgldvpkEEMEVVFRQHVARLFDsk 97
Cdd:cd07505    2 VIFDMDGVLIDTEPLHRQAWQLL--------------------ERKN---------------ALLLELIASEGLKLKP-- 44

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  98 ltaidGVHQLLEQIQ---VPMCVVSNGPVSKMQLSLGKTGLLPFMGDNLFSGYDLQRWKPDPAVLYKAAEVMQVDIKRCI 174
Cdd:cd07505   45 -----GVVELLDALKaagIPVAVATSSSRRNVELLLLELGLLRGYFDVIVSGDDVERGKPAPDIYLLAAERLGVDPERCL 119


                 ....*.
gi 917292859 175 LVEDSV 180
Cdd:cd07505  120 VFEDSL 125
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 8-180 9.32e-15

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 71.66  E-value: 9.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859   8 ANSHASPiDCVLFDCDGTLVDSEL-LCCEAYVEMFAHFGVT-VSFDemyktykgVKLYEIIAIIN----------KQHGL 75
Cdd:PLN02779  34 ASASALP-EALLFDCDGVLVETERdGHRVAFNDAFKEFGLRpVEWD--------VELYDELLNIGggkermtwyfNENGW 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  76 ------DVPKEE------------------MEVV------FRQHVARLFDSKLTAidgvhqlleQIQVPMCVVSN-GPVS 124
Cdd:PLN02779 105 ptstieKAPKDEeerkelvdslhdrktelfKELIesgalpLRPGVLRLMDEALAA---------GIKVAVCSTSNeKAVS 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 917292859 125 KMQLSLgkTGLLPFMGDNLFSGYDLQRWKPDPAVLYKAAEVMQVDIKRCILVEDSV 180
Cdd:PLN02779 176 KIVNTL--LGPERAQGLDVFAGDDVPKKKPDPDIYNLAAETLGVDPSRCVVVEDSV 229
PGP_bact TIGR01449
2-phosphoglycolate phosphatase, prokaryotic; PGP is an essential enzyme in the glycolate ...
 18-222 7.04e-14

2-phosphoglycolate phosphatase, prokaryotic; 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 Ralstonia (Alcaligenes) eutropha and Rhodobacter sphaeroides, the PGP gene (CbbZ) is located on an operon along with other Calvin cycle enzymes including RubisCO. The only other pertinent experimental evidence concerns the gene from E. coli. The in vitro activity of the Ralstonia and Escherichia enzymes was determined with crude cell extracts of strains containing PGP on expression plasmids and compared to controls. In E. coli, however, there does not appear to be a functional Calvin cycle (RubisCO is absent), although the E. coli PGP gene (gph) is on the same operon (dam) with ribulose-5-phosphate-3-epimerase (rpe), a gene in the pentose-phosphate pathway (along with other, unrelated genes). The E. coli enzyme is not expressed under normal laboratory conditions; the pathway to which it belongs has not been determined. In fact, the possibility exists, although unlikely, that the E. coli enzyme and others within this equivalog have as their physiological substrate another, closely related molecule. The other seed chosen for this model, from Xylella fastidiosa has no experimental evidence, but is a plant pathogen and thus may obtain phosphoglycolate from its host. This model has been restricted to encompass only proteobacteria as no related PGP has been verified outside of this clade. Sequences from Aquifex aeolicus and Treponema pallidum fall between the trusted and noise cutoffs. Just below the noise cutoff is a gene which is part of the operon for the biosynthesis of the blue pigment, indigoidine, from Erwinia (Pectobacterium) chrysanthemi, a plant pathogen. It does not seem likely, considering the proposed biosynthetic mechanism, that the dephosphorylation of phosphoglycolate or a closely related compound is required. Possibly, this gene is fortuitously located in this operon, or has an indirect relationship to the necessity for the biosynthesis of this compound. Sequences from 11 species have been annotated as PGP or putative PGP but fall below the noise cutoff. None of these have experimental validation. This enzyme is a member of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolase enzymes (pfam00702). [Energy metabolism, Sugars]


Pssm-ID: 130516 [Multi-domain]  Cd Length: 213  Bit Score: 67.92  E-value: 7.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859   18 VLFDCDGTLVDSELLCCEAYVEMFAHFGVTVSFDEMYKTYKGVKLYEIIAIINKQHGLDVPKE---EMEVVFRQHVARLF 94
Cdd:TIGR01449   1 VLFDLDGTLVDSAPDIAAAVNMALAALGLPPATLARVIGFIGNGVPVLMERVLAWAGQEPDAQrvaELRKLFDRHYEEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859   95 DSKLTAIDGVHQLLEQIQ---VPMCVVSNGPVSKMQLSLGKTGLLPFMgDNLFSGYDLQRWKPDPAVLYKAAEVMQVDIK 171
Cdd:TIGR01449  81 GELTSVFPGVEATLGALRakgLRLGLVTNKPTPLARPLLELLGLAKYF-SVLIGGDSLAQRKPHPDPLLLAAERLGVAPQ 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 917292859  172 RCILVEDSVAGAQAGIAAGIP--VFYYCADPHNPPLDNPLVTTFYDMRELPAL 222
Cdd:TIGR01449 160 QMVYVGDSRVDIQAARAAGCPsvLLTYGYRYGEAIDLLPPDVLYDSLNELPPL 212
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 18-180 1.92e-13

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; 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/E), (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 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe 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 relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 65.88  E-value: 1.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859   18 VLFDCDGTLVDSELLCCEAYVEMFAHFGVTvsfDEMYKTYKgvKLYEIIAIINKQHGLDVPKEemevvFRQHVARLFDSK 97
Cdd:TIGR01549   2 ILFDIDGTLVDIKFAIRRAFPQTFEEFGLD---PASFKALK--QAGGLAEEEWYRIATSALEE-----LQGRFWSEYDAE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859   98 LTAIDGVHQLLEQI---QVPMCVVSNGPVSKMQLSLGKTGLLPFmgDNLFSGYDLQRWKPDPAVLYKAAEVMQVDiKRCI 174
Cdd:TIGR01549  72 EAYIRGAADLLARLksaGIKLGIISNGSLRAQKLLLRLFGLGDY--FELILVSDEPGSKPEPEIFLAALESLGVP-PEVL 148


                  ....*.
gi 917292859  175 LVEDSV 180
Cdd:TIGR01549 149 HVGDNL 154
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 1-193 3.80e-13

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 66.79  E-value: 3.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859   1 MSVS--QNIANSHAS-----PIDCVLFDCDGTLVDSELLCCEAYVEMFAHF----GVTVSFDEMYKTYKGvKLYEIIAII 69
Cdd:PLN02770   1 MTVSsgENSVESKSSlsglaPLEAVLFDVDGTLCDSDPLHYYAFREMLQEInfngGVPITEEFFVENIAG-KHNEDIALG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  70 ----NKQHGLDVpKEEMEVVFRqhvaRLFDSKLTAIDGVHQLLEQIQ---VPMCVVSNGPVSKMQLSLGKTGLLPFMgDN 142
Cdd:PLN02770  80 lfpdDLERGLKF-TDDKEALFR----KLASEQLKPLNGLYKLKKWIEdrgLKRAAVTNAPRENAELMISLLGLSDFF-QA 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 917292859 143 LFSGYDLQRWKPDPAVLYKAAEVMQVDIKRCILVEDSVAGAQAGIAAGIPV 193
Cdd:PLN02770 154 VIIGSECEHAKPHPDPYLKALEVLKVSKDHTFVFEDSVSGIKAGVAAGMPV 204
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 15-179 3.95e-12

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. 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: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 63.07  E-value: 3.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  15 IDCVLFDCDGTLVDSELLCCEAYVEMFAHFGVTVSFDEMYKTYKGVKLYEIIAIINKQHgldvpKEEMEVVFRQHVARLF 94
Cdd:cd02616    1 ITTILFDLDGTLIDTNELIIKSFNHTLKEYGLEGYTREEVLPFIGPPLRETFEKIDPDK-----LEDMVEEFRKYYREHN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  95 DSKLTAIDGVHQLLEQIQ---VPMCVVSNGPVSKMQLSLGKTGLLPFMgDNLFSGYDLQRWKPDPAVLYKAAEVMQVDIK 171
Cdd:cd02616   76 DDLTKEYPGVYETLARLKsqgIKLGVVTTKLRETALKGLKLLGLDKYF-DVIVGGDDVTHHKPDPEPVLKALELLGAEPE 154


                 ....*...
gi 917292859 172 RCILVEDS 179
Cdd:cd02616  155 EALMVGDS 162
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
18-179 7.74e-11

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 59.82  E-value: 7.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  18 VLFDCDGTLVDSE---LLCCEAyveMFAHFGVTVSFDEMYKTY--KGV-KLYEIiAIINKQHGLDVPK-EEMEVVFRQHV 90
Cdd:PRK13222   9 VAFDLDGTLVDSApdlAAAVNA---ALAALGLPPAGEERVRTWvgNGAdVLVER-ALTWAGREPDEELlEKLRELFDRHY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  91 ARLFDSKLTAIDGVHQLLEQIQ---VPMCVVSNGPVSKMQLSLGKTGLlpfmgDNLFS----GYDLQRWKPDPAVLYKAA 163
Cdd:PRK13222  85 AENVAGGSRLYPGVKETLAALKaagYPLAVVTNKPTPFVAPLLEALGI-----ADYFSvvigGDSLPNKKPDPAPLLLAC 159

                        170
                 ....*....|....*.
gi 917292859 164 EVMQVDIKRCILVEDS 179
Cdd:PRK13222 160 EKLGLDPEEMLFVGDS 175
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 18-179 1.34e-10

Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGP; EC 3.1.3.18) catalyzes the conversion of 2-phosphoglycolate into glycolate and phosphate. 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 (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. 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: 319854 [Multi-domain]  Cd Length: 212  Bit Score: 58.79  E-value: 1.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  18 VLFDCDGTLVDSELLCCEAYVEMFAHFGVTVSFDEMYKTY--KGV-KLYEIiAIINKQHGLDVPK--EEMEVVFRQHVAR 92
Cdd:cd16417    2 VAFDLDGTLVDSAPDLAEAANAMLAALGLPPLPEETVRTWigNGAdVLVER-ALTGAREAEPDEElfKEARALFDRHYAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  93 LFDSKLTAIDGVHQLLEQIQ---VPMCVVSNGPVskmQLSLGktgLLPFMG-DNLFS----GYDLQRWKPDPAVLYKAAE 164
Cdd:cd16417   81 TLSVHSHLYPGVKEGLAALKaqgYPLACVTNKPE---RFVAP---LLEALGiSDYFSlvlgGDSLPEKKPDPAPLLHACE 154

                        170
                 ....*....|....*
gi 917292859 165 VMQVDIKRCILVEDS 179
Cdd:cd16417  155 KLGIAPAQMLMVGDS 169
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 15-179 6.12e-10

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 56.96  E-value: 6.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  15 IDCVLFDCDGTLVDSELLCCEAYVEMFAHFgvtvsFDEMYK-----TYKGVKLYEIIAIINKQHgldvpKEEMEVVFRQH 89
Cdd:PRK13288   3 INTVLFDLDGTLINTNELIISSFLHTLKTY-----YPNQYKredvlPFIGPSLHDTFSKIDESK-----VEEMITTYREF 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  90 VARLFDSKLTAIDGVHQLLEQIQ---VPMCVVSNGPVSKMQLSLGKTGLLPFMgDNLFSGYDLQRWKPDPAVLYKAAEVM 166
Cdd:PRK13288  73 NHEHHDELVTEYETVYETLKTLKkqgYKLGIVTTKMRDTVEMGLKLTGLDEFF-DVVITLDDVEHAKPDPEPVLKALELL 151

                        170
                 ....*....|...
gi 917292859 167 QVDIKRCILVEDS 179
Cdd:PRK13288 152 GAKPEEALMVGDN 164
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 18-180 6.70e-10

uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized Bacillus subtilis YhcW; This subfamily includes the uncharacterized Bacillus subtilis YhcW. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. 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: 319859 [Multi-domain]  Cd Length: 169  Bit Score: 56.11  E-value: 6.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  18 VLFDCDGTLVDSELLCCEAYVEMFahfgvtvsfdemyktykgvklyeiiaiiNKQHgldvpkeemevvfRQHVARLFDSK 97
Cdd:cd16423    2 VIFDFDGVIVDTEPLWYEAWQELL----------------------------NERR-------------NELIKRQFSEK 40

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  98 --LTAIDGVHQLLEQIQ---VPMCVVSNGPVSKMQLSLGKTGLLPFMgDNLFSGYDLQRWKPDPAVLYKAAEVMQVDIKR 172
Cdd:cd16423   41 tdLPPIEGVKELLEFLKekgIKLAVASSSPRRWIEPHLERLGLLDYF-EVIVTGDDVEKSKPDPDLYLEAAERLGVNPEE 119


                 ....*...
gi 917292859 173 CILVEDSV 180
Cdd:cd16423  120 CVVIEDSR 127
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 17-179 1.88e-09

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: 55.12  E-value: 1.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859   17 CVLFDCDGTLVDSEllccEAYVEMFAHFGVTVSFDEMYKTYKGvKLYEIIAIINKQHG-LDVPKEEMEVVFRQHVARLFD 95
Cdd:TIGR01509   1 AILFDLDGVLVDTE----FAIAKLINREELGLVPDELGVSAVG-RLELALRRFKAQYGrTISPEDAQLLYKQLFYEQIEE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859   96 -SKLTAIDGVHQLLEQI---QVPMCVVSNGPVSkMQLSLGKTGLLPFMGDNLFSGyDLQRWKPDPAVLYKAAEVMQVDIK 171
Cdd:TIGR01509  76 eAKLKPLPGVRALLEALrarGKKLALLTNSPRA-HKLVLALLGLRDLFDVVIDSS-DVGLGKPDPDIYLQALKALGLEPS 153


                  ....*...
gi 917292859  172 RCILVEDS 179
Cdd:TIGR01509 154 ECVFVDDS 161
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 18-179 3.42e-09

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: 54.71  E-value: 3.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  18 VLFDCDGTLVDSELLCCEAYVEMFAHFGVTVSFDEMYKTYKGVKLYEIIAIINKQHgldVPKEEMEVVFRQHVAR----L 93
Cdd:cd07533    2 VIFDWDGTLADSQHNIVAAMTAAFADLGLPVPSAAEVRSIIGLSLDEAIARLLPMA---TPALVAVAERYKEAFDilrlL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  94 FDSKLTAIDGVHQLLEQIQVP--MCVVSNGPvskmqlslGKTGLLPFMGDNLFSGY-------DLQRWKPDPAVLYKAAE 164
Cdd:cd07533   79 PEHAEPLFPGVREALDALAAQgvLLAVATGK--------SRRGLDRVLEQHGLGGYfdatrtaDDTPSKPHPEMLREILA 150

                        170
                 ....*....|....*
gi 917292859 165 VMQVDIKRCILVEDS 179
Cdd:cd07533  151 ELGVDPSRAVMVGDT 165
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 18-180 4.18e-09

subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides xylulose-1,5-bisphosphate phosphatase CbbY; This family includes Rhodobacter sphaeroides and Arabidopsis thaliana xylulose-1,5-bisphosphate phosphatase CbbY which convert xylulose-1,5-bisphosphate (a potent inhibitor of Ribulose-1,5-bisphosphate carboxylase/oxygenase, Rubisco), to the non-inhibitory compound xylulose-5-phosphate. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. 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: 319830 [Multi-domain]  Cd Length: 199  Bit Score: 54.69  E-value: 4.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  18 VLFDCDGTLVDSELLCCEAYVEMFAHF-GVTVSFD-EMYKTY----------------------KGVKLYEIIAIINKQ- 72
Cdd:cd07528    2 LIFDVDGTLAETEELHRRAFNNAFFAErGLDWYWDrELYGELlrvgggkeriaayfekvgwpesAPKDLKELIADLHKAk 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  73 --HGLDVPKEEmEVVFRQHVARLFDSKLTAidgvhqlleQIQVPMCVVSNGPVSKMQLS--LGKTGLLPFmgDNLFSGYD 148
Cdd:cd07528   82 teRYAELIAAG-LLPLRPGVARLIDEAKAA---------GVRLAIATTTSPANVDALLSalLGPERRAIF--DAIAAGDD 149

                        170       180       190
                 ....*....|....*....|....*....|..
gi 917292859 149 LQRWKPDPAVLYKAAEVMQVDIKRCILVEDSV 180
Cdd:cd07528  150 VAEKKPDPDIYLLALERLGVSPSDCLAIEDSA 181
PLN02940 PLN02940
riboflavin kinase
 7-180 5.69e-09

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 55.23  E-value: 5.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859   7 IANSHASPIDCVLFDCDGTLVDSELLCCEAYVEMFAHFGVTVSFDEMYKTYkGVKLYEIIAIINKQHGLDVPKEEMEVVF 86
Cdd:PLN02940   3 AAKPLKKLVSHVILDLDGTLLNTDGIVSDVLKAFLVKYGKQWDGREAQKIV-GKTPLEAAATVVEDYGLPCSTDEFNSEI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  87 RQHVARLFDsKLTAIDGVHQLLEQIQ---VPMCVVSNGPVSKMQLSL----GKTGLLPFM--GDNLFSGydlqrwKPDPA 157
Cdd:PLN02940  82 TPLLSEQWC-NIKALPGANRLIKHLKshgVPMALASNSPRANIEAKIschqGWKESFSVIvgGDEVEKG------KPSPD 154

                        170       180
                 ....*....|....*....|...
gi 917292859 158 VLYKAAEVMQVDIKRCILVEDSV 180
Cdd:PLN02940 155 IFLEAAKRLNVEPSNCLVIEDSL 177
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 18-179 9.28e-09

subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and Gpp2; This subfamily includes Arabidopsis thaliana AtGpp1 and AtGpp2, and Drosophila GS1-like protein (Dmel\Gs1l) of unknown function. AtGpp1 and AtGpp2 are constitutively expressed in all the Arabidopsis tissues and unaffected under abiotic stress. Overexpression of AtGpp2 in transgenic Arabidopsis plants increases the specific DL-glycerol-3-phosphatase activity and improves the plants tolerance to salt, osmotic and oxidative stress. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. 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: 319831 [Multi-domain]  Cd Length: 192  Bit Score: 53.51  E-value: 9.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  18 VLFDCDGTLVDSELLCCEAYVEMFAHFGVTVSFDEMYKTyKGVKLYEIIAIINKQHGLDVPKEEMEVVFRQHVARLFDSK 97
Cdd:cd07529    4 CIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKM-MGRPASEAARIIVDELKLPMSLEEEFDEQQEALAELFMGT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  98 LTAIDGVHQLLEQIQ---VPMCVVSNGPVSKMQLSLGKTGLLPFMGDNLFSGYD---LQRWKPDPAVLYKAA---EVMQV 168
Cdd:cd07529   83 AKLMPGAERLLRHLHahnIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDpevKGRGKPAPDIFLVAAkrfNEPPK 162

                        170
                 ....*....|.
gi 917292859 169 DIKRCILVEDS 179
Cdd:cd07529  163 DPSKCLVFEDS 173
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 2-179 1.66e-08

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 54.47  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859    2 SVSQNIANSHASPIDCVLFDCDGTLVDSELLCCEAYVEMFAHFGVTVSFDEM--------------YKTYKGVKLYEIIA 67
Cdd:PLN02919   62 SRGAEIATEEWGKVSAVLFDMDGVLCNSEEPSRRAAVDVFAEMGVEVTVEDFvpfmgtgeanflggVASVKGVKGFDPDA 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859   68 iinkqhgldvPKEEMEVVFRQHVARLfDSKLtAIDGVHQLLEQIQ---VPMCVVSNGPVSKMQLSLGKTGLLPFMGDNLF 144
Cdd:PLN02919  142 ----------AKKRFFEIYLEKYAKP-NSGI-GFPGALELITQCKnkgLKVAVASSADRIKVDANLAAAGLPLSMFDAIV 209

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 917292859  145 SGYDLQRWKPDPAVLYKAAEVMQVDIKRCILVEDS 179
Cdd:PLN02919  210 SADAFENLKPAPDIFLAAAKILGVPTSECVVIEDA 244
PRK10826 PRK10826
hexitol phosphatase HxpB;
10-180 1.41e-07

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 50.33  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  10 SHASPIDCVLFDCDGTLVDSELLCCEAYVEMFAHFGVTVSFDEMYKTYKGVKLYEIIAIINKQHGLDVPKEEmEVVFR-- 87
Cdd:PRK10826   2 STPRQILAAIFDMDGLLIDSEPLWDRAELDVMASLGVDISRREELPDTLGLRIDQVVDLWYARQPWNGPSRQ-EVVQRii 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  88 QHVARLFDSKLTAIDGVHQLLEQIQ---VPMCVVSNGPVSKMQLSLGKTGLLPFMgDNLFSGYDLQRWKPDPAVLYKAAE 164
Cdd:PRK10826  81 ARVISLIEETRPLLPGVREALALCKaqgLKIGLASASPLHMLEAVLTMFDLRDYF-DALASAEKLPYSKPHPEVYLNCAA 159

                        170
                 ....*....|....*.
gi 917292859 165 VMQVDIKRCILVEDSV 180
Cdd:PRK10826 160 KLGVDPLTCVALEDSF 175
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 93-179 1.53e-07

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: 48.31  E-value: 1.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  93 LFDSKLTAIDGVHQLLEQIQ--VPMCVVSNGPVSKMQLSLGKTGLLPFMgDNLFSGYDLQRWKPDPAVLYKAAEVMQVDI 170
Cdd:cd04305    3 IFDLDDTLLPGAKELLEELKkgYKLGIITNGPTEVQWEKLEQLGIHKYF-DHIVISEEVGVQKPNPEIFDYALNQLGVKP 81


                 ....*....
gi 917292859 171 KRCILVEDS 179
Cdd:cd04305   82 EETLMVGDS 90
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 18-176 2.96e-07

L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. 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: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 49.57  E-value: 2.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  18 VLFDCDGTLVDSELLCcEAYVEMFAHFGVTVS---FDEM------------YKTYKGVkLYEIIAIINKQHGLDVpkeem 82
Cdd:cd02588    3 LVFDVYGTLIDWHSGL-AAAERAFPGRGEELSrlwRQKQleytwlvtlmgpYVDFDEL-TRDALRATAAELGLEL----- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  83 evvFRQHVARLFDS--KLTAIDGVHQLLEQIQ---VPMCVVSNGPVSKMQLSLGKTGLLPFMgDNLFSGYDLQRWKPDPA 157
Cdd:cd02588   76 ---DESDLDELGDAylRLPPFPDVVAGLRRLReagYRLAILSNGSPDLIEDVVANAGLRDLF-DAVLSAEDVRAYKPAPA 151

                        170
                 ....*....|....*....
gi 917292859 158 VLYKAAEVMQVDIKRCILV 176
Cdd:cd02588  152 VYELAAERLGVPPDEILHV 170
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 17-222 3.04e-07

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


Pssm-ID: 319815 [Multi-domain]  Cd Length: 214  Bit Score: 49.24  E-value: 3.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  17 CVLFDCDGTLVDSELLCCEAYVEMFAHFGVT-VSFDEMYKT-YKGVKLYEIIAIINKQHGLDVP-KEEMEVVFRQH---- 89
Cdd:cd07512    1 AVIFDLDGTLIDSAPDLHAALNAVLAAEGLApLSLAEVRSFvGHGAPALIRRAFAAAGEDLDGPlHDALLARFLDHyead 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  90 ---VARLFDSKLTAIDGvhqlLEQIQVPMCVVSNGPVSKMQLSLGKTGLLPFMGDnLFSGYDLQRWKPDPAVLYKAAEVM 166
Cdd:cd07512   81 ppgLTRPYPGVIEALER----LRAAGWRLAICTNKPEAPARALLSALGLADLFAA-VVGGDTLPQRKPDPAPLRAAIRRL 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 917292859 167 QVDIKRCILVEDSVAGAQAGIAAGIPVFYYCADP-HNPPLDNPLVTTFYDMRELPAL 222
Cdd:cd07512  156 GGDVSRALMVGDSETDAATARAAGVPFVLVTFGYrHAPVAELPHDAVFSDFDALPDL 212
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 18-186 1.94e-06

subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p); This subfamily includes Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p). GPP1p and GPP2p are involved in glycerol biosynthesis, GPP1 is induced in response to both anaerobic and hyperosmotic stress, GPP2 is induced in response to hyperosmotic or oxidative stress, and during diauxic shift; overexpression of DOG1 or DOG2 confers 2-deoxyglucose resistance. These belong to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), and Escherichia coli 6-phosphogluconate phosphatase YieH. 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: 319829 [Multi-domain]  Cd Length: 205  Bit Score: 46.95  E-value: 1.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  18 VLFDCDGTLVDSEllccEAYVEMFAHFGVT--VSFDEMYKTYKGVKLYEIIAII-----NKQHGLDVPKEEMEVVfrqhv 90
Cdd:cd07527    2 LLFDMDGTLVDST----PAVERAWHKWAKEhgVDPEEVLKVSHGRRAIDVIRKLapddaDIELVLALETEEPESY----- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  91 arlfDSKLTAIDGVHQLL----EQIQVPMCVVSNGPV--SKMQLSLGKTglLPfmgDNLFSGYDLQRWKPDPAVLYKAAE 164
Cdd:cd07527   73 ----PEGVIAIPGAVDLLaslpAAGDRWAIVTSGTRAlaEARLEAAGLP--HP---EVLVTADDVKNGKPDPEPYLLGAK 143

                        170       180
                 ....*....|....*....|..
gi 917292859 165 VMQVDIKRCILVEDSVAGAQAG 186
Cdd:cd07527  144 LLGLDPSDCVVFEDAPAGIKAG 165
YjjG/YfnB TIGR02254
noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including ...
 15-179 1.64e-05

noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including YjjG from E. coli and YfnB from B. subtilis. YjjG has been shown to act as a house-cleaning enzyme, cleaving nucleotides with non-canonical nucleotide bases. This family is a member of the haloacid dehalogenase (HAD) superfamily of hydrolases which are characterized by three conserved sequence motifs. By virtue of an alpha helical domain in-between the first and second conserved motif, this family is a member of subfamily IA (TIGR01549).


Pssm-ID: 162788 [Multi-domain]  Cd Length: 224  Bit Score: 44.40  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859   15 IDCVLFDCDGTLVDSELLCCEAYVEMFAHFGVTvSFDEMYKTYKGV-----KLYEIIAIINKQ----------HGLDVPK 79
Cdd:TIGR02254   1 YKTLLFDLDDTILDFQAAEALALRLLFEDQGIP-LTEDMFAQYKEInqglwRAYEEGKITKDEvvntrfsallKEYNTEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859   80 EE--MEVVFRQHVARlfdsKLTAIDGVHQLLEQIQ--VPMCVVSNGpVSKMQ-LSLGKTGLLPFMgDNLFSGYDLQRWKP 154
Cdd:TIGR02254  80 DEalLNQKYLRFLEE----GHQLLPGAFELMENLQqkFRLYIVTNG-VRETQyKRLRKSGLFPFF-DDIFVSEDAGIQKP 153

                         170       180
                  ....*....|....*....|....*.
gi 917292859  155 DPAVLYKAAEVM-QVDIKRCILVEDS 179
Cdd:TIGR02254 154 DKEIFNYALERMpKFSKEEVLMIGDS 179
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 18-158 3.27e-05

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: 43.48  E-value: 3.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859   18 VLFDCDGTLVDSELL---CCEAY--------VEMFAH---FGVTVSFDEMYKTYKGVkLYEIIAIINKQHGLDVPKEEme 83
Cdd:TIGR01428   4 LVFDVYGTLFDVHSVaerAAELYggrgealsQLWRQKqleYSWLRTLMGPYKDFWDL-TREALRYLLGRLGLEDDESA-- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859   84 vvfrqhVARLFDSKLT------AIDGVHQLLEQIqVPMCVVSNGPVSKMQLSLGKTGL-LPFmgDNLFSGYDLQRWKPDP 156
Cdd:TIGR01428  81 ------ADRLAEAYLRlpphpdVPAGLRALKERG-YRLAILSNGSPAMLKSLVKHAGLdDPF--DAVLSADAVRAYKPAP 151


                  ..
gi 917292859  157 AV 158
Cdd:TIGR01428 152 QV 153
HAD_PHN cd02586
Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; ...
 15-180 3.97e-05

Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; Degradation of the ubiquitous natural phosphonate 2-aminoethylphosphonate (AEP) into useable forms of nitrogen, carbon, and phosphorus is a two-step metabolic pathway. The first step, catalyzed by AEP transaminase, involves the transfer of NH3 from AEP to pyruvate, yielding phosphonoacetaldehyde (P-Ald) and alanine. In the second step, phosphonatase catalyzes the hydrolytic P-C bond cleavage of P-Ald to form orthophosphate and acetaldehyde. 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: 319785 [Multi-domain]  Cd Length: 242  Bit Score: 43.44  E-value: 3.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  15 IDCVLFDCDGTLVD-SELLCCEAYVEMFAHFGVTVSFDEMYKTYKGVKLYEIIAIIN---------KQHGLDVPKEEMEV 84
Cdd:cd02586    1 IEAVIFDWAGTTVDyGSFAPVNAFVEAFAQRGVQITLEEARKPMGLLKIDHIRALLEmprvaeawrAVFGRLPTEADVDA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  85 VFRQHVARLFDSKLT-------AIDGVHQLLEQ-IQVPMCVVSNGPVskMQLSLGKTGLLPFMGDNLFSGYDLQRWKPDP 156
Cdd:cd02586   81 LYEEFEPILIASLAEysspipgVLEVIAKLRARgIKIGSTTGYTREM--MDIVLPEAAAQGYRPDSLVTPDDVPAGRPYP 158

                        170       180
                 ....*....|....*....|....*
gi 917292859 157 AVLYKAAEVMQV-DIKRCILVEDSV 180
Cdd:cd02586  159 WMCYKNAIELGVyDVAAVVKVGDTV 183
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 106-179 2.85e-04

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 41.17  E-value: 2.85e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917292859 106 QLLEQIQVPMCVVSNGPVSKMQLSLGKTGLLPFMgDNLFSGYDLQRWKPDPAVLYKAAEVMQVDIKRCILVEDS 179
Cdd:PLN03243 119 QALKKHEIPIAVASTRPRRYLERAIEAVGMEGFF-SVVLAAEDVYRGKPDPEMFMYAAERLGFIPERCIVFGNS 191
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 93-180 5.50e-04

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: 38.15  E-value: 5.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  93 LFDskltaIDG---VHQLLEQIQ---VPMCVVSNGPVSKMQLSLGKTGLLPFMgDNLFSGYDLQRWKPDPAVLYKAAEVM 166
Cdd:cd01427    3 LFD-----LDGtllAVELLKRLRaagIKLAIVTNRSREALRALLEKLGLGDLF-DGIIGSDGGGTPKPKPKPLLLLLLKL 76

                         90
                 ....*....|....
gi 917292859 167 QVDIKRCILVEDSV 180
Cdd:cd01427   77 GVDPEEVLFVGDSE 90
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 103-179 5.78e-04

beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); Lactococcus lactis beta-PGM catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate as an intermediate. In the forward G6P-forming direction, this reaction links polysaccharide phosphorolysis to glycolysis, in the reverse direction, the reaction provides G1P for the biosynthesis of exo-polysaccharides. This subfamily belongs to the beta-phosphoglucomutase-like family whose other members include Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. 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: 319788 [Multi-domain]  Cd Length: 174  Bit Score: 39.20  E-value: 5.78e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917292859 103 GVHQLLEQIQVPMCVVSNGPVSK-MQLSLGKTGLLPFMgDNLFSGYDLQRWKPDPAVLYKAAEVMQVDIKRCILVEDS 179
Cdd:cd02598   53 GIASLLVDLKAKGIKIALASASKnAPKILEKLGLAEYF-DAIVDGAVLAKGKPDPDIFLAAAEGLGLNPKDCIGVEDA 129
PRK13478 PRK13478
phosphonoacetaldehyde hydrolase; Provisional
 13-52 1.19e-03

phosphonoacetaldehyde hydrolase; Provisional


Pssm-ID: 184075 [Multi-domain]  Cd Length: 267  Bit Score: 39.07  E-value: 1.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 917292859  13 SPIDCVLFDCDGTLVDseLLCC---EAYVEMFAHFGVTVSFDE 52
Cdd:PRK13478   2 MKIQAVIFDWAGTTVD--FGSFaptQAFVEAFAQFGVEITLEE 42
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 107-179 2.02e-03

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 38.70  E-value: 2.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917292859 107 LLEQIQVPMCVVSNGPVSKMQLSLGKTGLLPFMgDNLFSGYDLQRWKPDPAVLYKAAEVMQVDIKRCILVEDS 179
Cdd:PLN02575 227 VLMNYKIPMALVSTRPRKTLENAIGSIGIRGFF-SVIVAAEDVYRGKPDPEMFIYAAQLLNFIPERCIVFGNS 298
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
16-179 2.34e-03

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 37.75  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  16 DCVLFDCDGTLVDSELLCCEAYVEMFAHFGVtvSFDEMYKT-YKGVKLYEIIAIINKQHGLDVPKEEMEvvfrQHVARLF 94
Cdd:PRK10725   6 AGLIFDMDGTILDTEPTHRKAWREVLGRYGL--QFDEQAMVaLNGSPTWRIAQAIIELNQADLDPHALA----REKTEAV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  95 DSKLtaIDGVhQLLEQIQV--------PMCVvSNGPVSKM-QLSLGKTGLLPFMgDNLFSGYDLQRWKPDPAVLYKAAEV 165
Cdd:PRK10725  80 KSML--LDSV-EPLPLIEVvkawhgrrPMAV-GTGSESAIaEALLAHLGLRRYF-DAVVAADDVQHHKPAPDTFLRCAQL 154

                        170
                 ....*....|....
gi 917292859 166 MQVDIKRCILVEDS 179
Cdd:PRK10725 155 MGVQPTQCVVFEDA 168
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 17-111 7.77e-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: 36.42  E-value: 7.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917292859  17 CVLFDCDGTLVDSELLCCEAYVEMFAHFGVTVSFDEMYKTYKGVKLYEIIAiinkQHGLDVPKEEMEVV--FRQHVAR-- 92
Cdd:cd04302    1 TILFDLDGTLTDSAEGITASVQYALEELGIPVPDESELRRFIGPPLEDSFR----ELLPFDEEEAQRAVdaYREYYKEkg 76

                         90
                 ....*....|....*....
gi 917292859  93 LFDSKLtaIDGVHQLLEQI 111
Cdd:cd04302   77 LFENEV--YPGIPELLEKL 93
 
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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