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Conserved domains on  [gi|489522578|ref|WP_003427364|]
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beta-phosphoglucomutase [Clostridioides difficile]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
bPGM super family cl33302
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 3-189 8.67e-85

beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which catalyzes the interconverison of beta-D-glucose-1-phosphate and beta-D-glucose-6-phosphate. The 6-phosphate is capable of non-enzymatic anomerization (alpha <-> beta) while the 1-phosphate is not. A separate enzyme is responsible for the isomerization of the alpha anomers. Beta-D-glucose-1-phosphate results from the phosphorylysis of maltose (2.4.1.8), trehalose (2.4.1.64) or trehalose-6-phosphate (2.4.1.216). Alternatively, these reactions can be run in the synthetic direction to create the disaccharides. All sequenced genomes which contain a member of this family also appear to contain at least one putative maltose or trehalose phosphorylase. Three species, Lactococcus, Enterococcus and Neisseria appear to contain a pair of paralogous beta-PGM's. Beta-phosphoglucomutase is a member of the haloacid dehalogenase superfamily of hydrolase enzymes. These enzymes are characterized by a series of three catalytic motifs positioned within an alpha-beta (Rossman) fold. beta-PGM contains an inserted alpha helical domain in between the first and second conserved motifs and thus is a member of subfamily IA of the superfamily. The third catalytic motif comes in three variants, the third of which, containing a conserved DD or ED, is the only one found here as well as in several other related enzymes (TIGR01509). The enzyme from L. lactis has been extensively characterized including a remarkable crystal structure which traps the pentacoordinate transition state. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


The actual alignment was detected with superfamily member TIGR01990:

Pssm-ID: 213672 [Multi-domain]  Cd Length: 185  Bit Score: 249.53  E-value: 8.67e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578    3 AVLFDLDGVITDTAKYHFEAWYEIAKSLDIEIDETFNEKLKGISREESLDKILLSANKvdSYTKEEKLKVCEEKNNIYIK 82
Cdd:TIGR01990   1 AVIFDLDGVITDTAEYHYLAWKHLADELGIPFDEEFNESLKGVSREESLERILDLGGK--KYSEEEKEELAERKNDYYVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   83 LINSLTYKDILPGINGLIKELKKNNVKLGIASASKNAPRILESLGIKDEFDCIVNPSLLERGKPYPDIFIEGSKMLNLKQ 162
Cdd:TIGR01990  79 LLKELTPADVLPGIKSLLADLKKNNIKIALASASKNAPTILEKLELIDYFDAIVDPAELKKGKPDPEIFLAAAEGLGVSP 158

                         170       180
                  ....*....|....*....|....*..
gi 489522578  163 YDCVGIEDSCSGIKAINAANMTSIGVG 189
Cdd:TIGR01990 159 SECIGIEDAQAGIEAIKAAGMFAVGVG 185
 
Name Accession Description Interval E-value
bPGM TIGR01990
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 3-189 8.67e-85

beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which catalyzes the interconverison of beta-D-glucose-1-phosphate and beta-D-glucose-6-phosphate. The 6-phosphate is capable of non-enzymatic anomerization (alpha <-> beta) while the 1-phosphate is not. A separate enzyme is responsible for the isomerization of the alpha anomers. Beta-D-glucose-1-phosphate results from the phosphorylysis of maltose (2.4.1.8), trehalose (2.4.1.64) or trehalose-6-phosphate (2.4.1.216). Alternatively, these reactions can be run in the synthetic direction to create the disaccharides. All sequenced genomes which contain a member of this family also appear to contain at least one putative maltose or trehalose phosphorylase. Three species, Lactococcus, Enterococcus and Neisseria appear to contain a pair of paralogous beta-PGM's. Beta-phosphoglucomutase is a member of the haloacid dehalogenase superfamily of hydrolase enzymes. These enzymes are characterized by a series of three catalytic motifs positioned within an alpha-beta (Rossman) fold. beta-PGM contains an inserted alpha helical domain in between the first and second conserved motifs and thus is a member of subfamily IA of the superfamily. The third catalytic motif comes in three variants, the third of which, containing a conserved DD or ED, is the only one found here as well as in several other related enzymes (TIGR01509). The enzyme from L. lactis has been extensively characterized including a remarkable crystal structure which traps the pentacoordinate transition state. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 213672 [Multi-domain]  Cd Length: 185  Bit Score: 249.53  E-value: 8.67e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578    3 AVLFDLDGVITDTAKYHFEAWYEIAKSLDIEIDETFNEKLKGISREESLDKILLSANKvdSYTKEEKLKVCEEKNNIYIK 82
Cdd:TIGR01990   1 AVIFDLDGVITDTAEYHYLAWKHLADELGIPFDEEFNESLKGVSREESLERILDLGGK--KYSEEEKEELAERKNDYYVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   83 LINSLTYKDILPGINGLIKELKKNNVKLGIASASKNAPRILESLGIKDEFDCIVNPSLLERGKPYPDIFIEGSKMLNLKQ 162
Cdd:TIGR01990  79 LLKELTPADVLPGIKSLLADLKKNNIKIALASASKNAPTILEKLELIDYFDAIVDPAELKKGKPDPEIFLAAAEGLGVSP 158

                         170       180
                  ....*....|....*....|....*..
gi 489522578  163 YDCVGIEDSCSGIKAINAANMTSIGVG 189
Cdd:TIGR01990 159 SECIGIEDAQAGIEAIKAAGMFAVGVG 185
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
1-203 8.68e-64

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 196.97  E-value: 8.68e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   1 MKAVLFDLDGVITDTAKYHFEAWYEIAKSLDIEIDETFNEKLKGISREESLDKILLSANKvdSYTKEEklkVCEEKNNIY 80
Cdd:COG0637    2 IKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGL--DLPEEE---LAARKEELY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  81 IKLInSLTYKDILPGINGLIKELKKNNVKLGIASASK--NAPRILESLGIKDEFDCIVNPSLLERGKPYPDIFIEGSKML 158
Cdd:COG0637   77 RELL-AEEGLPLIPGVVELLEALKEAGIKIAVATSSPreNAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERL 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489522578 159 NLKQYDCVGIEDSCSGIKAINAANMTSIGVG----KKEVLGKCDHIVED 203
Cdd:COG0637  156 GVDPEECVVFEDSPAGIRAAKAAGMRVVGVPdggtAEEELAGADLVVDD 204
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 3-214 2.79e-62

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: 191.74  E-value: 2.79e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   3 AVLFDLDGVITDTAKYHFEAWYEIAksldieidetfneklkgisreesldkillsankvdsytkeEKLKVCEEKNNIYIK 82
Cdd:cd02598    1 GVIFDLDGVITDTAEYHYRAWKKLA----------------------------------------DKEELAARKNRIYVE 40

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  83 LINSLTYKDILPGINGLIKELKKNNVKLGIASASKNAPRILESLGIKDEFDCIVNPSLLERGKPYPDIFIEGSKMLNLKQ 162
Cdd:cd02598   41 LIEELTPVDVLPGIASLLVDLKAKGIKIALASASKNAPKILEKLGLAEYFDAIVDGAVLAKGKPDPDIFLAAAEGLGLNP 120

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489522578 163 YDCVGIEDSCSGIKAINAANMTSIGVGKKEVLGKCDHIVEDT-SLLNYNTLLQ 214
Cdd:cd02598  121 KDCIGVEDAQAGIRAIKAAGFLVVGVGREEDLLGADIVVPDTtADLTIEELLE 173
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 1-182 1.98e-24

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: 95.35  E-value: 1.98e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578    1 MKAVLFDLDGVITDTAKYHFEAWYEIAKSLDIEIDETFNEKLKGISREESLDKIL---------LSANKVDSYTKEEKLK 71
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPLAKAIVAAAEDLPIPVEDFTARLLlgkrdwleeLDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   72 VCEEKNNIYIKLINSLTYkdILPGINGLIKELKKNNVKLGIASAS--KNAPRILESLGIKDEFDCIVNPSLLERGKPYPD 149
Cdd:pfam00702  81 TVVLVELLGVIALADELK--LYPGAAEALKALKERGIKVAILTGDnpEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPE 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 489522578  150 IFIEGSKMLNLKQYDCVGIEDSCSGIKAINAAN 182
Cdd:pfam00702 159 IYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
PRK10826 PRK10826
hexitol phosphatase HxpB;
2-188 3.49e-20

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 85.00  E-value: 3.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   2 KAVLFDLDGVITDTAKYHFEAWYEIAKSL--DIEIDETFNEKL-----------------KGISREESLDKILlsaNKVD 62
Cdd:PRK10826   8 LAAIFDMDGLLIDSEPLWDRAELDVMASLgvDISRREELPDTLglridqvvdlwyarqpwNGPSRQEVVQRII---ARVI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  63 SYTKEEKlkvceeknniyiklinsltykDILPGINGLIKELKKNNVKLGIASASKNA--PRILESLGIKDEFDCIVNPSL 140
Cdd:PRK10826  85 SLIEETR---------------------PLLPGVREALALCKAQGLKIGLASASPLHmlEAVLTMFDLRDYFDALASAEK 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 489522578 141 LERGKPYPDIFIEGSKMLNLKQYDCVGIEDSCSGIKAINAANMTSIGV 188
Cdd:PRK10826 144 LPYSKPHPEVYLNCAAKLGVDPLTCVALEDSFNGMIAAKAARMRSIVV 191
 
Name Accession Description Interval E-value
bPGM TIGR01990
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 3-189 8.67e-85

beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which catalyzes the interconverison of beta-D-glucose-1-phosphate and beta-D-glucose-6-phosphate. The 6-phosphate is capable of non-enzymatic anomerization (alpha <-> beta) while the 1-phosphate is not. A separate enzyme is responsible for the isomerization of the alpha anomers. Beta-D-glucose-1-phosphate results from the phosphorylysis of maltose (2.4.1.8), trehalose (2.4.1.64) or trehalose-6-phosphate (2.4.1.216). Alternatively, these reactions can be run in the synthetic direction to create the disaccharides. All sequenced genomes which contain a member of this family also appear to contain at least one putative maltose or trehalose phosphorylase. Three species, Lactococcus, Enterococcus and Neisseria appear to contain a pair of paralogous beta-PGM's. Beta-phosphoglucomutase is a member of the haloacid dehalogenase superfamily of hydrolase enzymes. These enzymes are characterized by a series of three catalytic motifs positioned within an alpha-beta (Rossman) fold. beta-PGM contains an inserted alpha helical domain in between the first and second conserved motifs and thus is a member of subfamily IA of the superfamily. The third catalytic motif comes in three variants, the third of which, containing a conserved DD or ED, is the only one found here as well as in several other related enzymes (TIGR01509). The enzyme from L. lactis has been extensively characterized including a remarkable crystal structure which traps the pentacoordinate transition state. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 213672 [Multi-domain]  Cd Length: 185  Bit Score: 249.53  E-value: 8.67e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578    3 AVLFDLDGVITDTAKYHFEAWYEIAKSLDIEIDETFNEKLKGISREESLDKILLSANKvdSYTKEEKLKVCEEKNNIYIK 82
Cdd:TIGR01990   1 AVIFDLDGVITDTAEYHYLAWKHLADELGIPFDEEFNESLKGVSREESLERILDLGGK--KYSEEEKEELAERKNDYYVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   83 LINSLTYKDILPGINGLIKELKKNNVKLGIASASKNAPRILESLGIKDEFDCIVNPSLLERGKPYPDIFIEGSKMLNLKQ 162
Cdd:TIGR01990  79 LLKELTPADVLPGIKSLLADLKKNNIKIALASASKNAPTILEKLELIDYFDAIVDPAELKKGKPDPEIFLAAAEGLGVSP 158

                         170       180
                  ....*....|....*....|....*..
gi 489522578  163 YDCVGIEDSCSGIKAINAANMTSIGVG 189
Cdd:TIGR01990 159 SECIGIEDAQAGIEAIKAAGMFAVGVG 185
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
1-203 8.68e-64

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 196.97  E-value: 8.68e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   1 MKAVLFDLDGVITDTAKYHFEAWYEIAKSLDIEIDETFNEKLKGISREESLDKILLSANKvdSYTKEEklkVCEEKNNIY 80
Cdd:COG0637    2 IKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGL--DLPEEE---LAARKEELY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  81 IKLInSLTYKDILPGINGLIKELKKNNVKLGIASASK--NAPRILESLGIKDEFDCIVNPSLLERGKPYPDIFIEGSKML 158
Cdd:COG0637   77 RELL-AEEGLPLIPGVVELLEALKEAGIKIAVATSSPreNAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERL 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489522578 159 NLKQYDCVGIEDSCSGIKAINAANMTSIGVG----KKEVLGKCDHIVED 203
Cdd:COG0637  156 GVDPEECVVFEDSPAGIRAAKAAGMRVVGVPdggtAEEELAGADLVVDD 204
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 2-188 1.64e-62

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: 192.94  E-value: 1.64e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578    2 KAVLFDLDGVITDTAKYHFEAWYEIAKSLDIEIDETFNEKLKGISREESLDKILLSANkvDSYTKEEKLKVCEEKNNIYI 81
Cdd:TIGR02009   2 KAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRG--DGLSLEEIHQLAERKNELYR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   82 KLINsLTYKDILPGINGLIKELKKNNVKLGIASASKNAPRILESLGIKDEFDCIVNPSLLERGKPYPDIFIEGSKMLNLK 161
Cdd:TIGR02009  80 ELLR-LTGVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKLGLRDYFDAIVDASEVKNGKPHPETFLLAAELLGVP 158

                         170       180
                  ....*....|....*....|....*..
gi 489522578  162 QYDCVGIEDSCSGIKAINAANMTSIGV 188
Cdd:TIGR02009 159 PNECIVFEDALAGVQAARAAGMFAVAV 185
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 3-214 2.79e-62

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: 191.74  E-value: 2.79e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   3 AVLFDLDGVITDTAKYHFEAWYEIAksldieidetfneklkgisreesldkillsankvdsytkeEKLKVCEEKNNIYIK 82
Cdd:cd02598    1 GVIFDLDGVITDTAEYHYRAWKKLA----------------------------------------DKEELAARKNRIYVE 40

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  83 LINSLTYKDILPGINGLIKELKKNNVKLGIASASKNAPRILESLGIKDEFDCIVNPSLLERGKPYPDIFIEGSKMLNLKQ 162
Cdd:cd02598   41 LIEELTPVDVLPGIASLLVDLKAKGIKIALASASKNAPKILEKLGLAEYFDAIVDGAVLAKGKPDPDIFLAAAEGLGLNP 120

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489522578 163 YDCVGIEDSCSGIKAINAANMTSIGVGKKEVLGKCDHIVEDT-SLLNYNTLLQ 214
Cdd:cd02598  121 KDCIGVEDAQAGIRAIKAAGFLVVGVGREEDLLGADIVVPDTtADLTIEELLE 173
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 3-188 9.41e-31

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: 110.40  E-value: 9.41e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   3 AVLFDLDGVITDTAKYHFEAWYEIAKsldieidetfneklkgisreesldkillsankvdsytkeeklkvceeKNNIYIK 82
Cdd:cd07505    1 AVIFDMDGVLIDTEPLHRQAWQLLER-----------------------------------------------KNALLLE 33

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  83 LINSLTYKdILPGINGLIKELKKNNVKLGIASAS--KNAPRILESLGIKDE-FDCIVNPSLLERGKPYPDIFIEGSKMLN 159
Cdd:cd07505   34 LIASEGLK-LKPGVVELLDALKAAGIPVAVATSSsrRNVELLLLELGLLRGyFDVIVSGDDVERGKPAPDIYLLAAERLG 112

                        170       180
                 ....*....|....*....|....*....
gi 489522578 160 LKQYDCVGIEDSCSGIKAINAANMTSIGV 188
Cdd:cd07505  113 VDPERCLVFEDSLAGIEAAKAAGMTVVAV 141
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 3-203 3.79e-28

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: 104.26  E-value: 3.79e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   3 AVLFDLDGVITDTAKYHFEAWYEIAKsldieidetfneklkgisreesldkillsankvdsytkeeklkvcEEKNNIYIK 82
Cdd:cd16423    1 AVIFDFDGVIVDTEPLWYEAWQELLN---------------------------------------------ERRNELIKR 35

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  83 LINSLTYKDILPGINGLIKELKKNNVKLGIASAS--KNAPRILESLGIKDEFDCIVNPSLLERGKPYPDIFIEGSKMLNL 160
Cdd:cd16423   36 QFSEKTDLPPIEGVKELLEFLKEKGIKLAVASSSprRWIEPHLERLGLLDYFEVIVTGDDVEKSKPDPDLYLEAAERLGV 115

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 489522578 161 KQYDCVGIEDSCSGIKAINAANMTSIGV----GKKEVLGKCDHIVED 203
Cdd:cd16423  116 NPEECVVIEDSRNGVLAAKAAGMKCVGVpnpvTGSQDFSKADLVLSS 162
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 3-188 1.39e-26

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: 100.57  E-value: 1.39e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578    3 AVLFDLDGVITDTAkyHFEAWYEIAKSLDIEIDETFNEKLkgISREESLDKIllsanKVDSYTKEEKLKVCEEKNNIYIK 82
Cdd:TIGR01509   1 AILFDLDGVLVDTE--FAIAKLINREELGLVPDELGVSAV--GRLELALRRF-----KAQYGRTISPEDAQLLYKQLFYE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   83 LINSLTYKDILPGINGLIKELKKNNVKLGIASaskNAPRI----LESLGIKDEFDCIVNPSLLERGKPYPDIFIEGSKML 158
Cdd:TIGR01509  72 QIEEEAKLKPLPGVRALLEALRARGKKLALLT---NSPRAhklvLALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKAL 148

                         170       180       190
                  ....*....|....*....|....*....|
gi 489522578  159 NLKQYDCVGIEDSCSGIKAINAANMTSIGV 188
Cdd:TIGR01509 149 GLEPSECVFVDDSPAGIEAAKAAGMHTVGV 178
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
1-203 6.54e-25

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 97.31  E-value: 6.54e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   1 MKAVLFDLDGVITDTAKYHFEAWYEIAKSLDIE-IDETFNEKLKGISREESLDKILlsaNKVDSYTKEEKLKVCEEknnI 79
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPpLDLEELRALIGLGLRELLRRLL---GEDPDEELEELLARFRE---L 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  80 YIKLINSLTykDILPGINGLIKELKKNNVKLGIAS--ASKNAPRILESLGIKDEFDCIVNPSLLERGKPYPDIFIEGSKM 157
Cdd:COG0546   75 YEEELLDET--RLFPGVRELLEALKARGIKLAVVTnkPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALER 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489522578 158 LNLKQYDCVGIEDSCSGIKAINAANMTSIGV----GKKEVLGKC--DHIVED 203
Cdd:COG0546  153 LGLDPEEVLMVGDSPHDIEAARAAGVPFIGVtwgyGSAEELEAAgaDYVIDS 204
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 1-182 1.98e-24

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: 95.35  E-value: 1.98e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578    1 MKAVLFDLDGVITDTAKYHFEAWYEIAKSLDIEIDETFNEKLKGISREESLDKIL---------LSANKVDSYTKEEKLK 71
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPLAKAIVAAAEDLPIPVEDFTARLLlgkrdwleeLDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   72 VCEEKNNIYIKLINSLTYkdILPGINGLIKELKKNNVKLGIASAS--KNAPRILESLGIKDEFDCIVNPSLLERGKPYPD 149
Cdd:pfam00702  81 TVVLVELLGVIALADELK--LYPGAAEALKALKERGIKVAILTGDnpEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPE 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 489522578  150 IFIEGSKMLNLKQYDCVGIEDSCSGIKAINAAN 182
Cdd:pfam00702 159 IYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
4-188 1.33e-21

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 87.64  E-value: 1.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578    4 VLFDLDGVITDTAKYHFEAWYEIAKSLDIEI--DETFNeKLKGISREESLDKILlsankvDSYTKEEKLKVceeknniYI 81
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYGElsEEEIL-KFIGLPLREIFRYLG------VSEDEEEKIEF-------YL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   82 KLINSLTYKDIL---PGINGLIKELKKNNVKLGIASA--SKNAPRILESLGIKDEFDCIVNPSLLERGKPYPDIFIEGSK 156
Cdd:pfam13419  67 RKYNEELHDKLVkpyPGIKELLEELKEQGYKLGIVTSksRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALE 146

                         170       180       190
                  ....*....|....*....|....*....|..
gi 489522578  157 MLNLKQYDCVGIEDSCSGIKAINAANMTSIGV 188
Cdd:pfam13419 147 QLGLKPEEVIYVGDSPRDIEAAKNAGIKVIAV 178
PRK10826 PRK10826
hexitol phosphatase HxpB;
2-188 3.49e-20

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 85.00  E-value: 3.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   2 KAVLFDLDGVITDTAKYHFEAWYEIAKSL--DIEIDETFNEKL-----------------KGISREESLDKILlsaNKVD 62
Cdd:PRK10826   8 LAAIFDMDGLLIDSEPLWDRAELDVMASLgvDISRREELPDTLglridqvvdlwyarqpwNGPSRQEVVQRII---ARVI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  63 SYTKEEKlkvceeknniyiklinsltykDILPGINGLIKELKKNNVKLGIASASKNA--PRILESLGIKDEFDCIVNPSL 140
Cdd:PRK10826  85 SLIEETR---------------------PLLPGVREALALCKAQGLKIGLASASPLHmlEAVLTMFDLRDYFDALASAEK 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 489522578 141 LERGKPYPDIFIEGSKMLNLKQYDCVGIEDSCSGIKAINAANMTSIGV 188
Cdd:PRK10826 144 LPYSKPHPEVYLNCAAKLGVDPLTCVALEDSFNGMIAAKAARMRSIVV 191
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 3-186 2.02e-19

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: 82.43  E-value: 2.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   3 AVLFDLDGVITDTAKYHFEAWYEIA---KSLDIEIDETFNEKLKGISreESLDKILLSANKVDSYTKEEKLK------VC 73
Cdd:cd07528    1 ALIFDVDGTLAETEELHRRAFNNAFfaeRGLDWYWDRELYGELLRVG--GGKERIAAYFEKVGWPESAPKDLkeliadLH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  74 EEKNNIYIKLINSLTYkDILPGINGLIKELKKNNVKLGIASAS--KNAPRILES-LGI--KDEFDCIVNPSLLERGKPYP 148
Cdd:cd07528   79 KAKTERYAELIAAGLL-PLRPGVARLIDEAKAAGVRLAIATTTspANVDALLSAlLGPerRAIFDAIAAGDDVAEKKPDP 157

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 489522578 149 DIFIEGSKMLNLKQYDCVGIEDSCSGIKAINAANMTSI 186
Cdd:cd07528  158 DIYLLALERLGVSPSDCLAIEDSAIGLQAAKAAGLPCI 195
PLN02940 PLN02940
riboflavin kinase
 93-188 4.40e-18

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 81.42  E-value: 4.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  93 LPGINGLIKELKKNNVKLGIASASKNA---PRILESLGIKDEFDCIVNPSLLERGKPYPDIFIEGSKMLNLKQYDCVGIE 169
Cdd:PLN02940  95 LPGANRLIKHLKSHGVPMALASNSPRAnieAKISCHQGWKESFSVIVGGDEVEKGKPSPDIFLEAAKRLNVEPSNCLVIE 174

                         90
                 ....*....|....*....
gi 489522578 170 DSCSGIKAINAANMTSIGV 188
Cdd:PLN02940 175 DSLPGVMAGKAAGMEVIAV 193
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 1-188 2.48e-17

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 77.96  E-value: 2.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   1 MKAVLFDLDGVITDTAKYHFEAWYEIAKSLD----IEIDETF-NEKLKGISREESldKILLSANKVdsytkEEKLKVCEE 75
Cdd:PLN02770  22 LEAVLFDVDGTLCDSDPLHYYAFREMLQEINfnggVPITEEFfVENIAGKHNEDI--ALGLFPDDL-----ERGLKFTDD 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  76 KNNIYIKLInsltyKDILPGINGLIKeLKKNNVKLGIASAS-KNAPR-----ILESLGIKDEFDCIVNPSLLERGKPYPD 149
Cdd:PLN02770  95 KEALFRKLA-----SEQLKPLNGLYK-LKKWIEDRGLKRAAvTNAPRenaelMISLLGLSDFFQAVIIGSECEHAKPHPD 168

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 489522578 150 IFIEGSKMLNLKQYDCVGIEDSCSGIKAINAANMTSIGV 188
Cdd:PLN02770 169 PYLKALEVLKVSKDHTFVFEDSVSGIKAGVAAGMPVVGL 207
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 3-205 6.18e-17

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: 75.84  E-value: 6.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   3 AVLFDLDGVITDTAKYHFEAWYEIAKSLDIEIDETFNEkLKGISREESLDKILLSANKVDSYTKEEKLkvceeknniyik 82
Cdd:cd07527    1 ALLFDMDGTLVDSTPAVERAWHKWAKEHGVDPEEVLKV-SHGRRAIDVIRKLAPDDADIELVLALETE------------ 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  83 LINSLTYKDI-LPGINGLIKELKKNNVKLGIASASKN--APRILESLGIKdefdcivNPSLL------ERGKPYPDIFIE 153
Cdd:cd07527   68 EPESYPEGVIaIPGAVDLLASLPAAGDRWAIVTSGTRalAEARLEAAGLP-------HPEVLvtaddvKNGKPDPEPYLL 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489522578 154 GSKMLNLKQYDCVGIEDSCSGIKAINAANMTSIGVG---KKEVL--GKCDHIVEDTS 205
Cdd:cd07527  141 GAKLLGLDPSDCVVFEDAPAGIKAGKAAGARVVAVNtshDLEQLeaAGADLVVEDLS 197
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 2-188 2.57e-16

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: 73.92  E-value: 2.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   2 KAVLFDLDGVITDTAKYHFEAWYEIAKSLDIEIDETFNEKLKGISREESLdKILLSANKVDsYTKEEKLkvcEEKNNIYI 81
Cdd:cd07529    2 THCIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAA-RIIVDELKLP-MSLEEEF---DEQQEALA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  82 KLINSLTykDILPGINGLIKELKKNNVKLGIASASKNAPRILESLGIKDEFD------CIVNPSLLERGKPYPDIFIEGS 155
Cdd:cd07529   77 ELFMGTA--KLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSlfhhvvTGDDPEVKGRGKPAPDIFLVAA 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489522578 156 KMLNLKQYD---CVGIEDSCSGIKAINAANMTSIGV 188
Cdd:cd07529  155 KRFNEPPKDpskCLVFEDSPNGVKAAKAAGMQVVMV 190
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 1-188 9.70e-16

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 75.66  E-value: 9.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578    1 MKAVLFDLDGVITDTAKYHFEAWYEIAKSLDIEIDETFNEKLKGISREESLDKILlSANKVDSY----TKEEKLKVCEEK 76
Cdd:PLN02919   75 VSAVLFDMDGVLCNSEEPSRRAAVDVFAEMGVEVTVEDFVPFMGTGEANFLGGVA-SVKGVKGFdpdaAKKRFFEIYLEK 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   77 nniYIKLINSLTYkdilPGINGLIKELKKNNVKLGIASAsknAPRI-----LESLGI-KDEFDCIVNPSLLERGKPYPDI 150
Cdd:PLN02919  154 ---YAKPNSGIGF----PGALELITQCKNKGLKVAVASS---ADRIkvdanLAAAGLpLSMFDAIVSADAFENLKPAPDI 223

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 489522578  151 FIEGSKMLNLKQYDCVGIEDSCSGIKAINAANMTSIGV 188
Cdd:PLN02919  224 FLAAAKILGVPTSECVVIEDALAGVQAARAAGMRCIAV 261
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 1-207 1.08e-15

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: 72.75  E-value: 1.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   1 MKAVLFDLDGVITDTAKYHFEAWYEIAKSLDIEID-ETFNEKLKGISRE--ESLDKILLSANKVDSYTKEE-KLKVCEEK 76
Cdd:COG1011    1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEaEELAEAYRAIEYAlwRRYERGEITFAELLRRLLEElGLDLAEEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  77 NNIYIKLINSLTykDILPGINGLIKELKKNNVKLGIAS--ASKNAPRILESLGIKDEFDCIVNPSLLERGKPYPDIFIEG 154
Cdd:COG1011   81 AEAFLAALPELV--EPYPDALELLEALKARGYRLALLTngSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIFELA 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489522578 155 SKMLNLKQYDCVGIEDSCSG-IKAINAANMTSI----GVGKKEVLGKCDHIVEDTSLL 207
Cdd:COG1011  159 LERLGVPPEEALFVGDSPETdVAGARAAGMRTVwvnrSGEPAPAEPRPDYVISDLAEL 216
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 1-186 3.81e-14

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 69.74  E-value: 3.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   1 MKAVLFDLDGVITDTAK-YHFEAWyeiaksldieiDETFNEK-LKGISREESLDKILLS----ANKVDSYTKE------- 67
Cdd:PLN02779  40 PEALLFDCDGVLVETERdGHRVAF-----------NDAFKEFgLRPVEWDVELYDELLNigggKERMTWYFNEngwptst 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  68 -EKLKVCEEKNNiyiKLINSL------TYKDIL--------PGINGLIKELKKNNVKLGIASAS--KNAPRILES-LGIK 129
Cdd:PLN02779 109 iEKAPKDEEERK---ELVDSLhdrkteLFKELIesgalplrPGVLRLMDEALAAGIKVAVCSTSneKAVSKIVNTlLGPE 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489522578 130 --DEFDCIVNpSLLERGKPYPDIFIEGSKMLNLKQYDCVGIEDSCSGIKAINAANMTSI 186
Cdd:PLN02779 186 raQGLDVFAG-DDVPKKKPDPDIYNLAAETLGVDPSRCVVVEDSVIGLQAAKAAGMRCI 243
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 2-189 3.31e-13

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: 65.76  E-value: 3.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   2 KAVLFDLDGVITDTAKyhfeawyEIAKSLdieiDETFNEK-LKGISREESLDKI----LLSANKVDSYTKEEKLkvcEEK 76
Cdd:cd02616    2 TTILFDLDGTLIDTNE-------LIIKSF----NHTLKEYgLEGYTREEVLPFIgpplRETFEKIDPDKLEDMV---EEF 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  77 NNIYIKLINSLT--YKDILPGinglIKELKKNNVKLGIASaSKN---APRILESLGIKDEFDCIVNPSLLERGKPYPDIF 151
Cdd:cd02616   68 RKYYREHNDDLTkeYPGVYET----LARLKSQGIKLGVVT-TKLretALKGLKLLGLDKYFDVIVGGDDVTHHKPDPEPV 142

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 489522578 152 IEGSKMLNLKQYDCVGIEDSCSGIKAINAANMTSIGVG 189
Cdd:cd02616  143 LKALELLGAEPEEALMVGDSPHDILAGKNAGVKTVGVT 180
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
3-188 4.20e-11

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 59.70  E-value: 4.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   3 AVLFDLDGVITDTAKYHFEAWYEIAKSLDIEIDETFNEKLKG----------ISREES-LDKILLSANKVDsytkeeklk 71
Cdd:PRK10725   7 GLIFDMDGTILDTEPTHRKAWREVLGRYGLQFDEQAMVALNGsptwriaqaiIELNQAdLDPHALAREKTE--------- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  72 vceeknniyikLINSLTYKDI--LPGINgLIKELK-KNNVKLGIASASKNAPRILESLGIKDEFDCIVNPSLLERGKPYP 148
Cdd:PRK10725  78 -----------AVKSMLLDSVepLPLIE-VVKAWHgRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADDVQHHKPAP 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 489522578 149 DIFIEGSKMLNLKQYDCVGIEDSCSGIKAINAANMTSIGV 188
Cdd:PRK10725 146 DTFLRCAQLMGVQPTQCVVFEDADFGIQAARAAGMDAVDV 185
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 4-212 1.67e-10

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 59.28  E-value: 1.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   4 VLFDLDGVIT-DTAKYHFEAWYEIAKSLDIEIDETFN-EKLKGISREESLDKILLSANKVdsytkEEKLKVCEEKNNIYI 81
Cdd:PLN03243  27 VVLEWEGVIVeDDSELERKAWRALAEEEGKRPPPAFLlKRAEGMKNEQAISEVLCWSRDF-----LQMKRLAIRKEDLYE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  82 KLINSlTYKdILPGINGLIKELKKNNVKLGIASAS--KNAPRILESLGIKDEFDCIVNPSLLERGKPYPDIFIEGSKMLN 159
Cdd:PLN03243 102 YMQGG-LYR-LRPGSREFVQALKKHEIPIAVASTRprRYLERAIEAVGMEGFFSVVLAAEDVYRGKPDPEMFMYAAERLG 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489522578 160 LKQYDCVGIEDSCSGIKAINAANMTSIGV-GKKEV--LGKCDHIV---EDTSLLNYNTL 212
Cdd:PLN03243 180 FIPERCIVFGNSNSSVEAAHDGCMKCVAVaGKHPVyeLSAGDLVVrrlDDLSVVDLKNL 238
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 2-187 1.78e-08

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: 51.55  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   2 KAVLFDLDGVITDTAKYHFEAWYEIAKSLDIEIDETFNEKLKGIsreesldkillsankvdsytkeeklkvceeknniyi 81
Cdd:cd07526    1 DLVIFDCDGVLVDSEVIAARVLVEVLAELGARVLAAFEAELQPI------------------------------------ 44

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  82 klinsltykdilPGINGLIKELkknNVKLGIASASKNaPRI---LESLGIKDEFDC-IVNPSLLERGKPYPDIFIEGSKM 157
Cdd:cd07526   45 ------------PGAAAALSAL---TLPFCVASNSSR-ERLthsLGLAGLLAYFEGrIFSASDVGRGKPAPDLFLHAAAQ 108

                        170       180       190
                 ....*....|....*....|....*....|
gi 489522578 158 LNLKQYDCVGIEDSCSGIKAINAANMTSIG 187
Cdd:cd07526  109 MGVAPERCLVIEDSPTGVRAALAAGMTVFG 138
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 99-188 2.77e-08

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: 50.09  E-value: 2.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  99 LIKELKKNNVKLGIASASKNAP--RILESLGIKDEFDCIVNPSLLERGKPYPDIFIEGSKMLNLKQYDCVGIEDSCSGIK 176
Cdd:cd01427   15 LLKRLRAAGIKLAIVTNRSREAlrALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSENDIE 94

                         90
                 ....*....|..
gi 489522578 177 AINAANMTSIGV 188
Cdd:cd01427   95 AARAAGGRTVAV 106
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
94-188 6.19e-07

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 48.27  E-value: 6.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  94 PGINGLIKELKKNNVKLGIAS--ASKNAPRILESLGIKDEFDCIVNPSLLERGKPYPDIFIEGSKMLNLKQYDCVGIEDS 171
Cdd:PRK13222  96 PGVKETLAALKAAGYPLAVVTnkPTPFVAPLLEALGIADYFSVVIGGDSLPNKKPDPAPLLLACEKLGLDPEEMLFVGDS 175

                         90
                 ....*....|....*..
gi 489522578 172 CSGIKAINAANMTSIGV 188
Cdd:PRK13222 176 RNDIQAARAAGCPSVGV 192
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 2-189 8.84e-07

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 47.72  E-value: 8.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   2 KAVLFDLDGVITDTAKYhfeawyeIAKSLDieidETFNEKLKG-ISREESLDKILLSAnkVDSYTK--EEKlkvCEEKNN 78
Cdd:PRK13288   4 NTVLFDLDGTLINTNEL-------IISSFL----HTLKTYYPNqYKREDVLPFIGPSL--HDTFSKidESK---VEEMIT 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  79 IYIKlINSLTYKDIL---PGINGLIKELKKNNVKLGIAS--ASKNAPRILESLGIKDEFDCIVNPSLLERGKPYPDIFIE 153
Cdd:PRK13288  68 TYRE-FNHEHHDELVteyETVYETLKTLKKQGYKLGIVTtkMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPDPEPVLK 146

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489522578 154 GSKMLNLKQYDCVGIEDSCSGIKAINAANMTSIGVG 189
Cdd:PRK13288 147 ALELLGAKPEEALMVGDNHHDILAGKNAGTKTAGVA 182
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 94-188 1.71e-06

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: 47.23  E-value: 1.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  94 PGINGLIKELKKNNVKLGIAS--ASKNAPRILESLGIKDEFDCIVN-PSLLERgKPYPDIFIEGSKMLNLKQYDCVGIED 170
Cdd:cd16417   90 PGVKEGLAALKAQGYPLACVTnkPERFVAPLLEALGISDYFSLVLGgDSLPEK-KPDPAPLLHACEKLGIAPAQMLMVGD 168

                         90
                 ....*....|....*...
gi 489522578 171 SCSGIKAINAANMTSIGV 188
Cdd:cd16417  169 SRNDILAARAAGCPSVGL 186
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 92-186 2.91e-06

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: 44.46  E-value: 2.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  92 ILPGINGLIKELKKNnVKLGIASaskNAPRI-----LESLGIKDEFDCIVNPSLLERGKPYPDIFIEGSKMLNLKQYDCV 166
Cdd:cd04305   10 LLPGAKELLEELKKG-YKLGIIT---NGPTEvqwekLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETL 85

                         90       100
                 ....*....|....*....|.
gi 489522578 167 GIEDSC-SGIKAINAANMTSI 186
Cdd:cd04305   86 MVGDSLeSDILGAKNAGIKTV 106
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 107-201 6.26e-06

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 46.01  E-value: 6.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578 107 NVKLGIASASKNAPRILE----SLGIKDEFDCIVNPSLLERGKPYPDIFIEGSKMLNLKQYDCVGIEDSCSGIKAINAAN 182
Cdd:PLN02575 230 NYKIPMALVSTRPRKTLEnaigSIGIRGFFSVIVAAEDVYRGKPDPEMFIYAAQLLNFIPERCIVFGNSNQTVEAAHDAR 309

                         90       100
                 ....*....|....*....|..
gi 489522578 183 MTSIGVGKKEV---LGKCDHIV 201
Cdd:PLN02575 310 MKCVAVASKHPiyeLGAADLVV 331
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 1-186 9.01e-06

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: 44.64  E-value: 9.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   1 MKAVLFDLDGVITDtakYHFEAWYE-IAKSLDIEIDETFNEKLKGiSREESLDKILLSANKVDSytkeeklKVCEEKNNI 79
Cdd:cd02603    1 IRAVLFDFGGVLID---PDPAAAVArFEALTGEPSEFVLDTEGLA-GAFLELERGRITEEEFWE-------ELREELGRP 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  80 YIKLINS---LTYKDILPGINGLIKELKKNNVKLGIASaskNAPRILESLG------IKDEFDCIVNPSLLERGKPYPDI 150
Cdd:cd02603   70 LSAELFEelvLAAVDPNPEMLDLLEALRAKGYKVYLLS---NTWPDHFKFQlellprRGDLFDGVVESCRLGVRKPDPEI 146

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489522578 151 FIEGSKMLNLKQYDCVGIEDSCSGIKAINAANMTSI 186
Cdd:cd02603  147 YQLALERLGVKPEEVLFIDDREENVEAARALGIHAI 182
PLN02811 PLN02811
hydrolase
 8-188 1.47e-05

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 44.36  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   8 LDGVITDTAKYHFEAWYEIAKSLDIEIDETFNEKLKGISREESLdKILLSANKV-DSYTKEEKLkvcEEKNNIYIKLINS 86
Cdd:PLN02811   1 MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAA-RIFVEESGLsDSLSPEDFL---VEREAMLQDLFPT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  87 ltyKDILPGINGLIKELKKNNVKLGIASASKNAPRILESLGIKDEFDC---IV--NPSLLERGKPYPDIFIEGSKMLNLK 161
Cdd:PLN02811  77 ---SDLMPGAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLmhhVVtgDDPEVKQGKPAPDIFLAAARRFEDG 153

                        170       180       190
                 ....*....|....*....|....*....|
gi 489522578 162 QYD---CVGIEDSCSGIKAINAANMTSIGV 188
Cdd:PLN02811 154 PVDpgkVLVFEDAPSGVEAAKNAGMSVVMV 183
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 3-189 2.01e-05

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: 43.73  E-value: 2.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   3 AVLFDLDGVITDTAKyhfeawyEIAKSL-----DIEIDETFNEKLK---GISREESLDKILLSANK-----VD---SYTK 66
Cdd:cd04302    1 TILFDLDGTLTDSAE-------GITASVqyaleELGIPVPDESELRrfiGPPLEDSFRELLPFDEEeaqraVDayrEYYK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  67 EEKLKVceekNNIYiklinsltykdilPGINGLIKELKKNNVKLGIASaSKNAP---RILESLGIKDEFDCIVNPSLLER 143
Cdd:cd04302   74 EKGLFE----NEVY-------------PGIPELLEKLKAAGYRLYVAT-SKPEVfarRILEHFGLDEYFDGIAGASLDGS 135

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 489522578 144 GKPYPDIFIEGSKMLNLKQYDCVGIEDSCSGIKAINAANMTSIGVG 189
Cdd:cd04302  136 RVHKADVIRYALDTLGIAPEQAVMIGDRKHDIIGARANGIDSIGVL 181
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 3-205 2.30e-05

phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase PGP/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: 319799 [Multi-domain]  Cd Length: 201  Bit Score: 43.50  E-value: 2.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   3 AVLFDLDGVITDTAKYHFEAWYEIAKSLDIE-IDETFNEKLKGISREESLDKILLSANKVDSYTKEEKLKVCEEKNNIYi 81
Cdd:cd04303    1 LIIFDFDGTLADSFPWFLSILNQLAARHGFKtVDEEEIEQLRQLSSREILKQLGVPLWKLPLIAKDFRRLMAEAAPELA- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  82 klinsltykdILPGINGLIKELKKNNVKLGIASAS--KNAPRILESLGIKDEFDCIVNPSLLerGKPYPDIFIEGSKMLN 159
Cdd:cd04303   80 ----------LFPGVEDMLRALHARGVRLAVVSSNseENIRRVLGPEELISLFAVIEGSSLF--GKAKKIRRVLRRTKIT 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489522578 160 LKQYDCVGieDSCSGIKAINAANMTSIGVG----KKEVLGKC--DHIVEDTS 205
Cdd:cd04303  148 AAQVIYVG--DETRDIEAARKVGLAFAAVSwgyaKPEVLKALapDHMLEDPE 197
PRK11587 PRK11587
putative phosphatase; Provisional
 2-188 7.05e-05

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 42.29  E-value: 7.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   2 KAVLFDLDGVITDTAKYHFEAWYEIAKSLDIEIDETFNeKLKGISREESLDKILLSANkvdsytkEEKLkvceEKNNIYI 81
Cdd:PRK11587   4 KGFLFDLDGTLVDSLPAVERAWSNWADRHGIAPDEVLN-FIHGKQAITSLRHFMAGAS-------EAEI----QAEFTRL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  82 KLINSLTYKDI--LPGINGLIKELKKNNVKLGI--------ASASKNAPRILESlgikDEFdciVNPSLLERGKPYPDIF 151
Cdd:PRK11587  72 EQIEATDTEGItaLPGAIALLNHLNKLGIPWAIvtsgsvpvASARHKAAGLPAP----EVF---VTAERVKRGKPEPDAY 144

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 489522578 152 IEGSKMLNLKQYDCVGIEDSCSGIKAINAANMTSIGV 188
Cdd:PRK11587 145 LLGAQLLGLAPQECVVVEDAPAGVLSGLAAGCHVIAV 181
HAD_PHN cd02586
Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; ...
 82-188 1.67e-04

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: 41.52  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  82 KLINSL-TYKDILPGINGLIKELKKNNVKLG---------IASASKNAprilESLGIKDEFdcIVNPSLLERGKPYPDIF 151
Cdd:cd02586   88 ILIASLaEYSSPIPGVLEVIAKLRARGIKIGsttgytremMDIVLPEA----AAQGYRPDS--LVTPDDVPAGRPYPWMC 161

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489522578 152 IEgsKMLNLKQYD---CVGIEDSCSGIKAINAANMTSIGV 188
Cdd:cd02586  162 YK--NAIELGVYDvaaVVKVGDTVPDIKEGLNAGMWTVGV 199
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-130 2.86e-04

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


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 40.59  E-value: 2.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578   1 MKAVLFDLDGVITDT------AKYHFEAWYEIAKSLDIEIDETFNEKLKG-ISREESLDKIL-----LSANKVDSYTKEe 68
Cdd:COG0560    3 MRLAVFDLDGTLIAGesidelARFLGRRGLVDRREVLEEVAAITERAMAGeLDFEESLRFRVallagLPEEELEELAER- 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489522578  69 klkVCEEKNNIYiklinsltykdilPGINGLIKELKKNNVKLGIASASkNAP---RILESLGIKD 130
Cdd:COG0560   82 ---LFEEVPRLY-------------PGARELIAEHRAAGHKVAIVSGG-FTFfvePIAERLGIDH 129
HAD_MDP-1_like cd07501
eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to ...
 94-139 3.13e-03

eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to Bacillus cereus phosphonoacetaldehyde hydrolase and Streptomyces FkbH; This family includes eukaryotic magnesium-dependent phosphatase-1 (MDP-1) which is most likely a phosphotyrosine phosphatase catalyzing the dephosphorylation of tyrosine-phosphorylated proteins, Bacillus cereus phosphonoacetaldehyde hydrolase (phosphonatase)which catalyzes the hydrolysis of phosphonoacetaldehyde to acetaldehyde and phosphate using Mg(II) as cofactor, and sequences annotated as FkbH including BafAIV an FkbH-like protein from Streptomyces griseus encoded in ORF12 of the bafilomycin synthesis gene cluster. 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: 319804 [Multi-domain]  Cd Length: 129  Bit Score: 36.56  E-value: 3.13e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 489522578  94 PGINGLIKELKKNNVKLGIAS---ASKNAPRILESLGIKDEFDCI-VNPS 139
Cdd:cd07501   37 PDAQEILKELKERGILLAVASrnnEFDHANEVLEKLDLKELFDAFeIYPG 86
PRK13478 PRK13478
phosphonoacetaldehyde hydrolase; Provisional
 82-188 7.64e-03

phosphonoacetaldehyde hydrolase; Provisional


Pssm-ID: 184075 [Multi-domain]  Cd Length: 267  Bit Score: 36.38  E-value: 7.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522578  82 KLINSL-TYKDILPGINGLIKELKKNNVKLG---------IASASKNAprilESLGIKDefDCIVNPSLLERGKPYPD-I 150
Cdd:PRK13478  91 LQIAKLaDYATPIPGVLEVIAALRARGIKIGsttgytremMDVVVPLA----AAQGYRP--DHVVTTDDVPAGRPYPWmA 164

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489522578 151 FiegSKMLNLKQYD---CVGIEDSCSGIKAINAANMTSIGV 188
Cdd:PRK13478 165 L---KNAIELGVYDvaaCVKVDDTVPGIEEGLNAGMWTVGV 202
 
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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