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Conserved domains on  [gi|506275212|ref|WP_015794987|]
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HAD family phosphatase [Catenulispora acidiphila]

Protein Classification

HAD family hydrolase( domain architecture ID 11428160)

haloacid dehalogenase (HAD) family hydrolase uses a nucleophilic aspartate in the phosphoryl transfer reaction; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
15-247 1.36e-62

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


:

Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 195.04  E-value: 1.36e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  15 RIRACLFDLDGVLTETAKVHAAAWKQMFDAYLksrpgpfVPFDPvaDYDRYVDGKTRSDGTRSFLASRNINLPDgspddp 94
Cdd:COG0637    1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELG-------IDLTE--EEYRRLMGRSREDILRYLLEEYGLDLPE------ 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  95 pgtetiNGLGNAKNEIVLKLLDTQGVHVYEGSVRFLKAVRAAGLHRAVVSSS--ANCANVLKAAGIDDMFEVRIDGVTIA 172
Cdd:COG0637   66 ------EELAARKEELYRELLAEEGLPLIPGVVELLEALKEAGIKIAVATSSprENAEAVLEAAGLLDYFDVIVTGDDVA 139

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506275212 173 KenlpGKPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGGFgFVVGVDRVGQADAlRSSGADTVVTDLADL 247
Cdd:COG0637  140 R----GKPDPDIYLLAAERLGVDPEECVVFEDSPAGIRAAKAAGM-RVVGVPDGGTAEE-ELAGADLVVDDLAEL 208
 
Name Accession Description Interval E-value
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
15-247 1.36e-62

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 195.04  E-value: 1.36e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  15 RIRACLFDLDGVLTETAKVHAAAWKQMFDAYLksrpgpfVPFDPvaDYDRYVDGKTRSDGTRSFLASRNINLPDgspddp 94
Cdd:COG0637    1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELG-------IDLTE--EEYRRLMGRSREDILRYLLEEYGLDLPE------ 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  95 pgtetiNGLGNAKNEIVLKLLDTQGVHVYEGSVRFLKAVRAAGLHRAVVSSS--ANCANVLKAAGIDDMFEVRIDGVTIA 172
Cdd:COG0637   66 ------EELAARKEELYRELLAEEGLPLIPGVVELLEALKEAGIKIAVATSSprENAEAVLEAAGLLDYFDVIVTGDDVA 139

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506275212 173 KenlpGKPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGGFgFVVGVDRVGQADAlRSSGADTVVTDLADL 247
Cdd:COG0637  140 R----GKPDPDIYLLAAERLGVDPEECVVFEDSPAGIRAAKAAGM-RVVGVPDGGTAEE-ELAGADLVVDDLAEL 208
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 16-223 8.63e-60

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: 187.16  E-value: 8.63e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212   16 IRACLFDLDGVLTETAKVHAAAWKQMFDAYLksrpgpfVPFDpvADYDRYVDGKTRSDGTRSFLASRNINLPDgspddpp 95
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYG-------ISFD--KQYNESLKGLSREDILRAILKLRGDGLSL------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212   96 gtETINGLGNAKNEIVLKLLDTQGVHVYEGSVRFLKAVRAAGLHRAVVSSSANCANVLKAAGIDDMFEVRIDGVTIAKen 175
Cdd:TIGR02009  65 --EEIHQLAERKNELYRELLRLTGVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKLGLRDYFDAIVDASEVKN-- 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 506275212  176 lpGKPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGGFgFVVGV 223
Cdd:TIGR02009 141 --GKPHPETFLLAAELLGVPPNECIVFEDALAGVQAARAAGM-FAVAV 185
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 18-252 2.67e-39

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: 134.34  E-value: 2.67e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  18 ACLFDLDGVLTETAKVHAAAWKQMFDaylksrpgpfvpfdpvadydryvdgktrsdgtRSFLASRninlpdgspddppgt 97
Cdd:cd02598    1 GVIFDLDGVITDTAEYHYRAWKKLAD--------------------------------KEELAAR--------------- 33

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  98 etinglgnaKNEIVLKLLDTQ-GVHVYEGSVRFLKAVRAAGLHRAVVSSSANCANVLKAAGIDDMFEVRIDGVTIAKenl 176
Cdd:cd02598   34 ---------KNRIYVELIEELtPVDVLPGIASLLVDLKAKGIKIALASASKNAPKILEKLGLAEYFDAIVDGAVLAK--- 101

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506275212 177 pGKPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGGFgFVVGVDRvgqadALRSSGADTVVTDLADLLKQED 252
Cdd:cd02598  102 -GKPDPDIFLAAAEGLGLNPKDCIGVEDAQAGIRAIKAAGF-LVVGVGR-----EEDLLGADIVVPDTTADLTIEE 170
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 16-216 1.06e-21

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: 89.18  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212   16 IRACLFDLDGVLTETAKVHAAAWKQMFDAYLKSRPGPFVPFDPVADYDRYvdGKTRSDGTRSFLASRNINLPDGSPDDPP 95
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPLAKAIVAAAEDLPIPVEDF--TARLLLGKRDWLEELDILRGLVETLEAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212   96 GTETINGlgnaknEIVLKLLDTQGVHVYEGSVRFLKAVRAAGLHRAVVSSS--ANCANVLKAAGIDDMFEVRIDGVTIAK 173
Cdd:pfam00702  79 GLTVVLV------ELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDnpEAAEALLRLLGLDDYFDVVISGDDVGV 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 506275212  174 enlpGKPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGG 216
Cdd:pfam00702 153 ----GKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
PLN02940 PLN02940
riboflavin kinase
 125-247 1.51e-13

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 69.48  E-value: 1.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212 125 GSVRFLKAVRAAGLHRAVVSSS--ANC-ANVLKAAGIDDMFEVRIDGVTIAKenlpGKPAPDTYLAAAKKLGIDPDQAAV 201
Cdd:PLN02940  97 GANRLIKHLKSHGVPMALASNSprANIeAKISCHQGWKESFSVIVGGDEVEK----GKPSPDIFLEAAKRLNVEPSNCLV 172

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 506275212 202 FEDALAGVEAGRSGGFGfVVGVDRVGQADALRSSgADTVVTDLADL 247
Cdd:PLN02940 173 IEDSLPGVMAGKAAGME-VIAVPSIPKQTHLYSS-ADEVINSLLDL 216
 
Name Accession Description Interval E-value
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
15-247 1.36e-62

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 195.04  E-value: 1.36e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  15 RIRACLFDLDGVLTETAKVHAAAWKQMFDAYLksrpgpfVPFDPvaDYDRYVDGKTRSDGTRSFLASRNINLPDgspddp 94
Cdd:COG0637    1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELG-------IDLTE--EEYRRLMGRSREDILRYLLEEYGLDLPE------ 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  95 pgtetiNGLGNAKNEIVLKLLDTQGVHVYEGSVRFLKAVRAAGLHRAVVSSS--ANCANVLKAAGIDDMFEVRIDGVTIA 172
Cdd:COG0637   66 ------EELAARKEELYRELLAEEGLPLIPGVVELLEALKEAGIKIAVATSSprENAEAVLEAAGLLDYFDVIVTGDDVA 139

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506275212 173 KenlpGKPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGGFgFVVGVDRVGQADAlRSSGADTVVTDLADL 247
Cdd:COG0637  140 R----GKPDPDIYLLAAERLGVDPEECVVFEDSPAGIRAAKAAGM-RVVGVPDGGTAEE-ELAGADLVVDDLAEL 208
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 16-223 8.63e-60

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: 187.16  E-value: 8.63e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212   16 IRACLFDLDGVLTETAKVHAAAWKQMFDAYLksrpgpfVPFDpvADYDRYVDGKTRSDGTRSFLASRNINLPDgspddpp 95
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYG-------ISFD--KQYNESLKGLSREDILRAILKLRGDGLSL------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212   96 gtETINGLGNAKNEIVLKLLDTQGVHVYEGSVRFLKAVRAAGLHRAVVSSSANCANVLKAAGIDDMFEVRIDGVTIAKen 175
Cdd:TIGR02009  65 --EEIHQLAERKNELYRELLRLTGVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKLGLRDYFDAIVDASEVKN-- 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 506275212  176 lpGKPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGGFgFVVGV 223
Cdd:TIGR02009 141 --GKPHPETFLLAAELLGVPPNECIVFEDALAGVQAARAAGM-FAVAV 185
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 18-252 2.67e-39

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: 134.34  E-value: 2.67e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  18 ACLFDLDGVLTETAKVHAAAWKQMFDaylksrpgpfvpfdpvadydryvdgktrsdgtRSFLASRninlpdgspddppgt 97
Cdd:cd02598    1 GVIFDLDGVITDTAEYHYRAWKKLAD--------------------------------KEELAAR--------------- 33

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  98 etinglgnaKNEIVLKLLDTQ-GVHVYEGSVRFLKAVRAAGLHRAVVSSSANCANVLKAAGIDDMFEVRIDGVTIAKenl 176
Cdd:cd02598   34 ---------KNRIYVELIEELtPVDVLPGIASLLVDLKAKGIKIALASASKNAPKILEKLGLAEYFDAIVDGAVLAK--- 101

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506275212 177 pGKPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGGFgFVVGVDRvgqadALRSSGADTVVTDLADLLKQED 252
Cdd:cd02598  102 -GKPDPDIFLAAAEGLGLNPKDCIGVEDAQAGIRAIKAAGF-LVVGVGR-----EEDLLGADIVVPDTTADLTIEE 170
bPGM TIGR01990
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 18-223 4.91e-32

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: 115.87  E-value: 4.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212   18 ACLFDLDGVLTETAKVHAAAWKQMFDAYlksrpgpFVPFDpvADYDRYVDGKTRSDGTRSFL--ASRNINlpdgspddpp 95
Cdd:TIGR01990   1 AVIFDLDGVITDTAEYHYLAWKHLADEL-------GIPFD--EEFNESLKGVSREESLERILdlGGKKYS---------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212   96 gTETINGLGNAKNEIVLKLL-DTQGVHVYEGSVRFLKAVRAAGLHRAVVSSSANCANVLKAAGIDDMFEVRIDGVTIAKe 174
Cdd:TIGR01990  62 -EEEKEELAERKNDYYVELLkELTPADVLPGIKSLLADLKKNNIKIALASASKNAPTILEKLELIDYFDAIVDPAELKK- 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 506275212  175 nlpGKPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGGFgFVVGV 223
Cdd:TIGR01990 140 ---GKPDPEIFLAAAEGLGVSPSECIGIEDAQAGIEAIKAAGM-FAVGV 184
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 18-224 6.12e-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: 111.94  E-value: 6.12e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  18 ACLFDLDGVLTETAKVHAAAWKqmfdaylksrpgpfvpfdpvadydryvdgktrsdgtrsflasrninlpdgspddppgt 97
Cdd:cd07505    1 AVIFDMDGVLIDTEPLHRQAWQ---------------------------------------------------------- 22

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  98 etingLGNAKNEIVLKLLDTQGVHVYEGSVRFLKAVRAAGLHRAVVSSSAnCANVLKAAGIDDMFEVRIDGVTIAKENLP 177
Cdd:cd07505   23 -----LLERKNALLLELIASEGLKLKPGVVELLDALKAAGIPVAVATSSS-RRNVELLLLELGLLRGYFDVIVSGDDVER 96

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 506275212 178 GKPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGGFgFVVGVD 224
Cdd:cd07505   97 GKPAPDIYLLAAERLGVDPERCLVFEDSLAGIEAAKAAGM-TVVAVP 142
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 18-223 5.80e-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: 99.80  E-value: 5.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212   18 ACLFDLDGVLTETAKVHAAaWKQMFDAylksrpgpfvPFDPVADYDRYVDgktrsdgtRSFLASRNINLPDGSPDDPpgt 97
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAIAK-LINREEL----------GLVPDELGVSAVG--------RLELALRRFKAQYGRTISP--- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212   98 ETINGLgnAKNEIVLKLLDTQGVHVYEGSVRFLKAVRAAGLHRAVVSSSANCAN-VLKAAGIDDMFEVRIDGVTIAKenl 176
Cdd:TIGR01509  59 EDAQLL--YKQLFYEQIEEEAKLKPLPGVRALLEALRARGKKLALLTNSPRAHKlVLALLGLRDLFDVVIDSSDVGL--- 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 506275212  177 pGKPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGGFGfVVGV 223
Cdd:TIGR01509 134 -GKPDPDIYLQALKALGLEPSECVFVDDSPAGIEAAKAAGMH-TVGV 178
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 18-247 5.94e-25

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: 98.18  E-value: 5.94e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  18 ACLFDLDGVLTETAKVHAAAWKQMFDAYlksrpgpfvPFDPVADYDRyVDGKTRSDGTRSFLAsrninlpdgspddppgt 97
Cdd:cd07527    1 ALLFDMDGTLVDSTPAVERAWHKWAKEH---------GVDPEEVLKV-SHGRRAIDVIRKLAP----------------- 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  98 etinglGNAKNEIVLKLL------DTQGVHVYEGSVRFLKAVRAAGLHRAVVSSSAN--CANVLKAAGIDDMfEVRI--D 167
Cdd:cd07527   54 ------DDADIELVLALEteepesYPEGVIAIPGAVDLLASLPAAGDRWAIVTSGTRalAEARLEAAGLPHP-EVLVtaD 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212 168 GVTIakenlpGKPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGGFgFVVGVDRVGQADALRSSGADTVVTDLADL 247
Cdd:cd07527  127 DVKN------GKPDPEPYLLGAKLLGLDPSDCVVFEDAPAGIKAGKAAGA-RVVAVNTSHDLEQLEAAGADLVVEDLSDI 199
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
16-248 2.07e-23

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 94.23  E-value: 2.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  16 IRACLFDLDGVLTETAKVHAAAWKQMFDAYLksrpgpfVPFDPVADYDRYVdGKTRSDGTRSFLasrninlpdgspdDPP 95
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAAALNEALAELG-------LPPLDLEELRALI-GLGLRELLRRLL-------------GED 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  96 GTETINGLGNAKNEIVLKLLDTQgVHVYEGSVRFLKAVRAAGLHRAVVSS--SANCANVLKAAGIDDMFEVRIDGVTIAk 173
Cdd:COG0546   60 PDEELEELLARFRELYEEELLDE-TRLFPGVRELLEALKARGIKLAVVTNkpREFAERLLEALGLDDYFDAIVGGDDVP- 137

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506275212 174 enlPGKPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGGFGFvVGVDR-VGQADALRSSGADTVVTDLADLL 248
Cdd:COG0546  138 ---PAKPKPEPLLEALERLGLDPEEVLMVGDSPHDIEAARAAGVPF-IGVTWgYGSAEELEAAGADYVIDSLAELL 209
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 16-216 1.06e-21

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: 89.18  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212   16 IRACLFDLDGVLTETAKVHAAAWKQMFDAYLKSRPGPFVPFDPVADYDRYvdGKTRSDGTRSFLASRNINLPDGSPDDPP 95
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPLAKAIVAAAEDLPIPVEDF--TARLLLGKRDWLEELDILRGLVETLEAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212   96 GTETINGlgnaknEIVLKLLDTQGVHVYEGSVRFLKAVRAAGLHRAVVSSS--ANCANVLKAAGIDDMFEVRIDGVTIAK 173
Cdd:pfam00702  79 GLTVVLV------ELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDnpEAAEALLRLLGLDDYFDVVISGDDVGV 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 506275212  174 enlpGKPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGG 216
Cdd:pfam00702 153 ----GKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 16-249 3.42e-17

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: 77.76  E-value: 3.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  16 IRACLFDLDGVLTETAKVHAAAWKQMFDAYlksrpGPFVPFDPVAD---------YDRYVDGK-TRSDGTRSFLASRNIN 85
Cdd:COG1011    1 IKAVLFDLDGTLLDFDPVIAEALRALAERL-----GLLDEAEELAEayraieyalWRRYERGEiTFAELLRRLLEELGLD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  86 LPDGSPDDppgtetinglgnakneiVLKLLDtQGVHVYEGSVRFLKAVRAAGLHRAVVS--SSANCANVLKAAGIDDMFe 163
Cdd:COG1011   76 LAEELAEA-----------------FLAALP-ELVEPYPDALELLEALKARGYRLALLTngSAELQEAKLRRLGLDDLF- 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212 164 vriDGVTIAKENLPGKPAPDTYLAAAKKLGIDPDQAAVFEDALAG-VEAGRSGGFGFVVgVDRVGQADALRSSgADTVVT 242
Cdd:COG1011  137 ---DAVVSSEEVGVRKPDPEIFELALERLGVPPEEALFVGDSPETdVAGARAAGMRTVW-VNRSGEPAPAEPR-PDYVIS 211


                 ....*..
gi 506275212 243 DLADLLK 249
Cdd:COG1011  212 DLAELLE 218
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 18-221 3.98e-17

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: 77.03  E-value: 3.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  18 ACLFDLDGVLTETAKVHaaawKQMFDAYLKSRPGPFVPFDPvADYDRY---VDGKTRsdgTRSFLasRNINLPDGSPDDP 94
Cdd:cd07528    1 ALIFDVDGTLAETEELH----RRAFNNAFFAERGLDWYWDR-ELYGELlrvGGGKER---IAAYF--EKVGWPESAPKDL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  95 PgtETINGLGNAKNEIVLKLLDTQGVHVYEGSVRFLKAVRAAGLHRAVVSSS--ANCANVLKAA-GID--DMFEVRIDGV 169
Cdd:cd07528   71 K--ELIADLHKAKTERYAELIAAGLLPLRPGVARLIDEAKAAGVRLAIATTTspANVDALLSALlGPErrAIFDAIAAGD 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 506275212 170 TIAKEnlpgKPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGGFGFVV 221
Cdd:cd07528  149 DVAEK----KPDPDIYLLALERLGVSPSDCLAIEDSAIGLQAAKAAGLPCIV 196
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
19-216 3.51e-16

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 73.77  E-value: 3.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212   19 CLFDLDGVLTETAKVHAAAWKQMFDAYLKSRPGP--FVPF--DPVADYDRYVDGKTRSDGTRSFLasrninlpdgspddp 94
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYGELSEeeILKFigLPLREIFRYLGVSEDEEEKIEFY--------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212   95 pgtetinglgnakNEIVLKLLDTQGVHVYEGSVRFLKAVRAAGLHRAVVSS--SANCANVLKAAGIDDMFEVRIDGVTIA 172
Cdd:pfam13419  66 -------------LRKYNEELHDKLVKPYPGIKELLEELKEQGYKLGIVTSksRENVEEFLKQLGLEDYFDVIVGGDDVE 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 506275212  173 KenlpGKPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGG 216
Cdd:pfam13419 133 G----KKPDPDPILKALEQLGLKPEEVIYVGDSPRDIEAAKNAG 172
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 107-246 6.76e-16

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: 73.06  E-value: 6.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212 107 KNEIVLKLLDTQGVH-VYEGSVRFLKAVRAAGLHRAVVSSS--ANCANVLKAAGIDDMFEVRIDGVTIAKenlpGKPAPD 183
Cdd:cd16423   29 RNELIKRQFSEKTDLpPIEGVKELLEFLKEKGIKLAVASSSprRWIEPHLERLGLLDYFEVIVTGDDVEK----SKPDPD 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506275212 184 TYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGGFgFVVGVDRVgQADALRSSGADTVVTDLAD 246
Cdd:cd16423  105 LYLEAAERLGVNPEECVVIEDSRNGVLAAKAAGM-KCVGVPNP-VTGSQDFSKADLVLSSFAE 165
PLN02940 PLN02940
riboflavin kinase
 125-247 1.51e-13

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 69.48  E-value: 1.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212 125 GSVRFLKAVRAAGLHRAVVSSS--ANC-ANVLKAAGIDDMFEVRIDGVTIAKenlpGKPAPDTYLAAAKKLGIDPDQAAV 201
Cdd:PLN02940  97 GANRLIKHLKSHGVPMALASNSprANIeAKISCHQGWKESFSVIVGGDEVEK----GKPSPDIFLEAAKRLNVEPSNCLV 172

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 506275212 202 FEDALAGVEAGRSGGFGfVVGVDRVGQADALRSSgADTVVTDLADL 247
Cdd:PLN02940 173 IEDSLPGVMAGKAAGME-VIAVPSIPKQTHLYSS-ADEVINSLLDL 216
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 15-216 1.74e-12

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 66.80  E-value: 1.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212   15 RIRACLFDLDGVLTETAKVHAAAWKQMF-DAYLKSRPGPFVPFDPVADYDrYVDGKTRSDGTRSF---LASR---NINLP 87
Cdd:PLN02919   74 KVSAVLFDMDGVLCNSEEPSRRAAVDVFaEMGVEVTVEDFVPFMGTGEAN-FLGGVASVKGVKGFdpdAAKKrffEIYLE 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212   88 DGSPDDppgtetiNGLGnakneivlklldtqgvhvYEGSVRFLKAVRAAGLHRAVVSSSANC---ANvLKAAGID-DMFE 163
Cdd:PLN02919  153 KYAKPN-------SGIG------------------FPGALELITQCKNKGLKVAVASSADRIkvdAN-LAAAGLPlSMFD 206

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 506275212  164 --VRIDgvtiAKENLpgKPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGG 216
Cdd:PLN02919  207 aiVSAD----AFENL--KPAPDIFLAAAKILGVPTSECVVIEDALAGVQAARAAG 255
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 121-248 1.86e-12

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: 64.56  E-value: 1.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212 121 HVYEGSVRFLKAVRAAGLHRAVVS--SSANCANVLKAAGIDDMFEVRIDGVTIAKEnlpgKPAPDTYLAAAKKLGIDPDQ 198
Cdd:cd16417   87 HLYPGVKEGLAALKAQGYPLACVTnkPERFVAPLLEALGISDYFSLVLGGDSLPEK----KPDPAPLLHACEKLGIAPAQ 162

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 506275212 199 AAVFEDALAGVEAGRSGGFGfVVGVdRVGQAD--ALRSSGADTVVTDLADLL 248
Cdd:cd16417  163 MLMVGDSRNDILAARAAGCP-SVGL-TYGYNYgeDIAASGPDAVIDSLAELL 212
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 16-216 4.56e-12

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: 63.14  E-value: 4.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  16 IRACLFDLDGVLTETAKVHAAAWKQMFDAYLKsrpgpfvpfDPVADYDRYVDGKTRSDGTRSFLASRNInlpdgspDDPP 95
Cdd:cd07529    1 VTHCIFDMDGLLLDTERIYTETTQEILARYGK---------TYTWDVKAKMMGRPASEAARIIVDELKL-------PMSL 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  96 GTETINglgnaKNEIVLKLLDTQgVHVYEGSVRFLKAVRAAGLHRAVVSSSANCANVLKAAGIDDMFE-----VRIDGVT 170
Cdd:cd07529   65 EEEFDE-----QQEALAELFMGT-AKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSlfhhvVTGDDPE 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 506275212 171 IAKEnlpGKPAPDTYLAAAKKLG---IDPDQAAVFEDALAGVEAGRSGG 216
Cdd:cd07529  139 VKGR---GKPAPDIFLVAAKRFNeppKDPSKCLVFEDSPNGVKAAKAAG 184
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 132-220 4.60e-12

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: 61.95  E-value: 4.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212 132 AVRAAGLHRAVVSSS--ANCANVLKAAGIDDMFEVRI-DGVTIAKenlpGKPAPDTYLAAAKKLGIDPDQAAVFEDALAG 208
Cdd:cd07526   50 ALSALTLPFCVASNSsrERLTHSLGLAGLLAYFEGRIfSASDVGR----GKPAPDLFLHAAAQMGVAPERCLVIEDSPTG 125

                         90
                 ....*....|....*
gi 506275212 209 VEAGRSGG---FGFV 220
Cdd:cd07526  126 VRAALAAGmtvFGFT 140
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 7-246 1.42e-11

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 62.80  E-value: 1.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212   7 STKTGLPErirACLFDLDGVLTETAK-VHAAAWKQMFDAYlKSRPgpfVPFDpVADYDRYVD---GKTRSdgTRSFlasR 82
Cdd:PLN02779  34 ASASALPE---ALLFDCDGVLVETERdGHRVAFNDAFKEF-GLRP---VEWD-VELYDELLNiggGKERM--TWYF---N 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  83 NINLPDGSPDDPPGTET-----INGLGNAKNEIVLKLLDTQGVHVYEGSVRFLKAVRAAGLHRAVVSSS-----ANCANV 152
Cdd:PLN02779 101 ENGWPTSTIEKAPKDEEerkelVDSLHDRKTELFKELIESGALPLRPGVLRLMDEALAAGIKVAVCSTSnekavSKIVNT 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212 153 LKAAGIDDMFEVRIDGVTIAKenlpgKPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRsgGFGFVVGVDRVGQADAL 232
Cdd:PLN02779 181 LLGPERAQGLDVFAGDDVPKK-----KPDPDIYNLAAETLGVDPSRCVVVEDSVIGLQAAK--AAGMRCIVTKSSYTADE 253

                        250
                 ....*....|....
gi 506275212 233 RSSGADTVVTDLAD 246
Cdd:PLN02779 254 DFSGADAVFDCLGD 267
PRK11587 PRK11587
putative phosphatase; Provisional
 20-254 4.24e-11

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 60.78  E-value: 4.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  20 LFDLDGVLTETAKVHAAAWKQMFDaylksRPGpfVPFDPVADYdryVDGKTRSDGTRSFLASRNinlpdgspddppgTET 99
Cdd:PRK11587   7 LFDLDGTLVDSLPAVERAWSNWAD-----RHG--IAPDEVLNF---IHGKQAITSLRHFMAGAS-------------EAE 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212 100 INGLGNAKNEIvlKLLDTQGVHVYEGSVRFLKAVRAAGLHRAVVSS------SANCanvlKAAGIDdMFEVRIDGVTIAK 173
Cdd:PRK11587  64 IQAEFTRLEQI--EATDTEGITALPGAIALLNHLNKLGIPWAIVTSgsvpvaSARH----KAAGLP-APEVFVTAERVKR 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212 174 enlpGKPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGGFGfVVGVDrvGQADALRSSGADTVVTDLADLL--KQE 251
Cdd:PRK11587 137 ----GKPEPDAYLLGAQLLGLAPQECVVVEDAPAGVLSGLAAGCH-VIAVN--APADTPRLDEVDLVLHSLEQLTvtKQP 209


                 ...
gi 506275212 252 DQA 254
Cdd:PRK11587 210 NGD 212
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 16-249 9.31e-11

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: 59.60  E-value: 9.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  16 IRACLFDLDGVLTETAKVHAAAWKQMFDAYLKSRPGPfvpfdpvADYDRYVdGKTRSDGTRSFLASRNINLPDgspddpp 95
Cdd:cd02616    1 ITTILFDLDGTLIDTNELIIKSFNHTLKEYGLEGYTR-------EEVLPFI-GPPLRETFEKIDPDKLEDMVE------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  96 gtETINGlgNAKNEIVLklldtqgVHVYEGSVRFLKAVRAAGLHRAVVSSSAN--CANVLKAAGIDDMFEVRIDGVTIAK 173
Cdd:cd02616   66 --EFRKY--YREHNDDL-------TKEYPGVYETLARLKSQGIKLGVVTTKLRetALKGLKLLGLDKYFDVIVGGDDVTH 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506275212 174 EnlpgKPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGGFGFVVGVDRVGQADALRSSGADTVVTDLADLLK 249
Cdd:cd02616  135 H----KPDPEPVLKALELLGAEPEEALMVGDSPHDILAGKNAGVKTVGVTWGYKGREYLKAFNPDFIIDKMSDLLT 206
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
13-249 1.56e-09

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 56.36  E-value: 1.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  13 PERIRACLFDLDGVLTETA-KVHAAAwkqmfDAYLKSRPGPFVPFDPVADY-----DRYVDgktrsdgtRSFlasrninl 86
Cdd:PRK13222   3 FMDIRAVAFDLDGTLVDSApDLAAAV-----NAALAALGLPPAGEERVRTWvgngaDVLVE--------RAL-------- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  87 pDGSPDDPPGTETinglgnaknEIVLKLLD-------TQGVHVYEGSVRFLKAVRAAGLHRAVVS--SSANCANVLKAAG 157
Cdd:PRK13222  62 -TWAGREPDEELL---------EKLRELFDrhyaenvAGGSRLYPGVKETLAALKAAGYPLAVVTnkPTPFVAPLLEALG 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212 158 IDDMFEVRIDGVTIAKEnlpgKPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGGFGfVVGVD---RVGQadALRS 234
Cdd:PRK13222 132 IADYFSVVIGGDSLPNK----KPDPAPLLLACEKLGLDPEEMLFVGDSRNDIQAARAAGCP-SVGVTygyNYGE--PIAL 204

                        250
                 ....*....|....*
gi 506275212 235 SGADTVVTDLADLLK 249
Cdd:PRK13222 205 SEPDVVIDHFAELLP 219
PLN02811 PLN02811
hydrolase
 125-246 3.70e-09

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 55.15  E-value: 3.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212 125 GSVRFLKAVRAAGLHRAVVSSSANCANVLKAAGIDDMFE-----VRIDGVTIAKenlpGKPAPDTYLAAAKKL---GIDP 196
Cdd:PLN02811  82 GAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSlmhhvVTGDDPEVKQ----GKPAPDIFLAAARRFedgPVDP 157

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 506275212 197 DQAAVFEDALAGVEAGRSGGFGFVVGVDrvGQADALRSSGADTVVTDLAD 246
Cdd:PLN02811 158 GKVLVFEDAPSGVEAAKNAGMSVVMVPD--PRLDKSYCKGADQVLSSLLD 205
Pyr-5-nucltdase TIGR01993
pyrimidine 5'-nucleotidase; This family of proteins includes the SDT1/SSM1 gene from yeast ...
 144-221 4.71e-09

pyrimidine 5'-nucleotidase; This family of proteins includes the SDT1/SSM1 gene from yeast which has been shown to code for a pyrimidine (UMP/CMP) 5'nucleotidase. The family spans plants, fungi and a small number of bacteria. These enzymes are members of the haloacid dehalogenase (HAD) superfamily of hydrolases, specifically the IA subfamily (variant 3, TIGR01509).


Pssm-ID: 273917 [Multi-domain]  Cd Length: 183  Bit Score: 54.28  E-value: 4.71e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506275212  144 SSSANCANVLKAAGIDDMFEVRIDGVTIAKENLPgKPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGGFGFVV 221
Cdd:TIGR01993 106 GDRAHARRALRRLGIEDCFDGIFCFDTANPDLLP-KPSPQAYEKALREAGVDPERAIFFDDSARNIAAGKALGMKTVL 182
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 16-246 8.58e-09

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 54.46  E-value: 8.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  16 IRACLFDLDGVLTETAKVHAAAWKQMFdayLKSRPGPFVPFDPvADYDRYVDGKTRSDGTRSFLasrninlpdgsPDDPP 95
Cdd:PLN02770  22 LEAVLFDVDGTLCDSDPLHYYAFREML---QEINFNGGVPITE-EFFVENIAGKHNEDIALGLF-----------PDDLE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  96 GtetinGLG-NAKNEIVLKLLDTQGVHVYEGSVRFLKAVRAAGLHRAVVSSS--ANCANVLKAAGIDDMFevriDGVTIA 172
Cdd:PLN02770  87 R-----GLKfTDDKEALFRKLASEQLKPLNGLYKLKKWIEDRGLKRAAVTNAprENAELMISLLGLSDFF----QAVIIG 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506275212 173 KENLPGKPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGGFGfVVGVDRVGQADALRSSGADTVVTDLAD 246
Cdd:PLN02770 158 SECEHAKPHPDPYLKALEVLKVSKDHTFVFEDSVSGIKAGVAAGMP-VVGLTTRNPESLLMEAKPTFLIKDYED 230
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 16-217 2.36e-08

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: 52.73  E-value: 2.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  16 IRACLFDLDGVLTETAkvhaaaWKQMFDAYLKSrpgPFVPFDPVADYDRYVDGKTRSDGTRSFLAS--RNINLPDGSPDD 93
Cdd:cd02603    1 IRAVLFDFGGVLIDPD------PAAAVARFEAL---TGEPSEFVLDTEGLAGAFLELERGRITEEEfwEELREELGRPLS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  94 PPGTEtinglgnaknEIVLKlldtqGVHVYEGSVRFLKAVRAAGLHRAVVSSSANCANVLKAAGIDDMFEvRIDGVTIAK 173
Cdd:cd02603   72 AELFE----------ELVLA-----AVDPNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLPRRGD-LFDGVVESC 135

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 506275212 174 ENLPGKPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGGF 217
Cdd:cd02603  136 RLGVRKPDPEIYQLALERLGVKPEEVLFIDDREENVEAARALGI 179
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
179-220 1.17e-07

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 50.46  E-value: 1.17e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 506275212 179 KPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGGFGFV 220
Cdd:PRK10725 142 KPAPDTFLRCAQLMGVQPTQCVVFEDADFGIQAARAAGMDAV 183
PRK10826 PRK10826
hexitol phosphatase HxpB;
130-213 1.25e-07

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 50.72  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212 130 LKAVRAAGLHRAVVSSS--ANCANVLKAAGIDDMFEVridgvTIAKENLP-GKPAPDTYLAAAKKLGIDPDQAAVFEDAL 206
Cdd:PRK10826 101 LALCKAQGLKIGLASASplHMLEAVLTMFDLRDYFDA-----LASAEKLPySKPHPEVYLNCAAKLGVDPLTCVALEDSF 175


                 ....*..
gi 506275212 207 AGVEAGR 213
Cdd:PRK10826 176 NGMIAAK 182
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 15-248 1.40e-06

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 47.72  E-value: 1.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  15 RIRACLFDLDGVLTETAKVHAAAWKQMFDAYLKSRPG-----PFV-P--FDPVADYDryvdgKTRSDGTRSFLASRNINL 86
Cdd:PRK13288   2 KINTVLFDLDGTLINTNELIISSFLHTLKTYYPNQYKredvlPFIgPslHDTFSKID-----ESKVEEMITTYREFNHEH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212  87 PDgspddppgtetinglgnakneivlkLLDTQGVHVYEGsvrfLKAVRAAGLHRAVVSSSA-NCANV-LKAAGIDDMFEV 164
Cdd:PRK13288  77 HD-------------------------ELVTEYETVYET----LKTLKKQGYKLGIVTTKMrDTVEMgLKLTGLDEFFDV 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212 165 RI--DGVTIAKenlpgkPAPDTYLAAAKKLGIDPDQAAV----FEDALAGVEAG-RSGGFGFVVgvdrVGQaDALRSSGA 237
Cdd:PRK13288 128 VItlDDVEHAK------PDPEPVLKALELLGAKPEEALMvgdnHHDILAGKNAGtKTAGVAWTI----KGR-EYLEQYKP 196

                        250
                 ....*....|.
gi 506275212 238 DTVVTDLADLL 248
Cdd:PRK13288 197 DFMLDKMSDLL 207
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 125-247 1.42e-06

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 48.10  E-value: 1.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212 125 GSVRFLKAVRAAGLHRAVVSSSAN--CANVLKAAGIDDMFEVridgVTIAKENLPGKPAPDTYLAAAKKLGIDPDQAAVF 202
Cdd:PLN03243 113 GSREFVQALKKHEIPIAVASTRPRryLERAIEAVGMEGFFSV----VLAAEDVYRGKPDPEMFMYAAERLGFIPERCIVF 188

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 506275212 203 EDALAGVEAGRSGGFGFVVgvdRVGQADALRSSGADTVVTDLADL 247
Cdd:PLN03243 189 GNSNSSVEAAHDGCMKCVA---VAGKHPVYELSAGDLVVRRLDDL 230
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 106-248 2.01e-06

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: 46.97  E-value: 2.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212 106 AKNEIVLKLLDTQGVHVYEGSVRFLKAVRAAGLHRAVVSSS--ANCANVLKAAGIDDMFEVridgvtIAKENLPGKPAPD 183
Cdd:cd04303   64 AKDFRRLMAEAAPELALFPGVEDMLRALHARGVRLAVVSSNseENIRRVLGPEELISLFAV------IEGSSLFGKAKKI 137

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506275212 184 TYLAAAKKlgIDPDQAAVFEDALAGVEAGRSGGFGFVV---GVDRvgqADALRSSGADTVVTDLADLL 248
Cdd:cd04303  138 RRVLRRTK--ITAAQVIYVGDETRDIEAARKVGLAFAAvswGYAK---PEVLKALAPDHMLEDPEDLI 200
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 145-221 2.18e-06

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p and Sdt1p; This family includes Saccharomyces cerevisiae Phm8p (phosphate metabolism protein 8) and Sdt1p (Suppressor of disruption of TFIIS). Phm8p participates in the ribose salvage pathway, it catalyzes the dephosphorylation of nucleotide monophosphates to nucleosides, its preferred substrates are nucleotide monophosphates AMP, GMP, CMP, and UMP. Phm8p is also a lysophosphatidic acid phosphatase, dephosphorylating lysophosphatidic acids (LPAs) to monoacylglycerol in response to phosphate starvation. Sdt1p is a pyrimidine and pyridine-specific 5'-nucleotidase; it is an NMN/NaMN 5'-nucleotidases involved in the production of nicotinamide riboside and nicotinic acid riboside, and is a pyrimidine 5'-nucleotidase with high specificity for UMP and 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: 319791 [Multi-domain]  Cd Length: 182  Bit Score: 46.86  E-value: 2.18e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506275212 145 SSANCAN-VLKAAGIDDMFevriDGVT-IAKENLPGKPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGGFGFVV 221
Cdd:cd02604  105 ASKNHAIrVLKRLGLADLF----DGIFdIEYAGPDPKPHPAAFEKAIREAGLDPKRAAFFDDSIRNLLAAKALGMKTVL 179
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 127-223 4.17e-05

Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGPase; 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: 319857 [Multi-domain]  Cd Length: 105  Bit Score: 41.67  E-value: 4.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212 127 VRFLKAVRAAGLHRAVVSSSANCA-NVLkaagIDDMFEVRIDGVTIAKENLPGKPAPDTYLAAAKKLGIDPDQAAVFEDA 205
Cdd:cd16421   13 LELLKALRQKGIKLAVLSNKPNEAvQVL----VEELFPGSFDFVLGEKEGIRRKPDPT*ALECAKVLGVPPDEVLYVGDS 88

                         90
                 ....*....|....*...
gi 506275212 206 LAGVEAGRSGGFgFVVGV 223
Cdd:cd16421   89 GVDMQTARNAGM-DEIGV 105
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 127-220 4.66e-05

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 41.61  E-value: 4.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212 127 VRFLKAVRAAGLHRAVVSSSANCA--NVLKAAGIDDMFevriDGVTIAKENLPGKPAPDTYLAAAKKLGIDPDQAAVFED 204
Cdd:cd01427   13 VELLKRLRAAGIKLAIVTNRSREAlrALLEKLGLGDLF----DGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGD 88

                         90
                 ....*....|....*.
gi 506275212 205 ALAGVEAGRSGGFGFV 220
Cdd:cd01427   89 SENDIEAARAAGGRTV 104
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 120-246 5.72e-05

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


Pssm-ID: 440011 [Multi-domain]  Cd Length: 176  Bit Score: 42.39  E-value: 5.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212 120 VHVYEGSVRFLKAVRAAGLHRAVVSssancaN-----------------------VLKAAGIddmfevRIDGV----TIA 172
Cdd:COG0241   27 FEFLPGVLEALARLNEAGYRLVVVT------NqsgigrglfteedlnavhakmleLLAAEGG------RIDAIyycpHHP 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506275212 173 KENLPG-KPAPDTYLAAAKKLGIDPDQAAVFEDALAGVEAGRSGGFGFVVgVDRVGQADALRSSGADTVVTDLAD 246
Cdd:COG0241   95 DDNCDCrKPKPGMLLQAAERLGIDLSNSYMIGDRLSDLQAAKAAGCKGIL-VLTGKGAEELAEALPDTVADDLAE 168
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 123-216 7.41e-04

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the uncharacterized Lactococcus lactis YsbA; The specific function of Lactococcus lactis YsbA is unknown. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases


Pssm-ID: 319825 [Multi-domain]  Cd Length: 173  Bit Score: 39.28  E-value: 7.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212 123 YEGSVRFLKAVRAAGLHRAVVSSSANCA-NVLKAAGIDDMFevrIDGVTIAkENLPGKPAPDTYLAAAKKLGIDPDQAAV 201
Cdd:cd07523   77 FPGAKAVLRWIKEQGGKNFLMTHRDHSAlTILKKDGIASYF---TEIVTSD-NGFPRKPNPEAINYLLNKYQLNPEETVM 152

                         90
                 ....*....|....*
gi 506275212 202 FEDALAGVEAGRSGG 216
Cdd:cd07523  153 IGDRELDIEAGHNAG 167
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 111-247 8.01e-04

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to Parvibaculum lavamentivorans HAD-superfamily hydrolase, subfamily IA, variant 1; This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319835 [Multi-domain]  Cd Length: 207  Bit Score: 39.69  E-value: 8.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212 111 VLKLLDTQGVHVYEGSVRFLKAVRAAGLHRAVVS--SSANCANVLKAAGIDDMFevriDGVTIAKENlPGKPAPDTYLAA 188
Cdd:cd07533   74 ILRLLPEHAEPLFPGVREALDALAAQGVLLAVATgkSRRGLDRVLEQHGLGGYF----DATRTADDT-PSKPHPEMLREI 148

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212 189 AKKLGIDPDQAAVFEDALAGVE-AGRSGGFGFVVGVDRVGQADaLRSSGADTVVTDLADL 247
Cdd:cd07533  149 LAELGVDPSRAVMVGDTAYDMQmAANAGAHAVGVAWGYHSLED-LRSAGADAVVDHFSEL 207
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 130-247 2.21e-03

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: 38.40  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506275212 130 LKAVRAAGLHRAVVSSSAN--CANVLKAAGIDDMFEVRIDGVTIAKEnlpgKPAPDTYLAAAKKLGIDPDQaaVFEDALA 207
Cdd:cd02588  100 LRRLREAGYRLAILSNGSPdlIEDVVANAGLRDLFDAVLSAEDVRAY----KPAPAVYELAAERLGVPPDE--ILHVASH 173

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 506275212 208 GVEAGRSGGFGFVVG-VDRVGQADALRSSGADTVVTDLADL 247
Cdd:cd02588  174 AWDLAGARALGLRTAwINRPGEVPDPLGPAPDFVVPDLGEL 214
 
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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