haloacid dehalogenase-like hydrolase family protein [Arabidopsis thaliana]
Protein Classification
PLN02919 family protein( domain architecture ID 11477289)
PLN02919 family protein
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||||||||||
| PLN02919 | PLN02919 | haloacid dehalogenase-like hydrolase family protein |
1-1055 | 0e+00 | |||||||||||||||
haloacid dehalogenase-like hydrolase family protein : Pssm-ID: 215497 [Multi-domain] Cd Length: 1057 Bit Score: 2114.52 E-value: 0e+00
|
|||||||||||||||||||
| Name | Accession | Description | Interval | E-value | |||||||||||||||
| PLN02919 | PLN02919 | haloacid dehalogenase-like hydrolase family protein |
1-1055 | 0e+00 | |||||||||||||||
haloacid dehalogenase-like hydrolase family protein Pssm-ID: 215497 [Multi-domain] Cd Length: 1057 Bit Score: 2114.52 E-value: 0e+00
|
|||||||||||||||||||
| NHL-2_like | cd14951 | NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL ... |
604-946 | 2.36e-175 | |||||||||||||||
NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL repeat-containing protein 2 (NHLRC2) and related bacterial proteins; members of this eukaryotic and bacterial family are uncharacterized, the NHL repeat domain is found C-terminally of a thioredoxin domain. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271321 [Multi-domain] Cd Length: 334 Bit Score: 515.20 E-value: 2.36e-175
|
|||||||||||||||||||
| YcjU | COG0637 | Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism]; |
73-284 | 5.38e-59 | |||||||||||||||
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism]; Pssm-ID: 440402 [Multi-domain] Cd Length: 208 Bit Score: 201.21 E-value: 5.38e-59
|
|||||||||||||||||||
| PGMB-YQAB-SF | TIGR02009 | beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ... |
74-260 | 2.23e-34 | |||||||||||||||
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: 130.16 E-value: 2.23e-34
|
|||||||||||||||||||
| HAD_2 | pfam13419 | Haloacid dehalogenase-like hydrolase; |
77-260 | 3.30e-33 | |||||||||||||||
Haloacid dehalogenase-like hydrolase; Pssm-ID: 404323 [Multi-domain] Cd Length: 178 Bit Score: 126.55 E-value: 3.30e-33
|
|||||||||||||||||||
| LY | smart00135 | Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) ... |
560-600 | 5.41e-03 | |||||||||||||||
Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. Also present in a variety of molecules similar to gp300/megalin. Pssm-ID: 214531 [Multi-domain] Cd Length: 43 Bit Score: 35.66 E-value: 5.41e-03
|
|||||||||||||||||||
| Name | Accession | Description | Interval | E-value | |||||||||||||||
| PLN02919 | PLN02919 | haloacid dehalogenase-like hydrolase family protein |
1-1055 | 0e+00 | |||||||||||||||
haloacid dehalogenase-like hydrolase family protein Pssm-ID: 215497 [Multi-domain] Cd Length: 1057 Bit Score: 2114.52 E-value: 0e+00
|
|||||||||||||||||||
| NHL-2_like | cd14951 | NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL ... |
604-946 | 2.36e-175 | |||||||||||||||
NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL repeat-containing protein 2 (NHLRC2) and related bacterial proteins; members of this eukaryotic and bacterial family are uncharacterized, the NHL repeat domain is found C-terminally of a thioredoxin domain. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271321 [Multi-domain] Cd Length: 334 Bit Score: 515.20 E-value: 2.36e-175
|
|||||||||||||||||||
| TlpA_like_DipZ_like | cd03012 | TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ... |
397-522 | 3.70e-59 | |||||||||||||||
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a TlpA-like TRX domain. Some members show domain architectures similar to that of E. coli DipZ protein (also known as DsbD). The only eukaryotic members of the TlpA family belong to this subfamily. TlpA is a disulfide reductase known to have a crucial role in the biogenesis of cytochrome aa3. Pssm-ID: 239310 [Multi-domain] Cd Length: 126 Bit Score: 198.68 E-value: 3.70e-59
|
|||||||||||||||||||
| YcjU | COG0637 | Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism]; |
73-284 | 5.38e-59 | |||||||||||||||
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism]; Pssm-ID: 440402 [Multi-domain] Cd Length: 208 Bit Score: 201.21 E-value: 5.38e-59
|
|||||||||||||||||||
| NHL_like_1 | cd14953 | Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ... |
556-884 | 3.77e-49 | |||||||||||||||
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat domains is found in a variety of domain architectures. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271323 [Multi-domain] Cd Length: 323 Bit Score: 177.34 E-value: 3.77e-49
|
|||||||||||||||||||
| NHL | cd05819 | NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ... |
562-884 | 7.38e-43 | |||||||||||||||
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats. Pssm-ID: 271320 [Multi-domain] Cd Length: 269 Bit Score: 157.48 E-value: 7.38e-43
|
|||||||||||||||||||
| HAD_BPGM-like | cd07505 | beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ... |
76-262 | 1.53e-42 | |||||||||||||||
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: 152.00 E-value: 1.53e-42
|
|||||||||||||||||||
| NHL_like_1 | cd14953 | Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ... |
607-885 | 4.23e-42 | |||||||||||||||
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat domains is found in a variety of domain architectures. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271323 [Multi-domain] Cd Length: 323 Bit Score: 156.92 E-value: 4.23e-42
|
|||||||||||||||||||
| Gph | COG0546 | Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion]; |
76-274 | 7.98e-41 | |||||||||||||||
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion]; Pssm-ID: 440312 [Multi-domain] Cd Length: 214 Bit Score: 149.69 E-value: 7.98e-41
|
|||||||||||||||||||
| NHL | cd05819 | NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ... |
616-887 | 1.64e-36 | |||||||||||||||
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats. Pssm-ID: 271320 [Multi-domain] Cd Length: 269 Bit Score: 138.99 E-value: 1.64e-36
|
|||||||||||||||||||
| PGMB-YQAB-SF | TIGR02009 | beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ... |
74-260 | 2.23e-34 | |||||||||||||||
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: 130.16 E-value: 2.23e-34
|
|||||||||||||||||||
| HAD_2 | pfam13419 | Haloacid dehalogenase-like hydrolase; |
77-260 | 3.30e-33 | |||||||||||||||
Haloacid dehalogenase-like hydrolase; Pssm-ID: 404323 [Multi-domain] Cd Length: 178 Bit Score: 126.55 E-value: 3.30e-33
|
|||||||||||||||||||
| TrxA | COG0526 | Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
390-535 | 2.85e-32 | |||||||||||||||
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 122.49 E-value: 2.85e-32
|
|||||||||||||||||||
| HAD_BPGM-like | cd16423 | uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ... |
76-261 | 7.33e-32 | |||||||||||||||
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: 122.36 E-value: 7.33e-32
|
|||||||||||||||||||
| Hydrolase | pfam00702 | haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ... |
74-254 | 4.18e-29 | |||||||||||||||
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: 115.38 E-value: 4.18e-29
|
|||||||||||||||||||
| TlpA_like_family | cd02966 | TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ... |
415-520 | 1.30e-28 | |||||||||||||||
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases. Pssm-ID: 239264 [Multi-domain] Cd Length: 116 Bit Score: 111.17 E-value: 1.30e-28
|
|||||||||||||||||||
| PLN02779 | PLN02779 | haloacid dehalogenase-like hydrolase family protein |
33-283 | 2.87e-28 | |||||||||||||||
haloacid dehalogenase-like hydrolase family protein Pssm-ID: 215416 [Multi-domain] Cd Length: 286 Bit Score: 115.58 E-value: 2.87e-28
|
|||||||||||||||||||
| HAD_CbbY-like | cd07528 | subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ... |
76-262 | 7.01e-28 | |||||||||||||||
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: 112.09 E-value: 7.01e-28
|
|||||||||||||||||||
| HAD_ScGPP-like | cd07527 | subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ... |
76-286 | 7.10e-28 | |||||||||||||||
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: 112.05 E-value: 7.10e-28
|
|||||||||||||||||||
| PRK10826 | PRK10826 | hexitol phosphatase HxpB; |
74-260 | 1.13e-27 | |||||||||||||||
hexitol phosphatase HxpB; Pssm-ID: 236770 [Multi-domain] Cd Length: 222 Bit Score: 111.96 E-value: 1.13e-27
|
|||||||||||||||||||
| YigB | COG1011 | FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ... |
74-258 | 1.19e-26 | |||||||||||||||
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: 108.96 E-value: 1.19e-26
|
|||||||||||||||||||
| NHL_like_3 | cd14956 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
563-878 | 2.03e-26 | |||||||||||||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271326 [Multi-domain] Cd Length: 274 Bit Score: 110.06 E-value: 2.03e-26
|
|||||||||||||||||||
| HAD_BPGM_like | cd07526 | subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ... |
76-258 | 2.16e-25 | |||||||||||||||
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: 102.78 E-value: 2.16e-25
|
|||||||||||||||||||
| Vgb | COG4257 | Streptogramin lyase [Defense mechanisms]; |
565-885 | 1.39e-24 | |||||||||||||||
Streptogramin lyase [Defense mechanisms]; Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 104.72 E-value: 1.39e-24
|
|||||||||||||||||||
| HAD_BPGM | cd02598 | beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ... |
163-290 | 4.12e-24 | |||||||||||||||
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: 100.06 E-value: 4.12e-24
|
|||||||||||||||||||
| bPGM | TIGR01990 | beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ... |
76-260 | 1.05e-23 | |||||||||||||||
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: 99.30 E-value: 1.05e-23
|
|||||||||||||||||||
| HAD-SF-IA-v3 | TIGR01509 | haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ... |
76-260 | 2.31e-23 | |||||||||||||||
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: 98.26 E-value: 2.31e-23
|
|||||||||||||||||||
| NHL_like_5 | cd14963 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
565-881 | 4.75e-23 | |||||||||||||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271333 [Multi-domain] Cd Length: 268 Bit Score: 100.06 E-value: 4.75e-23
|
|||||||||||||||||||
| NHL_TRIM71_like | cd14954 | NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ... |
566-881 | 1.54e-22 | |||||||||||||||
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; The E3 ubiquitin-protein ligase TRIM71 (LIN-41) is a RING-finger domain containing protein that has been associated with a variety of activities. The NHL repeat domain appears responsible for targeting TRIM71 to mRNAs, and TRIM71 appears responsible for translational repression and mRNA decay. Together with BRAT, TRIM71 may be part of a family of mRNA repressors that regulate proliferation and differentiation. TRIM has been shown to negatively regulate stability of Lin28B, which inhibits the pre-let-7 miRNA precursor from maturing by recruiting the terminal uriyltransferase TUT4. This family also contains the Caenorhabditis elegans NHL repeat containing 1 (NHL-1), a RING-finger-containing protein that was shown to interact with E2 ubiquitin conjugating enzymes in two-hybrid screens. Its domain architecture resembles that of the E3 ubiquitin protein ligases TRIM2, TRIM32, and TRIM71. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271324 [Multi-domain] Cd Length: 285 Bit Score: 98.77 E-value: 1.54e-22
|
|||||||||||||||||||
| NHL_like_2 | cd14957 | Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
566-882 | 1.82e-22 | |||||||||||||||
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271327 [Multi-domain] Cd Length: 280 Bit Score: 98.49 E-value: 1.82e-22
|
|||||||||||||||||||
| NHL_like_1 | cd14953 | Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ... |
790-887 | 6.48e-22 | |||||||||||||||
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat domains is found in a variety of domain architectures. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271323 [Multi-domain] Cd Length: 323 Bit Score: 97.99 E-value: 6.48e-22
|
|||||||||||||||||||
| HAD_AtGPP-like | cd07529 | subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ... |
74-260 | 1.69e-21 | |||||||||||||||
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: 93.18 E-value: 1.69e-21
|
|||||||||||||||||||
| HAD_PPase | cd02616 | pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ... |
74-284 | 1.80e-21 | |||||||||||||||
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: 93.50 E-value: 1.80e-21
|
|||||||||||||||||||
| Bcp | COG1225 | Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
416-535 | 1.81e-21 | |||||||||||||||
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440838 [Multi-domain] Cd Length: 136 Bit Score: 91.47 E-value: 1.81e-21
|
|||||||||||||||||||
| NHL_like_4 | cd14955 | Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
568-881 | 1.20e-20 | |||||||||||||||
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271325 [Multi-domain] Cd Length: 279 Bit Score: 93.41 E-value: 1.20e-20
|
|||||||||||||||||||
| PLN02940 | PLN02940 | riboflavin kinase |
74-260 | 1.36e-20 | |||||||||||||||
riboflavin kinase Pssm-ID: 178528 [Multi-domain] Cd Length: 382 Bit Score: 95.29 E-value: 1.36e-20
|
|||||||||||||||||||
| Thioredoxin_8 | pfam13905 | Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ... |
419-514 | 1.23e-18 | |||||||||||||||
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Pssm-ID: 464033 [Multi-domain] Cd Length: 95 Bit Score: 81.97 E-value: 1.23e-18
|
|||||||||||||||||||
| Vgb | COG4257 | Streptogramin lyase [Defense mechanisms]; |
620-896 | 6.76e-18 | |||||||||||||||
Streptogramin lyase [Defense mechanisms]; Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 85.07 E-value: 6.76e-18
|
|||||||||||||||||||
| PRK10725 | PRK10725 | fructose-1-phosphate/6-phosphogluconate phosphatase; |
76-262 | 8.78e-18 | |||||||||||||||
fructose-1-phosphate/6-phosphogluconate phosphatase; Pssm-ID: 182679 [Multi-domain] Cd Length: 188 Bit Score: 82.43 E-value: 8.78e-18
|
|||||||||||||||||||
| NHL_like_6 | cd14962 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
578-884 | 2.61e-16 | |||||||||||||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271332 [Multi-domain] Cd Length: 271 Bit Score: 80.32 E-value: 2.61e-16
|
|||||||||||||||||||
| NHL_like_2 | cd14957 | Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
612-881 | 3.18e-16 | |||||||||||||||
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271327 [Multi-domain] Cd Length: 280 Bit Score: 80.39 E-value: 3.18e-16
|
|||||||||||||||||||
| PLN02770 | PLN02770 | haloacid dehalogenase-like hydrolase family protein |
76-279 | 7.79e-16 | |||||||||||||||
haloacid dehalogenase-like hydrolase family protein Pssm-ID: 215413 [Multi-domain] Cd Length: 248 Bit Score: 78.34 E-value: 7.79e-16
|
|||||||||||||||||||
| PRK13222 | PRK13222 | N-acetylmuramic acid 6-phosphate phosphatase MupP; |
76-260 | 2.00e-15 | |||||||||||||||
N-acetylmuramic acid 6-phosphate phosphatase MupP; Pssm-ID: 237310 [Multi-domain] Cd Length: 226 Bit Score: 76.77 E-value: 2.00e-15
|
|||||||||||||||||||
| HAD_PGPase | cd16417 | Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ... |
76-260 | 2.78e-15 | |||||||||||||||
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: 75.73 E-value: 2.78e-15
|
|||||||||||||||||||
| HAD_like | cd01427 | Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ... |
165-260 | 3.51e-15 | |||||||||||||||
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: 72.43 E-value: 3.51e-15
|
|||||||||||||||||||
| HAD_sEH-N_like | cd02603 | N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ... |
76-261 | 5.71e-15 | |||||||||||||||
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: 74.69 E-value: 5.71e-15
|
|||||||||||||||||||
| HAD_PGPase | cd07512 | haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ... |
76-280 | 2.28e-14 | |||||||||||||||
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter sphaeroides CbbZ; Phosphoglycolate phosphatase catalyzes the dephosphorylation of phosphoglycolate; its activity requires divalent cations, especially Mg++. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. Pssm-ID: 319815 [Multi-domain] Cd Length: 214 Bit Score: 73.12 E-value: 2.28e-14
|
|||||||||||||||||||
| PRK11587 | PRK11587 | putative phosphatase; Provisional |
78-261 | 6.31e-14 | |||||||||||||||
putative phosphatase; Provisional Pssm-ID: 183215 [Multi-domain] Cd Length: 218 Bit Score: 71.95 E-value: 6.31e-14
|
|||||||||||||||||||
| YncE | COG3391 | DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
578-771 | 3.96e-13 | |||||||||||||||
DNA-binding beta-propeller fold protein YncE [General function prediction only]; Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 70.11 E-value: 3.96e-13
|
|||||||||||||||||||
| NHL | cd05819 | NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ... |
801-907 | 9.93e-13 | |||||||||||||||
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats. Pssm-ID: 271320 [Multi-domain] Cd Length: 269 Bit Score: 69.65 E-value: 9.93e-13
|
|||||||||||||||||||
| NHL_like_3 | cd14956 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
673-881 | 1.33e-12 | |||||||||||||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271326 [Multi-domain] Cd Length: 274 Bit Score: 69.23 E-value: 1.33e-12
|
|||||||||||||||||||
| PRK10563 | PRK10563 | 6-phosphogluconate phosphatase; Provisional |
74-255 | 1.47e-12 | |||||||||||||||
6-phosphogluconate phosphatase; Provisional Pssm-ID: 182552 [Multi-domain] Cd Length: 221 Bit Score: 68.18 E-value: 1.47e-12
|
|||||||||||||||||||
| HAD_like | cd07533 | uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ... |
77-280 | 1.88e-12 | |||||||||||||||
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: 67.42 E-value: 1.88e-12
|
|||||||||||||||||||
| PLN02811 | PLN02811 | hydrolase |
156-260 | 5.58e-12 | |||||||||||||||
hydrolase Pssm-ID: 178407 [Multi-domain] Cd Length: 220 Bit Score: 66.32 E-value: 5.58e-12
|
|||||||||||||||||||
| NHL_like_5 | cd14963 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
681-887 | 1.21e-11 | |||||||||||||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271333 [Multi-domain] Cd Length: 268 Bit Score: 66.16 E-value: 1.21e-11
|
|||||||||||||||||||
| NHL_like_4 | cd14955 | Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
600-881 | 1.27e-11 | |||||||||||||||
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271325 [Multi-domain] Cd Length: 279 Bit Score: 66.45 E-value: 1.27e-11
|
|||||||||||||||||||
| HAD-SF-IA-v1 | TIGR01549 | haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ... |
76-254 | 1.43e-11 | |||||||||||||||
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions.The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)(D/E), (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity] Pssm-ID: 273686 [Multi-domain] Cd Length: 164 Bit Score: 63.95 E-value: 1.43e-11
|
|||||||||||||||||||
| PRK03147 | PRK03147 | thiol-disulfide oxidoreductase ResA; |
383-521 | 2.39e-11 | |||||||||||||||
thiol-disulfide oxidoreductase ResA; Pssm-ID: 179545 [Multi-domain] Cd Length: 173 Bit Score: 63.48 E-value: 2.39e-11
|
|||||||||||||||||||
| PRK13288 | PRK13288 | pyrophosphatase PpaX; Provisional |
72-264 | 4.99e-11 | |||||||||||||||
pyrophosphatase PpaX; Provisional Pssm-ID: 237336 [Multi-domain] Cd Length: 214 Bit Score: 63.51 E-value: 4.99e-11
|
|||||||||||||||||||
| PLN03243 | PLN03243 | haloacid dehalogenase-like hydrolase; Provisional |
151-263 | 5.34e-11 | |||||||||||||||
haloacid dehalogenase-like hydrolase; Provisional Pssm-ID: 215644 [Multi-domain] Cd Length: 260 Bit Score: 64.28 E-value: 5.34e-11
|
|||||||||||||||||||
| HAD_dREG-2_like | cd16415 | uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ... |
165-258 | 5.74e-11 | |||||||||||||||
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to uncharacterized Drosophila melanogaster rhythmically expressed gene 2 protein and human haloacid dehalogenase-like hydrolase domain-containing protein 3; The haloacid dehalogenase-like (HAD) hydrolases are a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. Pssm-ID: 319852 [Multi-domain] Cd Length: 128 Bit Score: 61.15 E-value: 5.74e-11
|
|||||||||||||||||||
| HAD_5NT | cd04302 | haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ... |
76-284 | 2.54e-10 | |||||||||||||||
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: 61.45 E-value: 2.54e-10
|
|||||||||||||||||||
| PRK13223 | PRK13223 | phosphoglycolate phosphatase; Provisional |
77-281 | 2.33e-09 | |||||||||||||||
phosphoglycolate phosphatase; Provisional Pssm-ID: 171912 [Multi-domain] Cd Length: 272 Bit Score: 59.49 E-value: 2.33e-09
|
|||||||||||||||||||
| Hydrolase_like | pfam13242 | HAD-hyrolase-like; |
217-282 | 2.50e-09 | |||||||||||||||
HAD-hyrolase-like; Pssm-ID: 433056 [Multi-domain] Cd Length: 75 Bit Score: 54.54 E-value: 2.50e-09
|
|||||||||||||||||||
| HAD_type_II | TIGR01428 | 2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ... |
75-256 | 3.84e-09 | |||||||||||||||
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Belongs to the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases (pfam00702), class (subfamily) I. Note that the Type I HAD enzymes have not yet been fully characterized, but clearly utilize a substantially different catalytic mechanism and are thus unlikely to be related. Pssm-ID: 130495 [Multi-domain] Cd Length: 198 Bit Score: 57.73 E-value: 3.84e-09
|
|||||||||||||||||||
| NHL_like_6 | cd14962 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
673-887 | 6.98e-09 | |||||||||||||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271332 [Multi-domain] Cd Length: 271 Bit Score: 57.98 E-value: 6.98e-09
|
|||||||||||||||||||
| NHL_like_1 | cd14953 | Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ... |
836-887 | 8.40e-09 | |||||||||||||||
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat domains is found in a variety of domain architectures. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271323 [Multi-domain] Cd Length: 323 Bit Score: 58.31 E-value: 8.40e-09
|
|||||||||||||||||||
| HAD_L2-DEX | cd02588 | L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ... |
162-258 | 1.85e-08 | |||||||||||||||
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: 56.12 E-value: 1.85e-08
|
|||||||||||||||||||
| NHL_like_6 | cd14962 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
569-664 | 1.89e-08 | |||||||||||||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271332 [Multi-domain] Cd Length: 271 Bit Score: 56.83 E-value: 1.89e-08
|
|||||||||||||||||||
| NHL_TRIM32_like | cd14961 | NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; ... |
576-878 | 3.97e-08 | |||||||||||||||
NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; The E3 ubiquitin-protein ligase TRIM32 (HT2A) is widely expressed and is responsible for ubiquinating a large variety of targets, including dysbindin (DTNBP1), NPHP7/Glis2, TAp73, and others. TRIM32 promotes disassociation of the plakoglobin-PI3K complex and reduces PI3K-Akt-FoxO signaling. Mutations in TRIM32 have been implemented in the two diverse diseases limb-girdle muscular dystrophy type 2H (LGMD2H) or sarcotubular myopathy (STM) and Bardet-Biedl syndrome type 11 (BBS11). The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271331 [Multi-domain] Cd Length: 273 Bit Score: 55.75 E-value: 3.97e-08
|
|||||||||||||||||||
| HisB1/GmhB | COG0241 | Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ... |
149-281 | 5.04e-08 | |||||||||||||||
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: 53.95 E-value: 5.04e-08
|
|||||||||||||||||||
| NHL_PKND_like | cd14952 | NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ... |
561-879 | 5.48e-08 | |||||||||||||||
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein with a cytosolic kinase domain and an extracellular sensor domain that contains NHL repeats. It plays a key role in the development of central nervous system tuberculosis, by mediating the invasion of host brain endothelia. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271322 [Multi-domain] Cd Length: 247 Bit Score: 54.91 E-value: 5.48e-08
|
|||||||||||||||||||
| YncE | COG3391 | DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
558-825 | 1.54e-07 | |||||||||||||||
DNA-binding beta-propeller fold protein YncE [General function prediction only]; Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 53.54 E-value: 1.54e-07
|
|||||||||||||||||||
| PRK13478 | PRK13478 | phosphonoacetaldehyde hydrolase; Provisional |
72-267 | 1.56e-07 | |||||||||||||||
phosphonoacetaldehyde hydrolase; Provisional Pssm-ID: 184075 [Multi-domain] Cd Length: 267 Bit Score: 54.10 E-value: 1.56e-07
|
|||||||||||||||||||
| NHL_TRIM71_like | cd14954 | NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ... |
598-887 | 1.91e-07 | |||||||||||||||
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; The E3 ubiquitin-protein ligase TRIM71 (LIN-41) is a RING-finger domain containing protein that has been associated with a variety of activities. The NHL repeat domain appears responsible for targeting TRIM71 to mRNAs, and TRIM71 appears responsible for translational repression and mRNA decay. Together with BRAT, TRIM71 may be part of a family of mRNA repressors that regulate proliferation and differentiation. TRIM has been shown to negatively regulate stability of Lin28B, which inhibits the pre-let-7 miRNA precursor from maturing by recruiting the terminal uriyltransferase TUT4. This family also contains the Caenorhabditis elegans NHL repeat containing 1 (NHL-1), a RING-finger-containing protein that was shown to interact with E2 ubiquitin conjugating enzymes in two-hybrid screens. Its domain architecture resembles that of the E3 ubiquitin protein ligases TRIM2, TRIM32, and TRIM71. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271324 [Multi-domain] Cd Length: 285 Bit Score: 53.71 E-value: 1.91e-07
|
|||||||||||||||||||
| PLN02575 | PLN02575 | haloacid dehalogenase-like hydrolase |
164-260 | 1.92e-07 | |||||||||||||||
haloacid dehalogenase-like hydrolase Pssm-ID: 215313 [Multi-domain] Cd Length: 381 Bit Score: 54.49 E-value: 1.92e-07
|
|||||||||||||||||||
| Redoxin | pfam08534 | Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. |
391-533 | 2.59e-07 | |||||||||||||||
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. Pssm-ID: 400717 [Multi-domain] Cd Length: 148 Bit Score: 51.22 E-value: 2.59e-07
|
|||||||||||||||||||
| YncE | COG3391 | DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
709-890 | 3.08e-07 | |||||||||||||||
DNA-binding beta-propeller fold protein YncE [General function prediction only]; Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 52.77 E-value: 3.08e-07
|
|||||||||||||||||||
| HAD_Neu5Ac-Pase_like | cd04305 | human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ... |
162-258 | 5.42e-07 | |||||||||||||||
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases; N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. Pssm-ID: 319800 [Multi-domain] Cd Length: 109 Bit Score: 49.08 E-value: 5.42e-07
|
|||||||||||||||||||
| HAD_PHN | cd02586 | Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; ... |
74-269 | 9.75e-07 | |||||||||||||||
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: 51.15 E-value: 9.75e-07
|
|||||||||||||||||||
| NHL_like_6 | cd14962 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
728-894 | 1.11e-06 | |||||||||||||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271332 [Multi-domain] Cd Length: 271 Bit Score: 51.43 E-value: 1.11e-06
|
|||||||||||||||||||
| YncE | COG3391 | DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
693-878 | 2.08e-06 | |||||||||||||||
DNA-binding beta-propeller fold protein YncE [General function prediction only]; Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 50.08 E-value: 2.08e-06
|
|||||||||||||||||||
| NHL_like_3 | cd14956 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
738-887 | 3.23e-06 | |||||||||||||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271326 [Multi-domain] Cd Length: 274 Bit Score: 49.97 E-value: 3.23e-06
|
|||||||||||||||||||
| TRX_family | cd02947 | TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ... |
412-532 | 3.60e-06 | |||||||||||||||
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins. Pssm-ID: 239245 [Multi-domain] Cd Length: 93 Bit Score: 46.40 E-value: 3.60e-06
|
|||||||||||||||||||
| NHL_PAL_like | cd14958 | Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ... |
578-881 | 8.03e-06 | |||||||||||||||
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the N-dealkylation of peptidyl-alpha-hydroxyglycine, which results in an alpha-amidated peptide and glyoxylate. Amidation of the C-terminus is required for the activity of many peptide hormones and neuropeptides. The catalytic residues of PAL are located on several NHL-repeats. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271328 [Multi-domain] Cd Length: 300 Bit Score: 48.80 E-value: 8.03e-06
|
|||||||||||||||||||
| HAD_PGPase | cd16421 | Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ... |
166-260 | 2.91e-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: 43.98 E-value: 2.91e-05
|
|||||||||||||||||||
| HAD_PPase | cd07509 | inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ... |
217-262 | 3.40e-05 | |||||||||||||||
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP); LHPP hydrolyzes nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate as well as oxygen-phosphorus bonds in inorganic pyrophosphate in vitro. This family also includes human haloacid dehalogenase like hydrolase domain containing 2 protine (HDHD2) a phosphatase which may be involved in polygenic hypertension. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. Pssm-ID: 319812 [Multi-domain] Cd Length: 248 Bit Score: 46.50 E-value: 3.40e-05
|
|||||||||||||||||||
| TlpA_like_ScsD_MtbDsbE | cd03011 | TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ... |
406-514 | 3.84e-05 | |||||||||||||||
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE homolog subfamily; composed of ScsD, the DsbE homolog of Mycobacterium tuberculosis (MtbDsbE) and similar proteins, all containing a redox-active CXXC motif. The Salmonella typhimurium ScsD is a thioredoxin-like protein which confers copper tolerance to copper-sensitive mutants of E. coli. MtbDsbE has been characterized as an oxidase in vitro, catalyzing the disulfide bond formation of substrates like hirudin. The reduced form of MtbDsbE is more stable than its oxidized form, consistent with an oxidase function. This is in contrast to the function of DsbE from gram-negative bacteria which is a specific reductase of apocytochrome c. Pssm-ID: 239309 [Multi-domain] Cd Length: 123 Bit Score: 44.21 E-value: 3.84e-05
|
|||||||||||||||||||
| AhpC-TSA | pfam00578 | AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ... |
416-517 | 6.88e-05 | |||||||||||||||
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA). Pssm-ID: 425763 [Multi-domain] Cd Length: 124 Bit Score: 43.37 E-value: 6.88e-05
|
|||||||||||||||||||
| NHL_TRIM2_like | cd14960 | NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; ... |
582-704 | 9.46e-05 | |||||||||||||||
NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; The E3 ubiquitin-protein ligase TRIM2 is responsible for ubiquinating the apoptosis-inducing Bcl-2-interacting mediator of cell death (Bim), when the latter is phosphorylated by p42/p44 MAPK. TRIM2 regulates the ubiquitination of neurofilament light subunit (NF-L), deficiencies in TRIM2 result in increased NF-L levels in axons and subsequent axonopathy. TRIM2 is also involved in regulating axon outgrowth during development; it contains RING and BBOX domains, the NHL repeat domain is located at its C-terminus. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271330 [Multi-domain] Cd Length: 274 Bit Score: 45.41 E-value: 9.46e-05
|
|||||||||||||||||||
| YvrE | COG3386 | Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ... |
798-890 | 1.92e-04 | |||||||||||||||
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway Pssm-ID: 442613 [Multi-domain] Cd Length: 266 Bit Score: 44.50 E-value: 1.92e-04
|
|||||||||||||||||||
| NHL_like_3 | cd14956 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
805-907 | 2.46e-04 | |||||||||||||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271326 [Multi-domain] Cd Length: 274 Bit Score: 44.20 E-value: 2.46e-04
|
|||||||||||||||||||
| NHL_TRIM2_like | cd14960 | NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; ... |
782-881 | 4.20e-04 | |||||||||||||||
NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; The E3 ubiquitin-protein ligase TRIM2 is responsible for ubiquinating the apoptosis-inducing Bcl-2-interacting mediator of cell death (Bim), when the latter is phosphorylated by p42/p44 MAPK. TRIM2 regulates the ubiquitination of neurofilament light subunit (NF-L), deficiencies in TRIM2 result in increased NF-L levels in axons and subsequent axonopathy. TRIM2 is also involved in regulating axon outgrowth during development; it contains RING and BBOX domains, the NHL repeat domain is located at its C-terminus. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271330 [Multi-domain] Cd Length: 274 Bit Score: 43.49 E-value: 4.20e-04
|
|||||||||||||||||||
| PRK08942 | PRK08942 | D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase; |
163-281 | 6.52e-04 | |||||||||||||||
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase; Pssm-ID: 236354 [Multi-domain] Cd Length: 181 Bit Score: 41.73 E-value: 6.52e-04
|
|||||||||||||||||||
| NHL_TRIM32_like | cd14961 | NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; ... |
730-881 | 7.42e-04 | |||||||||||||||
NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; The E3 ubiquitin-protein ligase TRIM32 (HT2A) is widely expressed and is responsible for ubiquinating a large variety of targets, including dysbindin (DTNBP1), NPHP7/Glis2, TAp73, and others. TRIM32 promotes disassociation of the plakoglobin-PI3K complex and reduces PI3K-Akt-FoxO signaling. Mutations in TRIM32 have been implemented in the two diverse diseases limb-girdle muscular dystrophy type 2H (LGMD2H) or sarcotubular myopathy (STM) and Bardet-Biedl syndrome type 11 (BBS11). The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271331 [Multi-domain] Cd Length: 273 Bit Score: 42.65 E-value: 7.42e-04
|
|||||||||||||||||||
| PQQ_ABC_repeats | TIGR03866 | PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ... |
741-885 | 8.99e-04 | |||||||||||||||
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family consist of seven repeats each of the YVTN family beta-propeller repeat (see TIGR02276). Members occur invariably as part of a transport operon that is associated with PQQ-dependent catabolism of alcohols such as phenylethanol. Pssm-ID: 274824 [Multi-domain] Cd Length: 310 Bit Score: 42.72 E-value: 8.99e-04
|
|||||||||||||||||||
| TlpA_like_DsbE | cd03010 | TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ... |
396-520 | 1.20e-03 | |||||||||||||||
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, periplasmic TRX-like reductase containing a CXXC motif that specifically donates reducing equivalents to apocytochrome c via CcmH, another cytochrome c maturation (Ccm) factor with a redox active CXXC motif. Assembly of cytochrome c requires the ligation of heme to reduced thiols of the apocytochrome. In bacteria, this assembly occurs in the periplasm. The reductase activity of DsbE in the oxidizing environment of the periplasm is crucial in the maturation of cytochrome c. Pssm-ID: 239308 [Multi-domain] Cd Length: 127 Bit Score: 39.87 E-value: 1.20e-03
|
|||||||||||||||||||
| PTZ00051 | PTZ00051 | thioredoxin; Provisional |
408-520 | 2.46e-03 | |||||||||||||||
thioredoxin; Provisional Pssm-ID: 173347 [Multi-domain] Cd Length: 98 Bit Score: 38.32 E-value: 2.46e-03
|
|||||||||||||||||||
| serB | TIGR00338 | phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ... |
76-242 | 2.58e-03 | |||||||||||||||
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction 3-phospho-serine + H2O = L-serine + phosphate. It catalyzes the last of three steps in the biosynthesis of serine from D-3-phosphoglycerate. Note that this enzyme acts on free phosphoserine, not on phosphoserine residues of phosphoproteins. [Amino acid biosynthesis, Serine family] Pssm-ID: 273022 [Multi-domain] Cd Length: 219 Bit Score: 40.42 E-value: 2.58e-03
|
|||||||||||||||||||
| NHL | pfam01436 | NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ... |
857-882 | 4.34e-03 | |||||||||||||||
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is about 40 residues long and resembles the WD repeat pfam00400. The repeats have a catalytic activity in Swiss:P10731, proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Swiss:Q13049 interacts with the activation domain of Tat. This interaction is me diated by the NHL repeats. Pssm-ID: 396153 [Multi-domain] Cd Length: 28 Bit Score: 35.46 E-value: 4.34e-03
|
|||||||||||||||||||
| NHL | pfam01436 | NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ... |
622-648 | 4.65e-03 | |||||||||||||||
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is about 40 residues long and resembles the WD repeat pfam00400. The repeats have a catalytic activity in Swiss:P10731, proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Swiss:Q13049 interacts with the activation domain of Tat. This interaction is me diated by the NHL repeats. Pssm-ID: 396153 [Multi-domain] Cd Length: 28 Bit Score: 35.46 E-value: 4.65e-03
|
|||||||||||||||||||
| LY | smart00135 | Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) ... |
560-600 | 5.41e-03 | |||||||||||||||
Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. Also present in a variety of molecules similar to gp300/megalin. Pssm-ID: 214531 [Multi-domain] Cd Length: 43 Bit Score: 35.66 E-value: 5.41e-03
|
|||||||||||||||||||
| NHL_TRIM32_like | cd14961 | NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; ... |
622-898 | 7.94e-03 | |||||||||||||||
NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; The E3 ubiquitin-protein ligase TRIM32 (HT2A) is widely expressed and is responsible for ubiquinating a large variety of targets, including dysbindin (DTNBP1), NPHP7/Glis2, TAp73, and others. TRIM32 promotes disassociation of the plakoglobin-PI3K complex and reduces PI3K-Akt-FoxO signaling. Mutations in TRIM32 have been implemented in the two diverse diseases limb-girdle muscular dystrophy type 2H (LGMD2H) or sarcotubular myopathy (STM) and Bardet-Biedl syndrome type 11 (BBS11). The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271331 [Multi-domain] Cd Length: 273 Bit Score: 39.57 E-value: 7.94e-03
|
|||||||||||||||||||
| Blast search parameters | ||||
|
