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Conserved domains on  [gi|1779413605|emb|VUD39624|]
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hypothetical protein [Peduovirus P24C9]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 34-133 3.60e-06

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: 45.46  E-value: 3.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779413605  34 LRKLFAFLSSKGIKVIFLTNKNRNVRTHdgivTLDEYLKRKFPESIHFCRELDNNIPAkqtGKAIDFIMAALELKRNEMI 113
Cdd:cd01427    12 AVELLKRLRAAGIKLAIVTNRSREALRA----LLEKLGLGDLFDGIIGSDGGGTPKPK---PKPLLLLLLKLGVDPEEVL 84

                          90       100
                  ....*....|....*....|
gi 1779413605 114 YVGRSQEDLQAATNGNTLFI 133
Cdd:cd01427    85 FVGDSENDIEAARAAGGRTV 104
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 319-360 2.11e-05

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


:

Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 43.92  E-value: 2.11e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1779413605 319 PPKLKGKKILVIDDFCTEGNAHETARMYLKAAGANVINISWL 360
Cdd:cd06223    66 GGDVKGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVL 107
 
Name Accession Description Interval E-value
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 34-133 3.60e-06

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: 45.46  E-value: 3.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779413605  34 LRKLFAFLSSKGIKVIFLTNKNRNVRTHdgivTLDEYLKRKFPESIHFCRELDNNIPAkqtGKAIDFIMAALELKRNEMI 113
Cdd:cd01427    12 AVELLKRLRAAGIKLAIVTNRSREALRA----LLEKLGLGDLFDGIIGSDGGGTPKPK---PKPLLLLLLKLGVDPEEVL 84

                          90       100
                  ....*....|....*....|
gi 1779413605 114 YVGRSQEDLQAATNGNTLFI 133
Cdd:cd01427    85 FVGDSENDIEAARAAGGRTV 104
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 319-360 2.11e-05

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 43.92  E-value: 2.11e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1779413605 319 PPKLKGKKILVIDDFCTEGNAHETARMYLKAAGANVINISWL 360
Cdd:cd06223    66 GGDVKGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVL 107
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
35-159 1.28e-04

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 42.99  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779413605  35 RKLFAFLSSKGIKVIFLTNKNRN-----VRTH------DGIVTLDEYLKRK-FPESIHFcreldnnipakqtgkaidfIM 102
Cdd:COG0546    90 RELLEALKARGIKLAVVTNKPREfaerlLEALglddyfDAIVGGDDVPPAKpKPEPLLE-------------------AL 150

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1779413605 103 AALELKRNEMIYVGRSQEDLQAATNGNTLFINATW----YEPVTEYG--FQFSEPKEIARFID 159
Cdd:COG0546   151 ERLGLDPEEVLMVGDSPHDIEAARAAGVPFIGVTWgygsAEELEAAGadYVIDSLAELLALLA 213
 
Name Accession Description Interval E-value
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 34-133 3.60e-06

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: 45.46  E-value: 3.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779413605  34 LRKLFAFLSSKGIKVIFLTNKNRNVRTHdgivTLDEYLKRKFPESIHFCRELDNNIPAkqtGKAIDFIMAALELKRNEMI 113
Cdd:cd01427    12 AVELLKRLRAAGIKLAIVTNRSREALRA----LLEKLGLGDLFDGIIGSDGGGTPKPK---PKPLLLLLLKLGVDPEEVL 84

                          90       100
                  ....*....|....*....|
gi 1779413605 114 YVGRSQEDLQAATNGNTLFI 133
Cdd:cd01427    85 FVGDSENDIEAARAAGGRTV 104
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 319-360 2.11e-05

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 43.92  E-value: 2.11e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1779413605 319 PPKLKGKKILVIDDFCTEGNAHETARMYLKAAGANVINISWL 360
Cdd:cd06223    66 GGDVKGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVL 107
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
35-159 1.28e-04

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 42.99  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779413605  35 RKLFAFLSSKGIKVIFLTNKNRN-----VRTH------DGIVTLDEYLKRK-FPESIHFcreldnnipakqtgkaidfIM 102
Cdd:COG0546    90 RELLEALKARGIKLAVVTNKPREfaerlLEALglddyfDAIVGGDDVPPAKpKPEPLLE-------------------AL 150

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1779413605 103 AALELKRNEMIYVGRSQEDLQAATNGNTLFINATW----YEPVTEYG--FQFSEPKEIARFID 159
Cdd:COG0546   151 ERLGLDPEEVLMVGDSPHDIEAARAAGVPFIGVTWgygsAEELEAAGadYVIDSLAELLALLA 213
 
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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