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Conserved domains on  [gi|15600109|ref|NP_253603|]
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hypothetical protein PA4916 [Pseudomonas aeruginosa PAO1]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NUDIX_NadM_like cd18873
bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase and similar proteins; ...
 9-139 6.60e-36

bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase and similar proteins; Bacterial NadM-Nudix is a bifunctional enzyme containing a nicotinamide mononucleotide (NMN) adenylyltransferase (NMNAT) and an ADP-ribose pyrophosphatase (ADPRase) domain. NMNAT was initially identified as an NAD+ synthase that catalyzes the reversible conversion of NMN to NAD+ in the final step of both the de novo biosynthesis and salvage pathways in most organisms across all three kingdoms of life ADPRase is a member of the NUDIX family proteins, catalyzes the metal-induced and concerted general acid-base hydrolysis of ADP ribose (ADPR) into AMP and ribose-5'-phosphate (R5P). Additional members in this cd include bacterial transcriptional regulator, NrtR, which represses the transcription of NAD biosynthetic genes in vitro and adenosine diphosphate ribose (ADPR), as well as NadQ, a NUDIX-like ATP-responsive regulator of NAD biosynthesis. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belong to this superfamily requires a divalent cation, such as Mg2+ or Mn2+ for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, U=I, L or V) which functions as metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.


:

Pssm-ID: 467585 [Multi-domain]  Cd Length: 132  Bit Score: 123.42  E-value: 6.60e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600109   9 SVDIVALRLNpGHGLELLLIRRAQAPFAGQWALPGVLVNgrsADHSLDDAAVRALRDKARLEPAYIEQVATVGNAVRDPR 88
Cdd:cd18873   4 TVDCVIFGFD-DGELKVLLIKRKNEPFKGGWALPGGFVR---EDETLEDAARRELREETGLKDIYLEQLGTFGDPDRDPR 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15600109  89 GWSLSVFYLVLV--GPDTQVEDDDLDFVPLRDVRSERFALPFDHAQLVQQACE 139
Cdd:cd18873  80 GRVISVAYLALVpeEDLAPKAGDDAAEARWFPVDELLPPLAFDHAEIIADALE 132
 
Name Accession Description Interval E-value
NUDIX_NadM_like cd18873
bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase and similar proteins; ...
 9-139 6.60e-36

bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase and similar proteins; Bacterial NadM-Nudix is a bifunctional enzyme containing a nicotinamide mononucleotide (NMN) adenylyltransferase (NMNAT) and an ADP-ribose pyrophosphatase (ADPRase) domain. NMNAT was initially identified as an NAD+ synthase that catalyzes the reversible conversion of NMN to NAD+ in the final step of both the de novo biosynthesis and salvage pathways in most organisms across all three kingdoms of life ADPRase is a member of the NUDIX family proteins, catalyzes the metal-induced and concerted general acid-base hydrolysis of ADP ribose (ADPR) into AMP and ribose-5'-phosphate (R5P). Additional members in this cd include bacterial transcriptional regulator, NrtR, which represses the transcription of NAD biosynthetic genes in vitro and adenosine diphosphate ribose (ADPR), as well as NadQ, a NUDIX-like ATP-responsive regulator of NAD biosynthesis. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belong to this superfamily requires a divalent cation, such as Mg2+ or Mn2+ for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, U=I, L or V) which functions as metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.


Pssm-ID: 467585 [Multi-domain]  Cd Length: 132  Bit Score: 123.42  E-value: 6.60e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600109   9 SVDIVALRLNpGHGLELLLIRRAQAPFAGQWALPGVLVNgrsADHSLDDAAVRALRDKARLEPAYIEQVATVGNAVRDPR 88
Cdd:cd18873   4 TVDCVIFGFD-DGELKVLLIKRKNEPFKGGWALPGGFVR---EDETLEDAARRELREETGLKDIYLEQLGTFGDPDRDPR 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15600109  89 GWSLSVFYLVLV--GPDTQVEDDDLDFVPLRDVRSERFALPFDHAQLVQQACE 139
Cdd:cd18873  80 GRVISVAYLALVpeEDLAPKAGDDAAEARWFPVDELLPPLAFDHAEIIADALE 132
COG4111 COG4111
Uncharacterized conserved protein [Function unknown];
40-208 2.11e-34

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443287 [Multi-domain]  Cd Length: 170  Bit Score: 120.66  E-value: 2.11e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600109  40 ALPGVLVNgrsADHSLDDAAVRALRDKARLEPAYIEQVATVGNAVRDPRGWSLSVFYLVLVGPDTQV--EDDDLDFVPLR 117
Cdd:COG4111   1 ALPGGFVR---EHESLEDAARRWLAEQTGLELGYLEQLYTFGDPDRDPRGRVISVAYLALVREEELRadDADDAAWFPVD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600109 118 DVRSerfaLPFDHAQLVQQACERLASKSVYSALPLFLLAPRFTVAEALKAFECAIGQEVQHSSLRGRLERMkeaGWVEDT 197
Cdd:COG4111  78 ELPP----LAFDHRRILATALERLRAKLEYTPIGFELLPEKFTLSELQRLYEAILGRKLDKRNFRRKILSL---GLLEET 150

                       170
                ....*....|.
gi 15600109 198 GERQRPPMGRP 208
Cdd:COG4111 151 GEKQTGGAGRP 161
PRK05379 PRK05379
bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;
20-135 6.43e-05

bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;


Pssm-ID: 235436 [Multi-domain]  Cd Length: 340  Bit Score: 43.08  E-value: 6.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600109   20 GHgleLLLIRRAQAPFAGQWALPGVLVNgrsADHSLDDAAVRALRDKARLE-PAYIEQVATVGNAVRDPRGWSL------ 92
Cdd:PRK05379 214 GH---VLLVRRRAEPGKGLWALPGGFLE---QDETLLDACLRELREETGLKlPEPVLRGSIRDQQVFDHPGRSLrgrtit 287

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 15600109   93 SVFYLVLVG---PDTQVEDDDLDF--VPLRDVRSERFALPFDHAQLVQ 135
Cdd:PRK05379 288 HAFLFEFPAgelPRVKGGDDADKArwVPLAELLAMRDRMFEDHFQIIT 335
NUDIX pfam00293
NUDIX domain;
10-125 1.12e-04

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 40.93  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600109    10 VDIVALRLNPGHglELLLIRRAQAPFAGQWALPGVLVNgrsADHSLDDAAVRALRDKARLEPAYIEQVATVGNAV----R 85
Cdd:pfam00293   4 VAVGVVLLNEKG--RVLLVRRSKKPFPGWWSLPGGKVE---PGETPEEAARRELEEETGLEPELLELLGSLHYLApfdgR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 15600109    86 DPRGWSLSVFYLVLVG----PDTQVEDDDLDFVPLRDVRSERFA 125
Cdd:pfam00293  79 FPDEHEILYVFLAEVEgelePDPDGEVEEVRWVPLEELLLLKLA 122
 
Name Accession Description Interval E-value
NUDIX_NadM_like cd18873
bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase and similar proteins; ...
 9-139 6.60e-36

bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase and similar proteins; Bacterial NadM-Nudix is a bifunctional enzyme containing a nicotinamide mononucleotide (NMN) adenylyltransferase (NMNAT) and an ADP-ribose pyrophosphatase (ADPRase) domain. NMNAT was initially identified as an NAD+ synthase that catalyzes the reversible conversion of NMN to NAD+ in the final step of both the de novo biosynthesis and salvage pathways in most organisms across all three kingdoms of life ADPRase is a member of the NUDIX family proteins, catalyzes the metal-induced and concerted general acid-base hydrolysis of ADP ribose (ADPR) into AMP and ribose-5'-phosphate (R5P). Additional members in this cd include bacterial transcriptional regulator, NrtR, which represses the transcription of NAD biosynthetic genes in vitro and adenosine diphosphate ribose (ADPR), as well as NadQ, a NUDIX-like ATP-responsive regulator of NAD biosynthesis. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belong to this superfamily requires a divalent cation, such as Mg2+ or Mn2+ for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, U=I, L or V) which functions as metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.


Pssm-ID: 467585 [Multi-domain]  Cd Length: 132  Bit Score: 123.42  E-value: 6.60e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600109   9 SVDIVALRLNpGHGLELLLIRRAQAPFAGQWALPGVLVNgrsADHSLDDAAVRALRDKARLEPAYIEQVATVGNAVRDPR 88
Cdd:cd18873   4 TVDCVIFGFD-DGELKVLLIKRKNEPFKGGWALPGGFVR---EDETLEDAARRELREETGLKDIYLEQLGTFGDPDRDPR 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15600109  89 GWSLSVFYLVLV--GPDTQVEDDDLDFVPLRDVRSERFALPFDHAQLVQQACE 139
Cdd:cd18873  80 GRVISVAYLALVpeEDLAPKAGDDAAEARWFPVDELLPPLAFDHAEIIADALE 132
COG4111 COG4111
Uncharacterized conserved protein [Function unknown];
40-208 2.11e-34

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443287 [Multi-domain]  Cd Length: 170  Bit Score: 120.66  E-value: 2.11e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600109  40 ALPGVLVNgrsADHSLDDAAVRALRDKARLEPAYIEQVATVGNAVRDPRGWSLSVFYLVLVGPDTQV--EDDDLDFVPLR 117
Cdd:COG4111   1 ALPGGFVR---EHESLEDAARRWLAEQTGLELGYLEQLYTFGDPDRDPRGRVISVAYLALVREEELRadDADDAAWFPVD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600109 118 DVRSerfaLPFDHAQLVQQACERLASKSVYSALPLFLLAPRFTVAEALKAFECAIGQEVQHSSLRGRLERMkeaGWVEDT 197
Cdd:COG4111  78 ELPP----LAFDHRRILATALERLRAKLEYTPIGFELLPEKFTLSELQRLYEAILGRKLDKRNFRRKILSL---GLLEET 150

                       170
                ....*....|.
gi 15600109 198 GERQRPPMGRP 208
Cdd:COG4111 151 GEKQTGGAGRP 161
YjhB COG1051
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];
20-133 7.92e-14

ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];


Pssm-ID: 440671 [Multi-domain]  Cd Length: 125  Bit Score: 65.77  E-value: 7.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600109  20 GHGLELLLIRRAQAPFAGQWALPGVLVNgrsADHSLDDAAVRALRDKARLEPAYIEQVATVGNavrDPRGWSLSVFYLVL 99
Cdd:COG1051  15 RKDGRVLLVRRADEPGKGLWALPGGKVE---PGETPEEAALRELREETGLEVEVLELLGVFDH---PDRGHVVSVAFLAE 88

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15600109 100 VG---PDTQVEDDDLDFVPLRDVRSERFAlPFDHAQL 133
Cdd:COG1051  89 VLsgePRADDEIDEARWFPLDELPELAFT-PADHEIL 124
NUDIX_Hydrolase cd04681
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 24-127 4.09e-07

uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase.


Pssm-ID: 467564 [Multi-domain]  Cd Length: 135  Bit Score: 47.56  E-value: 4.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600109  24 ELLLIRRAQAPFAGQWALPGVLVNgrsADHSLDDAAVRALRDKARLEPAYIEQVATVGNA-------VRdprgwSLSVFY 96
Cdd:cd04681  18 EILFVRRAKEPGKGKLDLPGGFVD---PGESAEEALRRELREELGLKIPKLRYLCSLPNTylykgitYK-----TCDLFF 89

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15600109  97 LVLV--GPDTQVEDDDLD---FVPLRDVRSERFALP 127
Cdd:cd04681  90 TAELdeKPKLKKAEDEVAeleWLDLEEIEPEKLAFP 125
NUDIX_ADPRase cd04673
ADP-ribose pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1.13) catalyzes the ...
 21-137 5.92e-07

ADP-ribose pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1.13) catalyzes the hydrolysis of ADP-ribose to AMP and ribose-5-P. Like other members of the NUDIX hydrolase superfamily of enzymes, it is thought to require a divalent cation, such as Mg2+, for its activity. It also contains a 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the NUDIX motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. In humans, there are four distinct ADPRase activities, three putative cytosolic (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). ADPRase-m is also known as NUDT9. It can be distinugished from the cytosolic ADPRase by a N-terminal target sequence unique to mitochondrial ADPRase. NUDT9 functions as a monomer.


Pssm-ID: 467557 [Multi-domain]  Cd Length: 128  Bit Score: 47.12  E-value: 5.92e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600109  21 HGLELLLIRRAQAPFAGQWALPGVLVNgrsADHSLDDAAVRALRDKARLEPAYIEQVATVGNAVRDPRG-----WSLSVF 95
Cdd:cd04673  10 RDGRVLLVRRGNPPDAGLWSFPGGKVE---LGETLEDAALRELREETGLEAEVVGLLTVVDVIERDEAGrvrfhYVILDF 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15600109  96 YLVLVGPDTQVEDD--DLDFVPLRDVRseRFALPFDHAQLVQQA 137
Cdd:cd04673  87 LAEWVSGEPVAGDDalDARWFSLEELD--GLPLTPGTRDVLERA 128
NUDIX_Hydrolase cd02883
NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three ...
 24-110 1.18e-06

NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase.


Pssm-ID: 467528 [Multi-domain]  Cd Length: 106  Bit Score: 45.86  E-value: 1.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600109  24 ELLLIRRAQAPFAGQWALPGvlvnGR-SADHSLDDAAVRALRDKARLEPAYIEQVATVGNAVRDPRGWSLSVFYLVLVGP 102
Cdd:cd02883  13 RVLLVRRSDGPGPGGWELPG----GGvEPGETPEEAAVREVREETGLDVEVLRLLGVYEFPDPDEGRHVVVLVFLARVVG 88


                ....*...
gi 15600109 103 DTQVEDDD 110
Cdd:cd02883  89 GEPPPLDD 96
PRK05379 PRK05379
bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;
20-135 6.43e-05

bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;


Pssm-ID: 235436 [Multi-domain]  Cd Length: 340  Bit Score: 43.08  E-value: 6.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600109   20 GHgleLLLIRRAQAPFAGQWALPGVLVNgrsADHSLDDAAVRALRDKARLE-PAYIEQVATVGNAVRDPRGWSL------ 92
Cdd:PRK05379 214 GH---VLLVRRRAEPGKGLWALPGGFLE---QDETLLDACLRELREETGLKlPEPVLRGSIRDQQVFDHPGRSLrgrtit 287

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 15600109   93 SVFYLVLVG---PDTQVEDDDLDF--VPLRDVRSERFALPFDHAQLVQ 135
Cdd:PRK05379 288 HAFLFEFPAgelPRVKGGDDADKArwVPLAELLAMRDRMFEDHFQIIT 335
NUDIX pfam00293
NUDIX domain;
10-125 1.12e-04

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 40.93  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600109    10 VDIVALRLNPGHglELLLIRRAQAPFAGQWALPGVLVNgrsADHSLDDAAVRALRDKARLEPAYIEQVATVGNAV----R 85
Cdd:pfam00293   4 VAVGVVLLNEKG--RVLLVRRSKKPFPGWWSLPGGKVE---PGETPEEAARRELEEETGLEPELLELLGSLHYLApfdgR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 15600109    86 DPRGWSLSVFYLVLVG----PDTQVEDDDLDFVPLRDVRSERFA 125
Cdd:pfam00293  79 FPDEHEILYVFLAEVEgelePDPDGEVEEVRWVPLEELLLLKLA 122
NUDIX_ADPRase cd04691
ADP-ribose pyrophosphatase and similar proteins; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1. ...
 26-121 3.53e-04

ADP-ribose pyrophosphatase and similar proteins; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1.13) catalyzes the hydrolysis of ADP-ribose to AMP and ribose-5-P. Like other members of the NUDIX hydrolase superfamily of enzymes, it is thought to require a divalent cation, such as Mg2+, for its activity. It also contains a 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the NUDIX motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. In humans, there are four distinct ADPRase activities, three putative cytosolic (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). ADPRase-m is also known as NUDT9. It can be distinugished from the cytosolic ADPRase by a N-terminal target sequence unique to mitochondrial ADPRase. NUDT9 functions as a monomer.


Pssm-ID: 467573 [Multi-domain]  Cd Length: 122  Bit Score: 39.21  E-value: 3.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600109  26 LLIRRAQAPFAGQWALPGVLVNgrsADHSLDDAAVRALRDKARLEpayieqvATVGN--AVRD-PRGWSLS----VFYLV 98
Cdd:cd04691  15 LLVKRAYGPGKGRWTLPGGFVE---EGETLDEAIVREVLEETGID-------AKPVGiiGVRSgVIRDGKSdnyvVFLLE 84

                        90       100
                ....*....|....*....|....*.
gi 15600109  99 LVGPDTQV---EDDDLDFVPLRDVRS 121
Cdd:cd04691  85 YVGGEPKPderENSEAGFLTLEEALA 110
NUDIX_Hydrolase cd04674
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 13-108 1.47e-03

uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase.


Pssm-ID: 467558 [Multi-domain]  Cd Length: 118  Bit Score: 37.44  E-value: 1.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600109  13 VALRLNPGHGlELLLIRRAQAPFAGQWALPGVLVNgrsADHSLDDAAVRALRDKA--RLEPAYIEQVATVGnavrDPRGw 90
Cdd:cd04674   6 VVVALLPVRD-GLLVIRRGIEPGHGELALPGGYIE---YGETWQEAAVRELREETgvEADAAEVRLFAVRS----APDG- 76

                        90
                ....*....|....*...
gi 15600109  91 SLSVFylvLVGPDTQVED 108
Cdd:cd04674  77 TLLIF---GLLPERPVAD 91
NUDIX_CoAse_Nudt7 cd03426
coenzyme A pyrophosphatase and similar proteins; Coenzyme A pyrophosphatase (CoAse; EC 3.6.1.1) ...
 8-61 3.62e-03

coenzyme A pyrophosphatase and similar proteins; Coenzyme A pyrophosphatase (CoAse; EC 3.6.1.1), also called nucleoside diphosphate-linked moiety X)) motif 7, is a member of the NUDIX hydrolase superfamily, functions to catalyze the elimination of oxidized inactive CoA, which can inhibit CoA-utilizing enzymes. The need of CoAses mainly arises under conditions of oxidative stress. CoAse has a conserved NUDIX fold and requires a single divalent cation for catalysis. In addition to a signature NUDIX motif G[X5]E[X7]REUXEEXGU, where U is Ile, Leu, or Val, CoAse contains an additional motif upstream called the NuCoA motif (LLTXT(SA)X3RX3GX3FPGG) which is postulated to be involved in CoA recognition. CoA plays a central role in lipid metabolism. It is involved in the initial steps of fatty acid sythesis in the cytosol, in the oxidation of fatty acids and the citric acid cycle in the mitochondria, and in the oxidation of long-chain fatty acids in peroxisomes. CoA has the important role of activating fatty acids for further modification into key biological signalling molecules.


Pssm-ID: 467532 [Multi-domain]  Cd Length: 158  Bit Score: 36.70  E-value: 3.62e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15600109   8 ASVdIVALRLNPGhGLELLLIRRAQ--APFAGQWALPGvlvnGR--SADHSLDDAAVR 61
Cdd:cd03426   3 AAV-LIPLVEGDG-ELHVLLTKRAShlRSHPGQIAFPG----GKrePGDESPVETALR 54
 
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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