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Conserved domains on  [gi|2327535425|pdb|7Q94|B]
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Chain B, NADQ transcription factor

Protein Classification

NUDIX hydrolase( domain architecture ID 10008291)

NUDIX hydrolase catalyzes the hydrolysis of nucleoside diphosphates linked to other moieties (X); it requires a divalent cation, such as Mg2+ or Mn2+ for its activity

CATH:  3.90.79.10
EC:  3.6.1.-
Gene Ontology:  GO:0016817|GO:0009132|GO:0046872
PubMed:  15581572|16378245|27936487
SCOP:  3000098

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4111 COG4111
Uncharacterized conserved protein [Function unknown];
68-317 1.02e-68

Uncharacterized conserved protein [Function unknown];


:

Pssm-ID: 443287 [Multi-domain]  Cd Length: 170  Bit Score: 212.34  E-value: 1.02e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Q94_B       68 ALPSGPFEfGHRTLQSGLREWIHEQTHHPVGYLEQLYTFADRDRNNeilGGRTISIGYLGLVREQEapsgksafwhgwye 147
Cdd:COG4111   1 ALPGGFVR-EHESLEDAARRWLAEQTGLELGYLEQLYTFGDPDRDP---RGRVISVAYLALVREEE-------------- 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Q94_B      148 yfpwedhrqgrpdildsiidklrawadsepdsraqrhLRADFTfglDGGGWNEELTLqryellyeaglvgeaqseprinf 227
Cdd:COG4111  63 -------------------------------------LRADDA---DDAAWFPVDEL----------------------- 79

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Q94_B      228 gRPMFADHRRILATGIARLRAKIKYRPVVFELMADSFTLLQLQRAIEALAGLTLHKQNFRRLIEQQQLVEETGDMATETG 307
Cdd:COG4111  80 -PPLAFDHRRILATALERLRAKLEYTPIGFELLPEKFTLSELQRLYEAILGRKLDKRNFRRKILSLGLLEETGEKQTGGA 158

                       250
                ....*....|
7Q94_B      308 GRPAKLFRFR 317
Cdd:COG4111 159 GRPAKLYRFD 168
 
Name Accession Description Interval E-value
COG4111 COG4111
Uncharacterized conserved protein [Function unknown];
68-317 1.02e-68

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443287 [Multi-domain]  Cd Length: 170  Bit Score: 212.34  E-value: 1.02e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Q94_B       68 ALPSGPFEfGHRTLQSGLREWIHEQTHHPVGYLEQLYTFADRDRNNeilGGRTISIGYLGLVREQEapsgksafwhgwye 147
Cdd:COG4111   1 ALPGGFVR-EHESLEDAARRWLAEQTGLELGYLEQLYTFGDPDRDP---RGRVISVAYLALVREEE-------------- 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Q94_B      148 yfpwedhrqgrpdildsiidklrawadsepdsraqrhLRADFTfglDGGGWNEELTLqryellyeaglvgeaqseprinf 227
Cdd:COG4111  63 -------------------------------------LRADDA---DDAAWFPVDEL----------------------- 79

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Q94_B      228 gRPMFADHRRILATGIARLRAKIKYRPVVFELMADSFTLLQLQRAIEALAGLTLHKQNFRRLIEQQQLVEETGDMATETG 307
Cdd:COG4111  80 -PPLAFDHRRILATALERLRAKLEYTPIGFELLPEKFTLSELQRLYEAILGRKLDKRNFRRKILSLGLLEETGEKQTGGA 158

                       250
                ....*....|
7Q94_B      308 GRPAKLFRFR 317
Cdd:COG4111 159 GRPAKLYRFD 168
NUDIX_NadM_like cd18873
bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase and similar proteins; ...
 48-156 1.54e-21

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: 88.37  E-value: 1.54e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Q94_B       48 AVVTAITTDEPRVMTVREGA-------ALPSGPFEFgHRTLQSGLREWIHEQTHHPVGYLEQLYTFADRDRNneiLGGRT 120
Cdd:cd18873   7 CVIFGFDDGELKVLLIKRKNepfkggwALPGGFVRE-DETLEDAARRELREETGLKDIYLEQLGTFGDPDRD---PRGRV 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
7Q94_B      121 ISIGYLGLVREQEAPSgKSAFWHGWYEYFPWE--------DHRQ 156
Cdd:cd18873  83 ISVAYLALVPEEDLAP-KAGDDAAEARWFPVDellpplafDHAE 125
AraR_C pfam19368
AraR C-terminal winged HTH domain; This entry represents the C-terminal DNA-binding domain of ...
 252-316 5.78e-05

AraR C-terminal winged HTH domain; This entry represents the C-terminal DNA-binding domain of AraR proteins which are involved in regulating Arabinose utilization. This domain has a winged helix-turn-helix structure.


Pssm-ID: 437200  Cd Length: 82  Bit Score: 40.88  E-value: 5.78e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
7Q94_B        252 YRPVVFELMADSFTLLQLQRAIEALAGLTLHK-QNFRRLIEQQQLVEETGDMATETGGRPAKLFRF 316
Cdd:pfam19368   1 YSPIAFDVLPELFTLNDLYQFYTTVLGENFSDySNFRTRLLKLGFLSDTGKKVSRGAGRPASLYRF 66
 
Name Accession Description Interval E-value
COG4111 COG4111
Uncharacterized conserved protein [Function unknown];
68-317 1.02e-68

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443287 [Multi-domain]  Cd Length: 170  Bit Score: 212.34  E-value: 1.02e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Q94_B       68 ALPSGPFEfGHRTLQSGLREWIHEQTHHPVGYLEQLYTFADRDRNNeilGGRTISIGYLGLVREQEapsgksafwhgwye 147
Cdd:COG4111   1 ALPGGFVR-EHESLEDAARRWLAEQTGLELGYLEQLYTFGDPDRDP---RGRVISVAYLALVREEE-------------- 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Q94_B      148 yfpwedhrqgrpdildsiidklrawadsepdsraqrhLRADFTfglDGGGWNEELTLqryellyeaglvgeaqseprinf 227
Cdd:COG4111  63 -------------------------------------LRADDA---DDAAWFPVDEL----------------------- 79

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Q94_B      228 gRPMFADHRRILATGIARLRAKIKYRPVVFELMADSFTLLQLQRAIEALAGLTLHKQNFRRLIEQQQLVEETGDMATETG 307
Cdd:COG4111  80 -PPLAFDHRRILATALERLRAKLEYTPIGFELLPEKFTLSELQRLYEAILGRKLDKRNFRRKILSLGLLEETGEKQTGGA 158

                       250
                ....*....|
7Q94_B      308 GRPAKLFRFR 317
Cdd:COG4111 159 GRPAKLYRFD 168
NUDIX_NadM_like cd18873
bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase and similar proteins; ...
 48-156 1.54e-21

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: 88.37  E-value: 1.54e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Q94_B       48 AVVTAITTDEPRVMTVREGA-------ALPSGPFEFgHRTLQSGLREWIHEQTHHPVGYLEQLYTFADRDRNneiLGGRT 120
Cdd:cd18873   7 CVIFGFDDGELKVLLIKRKNepfkggwALPGGFVRE-DETLEDAARRELREETGLKDIYLEQLGTFGDPDRD---PRGRV 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
7Q94_B      121 ISIGYLGLVREQEAPSgKSAFWHGWYEYFPWE--------DHRQ 156
Cdd:cd18873  83 ISVAYLALVPEEDLAP-KAGDDAAEARWFPVDellpplafDHAE 125
AraR_C pfam19368
AraR C-terminal winged HTH domain; This entry represents the C-terminal DNA-binding domain of ...
 252-316 5.78e-05

AraR C-terminal winged HTH domain; This entry represents the C-terminal DNA-binding domain of AraR proteins which are involved in regulating Arabinose utilization. This domain has a winged helix-turn-helix structure.


Pssm-ID: 437200  Cd Length: 82  Bit Score: 40.88  E-value: 5.78e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
7Q94_B        252 YRPVVFELMADSFTLLQLQRAIEALAGLTLHK-QNFRRLIEQQQLVEETGDMATETGGRPAKLFRF 316
Cdd:pfam19368   1 YSPIAFDVLPELFTLNDLYQFYTTVLGENFSDySNFRTRLLKLGFLSDTGKKVSRGAGRPASLYRF 66
 
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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