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MULTISPECIES: multifunctional transcriptional regulator/nicotinamide-nucleotide adenylyltransferase/ribosylnicotinamide kinase NadR [Enterobacter]

Protein Classification

multifunctional transcriptional regulator/nicotinamide-nucleotide adenylyltransferase/ribosylnicotinamide kinase NadR( domain architecture ID 11483083)

multifunctional transcriptional regulator/nicotinamide-nucleotide adenylyltransferase/ribosylnicotinamide kinase NadR has three activities: DNA binding, nicotinamide mononucleotide (NMN) adenylyltransferase and ribosylnicotinamide (RN) kinase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08099 PRK08099
multifunctional transcriptional regulator/nicotinamide-nucleotide adenylyltransferase ...
 13-410 0e+00

multifunctional transcriptional regulator/nicotinamide-nucleotide adenylyltransferase/ribosylnicotinamide kinase NadR;


:

Pssm-ID: 236151 [Multi-domain]  Cd Length: 399  Bit Score: 835.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215  13 QKGCTLQQVADASGMTKGYLSQLLNAKIKSPSAQKLEALHRFLGLEFPRMQKNIGVVFGKFYPLHTGHIYLIQRACSQVD 92
Cdd:PRK08099   1 QQGCTLQQVADASGMTKGYLSQLLNAKIKSPSAQKLEALHRFLGLEFPRQMKKIGVVFGKFYPLHTGHIYLIQRACSQVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215  93 ELHIIMGYDETRDRQLFEDSAMSQQPTVPDRLRWLLQTFKYQKNIRIHAFNEEGMEPYPHGWDVWSNGIKAFMEEKGIAP 172
Cdd:PRK08099  81 ELHIIICYDDERDRKLFEDSAMSQQPTVSDRLRWLLQTFKYQKNIKIHAFNEEGMEPYPHGWDVWSNGIKAFMAEKGIQP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215 173 NWIYTSEESDAPQFREHLGIETVLIDPKRTFMNISGAQIRENPFRYWDYIPTEVKPFFVRTVAILGGESSGKSTLVNKLA 252
Cdd:PRK08099 161 DVIYTSEEQDAPQYEEHLGIETVLVDPKRTFMNISGTQIRENPFRYWEYIPTEVRPFFVRTVAILGGESSGKSTLVNKLA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215 253 NIFNTTSAWEYGRDYVFSHLGGDEMALQYSDYDKIALGHAQYIDFAVKYANKVAFIDTDFVTTQAFCKKYEGREHPFVQA 332
Cdd:PRK08099 241 NIFNTTSAWEYGREYVFSHLGGDEMALQYSDYDKIALGHAQYIDFAVKYANKVAFIDTDFVTTQAFCKKYEGREHPFVQA 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489953215 333 LIDEYRFDLVILLENNTPWVADGMRSLGSSVDRREFQTMLVEMLNENNVEFVHVEESDYDTRFLRCVELVKEMMGEQG 410
Cdd:PRK08099 321 LIDEYRFDLTILLENNTPWVADGLRSLGSSVDRKRFQNLLKEMLKENNIEYVHVESPDYDKRYLRCVELVDQMLGEQR 398
 
Name Accession Description Interval E-value
PRK08099 PRK08099
multifunctional transcriptional regulator/nicotinamide-nucleotide adenylyltransferase ...
 13-410 0e+00

multifunctional transcriptional regulator/nicotinamide-nucleotide adenylyltransferase/ribosylnicotinamide kinase NadR;


Pssm-ID: 236151 [Multi-domain]  Cd Length: 399  Bit Score: 835.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215  13 QKGCTLQQVADASGMTKGYLSQLLNAKIKSPSAQKLEALHRFLGLEFPRMQKNIGVVFGKFYPLHTGHIYLIQRACSQVD 92
Cdd:PRK08099   1 QQGCTLQQVADASGMTKGYLSQLLNAKIKSPSAQKLEALHRFLGLEFPRQMKKIGVVFGKFYPLHTGHIYLIQRACSQVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215  93 ELHIIMGYDETRDRQLFEDSAMSQQPTVPDRLRWLLQTFKYQKNIRIHAFNEEGMEPYPHGWDVWSNGIKAFMEEKGIAP 172
Cdd:PRK08099  81 ELHIIICYDDERDRKLFEDSAMSQQPTVSDRLRWLLQTFKYQKNIKIHAFNEEGMEPYPHGWDVWSNGIKAFMAEKGIQP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215 173 NWIYTSEESDAPQFREHLGIETVLIDPKRTFMNISGAQIRENPFRYWDYIPTEVKPFFVRTVAILGGESSGKSTLVNKLA 252
Cdd:PRK08099 161 DVIYTSEEQDAPQYEEHLGIETVLVDPKRTFMNISGTQIRENPFRYWEYIPTEVRPFFVRTVAILGGESSGKSTLVNKLA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215 253 NIFNTTSAWEYGRDYVFSHLGGDEMALQYSDYDKIALGHAQYIDFAVKYANKVAFIDTDFVTTQAFCKKYEGREHPFVQA 332
Cdd:PRK08099 241 NIFNTTSAWEYGREYVFSHLGGDEMALQYSDYDKIALGHAQYIDFAVKYANKVAFIDTDFVTTQAFCKKYEGREHPFVQA 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489953215 333 LIDEYRFDLVILLENNTPWVADGMRSLGSSVDRREFQTMLVEMLNENNVEFVHVEESDYDTRFLRCVELVKEMMGEQG 410
Cdd:PRK08099 321 LIDEYRFDLTILLENNTPWVADGLRSLGSSVDRKRFQNLLKEMLKENNIEYVHVESPDYDKRYLRCVELVDQMLGEQR 398
nadR_NMN_Atrans TIGR01526
nicotinamide-nucleotide adenylyltransferase, NadR type; The NadR protein of E. coli and ...
 64-395 0e+00

nicotinamide-nucleotide adenylyltransferase, NadR type; The NadR protein of E. coli and closely related bacteria is both enzyme and regulatory protein. The first 60 or so amino acids, N-terminal to the region covered by this model, is a DNA-binding helix-turn-helix domain (pfam01381) responsible for repressing the nadAB genes of NAD de novo biosynthesis. The NadR homologs in Mycobacterium tuberculosis, Haemophilus influenzae, and others appear to lack the repressor domain. NadR has recently been shown to act as an enzyme of the salvage pathway of NAD biosynthesis, nicotinamide-nucleotide adenylyltransferase; members of this family are presumed to share this activity. E. coli NadR has also been found to regulate the import of its substrate, nicotinamide ribonucleotide, but it is not known if the other members of this model share that activity.


Pssm-ID: 273670 [Multi-domain]  Cd Length: 325  Bit Score: 533.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215   64 KNIGVVFGKFYPLHTGHIYLIQRACSQVDELHIIMGYdetrdrqLFEDSAMSQQPTVPDRLRWLLQTFKYQKN-IRIHAF 142
Cdd:TIGR01526   1 KTIGVVFGKFYPLHTGHIYLIYEAFSKVDELHIVVGS-------LFYDSKAKRPPPVQDRLRWLREIFKYQKNqIFIHHL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215  143 NEEGMEPYPHGWDVWSNGIKAFMEEKGIAPNWIYTSEESDAPQFREHLGIETVLIDPKRTFMNISGAQIRENPFRYWDYI 222
Cdd:TIGR01526  74 NEDGIPEYPNGWDSWSNALKTLFHEKHFEPDIVFSSEPQYAAPYEKYLGLEVVLVDPDRTFFSVSATQIRENPFQHWKHI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215  223 PTEVKPFFVRTVAILGGESSGKSTLVNKLANIFNTTSAWEYGRDYVFSHLGGDEmALQYSDYDKIALGHAQYIDFAVKYA 302
Cdd:TIGR01526 154 PREVRPFFVKTVAILGGESTGKSTLVNKLAAVFNTTSAWEYAREYVEEKLGGDE-ALQYSDYAQIALGQQRYIDYAVRHA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215  303 NKVAFIDTDFVTTQAFCKKYEGREHPFVQALIDEYRFDLVILLENNTPWVADGMRSLGSSVDRREFQTMLVEMLNENNVE 382
Cdd:TIGR01526 233 HKIAFIDTDFITTQVFAKQYEGREHPFLDSDIAEYPFDLTLLLKPNTEWVDDGLRSLGSQKQRQEFQQLLKKLLDEYGVP 312

                         330
                  ....*....|...
gi 489953215  383 FVHVEESDYDTRF 395
Cdd:TIGR01526 313 FVVIESPDYLDRY 325
NMNAT_NadR cd02167
Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional NadR-like proteins; ...
 66-227 1.84e-77

Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional NadR-like proteins; NMNAT domain of NadR protein. The NadR protein (NadR) is a bifunctional enzyme possessing both NMN adenylytransferase (NMNAT) and ribosylnicotinamide kinase (RNK) activities. Its function is essential for the growth and survival of H. influenzae and thus may present a new highly specific anti-infectious drug target. The N-terminal domain that hosts the NMNAT activity is closely related to archaeal NMNAT. The bound NAD at the active site of the NMNAT domain reveals several critical interactions between NAD and the protein.The NMNAT domain of hiNadR defines yet another member of the pyridine nucleotide adenylyltransferase


Pssm-ID: 173918  Cd Length: 158  Bit Score: 237.00  E-value: 1.84e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215  66 IGVVFGKFYPLHTGHIYLIQRACSQVDELHIIMGYDETRDRQlfedsamSQQPTVPDRLRWLLQTFKYQKNIRIHAFNEE 145
Cdd:cd02167    1 IGIVFGKFAPLHTGHVYLIYKALSQVDELLIIVGSDDTRDDA-------RTGLPLEKRLRWLREIFPDQENIVVHTLNEP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215 146 GMEPYPHGWDVWSNGIKAFMEEKG-IAPNWIYTSEESDAPQF--REHLGIETVLIDPKRTFMNISGAQIRENPFRYWDYI 222
Cdd:cd02167   74 DIPEYPNGWDIWSNRVKTLIAENTrCRPDIVFTAEEYEAAFElvLAYLGAQVVLVDPDRTDISVSATQIRENPFRYWYHI 153


                 ....*
gi 489953215 223 PTEVK 227
Cdd:cd02167  154 PREVR 158
NadR3 COG3172
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ...
 224-408 1.03e-74

Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 442405 [Multi-domain]  Cd Length: 178  Bit Score: 230.48  E-value: 1.03e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215 224 TEVKPFFVRTVAILGGESSGKSTLVNKLANIFNTTSAWEYGRDYVFSHlggdEMALQYSDYDKIALGHAQYIDFAVKYAN 303
Cdd:COG3172    1 PEVRPSFVKKIVLLGAESTGKTTLARALAAHYNTPWVPEYGREYLEEK----GRALTYDDLLAIARGQLALEDAAAKRAN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215 304 KVAFIDTDFVTTQAFCKKYEGREHPFVQALIDEYRFDLVILLENNTPWVADGMRSLGSsvDRREFQTMLVEMLNENNVEF 383
Cdd:COG3172   77 KLLFCDTDALTTKVYSELYFGKCPPWLEALAAQRRYDLYLLLDPDIPWVADGLRDGPE--VREEFQQLLREELEERGIPY 154

                        170       180
                 ....*....|....*....|....*
gi 489953215 384 VHVeESDYDTRFLRCVELVKEMMGE 408
Cdd:COG3172  155 VVI-SGDYEERLEQALAAIDELLAK 178
AAA_28 pfam13521
AAA domain;
234-394 3.21e-34

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 124.68  E-value: 3.21e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215  234 VAILGGESSGKSTLVNKLANIFNTTSAWEYGRDYVFSHLGGDEMALQYSdYDKIALGH----AQYIDFAVKYANKVAFID 309
Cdd:pfam13521   2 IVITGGPSTGKTTLAEALAARFGYPVVPEAAREILEELGADGGDALPWV-EDLLAFARgvleAQLEDEAAAAANDLLFFD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215  310 TDFVTTQAFCKKYEGREHPFVQALIDEYRFDLVILLENNTPWVADGMRsLGSSVDRREFQTMLVEMLNENNVEFVHVEES 389
Cdd:pfam13521  81 RGPLDTLAYSRAYGGPCPPELEAAARASRYDLVFLLPPDPEIVQDGER-REDPEERERFHERLREALRELGIPVIIVPRG 159


                  ....*
gi 489953215  390 DYDTR 394
Cdd:pfam13521 160 SVEER 164
HTH_XRE smart00530
Helix-turn-helix XRE-family like proteins;
7-58 3.17e-07

Helix-turn-helix XRE-family like proteins;


Pssm-ID: 197775 [Multi-domain]  Cd Length: 56  Bit Score: 46.74  E-value: 3.17e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 489953215     7 IKTAIRQKGCTLQQVADASGMTKGYLSQLLNAKIKsPSAQKLEALHRFLGLE 58
Cdd:smart00530   2 LKELREEKGLTQEELAEKLGVSRSTLSRIENGKRK-PSLETLKKLAKALGVS 52
 
Name Accession Description Interval E-value
PRK08099 PRK08099
multifunctional transcriptional regulator/nicotinamide-nucleotide adenylyltransferase ...
 13-410 0e+00

multifunctional transcriptional regulator/nicotinamide-nucleotide adenylyltransferase/ribosylnicotinamide kinase NadR;


Pssm-ID: 236151 [Multi-domain]  Cd Length: 399  Bit Score: 835.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215  13 QKGCTLQQVADASGMTKGYLSQLLNAKIKSPSAQKLEALHRFLGLEFPRMQKNIGVVFGKFYPLHTGHIYLIQRACSQVD 92
Cdd:PRK08099   1 QQGCTLQQVADASGMTKGYLSQLLNAKIKSPSAQKLEALHRFLGLEFPRQMKKIGVVFGKFYPLHTGHIYLIQRACSQVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215  93 ELHIIMGYDETRDRQLFEDSAMSQQPTVPDRLRWLLQTFKYQKNIRIHAFNEEGMEPYPHGWDVWSNGIKAFMEEKGIAP 172
Cdd:PRK08099  81 ELHIIICYDDERDRKLFEDSAMSQQPTVSDRLRWLLQTFKYQKNIKIHAFNEEGMEPYPHGWDVWSNGIKAFMAEKGIQP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215 173 NWIYTSEESDAPQFREHLGIETVLIDPKRTFMNISGAQIRENPFRYWDYIPTEVKPFFVRTVAILGGESSGKSTLVNKLA 252
Cdd:PRK08099 161 DVIYTSEEQDAPQYEEHLGIETVLVDPKRTFMNISGTQIRENPFRYWEYIPTEVRPFFVRTVAILGGESSGKSTLVNKLA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215 253 NIFNTTSAWEYGRDYVFSHLGGDEMALQYSDYDKIALGHAQYIDFAVKYANKVAFIDTDFVTTQAFCKKYEGREHPFVQA 332
Cdd:PRK08099 241 NIFNTTSAWEYGREYVFSHLGGDEMALQYSDYDKIALGHAQYIDFAVKYANKVAFIDTDFVTTQAFCKKYEGREHPFVQA 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489953215 333 LIDEYRFDLVILLENNTPWVADGMRSLGSSVDRREFQTMLVEMLNENNVEFVHVEESDYDTRFLRCVELVKEMMGEQG 410
Cdd:PRK08099 321 LIDEYRFDLTILLENNTPWVADGLRSLGSSVDRKRFQNLLKEMLKENNIEYVHVESPDYDKRYLRCVELVDQMLGEQR 398
nadR_NMN_Atrans TIGR01526
nicotinamide-nucleotide adenylyltransferase, NadR type; The NadR protein of E. coli and ...
 64-395 0e+00

nicotinamide-nucleotide adenylyltransferase, NadR type; The NadR protein of E. coli and closely related bacteria is both enzyme and regulatory protein. The first 60 or so amino acids, N-terminal to the region covered by this model, is a DNA-binding helix-turn-helix domain (pfam01381) responsible for repressing the nadAB genes of NAD de novo biosynthesis. The NadR homologs in Mycobacterium tuberculosis, Haemophilus influenzae, and others appear to lack the repressor domain. NadR has recently been shown to act as an enzyme of the salvage pathway of NAD biosynthesis, nicotinamide-nucleotide adenylyltransferase; members of this family are presumed to share this activity. E. coli NadR has also been found to regulate the import of its substrate, nicotinamide ribonucleotide, but it is not known if the other members of this model share that activity.


Pssm-ID: 273670 [Multi-domain]  Cd Length: 325  Bit Score: 533.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215   64 KNIGVVFGKFYPLHTGHIYLIQRACSQVDELHIIMGYdetrdrqLFEDSAMSQQPTVPDRLRWLLQTFKYQKN-IRIHAF 142
Cdd:TIGR01526   1 KTIGVVFGKFYPLHTGHIYLIYEAFSKVDELHIVVGS-------LFYDSKAKRPPPVQDRLRWLREIFKYQKNqIFIHHL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215  143 NEEGMEPYPHGWDVWSNGIKAFMEEKGIAPNWIYTSEESDAPQFREHLGIETVLIDPKRTFMNISGAQIRENPFRYWDYI 222
Cdd:TIGR01526  74 NEDGIPEYPNGWDSWSNALKTLFHEKHFEPDIVFSSEPQYAAPYEKYLGLEVVLVDPDRTFFSVSATQIRENPFQHWKHI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215  223 PTEVKPFFVRTVAILGGESSGKSTLVNKLANIFNTTSAWEYGRDYVFSHLGGDEmALQYSDYDKIALGHAQYIDFAVKYA 302
Cdd:TIGR01526 154 PREVRPFFVKTVAILGGESTGKSTLVNKLAAVFNTTSAWEYAREYVEEKLGGDE-ALQYSDYAQIALGQQRYIDYAVRHA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215  303 NKVAFIDTDFVTTQAFCKKYEGREHPFVQALIDEYRFDLVILLENNTPWVADGMRSLGSSVDRREFQTMLVEMLNENNVE 382
Cdd:TIGR01526 233 HKIAFIDTDFITTQVFAKQYEGREHPFLDSDIAEYPFDLTLLLKPNTEWVDDGLRSLGSQKQRQEFQQLLKKLLDEYGVP 312

                         330
                  ....*....|...
gi 489953215  383 FVHVEESDYDTRF 395
Cdd:TIGR01526 313 FVVIESPDYLDRY 325
NMNAT_NadR cd02167
Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional NadR-like proteins; ...
 66-227 1.84e-77

Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional NadR-like proteins; NMNAT domain of NadR protein. The NadR protein (NadR) is a bifunctional enzyme possessing both NMN adenylytransferase (NMNAT) and ribosylnicotinamide kinase (RNK) activities. Its function is essential for the growth and survival of H. influenzae and thus may present a new highly specific anti-infectious drug target. The N-terminal domain that hosts the NMNAT activity is closely related to archaeal NMNAT. The bound NAD at the active site of the NMNAT domain reveals several critical interactions between NAD and the protein.The NMNAT domain of hiNadR defines yet another member of the pyridine nucleotide adenylyltransferase


Pssm-ID: 173918  Cd Length: 158  Bit Score: 237.00  E-value: 1.84e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215  66 IGVVFGKFYPLHTGHIYLIQRACSQVDELHIIMGYDETRDRQlfedsamSQQPTVPDRLRWLLQTFKYQKNIRIHAFNEE 145
Cdd:cd02167    1 IGIVFGKFAPLHTGHVYLIYKALSQVDELLIIVGSDDTRDDA-------RTGLPLEKRLRWLREIFPDQENIVVHTLNEP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215 146 GMEPYPHGWDVWSNGIKAFMEEKG-IAPNWIYTSEESDAPQF--REHLGIETVLIDPKRTFMNISGAQIRENPFRYWDYI 222
Cdd:cd02167   74 DIPEYPNGWDIWSNRVKTLIAENTrCRPDIVFTAEEYEAAFElvLAYLGAQVVLVDPDRTDISVSATQIRENPFRYWYHI 153


                 ....*
gi 489953215 223 PTEVK 227
Cdd:cd02167  154 PREVR 158
NadR3 COG3172
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ...
 224-408 1.03e-74

Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 442405 [Multi-domain]  Cd Length: 178  Bit Score: 230.48  E-value: 1.03e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215 224 TEVKPFFVRTVAILGGESSGKSTLVNKLANIFNTTSAWEYGRDYVFSHlggdEMALQYSDYDKIALGHAQYIDFAVKYAN 303
Cdd:COG3172    1 PEVRPSFVKKIVLLGAESTGKTTLARALAAHYNTPWVPEYGREYLEEK----GRALTYDDLLAIARGQLALEDAAAKRAN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215 304 KVAFIDTDFVTTQAFCKKYEGREHPFVQALIDEYRFDLVILLENNTPWVADGMRSLGSsvDRREFQTMLVEMLNENNVEF 383
Cdd:COG3172   77 KLLFCDTDALTTKVYSELYFGKCPPWLEALAAQRRYDLYLLLDPDIPWVADGLRDGPE--VREEFQQLLREELEERGIPY 154

                        170       180
                 ....*....|....*....|....*
gi 489953215 384 VHVeESDYDTRFLRCVELVKEMMGE 408
Cdd:COG3172  155 VVI-SGDYEERLEQALAAIDELLAK 178
NadR COG1056
Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; ...
 63-229 3.95e-36

Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; Nicotinamide mononucleotide adenylyltransferase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 440676 [Multi-domain]  Cd Length: 162  Bit Score: 129.93  E-value: 3.95e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215  63 QKNIGVVFGKFYPLHTGHIYLIQRACSQVDELHIIMGYDETRDRqlfedsaMSQQPTVPDRLRWLLQTFKYQ--KNIRIH 140
Cdd:COG1056    1 MMKRGLFIGRFQPFHLGHLAVIKWALEEVDELIIGIGSAQESHT-------PRNPFTAGERIEMIRAALKEEglSRVYIV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215 141 AFNEEgmepypHGWDVWSNGIKAFMEEkgiaPNWIYTSeESDAPQFREHLGIEtVLIDPKRTFMNISGAQIRENPFRY-- 218
Cdd:COG1056   74 PIPDI------NNNSLWVSHVKSLVPP----FDVVYSN-NPLVGRLFKEAGYE-VLLPPLFEREEYSGTEIRRLMLEGed 141

                        170
                 ....*....|..
gi 489953215 219 WDYI-PTEVKPF 229
Cdd:COG1056  142 WESLvPPAVAEV 153
AAA_28 pfam13521
AAA domain;
234-394 3.21e-34

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 124.68  E-value: 3.21e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215  234 VAILGGESSGKSTLVNKLANIFNTTSAWEYGRDYVFSHLGGDEMALQYSdYDKIALGH----AQYIDFAVKYANKVAFID 309
Cdd:pfam13521   2 IVITGGPSTGKTTLAEALAARFGYPVVPEAAREILEELGADGGDALPWV-EDLLAFARgvleAQLEDEAAAAANDLLFFD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215  310 TDFVTTQAFCKKYEGREHPFVQALIDEYRFDLVILLENNTPWVADGMRsLGSSVDRREFQTMLVEMLNENNVEFVHVEES 389
Cdd:pfam13521  81 RGPLDTLAYSRAYGGPCPPELEAAARASRYDLVFLLPPDPEIVQDGER-REDPEERERFHERLREALRELGIPVIIVPRG 159


                  ....*
gi 489953215  390 DYDTR 394
Cdd:pfam13521 160 SVEER 164
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 66-136 2.03e-13

cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.


Pssm-ID: 272920 [Multi-domain]  Cd Length: 66  Bit Score: 64.64  E-value: 2.03e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489953215   66 IGVVFGKFYPLHTGHIYLIQRACSQVDELHIIMGYDEtrdrqlfEDSAMSQQP-TVPDRLRWLLQTFKYQKN 136
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQ-------FVNPLKGEPvFSLEERLEMLKALKYVDE 65
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 66-213 3.42e-11

Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are known to use CTP or ATP and release pyrophosphate. Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown.


Pssm-ID: 185678 [Multi-domain]  Cd Length: 143  Bit Score: 60.92  E-value: 3.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215  66 IGVVFGKFYPLHTGHIYLIQRACSQV-DELHIIMGYDETRdRQLFEDSAmsqqpTVPDRLRWLLQTFKYQKNIRIHAFNE 144
Cdd:cd02039    1 VGIIIGRFEPFHLGHLKLIKEALEEAlDEVIIIIVSNPPK-KKRNKDPF-----SLHERVEMLKEILKDRLKVVPVDFPE 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489953215 145 EGmePYPHGWDVWS----NGIKAFMeekgIAPNWIYTSEESDAPQFREH-LGIETVLIDPKRTFMNISGAQIRE 213
Cdd:cd02039   75 VK--ILLAVVFILKillkVGPDKVV----VGEDFAFGKNASYNKDLKELfLDIEIVEVPRVRDGKKISSTLIRE 142
HTH_XRE cd00093
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ...
 7-59 1.46e-07

Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.


Pssm-ID: 238045 [Multi-domain]  Cd Length: 58  Bit Score: 47.93  E-value: 1.46e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489953215   7 IKTAIRQKGCTLQQVADASGMTKGYLSQLLNAKIkSPSAQKLEALHRFLGLEF 59
Cdd:cd00093    4 LKELRKEKGLTQEELAEKLGVSRSTISRIENGKR-NPSLETLEKLAKALGVSL 55
HTH_XRE smart00530
Helix-turn-helix XRE-family like proteins;
7-58 3.17e-07

Helix-turn-helix XRE-family like proteins;


Pssm-ID: 197775 [Multi-domain]  Cd Length: 56  Bit Score: 46.74  E-value: 3.17e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 489953215     7 IKTAIRQKGCTLQQVADASGMTKGYLSQLLNAKIKsPSAQKLEALHRFLGLE 58
Cdd:smart00530   2 LKELREEKGLTQEELAEKLGVSRSTLSRIENGKRK-PSLETLKKLAKALGVS 52
HipB COG1396
Transcriptional regulator, contains XRE-family HTH domain [Transcription];
7-57 1.13e-06

Transcriptional regulator, contains XRE-family HTH domain [Transcription];


Pssm-ID: 441006 [Multi-domain]  Cd Length: 83  Bit Score: 46.14  E-value: 1.13e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489953215   7 IKTAIRQKGCTLQQVADASGMTKGYLSQLLNAKiKSPSAQKLEALHRFLGL 57
Cdd:COG1396   12 LRELRKARGLTQEELAERLGVSRSTISRIERGR-RNPSLETLLKLAKALGV 61
HTH_3 pfam01381
Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and ...
 7-59 1.39e-06

Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and CI. Within the protein Swiss:Q5F9C2, the full protein fold incorporates a helix-turn-helix motif, but the function of this member is unlikely to be that of a DNA-binding regulator, the function of most other members, so is not necessarily characteriztic of the whole family.


Pssm-ID: 460181 [Multi-domain]  Cd Length: 55  Bit Score: 44.84  E-value: 1.39e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 489953215    7 IKTAIRQKGCTLQQVADASGMTKGYLSQLLNAKiKSPSAQKLEALHRFLGLEF 59
Cdd:pfam01381   1 LKELREELGLSQEELAEKLGVSRSTISKIENGK-REPSLETLKKLAEALGVSL 52
HTH_31 pfam13560
Helix-turn-helix domain; This domain is a helix-turn-helix domain that probably binds to DNA.
 12-57 2.34e-05

Helix-turn-helix domain; This domain is a helix-turn-helix domain that probably binds to DNA.


Pssm-ID: 433309 [Multi-domain]  Cd Length: 64  Bit Score: 41.74  E-value: 2.34e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 489953215   12 RQKGCTLQQVADASGMTKGYLSQLLNAKIKSPSAQKLEALHRFLGL 57
Cdd:pfam13560  11 ERAGLSQEALARRLGVSRSTLSRLETGRRGRPSPAVVERLARALGV 56
NMNAT_Archaea cd02166
Nicotinamide/nicotinate mononucleotide adenylyltransferase, archaeal; This family of archaeal ...
 67-99 1.91e-04

Nicotinamide/nicotinate mononucleotide adenylyltransferase, archaeal; This family of archaeal proteins exhibits nicotinamide-nucleotide adenylyltransferase (NMNAT) activity utilizing the salvage pathway to synthesize NAD. In some cases, the enzyme was tested and found also to have the activity of nicotinate-nucleotide adenylyltransferase an enzyme of NAD de novo biosynthesis, although with a higher Km. In some archaeal species, a number of proteins which are uncharacterized with respect to activity, are also present.


Pssm-ID: 173917  Cd Length: 163  Bit Score: 41.51  E-value: 1.91e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 489953215  67 GVVFGKFYPLHTGHIYLIQRACSQVDELHIIMG 99
Cdd:cd02166    2 ALFIGRFQPFHLGHLKVIKWILEEVDELIIGIG 34
PRK01153 PRK01153
nicotinamide-nucleotide adenylyltransferase; Provisional
 67-99 2.32e-04

nicotinamide-nucleotide adenylyltransferase; Provisional


Pssm-ID: 179235  Cd Length: 174  Bit Score: 41.78  E-value: 2.32e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 489953215  67 GVVFGKFYPLHTGHIYLIQRACSQVDELHIIMG 99
Cdd:PRK01153   3 ALFIGRFQPFHKGHLEVIKWILEEVDELIIGIG 35
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 66-143 5.42e-04

Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is an essential enzyme in bacteria, responsible for catalyzing the rate-limiting step in coenzyme A (CoA) biosynthesis. The dinucleotide-binding fold of PPAT is homologous to class I aminoacyl-tRNA synthetases. CoA has been shown to inhibit PPAT and competes with ATP, PhP, and dPCoA. PPAT is a homohexamer in E. coli.


Pssm-ID: 173914 [Multi-domain]  Cd Length: 153  Bit Score: 40.14  E-value: 5.42e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489953215  66 IGVVFGKFYPLHTGHIYLIQRACSQVDELHIIMGYDETRdRQLFedsamsqqpTVPDRLRWLLQTFKYQKNIRIHAFN 143
Cdd:cd02163    1 IAVYPGSFDPITNGHLDIIERASKLFDEVIVAVAVNPSK-KPLF---------SLEERVELIREATKHLPNVEVDGFD 68
NMNAT_Nudix cd02168
Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional proteins, also ...
 66-144 5.53e-03

Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional proteins, also containing a Nudix hydrolase domain; N-terminal NMNAT (Nicotinamide/nicotinate mononucleotide adenylyltransferase) domain of a novel bifunctional enzyme endowed with NMN adenylyltransferase and Nudix hydrolase activities. This domain is highly homologous to the archeal NMN adenyltransferase that catalyzes NAD synthesis from NMN and ATP. NMNAT is an essential enzyme in the biosynthesis of NAD(+) and NADP(+). Nicotinamide-nucleotide adenylyltransferase synthesizes NAD via the salvage pathway, while nicotinate-nucleotide adenylyltransferase synthesizes the immediate precursor of NAD via the de novo pathway. The C-terminal domain of this enzyme shares homology with the archaeal ADP-ribose pyrophosphatase, a member of the 'Nudix' hydrolase family.


Pssm-ID: 173919  Cd Length: 181  Bit Score: 37.74  E-value: 5.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953215  66 IGVVFGKFYPLHTGHIYLIQRACSQVDELHIIMG-YDETRD---------RQLFEDSAMSQQPTVPDRLRWLlqtfkyqk 135
Cdd:cd02168    1 YLVYIGRFQPFHNGHLAVVLIALEKAKKVIILIGsARTARNiknpwtseeREVMIEAALSDAGADLARVHFR-------- 72


                 ....*....
gi 489953215 136 NIRIHAFNE 144
Cdd:cd02168   73 PLRDHLYSD 81
HTH_19 pfam12844
Helix-turn-helix domain; Members of this family contains a DNA-binding helix-turn-helix domain. ...
 5-57 8.20e-03

Helix-turn-helix domain; Members of this family contains a DNA-binding helix-turn-helix domain. This family contains many example antitoxins from bacterial toxin-antitoxin systems. These antitoxins are likely to be DNA-binding domains.


Pssm-ID: 463728 [Multi-domain]  Cd Length: 64  Bit Score: 34.57  E-value: 8.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 489953215    5 DYIKTAIRQKGCTLQQVADASGMTKGYLSQLLNAKIKsPSAQKLEALHRFLGL 57
Cdd:pfam12844   2 ERLRKAREERGLTQEELAERLGISRSQLSAIENGKSV-PPAETLYKIAELLGV 53
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 66-103 9.26e-03

Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis]; Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 440380 [Multi-domain]  Cd Length: 131  Bit Score: 36.24  E-value: 9.26e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 489953215  66 IGVVFGKFYPLHTGHIYLIQRACSQVDELHIIMGYDET 103
Cdd:COG0615    2 RVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEF 39
 
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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