NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|309245187|gb|ADO54754|]
View 

NAD+ synthetase [Paenibacillus polymyxa SC2]

Protein Classification

adenine nucleotide alpha hydrolase family protein( domain architecture ID 188)

AANH (adenine nucleotide alpha hydrolase) family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
AANH_superfamily super family cl00292
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase ...
 2-267 4.24e-114

Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase (AANH) superfamily includes N-type ATP PPases, ATP sulfurylases, universal stress response proteins (USPs), and electron transfer flavoproteins (ETFs). The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.


The actual alignment was detected with superfamily member PRK00768:

Pssm-ID: 469708 [Multi-domain]  Cd Length: 268  Bit Score: 328.64  E-value: 4.24e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187   2 SLQEQIIAELGVQPTINVEAEVRKRVDFLKSYVTKTGSKGLLIAISGGIDSAVAAALCKQATDELTQEQG-QEYKTLGVF 80
Cdd:PRK00768   1 TLQQEIIAELGVKPTIDPEEEIRRRVDFLKDYLKKSGLKSLVLGISGGQDSTLAGRLAQLAVEELRAETGdDDYQFIAVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187  81 QPYGQQEDiEHSYAVAKAF-----NLKyageTNIKEAVDTIavevEHTLKDIGLErsITPQVRGNVKARTRMVVQYALAN 155
Cdd:PRK00768  81 LPYGVQAD-EDDAQDALAFiqpdrVLT----VNIKPAVDAS----VAALEAAGIE--LSDFVKGNIKARERMIAQYAIAG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187 156 ELNLLVVGTDHASEAITGFYTKWGDGAVDITPLSTLNKRQVRLLASYLGVPQAILDKAPTAGLWE---GQTDEKELGISY 232
Cdd:PRK00768 150 ATGGLVVGTDHAAEAVTGFFTKFGDGGADILPLFGLNKRQGRALLAALGAPEHLYEKVPTADLEDdrpGLPDEVALGVTY 229

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 309245187 233 EANSDYLEGKEIDPAAREKLESYFTRTAHKRTSIP 267
Cdd:PRK00768 230 DQIDDYLEGKPVSEEAAETIENWYLKTEHKRHLPI 264
 
Name Accession Description Interval E-value
nadE PRK00768
ammonia-dependent NAD(+) synthetase;
2-267 4.24e-114

ammonia-dependent NAD(+) synthetase;


Pssm-ID: 234831 [Multi-domain]  Cd Length: 268  Bit Score: 328.64  E-value: 4.24e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187   2 SLQEQIIAELGVQPTINVEAEVRKRVDFLKSYVTKTGSKGLLIAISGGIDSAVAAALCKQATDELTQEQG-QEYKTLGVF 80
Cdd:PRK00768   1 TLQQEIIAELGVKPTIDPEEEIRRRVDFLKDYLKKSGLKSLVLGISGGQDSTLAGRLAQLAVEELRAETGdDDYQFIAVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187  81 QPYGQQEDiEHSYAVAKAF-----NLKyageTNIKEAVDTIavevEHTLKDIGLErsITPQVRGNVKARTRMVVQYALAN 155
Cdd:PRK00768  81 LPYGVQAD-EDDAQDALAFiqpdrVLT----VNIKPAVDAS----VAALEAAGIE--LSDFVKGNIKARERMIAQYAIAG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187 156 ELNLLVVGTDHASEAITGFYTKWGDGAVDITPLSTLNKRQVRLLASYLGVPQAILDKAPTAGLWE---GQTDEKELGISY 232
Cdd:PRK00768 150 ATGGLVVGTDHAAEAVTGFFTKFGDGGADILPLFGLNKRQGRALLAALGAPEHLYEKVPTADLEDdrpGLPDEVALGVTY 229

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 309245187 233 EANSDYLEGKEIDPAAREKLESYFTRTAHKRTSIP 267
Cdd:PRK00768 230 DQIDDYLEGKPVSEEAAETIENWYLKTEHKRHLPI 264
NAD_synthase cd00553
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ...
 17-263 2.86e-88

NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de novo nicotinamide adenine dinucleotide (NAD(+)) biosynthesis, an amide transfer from either ammonia or glutamine to nicotinic acid adenine dinucleotide (NaAD). The conversion of NaAD to NAD(+) occurs via a NAD-adenylate intermediate and requires ATP and Mg(2+). The intermediate is subsequently cleaved into NAD(+) and AMP. In many prokaryotes, such as Escherichia coli, NAD synthase consists of a single domain and is strictly ammonia dependent. In contrast, eukaryotes and other prokaryotes have an additional N-terminal amidohydrolase domain that prefer glutamine. Interestingly, NAD(+) synthases in these prokaryotes, can also utilize ammonia as an amide source.


Pssm-ID: 467484 [Multi-domain]  Cd Length: 248  Bit Score: 262.49  E-value: 2.86e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187  17 INVEAEVRKRVDFLKSYVTKTGSKGLLIAISGGIDSAVAAALCKQATDEltqeqgqeYKTLGVFQPYG--QQEDIEHSYA 94
Cdd:cd00553    1 IDPEEIIEALVCFLRDYLRKSGAKGFVLGLSGGIDSAVVAALAVRALGA--------ENVLALIMPSRysSKETRDDAKA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187  95 VAKAFNLKYAgETNIKEAVDTIAVEVEHTLKDIglersITPQVRGNVKARTRMVVQYALANELNLLVVGTDHASEAITGF 174
Cdd:cd00553   73 LAENLGIEYR-TIDIDPIVDAFLKALEHAGGSE-----AEDLALGNIQARLRMVLLYALANLLGGLVLGTGNKSELLLGY 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187 175 YTKWGDGAVDITPLSTLNKRQVRLLASYLGVPQAILDKAPTAGLWEGQTDEKELGISYEANSDYLEGK------------ 242
Cdd:cd00553  147 FTKYGDGAADINPIGDLYKTQVRELARYLGVPEEIIEKPPSAELWPGQTDEDELGMPYEELDLILYGLvdgklgpeeils 226

                        250       260
                 ....*....|....*....|..
gi 309245187 243 -EIDPAAREKLESYFTRTAHKR 263
Cdd:cd00553  227 pGEDEEKVKRIFRLYRRNEHKR 248
NAD_synthase pfam02540
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ...
 22-264 1.41e-75

NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is induced by stress factors such as heat shock and glucose limitation.


Pssm-ID: 396888 [Multi-domain]  Cd Length: 241  Bit Score: 229.96  E-value: 1.41e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187   22 EVRKRVDFLKSYVTKTGSKGLLIAISGGIDSAVAAALCKQAtdeLTQEQgqeykTLGVFQPYGQQ--EDIEHSYAVAKAF 99
Cdd:pfam02540   1 EINALVDFLRDYVQKAGFKGVVLGLSGGIDSSLVAYLAVKA---LGKEN-----VLALIMPSSQSseEDVQDALALAENL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187  100 NLKYAgETNIKEAVDTIAVEVEHTLKDIglersitpqVRGNVKARTRMVVQYALANELNLLVVGTDHASEAITGFYTKWG 179
Cdd:pfam02540  73 GIEYK-TIDIKPIVRAFSQLFQDASEDF---------AKGNLKARIRMAILYYIANKFNYLVLGTGNKSELAVGYFTKYG 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187  180 DGAVDITPLSTLNKRQVRLLASYLGVPQAILDKAPTAGLWEGQTDEKELGISYEANSDYLE------------GKEIDPA 247
Cdd:pfam02540 143 DGACDIAPIGDLYKTQVYELARYLNVPERIIKKPPSADLWPGQTDEEELGIPYDELDDILKlvekklspeeiiGKGLPAE 222

                         250
                  ....*....|....*..
gi 309245187  248 AREKLESYFTRTAHKRT 264
Cdd:pfam02540 223 VVRRIENLIQKSEHKRR 239
nadE TIGR00552
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ...
 15-265 2.66e-74

NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the biosynthesis of the essensial cofactor NAD. The member of this family from Bacillus subtilis is a strictly NH(3)-dependent NAD(+) synthetase of 272 amino acids. Proteins consisting only of the domain modeled here may be named as NH3-dependent NAD+ synthetase. Amidotransferase activity may reside in a separate protein, or not be present. Some other members of the family, such as from Mycobacterium tuberculosis, are considerably longer, contain an apparent amidotransferase domain, and show glutamine-dependent as well as NH(3)-dependent activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]


Pssm-ID: 273132 [Multi-domain]  Cd Length: 250  Bit Score: 226.89  E-value: 2.66e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187   15 PTINVEAEVRkrvDFLKSYVTKTGSKGLLIAISGGIDSAVAAALCKQATDEltqeqgqeyKTLGVFQPYGQQ---EDIEH 91
Cdd:TIGR00552   1 NLIKYVEEIE---DFLRGYVQKSGAKGVVLGLSGGIDSAVVAALCVEALGE---------QNHALLLPHSVQtpeQDVQD 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187   92 SYAVAKAFNLKYageTNIKEAvDTIAVEVEHTLkDIGLERSITpqVRGNVKARTRMVVQYALANELNLLVVGTDHASEAI 171
Cdd:TIGR00552  69 ALALAEPLGINY---KNIDIA-PIAASFQAQTE-TGDELSDFL--AKGNLKARLRMAALYAIANKHNLLVLGTGNKSELM 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187  172 TGFYTKWGDGAVDITPLSTLNKRQVRLLASYLGVPQAILDKAPTAGLWEGQTDEKELGISYEANSDYLEGKEIDPAARE- 250
Cdd:TIGR00552 142 LGYFTKYGDGGCDIAPIGDLFKTQVYELAKRLNVPERIIEKPPTADLFDGQTDETELGITYDELDDYLKGIEELSQTVQe 221

                         250
                  ....*....|....*...
gi 309245187  251 ---KLESYFTRTAHKRTS 265
Cdd:TIGR00552 222 vvkRIESLVQKSEHKRRL 239
NadE COG0171
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ...
 5-267 1.65e-61

NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ synthetase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439941 [Multi-domain]  Cd Length: 542  Bit Score: 202.77  E-value: 1.65e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187   5 EQIIAELGVQPTINVEAEVRKRVDFLKSYVTKTGSKGLLIAISGGIDSAVAAALCKQAtdeltqeQGQEyKTLGVFQPYG 84
Cdd:COG0171  252 AEAAPPPPEEEEMDLEEVYDALVLGLRDYVRKNGFKGVVLGLSGGIDSALVAALAVDA-------LGPE-NVLGVTMPSR 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187  85 Q--QEDIEHSYAVAKAFNLKYAgETNIKEAVDTIAVEVEHTLKdiGLERSITpqvRGNVKARTRMVVQYALANELNLLVV 162
Cdd:COG0171  324 YtsDESLEDAEELAENLGIEYE-EIDITPAVEAFLEALPHAFG--GELDDVA---EENLQARIRMVILMALANKFGGLVL 397

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187 163 GTDHASEAITGFYTKWGDGAVDITPLSTLNKRQVRLLASYLG-----VPQAILDKAPTAGLWEGQTDEKELGiSYE---- 233
Cdd:COG0171  398 GTGNKSELAVGYFTKYGDGAGDLAPIADLYKTQVYALARWLNrngevIPEDIIDKPPSAELRPGQTDEDELG-PYEvlda 476

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 309245187 234 ---------ANSDYLEGKEIDPAAREKLESYFTRTAHKRTSIP 267
Cdd:COG0171  477 ilyayveegLSPEEIAAAGYDREWVERVLRLVRRNEYKRRQPP 519
 
Name Accession Description Interval E-value
nadE PRK00768
ammonia-dependent NAD(+) synthetase;
2-267 4.24e-114

ammonia-dependent NAD(+) synthetase;


Pssm-ID: 234831 [Multi-domain]  Cd Length: 268  Bit Score: 328.64  E-value: 4.24e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187   2 SLQEQIIAELGVQPTINVEAEVRKRVDFLKSYVTKTGSKGLLIAISGGIDSAVAAALCKQATDELTQEQG-QEYKTLGVF 80
Cdd:PRK00768   1 TLQQEIIAELGVKPTIDPEEEIRRRVDFLKDYLKKSGLKSLVLGISGGQDSTLAGRLAQLAVEELRAETGdDDYQFIAVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187  81 QPYGQQEDiEHSYAVAKAF-----NLKyageTNIKEAVDTIavevEHTLKDIGLErsITPQVRGNVKARTRMVVQYALAN 155
Cdd:PRK00768  81 LPYGVQAD-EDDAQDALAFiqpdrVLT----VNIKPAVDAS----VAALEAAGIE--LSDFVKGNIKARERMIAQYAIAG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187 156 ELNLLVVGTDHASEAITGFYTKWGDGAVDITPLSTLNKRQVRLLASYLGVPQAILDKAPTAGLWE---GQTDEKELGISY 232
Cdd:PRK00768 150 ATGGLVVGTDHAAEAVTGFFTKFGDGGADILPLFGLNKRQGRALLAALGAPEHLYEKVPTADLEDdrpGLPDEVALGVTY 229

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 309245187 233 EANSDYLEGKEIDPAAREKLESYFTRTAHKRTSIP 267
Cdd:PRK00768 230 DQIDDYLEGKPVSEEAAETIENWYLKTEHKRHLPI 264
NAD_synthase cd00553
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ...
 17-263 2.86e-88

NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de novo nicotinamide adenine dinucleotide (NAD(+)) biosynthesis, an amide transfer from either ammonia or glutamine to nicotinic acid adenine dinucleotide (NaAD). The conversion of NaAD to NAD(+) occurs via a NAD-adenylate intermediate and requires ATP and Mg(2+). The intermediate is subsequently cleaved into NAD(+) and AMP. In many prokaryotes, such as Escherichia coli, NAD synthase consists of a single domain and is strictly ammonia dependent. In contrast, eukaryotes and other prokaryotes have an additional N-terminal amidohydrolase domain that prefer glutamine. Interestingly, NAD(+) synthases in these prokaryotes, can also utilize ammonia as an amide source.


Pssm-ID: 467484 [Multi-domain]  Cd Length: 248  Bit Score: 262.49  E-value: 2.86e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187  17 INVEAEVRKRVDFLKSYVTKTGSKGLLIAISGGIDSAVAAALCKQATDEltqeqgqeYKTLGVFQPYG--QQEDIEHSYA 94
Cdd:cd00553    1 IDPEEIIEALVCFLRDYLRKSGAKGFVLGLSGGIDSAVVAALAVRALGA--------ENVLALIMPSRysSKETRDDAKA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187  95 VAKAFNLKYAgETNIKEAVDTIAVEVEHTLKDIglersITPQVRGNVKARTRMVVQYALANELNLLVVGTDHASEAITGF 174
Cdd:cd00553   73 LAENLGIEYR-TIDIDPIVDAFLKALEHAGGSE-----AEDLALGNIQARLRMVLLYALANLLGGLVLGTGNKSELLLGY 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187 175 YTKWGDGAVDITPLSTLNKRQVRLLASYLGVPQAILDKAPTAGLWEGQTDEKELGISYEANSDYLEGK------------ 242
Cdd:cd00553  147 FTKYGDGAADINPIGDLYKTQVRELARYLGVPEEIIEKPPSAELWPGQTDEDELGMPYEELDLILYGLvdgklgpeeils 226

                        250       260
                 ....*....|....*....|..
gi 309245187 243 -EIDPAAREKLESYFTRTAHKR 263
Cdd:cd00553  227 pGEDEEKVKRIFRLYRRNEHKR 248
NAD_synthase pfam02540
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ...
 22-264 1.41e-75

NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is induced by stress factors such as heat shock and glucose limitation.


Pssm-ID: 396888 [Multi-domain]  Cd Length: 241  Bit Score: 229.96  E-value: 1.41e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187   22 EVRKRVDFLKSYVTKTGSKGLLIAISGGIDSAVAAALCKQAtdeLTQEQgqeykTLGVFQPYGQQ--EDIEHSYAVAKAF 99
Cdd:pfam02540   1 EINALVDFLRDYVQKAGFKGVVLGLSGGIDSSLVAYLAVKA---LGKEN-----VLALIMPSSQSseEDVQDALALAENL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187  100 NLKYAgETNIKEAVDTIAVEVEHTLKDIglersitpqVRGNVKARTRMVVQYALANELNLLVVGTDHASEAITGFYTKWG 179
Cdd:pfam02540  73 GIEYK-TIDIKPIVRAFSQLFQDASEDF---------AKGNLKARIRMAILYYIANKFNYLVLGTGNKSELAVGYFTKYG 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187  180 DGAVDITPLSTLNKRQVRLLASYLGVPQAILDKAPTAGLWEGQTDEKELGISYEANSDYLE------------GKEIDPA 247
Cdd:pfam02540 143 DGACDIAPIGDLYKTQVYELARYLNVPERIIKKPPSADLWPGQTDEEELGIPYDELDDILKlvekklspeeiiGKGLPAE 222

                         250
                  ....*....|....*..
gi 309245187  248 AREKLESYFTRTAHKRT 264
Cdd:pfam02540 223 VVRRIENLIQKSEHKRR 239
nadE TIGR00552
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ...
 15-265 2.66e-74

NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the biosynthesis of the essensial cofactor NAD. The member of this family from Bacillus subtilis is a strictly NH(3)-dependent NAD(+) synthetase of 272 amino acids. Proteins consisting only of the domain modeled here may be named as NH3-dependent NAD+ synthetase. Amidotransferase activity may reside in a separate protein, or not be present. Some other members of the family, such as from Mycobacterium tuberculosis, are considerably longer, contain an apparent amidotransferase domain, and show glutamine-dependent as well as NH(3)-dependent activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]


Pssm-ID: 273132 [Multi-domain]  Cd Length: 250  Bit Score: 226.89  E-value: 2.66e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187   15 PTINVEAEVRkrvDFLKSYVTKTGSKGLLIAISGGIDSAVAAALCKQATDEltqeqgqeyKTLGVFQPYGQQ---EDIEH 91
Cdd:TIGR00552   1 NLIKYVEEIE---DFLRGYVQKSGAKGVVLGLSGGIDSAVVAALCVEALGE---------QNHALLLPHSVQtpeQDVQD 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187   92 SYAVAKAFNLKYageTNIKEAvDTIAVEVEHTLkDIGLERSITpqVRGNVKARTRMVVQYALANELNLLVVGTDHASEAI 171
Cdd:TIGR00552  69 ALALAEPLGINY---KNIDIA-PIAASFQAQTE-TGDELSDFL--AKGNLKARLRMAALYAIANKHNLLVLGTGNKSELM 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187  172 TGFYTKWGDGAVDITPLSTLNKRQVRLLASYLGVPQAILDKAPTAGLWEGQTDEKELGISYEANSDYLEGKEIDPAARE- 250
Cdd:TIGR00552 142 LGYFTKYGDGGCDIAPIGDLFKTQVYELAKRLNVPERIIEKPPTADLFDGQTDETELGITYDELDDYLKGIEELSQTVQe 221

                         250
                  ....*....|....*...
gi 309245187  251 ---KLESYFTRTAHKRTS 265
Cdd:TIGR00552 222 vvkRIESLVQKSEHKRRL 239
PRK13980 PRK13980
NAD synthetase; Provisional
 16-264 8.03e-70

NAD synthetase; Provisional


Pssm-ID: 184435 [Multi-domain]  Cd Length: 265  Bit Score: 216.23  E-value: 8.03e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187  16 TINVEAEVRKRVDFLKSYVTKTGSKGLLIAISGGIDSAVAAALCKQATdeltqeqGQEyKTLGVFQPY--GQQEDIEHSY 93
Cdd:PRK13980   7 ALDYEKVREIIVDFIREEVEKAGAKGVVLGLSGGIDSAVVAYLAVKAL-------GKE-NVLALLMPSsvSPPEDLEDAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187  94 AVAKAFNLKYAgETNIKEAVDTIAVevehTLKDIGLERsitpqvRGNVKARTRMVVQYALANELNLLVVGTDHASEAITG 173
Cdd:PRK13980  79 LVAEDLGIEYK-VIEITPIVDAFFS----AIPDADRLR------VGNIMARTRMVLLYDYANRENRLVLGTGNKSELLLG 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187 174 FYTKWGDGAVDITPLSTLNKRQVRLLASYLGVPQAILDKAPTAGLWEGQTDEKELGISYE--------------ANSDYL 239
Cdd:PRK13980 148 YFTKYGDGAVDLNPIGDLYKTQVRELARHLGVPEDIIEKPPSADLWEGQTDEGELGFSYEtideilyllfdkkmSREEIL 227

                        250       260
                 ....*....|....*....|....*
gi 309245187 240 EGKEIDPAAREKLESYFTRTAHKRT 264
Cdd:PRK13980 228 EELGVPEDLVDRVRRLVQRSQHKRR 252
NadE COG0171
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ...
 5-267 1.65e-61

NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ synthetase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439941 [Multi-domain]  Cd Length: 542  Bit Score: 202.77  E-value: 1.65e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187   5 EQIIAELGVQPTINVEAEVRKRVDFLKSYVTKTGSKGLLIAISGGIDSAVAAALCKQAtdeltqeQGQEyKTLGVFQPYG 84
Cdd:COG0171  252 AEAAPPPPEEEEMDLEEVYDALVLGLRDYVRKNGFKGVVLGLSGGIDSALVAALAVDA-------LGPE-NVLGVTMPSR 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187  85 Q--QEDIEHSYAVAKAFNLKYAgETNIKEAVDTIAVEVEHTLKdiGLERSITpqvRGNVKARTRMVVQYALANELNLLVV 162
Cdd:COG0171  324 YtsDESLEDAEELAENLGIEYE-EIDITPAVEAFLEALPHAFG--GELDDVA---EENLQARIRMVILMALANKFGGLVL 397

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187 163 GTDHASEAITGFYTKWGDGAVDITPLSTLNKRQVRLLASYLG-----VPQAILDKAPTAGLWEGQTDEKELGiSYE---- 233
Cdd:COG0171  398 GTGNKSELAVGYFTKYGDGAGDLAPIADLYKTQVYALARWLNrngevIPEDIIDKPPSAELRPGQTDEDELG-PYEvlda 476

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 309245187 234 ---------ANSDYLEGKEIDPAAREKLESYFTRTAHKRTSIP 267
Cdd:COG0171  477 ilyayveegLSPEEIAAAGYDREWVERVLRLVRRNEYKRRQPP 519
PTZ00323 PTZ00323
NAD+ synthase; Provisional
 3-262 3.93e-33

NAD+ synthase; Provisional


Pssm-ID: 185554 [Multi-domain]  Cd Length: 294  Bit Score: 122.19  E-value: 3.93e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187   3 LQEQIiAELGVQPTINVEAEVRKRVDFLKSYVTKTGSKGLLIAISGGIDSAVAAALCKQAtdeLTQEQGQEYKTLGVFQP 82
Cdd:PTZ00323  11 LQRVL-KEVRRKRAFNPAAWIEKKCAKLNEYMRRCGLKGCVTSVSGGIDSAVVLALCARA---MRMPNSPIQKNVGLCQP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187  83 YgqqedieHS--YAVAKAF-NLKYAGETNIkeAVDTIAVEVE-HTL--KDIGLERSitPQVRGNVKARTRMVVQYALANE 156
Cdd:PTZ00323  87 I-------HSsaWALNRGReNIQACGATEV--TVDQTEIHTQlSSLveKAVGIKGG--AFARGQLRSYMRTPVAFYVAQL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187 157 LN-----LLVVGTDHASE-AITGFYTKWGDGAVDITPLSTLNKRQVRLLASYLGVPQAILDKAPTAGLWEGQTDEKELGI 230
Cdd:PTZ00323 156 LSqegtpAVVMGTGNFDEdGYLGYFCKAGDGVVDVQLISDLHKSEVFLVARELGVPENTLQAAPSADLWEGQTDEDELGF 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 309245187 231 SYE----ANSDYLEGKE---------IDPAAREKLESY-------FTRTAHK 262
Cdd:PTZ00323 236 PYDfvelYTEWYLKLNEtekksflssLSEEARKQFEEYsaacelvHRRNAHK 287
nadE PRK00876
NAD(+) synthase;
16-225 9.85e-29

NAD(+) synthase;


Pssm-ID: 179150 [Multi-domain]  Cd Length: 326  Bit Score: 111.20  E-value: 9.85e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187  16 TINVEAEVRKRVDFLKSYVTKT-GSKGLLIAISGGIDSAVAAALCkqatdelTQEQGQEyKTLGVFQP--YGQQEDIEHS 92
Cdd:PRK00876   9 KIDAAAEAERIRAAIREQVRGTlRRRGVVLGLSGGIDSSVTAALC-------VRALGKE-RVYGLLMPerDSSPESLRLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187  93 YAVAKAFNLKYAGE--TNIKEAVD------------------------TIAVEVEHTLKDIGLERSITPQ-----VR--- 138
Cdd:PRK00876  81 REVAEHLGVEYVVEdiTPALEALGcyrrrdeairrvvpeygpgwkskiVLPNLLDGDGLNVFSLVVQDPDgevtrKRlpa 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187 139 ---------GNVKARTRMVVQYALANELNLLVVGTDHASEAITGFYTKWGDGAVDITPLSTLNKRQVRLLASYLGVPQAI 209
Cdd:PRK00876 161 naylqivaaTNFKQRTRKMVEYYHADRLNYAVAGTPNRLEYDQGFFVKNGDGAADLKPIAHLYKTQVYALAEHLGVPEEI 240

                        250
                 ....*....|....*..
gi 309245187 210 LDKAPTAGLWE-GQTDE 225
Cdd:PRK00876 241 RRRPPTTDTYSlPQTQE 257
PRK13981 PRK13981
NAD synthetase; Provisional
 30-225 2.90e-25

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 104.08  E-value: 2.90e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187  30 LKSYVTKTGSKGLLIAISGGIDSAVAAALckqATDELtqeqGQEyKTLGVFQP--YGQQEDIEHSYAVAKAFNLKYAgET 107
Cdd:PRK13981 271 LRDYVRKNGFPGVVLGLSGGIDSALVAAI---AVDAL----GAE-RVRAVMMPsrYTSEESLDDAAALAKNLGVRYD-II 341

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187 108 NIKEAVDTiaveVEHTLKDI--GLERSITPQvrgNVKARTRMVVQYALANELNLLVVGTDHASEAITGFYTKWGDGAVDI 185
Cdd:PRK13981 342 PIEPAFEA----FEAALAPLfaGTEPDITEE---NLQSRIRGTLLMALSNKFGSLVLTTGNKSEMAVGYATLYGDMAGGF 414

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 309245187 186 TPLSTLNKRQVRLLASYLG-------VPQAILDKAPTAGLWEGQTDE 225
Cdd:PRK13981 415 APIKDVYKTLVYRLCRWRNtvspgevIPERIITKPPSAELRPNQTDQ 461
PLN02339 PLN02339
NAD+ synthase (glutamine-hydrolysing)
 33-233 1.43e-10

NAD+ synthase (glutamine-hydrolysing)


Pssm-ID: 177973 [Multi-domain]  Cd Length: 700  Bit Score: 61.24  E-value: 1.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187  33 YVTKTGSKGLLIAISGGIDS-AVAA---ALCKQATDELTQEQGQEYKTLGVFQPYGQQEDIEHSYAVAK-AFNLKYAGET 107
Cdd:PLN02339 342 YLRRSGASGFLLPLSGGADSsSVAAivgSMCQLVVKAIREGDEQVKADARRIGNYADGEVPTDSKEFAKrIFYTVYMGSE 421

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187 108 NIKEA--------------------VDTIAVEVehtlkdIGLERSIT---P--QVRG----------NVKARTRMVVQYA 152
Cdd:PLN02339 422 NSSEEtrsrakqladeigsshldvkIDGVVSAV------LSLFQTLTgkrPryKVDGgsnaenlalqNIQARIRMVLAFM 495

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187 153 LANELN--------LLVVGTDHASEAITGFYTKWGDGAVDITPLSTLNKRQVRLL----ASYLGVPQ-AILDKA-PTAGL 218
Cdd:PLN02339 496 LASLLPwvrgksgfLLVLGSANVDEGLRGYLTKYDCSSADINPIGGISKQDLRSFlrwaATNLGYPSlAEVEAApPTAEL 575

                        250       260
                 ....*....|....*....|
gi 309245187 219 W-----EGQTDEKELGISYE 233
Cdd:PLN02339 576 EpirddYSQTDEEDMGMTYE 595
GMP_synthase_C cd01997
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ...
 38-214 5.17e-05

C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP synthetase (glutamine-hydrolyzing, EC 6.3.5.2) contains two subdomains: the ATP pyrophosphatase domain at the N-terminal and the dimerization domain at the C-terminal end. The ATP-PPase domain is a twisted, five-stranded parallel beta-sheet sandwiched between helical layers. It has a signature nucleotide-binding motif, or PP-loop, at the end of the first-beta strand. GMP synthetase is a homodimer, but in some archaea, it is a heterodimer made up of ATP pyrophosphatase (ATP-PPase) and a GATase subunit. In eukaryotes and bacteria, the two catalytic units are encoded by a single gene producing a two-domain-type GMP with a GATase domain in the N-terminus and an ATP-PPase domain in the C-terminus.


Pssm-ID: 467501 [Multi-domain]  Cd Length: 311  Bit Score: 43.68  E-value: 5.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187  38 GSKGLLIAISGGIDSAVAAALCKQAtdeLTQEQgqeykTLGVFqpygqqedIEH-------SYAVAKAFnlKYAGETNIk 110
Cdd:cd01997    6 GDKKVLCLVSGGVDSTVCAALLHKA---LGDER-----VIAVH--------IDNglmrkneSEQVEEAL--KKLGVINL- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187 111 eAVDTIAVEVEHTLKDIglersITPQVRGNVKARTRMVVQYALANELNL------LVVGT-------------DHASEAI 171
Cdd:cd01997   67 -AKVDASKRFLKKLKGV-----TDPEEKRKIIGDTFIEVFDEVAKELNLdpddvyLAQGTlypdliesasslaSSKADTI 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 309245187 172 ------TGFYTKWGDGAVdITPLSTLNKRQVRLLASYLGVPQAILDKAP 214
Cdd:cd01997  141 kthhnvGGLPRELLKGKL-VEPLRDLFKDEVRELGRELGLPEELVWRHP 188
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
 43-103 1.57e-04

MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467502 [Multi-domain]  Cd Length: 349  Bit Score: 42.49  E-value: 1.57e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 309245187  43 LIAISGGIDSAVAAALCKqatdeltqEQGQEYktLGVF-----------QPYGQQEDIEHSYAVAKAFNLKY 103
Cdd:cd01998    3 AVAMSGGVDSSVAAALLK--------EQGYDV--IGVFmknwddednekGGCCSEEDIEDARRVADQLGIPL 64
QueC pfam06508
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ...
 43-103 2.59e-04

Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis of 7-carboxy-7-deazaguanine. They catalyze the conversion of 7-deaza-7-carboxyguanine to preQ0.


Pssm-ID: 428982 [Multi-domain]  Cd Length: 210  Bit Score: 41.06  E-value: 2.59e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 309245187   43 LIAISGGIDSAVAAALCKqatdeltqEQGQEYKTLGVFqpYGQQEDIEHSYA--VAKAFNLKY 103
Cdd:pfam06508   3 VVLLSGGLDSTTCLAWAK--------KEGYEVYALSFD--YGQRHRKELECAkkIAKALGVEH 55
guaA PRK00074
GMP synthase; Reviewed
 21-67 4.08e-04

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 41.19  E-value: 4.08e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 309245187  21 AEVRKRVdflksyvtktGSKGLLIAISGGIDSAVAAALCKQAT-DELT 67
Cdd:PRK00074 207 EEIREQV----------GDKKVILGLSGGVDSSVAAVLLHKAIgDQLT 244
tRNA_Me_trans pfam03054
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ...
 43-208 5.88e-04

tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs.


Pssm-ID: 460787 [Multi-domain]  Cd Length: 202  Bit Score: 39.93  E-value: 5.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187   43 LIAISGGIDSAVAAALCKqatdeltqEQGqeYKTLGVF----------QPYGQ---QEDIEHSYAVAKAFNLKYagetni 109
Cdd:pfam03054   4 VVAMSGGVDSSVAAYLLK--------EQG--HNVIGVFmknwdeeqslDEEGKccsEEDLADAQRVCEQLGIPL------ 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309245187  110 kEAVDT-----IAVeVEHTLKDIGLERSITPQVRGNVKARTRMVVQYALANelnllvVGTDhaseAI-TGFYTK---WGD 180
Cdd:pfam03054  68 -YVVNFekeywEDV-FEPFLDEYKNGRTPNPDVLCNKEIKFGALLDYALEN------LGAD----YVaTGHYARvslNKD 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 309245187  181 G------AVD--------------------ITPLSTLNKRQVRLLASYLGVPQA 208
Cdd:pfam03054 136 GgsellrALDknkdqsyflstlsqeqleklLFPLGELTKEEVRKIAKEAGLATA 189
MnmA COG0482
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ...
 43-80 1.07e-03

tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ribosomal structure and biogenesis]; tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440250 [Multi-domain]  Cd Length: 353  Bit Score: 40.04  E-value: 1.07e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 309245187  43 LIAISGGIDSAVAAALCKqatdeltqEQGqeYKTLGVF 80
Cdd:COG0482    4 VVGMSGGVDSSVAAALLK--------EQG--YEVIGVT 31
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
 43-80 3.96e-03

tRNA-specific 2-thiouridylase MnmA; Reviewed


Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 38.13  E-value: 3.96e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 309245187  43 LIAISGGIDSAVAAALCKqatdeltqEQGqeYKTLGVF 80
Cdd:PRK00143   4 VVGMSGGVDSSVAAALLK--------EQG--YEVIGVF 31
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH