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Conserved domains on  [gi|971483006|ref|YP_009194505|]
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anaerobic ribonucleotide reductase small subunit [Klebsiella phage Matisse]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NrdG super family cl37123
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
 2-151 1.31e-69

anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of the radical-SAM family (pfam04055) and utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487). The two components form an alpha-2/beta-2 heterodimer. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism, Protein fate, Protein modification and repair]


The actual alignment was detected with superfamily member TIGR02491:

Pssm-ID: 274161 [Multi-domain]  Cd Length: 154  Bit Score: 207.20  E-value: 1.31e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971483006    2 NYIRIYNMDVVNGKGIRVVLFVAGCNHKCDGCYNRSSWNPCNGTPYTEETENHLISLLS-NPHVDGLTLTGGDPLYRDNY 80
Cdd:TIGR02491   1 NYMNIKPDDIVNGEGIRVSLFVAGCKHHCEGCFNKETWNFNGGKEFTEALEKEIIRDLNdNPLIDGLTLSGGDPLYPRNV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 971483006   81 PTILKLLERVSKELPKKNVWLWTGYTLEALQADPERSKLLPYIDVLIDGKYEKDLPTKKP-FRGSDNQRMIE 151
Cdd:TIGR02491  81 EELIELVKKIKAEFPEKDIWLWTGYTWEEILEDEKHLEVLKYIDVLVDGKFELSKKDLKLkFRGSSNQRIID 152
 
Name Accession Description Interval E-value
NrdG TIGR02491
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
 2-151 1.31e-69

anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of the radical-SAM family (pfam04055) and utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487). The two components form an alpha-2/beta-2 heterodimer. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism, Protein fate, Protein modification and repair]


Pssm-ID: 274161 [Multi-domain]  Cd Length: 154  Bit Score: 207.20  E-value: 1.31e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971483006    2 NYIRIYNMDVVNGKGIRVVLFVAGCNHKCDGCYNRSSWNPCNGTPYTEETENHLISLLS-NPHVDGLTLTGGDPLYRDNY 80
Cdd:TIGR02491   1 NYMNIKPDDIVNGEGIRVSLFVAGCKHHCEGCFNKETWNFNGGKEFTEALEKEIIRDLNdNPLIDGLTLSGGDPLYPRNV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 971483006   81 PTILKLLERVSKELPKKNVWLWTGYTLEALQADPERSKLLPYIDVLIDGKYEKDLPTKKP-FRGSDNQRMIE 151
Cdd:TIGR02491  81 EELIELVKKIKAEFPEKDIWLWTGYTWEEILEDEKHLEVLKYIDVLVDGKFELSKKDLKLkFRGSSNQRIID 152
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
 12-150 3.66e-65

4Fe-4S single cluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 433138 [Multi-domain]  Cd Length: 137  Bit Score: 195.47  E-value: 3.66e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971483006   12 VNGKGIRVVLFVAGCNHKCDGCYNRSSWNPCNGTPYTEETENHLISLLSNPHVDGLTLTGGDPLYrdNYPTILKLLERVS 91
Cdd:pfam13353   1 VNGPGVRCSLFVSGCNHHCKGCFNPETWDFKYGKPFTEELEDEIIEDLAKPYIQGLTLSGGEPLL--NAEALLELVKRVR 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 971483006   92 KELPKKNVWLWTGYTLEALQADpERSKLLPYIDVLIDGKYEKDLPT-KKPFRGSDNQRMI 150
Cdd:pfam13353  79 EECPEKDIWLWTGYTFEELQSK-DQLELLKLIDVLVDGKFEQSLKDpSLRFRGSSNQRII 137
nrdG PRK11121
anaerobic ribonucleoside-triphosphate reductase-activating protein;
1-147 3.46e-64

anaerobic ribonucleoside-triphosphate reductase-activating protein;


Pssm-ID: 236853  Cd Length: 154  Bit Score: 193.67  E-value: 3.46e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971483006   1 MNYIRIYNMDVVNGKGIRVVLFVAGCNHKCDGCYNRSSWNPCNGTPYTEETENHLISLLSNPHV--DGLTLTGGDPLYRD 78
Cdd:PRK11121   1 MNYHQYYPVDVVNGPGTRCTLFVSGCVHQCPGCYNKSTWRLNSGHPFTKEMEDQIIADLNDTRIkrQGLSLSGGDPLHPQ 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 971483006  79 NYPTILKLLERVSKELPKKNVWLWTGYTLEALqaDPERSKLLPYIDVLIDGKYEKDLptKKP---FRGSDNQ 147
Cdd:PRK11121  81 NVPDILKLVQRVKAECPGKDIWVWTGYKLDEL--NAAQRQVVDLIDVLVDGKFVQDL--ADPsliWRGSSNQ 148
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
 5-154 2.45e-12

Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 62.51  E-value: 2.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971483006   5 RIYN---MDVVNGKG-IRVVLFVAGCNHKCDGCYNRSSWNPCNGTPYTEETENHLISLLSNP-----HVDGLTLTGGDPL 75
Cdd:COG1180    6 RIYGispFSTVDGPGsIRLSVFTQGCNLRCPYCHNPEISQGRPDAAGRELSPEELVEEALKDrgfldSCGGVTFSGGEPT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971483006  76 YrdNYPTILKLLERVsKELPKKNVWLWTGY-TLEALQadpersKLLPYID-VLID------GKYEKdlptkkpFRGSDNQ 147
Cdd:COG1180   86 L--QPEFLLDLAKLA-KELGLHTALDTNGYiPEEALE------ELLPYLDaVNIDlkafddEFYRK-------LTGVSLE 149


                 ....*..
gi 971483006 148 RMIEFAK 154
Cdd:COG1180  150 PVLENLE 156
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 20-160 2.23e-06

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 45.79  E-value: 2.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971483006  20 VLFVAGCNHKCDGCYNRSSWNPCNGTPYTEETENHLISLLSNPHVDGLTLTGGDPLYrdnYPTILKLLERVSKELPKKNV 99
Cdd:cd01335    1 LELTRGCNLNCGFCSNPASKGRGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLL---YPELAELLRRLKKELPGFEI 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 971483006 100 -WLWTGY--TLEALQADPERSKLlpYIDVLIDGKYEkDLPTKKPFRGSDNQRMIEFAKNSIEIK 160
Cdd:cd01335   78 sIETNGTllTEELLKELKELGLD--GVGVSLDSGDE-EVADKIRGSGESFKERLEALKELREAG 138
 
Name Accession Description Interval E-value
NrdG TIGR02491
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
 2-151 1.31e-69

anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of the radical-SAM family (pfam04055) and utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487). The two components form an alpha-2/beta-2 heterodimer. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism, Protein fate, Protein modification and repair]


Pssm-ID: 274161 [Multi-domain]  Cd Length: 154  Bit Score: 207.20  E-value: 1.31e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971483006    2 NYIRIYNMDVVNGKGIRVVLFVAGCNHKCDGCYNRSSWNPCNGTPYTEETENHLISLLS-NPHVDGLTLTGGDPLYRDNY 80
Cdd:TIGR02491   1 NYMNIKPDDIVNGEGIRVSLFVAGCKHHCEGCFNKETWNFNGGKEFTEALEKEIIRDLNdNPLIDGLTLSGGDPLYPRNV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 971483006   81 PTILKLLERVSKELPKKNVWLWTGYTLEALQADPERSKLLPYIDVLIDGKYEKDLPTKKP-FRGSDNQRMIE 151
Cdd:TIGR02491  81 EELIELVKKIKAEFPEKDIWLWTGYTWEEILEDEKHLEVLKYIDVLVDGKFELSKKDLKLkFRGSSNQRIID 152
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
 12-150 3.66e-65

4Fe-4S single cluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 433138 [Multi-domain]  Cd Length: 137  Bit Score: 195.47  E-value: 3.66e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971483006   12 VNGKGIRVVLFVAGCNHKCDGCYNRSSWNPCNGTPYTEETENHLISLLSNPHVDGLTLTGGDPLYrdNYPTILKLLERVS 91
Cdd:pfam13353   1 VNGPGVRCSLFVSGCNHHCKGCFNPETWDFKYGKPFTEELEDEIIEDLAKPYIQGLTLSGGEPLL--NAEALLELVKRVR 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 971483006   92 KELPKKNVWLWTGYTLEALQADpERSKLLPYIDVLIDGKYEKDLPT-KKPFRGSDNQRMI 150
Cdd:pfam13353  79 EECPEKDIWLWTGYTFEELQSK-DQLELLKLIDVLVDGKFEQSLKDpSLRFRGSSNQRII 137
nrdG PRK11121
anaerobic ribonucleoside-triphosphate reductase-activating protein;
1-147 3.46e-64

anaerobic ribonucleoside-triphosphate reductase-activating protein;


Pssm-ID: 236853  Cd Length: 154  Bit Score: 193.67  E-value: 3.46e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971483006   1 MNYIRIYNMDVVNGKGIRVVLFVAGCNHKCDGCYNRSSWNPCNGTPYTEETENHLISLLSNPHV--DGLTLTGGDPLYRD 78
Cdd:PRK11121   1 MNYHQYYPVDVVNGPGTRCTLFVSGCVHQCPGCYNKSTWRLNSGHPFTKEMEDQIIADLNDTRIkrQGLSLSGGDPLHPQ 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 971483006  79 NYPTILKLLERVSKELPKKNVWLWTGYTLEALqaDPERSKLLPYIDVLIDGKYEKDLptKKP---FRGSDNQ 147
Cdd:PRK11121  81 NVPDILKLVQRVKAECPGKDIWVWTGYKLDEL--NAAQRQVVDLIDVLVDGKFVQDL--ADPsliWRGSSNQ 148
Fer4_14 pfam13394
4Fe-4S single cluster domain;
21-130 1.35e-37

4Fe-4S single cluster domain;


Pssm-ID: 433171 [Multi-domain]  Cd Length: 115  Bit Score: 124.78  E-value: 1.35e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971483006   21 LFVAGCNHKCDGCYNRSSWNPCNGTPYTEETENHLISLL--SNPHVDGLTLTGGDPLYRDNYPTILKLLERVSKELPKKN 98
Cdd:pfam13394   1 LFVSGCNHSCPGCDNKETWKFNYGEPFTEELEDQIIADLkdSYIKRQGLVLTGGEPLHPWNLPVLLKLLKRVKEEYPSKD 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 971483006   99 VWLWTGYTLEALQADP---ERSKLLPYIDVLIDGK 130
Cdd:pfam13394  81 IWLETGYTLAIDFEYPdteEQLFTLSVIDVLVDGK 115
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
 5-154 2.45e-12

Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 62.51  E-value: 2.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971483006   5 RIYN---MDVVNGKG-IRVVLFVAGCNHKCDGCYNRSSWNPCNGTPYTEETENHLISLLSNP-----HVDGLTLTGGDPL 75
Cdd:COG1180    6 RIYGispFSTVDGPGsIRLSVFTQGCNLRCPYCHNPEISQGRPDAAGRELSPEELVEEALKDrgfldSCGGVTFSGGEPT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971483006  76 YrdNYPTILKLLERVsKELPKKNVWLWTGY-TLEALQadpersKLLPYID-VLID------GKYEKdlptkkpFRGSDNQ 147
Cdd:COG1180   86 L--QPEFLLDLAKLA-KELGLHTALDTNGYiPEEALE------ELLPYLDaVNIDlkafddEFYRK-------LTGVSLE 149


                 ....*..
gi 971483006 148 RMIEFAK 154
Cdd:COG1180  150 PVLENLE 156
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
 25-113 2.15e-06

Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation.


Pssm-ID: 427681 [Multi-domain]  Cd Length: 159  Bit Score: 45.21  E-value: 2.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971483006   25 GCNHKCDGCYNRSSWNPCNGTPYTEETENHLISLLSNPHVDGLTLTGGDPLYRDNYPTILKLLERVSKELPKKNVWLWTG 104
Cdd:pfam04055   4 GCNLRCTYCAFPSIRARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLELAEGIRITLETNG 83


                  ....*....
gi 971483006  105 YTLEALQAD 113
Cdd:pfam04055  84 TLLDEELLE 92
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 20-160 2.23e-06

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 45.79  E-value: 2.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971483006  20 VLFVAGCNHKCDGCYNRSSWNPCNGTPYTEETENHLISLLSNPHVDGLTLTGGDPLYrdnYPTILKLLERVSKELPKKNV 99
Cdd:cd01335    1 LELTRGCNLNCGFCSNPASKGRGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLL---YPELAELLRRLKKELPGFEI 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 971483006 100 -WLWTGY--TLEALQADPERSKLlpYIDVLIDGKYEkDLPTKKPFRGSDNQRMIEFAKNSIEIK 160
Cdd:cd01335   78 sIETNGTllTEELLKELKELGLD--GVGVSLDSGDE-EVADKIRGSGESFKERLEALKELREAG 138
pflA PRK11145
pyruvate formate lyase 1-activating protein;
12-40 3.11e-04

pyruvate formate lyase 1-activating protein;


Pssm-ID: 182994 [Multi-domain]  Cd Length: 246  Bit Score: 39.63  E-value: 3.11e-04
                         10        20
                 ....*....|....*....|....*....
gi 971483006  12 VNGKGIRVVLFVAGCNHKCDGCYNRSSWN 40
Cdd:PRK11145  16 VDGPGIRFITFFQGCLMRCLYCHNRDTWD 44
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
 21-89 4.75e-04

Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic radical activating enzyme NrdG/QueE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440367 [Multi-domain]  Cd Length: 205  Bit Score: 38.97  E-value: 4.75e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 971483006  21 LFV--AGCNHKCDGC---YnrsSWNPCNGTPYTEETENHLISLLSNPHVdglTLTGGDPL-YRDNYPTILKLLER 89
Cdd:COG0602   23 VFVrlAGCNLRCSWCdtkY---AWDGEGGKRMSAEEILEEVAALGARHV---VITGGEPLlQDDLAELLEALKDA 91
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
 26-110 1.37e-03

Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, chromosome partitioning, Coenzyme transport and metabolism];


Pssm-ID: 440301 [Multi-domain]  Cd Length: 159  Bit Score: 37.19  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971483006  26 CNHKCDGCYNRSswNPCNGTPYTEETENHLISLLSNPHVDGLTLTGGDPLYRDNyptILKLLERVSKELPKKNV----WL 101
Cdd:COG0535   10 CNLRCKHCYADA--GPKRPGELSTEEAKRILDELAELGVKVVGLTGGEPLLRPD---LFELVEYAKELGIRVNLstngTL 84


                 ....*....
gi 971483006 102 WTGYTLEAL 110
Cdd:COG0535   85 LTEELAERL 93
NrdG2 TIGR02495
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
 20-75 6.97e-03

anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of the radical-SAM family (pfam04055). It is often gene clustered with the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487) and presumably fulfills the identical function as NrdG, which utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in NrdD. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism, Protein fate, Protein modification and repair]


Pssm-ID: 274164 [Multi-domain]  Cd Length: 192  Bit Score: 35.42  E-value: 6.97e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 971483006   20 VLFVAGCNHKCDGCYNrssWNPcngtPYTEETE----NHLISLL--SNPHVDGLTLTGGDPL 75
Cdd:TIGR02495  20 TIFLQGCNLKCPYCHN---PLL----IPRRGSGeievEELLEFLrrRRGLLDGVVITGGEPT 74
 
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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