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Conserved domains on  [gi|15229476|ref|NP_189000|]
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ribonucleotide reductase 2A [Arabidopsis thaliana]

Protein Classification

ribonucleoside-diphosphate reductase small subunit( domain architecture ID 10791385)

ribonucleoside-diphosphate reductase small subunit catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02492 PLN02492
ribonucleoside-diphosphate reductase
 19-341 0e+00

ribonucleoside-diphosphate reductase


:

Pssm-ID: 215272  Cd Length: 324  Bit Score: 690.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476   19 EPLLMAQNQRFTMFPIRYKSIWEMYKKAEASFWTAEEVDLSTDVQQWEALTDSEKHFISHILAFFAASDGIVLENLAARF 98
Cdd:PLN02492   1 EPLLAENPDRFCMFPIKYPQIWEMYKKAEASFWTAEEVDLSADLKDWEKLTDDERHFISHVLAFFAASDGIVLENLAARF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476   99 LNDVQVPEARAFYGFQIAMENIHSEMYSLLLETFIKDSKEKDRLFNAIETIPCISKKAKWCLDWIQSPMSFAVRLVAFAC 178
Cdd:PLN02492  81 MKEVQVPEARAFYGFQIAIENIHSEMYSLLLDTYIKDPKEKDRLFNAIETIPCVAKKADWALRWIDSSASFAERLVAFAC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  179 VEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLQKQLPLEKVYQIVHEAVEIETEFVCKALPC 258
Cdd:PLN02492 161 VEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLKNKLSEERVKEIVCEAVEIEKEFVCDALPC 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  259 DLIGMNSNLMSQYIQFVADRLLVTLGCERTYKAENPFDWMEFISLQGKTNFFEKRVGEYQKASVMSNLQNG-NQNYEFTT 337
Cdd:PLN02492 241 ALVGMNADLMSQYIEFVADRLLVALGYEKVYNVVNPFDWMELISLQGKTNFFEKRVGEYQKAGVMSSLNGGgADNHVFSL 320


                 ....
gi 15229476  338 EEDF 341
Cdd:PLN02492 321 DEDF 324
 
Name Accession Description Interval E-value
PLN02492 PLN02492
ribonucleoside-diphosphate reductase
 19-341 0e+00

ribonucleoside-diphosphate reductase


Pssm-ID: 215272  Cd Length: 324  Bit Score: 690.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476   19 EPLLMAQNQRFTMFPIRYKSIWEMYKKAEASFWTAEEVDLSTDVQQWEALTDSEKHFISHILAFFAASDGIVLENLAARF 98
Cdd:PLN02492   1 EPLLAENPDRFCMFPIKYPQIWEMYKKAEASFWTAEEVDLSADLKDWEKLTDDERHFISHVLAFFAASDGIVLENLAARF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476   99 LNDVQVPEARAFYGFQIAMENIHSEMYSLLLETFIKDSKEKDRLFNAIETIPCISKKAKWCLDWIQSPMSFAVRLVAFAC 178
Cdd:PLN02492  81 MKEVQVPEARAFYGFQIAIENIHSEMYSLLLDTYIKDPKEKDRLFNAIETIPCVAKKADWALRWIDSSASFAERLVAFAC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  179 VEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLQKQLPLEKVYQIVHEAVEIETEFVCKALPC 258
Cdd:PLN02492 161 VEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLKNKLSEERVKEIVCEAVEIEKEFVCDALPC 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  259 DLIGMNSNLMSQYIQFVADRLLVTLGCERTYKAENPFDWMEFISLQGKTNFFEKRVGEYQKASVMSNLQNG-NQNYEFTT 337
Cdd:PLN02492 241 ALVGMNADLMSQYIEFVADRLLVALGYEKVYNVVNPFDWMELISLQGKTNFFEKRVGEYQKAGVMSSLNGGgADNHVFSL 320


                 ....
gi 15229476  338 EEDF 341
Cdd:PLN02492 321 DEDF 324
Ribonuc_red_sm pfam00268
Ribonucleotide reductase, small chain;
28-294 2.90e-147

Ribonucleotide reductase, small chain;


Pssm-ID: 425568 [Multi-domain]  Cd Length: 276  Bit Score: 416.13  E-value: 2.90e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476    28 RFTMFPIRYKSIWEMYKKAEASFWTAEEVDLSTDVQQWEALTDSEKHFISHILAFFAASDGIVLENLAARFLNDVQVPEA 107
Cdd:pfam00268   1 RFNLNPIKYPEIWEFYKKLEANFWTPEEIPLSKDIKDWKKLSEDEREFIKRVLAFLALLDTLVNENLVERFSREVQTPEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476   108 RAFYGFQIAMENIHSEMYSLLLETFIKDSKEKDRLFNAIETIPCISKKAKWCLDWIQSPMS-FAVRLVAFACVEGIFFSG 186
Cdd:pfam00268  81 RAFYGFQAFMENIHSESYSYILDTLGKDPEEIDELFNWIETNPALQKKAEWILKWYQDFDSdFLERLVAFAILEGIFFYS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476   187 SFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLQKQLPL-------EKVYQIVHEAVEIETEFVCKALPCD 259
Cdd:pfam00268 161 GFAAILWLKRRGKMPGLAEIIELISRDEGLHGDFACLLFQHLKEENPEletkelkEEVYDLIKEAVELEKEFLDDALPVG 240

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 15229476   260 LIGMNSNLMSQYIQFVADRLLVTLGCERTYKAE-NP 294
Cdd:pfam00268 241 LLGMNAEDVKQYIEYVADRRLMNLGYEKLYNVEvNP 276
RNRR2 cd01049
Ribonucleotide Reductase, R2/beta subunit, ferritin-like diiron-binding domain; Ribonucleotide ...
 29-303 4.06e-135

Ribonucleotide Reductase, R2/beta subunit, ferritin-like diiron-binding domain; Ribonucleotide Reductase, R2/beta subunit (RNRR2) is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. The RNR protein catalyzes the conversion of ribonucleotides to deoxyribonucleotides and is found in all eukaryotes, many prokaryotes, several viruses, and few archaea. The catalytically active form of RNR is a proposed alpha2-beta2 tetramer. The homodimeric alpha subunit (R1) contains the active site and redox active cysteines as well as the allosteric binding sites. The beta subunit (R2) contains a diiron cluster that, in its reduced state, reacts with dioxygen to form a stable tyrosyl radical and a diiron(III) cluster. This essential tyrosyl radical is proposed to generate a thiyl radical, located on a cysteine residue in the R1 active site that initiates ribonucleotide reduction. The beta subunit is composed of 10-13 helices, the 8 longest helices form an alpha-helical bundle; some have 2 addition beta strands. Yeast is unique in that it assembles both homodimers and heterodimers of RNRR2. The yeast heterodimer, Y2Y4, contains R2 (Y2) and a R2 homolog (Y4) that lacks the diiron center and is proposed to only assist in cofactor assembly, and perhaps stabilize R1 (Y1) in its active conformation.


Pssm-ID: 153108 [Multi-domain]  Cd Length: 288  Bit Score: 385.83  E-value: 4.06e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  29 FTMFPIRYKSIWEMYKKAEASFWTAEEVDLSTDVQQWEALTDSEKHFISHILAFFAASDGIVLENLAARFLNDVQVPEAR 108
Cdd:cd01049   1 FNLNPIKYPWAWELYKKAEANFWTPEEIDLSKDLKDWEKLTEAERHFIKRVLAFLAALDSIVGENLVELFSRHVQIPEAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476 109 AFYGFQIAMENIHSEMYSLLLETFIKDSkEKDRLFNAIETIPCISKKAKWCLDWIQ-----SPMSFAVRLVAFACVEGIF 183
Cdd:cd01049  81 AFYGFQAFMENIHSESYSYILDTLGKDE-ERDELFEAIETDPALKKKADWILRWYDnlddnTKESFAERLVAFAILEGIF 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476 184 FSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLQKQLPL-------EKVYQIVHEAVEIETEFVCKAL 256
Cdd:cd01049 160 FYSGFAAIFWLARRGKMPGLAEIIELISRDESLHGDFACLLIRELLNENPElfteefkEEVYELIKEAVELEKEFARDLL 239

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15229476 257 PCDLIGMNSNLMSQYIQFVADRLLVTLGCERTY--KAENPFDWMEFISL 303
Cdd:cd01049 240 PDGILGLNKEDMKQYIEYVANRRLENLGLEKLFnvEDKNPFDWMELISD 288
NrdB COG0208
Ribonucleotide reductase beta subunit, ferritin-like domain [Nucleotide transport and ...
 17-324 2.28e-118

Ribonucleotide reductase beta subunit, ferritin-like domain [Nucleotide transport and metabolism]; Ribonucleotide reductase beta subunit, ferritin-like domain is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 439978 [Multi-domain]  Cd Length: 326  Bit Score: 344.46  E-value: 2.28e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  17 SEEPLLMAQN-QRFTMFPIRYKSIWEMYKKAEASFWTAEEVDLSTDVQQWEALTDSEKHFISHILAFFAASDGIVLENLA 95
Cdd:COG0208   1 LDEPIINGLTtNRINWNPIKYPWAYELYKKQLANFWLPEEVPLSNDIKDWKKLSDDERHLIKRVLGFLTLLDSIQGNNLV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  96 ARFLNDVQVPEARAFYGFQIAMENIHSEMYSLLLETFIKDskeKDRLFNAIETIPCISKKAKWCLDWIQ------SPMSF 169
Cdd:COG0208  81 LALYPHVTAPEVRAVLSRQAFMEAIHAKSYSYILETLGLD---IDEIFNWIEENPALQKKAEFILKYYDdlgtreTKKDL 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476 170 AVRLVAFACVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLQKQLPL-------EKVYQIVH 242
Cdd:COG0208 158 LKSLVASVFLEGIFFYSGFAYPLSLARRGKMKGTAEIIRLILRDESLHGNFGIYLINTIREENPElfteelkEEIYELLK 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476 243 EAVEIETEFVCKALPCDLIGMNSNLMSQYIQFVADRLLVTLGCERTY-KAENPFDWM-EFISLQGKTNFFEKRVGEYQKA 320
Cdd:COG0208 238 EAVELEKEYADDLFPDGILGLNAEDVKQYIRYIANKRLMNLGLEPLFeGDVNPFPWMsEGLDLNKKTDFFETRVTEYQKG 317


                ....
gi 15229476 321 SVMS 324
Cdd:COG0208 318 GVES 321
 
Name Accession Description Interval E-value
PLN02492 PLN02492
ribonucleoside-diphosphate reductase
 19-341 0e+00

ribonucleoside-diphosphate reductase


Pssm-ID: 215272  Cd Length: 324  Bit Score: 690.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476   19 EPLLMAQNQRFTMFPIRYKSIWEMYKKAEASFWTAEEVDLSTDVQQWEALTDSEKHFISHILAFFAASDGIVLENLAARF 98
Cdd:PLN02492   1 EPLLAENPDRFCMFPIKYPQIWEMYKKAEASFWTAEEVDLSADLKDWEKLTDDERHFISHVLAFFAASDGIVLENLAARF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476   99 LNDVQVPEARAFYGFQIAMENIHSEMYSLLLETFIKDSKEKDRLFNAIETIPCISKKAKWCLDWIQSPMSFAVRLVAFAC 178
Cdd:PLN02492  81 MKEVQVPEARAFYGFQIAIENIHSEMYSLLLDTYIKDPKEKDRLFNAIETIPCVAKKADWALRWIDSSASFAERLVAFAC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  179 VEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLQKQLPLEKVYQIVHEAVEIETEFVCKALPC 258
Cdd:PLN02492 161 VEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLKNKLSEERVKEIVCEAVEIEKEFVCDALPC 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  259 DLIGMNSNLMSQYIQFVADRLLVTLGCERTYKAENPFDWMEFISLQGKTNFFEKRVGEYQKASVMSNLQNG-NQNYEFTT 337
Cdd:PLN02492 241 ALVGMNADLMSQYIEFVADRLLVALGYEKVYNVVNPFDWMELISLQGKTNFFEKRVGEYQKAGVMSSLNGGgADNHVFSL 320


                 ....
gi 15229476  338 EEDF 341
Cdd:PLN02492 321 DEDF 324
PTZ00211 PTZ00211
ribonucleoside-diphosphate reductase small subunit; Provisional
 9-341 0e+00

ribonucleoside-diphosphate reductase small subunit; Provisional


Pssm-ID: 240315 [Multi-domain]  Cd Length: 330  Bit Score: 591.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476    9 GRDMEEGESEEPLLMAQNQRFTMFPIRYKSIWEMYKKAEASFWTAEEVDLSTDVQQWEALTDSEKHFISHILAFFAASDG 88
Cdd:PTZ00211   2 KEAMKENEEEEPLLKENPDRFVLFPIKYPDIWRMYKKAEASFWTAEEIDLGNDLKDWEKLNDGERHFIKHVLAFFAASDG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476   89 IVLENLAARFLNDVQVPEARAFYGFQIAMENIHSEMYSLLLETFIKDSKEKDRLFNAIETIPCISKKAKWCLDWIQSPMS 168
Cdd:PTZ00211  82 IVLENLAQRFMREVQVPEARCFYGFQIAMENIHSETYSLLIDTYITDEEEKDRLFHAIETIPAIKKKAEWAAKWINSSNS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  169 FAVRLVAFACVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLQKQLPLEKVYQIVHEAVEIE 248
Cdd:PTZ00211 162 FAERLVAFAAVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHTDFACLLYSHLKNKLPRERVQEIIKEAVEIE 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  249 TEFVCKALPCDLIGMNSNLMSQYIQFVADRLLVTLGCERTYKAENPFDWMEFISLQGKTNFFEKRVGEYQKASVMSNlqn 328
Cdd:PTZ00211 242 REFICDALPVDLIGMNSRLMAQYIEFVADRLLVALGVPKIYNSKNPFDWMDMISLQGKTNFFEKRVGEYQKAGVMAE--- 318

                        330
                 ....*....|...
gi 15229476  329 gNQNYEFTTEEDF 341
Cdd:PTZ00211 319 -RTSKVFSLDADF 330
Ribonuc_red_sm pfam00268
Ribonucleotide reductase, small chain;
28-294 2.90e-147

Ribonucleotide reductase, small chain;


Pssm-ID: 425568 [Multi-domain]  Cd Length: 276  Bit Score: 416.13  E-value: 2.90e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476    28 RFTMFPIRYKSIWEMYKKAEASFWTAEEVDLSTDVQQWEALTDSEKHFISHILAFFAASDGIVLENLAARFLNDVQVPEA 107
Cdd:pfam00268   1 RFNLNPIKYPEIWEFYKKLEANFWTPEEIPLSKDIKDWKKLSEDEREFIKRVLAFLALLDTLVNENLVERFSREVQTPEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476   108 RAFYGFQIAMENIHSEMYSLLLETFIKDSKEKDRLFNAIETIPCISKKAKWCLDWIQSPMS-FAVRLVAFACVEGIFFSG 186
Cdd:pfam00268  81 RAFYGFQAFMENIHSESYSYILDTLGKDPEEIDELFNWIETNPALQKKAEWILKWYQDFDSdFLERLVAFAILEGIFFYS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476   187 SFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLQKQLPL-------EKVYQIVHEAVEIETEFVCKALPCD 259
Cdd:pfam00268 161 GFAAILWLKRRGKMPGLAEIIELISRDEGLHGDFACLLFQHLKEENPEletkelkEEVYDLIKEAVELEKEFLDDALPVG 240

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 15229476   260 LIGMNSNLMSQYIQFVADRLLVTLGCERTYKAE-NP 294
Cdd:pfam00268 241 LLGMNAEDVKQYIEYVADRRLMNLGYEKLYNVEvNP 276
RNRR2 cd01049
Ribonucleotide Reductase, R2/beta subunit, ferritin-like diiron-binding domain; Ribonucleotide ...
 29-303 4.06e-135

Ribonucleotide Reductase, R2/beta subunit, ferritin-like diiron-binding domain; Ribonucleotide Reductase, R2/beta subunit (RNRR2) is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. The RNR protein catalyzes the conversion of ribonucleotides to deoxyribonucleotides and is found in all eukaryotes, many prokaryotes, several viruses, and few archaea. The catalytically active form of RNR is a proposed alpha2-beta2 tetramer. The homodimeric alpha subunit (R1) contains the active site and redox active cysteines as well as the allosteric binding sites. The beta subunit (R2) contains a diiron cluster that, in its reduced state, reacts with dioxygen to form a stable tyrosyl radical and a diiron(III) cluster. This essential tyrosyl radical is proposed to generate a thiyl radical, located on a cysteine residue in the R1 active site that initiates ribonucleotide reduction. The beta subunit is composed of 10-13 helices, the 8 longest helices form an alpha-helical bundle; some have 2 addition beta strands. Yeast is unique in that it assembles both homodimers and heterodimers of RNRR2. The yeast heterodimer, Y2Y4, contains R2 (Y2) and a R2 homolog (Y4) that lacks the diiron center and is proposed to only assist in cofactor assembly, and perhaps stabilize R1 (Y1) in its active conformation.


Pssm-ID: 153108 [Multi-domain]  Cd Length: 288  Bit Score: 385.83  E-value: 4.06e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  29 FTMFPIRYKSIWEMYKKAEASFWTAEEVDLSTDVQQWEALTDSEKHFISHILAFFAASDGIVLENLAARFLNDVQVPEAR 108
Cdd:cd01049   1 FNLNPIKYPWAWELYKKAEANFWTPEEIDLSKDLKDWEKLTEAERHFIKRVLAFLAALDSIVGENLVELFSRHVQIPEAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476 109 AFYGFQIAMENIHSEMYSLLLETFIKDSkEKDRLFNAIETIPCISKKAKWCLDWIQ-----SPMSFAVRLVAFACVEGIF 183
Cdd:cd01049  81 AFYGFQAFMENIHSESYSYILDTLGKDE-ERDELFEAIETDPALKKKADWILRWYDnlddnTKESFAERLVAFAILEGIF 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476 184 FSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLQKQLPL-------EKVYQIVHEAVEIETEFVCKAL 256
Cdd:cd01049 160 FYSGFAAIFWLARRGKMPGLAEIIELISRDESLHGDFACLLIRELLNENPElfteefkEEVYELIKEAVELEKEFARDLL 239

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15229476 257 PCDLIGMNSNLMSQYIQFVADRLLVTLGCERTY--KAENPFDWMEFISL 303
Cdd:cd01049 240 PDGILGLNKEDMKQYIEYVANRRLENLGLEKLFnvEDKNPFDWMELISD 288
NrdB COG0208
Ribonucleotide reductase beta subunit, ferritin-like domain [Nucleotide transport and ...
 17-324 2.28e-118

Ribonucleotide reductase beta subunit, ferritin-like domain [Nucleotide transport and metabolism]; Ribonucleotide reductase beta subunit, ferritin-like domain is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 439978 [Multi-domain]  Cd Length: 326  Bit Score: 344.46  E-value: 2.28e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  17 SEEPLLMAQN-QRFTMFPIRYKSIWEMYKKAEASFWTAEEVDLSTDVQQWEALTDSEKHFISHILAFFAASDGIVLENLA 95
Cdd:COG0208   1 LDEPIINGLTtNRINWNPIKYPWAYELYKKQLANFWLPEEVPLSNDIKDWKKLSDDERHLIKRVLGFLTLLDSIQGNNLV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  96 ARFLNDVQVPEARAFYGFQIAMENIHSEMYSLLLETFIKDskeKDRLFNAIETIPCISKKAKWCLDWIQ------SPMSF 169
Cdd:COG0208  81 LALYPHVTAPEVRAVLSRQAFMEAIHAKSYSYILETLGLD---IDEIFNWIEENPALQKKAEFILKYYDdlgtreTKKDL 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476 170 AVRLVAFACVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLQKQLPL-------EKVYQIVH 242
Cdd:COG0208 158 LKSLVASVFLEGIFFYSGFAYPLSLARRGKMKGTAEIIRLILRDESLHGNFGIYLINTIREENPElfteelkEEIYELLK 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476 243 EAVEIETEFVCKALPCDLIGMNSNLMSQYIQFVADRLLVTLGCERTY-KAENPFDWM-EFISLQGKTNFFEKRVGEYQKA 320
Cdd:COG0208 238 EAVELEKEYADDLFPDGILGLNAEDVKQYIRYIANKRLMNLGLEPLFeGDVNPFPWMsEGLDLNKKTDFFETRVTEYQKG 317


                ....
gi 15229476 321 SVMS 324
Cdd:COG0208 318 GVES 321
PRK07209 PRK07209
ribonucleotide-diphosphate reductase subunit beta; Validated
 33-324 1.49e-53

ribonucleotide-diphosphate reductase subunit beta; Validated


Pssm-ID: 235968  Cd Length: 369  Bit Score: 180.19  E-value: 1.49e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476   33 PIRYKSIWEMYKKAEASFWTAEEVDLSTDVQQWE---ALTDSEKHFISHILAFFAASDGIVLENLAARFLNDVQVPEARA 109
Cdd:PRK07209  53 PFKYKWAWEKYLAGCANHWMPQEVNMSRDIALWKspnGLTEDERRIVKRNLGFFSTADSLVANNIVLAIYRHITNPECRQ 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  110 FYGFQIAMENIHSEMYSLLLETFIKDSKEkdrLFNAIETIPCISKKAKWCLDWIQSPM-------------SFAVRLVAF 176
Cdd:PRK07209 133 YLLRQAFEEAIHTHAYQYIVESLGLDEGE---IFNMYHEVPSIRAKDEFLIPFTRSLTdpnfktgtpendqKLLRNLIAF 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  177 ACV-EGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLQKQLPL-------EKVYQIVHEAVEIE 248
Cdd:PRK07209 210 YCImEGIFFYVGFTQILSLGRQNKMTGIAEQYQYILRDESMHLNFGIDLINQIKLENPHlwtaefqAEIRELIKEAVELE 289

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229476  249 TEFVCKALPCDLIGMNSNLMSQYIQFVADRLLVTLGCERTYK-AENPFDWM-EFISLQGKTNFFEKRVGEYQKASVMS 324
Cdd:PRK07209 290 YRYARDTMPRGVLGLNASMFKDYLRFIANRRLQQIGLKPQYPgTENPFPWMsEMIDLKKEKNFFETRVIEYQTGGALS 367
nrdF PRK09614
ribonucleotide-diphosphate reductase subunit beta; Reviewed
 33-322 2.10e-51

ribonucleotide-diphosphate reductase subunit beta; Reviewed


Pssm-ID: 236591 [Multi-domain]  Cd Length: 324  Bit Score: 173.09  E-value: 2.10e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476   33 PIRYKSIWEMYKKAEASFWTAEEVDLSTDVQQWEALTDSEKHFISHILAFFAASDGIVLENLAARFLNDVQVPEARAFYG 112
Cdd:PRK09614  16 KIEDPWDYEAWKRLTANFWLPEEVPLSNDLKDWKKLSDEEKNLYTRVFGGLTLLDTLQNNNGMPNLMPDITTPEEEAVLA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  113 FQIAMENIHSEMYSLLLETfIKDSKEKDRLFNAIETIPCISKKAKWCLDWIQS--PMSFAVRLVAFACVEGIFFSGSFCA 190
Cdd:PRK09614  96 NIAFMEAVHAKSYSYIFST-LCSPEEIDEAFEWAEENPYLQKKADIIQDFYEPlkKKILRKAAVASVFLEGFLFYSGFYY 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  191 IFWLKKRGLMPGltfSNELIS---RDEGLHCDFACLLYSLLQKQLPLEK-------VYQIVHEAVEIETEFVCKALpcDL 260
Cdd:PRK09614 175 PLYLARQGKMTG---TAQIIRliiRDESLHGYYIGYLFQEGLEELPELEqeelkdeIYDLLYELYENEEAYTELLY--DI 249

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229476  261 IGmNSNLMSQYIQFVADRLLVTLGCERTYKAENPFD--WMEFISLQG--KTNFFEKRVGEYQKASV 322
Cdd:PRK09614 250 VG-LAEDVKKYIRYNANKRLMNLGLEPLFPEEEEVNpiWLNGLSNNAdeNHDFFEGKGTSYVKGAT 314
PRK12759 PRK12759
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional
 30-325 1.38e-27

bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional


Pssm-ID: 139206 [Multi-domain]  Cd Length: 410  Bit Score: 111.66  E-value: 1.38e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476   30 TMFPIRYKSIWEMYKKAEASFWTAEEVDLSTDVQQWE--ALTDSEKHFISHILAFFAASDGIVLENLAARFLNDVQVPEA 107
Cdd:PRK12759  99 TYKPFNYPWAVDLTVKHEKAHWIEDEIDLSEDVTDWKngKITKVEKEYITNILRLFTQSDVAVGQNYYDQFIPLFKNNEI 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  108 RAFYGFQIAMENIHSEMYSLLLETF-IKDSKekdrlFNAIETIPCISKKAKWCLDwiQSPMS---FAVRLVAFACVEGIF 183
Cdd:PRK12759 179 RNMLGSFAAREGIHQRAYALLNDTLgLPDSE-----YHAFLEYKAMTDKIDFMMD--ADPTTrrgLGLCLAKTVFNEGVA 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  184 FSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLQKQLPL-------EKVYQIVHEAVEIETEFVCKAL 256
Cdd:PRK12759 252 LFASFAMLLNFQRFGKMKGMGKVVEWSIRDESMHVEGNAALFRIYCQENPYivdnefkKEIYLMASKAVELEDRFIELAY 331

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229476  257 PCDLI-GMNSNLMSQYIQFVADRLLVTLGCERTYKAE-NPFDWMEFIsLQG--KTNFFEKRVGEYQKASVMSN 325
Cdd:PRK12759 332 ELGTIeGLKADEVKQYIRHITDRRLNQLGLKEIYNIEkNPLTWLEWI-LNGadHTNFFENRVTEYEVAGLTGS 403
nrdF2 PRK13966
ribonucleotide-diphosphate reductase subunit beta; Provisional
 41-289 1.21e-14

ribonucleotide-diphosphate reductase subunit beta; Provisional


Pssm-ID: 140022  Cd Length: 324  Bit Score: 73.60  E-value: 1.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476   41 EMYKKAEASFWTAEEVDLSTDVQQWEALTDSEKHFISHILAFFAASDGIVLENLAARFLNDVQVPEARAFYGFQIAMENI 120
Cdd:PRK13966  26 EVWDRLTGNFWLPEKVPVSNDIPSWGTLTAGEKQLTMRVFTGLTMLDTIQGTVGAVSLIPDALTPHEEAVLTNIAFMESV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  121 HSEMYSLLLETFIKdSKEKDRLFNAIETIPCISKKAKWCLDWIQSPMSFAVRLVAFACVEGIFFSGSFCAIFWlKKRGLM 200
Cdd:PRK13966 106 HAKSYSQIFSTLCS-TAEIDDAFRWSEENRNLQRKAEIVLQYYRGDEPLKRKVASTLLESFLFYSGFYLPMYW-SSRAKL 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  201 PGLTFSNELISRDEGLHCDFACLLY----SLL---QKQLPLEKVYQIVHEAVEIETEFVCKALpcDLIGMNSNLmSQYIQ 273
Cdd:PRK13966 184 TNTADMIRLIIRDEAVHGYYIGYKFqrglALVddvTRAELKDYTYELLFELYDNEVEYTQDLY--DEVGLTEDV-KKFLR 260

                        250
                 ....*....|....*.
gi 15229476  274 FVADRLLVTLGCERTY 289
Cdd:PRK13966 261 YNANKALMNLGYEALF 276
nrdF1 PRK13967
ribonucleotide-diphosphate reductase subunit beta; Provisional
 41-217 3.08e-12

ribonucleotide-diphosphate reductase subunit beta; Provisional


Pssm-ID: 140023  Cd Length: 322  Bit Score: 66.68  E-value: 3.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476   41 EMYKKAEASFWTAEEVDLSTDVQQWEALTDSEKHFISHILAFFAASDGIVLENLAARFLNDVQVPEARAFYGFQIAMENI 120
Cdd:PRK13967  24 QVWERLTGNFWLPEKIPLSNDLASWQTLSSTEQQTTIRVFTGLTLLDTAQATVGAVAMIDDAVTPHEEAVLTNMAFMESV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  121 HSEMYSLLLETFIKdSKEKDRLFNAIETIPCISKKAKWCLDWIQSPMSFAVRLVAFACVEGIFFSGSFCAIFWlKKRGLM 200
Cdd:PRK13967 104 HAKSYSSIFSTLCS-TKQIDDAFDWSEQNPYLQRKAQIIVDYYRGDDALKRKASSVMLESFLFYSGFYLPMYW-SSRGKL 181

                        170
                 ....*....|....*..
gi 15229476  201 PGLTFSNELISRDEGLH 217
Cdd:PRK13967 182 TNTADLIRLIIRDEAVH 198
PRK13965 PRK13965
ribonucleotide-diphosphate reductase subunit beta; Provisional
 41-292 1.84e-11

ribonucleotide-diphosphate reductase subunit beta; Provisional


Pssm-ID: 184425 [Multi-domain]  Cd Length: 335  Bit Score: 64.41  E-value: 1.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476   41 EMYKKAEASFWTAEEVDLSTDVQQWEALTDSEKHFISHILAffaasdGIVLENLAARFLNDV-QVPEAR-----AFYGFQ 114
Cdd:PRK13965  37 EVWNRVTQNFWLPEKVPVSNDLNSWRSLGEDWQQLITRTFT------GLTLLDTVQATVGDVaQIPHSQtdheqVIYTNF 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  115 IAMENIHSEMYSLLLETfIKDSKEKDRLFNAIETIPCISKKAKWCLDWIQ--SPMSfavRLVAFACVEGIFFSGSFCAIF 192
Cdd:PRK13965 111 AFMVAIHARSYGTIFST-LCSSEQIEEAHEWVVSTESLQRRARVLIPYYTgdDPLK---SKVAAAMMPGFLLYGGFYLPF 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  193 WLKKRGLMPGLTFSNELISRDEGLHCDFACLLYsllQKQLPLEK----------VYQIVHEAVEIETEFVCKALpcDLIG 262
Cdd:PRK13965 187 YLSARGKLPNTSDIIRLILRDKVIHNYYSGYKY---QQKVARLSpekqaemkafVFDLLYELIDLEKAYLRELY--AGFD 261

                        250       260       270
                 ....*....|....*....|....*....|
gi 15229476  263 MNSNLMSqYIQFVADRLLVTLGCERTYKAE 292
Cdd:PRK13965 262 LAEDAIR-FSLYNAGKFLQNLGYESPFTEE 290
nrdB PRK09101
ribonucleotide-diphosphate reductase subunit beta; Reviewed
 50-298 5.99e-10

ribonucleotide-diphosphate reductase subunit beta; Reviewed


Pssm-ID: 181647  Cd Length: 376  Bit Score: 59.98  E-value: 5.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476   50 FWTAEEVDLSTDVQQWEALTDSEKH-FISHiLAFFAASDGIVLENLAARFLNDVQVPEARAF---YGFQiamENIHSEMY 125
Cdd:PRK09101  48 FWRPEEVDVSRDRIDYQALPEHEKHiFISN-LKYQTLLDSIQGRSPNVALLPLVSIPELETWietWSFS---ETIHSRSY 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  126 SLLLETFIKD---------------------SKEKDRLFNAIE-------------------TIPCISKKAKWCLdwiqs 165
Cdd:PRK09101 124 THIIRNIVNDpsvvfddivtneeilkrakdiSSYYDDLIEMTSyyhllgegthtvngktvtvSLRELKKKLYLCL----- 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  166 pMSFAVrlvafacVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLQ--------KQLPLE-- 235
Cdd:PRK09101 199 -MSVNA-------LEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLMRsgkddpemAEIAEEck 270

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229476  236 -KVYQIVHEAVEIETEFVcKALPCD--LIGMNSNLMSQYIQFVADRLLVTLGCERTYKAE-NPFDWM 298
Cdd:PRK09101 271 qECYDLFVQAAEQEKEWA-DYLFKDgsMIGLNKDILCQYVEYITNIRMQAVGLDLPFQTRsNPIPWI 336
PRK08326 PRK08326
R2-like ligand-binding oxidase;
32-217 1.86e-09

R2-like ligand-binding oxidase;


Pssm-ID: 236242  Cd Length: 311  Bit Score: 58.09  E-value: 1.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476   32 FPIRyksiweMYKKAEASFWTAEEVDLSTDVQQWEALTDSEKHFISHILAFFAASDGIVLENL-----AAR--------- 97
Cdd:PRK08326  26 FPMK------LFAKGNAKFWNPADIDFSRDAEDWEKLSDEERDYATRLCAQFIAGEEAVTLDIqplisAMAaegrledem 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476   98 FLNDVQVPEARafygfqiameniHSEMYSLLLET---------FIKDSKEKDRLFnaIETIPciskKAKWCLDWIQSPMS 168
Cdd:PRK08326 100 YLTQFAFEEAK------------HTEAFRRWFDAvgvtedlsvYTDDNPSYRQIF--YEELP----AALNRLSTDPSPEN 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15229476  169 FAVRLVAF-ACVEGIFFSGSFCAIFWL-KKRGLMPGLTFSNELISRDEGLH 217
Cdd:PRK08326 162 QVRASVTYnHVVEGVLAETGYYAWRKIcVTRGILPGLQELVRRIGDDERRH 212
RNRR2_Rv0233_like cd07911
Ribonucleotide Reductase R2-like protein, Mn/Fe-binding domain; Rv0233 is a Mycobacterium ...
 41-217 2.08e-05

Ribonucleotide Reductase R2-like protein, Mn/Fe-binding domain; Rv0233 is a Mycobacterium tuberculosis ribonucleotide reductase R2 protein with a heterodinuclear manganese/iron-carboxylate cofactor located in its metal center. The Rv0233-like family may represent a structural/functional counterpart of the evolutionary ancestor of the RNRR2's (Ribonucleotide Reductase, R2/beta subunit) and the bacterial multicomponent monooxygenases. RNRR2s belong to a broad superfamily of ferritin-like diiron-carboxylate proteins. The RNR protein catalyzes the conversion of ribonucleotides to deoxyribonucleotides and is found in prokaryotes and archaea. The catalytically active form of RNR is a proposed alpha2-beta2 tetramer. The homodimeric alpha subunit (R1) contains the active site and redox active cysteines as well as the allosteric binding sites.


Pssm-ID: 153120  Cd Length: 280  Bit Score: 45.41  E-value: 2.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476  41 EMYKKAEA-SFWTAEEVDLSTDVQQWEALTDSEKHFISHILAFFAASDGIVLENLA------AR--------FLNDVQVP 105
Cdd:cd07911  11 KLFEKGKRkGFWNPADIDFSQDREDWEQLSEEERDLALRLCAGFIAGEEAVTLDLLplmmamAAegrleeemYLTQFLFE 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229476 106 EARafygfqiameniHSEMYSL---------LLETFIKDSKEK---DRLFNAIETIpciskkakwCLDwiQSPMSFAVRL 173
Cdd:cd07911  91 EAK------------HTDFFRRwldavgvsdDLSDLHTAVYREpfyEALPYAELRL---------YLD--ASPAAQVRAS 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15229476 174 VAF-ACVEGIFFSGSFCAIF-WLKKRGLMPGLTFSNELISRDEGLH 217
Cdd:cd07911 148 VTYnMIVEGVLAETGYYAWRtICEKRGILPGMQEGIRRLGDDESRH 193
 
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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