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Conserved domains on  [gi|124808087|ref|XP_001348226|]
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ribonucleoside-diphosphate reductase small chain, putative [Plasmodium falciparum 3D7]

Protein Classification

ribonucleoside-diphosphate reductase small subunit( domain architecture ID 10794343)

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
PTZ00211 PTZ00211
ribonucleoside-diphosphate reductase small subunit; Provisional
20-349 0e+00

ribonucleoside-diphosphate reductase small subunit; Provisional


:

Pssm-ID: 240315 [Multi-domain]  Cd Length: 330  Bit Score: 631.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087  20 FSDLQKGKEINEKILNKESDRFTLYPILYPDVWDFYKKAEASFWTAEEIDLSSDLKDFEKLNENEKHFIKHVLAFFAASD 99
Cdd:PTZ00211   1 HKEAMKENEEEEPLLKENPDRFVLFPIKYPDIWRMYKKAEASFWTAEEIDLGNDLKDWEKLNDGERHFIKHVLAFFAASD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 100 GIVLENLASKFLREVQITEAKKFYSFQIAVENIHSETYSLLIDNYIKDEKERLNLFHAIENIPAVKNKALWAAKWINDTN 179
Cdd:PTZ00211  81 GIVLENLAQRFMREVQVPEARCFYGFQIAMENIHSETYSLLIDTYITDEEEKDRLFHAIETIPAIKKKAEWAAKWINSSN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 180 SFAERIVANACVEGILFSGSFCAIFWFKKQNKLHGLTFSNELISRDEGLHTDFNCLIYSLLDNKLPEQMVQNIVKEAVEV 259
Cdd:PTZ00211 161 SFAERLVAFAAVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHTDFACLLYSHLKNKLPRERVQEIIKEAVEI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 260 ERSFICESLPCDLIGMNSRLMSQYIEFVADRLLECLGCSKIFHSKNPFNWMDLISLQGKTNFFEKRVADYQKSGVMAQRK 339
Cdd:PTZ00211 241 EREFICDALPVDLIGMNSRLMAQYIEFVADRLLVALGVPKIYNSKNPFDWMDMISLQGKTNFFEKRVGEYQKAGVMAERT 320
                        330
                 ....*....|
gi 124808087 340 DQVFCLNTEF 349
Cdd:PTZ00211 321 SKVFSLDADF 330
 
Name Accession Description Interval E-value
PTZ00211 PTZ00211
ribonucleoside-diphosphate reductase small subunit; Provisional
20-349 0e+00

ribonucleoside-diphosphate reductase small subunit; Provisional


Pssm-ID: 240315 [Multi-domain]  Cd Length: 330  Bit Score: 631.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087  20 FSDLQKGKEINEKILNKESDRFTLYPILYPDVWDFYKKAEASFWTAEEIDLSSDLKDFEKLNENEKHFIKHVLAFFAASD 99
Cdd:PTZ00211   1 HKEAMKENEEEEPLLKENPDRFVLFPIKYPDIWRMYKKAEASFWTAEEIDLGNDLKDWEKLNDGERHFIKHVLAFFAASD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 100 GIVLENLASKFLREVQITEAKKFYSFQIAVENIHSETYSLLIDNYIKDEKERLNLFHAIENIPAVKNKALWAAKWINDTN 179
Cdd:PTZ00211  81 GIVLENLAQRFMREVQVPEARCFYGFQIAMENIHSETYSLLIDTYITDEEEKDRLFHAIETIPAIKKKAEWAAKWINSSN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 180 SFAERIVANACVEGILFSGSFCAIFWFKKQNKLHGLTFSNELISRDEGLHTDFNCLIYSLLDNKLPEQMVQNIVKEAVEV 259
Cdd:PTZ00211 161 SFAERLVAFAAVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHTDFACLLYSHLKNKLPRERVQEIIKEAVEI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 260 ERSFICESLPCDLIGMNSRLMSQYIEFVADRLLECLGCSKIFHSKNPFNWMDLISLQGKTNFFEKRVADYQKSGVMAQRK 339
Cdd:PTZ00211 241 EREFICDALPVDLIGMNSRLMAQYIEFVADRLLVALGVPKIYNSKNPFDWMDMISLQGKTNFFEKRVGEYQKAGVMAERT 320
                        330
                 ....*....|
gi 124808087 340 DQVFCLNTEF 349
Cdd:PTZ00211 321 SKVFSLDADF 330
Ribonuc_red_sm pfam00268
Ribonucleotide reductase, small chain;
40-306 8.62e-134

Ribonucleotide reductase, small chain;


Pssm-ID: 425568 [Multi-domain]  Cd Length: 276  Bit Score: 382.23  E-value: 8.62e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087   40 RFTLYPILYPDVWDFYKKAEASFWTAEEIDLSSDLKDFEKLNENEKHFIKHVLAFFAASDGIVLENLASKFLREVQITEA 119
Cdd:pfam00268   1 RFNLNPIKYPEIWEFYKKLEANFWTPEEIPLSKDIKDWKKLSEDEREFIKRVLAFLALLDTLVNENLVERFSREVQTPEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087  120 KKFYSFQIAVENIHSETYSLLIDNYIKDEKERLNLFHAIENIPAVKNKALWAAKWINDTNS-FAERIVANACVEGILFSG 198
Cdd:pfam00268  81 RAFYGFQAFMENIHSESYSYILDTLGKDPEEIDELFNWIETNPALQKKAEWILKWYQDFDSdFLERLVAFAILEGIFFYS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087  199 SFCAIFWFKKQNKLHGLTFSNELISRDEGLHTDFNCLIYSLLDNKLPE-------QMVQNIVKEAVEVERSFICESLPCD 271
Cdd:pfam00268 161 GFAAILWLKRRGKMPGLAEIIELISRDEGLHGDFACLLFQHLKEENPEletkelkEEVYDLIKEAVELEKEFLDDALPVG 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 124808087  272 LIGMNSRLMSQYIEFVADRLLECLGCSKIFHS-KNP 306
Cdd:pfam00268 241 LLGMNAEDVKQYIEYVADRRLMNLGYEKLYNVeVNP 276
RNRR2 cd01049
Ribonucleotide Reductase, R2/beta subunit, ferritin-like diiron-binding domain; Ribonucleotide ...
41-315 4.80e-122

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: 353.08  E-value: 4.80e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087  41 FTLYPILYPDVWDFYKKAEASFWTAEEIDLSSDLKDFEKLNENEKHFIKHVLAFFAASDGIVLENLASKFLREVQITEAK 120
Cdd:cd01049    1 FNLNPIKYPWAWELYKKAEANFWTPEEIDLSKDLKDWEKLTEAERHFIKRVLAFLAALDSIVGENLVELFSRHVQIPEAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 121 KFYSFQIAVENIHSETYSLLIDNYIKDEkERLNLFHAIENIPAVKNKALWAAKWINDTN-----SFAERIVANACVEGIL 195
Cdd:cd01049   81 AFYGFQAFMENIHSESYSYILDTLGKDE-ERDELFEAIETDPALKKKADWILRWYDNLDdntkeSFAERLVAFAILEGIF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 196 FSGSFCAIFWFKKQNKLHGLTFSNELISRDEGLHTDFNCLIYSLLDNKLPEQM-------VQNIVKEAVEVERSFICESL 268
Cdd:cd01049  160 FYSGFAAIFWLARRGKMPGLAEIIELISRDESLHGDFACLLIRELLNENPELFteefkeeVYELIKEAVELEKEFARDLL 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 124808087 269 PCDLIGMNSRLMSQYIEFVADRLLECLGCSKIFHS--KNPFNWMDLISL 315
Cdd:cd01049  240 PDGILGLNKEDMKQYIEYVANRRLENLGLEKLFNVedKNPFDWMELISD 288
NrdB COG0208
Ribonucleotide reductase beta subunit, ferritin-like domain [Nucleotide transport and ...
30-336 3.28e-109

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: 321.73  E-value: 3.28e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087  30 NEKILN-KESDRFTLYPILYPDVWDFYKKAEASFWTAEEIDLSSDLKDFEKLNENEKHFIKHVLAFFAASDGIVLENLAS 108
Cdd:COG0208    2 DEPIINgLTTNRINWNPIKYPWAYELYKKQLANFWLPEEVPLSNDIKDWKKLSDDERHLIKRVLGFLTLLDSIQGNNLVL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 109 KFLREVQITEAKKFYSFQIAVENIHSETYSLLIDNYIKDEKErlnLFHAIENIPAVKNKALWAAKWINDTNS------FA 182
Cdd:COG0208   82 ALYPHVTAPEVRAVLSRQAFMEAIHAKSYSYILETLGLDIDE---IFNWIEENPALQKKAEFILKYYDDLGTretkkdLL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 183 ERIVANACVEGILFSGSFCAIFWFKKQNKLHGLTFSNELISRDEGLHTDFNCLIYSLLDNKLPE-------QMVQNIVKE 255
Cdd:COG0208  159 KSLVASVFLEGIFFYSGFAYPLSLARRGKMKGTAEIIRLILRDESLHGNFGIYLINTIREENPElfteelkEEIYELLKE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 256 AVEVERSFICESLPCDLIGMNSRLMSQYIEFVADRLLECLGCSKIF-HSKNPFNWMD-LISLQGKTNFFEKRVADYQKSG 333
Cdd:COG0208  239 AVELEKEYADDLFPDGILGLNAEDVKQYIRYIANKRLMNLGLEPLFeGDVNPFPWMSeGLDLNKKTDFFETRVTEYQKGG 318

                 ...
gi 124808087 334 VMA 336
Cdd:COG0208  319 VES 321
 
Name Accession Description Interval E-value
PTZ00211 PTZ00211
ribonucleoside-diphosphate reductase small subunit; Provisional
20-349 0e+00

ribonucleoside-diphosphate reductase small subunit; Provisional


Pssm-ID: 240315 [Multi-domain]  Cd Length: 330  Bit Score: 631.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087  20 FSDLQKGKEINEKILNKESDRFTLYPILYPDVWDFYKKAEASFWTAEEIDLSSDLKDFEKLNENEKHFIKHVLAFFAASD 99
Cdd:PTZ00211   1 HKEAMKENEEEEPLLKENPDRFVLFPIKYPDIWRMYKKAEASFWTAEEIDLGNDLKDWEKLNDGERHFIKHVLAFFAASD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 100 GIVLENLASKFLREVQITEAKKFYSFQIAVENIHSETYSLLIDNYIKDEKERLNLFHAIENIPAVKNKALWAAKWINDTN 179
Cdd:PTZ00211  81 GIVLENLAQRFMREVQVPEARCFYGFQIAMENIHSETYSLLIDTYITDEEEKDRLFHAIETIPAIKKKAEWAAKWINSSN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 180 SFAERIVANACVEGILFSGSFCAIFWFKKQNKLHGLTFSNELISRDEGLHTDFNCLIYSLLDNKLPEQMVQNIVKEAVEV 259
Cdd:PTZ00211 161 SFAERLVAFAAVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHTDFACLLYSHLKNKLPRERVQEIIKEAVEI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 260 ERSFICESLPCDLIGMNSRLMSQYIEFVADRLLECLGCSKIFHSKNPFNWMDLISLQGKTNFFEKRVADYQKSGVMAQRK 339
Cdd:PTZ00211 241 EREFICDALPVDLIGMNSRLMAQYIEFVADRLLVALGVPKIYNSKNPFDWMDMISLQGKTNFFEKRVGEYQKAGVMAERT 320
                        330
                 ....*....|
gi 124808087 340 DQVFCLNTEF 349
Cdd:PTZ00211 321 SKVFSLDADF 330
PLN02492 PLN02492
ribonucleoside-diphosphate reductase
31-349 0e+00

ribonucleoside-diphosphate reductase


Pssm-ID: 215272  Cd Length: 324  Bit Score: 570.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087  31 EKILNKESDRFTLYPILYPDVWDFYKKAEASFWTAEEIDLSSDLKDFEKLNENEKHFIKHVLAFFAASDGIVLENLASKF 110
Cdd:PLN02492   1 EPLLAENPDRFCMFPIKYPQIWEMYKKAEASFWTAEEVDLSADLKDWEKLTDDERHFISHVLAFFAASDGIVLENLAARF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 111 LREVQITEAKKFYSFQIAVENIHSETYSLLIDNYIKDEKERLNLFHAIENIPAVKNKALWAAKWINDTNSFAERIVANAC 190
Cdd:PLN02492  81 MKEVQVPEARAFYGFQIAIENIHSEMYSLLLDTYIKDPKEKDRLFNAIETIPCVAKKADWALRWIDSSASFAERLVAFAC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 191 VEGILFSGSFCAIFWFKKQNKLHGLTFSNELISRDEGLHTDFNCLIYSLLDNKLPEQMVQNIVKEAVEVERSFICESLPC 270
Cdd:PLN02492 161 VEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLKNKLSEERVKEIVCEAVEIEKEFVCDALPC 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 271 DLIGMNSRLMSQYIEFVADRLLECLGCSKIFHSKNPFNWMDLISLQGKTNFFEKRVADYQKSGVMA-----QRKDQVFCL 345
Cdd:PLN02492 241 ALVGMNADLMSQYIEFVADRLLVALGYEKVYNVVNPFDWMELISLQGKTNFFEKRVGEYQKAGVMSslnggGADNHVFSL 320

                 ....
gi 124808087 346 NTEF 349
Cdd:PLN02492 321 DEDF 324
Ribonuc_red_sm pfam00268
Ribonucleotide reductase, small chain;
40-306 8.62e-134

Ribonucleotide reductase, small chain;


Pssm-ID: 425568 [Multi-domain]  Cd Length: 276  Bit Score: 382.23  E-value: 8.62e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087   40 RFTLYPILYPDVWDFYKKAEASFWTAEEIDLSSDLKDFEKLNENEKHFIKHVLAFFAASDGIVLENLASKFLREVQITEA 119
Cdd:pfam00268   1 RFNLNPIKYPEIWEFYKKLEANFWTPEEIPLSKDIKDWKKLSEDEREFIKRVLAFLALLDTLVNENLVERFSREVQTPEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087  120 KKFYSFQIAVENIHSETYSLLIDNYIKDEKERLNLFHAIENIPAVKNKALWAAKWINDTNS-FAERIVANACVEGILFSG 198
Cdd:pfam00268  81 RAFYGFQAFMENIHSESYSYILDTLGKDPEEIDELFNWIETNPALQKKAEWILKWYQDFDSdFLERLVAFAILEGIFFYS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087  199 SFCAIFWFKKQNKLHGLTFSNELISRDEGLHTDFNCLIYSLLDNKLPE-------QMVQNIVKEAVEVERSFICESLPCD 271
Cdd:pfam00268 161 GFAAILWLKRRGKMPGLAEIIELISRDEGLHGDFACLLFQHLKEENPEletkelkEEVYDLIKEAVELEKEFLDDALPVG 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 124808087  272 LIGMNSRLMSQYIEFVADRLLECLGCSKIFHS-KNP 306
Cdd:pfam00268 241 LLGMNAEDVKQYIEYVADRRLMNLGYEKLYNVeVNP 276
RNRR2 cd01049
Ribonucleotide Reductase, R2/beta subunit, ferritin-like diiron-binding domain; Ribonucleotide ...
41-315 4.80e-122

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: 353.08  E-value: 4.80e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087  41 FTLYPILYPDVWDFYKKAEASFWTAEEIDLSSDLKDFEKLNENEKHFIKHVLAFFAASDGIVLENLASKFLREVQITEAK 120
Cdd:cd01049    1 FNLNPIKYPWAWELYKKAEANFWTPEEIDLSKDLKDWEKLTEAERHFIKRVLAFLAALDSIVGENLVELFSRHVQIPEAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 121 KFYSFQIAVENIHSETYSLLIDNYIKDEkERLNLFHAIENIPAVKNKALWAAKWINDTN-----SFAERIVANACVEGIL 195
Cdd:cd01049   81 AFYGFQAFMENIHSESYSYILDTLGKDE-ERDELFEAIETDPALKKKADWILRWYDNLDdntkeSFAERLVAFAILEGIF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 196 FSGSFCAIFWFKKQNKLHGLTFSNELISRDEGLHTDFNCLIYSLLDNKLPEQM-------VQNIVKEAVEVERSFICESL 268
Cdd:cd01049  160 FYSGFAAIFWLARRGKMPGLAEIIELISRDESLHGDFACLLIRELLNENPELFteefkeeVYELIKEAVELEKEFARDLL 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 124808087 269 PCDLIGMNSRLMSQYIEFVADRLLECLGCSKIFHS--KNPFNWMDLISL 315
Cdd:cd01049  240 PDGILGLNKEDMKQYIEYVANRRLENLGLEKLFNVedKNPFDWMELISD 288
NrdB COG0208
Ribonucleotide reductase beta subunit, ferritin-like domain [Nucleotide transport and ...
30-336 3.28e-109

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: 321.73  E-value: 3.28e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087  30 NEKILN-KESDRFTLYPILYPDVWDFYKKAEASFWTAEEIDLSSDLKDFEKLNENEKHFIKHVLAFFAASDGIVLENLAS 108
Cdd:COG0208    2 DEPIINgLTTNRINWNPIKYPWAYELYKKQLANFWLPEEVPLSNDIKDWKKLSDDERHLIKRVLGFLTLLDSIQGNNLVL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 109 KFLREVQITEAKKFYSFQIAVENIHSETYSLLIDNYIKDEKErlnLFHAIENIPAVKNKALWAAKWINDTNS------FA 182
Cdd:COG0208   82 ALYPHVTAPEVRAVLSRQAFMEAIHAKSYSYILETLGLDIDE---IFNWIEENPALQKKAEFILKYYDDLGTretkkdLL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 183 ERIVANACVEGILFSGSFCAIFWFKKQNKLHGLTFSNELISRDEGLHTDFNCLIYSLLDNKLPE-------QMVQNIVKE 255
Cdd:COG0208  159 KSLVASVFLEGIFFYSGFAYPLSLARRGKMKGTAEIIRLILRDESLHGNFGIYLINTIREENPElfteelkEEIYELLKE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 256 AVEVERSFICESLPCDLIGMNSRLMSQYIEFVADRLLECLGCSKIF-HSKNPFNWMD-LISLQGKTNFFEKRVADYQKSG 333
Cdd:COG0208  239 AVELEKEYADDLFPDGILGLNAEDVKQYIRYIANKRLMNLGLEPLFeGDVNPFPWMSeGLDLNKKTDFFETRVTEYQKGG 318

                 ...
gi 124808087 334 VMA 336
Cdd:COG0208  319 VES 321
PRK07209 PRK07209
ribonucleotide-diphosphate reductase subunit beta; Validated
32-335 1.51e-44

ribonucleotide-diphosphate reductase subunit beta; Validated


Pssm-ID: 235968  Cd Length: 369  Bit Score: 156.69  E-value: 1.51e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087  32 KILNKESDRFTLYPILYPDVWDFYKKAEASFWTAEEIDLSSDL---KDFEKLNENEKHFIKHVLAFFAASDGIVLENLAS 108
Cdd:PRK07209  40 RIINCRADVNQLVPFKYKWAWEKYLAGCANHWMPQEVNMSRDIalwKSPNGLTEDERRIVKRNLGFFSTADSLVANNIVL 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 109 KFLREVQITEAKKFYSFQIAVENIHSETYSLLIDNYIKDEKERLNLFHaieNIPAVKNKALWAAKWIND-------TNS- 180
Cdd:PRK07209 120 AIYRHITNPECRQYLLRQAFEEAIHTHAYQYIVESLGLDEGEIFNMYH---EVPSIRAKDEFLIPFTRSltdpnfkTGTp 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 181 -----FAERIVANACV-EGILFSGSFCAIFWFKKQNKLHGLTFSNELISRDEGLHTDFNC-LIYSL-LDNklPE------ 246
Cdd:PRK07209 197 endqkLLRNLIAFYCImEGIFFYVGFTQILSLGRQNKMTGIAEQYQYILRDESMHLNFGIdLINQIkLEN--PHlwtaef 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 247 -QMVQNIVKEAVEVERSFICESLPCDLIGMNSRLMSQYIEFVADRLLECLGCSKIF-HSKNPFNWM-DLISLQGKTNFFE 323
Cdd:PRK07209 275 qAEIRELIKEAVELEYRYARDTMPRGVLGLNASMFKDYLRFIANRRLQQIGLKPQYpGTENPFPWMsEMIDLKKEKNFFE 354
                        330
                 ....*....|..
gi 124808087 324 KRVADYQKSGVM 335
Cdd:PRK07209 355 TRVIEYQTGGAL 366
nrdF PRK09614
ribonucleotide-diphosphate reductase subunit beta; Reviewed
45-332 6.42e-42

ribonucleotide-diphosphate reductase subunit beta; Reviewed


Pssm-ID: 236591 [Multi-domain]  Cd Length: 324  Bit Score: 148.43  E-value: 6.42e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087  45 PILYPDVWDFYKKAEASFWTAEEIDLSSDLKDFEKLNENEKHFIKHVLAFFAASDGIVLENLASKFLREVQITEAKKFYS 124
Cdd:PRK09614  16 KIEDPWDYEAWKRLTANFWLPEEVPLSNDLKDWKKLSDEEKNLYTRVFGGLTLLDTLQNNNGMPNLMPDITTPEEEAVLA 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 125 FQIAVENIHSETYSLLIDNyIKDEKERLNLFHAIENIPAVKNKALWAAKWINDT--NSFAERIVANACVEGILFSGSFCA 202
Cdd:PRK09614  96 NIAFMEAVHAKSYSYIFST-LCSPEEIDEAFEWAEENPYLQKKADIIQDFYEPLkkKILRKAAVASVFLEGFLFYSGFYY 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 203 IFWFKKQNKLHGltfSNELIS---RDEGLHTDFNCLIYSLLDNKLPEQM-------VQNIVKEAVEVERSFICESLpcDL 272
Cdd:PRK09614 175 PLYLARQGKMTG---TAQIIRliiRDESLHGYYIGYLFQEGLEELPELEqeelkdeIYDLLYELYENEEAYTELLY--DI 249
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124808087 273 IGmNSRLMSQYIEFVADRLLECLGCSKIFHSKNPFN--WMDLISLQG--KTNFFEKRVADYQKS 332
Cdd:PRK09614 250 VG-LAEDVKKYIRYNANKRLMNLGLEPLFPEEEEVNpiWLNGLSNNAdeNHDFFEGKGTSYVKG 312
PRK12759 PRK12759
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional
42-334 9.12e-26

bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional


Pssm-ID: 139206 [Multi-domain]  Cd Length: 410  Bit Score: 106.65  E-value: 9.12e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087  42 TLYPILYPDVWDFYKKAEASFWTAEEIDLSSDLKDFE--KLNENEKHFIKHVLAFFAASDGIVLENLASKFLREVQITEA 119
Cdd:PRK12759  99 TYKPFNYPWAVDLTVKHEKAHWIEDEIDLSEDVTDWKngKITKVEKEYITNILRLFTQSDVAVGQNYYDQFIPLFKNNEI 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 120 KKFYSFQIAVENIHSETYSLLIDNYIKDEKErlnlFHAIENIPAVKNKalwaAKWINDTNSFAER-----IVANACVEGI 194
Cdd:PRK12759 179 RNMLGSFAAREGIHQRAYALLNDTLGLPDSE----YHAFLEYKAMTDK----IDFMMDADPTTRRglglcLAKTVFNEGV 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 195 LFSGSFCAIFWFKKQNKLHGLTFSNELISRDEGLHTDFNCLIYS--------LLDNKLPEQMVQnIVKEAVEVERSFICE 266
Cdd:PRK12759 251 ALFASFAMLLNFQRFGKMKGMGKVVEWSIRDESMHVEGNAALFRiycqenpyIVDNEFKKEIYL-MASKAVELEDRFIEL 329
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124808087 267 SLPCDLI-GMNSRLMSQYIEFVADRLLECLGCSKIFH-SKNPFNWMDLIsLQG--KTNFFEKRVADYQKSGV 334
Cdd:PRK12759 330 AYELGTIeGLKADEVKQYIRHITDRRLNQLGLKEIYNiEKNPLTWLEWI-LNGadHTNFFENRVTEYEVAGL 400
nrdB PRK09101
ribonucleotide-diphosphate reductase subunit beta; Reviewed
62-310 1.09e-10

ribonucleotide-diphosphate reductase subunit beta; Reviewed


Pssm-ID: 181647  Cd Length: 376  Bit Score: 62.29  E-value: 1.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087  62 FWTAEEIDLSSDLKDFEKLNENEKH-FIKHvLAFFAASDGIVLENLASKFLREVQITEAKKF---YSFQiavENIHSETY 137
Cdd:PRK09101  48 FWRPEEVDVSRDRIDYQALPEHEKHiFISN-LKYQTLLDSIQGRSPNVALLPLVSIPELETWietWSFS---ETIHSRSY 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 138 SLLIDNYIKDEKErlnLFHAIENIPAVKNKALWAAKW----INDTNSF-----------AERIVANA---------CV-- 191
Cdd:PRK09101 124 THIIRNIVNDPSV---VFDDIVTNEEILKRAKDISSYyddlIEMTSYYhllgegthtvnGKTVTVSLrelkkklylCLms 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 192 ----EGILFSGSFCAIFWFKKQNKLHGLTFSNELISRDEGLHTDFNCLIYSLLDN-----------KLPEQMVQNIVKEA 256
Cdd:PRK09101 201 vnalEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLMRSgkddpemaeiaEECKQECYDLFVQA 280
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 124808087 257 VEVERSFiCESLPCD--LIGMNSRLMSQYIEFVADRLLECLGCSKIFHSK-NPFNWM 310
Cdd:PRK09101 281 AEQEKEW-ADYLFKDgsMIGLNKDILCQYVEYITNIRMQAVGLDLPFQTRsNPIPWI 336
PRK08326 PRK08326
R2-like ligand-binding oxidase;
55-229 1.31e-08

R2-like ligand-binding oxidase;


Pssm-ID: 236242  Cd Length: 311  Bit Score: 55.39  E-value: 1.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087  55 YKKAEASFWTAEEIDLSSDLKDFEKLNENEKHFIKHVLAFFAASDGIVLENLA------------------SKFLREvqi 116
Cdd:PRK08326  31 FAKGNAKFWNPADIDFSRDAEDWEKLSDEERDYATRLCAQFIAGEEAVTLDIQplisamaaegrledemylTQFAFE--- 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 117 tEAKK---FYSFQIAVeNIHSETYSLLIDNyikdekerlNLFHAI--ENIPAvknkALWAakwINDTNSFAERIVA---- 187
Cdd:PRK08326 108 -EAKHteaFRRWFDAV-GVTEDLSVYTDDN---------PSYRQIfyEELPA----ALNR---LSTDPSPENQVRAsvty 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 124808087 188 NACVEGIL-FSGSFcaiFWFK---KQNKLHGLTFSNELISRDEGLH 229
Cdd:PRK08326 170 NHVVEGVLaETGYY---AWRKicvTRGILPGLQELVRRIGDDERRH 212
nrdF2 PRK13966
ribonucleotide-diphosphate reductase subunit beta; Provisional
53-229 3.20e-05

ribonucleotide-diphosphate reductase subunit beta; Provisional


Pssm-ID: 140022  Cd Length: 324  Bit Score: 45.10  E-value: 3.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087  53 DFYKKAEASFWTAEEIDLSSDLKDFEKLNENEKHFIKHVLAFFAASDGIVLENLASKFLREVQITEAKKFYSFQIAVENI 132
Cdd:PRK13966  26 EVWDRLTGNFWLPEKVPVSNDIPSWGTLTAGEKQLTMRVFTGLTMLDTIQGTVGAVSLIPDALTPHEEAVLTNIAFMESV 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808087 133 HSETYSLLIDNyIKDEKERLNLFHAIENIPAVKNKALWAAKWINDTNSFaERIVANACVEGILFSGSFCAIFWFKKQNKL 212
Cdd:PRK13966 106 HAKSYSQIFST-LCSTAEIDDAFRWSEENRNLQRKAEIVLQYYRGDEPL-KRKVASTLLESFLFYSGFYLPMYWSSRAKL 183
                        170
                 ....*....|....*..
gi 124808087 213 HGLTFSNELISRDEGLH 229
Cdd:PRK13966 184 TNTADMIRLIIRDEAVH 200
RNRR2_Rv0233_like cd07911
Ribonucleotide Reductase R2-like protein, Mn/Fe-binding domain; Rv0233 is a Mycobacterium ...
55-107 1.65e-04

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: 42.71  E-value: 1.65e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 124808087  55 YKKAEA-SFWTAEEIDLSSDLKDFEKLNENEKHFIKHVLAFFAASDGIVLENLA 107
Cdd:cd07911   13 FEKGKRkGFWNPADIDFSQDREDWEQLSEEERDLALRLCAGFIAGEEAVTLDLL 66
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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