|
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
|
|
|