|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02492 |
PLN02492 |
ribonucleoside-diphosphate reductase |
1-335 |
0e+00 |
|
ribonucleoside-diphosphate reductase
Pssm-ID: 215272 Cd Length: 324 Bit Score: 627.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 1 EPICRtdEEGSRFSLFPIAYPDLWSMYKQHVASFWTADEIDLSADLSDWHKkLNPDERHFISMVLAFFAGADGIVVENLA 80
Cdd:PLN02492 1 EPLLA--ENPDRFCMFPIKYPQIWEMYKKAEASFWTAEEVDLSADLKDWEK-LTDDERHFISHVLAFFAASDGIVLENLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 81 ERFCREVTVPEARCFYGFQMAMESIHQETYCLLIDTYITDPKVRERLFSAHATVPSVERKASWAQRYIGSKASFAERLVA 160
Cdd:PLN02492 78 ARFMKEVQVPEARAFYGFQIAIENIHSEMYSLLLDTYIKDPKEKDRLFNAIETIPCVAKKADWALRWIDSSASFAERLVA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 161 FAAVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCSFACQLYSKLKLKLSQEEIQTIINEAVDVEKSFICDA 240
Cdd:PLN02492 158 FACVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLKNKLSEERVKEIVCEAVEIEKEFVCDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 241 LPVSLIGMNSRLMAQYIEFVADRMLTDLGYQAMYGSKNPFDWMDMISLEGKTNFFEKRVGEYQKSGVMASLEGKSAEsss 320
Cdd:PLN02492 238 LPCALVGMNADLMSQYIEFVADRLLVALGYEKVYNVVNPFDWMELISLQGKTNFFEKRVGEYQKAGVMSSLNGGGAD--- 314
|
330
....*....|....*
gi 224000239 321 sggvaAKELDFAADF 335
Cdd:PLN02492 315 -----NHVFSLDEDF 324
|
|
| Ribonuc_red_sm |
pfam00268 |
Ribonucleotide reductase, small chain; |
12-279 |
9.20e-139 |
|
Ribonucleotide reductase, small chain;
Pssm-ID: 425568 [Multi-domain] Cd Length: 276 Bit Score: 394.17 E-value: 9.20e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 12 RFSLFPIAYPDLWSMYKQHVASFWTADEIDLSADLSDWhKKLNPDERHFISMVLAFFAGADGIVVENLAERFCREVTVPE 91
Cdd:pfam00268 1 RFNLNPIKYPEIWEFYKKLEANFWTPEEIPLSKDIKDW-KKLSEDEREFIKRVLAFLALLDTLVNENLVERFSREVQTPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 92 ARCFYGFQMAMESIHQETYCLLIDTYITDPKVRERLFSAHATVPSVERKASWAQRYI-GSKASFAERLVAFAAVEGIFFS 170
Cdd:pfam00268 80 ARAFYGFQAFMENIHSESYSYILDTLGKDPEEIDELFNWIETNPALQKKAEWILKWYqDFDSDFLERLVAFAILEGIFFY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 171 GSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCSFACQLYSKLKLKL-------SQEEIQTIINEAVDVEKSFICDALPV 243
Cdd:pfam00268 160 SGFAAILWLKRRGKMPGLAEIIELISRDEGLHGDFACLLFQHLKEENpeletkeLKEEVYDLIKEAVELEKEFLDDALPV 239
|
250 260 270
....*....|....*....|....*....|....*..
gi 224000239 244 SLIGMNSRLMAQYIEFVADRMLTDLGYQAMYGS-KNP 279
Cdd:pfam00268 240 GLLGMNAEDVKQYIEYVADRRLMNLGYEKLYNVeVNP 276
|
|
| RNRR2 |
cd01049 |
Ribonucleotide Reductase, R2/beta subunit, ferritin-like diiron-binding domain; Ribonucleotide ... |
13-288 |
7.76e-130 |
|
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: 371.96 E-value: 7.76e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 13 FSLFPIAYPDLWSMYKQHVASFWTADEIDLSADLSDWhKKLNPDERHFISMVLAFFAGADGIVVENLAERFCREVTVPEA 92
Cdd:cd01049 1 FNLNPIKYPWAWELYKKAEANFWTPEEIDLSKDLKDW-EKLTEAERHFIKRVLAFLAALDSIVGENLVELFSRHVQIPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 93 RCFYGFQMAMESIHQETYCLLIDTYITDPKvRERLFSAHATVPSVERKASWAQRYI-----GSKASFAERLVAFAAVEGI 167
Cdd:cd01049 80 RAFYGFQAFMENIHSESYSYILDTLGKDEE-RDELFEAIETDPALKKKADWILRWYdnlddNTKESFAERLVAFAILEGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 168 FFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCSFACQLYSKLKLK-------LSQEEIQTIINEAVDVEKSFICDA 240
Cdd:cd01049 159 FFYSGFAAIFWLARRGKMPGLAEIIELISRDESLHGDFACLLIRELLNEnpelfteEFKEEVYELIKEAVELEKEFARDL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 224000239 241 LPVSLIGMNSRLMAQYIEFVADRMLTDLGYQAMYGS--KNPFDWMDMISL 288
Cdd:cd01049 239 LPDGILGLNKEDMKQYIEYVANRRLENLGLEKLFNVedKNPFDWMELISD 288
|
|
| NrdB |
COG0208 |
Ribonucleotide reductase beta subunit, ferritin-like domain [Nucleotide transport and ... |
12-310 |
2.10e-114 |
|
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: 334.44 E-value: 2.10e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 12 RFSLFPIAYPDLWSMYKQHVASFWTADEIDLSADLSDWhKKLNPDERHFISMVLAFFAGADGIVVENLAERFCREVTVPE 91
Cdd:COG0208 13 RINWNPIKYPWAYELYKKQLANFWLPEEVPLSNDIKDW-KKLSDDERHLIKRVLGFLTLLDSIQGNNLVLALYPHVTAPE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 92 ARCFYGFQMAMESIHQETYCLLIDTYITDPkvrERLFSAHATVPSVERKASWAQRYI------GSKASFAERLVAFAAVE 165
Cdd:COG0208 92 VRAVLSRQAFMEAIHAKSYSYILETLGLDI---DEIFNWIEENPALQKKAEFILKYYddlgtrETKKDLLKSLVASVFLE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 166 GIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCSFACQLYSKLKLKLS-------QEEIQTIINEAVDVEKSFIC 238
Cdd:COG0208 169 GIFFYSGFAYPLSLARRGKMKGTAEIIRLILRDESLHGNFGIYLINTIREENPelfteelKEEIYELLKEAVELEKEYAD 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224000239 239 DALPVSLIGMNSRLMAQYIEFVADRMLTDLGYQAMY-GSKNPFDWMD-MISLEGKTNFFEKRVGEYQKSGVMAS 310
Cdd:COG0208 249 DLFPDGILGLNAEDVKQYIRYIANKRLMNLGLEPLFeGDVNPFPWMSeGLDLNKKTDFFETRVTEYQKGGVEST 322
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02492 |
PLN02492 |
ribonucleoside-diphosphate reductase |
1-335 |
0e+00 |
|
ribonucleoside-diphosphate reductase
Pssm-ID: 215272 Cd Length: 324 Bit Score: 627.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 1 EPICRtdEEGSRFSLFPIAYPDLWSMYKQHVASFWTADEIDLSADLSDWHKkLNPDERHFISMVLAFFAGADGIVVENLA 80
Cdd:PLN02492 1 EPLLA--ENPDRFCMFPIKYPQIWEMYKKAEASFWTAEEVDLSADLKDWEK-LTDDERHFISHVLAFFAASDGIVLENLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 81 ERFCREVTVPEARCFYGFQMAMESIHQETYCLLIDTYITDPKVRERLFSAHATVPSVERKASWAQRYIGSKASFAERLVA 160
Cdd:PLN02492 78 ARFMKEVQVPEARAFYGFQIAIENIHSEMYSLLLDTYIKDPKEKDRLFNAIETIPCVAKKADWALRWIDSSASFAERLVA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 161 FAAVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCSFACQLYSKLKLKLSQEEIQTIINEAVDVEKSFICDA 240
Cdd:PLN02492 158 FACVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLKNKLSEERVKEIVCEAVEIEKEFVCDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 241 LPVSLIGMNSRLMAQYIEFVADRMLTDLGYQAMYGSKNPFDWMDMISLEGKTNFFEKRVGEYQKSGVMASLEGKSAEsss 320
Cdd:PLN02492 238 LPCALVGMNADLMSQYIEFVADRLLVALGYEKVYNVVNPFDWMELISLQGKTNFFEKRVGEYQKAGVMSSLNGGGAD--- 314
|
330
....*....|....*
gi 224000239 321 sggvaAKELDFAADF 335
Cdd:PLN02492 315 -----NHVFSLDEDF 324
|
|
| PTZ00211 |
PTZ00211 |
ribonucleoside-diphosphate reductase small subunit; Provisional |
1-314 |
0e+00 |
|
ribonucleoside-diphosphate reductase small subunit; Provisional
Pssm-ID: 240315 [Multi-domain] Cd Length: 330 Bit Score: 559.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 1 EPICRtdEEGSRFSLFPIAYPDLWSMYKQHVASFWTADEIDLSADLSDWHKkLNPDERHFISMVLAFFAGADGIVVENLA 80
Cdd:PTZ00211 12 EPLLK--ENPDRFVLFPIKYPDIWRMYKKAEASFWTAEEIDLGNDLKDWEK-LNDGERHFIKHVLAFFAASDGIVLENLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 81 ERFCREVTVPEARCFYGFQMAMESIHQETYCLLIDTYITDPKVRERLFSAHATVPSVERKASWAQRYIGSKASFAERLVA 160
Cdd:PTZ00211 89 QRFMREVQVPEARCFYGFQIAMENIHSETYSLLIDTYITDEEEKDRLFHAIETIPAIKKKAEWAAKWINSSNSFAERLVA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 161 FAAVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCSFACQLYSKLKLKLSQEEIQTIINEAVDVEKSFICDA 240
Cdd:PTZ00211 169 FAAVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHTDFACLLYSHLKNKLPRERVQEIIKEAVEIEREFICDA 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224000239 241 LPVSLIGMNSRLMAQYIEFVADRMLTDLGYQAMYGSKNPFDWMDMISLEGKTNFFEKRVGEYQKSGVMASLEGK 314
Cdd:PTZ00211 249 LPVDLIGMNSRLMAQYIEFVADRLLVALGVPKIYNSKNPFDWMDMISLQGKTNFFEKRVGEYQKAGVMAERTSK 322
|
|
| Ribonuc_red_sm |
pfam00268 |
Ribonucleotide reductase, small chain; |
12-279 |
9.20e-139 |
|
Ribonucleotide reductase, small chain;
Pssm-ID: 425568 [Multi-domain] Cd Length: 276 Bit Score: 394.17 E-value: 9.20e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 12 RFSLFPIAYPDLWSMYKQHVASFWTADEIDLSADLSDWhKKLNPDERHFISMVLAFFAGADGIVVENLAERFCREVTVPE 91
Cdd:pfam00268 1 RFNLNPIKYPEIWEFYKKLEANFWTPEEIPLSKDIKDW-KKLSEDEREFIKRVLAFLALLDTLVNENLVERFSREVQTPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 92 ARCFYGFQMAMESIHQETYCLLIDTYITDPKVRERLFSAHATVPSVERKASWAQRYI-GSKASFAERLVAFAAVEGIFFS 170
Cdd:pfam00268 80 ARAFYGFQAFMENIHSESYSYILDTLGKDPEEIDELFNWIETNPALQKKAEWILKWYqDFDSDFLERLVAFAILEGIFFY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 171 GSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCSFACQLYSKLKLKL-------SQEEIQTIINEAVDVEKSFICDALPV 243
Cdd:pfam00268 160 SGFAAILWLKRRGKMPGLAEIIELISRDEGLHGDFACLLFQHLKEENpeletkeLKEEVYDLIKEAVELEKEFLDDALPV 239
|
250 260 270
....*....|....*....|....*....|....*..
gi 224000239 244 SLIGMNSRLMAQYIEFVADRMLTDLGYQAMYGS-KNP 279
Cdd:pfam00268 240 GLLGMNAEDVKQYIEYVADRRLMNLGYEKLYNVeVNP 276
|
|
| RNRR2 |
cd01049 |
Ribonucleotide Reductase, R2/beta subunit, ferritin-like diiron-binding domain; Ribonucleotide ... |
13-288 |
7.76e-130 |
|
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: 371.96 E-value: 7.76e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 13 FSLFPIAYPDLWSMYKQHVASFWTADEIDLSADLSDWhKKLNPDERHFISMVLAFFAGADGIVVENLAERFCREVTVPEA 92
Cdd:cd01049 1 FNLNPIKYPWAWELYKKAEANFWTPEEIDLSKDLKDW-EKLTEAERHFIKRVLAFLAALDSIVGENLVELFSRHVQIPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 93 RCFYGFQMAMESIHQETYCLLIDTYITDPKvRERLFSAHATVPSVERKASWAQRYI-----GSKASFAERLVAFAAVEGI 167
Cdd:cd01049 80 RAFYGFQAFMENIHSESYSYILDTLGKDEE-RDELFEAIETDPALKKKADWILRWYdnlddNTKESFAERLVAFAILEGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 168 FFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCSFACQLYSKLKLK-------LSQEEIQTIINEAVDVEKSFICDA 240
Cdd:cd01049 159 FFYSGFAAIFWLARRGKMPGLAEIIELISRDESLHGDFACLLIRELLNEnpelfteEFKEEVYELIKEAVELEKEFARDL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 224000239 241 LPVSLIGMNSRLMAQYIEFVADRMLTDLGYQAMYGS--KNPFDWMDMISL 288
Cdd:cd01049 239 LPDGILGLNKEDMKQYIEYVANRRLENLGLEKLFNVedKNPFDWMELISD 288
|
|
| NrdB |
COG0208 |
Ribonucleotide reductase beta subunit, ferritin-like domain [Nucleotide transport and ... |
12-310 |
2.10e-114 |
|
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: 334.44 E-value: 2.10e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 12 RFSLFPIAYPDLWSMYKQHVASFWTADEIDLSADLSDWhKKLNPDERHFISMVLAFFAGADGIVVENLAERFCREVTVPE 91
Cdd:COG0208 13 RINWNPIKYPWAYELYKKQLANFWLPEEVPLSNDIKDW-KKLSDDERHLIKRVLGFLTLLDSIQGNNLVLALYPHVTAPE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 92 ARCFYGFQMAMESIHQETYCLLIDTYITDPkvrERLFSAHATVPSVERKASWAQRYI------GSKASFAERLVAFAAVE 165
Cdd:COG0208 92 VRAVLSRQAFMEAIHAKSYSYILETLGLDI---DEIFNWIEENPALQKKAEFILKYYddlgtrETKKDLLKSLVASVFLE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 166 GIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCSFACQLYSKLKLKLS-------QEEIQTIINEAVDVEKSFIC 238
Cdd:COG0208 169 GIFFYSGFAYPLSLARRGKMKGTAEIIRLILRDESLHGNFGIYLINTIREENPelfteelKEEIYELLKEAVELEKEYAD 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224000239 239 DALPVSLIGMNSRLMAQYIEFVADRMLTDLGYQAMY-GSKNPFDWMD-MISLEGKTNFFEKRVGEYQKSGVMAS 310
Cdd:COG0208 249 DLFPDGILGLNAEDVKQYIRYIANKRLMNLGLEPLFeGDVNPFPWMSeGLDLNKKTDFFETRVTEYQKGGVEST 322
|
|
| PRK07209 |
PRK07209 |
ribonucleotide-diphosphate reductase subunit beta; Validated |
4-308 |
2.44e-59 |
|
ribonucleotide-diphosphate reductase subunit beta; Validated
Pssm-ID: 235968 Cd Length: 369 Bit Score: 194.83 E-value: 2.44e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 4 CRTDEEgsrfSLFPIAYPDLWSMYKQHVASFWTADEIDLSADLSDWHKK--LNPDERHFISMVLAFFAGADGIVVENLAE 81
Cdd:PRK07209 44 CRADVN----QLVPFKYKWAWEKYLAGCANHWMPQEVNMSRDIALWKSPngLTEDERRIVKRNLGFFSTADSLVANNIVL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 82 RFCREVTVPEARCFYGFQMAMESIHQETYCLLIDTYITDPkvrERLFSAHATVPSVERKASWAQRYIGSKA--------- 152
Cdd:PRK07209 120 AIYRHITNPECRQYLLRQAFEEAIHTHAYQYIVESLGLDE---GEIFNMYHEVPSIRAKDEFLIPFTRSLTdpnfktgtp 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 153 ----SFAERLVAFAAV-EGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCSFACQLYSKLKLKLS-------QE 220
Cdd:PRK07209 197 endqKLLRNLIAFYCImEGIFFYVGFTQILSLGRQNKMTGIAEQYQYILRDESMHLNFGIDLINQIKLENPhlwtaefQA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 221 EIQTIINEAVDVEKSFICDALPVSLIGMNSRLMAQYIEFVADRMLTDLGYQAMY-GSKNPFDWM-DMISLEGKTNFFEKR 298
Cdd:PRK07209 277 EIRELIKEAVELEYRYARDTMPRGVLGLNASMFKDYLRFIANRRLQQIGLKPQYpGTENPFPWMsEMIDLKKEKNFFETR 356
|
330
....*....|
gi 224000239 299 VGEYQKSGVM 308
Cdd:PRK07209 357 VIEYQTGGAL 366
|
|
| nrdF |
PRK09614 |
ribonucleotide-diphosphate reductase subunit beta; Reviewed |
17-305 |
2.50e-49 |
|
ribonucleotide-diphosphate reductase subunit beta; Reviewed
Pssm-ID: 236591 [Multi-domain] Cd Length: 324 Bit Score: 167.31 E-value: 2.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 17 PIAYPDLWSMYKQHVASFWTADEIDLSADLSDWhKKLNPDERHFISMVLAFFAGADGIVVENLAERFCREVTVPEARCFY 96
Cdd:PRK09614 16 KIEDPWDYEAWKRLTANFWLPEEVPLSNDLKDW-KKLSDEEKNLYTRVFGGLTLLDTLQNNNGMPNLMPDITTPEEEAVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 97 GFQMAMESIHQETYCLLIDTyITDPKVRERLFSAHATVPSVERKASWAQR-YIGSKASFAERLVAFAAV-EGIFFSGSFC 174
Cdd:PRK09614 95 ANIAFMEAVHAKSYSYIFST-LCSPEEIDEAFEWAEENPYLQKKADIIQDfYEPLKKKILRKAAVASVFlEGFLFYSGFY 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 175 AIFWLKKRGLMPGltfSNELIS---RDEGLHCSFACQLYSKLKLKLS-------QEEIQTIINEAVDVEKSFICDALPVs 244
Cdd:PRK09614 174 YPLYLARQGKMTG---TAQIIRliiRDESLHGYYIGYLFQEGLEELPeleqeelKDEIYDLLYELYENEEAYTELLYDI- 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224000239 245 lIGmNSRLMAQYIEFVADRMLTDLGYQAMYGS--KNPFDWMDMISLEG--KTNFFEKRVGEYQKS 305
Cdd:PRK09614 250 -VG-LAEDVKKYIRYNANKRLMNLGLEPLFPEeeEVNPIWLNGLSNNAdeNHDFFEGKGTSYVKG 312
|
|
| PRK12759 |
PRK12759 |
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional |
9-310 |
1.03e-26 |
|
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional
Pssm-ID: 139206 [Multi-domain] Cd Length: 410 Bit Score: 108.96 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 9 EGSRFSLF-----PIAYPDLWSMYKQHVASFWTADEIDLSADLSDWHK-KLNPDERHFISMVLAFFAGADGIVVENLAER 82
Cdd:PRK12759 89 KGSSLTTFsktykPFNYPWAVDLTVKHEKAHWIEDEIDLSEDVTDWKNgKITKVEKEYITNILRLFTQSDVAVGQNYYDQ 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 83 FCREVTVPEARCFYGFQMAMESIHQETYCLLIDTYitdpkvrerlfsahaTVPSVERKASWAQRYIGSKASF-------A 155
Cdd:PRK12759 169 FIPLFKNNEIRNMLGSFAAREGIHQRAYALLNDTL---------------GLPDSEYHAFLEYKAMTDKIDFmmdadptT 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 156 ERLVAFAAVEGIFFSG-----SFCAIFWLKKRGLMPGLTFSNELISRDEGLHCS-------FACQLYSKLKLKLSQEEIQ 223
Cdd:PRK12759 234 RRGLGLCLAKTVFNEGvalfaSFAMLLNFQRFGKMKGMGKVVEWSIRDESMHVEgnaalfrIYCQENPYIVDNEFKKEIY 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 224 TIINEAVDVEKSFICDALPVSLI-GMNSRLMAQYIEFVADRMLTDLGYQAMYG-SKNPFDWMDMIsLEG--KTNFFEKRV 299
Cdd:PRK12759 314 LMASKAVELEDRFIELAYELGTIeGLKADEVKQYIRHITDRRLNQLGLKEIYNiEKNPLTWLEWI-LNGadHTNFFENRV 392
|
330
....*....|.
gi 224000239 300 GEYQKSGVMAS 310
Cdd:PRK12759 393 TEYEVAGLTGS 403
|
|
| nrdF2 |
PRK13966 |
ribonucleotide-diphosphate reductase subunit beta; Provisional |
26-274 |
5.05e-09 |
|
ribonucleotide-diphosphate reductase subunit beta; Provisional
Pssm-ID: 140022 Cd Length: 324 Bit Score: 56.65 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 26 MYKQHVASFWTADEIDLSADLSDWHKkLNPDERHFISMVLAFFAGADGIVVENLAERFCREVTVPEARCFYGFQMAMESI 105
Cdd:PRK13966 27 VWDRLTGNFWLPEKVPVSNDIPSWGT-LTAGEKQLTMRVFTGLTMLDTIQGTVGAVSLIPDALTPHEEAVLTNIAFMESV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 106 HQETYCLLIDTYITDPKVRERlFSAHATVPSVERKASWAQRYIGSKASFAERLVAFAAVEGIFFSGSFCAIFWlKKRGLM 185
Cdd:PRK13966 106 HAKSYSQIFSTLCSTAEIDDA-FRWSEENRNLQRKAEIVLQYYRGDEPLKRKVASTLLESFLFYSGFYLPMYW-SSRAKL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 186 PGLTFSNELISRDEGLHCSFACQLYSKLKLKLSQEEIQTIIN-------EAVDVEKSFICDALpvSLIGMNSRLmAQYIE 258
Cdd:PRK13966 184 TNTADMIRLIIRDEAVHGYYIGYKFQRGLALVDDVTRAELKDytyellfELYDNEVEYTQDLY--DEVGLTEDV-KKFLR 260
|
250
....*....|....*.
gi 224000239 259 FVADRMLTDLGYQAMY 274
Cdd:PRK13966 261 YNANKALMNLGYEALF 276
|
|
| nrdF1 |
PRK13967 |
ribonucleotide-diphosphate reductase subunit beta; Provisional |
26-274 |
4.00e-06 |
|
ribonucleotide-diphosphate reductase subunit beta; Provisional
Pssm-ID: 140023 Cd Length: 322 Bit Score: 47.80 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 26 MYKQHVASFWTADEIDLSADLSDWhKKLNPDERHFISMVLAFFAGADGIVVENLAERFCREVTVPEARCFYGFQMAMESI 105
Cdd:PRK13967 25 VWERLTGNFWLPEKIPLSNDLASW-QTLSSTEQQTTIRVFTGLTLLDTAQATVGAVAMIDDAVTPHEEAVLTNMAFMESV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 106 HQETYCLLIDTYITDPKVRERlFSAHATVPSVERKASWAQRYIGSKASFAERLVAFAAVEGIFFSGSFCAIFWlKKRGLM 185
Cdd:PRK13967 104 HAKSYSSIFSTLCSTKQIDDA-FDWSEQNPYLQRKAQIIVDYYRGDDALKRKASSVMLESFLFYSGFYLPMYW-SSRGKL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 186 PGLTFSNELISRDEGLH---CSFACQL------------YSKLKLKLSQEEIQTIINEAVDV--EKSFICDALPvsligm 248
Cdd:PRK13967 182 TNTADLIRLIIRDEAVHgyyIGYKCQRgladltdaeradHREYTCELLHTLYANEIDYAHDLydELGWTDDVLP------ 255
|
250 260
....*....|....*....|....*.
gi 224000239 249 nsrlmaqYIEFVADRMLTDLGYQAMY 274
Cdd:PRK13967 256 -------YMRYNANKALANLGYQPAF 274
|
|
| PRK08326 |
PRK08326 |
R2-like ligand-binding oxidase; |
32-205 |
8.96e-06 |
|
R2-like ligand-binding oxidase;
Pssm-ID: 236242 Cd Length: 311 Bit Score: 46.53 E-value: 8.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 32 ASFWTADEIDLSADLSDWhKKLNPDERHFISMVLAFFAGADGIVVENLA------------------ERFCREvtvpEAR 93
Cdd:PRK08326 36 AKFWNPADIDFSRDAEDW-EKLSDEERDYATRLCAQFIAGEEAVTLDIQplisamaaegrledemylTQFAFE----EAK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 94 CFYGFQMAMES--IHQETYCLLIDtyitDPKVReRLFsaHATVPSverkASWAQRYIGSKASFAERLVAF-AAVEGIFFS 170
Cdd:PRK08326 111 HTEAFRRWFDAvgVTEDLSVYTDD----NPSYR-QIF--YEELPA----ALNRLSTDPSPENQVRASVTYnHVVEGVLAE 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 224000239 171 GSFCAIFWL-KKRGLMPGLTFSNELISRDEGLHCSF 205
Cdd:PRK08326 180 TGYYAWRKIcVTRGILPGLQELVRRIGDDERRHIAW 215
|
|
| RNRR2_Rv0233_like |
cd07911 |
Ribonucleotide Reductase R2-like protein, Mn/Fe-binding domain; Rv0233 is a Mycobacterium ... |
34-205 |
2.98e-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: 41.94 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 34 FWTADEIDLSADLSDWhKKLNPDERHFISMVLAFFAGADGIVVENLAE------------------RFCREvtvpEARCF 95
Cdd:cd07911 21 FWNPADIDFSQDREDW-EQLSEEERDLALRLCAGFIAGEEAVTLDLLPlmmamaaegrleeemyltQFLFE----EAKHT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224000239 96 YGFQMAMESIHQETyclLIDTYITDPKVR---ERLFSAH---ATVPSVERKASWAQRYIGSkasfaerlvafaaVEGIFF 169
Cdd:cd07911 96 DFFRRWLDAVGVSD---DLSDLHTAVYREpfyEALPYAElrlYLDASPAAQVRASVTYNMI-------------VEGVLA 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 224000239 170 SGSFCAIF-WLKKRGLMPGLTFSNELISRDEGLHCSF 205
Cdd:cd07911 160 ETGYYAWRtICEKRGILPGMQEGIRRLGDDESRHIAW 196
|
|
|