|
Name |
Accession |
Description |
Interval |
E-value |
| nrdB |
PRK09101 |
ribonucleotide-diphosphate reductase subunit beta; Reviewed |
1-375 |
0e+00 |
|
ribonucleotide-diphosphate reductase subunit beta; Reviewed
Pssm-ID: 181647 Cd Length: 376 Bit Score: 900.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 1 AYTTFSQTKNDQLKEPMFFGQPVNVARYDQQKYDIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKYQ 80
Cdd:PRK09101 2 AYTTFSQTKNDQLKEPMFFGQSVNVARYDQQKYEIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKYQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 81 TLLDSIQGRSPNVALLPLISIPELETWVETWAFSETIHSRSYTHIIRNIVNDPSVVFDDIVTNEQIQKRAEGISSYYDEL 160
Cdd:PRK09101 82 TLLDSIQGRSPNVALLPLVSIPELETWIETWSFSETIHSRSYTHIIRNIVNDPSVVFDDIVTNEEILKRAKDISSYYDDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 161 IEMTSYWHLLGEGTHTVNGKTVTVSLRELKKKLYLCLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEAL 240
Cdd:PRK09101 162 IEMTSYYHLLGEGTHTVNGKTVTVSLRELKKKLYLCLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 241 HLTGTQHMLNLLRSGADDPEMAEIAEECKQECYDLFVQAAQQEKDWADYLFRDGSMIGLNKDILCQYVEYITNIRMQAVG 320
Cdd:PRK09101 242 HLTGTQHMLNLMRSGKDDPEMAEIAEECKQECYDLFVQAAEQEKEWADYLFKDGSMIGLNKDILCQYVEYITNIRMQAVG 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
1R65_A 321 LDLPFNTRSNPIPWINTWLVSDNVQVAPQEVEVSSYLVGQIDSEVDTDDLSNFQL 375
Cdd:PRK09101 322 LDLPFQTRSNPIPWINAWLVSDNVQVAPQEVEVSSYLVGQIDSEVDTDDLSDFEL 376
|
|
| NrdB |
COG0208 |
Ribonucleotide reductase beta subunit, ferritin-like domain [Nucleotide transport and ... |
13-368 |
6.91e-142 |
|
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: 405.71 E-value: 6.91e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 13 LKEPMFFGQPVNVARYDQQKYDIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKYQTLLDSIQGRSPN 92
Cdd:COG0208 1 LDEPIINGLTTNRINWNPIKYPWAYELYKKQLANFWLPEEVPLSNDIKDWKKLSDDERHLIKRVLGFLTLLDSIQGNNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 93 VALLPLISIPELETWVETWAFSETIHSRSYTHIIRNIVNDPSVVFDDIVTNEQIQKRAEGISSYYDELIEmtsywhllge 172
Cdd:COG0208 81 LALYPHVTAPEVRAVLSRQAFMEAIHAKSYSYILETLGLDIDEIFNWIEENPALQKKAEFILKYYDDLGT---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 173 gthtvngktvtvslRELKKKLYLCLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLL 252
Cdd:COG0208 151 --------------RETKKDLLKSLVASVFLEGIFFYSGFAYPLSLARRGKMKGTAEIIRLILRDESLHGNFGIYLINTI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 253 RsgADDPEMaeIAEECKQECYDLFVQAAQQEKDWADYLFrDGSMIGLNKDILCQYVEYITNIRMQAVGLDLPFNTRSNPI 332
Cdd:COG0208 217 R--EENPEL--FTEELKEEIYELLKEAVELEKEYADDLF-PDGILGLNAEDVKQYIRYIANKRLMNLGLEPLFEGDVNPF 291
|
330 340 350
....*....|....*....|....*....|....*.
1R65_A 333 PWINTWLVSDNvQVAPQEVEVSSYLVGQIDSEVDTD 368
Cdd:COG0208 292 PWMSEGLDLNK-KTDFFETRVTEYQKGGVESTFDED 326
|
|
| RNRR2 |
cd01049 |
Ribonucleotide Reductase, R2/beta subunit, ferritin-like diiron-binding domain; Ribonucleotide ... |
28-340 |
3.73e-85 |
|
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: 259.86 E-value: 3.73e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 28 YDQQKYDIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKYQTLLDSIQGRSPNVALLPLISIPELETW 107
Cdd:cd01049 3 LNPIKYPWAWELYKKAEANFWTPEEIDLSKDLKDWEKLTEAERHFIKRVLAFLAALDSIVGENLVELFSRHVQIPEARAF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 108 VETWAFSETIHSRSYTHIIRNIVNDPSV--VFDDIVTNEQIQKRAEGISSYYDELIEMTsywhllgegthtvngktvtvs 185
Cdd:cd01049 83 YGFQAFMENIHSESYSYILDTLGKDEERdeLFEAIETDPALKKKADWILRWYDNLDDNT--------------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 186 lrelKKKLYLCLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLLRSGADDpemaEIA 265
Cdd:cd01049 142 ----KESFAERLVAFAILEGIFFYSGFAAIFWLARRGKMPGLAEIIELISRDESLHGDFACLLIRELLNENPE----LFT 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1R65_A 266 EECKQECYDLFVQAAQQEKDWADYLFRDGsMIGLNKDILCQYVEYITNIRMQAVGLDLPFNTR-SNPIPWINTWLV 340
Cdd:cd01049 214 EEFKEEVYELIKEAVELEKEFARDLLPDG-ILGLNKEDMKQYIEYVANRRLENLGLEKLFNVEdKNPFDWMELISD 288
|
|
| Ribonuc_red_sm |
pfam00268 |
Ribonucleotide reductase, small chain; |
32-331 |
2.34e-50 |
|
Ribonucleotide reductase, small chain;
Pssm-ID: 425568 [Multi-domain] Cd Length: 276 Bit Score: 169.99 E-value: 2.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 32 KYDIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKYQTLLDSIQGRSPNVALLPLISIPELETWVETW 111
Cdd:pfam00268 8 KYPEIWEFYKKLEANFWTPEEIPLSKDIKDWKKLSEDEREFIKRVLAFLALLDTLVNENLVERFSREVQTPEARAFYGFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 112 AFSETIHSRSYTHIIRNIVNDPS---VVFDDIVTNEQIQKRAEGISSYYDELIEmtsywhllgegthtvngktvtvslrE 188
Cdd:pfam00268 88 AFMENIHSESYSYILDTLGKDPEeidELFNWIETNPALQKKAEWILKWYQDFDS-------------------------D 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 189 LKKKLylcLMSVnALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLLRSGADDPEmaeiAEEC 268
Cdd:pfam00268 143 FLERL---VAFA-ILEGIFFYSGFAAILWLKRRGKMPGLAEIIELISRDEGLHGDFACLLFQHLKEENPELE----TKEL 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
1R65_A 269 KQECYDLFVQAAQQEKDWADYLFRDGsMIGLNKDILCQYVEYITNIRMQAVGLDLPFNTRSNP 331
Cdd:pfam00268 215 KEEVYDLIKEAVELEKEFLDDALPVG-LLGMNAEDVKQYIEYVADRRLMNLGYEKLYNVEVNP 276
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| nrdB |
PRK09101 |
ribonucleotide-diphosphate reductase subunit beta; Reviewed |
1-375 |
0e+00 |
|
ribonucleotide-diphosphate reductase subunit beta; Reviewed
Pssm-ID: 181647 Cd Length: 376 Bit Score: 900.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 1 AYTTFSQTKNDQLKEPMFFGQPVNVARYDQQKYDIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKYQ 80
Cdd:PRK09101 2 AYTTFSQTKNDQLKEPMFFGQSVNVARYDQQKYEIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKYQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 81 TLLDSIQGRSPNVALLPLISIPELETWVETWAFSETIHSRSYTHIIRNIVNDPSVVFDDIVTNEQIQKRAEGISSYYDEL 160
Cdd:PRK09101 82 TLLDSIQGRSPNVALLPLVSIPELETWIETWSFSETIHSRSYTHIIRNIVNDPSVVFDDIVTNEEILKRAKDISSYYDDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 161 IEMTSYWHLLGEGTHTVNGKTVTVSLRELKKKLYLCLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEAL 240
Cdd:PRK09101 162 IEMTSYYHLLGEGTHTVNGKTVTVSLRELKKKLYLCLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 241 HLTGTQHMLNLLRSGADDPEMAEIAEECKQECYDLFVQAAQQEKDWADYLFRDGSMIGLNKDILCQYVEYITNIRMQAVG 320
Cdd:PRK09101 242 HLTGTQHMLNLMRSGKDDPEMAEIAEECKQECYDLFVQAAEQEKEWADYLFKDGSMIGLNKDILCQYVEYITNIRMQAVG 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
1R65_A 321 LDLPFNTRSNPIPWINTWLVSDNVQVAPQEVEVSSYLVGQIDSEVDTDDLSNFQL 375
Cdd:PRK09101 322 LDLPFQTRSNPIPWINAWLVSDNVQVAPQEVEVSSYLVGQIDSEVDTDDLSDFEL 376
|
|
| NrdB |
COG0208 |
Ribonucleotide reductase beta subunit, ferritin-like domain [Nucleotide transport and ... |
13-368 |
6.91e-142 |
|
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: 405.71 E-value: 6.91e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 13 LKEPMFFGQPVNVARYDQQKYDIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKYQTLLDSIQGRSPN 92
Cdd:COG0208 1 LDEPIINGLTTNRINWNPIKYPWAYELYKKQLANFWLPEEVPLSNDIKDWKKLSDDERHLIKRVLGFLTLLDSIQGNNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 93 VALLPLISIPELETWVETWAFSETIHSRSYTHIIRNIVNDPSVVFDDIVTNEQIQKRAEGISSYYDELIEmtsywhllge 172
Cdd:COG0208 81 LALYPHVTAPEVRAVLSRQAFMEAIHAKSYSYILETLGLDIDEIFNWIEENPALQKKAEFILKYYDDLGT---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 173 gthtvngktvtvslRELKKKLYLCLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLL 252
Cdd:COG0208 151 --------------RETKKDLLKSLVASVFLEGIFFYSGFAYPLSLARRGKMKGTAEIIRLILRDESLHGNFGIYLINTI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 253 RsgADDPEMaeIAEECKQECYDLFVQAAQQEKDWADYLFrDGSMIGLNKDILCQYVEYITNIRMQAVGLDLPFNTRSNPI 332
Cdd:COG0208 217 R--EENPEL--FTEELKEEIYELLKEAVELEKEYADDLF-PDGILGLNAEDVKQYIRYIANKRLMNLGLEPLFEGDVNPF 291
|
330 340 350
....*....|....*....|....*....|....*.
1R65_A 333 PWINTWLVSDNvQVAPQEVEVSSYLVGQIDSEVDTD 368
Cdd:COG0208 292 PWMSEGLDLNK-KTDFFETRVTEYQKGGVESTFDED 326
|
|
| RNRR2 |
cd01049 |
Ribonucleotide Reductase, R2/beta subunit, ferritin-like diiron-binding domain; Ribonucleotide ... |
28-340 |
3.73e-85 |
|
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: 259.86 E-value: 3.73e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 28 YDQQKYDIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKYQTLLDSIQGRSPNVALLPLISIPELETW 107
Cdd:cd01049 3 LNPIKYPWAWELYKKAEANFWTPEEIDLSKDLKDWEKLTEAERHFIKRVLAFLAALDSIVGENLVELFSRHVQIPEARAF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 108 VETWAFSETIHSRSYTHIIRNIVNDPSV--VFDDIVTNEQIQKRAEGISSYYDELIEMTsywhllgegthtvngktvtvs 185
Cdd:cd01049 83 YGFQAFMENIHSESYSYILDTLGKDEERdeLFEAIETDPALKKKADWILRWYDNLDDNT--------------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 186 lrelKKKLYLCLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLLRSGADDpemaEIA 265
Cdd:cd01049 142 ----KESFAERLVAFAILEGIFFYSGFAAIFWLARRGKMPGLAEIIELISRDESLHGDFACLLIRELLNENPE----LFT 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1R65_A 266 EECKQECYDLFVQAAQQEKDWADYLFRDGsMIGLNKDILCQYVEYITNIRMQAVGLDLPFNTR-SNPIPWINTWLV 340
Cdd:cd01049 214 EEFKEEVYELIKEAVELEKEFARDLLPDG-ILGLNKEDMKQYIEYVANRRLENLGLEKLFNVEdKNPFDWMELISD 288
|
|
| nrdF |
PRK09614 |
ribonucleotide-diphosphate reductase subunit beta; Reviewed |
16-373 |
3.30e-51 |
|
ribonucleotide-diphosphate reductase subunit beta; Reviewed
Pssm-ID: 236591 [Multi-domain] Cd Length: 324 Bit Score: 173.47 E-value: 3.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 16 PMFFGQPVNVARYDQQKYDIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKYQTLLDSIQGRSPNVAL 95
Cdd:PRK09614 2 KIIGGNTYSAINWNKIEDPWDYEAWKRLTANFWLPEEVPLSNDLKDWKKLSDEEKNLYTRVFGGLTLLDTLQNNNGMPNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 96 LPLISIPELETWVETWAFSETIHSRSYTHIIRNIVNDPSV--VFDDIVTNEQIQKRAEGISSYYdeliemtsywhllgeg 173
Cdd:PRK09614 82 MPDITTPEEEAVLANIAFMEAVHAKSYSYIFSTLCSPEEIdeAFEWAEENPYLQKKADIIQDFY---------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 174 thtvngktvtvslRELKKKLYLCLMSVNA-LEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLL 252
Cdd:PRK09614 146 -------------EPLKKKILRKAAVASVfLEGFLFYSGFYYPLYLARQGKMTGTAQIIRLIIRDESLHGYYIGYLFQEG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 253 RSGADDPEMAEIaeecKQECYDLFVQAAQQEKDWADYLFRDgsmIGLNKDILcQYVEYITNIRMQAVGLDLPFNTR-SNP 331
Cdd:PRK09614 213 LEELPELEQEEL----KDEIYDLLYELYENEEAYTELLYDI---VGLAEDVK-KYIRYNANKRLMNLGLEPLFPEEeEVN 284
|
330 340 350 360
....*....|....*....|....*....|....*....|...
1R65_A 332 IPWINTwLVSDNVQVAPQ-EVEVSSYLVGQidSEVDTDDLSNF 373
Cdd:PRK09614 285 PIWLNG-LSNNADENHDFfEGKGTSYVKGA--TEATEDDDWDF 324
|
|
| Ribonuc_red_sm |
pfam00268 |
Ribonucleotide reductase, small chain; |
32-331 |
2.34e-50 |
|
Ribonucleotide reductase, small chain;
Pssm-ID: 425568 [Multi-domain] Cd Length: 276 Bit Score: 169.99 E-value: 2.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 32 KYDIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKYQTLLDSIQGRSPNVALLPLISIPELETWVETW 111
Cdd:pfam00268 8 KYPEIWEFYKKLEANFWTPEEIPLSKDIKDWKKLSEDEREFIKRVLAFLALLDTLVNENLVERFSREVQTPEARAFYGFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 112 AFSETIHSRSYTHIIRNIVNDPS---VVFDDIVTNEQIQKRAEGISSYYDELIEmtsywhllgegthtvngktvtvslrE 188
Cdd:pfam00268 88 AFMENIHSESYSYILDTLGKDPEeidELFNWIETNPALQKKAEWILKWYQDFDS-------------------------D 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 189 LKKKLylcLMSVnALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLLRSGADDPEmaeiAEEC 268
Cdd:pfam00268 143 FLERL---VAFA-ILEGIFFYSGFAAILWLKRRGKMPGLAEIIELISRDEGLHGDFACLLFQHLKEENPELE----TKEL 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
1R65_A 269 KQECYDLFVQAAQQEKDWADYLFRDGsMIGLNKDILCQYVEYITNIRMQAVGLDLPFNTRSNP 331
Cdd:pfam00268 215 KEEVYDLIKEAVELEKEFLDDALPVG-LLGMNAEDVKQYIEYVADRRLMNLGYEKLYNVEVNP 276
|
|
| PRK07209 |
PRK07209 |
ribonucleotide-diphosphate reductase subunit beta; Validated |
48-334 |
5.18e-21 |
|
ribonucleotide-diphosphate reductase subunit beta; Validated
Pssm-ID: 235968 Cd Length: 369 Bit Score: 93.14 E-value: 5.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 48 WRPEEVDVSRDrI----DYQALPEHEKHIFISNLKYQTLLDSIQGRSPNVALLPLISIPELETWVETWAFSETIHSRSYT 123
Cdd:PRK07209 71 WMPQEVNMSRD-IalwkSPNGLTEDERRIVKRNLGFFSTADSLVANNIVLAIYRHITNPECRQYLLRQAFEEAIHTHAYQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 124 HIIRNIVNDPSVVFDDIVTNEQIQKRAEGISSYYDELIEMtsywhllgegthtvNGKTVTV-SLRELKKKL--YLCLMsv 200
Cdd:PRK07209 150 YIVESLGLDEGEIFNMYHEVPSIRAKDEFLIPFTRSLTDP--------------NFKTGTPeNDQKLLRNLiaFYCIM-- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 201 nalEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLLRsgADDPEMAeiAEECKQECYDLFVQAA 280
Cdd:PRK07209 214 ---EGIFFYVGFTQILSLGRQNKMTGIAEQYQYILRDESMHLNFGIDLINQIK--LENPHLW--TAEFQAEIRELIKEAV 286
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
1R65_A 281 QQEKDWA-DYLFRDgsMIGLNKDILCQYVEYITNIRMQAVGLDLPFNTRSNPIPW 334
Cdd:PRK07209 287 ELEYRYArDTMPRG--VLGLNASMFKDYLRFIANRRLQQIGLKPQYPGTENPFPW 339
|
|
| PTZ00211 |
PTZ00211 |
ribonucleoside-diphosphate reductase small subunit; Provisional |
6-356 |
1.10e-18 |
|
ribonucleoside-diphosphate reductase small subunit; Provisional
Pssm-ID: 240315 [Multi-domain] Cd Length: 330 Bit Score: 85.98 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 6 SQTKNDQLKEPMFFGQPVNVARYDQQKYDIFEKLiEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHiFISN-LKYQTLLD 84
Cdd:PTZ00211 3 EAMKENEEEEPLLKENPDRFVLFPIKYPDIWRMY-KKAEASFWTAEEIDLGNDLKDWEKLNDGERH-FIKHvLAFFAASD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 85 SIQGRSPNVALLPLISIPELETWvetWAFS---ETIHSRSYTHIIRNIVNDPS---VVFDDIVTNEQIQKRAEgissyyd 158
Cdd:PTZ00211 81 GIVLENLAQRFMREVQVPEARCF---YGFQiamENIHSETYSLLIDTYITDEEekdRLFHAIETIPAIKKKAE------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 159 eliemtsyWhllgeGTHTVNGKTvtvSLRELkkklylcLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDE 238
Cdd:PTZ00211 151 --------W-----AAKWINSSN---SFAER-------LVAFAAVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 239 ALHLTGTQHMLNLLRSGADDPEMAEIAEEckqecydlfvqAAQQEKDW-ADYLFRDgsMIGLNKDILCQYVEYITNIRMQ 317
Cdd:PTZ00211 208 GLHTDFACLLYSHLKNKLPRERVQEIIKE-----------AVEIEREFiCDALPVD--LIGMNSRLMAQYIEFVADRLLV 274
|
330 340 350
....*....|....*....|....*....|....*....
1R65_A 318 AVGLDLPFNTrSNPIPWINtwLVSDNVQVAPQEVEVSSY 356
Cdd:PTZ00211 275 ALGVPKIYNS-KNPFDWMD--MISLQGKTNFFEKRVGEY 310
|
|
| PRK13965 |
PRK13965 |
ribonucleotide-diphosphate reductase subunit beta; Provisional |
2-325 |
2.27e-18 |
|
ribonucleotide-diphosphate reductase subunit beta; Provisional
Pssm-ID: 184425 [Multi-domain] Cd Length: 335 Bit Score: 85.21 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 2 YTTFSQTKND-QLKEPMFFGQPVNVARYDQQK-YDIFEKLIEKqlsfFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKY 79
Cdd:PRK13965 3 YYDRSQSPIEyALSETQKPLRSINWNYLNDDKdLEVWNRVTQN----FWLPEKVPVSNDLNSWRSLGEDWQQLITRTFTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 80 QTLLDSIQGRSPNVALLPlISIPELETWVET-WAFSETIHSRSYTHIIRNIVNDPSV--VFDDIVTNEQIQKRAEGISSY 156
Cdd:PRK13965 79 LTLLDTVQATVGDVAQIP-HSQTDHEQVIYTnFAFMVAIHARSYGTIFSTLCSSEQIeeAHEWVVSTESLQRRARVLIPY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 157 YDeliemtsywhllGEGThtvngktvtvslreLKKKLYLCLMSvnaleAIRFYVSFACSFAFAERELMEGNAKIIRLIAR 236
Cdd:PRK13965 158 YT------------GDDP--------------LKSKVAAAMMP-----GFLLYGGFYLPFYLSARGKLPNTSDIIRLILR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 237 DEALH--LTGTQHMLNLlrsgadDPEMAEIAEECKQECYDLFVQAAQQEKDWADYLFRDgsmIGLNKDILcQYVEYITNI 314
Cdd:PRK13965 207 DKVIHnyYSGYKYQQKV------ARLSPEKQAEMKAFVFDLLYELIDLEKAYLRELYAG---FDLAEDAI-RFSLYNAGK 276
|
330
....*....|.
1R65_A 315 RMQAVGLDLPF 325
Cdd:PRK13965 277 FLQNLGYESPF 287
|
|
| nrdF2 |
PRK13966 |
ribonucleotide-diphosphate reductase subunit beta; Provisional |
47-331 |
1.73e-16 |
|
ribonucleotide-diphosphate reductase subunit beta; Provisional
Pssm-ID: 140022 Cd Length: 324 Bit Score: 79.38 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 47 FWRPEEVDVSRDRIDYQALPEHEKHIFISNLKYQTLLDSIQGRSPNVALLPLISIPELETWVETWAFSETIHSRSYTHII 126
Cdd:PRK13966 35 FWLPEKVPVSNDIPSWGTLTAGEKQLTMRVFTGLTMLDTIQGTVGAVSLIPDALTPHEEAVLTNIAFMESVHAKSYSQIF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 127 RNIVNDPSV--VFDDIVTNEQIQKRAEGISSYY--DEliemtsywhllgegthtvngktvtvslrELKKKLYLCLmsvna 202
Cdd:PRK13966 115 STLCSTAEIddAFRWSEENRNLQRKAEIVLQYYrgDE----------------------------PLKRKVASTL----- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 203 LEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALH--LTGTQHMLNLlrsgaddpemAEIAEECKQE----CYDLF 276
Cdd:PRK13966 162 LESFLFYSGFYLPMYWSSRAKLTNTADMIRLIIRDEAVHgyYIGYKFQRGL----------ALVDDVTRAElkdyTYELL 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
1R65_A 277 VQAAQQEKDWADYLFrdgSMIGLNKDILcQYVEYITNIRMQAVGLDLPF---NTRSNP 331
Cdd:PRK13966 232 FELYDNEVEYTQDLY---DEVGLTEDVK-KFLRYNANKALMNLGYEALFprdETDVNP 285
|
|
| PRK12759 |
PRK12759 |
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional |
48-366 |
1.14e-14 |
|
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional
Pssm-ID: 139206 [Multi-domain] Cd Length: 410 Bit Score: 74.68 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 48 WRPEEVDVSRDRIDYQ--ALPEHEKHIFISNLKYQTLLDSIQGRSPNVALLPLISIPELETWVETWAFSETIHSRSYThi 125
Cdd:PRK12759 120 WIEDEIDLSEDVTDWKngKITKVEKEYITNILRLFTQSDVAVGQNYYDQFIPLFKNNEIRNMLGSFAAREGIHQRAYA-- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 126 irnIVNDPSVVFDdivtneqiqkraegisSYYDELIE---MTSYWHLLGEGTHTVngktvtvslrelKKKLYLCLMSVNA 202
Cdd:PRK12759 198 ---LLNDTLGLPD----------------SEYHAFLEykaMTDKIDFMMDADPTT------------RRGLGLCLAKTVF 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 203 LEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLLrsGADDPEMAEiaEECKQECYDLFVQAAQQ 282
Cdd:PRK12759 247 NEGVALFASFAMLLNFQRFGKMKGMGKVVEWSIRDESMHVEGNAALFRIY--CQENPYIVD--NEFKKEIYLMASKAVEL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 283 EKDWADYLFRDGSMIGLNKDILCQYVEYITNIRMQAVGLDLPFNTRSNPIPWINtWLVSDNVQVAPQEVEVSSYLVGQID 362
Cdd:PRK12759 323 EDRFIELAYELGTIEGLKADEVKQYIRHITDRRLNQLGLKEIYNIEKNPLTWLE-WILNGADHTNFFENRVTEYEVAGLT 401
|
....
1R65_A 363 SEVD 366
Cdd:PRK12759 402 GSWD 405
|
|
| nrdF1 |
PRK13967 |
ribonucleotide-diphosphate reductase subunit beta; Provisional |
29-326 |
1.78e-14 |
|
ribonucleotide-diphosphate reductase subunit beta; Provisional
Pssm-ID: 140023 Cd Length: 322 Bit Score: 73.61 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 29 DQQKYDIFEKLIEKqlsfFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKYQTLLDSIQGRSPNVALLPLISIPELETWV 108
Cdd:PRK13967 19 DAKDLQVWERLTGN----FWLPEKIPLSNDLASWQTLSSTEQQTTIRVFTGLTLLDTAQATVGAVAMIDDAVTPHEEAVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 109 ETWAFSETIHSRSYTHIIRNIVNDPSV--VFDDIVTNEQIQKRAEGISSYYdeliemtsywhllgEGTHTVNGKTVTVsl 186
Cdd:PRK13967 95 TNMAFMESVHAKSYSSIFSTLCSTKQIddAFDWSEQNPYLQRKAQIIVDYY--------------RGDDALKRKASSV-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 187 relkkklylclmsvnALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHltgTQHMLNLLRSGADDPEMAEIAE 266
Cdd:PRK13967 159 ---------------MLESFLFYSGFYLPMYWSSRGKLTNTADLIRLIIRDEAVH---GYYIGYKCQRGLADLTDAERAD 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 267 ECKQECyDLFVQAAQQEKDWADYLFRDgsmIGLNKDILcQYVEYITNIRMQAVGLDLPFN 326
Cdd:PRK13967 221 HREYTC-ELLHTLYANEIDYAHDLYDE---LGWTDDVL-PYMRYNANKALANLGYQPAFD 275
|
|
| PLN02492 |
PLN02492 |
ribonucleoside-diphosphate reductase |
32-335 |
5.97e-13 |
|
ribonucleoside-diphosphate reductase
Pssm-ID: 215272 Cd Length: 324 Bit Score: 68.92 E-value: 5.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 32 KYDIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHiFISN-LKYQTLLDSIQGRSPNVALLPLISIPELETWvet 110
Cdd:PLN02492 17 KYPQIWEMYKKAEASFWTAEEVDLSADLKDWEKLTDDERH-FISHvLAFFAASDGIVLENLAARFMKEVQVPEARAF--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 111 WAFS---ETIHSRSYTHIIRNIVNDPSV---VFDDIVTNEQIQKRAEgissyydeliemtsyWHLLGEGTHTvngktvtv 184
Cdd:PLN02492 93 YGFQiaiENIHSEMYSLLLDTYIKDPKEkdrLFNAIETIPCVAKKAD---------------WALRWIDSSA-------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R65_A 185 SLRELkkklylcLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLLRSGADDPEMAEI 264
Cdd:PLN02492 150 SFAER-------LVAFACVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLKNKLSEERVKEI 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1R65_A 265 AEEckqecydlfvqAAQQEKDW-ADYLfrDGSMIGLNKDILCQYVEYITNIRMQAVGLDLPFNTRsNPIPWI 335
Cdd:PLN02492 223 VCE-----------AVEIEKEFvCDAL--PCALVGMNADLMSQYIEFVADRLLVALGYEKVYNVV-NPFDWM 280
|
|
| |
