|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02492 |
PLN02492 |
ribonucleoside-diphosphate reductase |
71-390 |
0e+00 |
|
ribonucleoside-diphosphate reductase
Pssm-ID: 215272 Cd Length: 324 Bit Score: 621.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 71 EPLLRENPRRFVVFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWEALKPDERHFISHVLAFFAASDGIVNENLVERF 150
Cdd:PLN02492 1 EPLLAENPDRFCMFPIKYPQIWEMYKKAEASFWTAEEVDLSADLKDWEKLTDDERHFISHVLAFFAASDGIVLENLAARF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 151 SQEVQVTEARCFYGFQIAMENIHSEMYSLLIDTYIKDSKEREYLFNAIETMPCVKKKADWALRWIgDKEATYGERVVAFA 230
Cdd:PLN02492 81 MKEVQVPEARAFYGFQIAIENIHSEMYSLLLDTYIKDPKEKDRLFNAIETIPCVAKKADWALRWI-DSSASFAERLVAFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 231 AVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEQRVKEIITNSVRIEQEFLTEALP 310
Cdd:PLN02492 160 CVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLKNKLSEERVKEIVCEAVEIEKEFVCDALP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 311 VKLIGMNCTLMKQYIEFVADRLMLELGFNKIFKVENPFDFMENISLEGKTNFFEKRVGEYQRMGVMSN-----STENSFT 385
Cdd:PLN02492 240 CALVGMNADLMSQYIEFVADRLLVALGYEKVYNVVNPFDWMELISLQGKTNFFEKRVGEYQKAGVMSSlngggADNHVFS 319
|
....*
gi 77416595 386 LDADF 390
Cdd:PLN02492 320 LDEDF 324
|
|
| Ribonuc_red_sm |
pfam00268 |
Ribonucleotide reductase, small chain; |
80-347 |
1.67e-155 |
|
Ribonucleotide reductase, small chain;
Pssm-ID: 425568 [Multi-domain] Cd Length: 276 Bit Score: 438.86 E-value: 1.67e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 80 RFVVFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWEALKPDERHFISHVLAFFAASDGIVNENLVERFSQEVQVTEA 159
Cdd:pfam00268 1 RFNLNPIKYPEIWEFYKKLEANFWTPEEIPLSKDIKDWKKLSEDEREFIKRVLAFLALLDTLVNENLVERFSREVQTPEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 160 RCFYGFQIAMENIHSEMYSLLIDTYIKDSKEREYLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSG 239
Cdd:pfam00268 81 RAFYGFQAFMENIHSESYSYILDTLGKDPEEIDELFNWIETNPALQKKAEWILKWYQDFDSDFLERLVAFAILEGIFFYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 240 SFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLV-------HKPSEQRVKEIITNSVRIEQEFLTEALPVK 312
Cdd:pfam00268 161 GFAAILWLKRRGKMPGLAEIIELISRDEGLHGDFACLLFQHLKeenpeleTKELKEEVYDLIKEAVELEKEFLDDALPVG 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 77416595 313 LIGMNCTLMKQYIEFVADRLMLELGFNKIFKVE-NP 347
Cdd:pfam00268 241 LLGMNAEDVKQYIEYVADRRLMNLGYEKLYNVEvNP 276
|
|
| RNRR2 |
cd01049 |
Ribonucleotide Reductase, R2/beta subunit, ferritin-like diiron-binding domain; Ribonucleotide ... |
81-356 |
7.61e-141 |
|
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: 402.39 E-value: 7.61e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 81 FVVFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWEALKPDERHFISHVLAFFAASDGIVNENLVERFSQEVQVTEAR 160
Cdd:cd01049 1 FNLNPIKYPWAWELYKKAEANFWTPEEIDLSKDLKDWEKLTEAERHFIKRVLAFLAALDSIVGENLVELFSRHVQIPEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 161 CFYGFQIAMENIHSEMYSLLIDTYIKDSkEREYLFNAIETMPCVKKKADWALRWIGD----KEATYGERVVAFAAVEGIF 236
Cdd:cd01049 81 AFYGFQAFMENIHSESYSYILDTLGKDE-ERDELFEAIETDPALKKKADWILRWYDNlddnTKESFAERLVAFAILEGIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 237 FSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHK-------PSEQRVKEIITNSVRIEQEFLTEAL 309
Cdd:cd01049 160 FYSGFAAIFWLARRGKMPGLAEIIELISRDESLHGDFACLLIRELLNEnpelfteEFKEEVYELIKEAVELEKEFARDLL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 77416595 310 PVKLIGMNCTLMKQYIEFVADRLMLELGFNKIFKV--ENPFDFMENISL 356
Cdd:cd01049 240 PDGILGLNKEDMKQYIEYVANRRLENLGLEKLFNVedKNPFDWMELISD 288
|
|
| NrdB |
COG0208 |
Ribonucleotide reductase beta subunit, ferritin-like domain [Nucleotide transport and ... |
69-377 |
3.37e-113 |
|
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: 333.29 E-value: 3.37e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 69 EEEPLLRENP-RRFVVFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWEALKPDERHFISHVLAFFAASDGIVNENLV 147
Cdd:COG0208 1 LDEPIINGLTtNRINWNPIKYPWAYELYKKQLANFWLPEEVPLSNDIKDWKKLSDDERHLIKRVLGFLTLLDSIQGNNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 148 ERFSQEVQVTEARCFYGFQIAMENIHSEMYSLLIDTYIKDskeREYLFNAIETMPCVKKKADWALRWIGDKEATYG---- 223
Cdd:COG0208 81 LALYPHVTAPEVRAVLSRQAFMEAIHAKSYSYILETLGLD---IDEIFNWIEENPALQKKAEFILKYYDDLGTRETkkdl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 224 -ERVVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFK-------HLVHKPSEQRVKEIIT 295
Cdd:COG0208 158 lKSLVASVFLEGIFFYSGFAYPLSLARRGKMKGTAEIIRLILRDESLHGNFGIYLINtireenpELFTEELKEEIYELLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 296 NSVRIEQEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFNKIFKV-ENPFDFMEN-ISLEGKTNFFEKRVGEYQRM 373
Cdd:COG0208 238 EAVELEKEYADDLFPDGILGLNAEDVKQYIRYIANKRLMNLGLEPLFEGdVNPFPWMSEgLDLNKKTDFFETRVTEYQKG 317
|
....
gi 77416595 374 GVMS 377
Cdd:COG0208 318 GVES 321
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02492 |
PLN02492 |
ribonucleoside-diphosphate reductase |
71-390 |
0e+00 |
|
ribonucleoside-diphosphate reductase
Pssm-ID: 215272 Cd Length: 324 Bit Score: 621.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 71 EPLLRENPRRFVVFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWEALKPDERHFISHVLAFFAASDGIVNENLVERF 150
Cdd:PLN02492 1 EPLLAENPDRFCMFPIKYPQIWEMYKKAEASFWTAEEVDLSADLKDWEKLTDDERHFISHVLAFFAASDGIVLENLAARF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 151 SQEVQVTEARCFYGFQIAMENIHSEMYSLLIDTYIKDSKEREYLFNAIETMPCVKKKADWALRWIgDKEATYGERVVAFA 230
Cdd:PLN02492 81 MKEVQVPEARAFYGFQIAIENIHSEMYSLLLDTYIKDPKEKDRLFNAIETIPCVAKKADWALRWI-DSSASFAERLVAFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 231 AVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEQRVKEIITNSVRIEQEFLTEALP 310
Cdd:PLN02492 160 CVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLKNKLSEERVKEIVCEAVEIEKEFVCDALP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 311 VKLIGMNCTLMKQYIEFVADRLMLELGFNKIFKVENPFDFMENISLEGKTNFFEKRVGEYQRMGVMSN-----STENSFT 385
Cdd:PLN02492 240 CALVGMNADLMSQYIEFVADRLLVALGYEKVYNVVNPFDWMELISLQGKTNFFEKRVGEYQKAGVMSSlngggADNHVFS 319
|
....*
gi 77416595 386 LDADF 390
Cdd:PLN02492 320 LDEDF 324
|
|
| PTZ00211 |
PTZ00211 |
ribonucleoside-diphosphate reductase small subunit; Provisional |
64-390 |
0e+00 |
|
ribonucleoside-diphosphate reductase small subunit; Provisional
Pssm-ID: 240315 [Multi-domain] Cd Length: 330 Bit Score: 597.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 64 TKPSIEEEPLLRENPRRFVVFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWEALKPDERHFISHVLAFFAASDGIVN 143
Cdd:PTZ00211 5 MKENEEEEPLLKENPDRFVLFPIKYPDIWRMYKKAEASFWTAEEIDLGNDLKDWEKLNDGERHFIKHVLAFFAASDGIVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 144 ENLVERFSQEVQVTEARCFYGFQIAMENIHSEMYSLLIDTYIKDSKEREYLFNAIETMPCVKKKADWALRWIGDkEATYG 223
Cdd:PTZ00211 85 ENLAQRFMREVQVPEARCFYGFQIAMENIHSETYSLLIDTYITDEEEKDRLFHAIETIPAIKKKAEWAAKWINS-SNSFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 224 ERVVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEQRVKEIITNSVRIEQE 303
Cdd:PTZ00211 164 ERLVAFAAVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHTDFACLLYSHLKNKLPRERVQEIIKEAVEIERE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 304 FLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFNKIFKVENPFDFMENISLEGKTNFFEKRVGEYQRMGVMSNSTENS 383
Cdd:PTZ00211 244 FICDALPVDLIGMNSRLMAQYIEFVADRLLVALGVPKIYNSKNPFDWMDMISLQGKTNFFEKRVGEYQKAGVMAERTSKV 323
|
....*..
gi 77416595 384 FTLDADF 390
Cdd:PTZ00211 324 FSLDADF 330
|
|
| Ribonuc_red_sm |
pfam00268 |
Ribonucleotide reductase, small chain; |
80-347 |
1.67e-155 |
|
Ribonucleotide reductase, small chain;
Pssm-ID: 425568 [Multi-domain] Cd Length: 276 Bit Score: 438.86 E-value: 1.67e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 80 RFVVFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWEALKPDERHFISHVLAFFAASDGIVNENLVERFSQEVQVTEA 159
Cdd:pfam00268 1 RFNLNPIKYPEIWEFYKKLEANFWTPEEIPLSKDIKDWKKLSEDEREFIKRVLAFLALLDTLVNENLVERFSREVQTPEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 160 RCFYGFQIAMENIHSEMYSLLIDTYIKDSKEREYLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSG 239
Cdd:pfam00268 81 RAFYGFQAFMENIHSESYSYILDTLGKDPEEIDELFNWIETNPALQKKAEWILKWYQDFDSDFLERLVAFAILEGIFFYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 240 SFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLV-------HKPSEQRVKEIITNSVRIEQEFLTEALPVK 312
Cdd:pfam00268 161 GFAAILWLKRRGKMPGLAEIIELISRDEGLHGDFACLLFQHLKeenpeleTKELKEEVYDLIKEAVELEKEFLDDALPVG 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 77416595 313 LIGMNCTLMKQYIEFVADRLMLELGFNKIFKVE-NP 347
Cdd:pfam00268 241 LLGMNAEDVKQYIEYVADRRLMNLGYEKLYNVEvNP 276
|
|
| RNRR2 |
cd01049 |
Ribonucleotide Reductase, R2/beta subunit, ferritin-like diiron-binding domain; Ribonucleotide ... |
81-356 |
7.61e-141 |
|
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: 402.39 E-value: 7.61e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 81 FVVFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWEALKPDERHFISHVLAFFAASDGIVNENLVERFSQEVQVTEAR 160
Cdd:cd01049 1 FNLNPIKYPWAWELYKKAEANFWTPEEIDLSKDLKDWEKLTEAERHFIKRVLAFLAALDSIVGENLVELFSRHVQIPEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 161 CFYGFQIAMENIHSEMYSLLIDTYIKDSkEREYLFNAIETMPCVKKKADWALRWIGD----KEATYGERVVAFAAVEGIF 236
Cdd:cd01049 81 AFYGFQAFMENIHSESYSYILDTLGKDE-ERDELFEAIETDPALKKKADWILRWYDNlddnTKESFAERLVAFAILEGIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 237 FSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHK-------PSEQRVKEIITNSVRIEQEFLTEAL 309
Cdd:cd01049 160 FYSGFAAIFWLARRGKMPGLAEIIELISRDESLHGDFACLLIRELLNEnpelfteEFKEEVYELIKEAVELEKEFARDLL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 77416595 310 PVKLIGMNCTLMKQYIEFVADRLMLELGFNKIFKV--ENPFDFMENISL 356
Cdd:cd01049 240 PDGILGLNKEDMKQYIEYVANRRLENLGLEKLFNVedKNPFDWMELISD 288
|
|
| NrdB |
COG0208 |
Ribonucleotide reductase beta subunit, ferritin-like domain [Nucleotide transport and ... |
69-377 |
3.37e-113 |
|
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: 333.29 E-value: 3.37e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 69 EEEPLLRENP-RRFVVFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWEALKPDERHFISHVLAFFAASDGIVNENLV 147
Cdd:COG0208 1 LDEPIINGLTtNRINWNPIKYPWAYELYKKQLANFWLPEEVPLSNDIKDWKKLSDDERHLIKRVLGFLTLLDSIQGNNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 148 ERFSQEVQVTEARCFYGFQIAMENIHSEMYSLLIDTYIKDskeREYLFNAIETMPCVKKKADWALRWIGDKEATYG---- 223
Cdd:COG0208 81 LALYPHVTAPEVRAVLSRQAFMEAIHAKSYSYILETLGLD---IDEIFNWIEENPALQKKAEFILKYYDDLGTRETkkdl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 224 -ERVVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFK-------HLVHKPSEQRVKEIIT 295
Cdd:COG0208 158 lKSLVASVFLEGIFFYSGFAYPLSLARRGKMKGTAEIIRLILRDESLHGNFGIYLINtireenpELFTEELKEEIYELLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 296 NSVRIEQEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFNKIFKV-ENPFDFMEN-ISLEGKTNFFEKRVGEYQRM 373
Cdd:COG0208 238 EAVELEKEYADDLFPDGILGLNAEDVKQYIRYIANKRLMNLGLEPLFEGdVNPFPWMSEgLDLNKKTDFFETRVTEYQKG 317
|
....
gi 77416595 374 GVMS 377
Cdd:COG0208 318 GVES 321
|
|
| PRK07209 |
PRK07209 |
ribonucleotide-diphosphate reductase subunit beta; Validated |
85-377 |
8.78e-48 |
|
ribonucleotide-diphosphate reductase subunit beta; Validated
Pssm-ID: 235968 Cd Length: 369 Bit Score: 166.32 E-value: 8.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 85 PIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWE---ALKPDERHFISHVLAFFAASDGIVNENLVERFSQEVQVTEARC 161
Cdd:PRK07209 53 PFKYKWAWEKYLAGCANHWMPQEVNMSRDIALWKspnGLTEDERRIVKRNLGFFSTADSLVANNIVLAIYRHITNPECRQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 162 FYGFQIAMENIHSEMYSllidtYIKDS---KEREyLFNAIETMPCVKKKADWAL---RWIGDKEATYG---------ERV 226
Cdd:PRK07209 133 YLLRQAFEEAIHTHAYQ-----YIVESlglDEGE-IFNMYHEVPSIRAKDEFLIpftRSLTDPNFKTGtpendqkllRNL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 227 VAFAAV-EGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFK-------HLVHKPSEQRVKEIITNSV 298
Cdd:PRK07209 207 IAFYCImEGIFFYVGFTQILSLGRQNKMTGIAEQYQYILRDESMHLNFGIDLINqiklenpHLWTAEFQAEIRELIKEAV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 299 RIEQEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFNKIFK-VENPFDFM-ENISLEGKTNFFEKRVGEYQRMGVM 376
Cdd:PRK07209 287 ELEYRYARDTMPRGVLGLNASMFKDYLRFIANRRLQQIGLKPQYPgTENPFPWMsEMIDLKKEKNFFETRVIEYQTGGAL 366
|
.
gi 77416595 377 S 377
Cdd:PRK07209 367 S 367
|
|
| nrdF |
PRK09614 |
ribonucleotide-diphosphate reductase subunit beta; Reviewed |
85-390 |
4.86e-43 |
|
ribonucleotide-diphosphate reductase subunit beta; Reviewed
Pssm-ID: 236591 [Multi-domain] Cd Length: 324 Bit Score: 152.67 E-value: 4.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 85 PIEY---HDIWqmyKKAEASFWTAEEVDLSKDIQHWEALKPDERHFISHVLAFFAASDGIVNENLVERFSQEVQVTEARC 161
Cdd:PRK09614 16 KIEDpwdYEAW---KRLTANFWLPEEVPLSNDLKDWKKLSDEEKNLYTRVFGGLTLLDTLQNNNGMPNLMPDITTPEEEA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 162 FYGFQIAMENIHSEMYSLLIDTyIKDSKEREYLFNAIETMPCVKKKADWALRWIGD-KEATYGERVVAFAAVEGIFFSGS 240
Cdd:PRK09614 93 VLANIAFMEAVHAKSYSYIFST-LCSPEEIDEAFEWAEENPYLQKKADIIQDFYEPlKKKILRKAAVASVFLEGFLFYSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 241 FASIFWLKKRGLMPGltfSNELIS---RDEGLHCDFACLMFKHLVHKPSE-------QRVKEIITNSVRIEQEFLTEALP 310
Cdd:PRK09614 172 FYYPLYLARQGKMTG---TAQIIRliiRDESLHGYYIGYLFQEGLEELPEleqeelkDEIYDLLYELYENEEAYTELLYD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 311 VklIGmNCTLMKQYIEFVADRLMLELGFNKIF--KVENPFDFMENISLEG--KTNFFEKRVGEYQRMgvmsnSTENSFtl 386
Cdd:PRK09614 249 I--VG-LAEDVKKYIRYNANKRLMNLGLEPLFpeEEEVNPIWLNGLSNNAdeNHDFFEGKGTSYVKG-----ATEATE-- 318
|
....
gi 77416595 387 DADF 390
Cdd:PRK09614 319 DDDW 322
|
|
| PRK12759 |
PRK12759 |
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional |
85-381 |
1.78e-25 |
|
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional
Pssm-ID: 139206 [Multi-domain] Cd Length: 410 Bit Score: 106.65 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 85 PIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWE--ALKPDERHFISHVLAFFAASDGIVNENLVERFSQEVQVTEARCF 162
Cdd:PRK12759 102 PFNYPWAVDLTVKHEKAHWIEDEIDLSEDVTDWKngKITKVEKEYITNILRLFTQSDVAVGQNYYDQFIPLFKNNEIRNM 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 163 YGFQIAMENIHSEMYSLLIDTY-IKDSKereylFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSF 241
Cdd:PRK12759 182 LGSFAAREGIHQRAYALLNDTLgLPDSE-----YHAFLEYKAMTDKIDFMMDADPTTRRGLGLCLAKTVFNEGVALFASF 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 242 ASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFK-------HLVHKPSEQRVKEIITNSVRIEQEFLTEALPVKLI 314
Cdd:PRK12759 257 AMLLNFQRFGKMKGMGKVVEWSIRDESMHVEGNAALFRiycqenpYIVDNEFKKEIYLMASKAVELEDRFIELAYELGTI 336
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 77416595 315 -GMNCTLMKQYIEFVADRLMLELGFNKIFKVE-NPFDFMENIsLEG--KTNFFEKRVGEYQRMGVMSNSTE 381
Cdd:PRK12759 337 eGLKADEVKQYIRHITDRRLNQLGLKEIYNIEkNPLTWLEWI-LNGadHTNFFENRVTEYEVAGLTGSWDE 406
|
|
| nrdF2 |
PRK13966 |
ribonucleotide-diphosphate reductase subunit beta; Provisional |
93-342 |
7.87e-09 |
|
ribonucleotide-diphosphate reductase subunit beta; Provisional
Pssm-ID: 140022 Cd Length: 324 Bit Score: 56.65 E-value: 7.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 93 QMYKKAEASFWTAEEVDLSKDIQHWEALKPDERHFISHVLAFFAASDGIVNE-NLVERFSQEVQVTEARCFYGFQIaMEN 171
Cdd:PRK13966 26 EVWDRLTGNFWLPEKVPVSNDIPSWGTLTAGEKQLTMRVFTGLTMLDTIQGTvGAVSLIPDALTPHEEAVLTNIAF-MES 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 172 IHSEMYSLLIDTyIKDSKEREYLFNAIETMPCVKKKADWALRWIGDKEATygERVVAFAAVEG-IFFSGSFASIFWlKKR 250
Cdd:PRK13966 105 VHAKSYSQIFST-LCSTAEIDDAFRWSEENRNLQRKAEIVLQYYRGDEPL--KRKVASTLLESfLFYSGFYLPMYW-SSR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 251 GLMPGLTFSNELISRDEGLHCDFACLMFKH---LVHKPSEQRVK--------EIITNSVRIEQEFLTEalpvklIGMNcT 319
Cdd:PRK13966 181 AKLTNTADMIRLIIRDEAVHGYYIGYKFQRglaLVDDVTRAELKdytyellfELYDNEVEYTQDLYDE------VGLT-E 253
|
250 260
....*....|....*....|...
gi 77416595 320 LMKQYIEFVADRLMLELGFNKIF 342
Cdd:PRK13966 254 DVKKFLRYNANKALMNLGYEALF 276
|
|
| PRK08326 |
PRK08326 |
R2-like ligand-binding oxidase; |
94-282 |
2.94e-08 |
|
R2-like ligand-binding oxidase;
Pssm-ID: 236242 Cd Length: 311 Bit Score: 54.62 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 94 MYKKAEASFWTAEEVDLSKDIQHWEALKPDERHFISHVLAFFAASDGIVNENLVE---------RFSQEVQVT-----EA 159
Cdd:PRK08326 30 LFAKGNAKFWNPADIDFSRDAEDWEKLSDEERDYATRLCAQFIAGEEAVTLDIQPlisamaaegRLEDEMYLTqfafeEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 160 RcfygfqiameniHSEMYSLLIDT---------YIKDSKEREYLFnaIETMPcvkkKADWALRwIGDKEATYGERVVAF- 229
Cdd:PRK08326 110 K------------HTEAFRRWFDAvgvtedlsvYTDDNPSYRQIF--YEELP----AALNRLS-TDPSPENQVRASVTYn 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 77416595 230 AAVEGIF-FSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLV 282
Cdd:PRK08326 171 HVVEGVLaETGYYAWRKICVTRGILPGLQELVRRIGDDERRHIAWGTYTCRRLV 224
|
|
| PRK13965 |
PRK13965 |
ribonucleotide-diphosphate reductase subunit beta; Provisional |
90-345 |
3.78e-08 |
|
ribonucleotide-diphosphate reductase subunit beta; Provisional
Pssm-ID: 184425 [Multi-domain] Cd Length: 335 Bit Score: 54.39 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 90 DIWQmykKAEASFWTAEEVDLSKDIQHWEALKPDERHFISHVLAFFAASDGIvnENLVERFSQ--EVQVTEARCFYGFQI 167
Cdd:PRK13965 37 EVWN---RVTQNFWLPEKVPVSNDLNSWRSLGEDWQQLITRTFTGLTLLDTV--QATVGDVAQipHSQTDHEQVIYTNFA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 168 AMENIHSEMYSLLIDTyIKDSKEREYLFNAIETMPCVKKKADWALR-WIGDKEAtygERVVAFAAVEGIFFSGSFASIFW 246
Cdd:PRK13965 112 FMVAIHARSYGTIFST-LCSSEQIEEAHEWVVSTESLQRRARVLIPyYTGDDPL---KSKVAAAMMPGFLLYGGFYLPFY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 247 LKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEQRVKEIITNSVRIEQEFL-TEALPVKLIGMNCTLMKQYI 325
Cdd:PRK13965 188 LSARGKLPNTSDIIRLILRDKVIHNYYSGYKYQQKVARLSPEKQAEMKAFVFDLLYELIdLEKAYLRELYAGFDLAEDAI 267
|
250 260
....*....|....*....|...
gi 77416595 326 EFV---ADRLMLELGFNKIFKVE 345
Cdd:PRK13965 268 RFSlynAGKFLQNLGYESPFTEE 290
|
|
| nrdB |
PRK09101 |
ribonucleotide-diphosphate reductase subunit beta; Reviewed |
102-353 |
1.04e-07 |
|
ribonucleotide-diphosphate reductase subunit beta; Reviewed
Pssm-ID: 181647 Cd Length: 376 Bit Score: 53.43 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 102 FWTAEEVDLSKDIQHWEALKPDERH-FISHvLAFFAASDGI----VN------------ENLVERFSqevqvtearcfyg 164
Cdd:PRK09101 48 FWRPEEVDVSRDRIDYQALPEHEKHiFISN-LKYQTLLDSIqgrsPNvallplvsipelETWIETWS------------- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 165 FQiamENIHSEMYSLLIDTYIKDSKEreyLFNAIETMPCVKKKA---------------DWALRWIGD-----KEATYGE 224
Cdd:PRK09101 114 FS---ETIHSRSYTHIIRNIVNDPSV---VFDDIVTNEEILKRAkdissyyddliemtsYYHLLGEGThtvngKTVTVSL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 225 R---------VVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEQRVKEIit 295
Cdd:PRK09101 188 RelkkklylcLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLMRSGKDDPEMAEI-- 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 77416595 296 nSVRIEQE----FLTEALPVK-----------LIGMNCTLMKQYIEFVADRLMLELGFNKIFKVE-NPFDFMEN 353
Cdd:PRK09101 266 -AEECKQEcydlFVQAAEQEKewadylfkdgsMIGLNKDILCQYVEYITNIRMQAVGLDLPFQTRsNPIPWINA 338
|
|
| RNRR2_Rv0233_like |
cd07911 |
Ribonucleotide Reductase R2-like protein, Mn/Fe-binding domain; Rv0233 is a Mycobacterium ... |
93-337 |
2.16e-07 |
|
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: 51.96 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 93 QMYKKAEA-SFWTAEEVDLSKDIQHWEALKPDERHFISHVLAFFAASDGIVNENLVE---------RFSQEVQVT----- 157
Cdd:cd07911 11 KLFEKGKRkGFWNPADIDFSQDREDWEQLSEEERDLALRLCAGFIAGEEAVTLDLLPlmmamaaegRLEEEMYLTqflfe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 158 EARcfygfqiameniHSEMYSLLID---------TYIKDSKER---EYLFNAIEtmpcvKKKADWALRWIGDKEATYGER 225
Cdd:cd07911 91 EAK------------HTDFFRRWLDavgvsddlsDLHTAVYREpfyEALPYAEL-----RLYLDASPAAQVRASVTYNMI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 226 VVAFAAVEGIFfsgSFASIfwLKKRGLMPGLTFSNELISRDEGLHCDFAC-LMFKHLVHKPS-----EQRVKEIITNSVR 299
Cdd:cd07911 154 VEGVLAETGYY---AWRTI--CEKRGILPGMQEGIRRLGDDESRHIAWGTfTCRRLVAADDAnwdvfEERMNELVPHALG 228
|
250 260 270
....*....|....*....|....*....|....*...
gi 77416595 300 IEQEfLTEALPVKLIGMNCTLMKQYiefVADRLMLELG 337
Cdd:cd07911 229 LIDE-IFELYDEMPFGLDPDELMQY---AVDQFQRRLG 262
|
|
| nrdF1 |
PRK13967 |
ribonucleotide-diphosphate reductase subunit beta; Provisional |
93-270 |
2.84e-06 |
|
ribonucleotide-diphosphate reductase subunit beta; Provisional
Pssm-ID: 140023 Cd Length: 322 Bit Score: 48.57 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 93 QMYKKAEASFWTAEEVDLSKDIQHWEALKPDERHFISHVLAFFAASD-GIVNENLVERFSQEVQVTEARCFYGFQIaMEN 171
Cdd:PRK13967 24 QVWERLTGNFWLPEKIPLSNDLASWQTLSSTEQQTTIRVFTGLTLLDtAQATVGAVAMIDDAVTPHEEAVLTNMAF-MES 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416595 172 IHSEMYSLLIDTyIKDSKEREYLFNAIETMPCVKKKADWALRWIGDKEATygERVVAFAAVEG-IFFSGSFASIFWlKKR 250
Cdd:PRK13967 103 VHAKSYSSIFST-LCSTKQIDDAFDWSEQNPYLQRKAQIIVDYYRGDDAL--KRKASSVMLESfLFYSGFYLPMYW-SSR 178
|
170 180
....*....|....*....|
gi 77416595 251 GLMPGLTFSNELISRDEGLH 270
Cdd:PRK13967 179 GKLTNTADLIRLIIRDEAVH 198
|
|
|