|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02492 |
PLN02492 |
ribonucleoside-diphosphate reductase |
70-389 |
0e+00 |
|
ribonucleoside-diphosphate reductase
Pssm-ID: 215272 Cd Length: 324 Bit Score: 620.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 70 EPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVERF 149
Cdd:PLN02492 1 EPLLAENPDRFCMFPIKYPQIWEMYKKAEASFWTAEEVDLSADLKDWEKLTDDERHFISHVLAFFAASDGIVLENLAARF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 150 SQEVQITEARCFYGFQIAMENIHSEMYSLLIDTYIKDPKEREFLFNAIETMPCVKKKADWALRWIgDKEATYGERVVAFA 229
Cdd:PLN02492 81 MKEVQVPEARAFYGFQIAIENIHSEMYSLLLDTYIKDPKEKDRLFNAIETIPCVAKKADWALRWI-DSSASFAERLVAFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 230 AVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIEQEFLTEALP 309
Cdd:PLN02492 160 CVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLKNKLSEERVKEIVCEAVEIEKEFVCDALP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 310 VKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFMENISLEGKTNFFEKRVGEYQRMGVMSS-----PTENSFT 384
Cdd:PLN02492 240 CALVGMNADLMSQYIEFVADRLLVALGYEKVYNVVNPFDWMELISLQGKTNFFEKRVGEYQKAGVMSSlngggADNHVFS 319
|
....*
gi 4557845 385 LDADF 389
Cdd:PLN02492 320 LDEDF 324
|
|
| Ribonuc_red_sm |
pfam00268 |
Ribonucleotide reductase, small chain; |
79-346 |
3.58e-157 |
|
Ribonucleotide reductase, small chain;
Pssm-ID: 425568 [Multi-domain] Cd Length: 276 Bit Score: 443.09 E-value: 3.58e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 79 RFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEA 158
Cdd:pfam00268 1 RFNLNPIKYPEIWEFYKKLEANFWTPEEIPLSKDIKDWKKLSEDEREFIKRVLAFLALLDTLVNENLVERFSREVQTPEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 159 RCFYGFQIAMENIHSEMYSLLIDTYIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSG 238
Cdd:pfam00268 81 RAFYGFQAFMENIHSESYSYILDTLGKDPEEIDELFNWIETNPALQKKAEWILKWYQDFDSDFLERLVAFAILEGIFFYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 239 SFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLV-------HKPSEERVREIIINAVRIEQEFLTEALPVK 311
Cdd:pfam00268 161 GFAAILWLKRRGKMPGLAEIIELISRDEGLHGDFACLLFQHLKeenpeleTKELKEEVYDLIKEAVELEKEFLDDALPVG 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 4557845 312 LIGMNCTLMKQYIEFVADRLMLELGFSKVFRVE-NP 346
Cdd:pfam00268 241 LLGMNAEDVKQYIEYVADRRLMNLGYEKLYNVEvNP 276
|
|
| RNRR2 |
cd01049 |
Ribonucleotide Reductase, R2/beta subunit, ferritin-like diiron-binding domain; Ribonucleotide ... |
80-355 |
4.70e-144 |
|
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: 410.48 E-value: 4.70e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 80 FVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEAR 159
Cdd:cd01049 1 FNLNPIKYPWAWELYKKAEANFWTPEEIDLSKDLKDWEKLTEAERHFIKRVLAFLAALDSIVGENLVELFSRHVQIPEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 160 CFYGFQIAMENIHSEMYSLLIDTYIKDPkEREFLFNAIETMPCVKKKADWALRWIGD----KEATYGERVVAFAAVEGIF 235
Cdd:cd01049 81 AFYGFQAFMENIHSESYSYILDTLGKDE-ERDELFEAIETDPALKKKADWILRWYDNlddnTKESFAERLVAFAILEGIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 236 FSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHK-------PSEERVREIIINAVRIEQEFLTEAL 308
Cdd:cd01049 160 FYSGFAAIFWLARRGKMPGLAEIIELISRDESLHGDFACLLIRELLNEnpelfteEFKEEVYELIKEAVELEKEFARDLL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 4557845 309 PVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRV--ENPFDFMENISL 355
Cdd:cd01049 240 PDGILGLNKEDMKQYIEYVANRRLENLGLEKLFNVedKNPFDWMELISD 288
|
|
| NrdB |
COG0208 |
Ribonucleotide reductase beta subunit, ferritin-like domain [Nucleotide transport and ... |
68-377 |
1.64e-115 |
|
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: 339.45 E-value: 1.64e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 68 EDEPLLRENP-RRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLV 146
Cdd:COG0208 1 LDEPIINGLTtNRINWNPIKYPWAYELYKKQLANFWLPEEVPLSNDIKDWKKLSDDERHLIKRVLGFLTLLDSIQGNNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 147 ERFSQEVQITEARCFYGFQIAMENIHSEMYSLLIDTYIKDPKErefLFNAIETMPCVKKKADWALRWIGDKEATYG---- 222
Cdd:COG0208 81 LALYPHVTAPEVRAVLSRQAFMEAIHAKSYSYILETLGLDIDE---IFNWIEENPALQKKAEFILKYYDDLGTRETkkdl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 223 -ERVVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFK-------HLVHKPSEERVREIII 294
Cdd:COG0208 158 lKSLVASVFLEGIFFYSGFAYPLSLARRGKMKGTAEIIRLILRDESLHGNFGIYLINtireenpELFTEELKEEIYELLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 295 NAVRIEQEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRV-ENPFDFMEN-ISLEGKTNFFEKRVGEYQRM 372
Cdd:COG0208 238 EAVELEKEYADDLFPDGILGLNAEDVKQYIRYIANKRLMNLGLEPLFEGdVNPFPWMSEgLDLNKKTDFFETRVTEYQKG 317
|
....*
gi 4557845 373 GVMSS 377
Cdd:COG0208 318 GVEST 322
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02492 |
PLN02492 |
ribonucleoside-diphosphate reductase |
70-389 |
0e+00 |
|
ribonucleoside-diphosphate reductase
Pssm-ID: 215272 Cd Length: 324 Bit Score: 620.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 70 EPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVERF 149
Cdd:PLN02492 1 EPLLAENPDRFCMFPIKYPQIWEMYKKAEASFWTAEEVDLSADLKDWEKLTDDERHFISHVLAFFAASDGIVLENLAARF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 150 SQEVQITEARCFYGFQIAMENIHSEMYSLLIDTYIKDPKEREFLFNAIETMPCVKKKADWALRWIgDKEATYGERVVAFA 229
Cdd:PLN02492 81 MKEVQVPEARAFYGFQIAIENIHSEMYSLLLDTYIKDPKEKDRLFNAIETIPCVAKKADWALRWI-DSSASFAERLVAFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 230 AVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIEQEFLTEALP 309
Cdd:PLN02492 160 CVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLKNKLSEERVKEIVCEAVEIEKEFVCDALP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 310 VKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFMENISLEGKTNFFEKRVGEYQRMGVMSS-----PTENSFT 384
Cdd:PLN02492 240 CALVGMNADLMSQYIEFVADRLLVALGYEKVYNVVNPFDWMELISLQGKTNFFEKRVGEYQKAGVMSSlngggADNHVFS 319
|
....*
gi 4557845 385 LDADF 389
Cdd:PLN02492 320 LDEDF 324
|
|
| PTZ00211 |
PTZ00211 |
ribonucleoside-diphosphate reductase small subunit; Provisional |
68-389 |
0e+00 |
|
ribonucleoside-diphosphate reductase small subunit; Provisional
Pssm-ID: 240315 [Multi-domain] Cd Length: 330 Bit Score: 596.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 68 EDEPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVE 147
Cdd:PTZ00211 10 EEEPLLKENPDRFVLFPIKYPDIWRMYKKAEASFWTAEEIDLGNDLKDWEKLNDGERHFIKHVLAFFAASDGIVLENLAQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 148 RFSQEVQITEARCFYGFQIAMENIHSEMYSLLIDTYIKDPKEREFLFNAIETMPCVKKKADWALRWIGDkEATYGERVVA 227
Cdd:PTZ00211 90 RFMREVQVPEARCFYGFQIAMENIHSETYSLLIDTYITDEEEKDRLFHAIETIPAIKKKAEWAAKWINS-SNSFAERLVA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 228 FAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIEQEFLTEA 307
Cdd:PTZ00211 169 FAAVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHTDFACLLYSHLKNKLPRERVQEIIKEAVEIEREFICDA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 308 LPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFMENISLEGKTNFFEKRVGEYQRMGVMSSPTENSFTLDA 387
Cdd:PTZ00211 249 LPVDLIGMNSRLMAQYIEFVADRLLVALGVPKIYNSKNPFDWMDMISLQGKTNFFEKRVGEYQKAGVMAERTSKVFSLDA 328
|
..
gi 4557845 388 DF 389
Cdd:PTZ00211 329 DF 330
|
|
| Ribonuc_red_sm |
pfam00268 |
Ribonucleotide reductase, small chain; |
79-346 |
3.58e-157 |
|
Ribonucleotide reductase, small chain;
Pssm-ID: 425568 [Multi-domain] Cd Length: 276 Bit Score: 443.09 E-value: 3.58e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 79 RFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEA 158
Cdd:pfam00268 1 RFNLNPIKYPEIWEFYKKLEANFWTPEEIPLSKDIKDWKKLSEDEREFIKRVLAFLALLDTLVNENLVERFSREVQTPEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 159 RCFYGFQIAMENIHSEMYSLLIDTYIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSG 238
Cdd:pfam00268 81 RAFYGFQAFMENIHSESYSYILDTLGKDPEEIDELFNWIETNPALQKKAEWILKWYQDFDSDFLERLVAFAILEGIFFYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 239 SFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLV-------HKPSEERVREIIINAVRIEQEFLTEALPVK 311
Cdd:pfam00268 161 GFAAILWLKRRGKMPGLAEIIELISRDEGLHGDFACLLFQHLKeenpeleTKELKEEVYDLIKEAVELEKEFLDDALPVG 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 4557845 312 LIGMNCTLMKQYIEFVADRLMLELGFSKVFRVE-NP 346
Cdd:pfam00268 241 LLGMNAEDVKQYIEYVADRRLMNLGYEKLYNVEvNP 276
|
|
| RNRR2 |
cd01049 |
Ribonucleotide Reductase, R2/beta subunit, ferritin-like diiron-binding domain; Ribonucleotide ... |
80-355 |
4.70e-144 |
|
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: 410.48 E-value: 4.70e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 80 FVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEAR 159
Cdd:cd01049 1 FNLNPIKYPWAWELYKKAEANFWTPEEIDLSKDLKDWEKLTEAERHFIKRVLAFLAALDSIVGENLVELFSRHVQIPEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 160 CFYGFQIAMENIHSEMYSLLIDTYIKDPkEREFLFNAIETMPCVKKKADWALRWIGD----KEATYGERVVAFAAVEGIF 235
Cdd:cd01049 81 AFYGFQAFMENIHSESYSYILDTLGKDE-ERDELFEAIETDPALKKKADWILRWYDNlddnTKESFAERLVAFAILEGIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 236 FSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHK-------PSEERVREIIINAVRIEQEFLTEAL 308
Cdd:cd01049 160 FYSGFAAIFWLARRGKMPGLAEIIELISRDESLHGDFACLLIRELLNEnpelfteEFKEEVYELIKEAVELEKEFARDLL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 4557845 309 PVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRV--ENPFDFMENISL 355
Cdd:cd01049 240 PDGILGLNKEDMKQYIEYVANRRLENLGLEKLFNVedKNPFDWMELISD 288
|
|
| NrdB |
COG0208 |
Ribonucleotide reductase beta subunit, ferritin-like domain [Nucleotide transport and ... |
68-377 |
1.64e-115 |
|
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: 339.45 E-value: 1.64e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 68 EDEPLLRENP-RRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLV 146
Cdd:COG0208 1 LDEPIINGLTtNRINWNPIKYPWAYELYKKQLANFWLPEEVPLSNDIKDWKKLSDDERHLIKRVLGFLTLLDSIQGNNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 147 ERFSQEVQITEARCFYGFQIAMENIHSEMYSLLIDTYIKDPKErefLFNAIETMPCVKKKADWALRWIGDKEATYG---- 222
Cdd:COG0208 81 LALYPHVTAPEVRAVLSRQAFMEAIHAKSYSYILETLGLDIDE---IFNWIEENPALQKKAEFILKYYDDLGTRETkkdl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 223 -ERVVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFK-------HLVHKPSEERVREIII 294
Cdd:COG0208 158 lKSLVASVFLEGIFFYSGFAYPLSLARRGKMKGTAEIIRLILRDESLHGNFGIYLINtireenpELFTEELKEEIYELLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 295 NAVRIEQEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRV-ENPFDFMEN-ISLEGKTNFFEKRVGEYQRM 372
Cdd:COG0208 238 EAVELEKEYADDLFPDGILGLNAEDVKQYIRYIANKRLMNLGLEPLFEGdVNPFPWMSEgLDLNKKTDFFETRVTEYQKG 317
|
....*
gi 4557845 373 GVMSS 377
Cdd:COG0208 318 GVEST 322
|
|
| PRK07209 |
PRK07209 |
ribonucleotide-diphosphate reductase subunit beta; Validated |
82-376 |
2.84e-48 |
|
ribonucleotide-diphosphate reductase subunit beta; Validated
Pssm-ID: 235968 Cd Length: 369 Bit Score: 167.48 E-value: 2.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 82 IFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWES---LKPEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEA 158
Cdd:PRK07209 51 LVPFKYKWAWEKYLAGCANHWMPQEVNMSRDIALWKSpngLTEDERRIVKRNLGFFSTADSLVANNIVLAIYRHITNPEC 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 159 RCFYGFQIAMENIHSEMYSLLIDTYIKDPKErefLFNAIETMPCVKKKADWAL---RWIGDKEATYG---------ERVV 226
Cdd:PRK07209 131 RQYLLRQAFEEAIHTHAYQYIVESLGLDEGE---IFNMYHEVPSIRAKDEFLIpftRSLTDPNFKTGtpendqkllRNLI 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 227 AFAAV-EGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFK-------HLVHKPSEERVREIIINAVR 298
Cdd:PRK07209 208 AFYCImEGIFFYVGFTQILSLGRQNKMTGIAEQYQYILRDESMHLNFGIDLINqiklenpHLWTAEFQAEIRELIKEAVE 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 299 IEQEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFR-VENPFDFM-ENISLEGKTNFFEKRVGEYQRMGVMS 376
Cdd:PRK07209 288 LEYRYARDTMPRGVLGLNASMFKDYLRFIANRRLQQIGLKPQYPgTENPFPWMsEMIDLKKEKNFFETRVIEYQTGGALS 367
|
|
| nrdF |
PRK09614 |
ribonucleotide-diphosphate reductase subunit beta; Reviewed |
84-372 |
2.06e-42 |
|
ribonucleotide-diphosphate reductase subunit beta; Reviewed
Pssm-ID: 236591 [Multi-domain] Cd Length: 324 Bit Score: 150.75 E-value: 2.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 84 PIEY---HDIWqmyKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEARC 160
Cdd:PRK09614 16 KIEDpwdYEAW---KRLTANFWLPEEVPLSNDLKDWKKLSDEEKNLYTRVFGGLTLLDTLQNNNGMPNLMPDITTPEEEA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 161 FYGFQIAMENIHSEMYSLLIDTyIKDPKEREFLFNAIETMPCVKKKADWALRWIGD-KEATYGERVVAFAAVEGIFFSGS 239
Cdd:PRK09614 93 VLANIAFMEAVHAKSYSYIFST-LCSPEEIDEAFEWAEENPYLQKKADIIQDFYEPlKKKILRKAAVASVFLEGFLFYSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 240 FASIFWLKKRGLMPGltfSNELIS---RDEGLHCDFACLMFKHLVHKPSE-------ERVREIIINAVRIEQEFLTEALP 309
Cdd:PRK09614 172 FYYPLYLARQGKMTG---TAQIIRliiRDESLHGYYIGYLFQEGLEELPEleqeelkDEIYDLLYELYENEEAYTELLYD 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4557845 310 VklIGmNCTLMKQYIEFVADRLMLELGFSKVF--RVENPFDFMENISLEG--KTNFFEKRVGEYQRM 372
Cdd:PRK09614 249 I--VG-LAEDVKKYIRYNANKRLMNLGLEPLFpeEEEVNPIWLNGLSNNAdeNHDFFEGKGTSYVKG 312
|
|
| PRK12759 |
PRK12759 |
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional |
84-380 |
3.57e-24 |
|
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional
Pssm-ID: 139206 [Multi-domain] Cd Length: 410 Bit Score: 102.80 E-value: 3.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 84 PIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLK--PEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEARCF 161
Cdd:PRK12759 102 PFNYPWAVDLTVKHEKAHWIEDEIDLSEDVTDWKNGKitKVEKEYITNILRLFTQSDVAVGQNYYDQFIPLFKNNEIRNM 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 162 YGFQIAMENIHSEMYSLLIDTY-IKDPKEREFLfnaieTMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSF 240
Cdd:PRK12759 182 LGSFAAREGIHQRAYALLNDTLgLPDSEYHAFL-----EYKAMTDKIDFMMDADPTTRRGLGLCLAKTVFNEGVALFASF 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 241 ASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFK-------HLVHKPSEERVREIIINAVRIEQEFLTEALPVKLI 313
Cdd:PRK12759 257 AMLLNFQRFGKMKGMGKVVEWSIRDESMHVEGNAALFRiycqenpYIVDNEFKKEIYLMASKAVELEDRFIELAYELGTI 336
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4557845 314 -GMNCTLMKQYIEFVADRLMLELGFSKVFRVE-NPFDFMENIsLEG--KTNFFEKRVGEYQRMGVMSSPTE 380
Cdd:PRK12759 337 eGLKADEVKQYIRHITDRRLNQLGLKEIYNIEkNPLTWLEWI-LNGadHTNFFENRVTEYEVAGLTGSWDE 406
|
|
| RNRR2_Rv0233_like |
cd07911 |
Ribonucleotide Reductase R2-like protein, Mn/Fe-binding domain; Rv0233 is a Mycobacterium ... |
92-336 |
2.70e-09 |
|
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: 57.74 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 92 QMYKKAEA-SFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVE---------RFSQEVQIT----- 156
Cdd:cd07911 11 KLFEKGKRkGFWNPADIDFSQDREDWEQLSEEERDLALRLCAGFIAGEEAVTLDLLPlmmamaaegRLEEEMYLTqflfe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 157 EARcfygfqiameniHSEMYSLLID---------TYIKDPKEREF---LFNAIEtmpcvKKKADWALRWIGDKEATYGER 224
Cdd:cd07911 91 EAK------------HTDFFRRWLDavgvsddlsDLHTAVYREPFyeaLPYAEL-----RLYLDASPAAQVRASVTYNMI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 225 VVAFAAVEGIFfsgSFASIfwLKKRGLMPGLTFSNELISRDEGLHCDFAC-LMFKHLVHKPS-----EERVREIIINAVR 298
Cdd:cd07911 154 VEGVLAETGYY---AWRTI--CEKRGILPGMQEGIRRLGDDESRHIAWGTfTCRRLVAADDAnwdvfEERMNELVPHALG 228
|
250 260 270
....*....|....*....|....*....|....*...
gi 4557845 299 IEQEfLTEALPVKLIGMNCTLMKQYiefVADRLMLELG 336
Cdd:cd07911 229 LIDE-IFELYDEMPFGLDPDELMQY---AVDQFQRRLG 262
|
|
| PRK08326 |
PRK08326 |
R2-like ligand-binding oxidase; |
93-336 |
3.16e-09 |
|
R2-like ligand-binding oxidase;
Pssm-ID: 236242 Cd Length: 311 Bit Score: 57.70 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 93 MYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVE---------RFSQEVQIT-----EA 158
Cdd:PRK08326 30 LFAKGNAKFWNPADIDFSRDAEDWEKLSDEERDYATRLCAQFIAGEEAVTLDIQPlisamaaegRLEDEMYLTqfafeEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 159 RcfygfqiameniHSEMYSLLIDT---------YIKD-PKEREFLFnaiETMPcvkkKADWALRwIGDKEATYGERVVAF 228
Cdd:PRK08326 110 K------------HTEAFRRWFDAvgvtedlsvYTDDnPSYRQIFY---EELP----AALNRLS-TDPSPENQVRASVTY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 229 -AAVEGIF-FSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLV------HKPSEERVREIIINAVR-I 299
Cdd:PRK08326 170 nHVVEGVLaETGYYAWRKICVTRGILPGLQELVRRIGDDERRHIAWGTYTCRRLVaaddsnWDVFEERMNELLPLALGlI 249
|
250 260 270
....*....|....*....|....*....|....*..
gi 4557845 300 EQEFLTEALPVKLIGMNCTLMkqyiEFVADRLMLELG 336
Cdd:PRK08326 250 DEIFALYGDQIPFELSNDEFV----DYAADRGQRRLG 282
|
|
| nrdB |
PRK09101 |
ribonucleotide-diphosphate reductase subunit beta; Reviewed |
101-352 |
1.44e-08 |
|
ribonucleotide-diphosphate reductase subunit beta; Reviewed
Pssm-ID: 181647 Cd Length: 376 Bit Score: 56.12 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 101 FWTAEEVDLSKDIQHWESLKPEERY-FISHvLAFFAASDGI----VN------------ENLVERFSqevqitearcfyg 163
Cdd:PRK09101 48 FWRPEEVDVSRDRIDYQALPEHEKHiFISN-LKYQTLLDSIqgrsPNvallplvsipelETWIETWS------------- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 164 FQiamENIHSEMYSLLIDTYIKDPKErefLFNAIETMPCVKKKA---------------DWALRWIGD-----KEATYGE 223
Cdd:PRK09101 114 FS---ETIHSRSYTHIIRNIVNDPSV---VFDDIVTNEEILKRAkdissyyddliemtsYYHLLGEGThtvngKTVTVSL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 224 R---------VVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHL-----------VHK 283
Cdd:PRK09101 188 RelkkklylcLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLMrsgkddpemaeIAE 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4557845 284 PSEERVREIIINAVRIEQEFlTEALpVK---LIGMNCTLMKQYIEFVADRLMLELGFSKVFRVE-NPFDFMEN 352
Cdd:PRK09101 268 ECKQECYDLFVQAAEQEKEW-ADYL-FKdgsMIGLNKDILCQYVEYITNIRMQAVGLDLPFQTRsNPIPWINA 338
|
|
| PRK13965 |
PRK13965 |
ribonucleotide-diphosphate reductase subunit beta; Provisional |
89-344 |
1.56e-07 |
|
ribonucleotide-diphosphate reductase subunit beta; Provisional
Pssm-ID: 184425 [Multi-domain] Cd Length: 335 Bit Score: 52.47 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 89 DIWQmykKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIvnENLVERFSqevQITEAR-----CFYG 163
Cdd:PRK13965 37 EVWN---RVTQNFWLPEKVPVSNDLNSWRSLGEDWQQLITRTFTGLTLLDTV--QATVGDVA---QIPHSQtdheqVIYT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 164 FQIAMENIHSEMYSLLIDTYIKDPKEREFLFNAIETmPCVKKKADWALR-WIGDKEAtygERVVAFAAVEGIFFSGSFAS 242
Cdd:PRK13965 109 NFAFMVAIHARSYGTIFSTLCSSEQIEEAHEWVVST-ESLQRRARVLIPyYTGDDPL---KSKVAAAMMPGFLLYGGFYL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 243 IFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEER-------VREIIINAVRIEQEFLTEalpvklIGM 315
Cdd:PRK13965 185 PFYLSARGKLPNTSDIIRLILRDKVIHNYYSGYKYQQKVARLSPEKqaemkafVFDLLYELIDLEKAYLRE------LYA 258
|
250 260 270
....*....|....*....|....*....|..
gi 4557845 316 NCTLMKQYIEFV---ADRLMLELGFSKVFRVE 344
Cdd:PRK13965 259 GFDLAEDAIRFSlynAGKFLQNLGYESPFTEE 290
|
|
| nrdF2 |
PRK13966 |
ribonucleotide-diphosphate reductase subunit beta; Provisional |
92-341 |
3.84e-07 |
|
ribonucleotide-diphosphate reductase subunit beta; Provisional
Pssm-ID: 140022 Cd Length: 324 Bit Score: 51.26 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 92 QMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNE-NLVERFSQEVQITEARCFYGFQIaMEN 170
Cdd:PRK13966 26 EVWDRLTGNFWLPEKVPVSNDIPSWGTLTAGEKQLTMRVFTGLTMLDTIQGTvGAVSLIPDALTPHEEAVLTNIAF-MES 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 171 IHSEMYSLLIDTyIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATygERVVAFAAVEG-IFFSGSFASIFWlKKR 249
Cdd:PRK13966 105 VHAKSYSQIFST-LCSTAEIDDAFRWSEENRNLQRKAEIVLQYYRGDEPL--KRKVASTLLESfLFYSGFYLPMYW-SSR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 250 GLMPGLTFSNELISRDEGLHCDFACLMFKH---LVHKPSEERVR--------EIIINAVRIEQEFLTEalpvklIGMNcT 318
Cdd:PRK13966 181 AKLTNTADMIRLIIRDEAVHGYYIGYKFQRglaLVDDVTRAELKdytyellfELYDNEVEYTQDLYDE------VGLT-E 253
|
250 260
....*....|....*....|...
gi 4557845 319 LMKQYIEFVADRLMLELGFSKVF 341
Cdd:PRK13966 254 DVKKFLRYNANKALMNLGYEALF 276
|
|
| nrdF1 |
PRK13967 |
ribonucleotide-diphosphate reductase subunit beta; Provisional |
92-269 |
5.14e-06 |
|
ribonucleotide-diphosphate reductase subunit beta; Provisional
Pssm-ID: 140023 Cd Length: 322 Bit Score: 47.80 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 92 QMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASD-GIVNENLVERFSQEVQITEARCFYGFQIaMEN 170
Cdd:PRK13967 24 QVWERLTGNFWLPEKIPLSNDLASWQTLSSTEQQTTIRVFTGLTLLDtAQATVGAVAMIDDAVTPHEEAVLTNMAF-MES 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557845 171 IHSEMYSLLIDTyIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATygERVVAFAAVEG-IFFSGSFASIFWlKKR 249
Cdd:PRK13967 103 VHAKSYSSIFST-LCSTKQIDDAFDWSEQNPYLQRKAQIIVDYYRGDDAL--KRKASSVMLESfLFYSGFYLPMYW-SSR 178
|
170 180
....*....|....*....|
gi 4557845 250 GLMPGLTFSNELISRDEGLH 269
Cdd:PRK13967 179 GKLTNTADLIRLIIRDEAVH 198
|
|
|