|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02492 |
PLN02492 |
ribonucleoside-diphosphate reductase |
130-449 |
0e+00 |
|
ribonucleoside-diphosphate reductase
Pssm-ID: 215272 Cd Length: 324 Bit Score: 627.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 130 EPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVERF 209
Cdd:PLN02492 1 EPLLAENPDRFCMFPIKYPQIWEMYKKAEASFWTAEEVDLSADLKDWEKLTDDERHFISHVLAFFAASDGIVLENLAARF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 210 SQEVQITEARCFYGFQIAMENIHSEMYSLLIDTYIKDPKEREFLFNAIETMPCVKKKADWALRWIgDKEATYGERVVAFA 289
Cdd:PLN02492 81 MKEVQVPEARAFYGFQIAIENIHSEMYSLLLDTYIKDPKEKDRLFNAIETIPCVAKKADWALRWI-DSSASFAERLVAFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 290 AVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIEQEFLTEALP 369
Cdd:PLN02492 160 CVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLKNKLSEERVKEIVCEAVEIEKEFVCDALP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 370 VKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFMENISLEGKTNFFEKRVGEYQRMGVMSS-----PTENSFT 444
Cdd:PLN02492 240 CALVGMNADLMSQYIEFVADRLLVALGYEKVYNVVNPFDWMELISLQGKTNFFEKRVGEYQKAGVMSSlngggADNHVFS 319
|
....*
gi 260064013 445 LDADF 449
Cdd:PLN02492 320 LDEDF 324
|
|
| Ribonuc_red_sm |
pfam00268 |
Ribonucleotide reductase, small chain; |
139-406 |
2.10e-161 |
|
Ribonucleotide reductase, small chain;
Pssm-ID: 425568 [Multi-domain] Cd Length: 276 Bit Score: 456.19 E-value: 2.10e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 139 RFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEA 218
Cdd:pfam00268 1 RFNLNPIKYPEIWEFYKKLEANFWTPEEIPLSKDIKDWKKLSEDEREFIKRVLAFLALLDTLVNENLVERFSREVQTPEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 219 RCFYGFQIAMENIHSEMYSLLIDTYIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSG 298
Cdd:pfam00268 81 RAFYGFQAFMENIHSESYSYILDTLGKDPEEIDELFNWIETNPALQKKAEWILKWYQDFDSDFLERLVAFAILEGIFFYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 299 SFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLV-------HKPSEERVREIIINAVRIEQEFLTEALPVK 371
Cdd:pfam00268 161 GFAAILWLKRRGKMPGLAEIIELISRDEGLHGDFACLLFQHLKeenpeleTKELKEEVYDLIKEAVELEKEFLDDALPVG 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 260064013 372 LIGMNCTLMKQYIEFVADRLMLELGFSKVFRVE-NP 406
Cdd:pfam00268 241 LLGMNAEDVKQYIEYVADRRLMNLGYEKLYNVEvNP 276
|
|
| RNRR2 |
cd01049 |
Ribonucleotide Reductase, R2/beta subunit, ferritin-like diiron-binding domain; Ribonucleotide ... |
140-415 |
1.03e-148 |
|
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: 424.73 E-value: 1.03e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 140 FVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEAR 219
Cdd:cd01049 1 FNLNPIKYPWAWELYKKAEANFWTPEEIDLSKDLKDWEKLTEAERHFIKRVLAFLAALDSIVGENLVELFSRHVQIPEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 220 CFYGFQIAMENIHSEMYSLLIDTYIKDPkEREFLFNAIETMPCVKKKADWALRWIGD----KEATYGERVVAFAAVEGIF 295
Cdd:cd01049 81 AFYGFQAFMENIHSESYSYILDTLGKDE-ERDELFEAIETDPALKKKADWILRWYDNlddnTKESFAERLVAFAILEGIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 296 FSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHK-------PSEERVREIIINAVRIEQEFLTEAL 368
Cdd:cd01049 160 FYSGFAAIFWLARRGKMPGLAEIIELISRDESLHGDFACLLIRELLNEnpelfteEFKEEVYELIKEAVELEKEFARDLL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 260064013 369 PVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRV--ENPFDFMENISL 415
Cdd:cd01049 240 PDGILGLNKEDMKQYIEYVANRRLENLGLEKLFNVedKNPFDWMELISD 288
|
|
| NrdB |
COG0208 |
Ribonucleotide reductase beta subunit, ferritin-like domain [Nucleotide transport and ... |
128-437 |
1.70e-118 |
|
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: 349.08 E-value: 1.70e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 128 EDEPLLRENP-RRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLV 206
Cdd:COG0208 1 LDEPIINGLTtNRINWNPIKYPWAYELYKKQLANFWLPEEVPLSNDIKDWKKLSDDERHLIKRVLGFLTLLDSIQGNNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 207 ERFSQEVQITEARCFYGFQIAMENIHSEMYSLLIDTYIKDPKErefLFNAIETMPCVKKKADWALRWIGDKEATYG---- 282
Cdd:COG0208 81 LALYPHVTAPEVRAVLSRQAFMEAIHAKSYSYILETLGLDIDE---IFNWIEENPALQKKAEFILKYYDDLGTRETkkdl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 283 -ERVVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFK-------HLVHKPSEERVREIII 354
Cdd:COG0208 158 lKSLVASVFLEGIFFYSGFAYPLSLARRGKMKGTAEIIRLILRDESLHGNFGIYLINtireenpELFTEELKEEIYELLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 355 NAVRIEQEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRV-ENPFDFMEN-ISLEGKTNFFEKRVGEYQRM 432
Cdd:COG0208 238 EAVELEKEYADDLFPDGILGLNAEDVKQYIRYIANKRLMNLGLEPLFEGdVNPFPWMSEgLDLNKKTDFFETRVTEYQKG 317
|
....*
gi 260064013 433 GVMSS 437
Cdd:COG0208 318 GVEST 322
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02492 |
PLN02492 |
ribonucleoside-diphosphate reductase |
130-449 |
0e+00 |
|
ribonucleoside-diphosphate reductase
Pssm-ID: 215272 Cd Length: 324 Bit Score: 627.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 130 EPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVERF 209
Cdd:PLN02492 1 EPLLAENPDRFCMFPIKYPQIWEMYKKAEASFWTAEEVDLSADLKDWEKLTDDERHFISHVLAFFAASDGIVLENLAARF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 210 SQEVQITEARCFYGFQIAMENIHSEMYSLLIDTYIKDPKEREFLFNAIETMPCVKKKADWALRWIgDKEATYGERVVAFA 289
Cdd:PLN02492 81 MKEVQVPEARAFYGFQIAIENIHSEMYSLLLDTYIKDPKEKDRLFNAIETIPCVAKKADWALRWI-DSSASFAERLVAFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 290 AVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIEQEFLTEALP 369
Cdd:PLN02492 160 CVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLKNKLSEERVKEIVCEAVEIEKEFVCDALP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 370 VKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFMENISLEGKTNFFEKRVGEYQRMGVMSS-----PTENSFT 444
Cdd:PLN02492 240 CALVGMNADLMSQYIEFVADRLLVALGYEKVYNVVNPFDWMELISLQGKTNFFEKRVGEYQKAGVMSSlngggADNHVFS 319
|
....*
gi 260064013 445 LDADF 449
Cdd:PLN02492 320 LDEDF 324
|
|
| PTZ00211 |
PTZ00211 |
ribonucleoside-diphosphate reductase small subunit; Provisional |
128-449 |
0e+00 |
|
ribonucleoside-diphosphate reductase small subunit; Provisional
Pssm-ID: 240315 [Multi-domain] Cd Length: 330 Bit Score: 608.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 128 EDEPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVE 207
Cdd:PTZ00211 10 EEEPLLKENPDRFVLFPIKYPDIWRMYKKAEASFWTAEEIDLGNDLKDWEKLNDGERHFIKHVLAFFAASDGIVLENLAQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 208 RFSQEVQITEARCFYGFQIAMENIHSEMYSLLIDTYIKDPKEREFLFNAIETMPCVKKKADWALRWIGDkEATYGERVVA 287
Cdd:PTZ00211 90 RFMREVQVPEARCFYGFQIAMENIHSETYSLLIDTYITDEEEKDRLFHAIETIPAIKKKAEWAAKWINS-SNSFAERLVA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 288 FAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIEQEFLTEA 367
Cdd:PTZ00211 169 FAAVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHTDFACLLYSHLKNKLPRERVQEIIKEAVEIEREFICDA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 368 LPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFMENISLEGKTNFFEKRVGEYQRMGVMSSPTENSFTLDA 447
Cdd:PTZ00211 249 LPVDLIGMNSRLMAQYIEFVADRLLVALGVPKIYNSKNPFDWMDMISLQGKTNFFEKRVGEYQKAGVMAERTSKVFSLDA 328
|
..
gi 260064013 448 DF 449
Cdd:PTZ00211 329 DF 330
|
|
| Ribonuc_red_sm |
pfam00268 |
Ribonucleotide reductase, small chain; |
139-406 |
2.10e-161 |
|
Ribonucleotide reductase, small chain;
Pssm-ID: 425568 [Multi-domain] Cd Length: 276 Bit Score: 456.19 E-value: 2.10e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 139 RFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEA 218
Cdd:pfam00268 1 RFNLNPIKYPEIWEFYKKLEANFWTPEEIPLSKDIKDWKKLSEDEREFIKRVLAFLALLDTLVNENLVERFSREVQTPEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 219 RCFYGFQIAMENIHSEMYSLLIDTYIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSG 298
Cdd:pfam00268 81 RAFYGFQAFMENIHSESYSYILDTLGKDPEEIDELFNWIETNPALQKKAEWILKWYQDFDSDFLERLVAFAILEGIFFYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 299 SFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLV-------HKPSEERVREIIINAVRIEQEFLTEALPVK 371
Cdd:pfam00268 161 GFAAILWLKRRGKMPGLAEIIELISRDEGLHGDFACLLFQHLKeenpeleTKELKEEVYDLIKEAVELEKEFLDDALPVG 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 260064013 372 LIGMNCTLMKQYIEFVADRLMLELGFSKVFRVE-NP 406
Cdd:pfam00268 241 LLGMNAEDVKQYIEYVADRRLMNLGYEKLYNVEvNP 276
|
|
| RNRR2 |
cd01049 |
Ribonucleotide Reductase, R2/beta subunit, ferritin-like diiron-binding domain; Ribonucleotide ... |
140-415 |
1.03e-148 |
|
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: 424.73 E-value: 1.03e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 140 FVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEAR 219
Cdd:cd01049 1 FNLNPIKYPWAWELYKKAEANFWTPEEIDLSKDLKDWEKLTEAERHFIKRVLAFLAALDSIVGENLVELFSRHVQIPEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 220 CFYGFQIAMENIHSEMYSLLIDTYIKDPkEREFLFNAIETMPCVKKKADWALRWIGD----KEATYGERVVAFAAVEGIF 295
Cdd:cd01049 81 AFYGFQAFMENIHSESYSYILDTLGKDE-ERDELFEAIETDPALKKKADWILRWYDNlddnTKESFAERLVAFAILEGIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 296 FSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHK-------PSEERVREIIINAVRIEQEFLTEAL 368
Cdd:cd01049 160 FYSGFAAIFWLARRGKMPGLAEIIELISRDESLHGDFACLLIRELLNEnpelfteEFKEEVYELIKEAVELEKEFARDLL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 260064013 369 PVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRV--ENPFDFMENISL 415
Cdd:cd01049 240 PDGILGLNKEDMKQYIEYVANRRLENLGLEKLFNVedKNPFDWMELISD 288
|
|
| NrdB |
COG0208 |
Ribonucleotide reductase beta subunit, ferritin-like domain [Nucleotide transport and ... |
128-437 |
1.70e-118 |
|
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: 349.08 E-value: 1.70e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 128 EDEPLLRENP-RRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLV 206
Cdd:COG0208 1 LDEPIINGLTtNRINWNPIKYPWAYELYKKQLANFWLPEEVPLSNDIKDWKKLSDDERHLIKRVLGFLTLLDSIQGNNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 207 ERFSQEVQITEARCFYGFQIAMENIHSEMYSLLIDTYIKDPKErefLFNAIETMPCVKKKADWALRWIGDKEATYG---- 282
Cdd:COG0208 81 LALYPHVTAPEVRAVLSRQAFMEAIHAKSYSYILETLGLDIDE---IFNWIEENPALQKKAEFILKYYDDLGTRETkkdl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 283 -ERVVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFK-------HLVHKPSEERVREIII 354
Cdd:COG0208 158 lKSLVASVFLEGIFFYSGFAYPLSLARRGKMKGTAEIIRLILRDESLHGNFGIYLINtireenpELFTEELKEEIYELLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 355 NAVRIEQEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRV-ENPFDFMEN-ISLEGKTNFFEKRVGEYQRM 432
Cdd:COG0208 238 EAVELEKEYADDLFPDGILGLNAEDVKQYIRYIANKRLMNLGLEPLFEGdVNPFPWMSEgLDLNKKTDFFETRVTEYQKG 317
|
....*
gi 260064013 433 GVMSS 437
Cdd:COG0208 318 GVEST 322
|
|
| PRK07209 |
PRK07209 |
ribonucleotide-diphosphate reductase subunit beta; Validated |
142-436 |
1.57e-48 |
|
ribonucleotide-diphosphate reductase subunit beta; Validated
Pssm-ID: 235968 Cd Length: 369 Bit Score: 169.79 E-value: 1.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 142 IFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWES---LKPEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEA 218
Cdd:PRK07209 51 LVPFKYKWAWEKYLAGCANHWMPQEVNMSRDIALWKSpngLTEDERRIVKRNLGFFSTADSLVANNIVLAIYRHITNPEC 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 219 RCFYGFQIAMENIHSEMYSLLIDTYIKDPKErefLFNAIETMPCVKKKADWAL---RWIGDKEATYG---------ERVV 286
Cdd:PRK07209 131 RQYLLRQAFEEAIHTHAYQYIVESLGLDEGE---IFNMYHEVPSIRAKDEFLIpftRSLTDPNFKTGtpendqkllRNLI 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 287 AFAAV-EGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFK-------HLVHKPSEERVREIIINAVR 358
Cdd:PRK07209 208 AFYCImEGIFFYVGFTQILSLGRQNKMTGIAEQYQYILRDESMHLNFGIDLINqiklenpHLWTAEFQAEIRELIKEAVE 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 359 IEQEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFR-VENPFDFM-ENISLEGKTNFFEKRVGEYQRMGVMS 436
Cdd:PRK07209 288 LEYRYARDTMPRGVLGLNASMFKDYLRFIANRRLQQIGLKPQYPgTENPFPWMsEMIDLKKEKNFFETRVIEYQTGGALS 367
|
|
| nrdF |
PRK09614 |
ribonucleotide-diphosphate reductase subunit beta; Reviewed |
144-432 |
1.04e-43 |
|
ribonucleotide-diphosphate reductase subunit beta; Reviewed
Pssm-ID: 236591 [Multi-domain] Cd Length: 324 Bit Score: 155.75 E-value: 1.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 144 PIEY---HDIWqmyKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEARC 220
Cdd:PRK09614 16 KIEDpwdYEAW---KRLTANFWLPEEVPLSNDLKDWKKLSDEEKNLYTRVFGGLTLLDTLQNNNGMPNLMPDITTPEEEA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 221 FYGFQIAMENIHSEMYSLLIDTyIKDPKEREFLFNAIETMPCVKKKADWALRWIGD-KEATYGERVVAFAAVEGIFFSGS 299
Cdd:PRK09614 93 VLANIAFMEAVHAKSYSYIFST-LCSPEEIDEAFEWAEENPYLQKKADIIQDFYEPlKKKILRKAAVASVFLEGFLFYSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 300 FASIFWLKKRGLMPGltfSNELIS---RDEGLHCDFACLMFKHLVHKPSE-------ERVREIIINAVRIEQEFLTEALP 369
Cdd:PRK09614 172 FYYPLYLARQGKMTG---TAQIIRliiRDESLHGYYIGYLFQEGLEELPEleqeelkDEIYDLLYELYENEEAYTELLYD 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260064013 370 VklIGmNCTLMKQYIEFVADRLMLELGFSKVF--RVENPFDFMENISLEG--KTNFFEKRVGEYQRM 432
Cdd:PRK09614 249 I--VG-LAEDVKKYIRYNANKRLMNLGLEPLFpeEEEVNPIWLNGLSNNAdeNHDFFEGKGTSYVKG 312
|
|
| PRK12759 |
PRK12759 |
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional |
144-440 |
9.02e-25 |
|
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional
Pssm-ID: 139206 [Multi-domain] Cd Length: 410 Bit Score: 105.49 E-value: 9.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 144 PIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLK--PEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEARCF 221
Cdd:PRK12759 102 PFNYPWAVDLTVKHEKAHWIEDEIDLSEDVTDWKNGKitKVEKEYITNILRLFTQSDVAVGQNYYDQFIPLFKNNEIRNM 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 222 YGFQIAMENIHSEMYSLLIDTY-IKDPKEREFLfnaieTMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSF 300
Cdd:PRK12759 182 LGSFAAREGIHQRAYALLNDTLgLPDSEYHAFL-----EYKAMTDKIDFMMDADPTTRRGLGLCLAKTVFNEGVALFASF 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 301 ASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFK-------HLVHKPSEERVREIIINAVRIEQEFLTEALPVKLI 373
Cdd:PRK12759 257 AMLLNFQRFGKMKGMGKVVEWSIRDESMHVEGNAALFRiycqenpYIVDNEFKKEIYLMASKAVELEDRFIELAYELGTI 336
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 260064013 374 -GMNCTLMKQYIEFVADRLMLELGFSKVFRVE-NPFDFMENIsLEG--KTNFFEKRVGEYQRMGVMSSPTE 440
Cdd:PRK12759 337 eGLKADEVKQYIRHITDRRLNQLGLKEIYNIEkNPLTWLEWI-LNGadHTNFFENRVTEYEVAGLTGSWDE 406
|
|
| RNRR2_Rv0233_like |
cd07911 |
Ribonucleotide Reductase R2-like protein, Mn/Fe-binding domain; Rv0233 is a Mycobacterium ... |
152-396 |
1.27e-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: 58.89 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 152 QMYKKAEA-SFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVE---------RFSQEVQIT----- 216
Cdd:cd07911 11 KLFEKGKRkGFWNPADIDFSQDREDWEQLSEEERDLALRLCAGFIAGEEAVTLDLLPlmmamaaegRLEEEMYLTqflfe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 217 EARcfygfqiameniHSEMYSLLID---------TYIKDPKEREF---LFNAIEtmpcvKKKADWALRWIGDKEATYGER 284
Cdd:cd07911 91 EAK------------HTDFFRRWLDavgvsddlsDLHTAVYREPFyeaLPYAEL-----RLYLDASPAAQVRASVTYNMI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 285 VVAFAAVEGIFfsgSFASIfwLKKRGLMPGLTFSNELISRDEGLHCDFAC-LMFKHLVHKPS-----EERVREIIINAVR 358
Cdd:cd07911 154 VEGVLAETGYY---AWRTI--CEKRGILPGMQEGIRRLGDDESRHIAWGTfTCRRLVAADDAnwdvfEERMNELVPHALG 228
|
250 260 270
....*....|....*....|....*....|....*...
gi 260064013 359 IEQEfLTEALPVKLIGMNCTLMKQYiefVADRLMLELG 396
Cdd:cd07911 229 LIDE-IFELYDEMPFGLDPDELMQY---AVDQFQRRLG 262
|
|
| PRK08326 |
PRK08326 |
R2-like ligand-binding oxidase; |
153-396 |
1.78e-09 |
|
R2-like ligand-binding oxidase;
Pssm-ID: 236242 Cd Length: 311 Bit Score: 58.86 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 153 MYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVE---------RFSQEVQIT-----EA 218
Cdd:PRK08326 30 LFAKGNAKFWNPADIDFSRDAEDWEKLSDEERDYATRLCAQFIAGEEAVTLDIQPlisamaaegRLEDEMYLTqfafeEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 219 RcfygfqiameniHSEMYSLLIDT---------YIKD-PKEREFLFnaiETMPcvkkKADWALRwIGDKEATYGERVVAF 288
Cdd:PRK08326 110 K------------HTEAFRRWFDAvgvtedlsvYTDDnPSYRQIFY---EELP----AALNRLS-TDPSPENQVRASVTY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 289 -AAVEGIF-FSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLV------HKPSEERVREIIINAVR-I 359
Cdd:PRK08326 170 nHVVEGVLaETGYYAWRKICVTRGILPGLQELVRRIGDDERRHIAWGTYTCRRLVaaddsnWDVFEERMNELLPLALGlI 249
|
250 260 270
....*....|....*....|....*....|....*..
gi 260064013 360 EQEFLTEALPVKLIGMNCTLMkqyiEFVADRLMLELG 396
Cdd:PRK08326 250 DEIFALYGDQIPFELSNDEFV----DYAADRGQRRLG 282
|
|
| nrdB |
PRK09101 |
ribonucleotide-diphosphate reductase subunit beta; Reviewed |
161-412 |
2.22e-09 |
|
ribonucleotide-diphosphate reductase subunit beta; Reviewed
Pssm-ID: 181647 Cd Length: 376 Bit Score: 58.82 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 161 FWTAEEVDLSKDIQHWESLKPEERY-FISHvLAFFAASDGI----VN------------ENLVERFSqevqitearcfyg 223
Cdd:PRK09101 48 FWRPEEVDVSRDRIDYQALPEHEKHiFISN-LKYQTLLDSIqgrsPNvallplvsipelETWIETWS------------- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 224 FQiamENIHSEMYSLLIDTYIKDPKErefLFNAIETMPCVKKKA---------------DWALRWIGD-----KEATYGE 283
Cdd:PRK09101 114 FS---ETIHSRSYTHIIRNIVNDPSV---VFDDIVTNEEILKRAkdissyyddliemtsYYHLLGEGThtvngKTVTVSL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 284 R---------VVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHL-----------VHK 343
Cdd:PRK09101 188 RelkkklylcLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLMrsgkddpemaeIAE 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260064013 344 PSEERVREIIINAVRIEQEFlTEALpVK---LIGMNCTLMKQYIEFVADRLMLELGFSKVFRVE-NPFDFMEN 412
Cdd:PRK09101 268 ECKQECYDLFVQAAEQEKEW-ADYL-FKdgsMIGLNKDILCQYVEYITNIRMQAVGLDLPFQTRsNPIPWINA 338
|
|
| PRK13965 |
PRK13965 |
ribonucleotide-diphosphate reductase subunit beta; Provisional |
149-404 |
7.47e-08 |
|
ribonucleotide-diphosphate reductase subunit beta; Provisional
Pssm-ID: 184425 [Multi-domain] Cd Length: 335 Bit Score: 54.01 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 149 DIWQmykKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIvnENLVERFSqevQITEAR-----CFYG 223
Cdd:PRK13965 37 EVWN---RVTQNFWLPEKVPVSNDLNSWRSLGEDWQQLITRTFTGLTLLDTV--QATVGDVA---QIPHSQtdheqVIYT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 224 FQIAMENIHSEMYSLLIDTYIKDPKEREFLFNAIETmPCVKKKADWALR-WIGDKEAtygERVVAFAAVEGIFFSGSFAS 302
Cdd:PRK13965 109 NFAFMVAIHARSYGTIFSTLCSSEQIEEAHEWVVST-ESLQRRARVLIPyYTGDDPL---KSKVAAAMMPGFLLYGGFYL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 303 IFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEER-------VREIIINAVRIEQEFLTEalpvklIGM 375
Cdd:PRK13965 185 PFYLSARGKLPNTSDIIRLILRDKVIHNYYSGYKYQQKVARLSPEKqaemkafVFDLLYELIDLEKAYLRE------LYA 258
|
250 260 270
....*....|....*....|....*....|..
gi 260064013 376 NCTLMKQYIEFV---ADRLMLELGFSKVFRVE 404
Cdd:PRK13965 259 GFDLAEDAIRFSlynAGKFLQNLGYESPFTEE 290
|
|
| nrdF2 |
PRK13966 |
ribonucleotide-diphosphate reductase subunit beta; Provisional |
152-401 |
1.37e-07 |
|
ribonucleotide-diphosphate reductase subunit beta; Provisional
Pssm-ID: 140022 Cd Length: 324 Bit Score: 53.19 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 152 QMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNE-NLVERFSQEVQITEARCFYGFQIaMEN 230
Cdd:PRK13966 26 EVWDRLTGNFWLPEKVPVSNDIPSWGTLTAGEKQLTMRVFTGLTMLDTIQGTvGAVSLIPDALTPHEEAVLTNIAF-MES 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 231 IHSEMYSLLIDTyIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATygERVVAFAAVEG-IFFSGSFASIFWlKKR 309
Cdd:PRK13966 105 VHAKSYSQIFST-LCSTAEIDDAFRWSEENRNLQRKAEIVLQYYRGDEPL--KRKVASTLLESfLFYSGFYLPMYW-SSR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 310 GLMPGLTFSNELISRDEGLHCDFACLMFKH---LVHKPSEERVR--------EIIINAVRIEQEFLTEalpvklIGMNcT 378
Cdd:PRK13966 181 AKLTNTADMIRLIIRDEAVHGYYIGYKFQRglaLVDDVTRAELKdytyellfELYDNEVEYTQDLYDE------VGLT-E 253
|
250 260
....*....|....*....|...
gi 260064013 379 LMKQYIEFVADRLMLELGFSKVF 401
Cdd:PRK13966 254 DVKKFLRYNANKALMNLGYEALF 276
|
|
| nrdF1 |
PRK13967 |
ribonucleotide-diphosphate reductase subunit beta; Provisional |
152-329 |
5.93e-06 |
|
ribonucleotide-diphosphate reductase subunit beta; Provisional
Pssm-ID: 140023 Cd Length: 322 Bit Score: 48.19 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 152 QMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASD-GIVNENLVERFSQEVQITEARCFYGFQIaMEN 230
Cdd:PRK13967 24 QVWERLTGNFWLPEKIPLSNDLASWQTLSSTEQQTTIRVFTGLTLLDtAQATVGAVAMIDDAVTPHEEAVLTNMAF-MES 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260064013 231 IHSEMYSLLIDTyIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATygERVVAFAAVEG-IFFSGSFASIFWlKKR 309
Cdd:PRK13967 103 VHAKSYSSIFST-LCSTKQIDDAFDWSEQNPYLQRKAQIIVDYYRGDDAL--KRKASSVMLESfLFYSGFYLPMYW-SSR 178
|
170 180
....*....|....*....|
gi 260064013 310 GLMPGLTFSNELISRDEGLH 329
Cdd:PRK13967 179 GKLTNTADLIRLIIRDEAVH 198
|
|
|