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Conserved domains on  [gi|219110949|ref|XP_002177226|]
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predicted protein [Phaeodactylum tricornutum CCAP 1055/1]

Protein Classification

ribonucleoside-diphosphate reductase small subunit( domain architecture ID 10791385)

ribonucleoside-diphosphate reductase small subunit catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02492 PLN02492
ribonucleoside-diphosphate reductase
 82-409 0e+00

ribonucleoside-diphosphate reductase


:

Pssm-ID: 215272  Cd Length: 324  Bit Score: 631.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949  82 EPVCqhDDSGSRFSLFPIEHDDLWGMYKQHVASFWTVDEIDLSADLTDWhERLNDNERHFISMVLAFFAGADGIVVENLA 161
Cdd:PLN02492   1 EPLL--AENPDRFCMFPIKYPQIWEMYKKAEASFWTAEEVDLSADLKDW-EKLTDDERHFISHVLAFFAASDGIVLENLA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 162 ERFCREVTVPEARAFYGFQMAMEGIHQETYCLLIDSYISDPKDREMLFAAHTKVPSVEKKARWAQRYIGSDASFAERLVA 241
Cdd:PLN02492  78 ARFMKEVQVPEARAFYGFQIAIENIHSEMYSLLLDTYIKDPKEKDRLFNAIETIPCVAKKADWALRWIDSSASFAERLVA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 242 FAAVEGIFFSGAFCSIFWLKKRGLMPGLTFSNELISRDEGLHCSFACQLYSKLERKLSETDMHKLIGEAVEVEKGFVCDA 321
Cdd:PLN02492 158 FACVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLKNKLSEERVKEIVCEAVEIEKEFVCDA 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 322 LPVGLIGMNASLMSQYVEFVADRLLHDLGYRTLYGSKNPFDWMDMISLEGKTNFFEKRVGEYQKSGVMASLSDDHtHGRK 401
Cdd:PLN02492 238 LPCALVGMNADLMSQYIEFVADRLLVALGYEKVYNVVNPFDWMELISLQGKTNFFEKRVGEYQKAGVMSSLNGGG-ADNH 316


                 ....*...
gi 219110949 402 SFNLDADF 409
Cdd:PLN02492 317 VFSLDEDF 324
 
Name Accession Description Interval E-value
PLN02492 PLN02492
ribonucleoside-diphosphate reductase
 82-409 0e+00

ribonucleoside-diphosphate reductase


Pssm-ID: 215272  Cd Length: 324  Bit Score: 631.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949  82 EPVCqhDDSGSRFSLFPIEHDDLWGMYKQHVASFWTVDEIDLSADLTDWhERLNDNERHFISMVLAFFAGADGIVVENLA 161
Cdd:PLN02492   1 EPLL--AENPDRFCMFPIKYPQIWEMYKKAEASFWTAEEVDLSADLKDW-EKLTDDERHFISHVLAFFAASDGIVLENLA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 162 ERFCREVTVPEARAFYGFQMAMEGIHQETYCLLIDSYISDPKDREMLFAAHTKVPSVEKKARWAQRYIGSDASFAERLVA 241
Cdd:PLN02492  78 ARFMKEVQVPEARAFYGFQIAIENIHSEMYSLLLDTYIKDPKEKDRLFNAIETIPCVAKKADWALRWIDSSASFAERLVA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 242 FAAVEGIFFSGAFCSIFWLKKRGLMPGLTFSNELISRDEGLHCSFACQLYSKLERKLSETDMHKLIGEAVEVEKGFVCDA 321
Cdd:PLN02492 158 FACVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLKNKLSEERVKEIVCEAVEIEKEFVCDA 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 322 LPVGLIGMNASLMSQYVEFVADRLLHDLGYRTLYGSKNPFDWMDMISLEGKTNFFEKRVGEYQKSGVMASLSDDHtHGRK 401
Cdd:PLN02492 238 LPCALVGMNADLMSQYIEFVADRLLVALGYEKVYNVVNPFDWMELISLQGKTNFFEKRVGEYQKAGVMSSLNGGG-ADNH 316


                 ....*...
gi 219110949 402 SFNLDADF 409
Cdd:PLN02492 317 VFSLDEDF 324
Ribonuc_red_sm pfam00268
Ribonucleotide reductase, small chain;
93-360 6.68e-136

Ribonucleotide reductase, small chain;


Pssm-ID: 425568 [Multi-domain]  Cd Length: 276  Bit Score: 389.94  E-value: 6.68e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949   93 RFSLFPIEHDDLWGMYKQHVASFWTVDEIDLSADLTDWHeRLNDNERHFISMVLAFFAGADGIVVENLAERFCREVTVPE 172
Cdd:pfam00268   1 RFNLNPIKYPEIWEFYKKLEANFWTPEEIPLSKDIKDWK-KLSEDEREFIKRVLAFLALLDTLVNENLVERFSREVQTPE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949  173 ARAFYGFQMAMEGIHQETYCLLIDSYISDPKDREMLFAAHTKVPSVEKKARWAQRYI-GSDASFAERLVAFAAVEGIFFS 251
Cdd:pfam00268  80 ARAFYGFQAFMENIHSESYSYILDTLGKDPEEIDELFNWIETNPALQKKAEWILKWYqDFDSDFLERLVAFAILEGIFFY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949  252 GAFCSIFWLKKRGLMPGLTFSNELISRDEGLHCSFACQLYSKL-------ERKLSETDMHKLIGEAVEVEKGFVCDALPV 324
Cdd:pfam00268 160 SGFAAILWLKRRGKMPGLAEIIELISRDEGLHGDFACLLFQHLkeenpelETKELKEEVYDLIKEAVELEKEFLDDALPV 239

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 219110949  325 GLIGMNASLMSQYVEFVADRLLHDLGYRTLYGS-KNP 360
Cdd:pfam00268 240 GLLGMNAEDVKQYIEYVADRRLMNLGYEKLYNVeVNP 276
RNRR2 cd01049
Ribonucleotide Reductase, R2/beta subunit, ferritin-like diiron-binding domain; Ribonucleotide ...
 94-369 2.93e-126

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: 365.79  E-value: 2.93e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949  94 FSLFPIEHDDLWGMYKQHVASFWTVDEIDLSADLTDWHErLNDNERHFISMVLAFFAGADGIVVENLAERFCREVTVPEA 173
Cdd:cd01049    1 FNLNPIKYPWAWELYKKAEANFWTPEEIDLSKDLKDWEK-LTEAERHFIKRVLAFLAALDSIVGENLVELFSRHVQIPEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 174 RAFYGFQMAMEGIHQETYCLLIDSYISDPKdREMLFAAHTKVPSVEKKARWAQRYI-----GSDASFAERLVAFAAVEGI 248
Cdd:cd01049   80 RAFYGFQAFMENIHSESYSYILDTLGKDEE-RDELFEAIETDPALKKKADWILRWYdnlddNTKESFAERLVAFAILEGI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 249 FFSGAFCSIFWLKKRGLMPGLTFSNELISRDEGLHCSFACQLYSKLERKLSET-------DMHKLIGEAVEVEKGFVCDA 321
Cdd:cd01049  159 FFYSGFAAIFWLARRGKMPGLAEIIELISRDESLHGDFACLLIRELLNENPELfteefkeEVYELIKEAVELEKEFARDL 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 219110949 322 LPVGLIGMNASLMSQYVEFVADRLLHDLGYRTLYGS--KNPFDWMDMISL 369
Cdd:cd01049  239 LPDGILGLNKEDMKQYIEYVANRRLENLGLEKLFNVedKNPFDWMELISD 288
NrdB COG0208
Ribonucleotide reductase beta subunit, ferritin-like domain [Nucleotide transport and ...
 93-395 2.90e-110

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: 326.74  E-value: 2.90e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949  93 RFSLFPIEHDDLWGMYKQHVASFWTVDEIDLSADLTDWHeRLNDNERHFISMVLAFFAGADGIVVENLAERFCREVTVPE 172
Cdd:COG0208   13 RINWNPIKYPWAYELYKKQLANFWLPEEVPLSNDIKDWK-KLSDDERHLIKRVLGFLTLLDSIQGNNLVLALYPHVTAPE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 173 ARAFYGFQMAMEGIHQETYCLLIDSYISDPKDremLFAAHTKVPSVEKKARWAQRYI------GSDASFAERLVAFAAVE 246
Cdd:COG0208   92 VRAVLSRQAFMEAIHAKSYSYILETLGLDIDE---IFNWIEENPALQKKAEFILKYYddlgtrETKKDLLKSLVASVFLE 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 247 GIFFSGAFCSIFWLKKRGLMPGLTFSNELISRDEGLHCSFACQLY-------SKLERKLSETDMHKLIGEAVEVEKGFVC 319
Cdd:COG0208  169 GIFFYSGFAYPLSLARRGKMKGTAEIIRLILRDESLHGNFGIYLIntireenPELFTEELKEEIYELLKEAVELEKEYAD 248

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219110949 320 DALPVGLIGMNASLMSQYVEFVADRLLHDLGYRTLY-GSKNPFDWMD-MISLEGKTNFFEKRVGEYQKSGVMASLSDD 395
Cdd:COG0208  249 DLFPDGILGLNAEDVKQYIRYIANKRLMNLGLEPLFeGDVNPFPWMSeGLDLNKKTDFFETRVTEYQKGGVESTFDED 326
 
Name Accession Description Interval E-value
PLN02492 PLN02492
ribonucleoside-diphosphate reductase
 82-409 0e+00

ribonucleoside-diphosphate reductase


Pssm-ID: 215272  Cd Length: 324  Bit Score: 631.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949  82 EPVCqhDDSGSRFSLFPIEHDDLWGMYKQHVASFWTVDEIDLSADLTDWhERLNDNERHFISMVLAFFAGADGIVVENLA 161
Cdd:PLN02492   1 EPLL--AENPDRFCMFPIKYPQIWEMYKKAEASFWTAEEVDLSADLKDW-EKLTDDERHFISHVLAFFAASDGIVLENLA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 162 ERFCREVTVPEARAFYGFQMAMEGIHQETYCLLIDSYISDPKDREMLFAAHTKVPSVEKKARWAQRYIGSDASFAERLVA 241
Cdd:PLN02492  78 ARFMKEVQVPEARAFYGFQIAIENIHSEMYSLLLDTYIKDPKEKDRLFNAIETIPCVAKKADWALRWIDSSASFAERLVA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 242 FAAVEGIFFSGAFCSIFWLKKRGLMPGLTFSNELISRDEGLHCSFACQLYSKLERKLSETDMHKLIGEAVEVEKGFVCDA 321
Cdd:PLN02492 158 FACVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLKNKLSEERVKEIVCEAVEIEKEFVCDA 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 322 LPVGLIGMNASLMSQYVEFVADRLLHDLGYRTLYGSKNPFDWMDMISLEGKTNFFEKRVGEYQKSGVMASLSDDHtHGRK 401
Cdd:PLN02492 238 LPCALVGMNADLMSQYIEFVADRLLVALGYEKVYNVVNPFDWMELISLQGKTNFFEKRVGEYQKAGVMSSLNGGG-ADNH 316


                 ....*...
gi 219110949 402 SFNLDADF 409
Cdd:PLN02492 317 VFSLDEDF 324
PTZ00211 PTZ00211
ribonucleoside-diphosphate reductase small subunit; Provisional
 74-409 0e+00

ribonucleoside-diphosphate reductase small subunit; Provisional


Pssm-ID: 240315 [Multi-domain]  Cd Length: 330  Bit Score: 557.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949  74 EEEEATFIEPVCQHDDSgsRFSLFPIEHDDLWGMYKQHVASFWTVDEIDLSADLTDWhERLNDNERHFISMVLAFFAGAD 153
Cdd:PTZ00211   4 AMKENEEEEPLLKENPD--RFVLFPIKYPDIWRMYKKAEASFWTAEEIDLGNDLKDW-EKLNDGERHFIKHVLAFFAASD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 154 GIVVENLAERFCREVTVPEARAFYGFQMAMEGIHQETYCLLIDSYISDPKDREMLFAAHTKVPSVEKKARWAQRYIGSDA 233
Cdd:PTZ00211  81 GIVLENLAQRFMREVQVPEARCFYGFQIAMENIHSETYSLLIDTYITDEEEKDRLFHAIETIPAIKKKAEWAAKWINSSN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 234 SFAERLVAFAAVEGIFFSGAFCSIFWLKKRGLMPGLTFSNELISRDEGLHCSFACQLYSKLERKLSETDMHKLIGEAVEV 313
Cdd:PTZ00211 161 SFAERLVAFAAVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHTDFACLLYSHLKNKLPRERVQEIIKEAVEI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 314 EKGFVCDALPVGLIGMNASLMSQYVEFVADRLLHDLGYRTLYGSKNPFDWMDMISLEGKTNFFEKRVGEYQKSGVMASLS 393
Cdd:PTZ00211 241 EREFICDALPVDLIGMNSRLMAQYIEFVADRLLVALGVPKIYNSKNPFDWMDMISLQGKTNFFEKRVGEYQKAGVMAERT 320

                        330
                 ....*....|....*.
gi 219110949 394 DdhthgrKSFNLDADF 409
Cdd:PTZ00211 321 S------KVFSLDADF 330
Ribonuc_red_sm pfam00268
Ribonucleotide reductase, small chain;
93-360 6.68e-136

Ribonucleotide reductase, small chain;


Pssm-ID: 425568 [Multi-domain]  Cd Length: 276  Bit Score: 389.94  E-value: 6.68e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949   93 RFSLFPIEHDDLWGMYKQHVASFWTVDEIDLSADLTDWHeRLNDNERHFISMVLAFFAGADGIVVENLAERFCREVTVPE 172
Cdd:pfam00268   1 RFNLNPIKYPEIWEFYKKLEANFWTPEEIPLSKDIKDWK-KLSEDEREFIKRVLAFLALLDTLVNENLVERFSREVQTPE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949  173 ARAFYGFQMAMEGIHQETYCLLIDSYISDPKDREMLFAAHTKVPSVEKKARWAQRYI-GSDASFAERLVAFAAVEGIFFS 251
Cdd:pfam00268  80 ARAFYGFQAFMENIHSESYSYILDTLGKDPEEIDELFNWIETNPALQKKAEWILKWYqDFDSDFLERLVAFAILEGIFFY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949  252 GAFCSIFWLKKRGLMPGLTFSNELISRDEGLHCSFACQLYSKL-------ERKLSETDMHKLIGEAVEVEKGFVCDALPV 324
Cdd:pfam00268 160 SGFAAILWLKRRGKMPGLAEIIELISRDEGLHGDFACLLFQHLkeenpelETKELKEEVYDLIKEAVELEKEFLDDALPV 239

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 219110949  325 GLIGMNASLMSQYVEFVADRLLHDLGYRTLYGS-KNP 360
Cdd:pfam00268 240 GLLGMNAEDVKQYIEYVADRRLMNLGYEKLYNVeVNP 276
RNRR2 cd01049
Ribonucleotide Reductase, R2/beta subunit, ferritin-like diiron-binding domain; Ribonucleotide ...
 94-369 2.93e-126

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: 365.79  E-value: 2.93e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949  94 FSLFPIEHDDLWGMYKQHVASFWTVDEIDLSADLTDWHErLNDNERHFISMVLAFFAGADGIVVENLAERFCREVTVPEA 173
Cdd:cd01049    1 FNLNPIKYPWAWELYKKAEANFWTPEEIDLSKDLKDWEK-LTEAERHFIKRVLAFLAALDSIVGENLVELFSRHVQIPEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 174 RAFYGFQMAMEGIHQETYCLLIDSYISDPKdREMLFAAHTKVPSVEKKARWAQRYI-----GSDASFAERLVAFAAVEGI 248
Cdd:cd01049   80 RAFYGFQAFMENIHSESYSYILDTLGKDEE-RDELFEAIETDPALKKKADWILRWYdnlddNTKESFAERLVAFAILEGI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 249 FFSGAFCSIFWLKKRGLMPGLTFSNELISRDEGLHCSFACQLYSKLERKLSET-------DMHKLIGEAVEVEKGFVCDA 321
Cdd:cd01049  159 FFYSGFAAIFWLARRGKMPGLAEIIELISRDESLHGDFACLLIRELLNENPELfteefkeEVYELIKEAVELEKEFARDL 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 219110949 322 LPVGLIGMNASLMSQYVEFVADRLLHDLGYRTLYGS--KNPFDWMDMISL 369
Cdd:cd01049  239 LPDGILGLNKEDMKQYIEYVANRRLENLGLEKLFNVedKNPFDWMELISD 288
NrdB COG0208
Ribonucleotide reductase beta subunit, ferritin-like domain [Nucleotide transport and ...
 93-395 2.90e-110

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: 326.74  E-value: 2.90e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949  93 RFSLFPIEHDDLWGMYKQHVASFWTVDEIDLSADLTDWHeRLNDNERHFISMVLAFFAGADGIVVENLAERFCREVTVPE 172
Cdd:COG0208   13 RINWNPIKYPWAYELYKKQLANFWLPEEVPLSNDIKDWK-KLSDDERHLIKRVLGFLTLLDSIQGNNLVLALYPHVTAPE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 173 ARAFYGFQMAMEGIHQETYCLLIDSYISDPKDremLFAAHTKVPSVEKKARWAQRYI------GSDASFAERLVAFAAVE 246
Cdd:COG0208   92 VRAVLSRQAFMEAIHAKSYSYILETLGLDIDE---IFNWIEENPALQKKAEFILKYYddlgtrETKKDLLKSLVASVFLE 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 247 GIFFSGAFCSIFWLKKRGLMPGLTFSNELISRDEGLHCSFACQLY-------SKLERKLSETDMHKLIGEAVEVEKGFVC 319
Cdd:COG0208  169 GIFFYSGFAYPLSLARRGKMKGTAEIIRLILRDESLHGNFGIYLIntireenPELFTEELKEEIYELLKEAVELEKEYAD 248

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219110949 320 DALPVGLIGMNASLMSQYVEFVADRLLHDLGYRTLY-GSKNPFDWMD-MISLEGKTNFFEKRVGEYQKSGVMASLSDD 395
Cdd:COG0208  249 DLFPDGILGLNAEDVKQYIRYIANKRLMNLGLEPLFeGDVNPFPWMSeGLDLNKKTDFFETRVTEYQKGGVESTFDED 326
PRK07209 PRK07209
ribonucleotide-diphosphate reductase subunit beta; Validated
 85-389 8.96e-59

ribonucleotide-diphosphate reductase subunit beta; Validated


Pssm-ID: 235968  Cd Length: 369  Bit Score: 195.60  E-value: 8.96e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949  85 CQHDDSgsrfSLFPIEHDDLWGMYKQHVASFWTVDEIDLSADLTDWHER--LNDNERHFISMVLAFFAGADGIVVENLAE 162
Cdd:PRK07209  44 CRADVN----QLVPFKYKWAWEKYLAGCANHWMPQEVNMSRDIALWKSPngLTEDERRIVKRNLGFFSTADSLVANNIVL 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 163 RFCREVTVPEARAFYGFQMAMEGIHQETYCLLIDSYISDPKDremLFAAHTKVPSVEKKARWAQRYIGS----------- 231
Cdd:PRK07209 120 AIYRHITNPECRQYLLRQAFEEAIHTHAYQYIVESLGLDEGE---IFNMYHEVPSIRAKDEFLIPFTRSltdpnfktgtp 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 232 --DASFAERLVAFAAV-EGIFFSGAFCSIFWLKKRGLMPGLTFSNELISRDEGLHCSFACQLYS--KLERKLSETD---- 302
Cdd:PRK07209 197 enDQKLLRNLIAFYCImEGIFFYVGFTQILSLGRQNKMTGIAEQYQYILRDESMHLNFGIDLINqiKLENPHLWTAefqa 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 303 -MHKLIGEAVEVEKGFVCDALPVGLIGMNASLMSQYVEFVADRLLHDLGYRTLY-GSKNPFDWM-DMISLEGKTNFFEKR 379
Cdd:PRK07209 277 eIRELIKEAVELEYRYARDTMPRGVLGLNASMFKDYLRFIANRRLQQIGLKPQYpGTENPFPWMsEMIDLKKEKNFFETR 356

                        330
                 ....*....|
gi 219110949 380 VGEYQKSGVM 389
Cdd:PRK07209 357 VIEYQTGGAL 366
nrdF PRK09614
ribonucleotide-diphosphate reductase subunit beta; Reviewed
 108-395 8.69e-46

ribonucleotide-diphosphate reductase subunit beta; Reviewed


Pssm-ID: 236591 [Multi-domain]  Cd Length: 324  Bit Score: 160.38  E-value: 8.69e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 108 YKQHVASFWTVDEIDLSADLTDWHeRLNDNERHFISMVLAFFAGADGIVVENLAERFCREVTVPEARAFYGFQMAMEGIH 187
Cdd:PRK09614  26 WKRLTANFWLPEEVPLSNDLKDWK-KLSDEEKNLYTRVFGGLTLLDTLQNNNGMPNLMPDITTPEEEAVLANIAFMEAVH 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 188 QETYCLLIDSyISDPKDREMLFAAHTKVPSVEKKARWAQR-YIGSDASFAERLVAFAAV-EGI-FFSGaFCSIFWLKKRG 264
Cdd:PRK09614 105 AKSYSYIFST-LCSPEEIDEAFEWAEENPYLQKKADIIQDfYEPLKKKILRKAAVASVFlEGFlFYSG-FYYPLYLARQG 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 265 LMPGltfSNELIS---RDEGLHCSFACQLYSKLERKLSE-------TDMHKLIGEAVEVEKGFVCDALPVglIGmNASLM 334
Cdd:PRK09614 183 KMTG---TAQIIRliiRDESLHGYYIGYLFQEGLEELPEleqeelkDEIYDLLYELYENEEAYTELLYDI--VG-LAEDV 256

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219110949 335 SQYVEFVADRLLHDLGYRTLYGS--KNPFDWMDMISLEG--KTNFFEKRVGEYQKSGVMASLSDD 395
Cdd:PRK09614 257 KKYIRYNANKRLMNLGLEPLFPEeeEVNPIWLNGLSNNAdeNHDFFEGKGTSYVKGATEATEDDD 321
PRK12759 PRK12759
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional
 110-398 7.36e-27

bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional


Pssm-ID: 139206 [Multi-domain]  Cd Length: 410  Bit Score: 110.89  E-value: 7.36e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 110 QHVASFWTVDEIDLSADLTDWHE-RLNDNERHFISMVLAFFAGADGIVVENLAERFCREVTVPEARAFYGFQMAMEGIHQ 188
Cdd:PRK12759 114 KHEKAHWIEDEIDLSEDVTDWKNgKITKVEKEYITNILRLFTQSDVAVGQNYYDQFIPLFKNNEIRNMLGSFAAREGIHQ 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 189 ETYCLLIDSyISDPKDREMLFaahtkvpsVEKKARWAQRYIGSDASFAER------LVAFAAVEGIFFSGAFCSIFWLKK 262
Cdd:PRK12759 194 RAYALLNDT-LGLPDSEYHAF--------LEYKAMTDKIDFMMDADPTTRrglglcLAKTVFNEGVALFASFAMLLNFQR 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 263 RGLMPGLTFSNELISRDEGLHCS-------FACQLYSKLERKLSETDMHKLIGEAVEVEKGFVCDALPVGLI-GMNASLM 334
Cdd:PRK12759 265 FGKMKGMGKVVEWSIRDESMHVEgnaalfrIYCQENPYIVDNEFKKEIYLMASKAVELEDRFIELAYELGTIeGLKADEV 344

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 219110949 335 SQYVEFVADRLLHDLGYRTLYG-SKNPFDWMDMIsLEG--KTNFFEKRVGEYQKSGVMASLSDDHTH 398
Cdd:PRK12759 345 KQYIRHITDRRLNQLGLKEIYNiEKNPLTWLEWI-LNGadHTNFFENRVTEYEVAGLTGSWDEAYSA 410
nrdF2 PRK13966
ribonucleotide-diphosphate reductase subunit beta; Provisional
 107-355 1.51e-08

ribonucleotide-diphosphate reductase subunit beta; Provisional


Pssm-ID: 140022  Cd Length: 324  Bit Score: 55.88  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 107 MYKQHVASFWTVDEIDLSADLTDWHErLNDNERHFISMVLAFFAGADGIVVENLAERFCREVTVPEARAFYGFQMAMEGI 186
Cdd:PRK13966  27 VWDRLTGNFWLPEKVPVSNDIPSWGT-LTAGEKQLTMRVFTGLTMLDTIQGTVGAVSLIPDALTPHEEAVLTNIAFMESV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 187 HQETYCLLIDSYISDPKDREMlFAAHTKVPSVEKKARWAQRYIGSDASFAERLVAFAAVEGIFFSGAFCSIFWlKKRGLM 266
Cdd:PRK13966 106 HAKSYSQIFSTLCSTAEIDDA-FRWSEENRNLQRKAEIVLQYYRGDEPLKRKVASTLLESFLFYSGFYLPMYW-SSRAKL 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 267 PGLTFSNELISRDEGLHCSFACQLYSK------LERKLSETD-MHKLIGEAVEVEKGFVCDAL-PVGLigmnASLMSQYV 338
Cdd:PRK13966 184 TNTADMIRLIIRDEAVHGYYIGYKFQRglalvdDVTRAELKDyTYELLFELYDNEVEYTQDLYdEVGL----TEDVKKFL 259

                        250
                 ....*....|....*..
gi 219110949 339 EFVADRLLHDLGYRTLY 355
Cdd:PRK13966 260 RYNANKALMNLGYEALF 276
PRK08326 PRK08326
R2-like ligand-binding oxidase;
113-351 2.52e-06

R2-like ligand-binding oxidase;


Pssm-ID: 236242  Cd Length: 311  Bit Score: 48.84  E-value: 2.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 113 ASFWTVDEIDLSADLTDWhERLNDNERHFISMVLAFFAGADGIVVENLA------------------ERFCREvtvpEAR 174
Cdd:PRK08326  36 AKFWNPADIDFSRDAEDW-EKLSDEERDYATRLCAQFIAGEEAVTLDIQplisamaaegrledemylTQFAFE----EAK 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 175 AFYGFQMAME--GIHQETYCLLIDS-------YISDPKDREMLfaahTKVPSVEKKARWAQRYIGSdasfaerlvafaaV 245
Cdd:PRK08326 111 HTEAFRRWFDavGVTEDLSVYTDDNpsyrqifYEELPAALNRL----STDPSPENQVRASVTYNHV-------------V 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 246 EGIF-FSG--AFCSIFwlKKRGLMPGLTFSNELISRDEGLHCSFA---CQLYSKLER---KLSETDMHKLIGEAVE-VEK 315
Cdd:PRK08326 174 EGVLaETGyyAWRKIC--VTRGILPGLQELVRRIGDDERRHIAWGtytCRRLVAADDsnwDVFEERMNELLPLALGlIDE 251

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 219110949 316 GFVC--DALPVGLIgmnaslMSQYVEFVADRLLHDLGY 351
Cdd:PRK08326 252 IFALygDQIPFELS------NDEFVDYAADRGQRRLGA 283
nrdB PRK09101
ribonucleotide-diphosphate reductase subunit beta; Reviewed
 115-364 3.28e-06

ribonucleotide-diphosphate reductase subunit beta; Reviewed


Pssm-ID: 181647  Cd Length: 376  Bit Score: 48.81  E-value: 3.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 115 FWTVDEIDLSADLTDWhERLNDNERH-FISMvLAFFAGADGIV--VENLAerFCREVTVPEARAF---YGFQmamEGIHQ 188
Cdd:PRK09101  48 FWRPEEVDVSRDRIDY-QALPEHEKHiFISN-LKYQTLLDSIQgrSPNVA--LLPLVSIPELETWietWSFS---ETIHS 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 189 ETYCLLIDSYISDP--------KDREMLFAA------------------------HT---KVPSVEKKARWAQRYIGsda 233
Cdd:PRK09101 121 RSYTHIIRNIVNDPsvvfddivTNEEILKRAkdissyyddliemtsyyhllgegtHTvngKTVTVSLRELKKKLYLC--- 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 234 sfaerLVAFAAVEGIFFSGAF-CSiFWLKKRGLMPGLTFSNELISRDEGLHCSfACQLYSKLER------------KLSE 300
Cdd:PRK09101 198 -----LMSVNALEAIRFYVSFaCS-FAFAERELMEGNAKIIRLIARDEALHLT-GTQHMLNLMRsgkddpemaeiaEECK 270

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 219110949 301 TDMHKLIGEAVEVEKGFVCDALPVG-LIGMNASLMSQYVEFVADRLLHDLGYRTLYGSK-NPFDWM 364
Cdd:PRK09101 271 QECYDLFVQAAEQEKEWADYLFKDGsMIGLNKDILCQYVEYITNIRMQAVGLDLPFQTRsNPIPWI 336
nrdF1 PRK13967
ribonucleotide-diphosphate reductase subunit beta; Provisional
 107-355 3.51e-06

ribonucleotide-diphosphate reductase subunit beta; Provisional


Pssm-ID: 140023  Cd Length: 322  Bit Score: 48.57  E-value: 3.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 107 MYKQHVASFWTVDEIDLSADLTDWhERLNDNERHFISMVLAFFAGADGIVVENLAERFCREVTVPEARAFYGFQMAMEGI 186
Cdd:PRK13967  25 VWERLTGNFWLPEKIPLSNDLASW-QTLSSTEQQTTIRVFTGLTLLDTAQATVGAVAMIDDAVTPHEEAVLTNMAFMESV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 187 HQETYCLLIDSYISDpKDREMLFAAHTKVPSVEKKARWAQRYIGSDASFAERLVAFAAVEGIFFSGAFCSIFWlKKRGLM 266
Cdd:PRK13967 104 HAKSYSSIFSTLCST-KQIDDAFDWSEQNPYLQRKAQIIVDYYRGDDALKRKASSVMLESFLFYSGFYLPMYW-SSRGKL 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 267 PGLTFSNELISRDEGLHCSFacqLYSKLERKLSE-TD-------------MHKLIGEAVEV------EKGFVCDALPvgl 326
Cdd:PRK13967 182 TNTADLIRLIIRDEAVHGYY---IGYKCQRGLADlTDaeradhreytcelLHTLYANEIDYahdlydELGWTDDVLP--- 255

                        250       260
                 ....*....|....*....|....*....
gi 219110949 327 igmnaslmsqYVEFVADRLLHDLGYRTLY 355
Cdd:PRK13967 256 ----------YMRYNANKALANLGYQPAF 274
RNRR2_Rv0233_like cd07911
Ribonucleotide Reductase R2-like protein, Mn/Fe-binding domain; Rv0233 is a Mycobacterium ...
 115-312 4.90e-05

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: 44.64  E-value: 4.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 115 FWTVDEIDLSADLTDWhERLNDNERHFISMVLAFFAGADGIVVENLAE------------------RFCREvtvpEARAF 176
Cdd:cd07911   21 FWNPADIDFSQDREDW-EQLSEEERDLALRLCAGFIAGEEAVTLDLLPlmmamaaegrleeemyltQFLFE----EAKHT 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219110949 177 YGFQMAME--GIHQetyclLIDSYISDPKDR---EMLFAAHTKV---PSVEKKARWAQRYIGSdasfaerlvafaaVEGI 248
Cdd:cd07911   96 DFFRRWLDavGVSD-----DLSDLHTAVYREpfyEALPYAELRLyldASPAAQVRASVTYNMI-------------VEGV 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219110949 249 FFSGAFCSIF-WLKKRGLMPGLTFSNELISRDEGLHCS---FACQ--------LYSKLERKLSETDMHKL--IGEAVE 312
Cdd:cd07911  158 LAETGYYAWRtICEKRGILPGMQEGIRRLGDDESRHIAwgtFTCRrlvaaddaNWDVFEERMNELVPHALglIDEIFE 235
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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