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Conserved domains on  [gi|1622961223|ref|XP_015001291|]
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LOW QUALITY PROTEIN: ribonucleoside-diphosphate reductase subunit M2 B [Macaca mulatta]

Protein Classification

ferritin family protein( domain architecture ID 38)

ferritin family protein similar to rubrerythrin, a non-heme di-iron that is involved in oxidative stress defense as a peroxide scavenger in a wide range of organisms

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ferritin_like super family cl00264
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
104-423 0e+00

Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF).


The actual alignment was detected with superfamily member PLN02492:

Pssm-ID: 469698  Cd Length: 324  Bit Score: 602.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 104 EPLLRKSSRRFVIFPIQYPDIWKMYKQAQASFWTAEEVDLSKDLPHWNKLKADEKYFISHILAFFAASDGIVNENLVERF 183
Cdd:PLN02492    1 EPLLAENPDRFCMFPIKYPQIWEMYKKAEASFWTAEEVDLSADLKDWEKLTDDERHFISHVLAFFAASDGIVLENLAARF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 184 SQEVQVPEARCFYGFQILIENVHSEMYSLLIDTYIRDPKKREFLFNAIETMPYVKKKADWALRWIaDRKSTFGERVVAFA 263
Cdd:PLN02492   81 MKEVQVPEARAFYGFQIAIENIHSEMYSLLLDTYIKDPKEKDRLFNAIETIPCVAKKADWALRWI-DSSASFAERLVAFA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 264 AVEGIFFSGSFAAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQYLVNKPSEERVREIIVDAVQIEQEFLTEALP 343
Cdd:PLN02492  160 CVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLKNKLSEERVKEIVCEAVEIEKEFVCDALP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 344 VGLIGMNCILMKQYIEFVADRLLVELGFSKIFQAENPFDFMENISLEGKTNFFEKRVSEYQRFAVMAETTDN-----VFT 418
Cdd:PLN02492  240 CALVGMNADLMSQYIEFVADRLLVALGYEKVYNVVNPFDWMELISLQGKTNFFEKRVGEYQKAGVMSSLNGGgadnhVFS 319

                  ....*
gi 1622961223 419 LDADF 423
Cdd:PLN02492  320 LDEDF 324
 
Name Accession Description Interval E-value
PLN02492 PLN02492
ribonucleoside-diphosphate reductase
104-423 0e+00

ribonucleoside-diphosphate reductase


Pssm-ID: 215272  Cd Length: 324  Bit Score: 602.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 104 EPLLRKSSRRFVIFPIQYPDIWKMYKQAQASFWTAEEVDLSKDLPHWNKLKADEKYFISHILAFFAASDGIVNENLVERF 183
Cdd:PLN02492    1 EPLLAENPDRFCMFPIKYPQIWEMYKKAEASFWTAEEVDLSADLKDWEKLTDDERHFISHVLAFFAASDGIVLENLAARF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 184 SQEVQVPEARCFYGFQILIENVHSEMYSLLIDTYIRDPKKREFLFNAIETMPYVKKKADWALRWIaDRKSTFGERVVAFA 263
Cdd:PLN02492   81 MKEVQVPEARAFYGFQIAIENIHSEMYSLLLDTYIKDPKEKDRLFNAIETIPCVAKKADWALRWI-DSSASFAERLVAFA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 264 AVEGIFFSGSFAAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQYLVNKPSEERVREIIVDAVQIEQEFLTEALP 343
Cdd:PLN02492  160 CVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLKNKLSEERVKEIVCEAVEIEKEFVCDALP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 344 VGLIGMNCILMKQYIEFVADRLLVELGFSKIFQAENPFDFMENISLEGKTNFFEKRVSEYQRFAVMAETTDN-----VFT 418
Cdd:PLN02492  240 CALVGMNADLMSQYIEFVADRLLVALGYEKVYNVVNPFDWMELISLQGKTNFFEKRVGEYQKAGVMSSLNGGgadnhVFS 319

                  ....*
gi 1622961223 419 LDADF 423
Cdd:PLN02492  320 LDEDF 324
Ribonuc_red_sm pfam00268
Ribonucleotide reductase, small chain;
113-380 3.07e-157

Ribonucleotide reductase, small chain;


Pssm-ID: 425568 [Multi-domain]  Cd Length: 276  Bit Score: 444.64  E-value: 3.07e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 113 RFVIFPIQYPDIWKMYKQAQASFWTAEEVDLSKDLPHWNKLKADEKYFISHILAFFAASDGIVNENLVERFSQEVQVPEA 192
Cdd:pfam00268   1 RFNLNPIKYPEIWEFYKKLEANFWTPEEIPLSKDIKDWKKLSEDEREFIKRVLAFLALLDTLVNENLVERFSREVQTPEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 193 RCFYGFQILIENVHSEMYSLLIDTYIRDPKKREFLFNAIETMPYVKKKADWALRWIADRKSTFGERVVAFAAVEGIFFSG 272
Cdd:pfam00268  81 RAFYGFQAFMENIHSESYSYILDTLGKDPEEIDELFNWIETNPALQKKAEWILKWYQDFDSDFLERLVAFAILEGIFFYS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 273 SFAAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQYLV-------NKPSEERVREIIVDAVQIEQEFLTEALPVG 345
Cdd:pfam00268 161 GFAAILWLKRRGKMPGLAEIIELISRDEGLHGDFACLLFQHLKeenpeleTKELKEEVYDLIKEAVELEKEFLDDALPVG 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1622961223 346 LIGMNCILMKQYIEFVADRLLVELGFSKIFQAE-NP 380
Cdd:pfam00268 241 LLGMNAEDVKQYIEYVADRRLMNLGYEKLYNVEvNP 276
RNRR2 cd01049
Ribonucleotide Reductase, R2/beta subunit, ferritin-like diiron-binding domain; Ribonucleotide ...
114-389 6.90e-143

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: 408.94  E-value: 6.90e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 114 FVIFPIQYPDIWKMYKQAQASFWTAEEVDLSKDLPHWNKLKADEKYFISHILAFFAASDGIVNENLVERFSQEVQVPEAR 193
Cdd:cd01049     1 FNLNPIKYPWAWELYKKAEANFWTPEEIDLSKDLKDWEKLTEAERHFIKRVLAFLAALDSIVGENLVELFSRHVQIPEAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 194 CFYGFQILIENVHSEMYSLLIDTYIRDPkKREFLFNAIETMPYVKKKADWALRWIAD----RKSTFGERVVAFAAVEGIF 269
Cdd:cd01049    81 AFYGFQAFMENIHSESYSYILDTLGKDE-ERDELFEAIETDPALKKKADWILRWYDNlddnTKESFAERLVAFAILEGIF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 270 FSGSFAAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQYLVNK-------PSEERVREIIVDAVQIEQEFLTEAL 342
Cdd:cd01049   160 FYSGFAAIFWLARRGKMPGLAEIIELISRDESLHGDFACLLIRELLNEnpelfteEFKEEVYELIKEAVELEKEFARDLL 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1622961223 343 PVGLIGMNCILMKQYIEFVADRLLVELGFSKIF--QAENPFDFMENISL 389
Cdd:cd01049   240 PDGILGLNKEDMKQYIEYVANRRLENLGLEKLFnvEDKNPFDWMELISD 288
NrdB COG0208
Ribonucleotide reductase beta subunit, ferritin-like domain [Nucleotide transport and ...
109-415 1.12e-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: 340.99  E-value: 1.12e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 109 KSSRRFVIFPIQYPDIWKMYKQAQASFWTAEEVDLSKDLPHWNKLKADEKYFISHILAFFAASDGIVNENLVERFSQEVQ 188
Cdd:COG0208     9 LTTNRINWNPIKYPWAYELYKKQLANFWLPEEVPLSNDIKDWKKLSDDERHLIKRVLGFLTLLDSIQGNNLVLALYPHVT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 189 VPEARCFYGFQILIENVHSEMYSLLIDTYIRDPKKrefLFNAIETMPYVKKKADWALRWIADRKS-----TFGERVVAFA 263
Cdd:COG0208    89 APEVRAVLSRQAFMEAIHAKSYSYILETLGLDIDE---IFNWIEENPALQKKAEFILKYYDDLGTretkkDLLKSLVASV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 264 AVEGIFFSGSFAAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQYLVNKPSE-------ERVREIIVDAVQIEQE 336
Cdd:COG0208   166 FLEGIFFYSGFAYPLSLARRGKMKGTAEIIRLILRDESLHGNFGIYLINTIREENPElfteelkEEIYELLKEAVELEKE 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 337 FLTEALPVGLIGMNCILMKQYIEFVADRLLVELGFSKIFQ-AENPFDFMEN-ISLEGKTNFFEKRVSEYQRfAVMAETTD 414
Cdd:COG0208   246 YADDLFPDGILGLNAEDVKQYIRYIANKRLMNLGLEPLFEgDVNPFPWMSEgLDLNKKTDFFETRVTEYQK-GGVESTFD 324

                  .
gi 1622961223 415 N 415
Cdd:COG0208   325 E 325
 
Name Accession Description Interval E-value
PLN02492 PLN02492
ribonucleoside-diphosphate reductase
104-423 0e+00

ribonucleoside-diphosphate reductase


Pssm-ID: 215272  Cd Length: 324  Bit Score: 602.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 104 EPLLRKSSRRFVIFPIQYPDIWKMYKQAQASFWTAEEVDLSKDLPHWNKLKADEKYFISHILAFFAASDGIVNENLVERF 183
Cdd:PLN02492    1 EPLLAENPDRFCMFPIKYPQIWEMYKKAEASFWTAEEVDLSADLKDWEKLTDDERHFISHVLAFFAASDGIVLENLAARF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 184 SQEVQVPEARCFYGFQILIENVHSEMYSLLIDTYIRDPKKREFLFNAIETMPYVKKKADWALRWIaDRKSTFGERVVAFA 263
Cdd:PLN02492   81 MKEVQVPEARAFYGFQIAIENIHSEMYSLLLDTYIKDPKEKDRLFNAIETIPCVAKKADWALRWI-DSSASFAERLVAFA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 264 AVEGIFFSGSFAAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQYLVNKPSEERVREIIVDAVQIEQEFLTEALP 343
Cdd:PLN02492  160 CVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLKNKLSEERVKEIVCEAVEIEKEFVCDALP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 344 VGLIGMNCILMKQYIEFVADRLLVELGFSKIFQAENPFDFMENISLEGKTNFFEKRVSEYQRFAVMAETTDN-----VFT 418
Cdd:PLN02492  240 CALVGMNADLMSQYIEFVADRLLVALGYEKVYNVVNPFDWMELISLQGKTNFFEKRVGEYQKAGVMSSLNGGgadnhVFS 319

                  ....*
gi 1622961223 419 LDADF 423
Cdd:PLN02492  320 LDEDF 324
PTZ00211 PTZ00211
ribonucleoside-diphosphate reductase small subunit; Provisional
103-423 0e+00

ribonucleoside-diphosphate reductase small subunit; Provisional


Pssm-ID: 240315 [Multi-domain]  Cd Length: 330  Bit Score: 587.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 103 EEPLLRKSSRRFVIFPIQYPDIWKMYKQAQASFWTAEEVDLSKDLPHWNKLKADEKYFISHILAFFAASDGIVNENLVER 182
Cdd:PTZ00211   11 EEPLLKENPDRFVLFPIKYPDIWRMYKKAEASFWTAEEIDLGNDLKDWEKLNDGERHFIKHVLAFFAASDGIVLENLAQR 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 183 FSQEVQVPEARCFYGFQILIENVHSEMYSLLIDTYIRDPKKREFLFNAIETMPYVKKKADWALRWIADRKStFGERVVAF 262
Cdd:PTZ00211   91 FMREVQVPEARCFYGFQIAMENIHSETYSLLIDTYITDEEEKDRLFHAIETIPAIKKKAEWAAKWINSSNS-FAERLVAF 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 263 AAVEGIFFSGSFAAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQYLVNKPSEERVREIIVDAVQIEQEFLTEAL 342
Cdd:PTZ00211  170 AAVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHTDFACLLYSHLKNKLPRERVQEIIKEAVEIEREFICDAL 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 343 PVGLIGMNCILMKQYIEFVADRLLVELGFSKIFQAENPFDFMENISLEGKTNFFEKRVSEYQRFAVMAETTDNVFTLDAD 422
Cdd:PTZ00211  250 PVDLIGMNSRLMAQYIEFVADRLLVALGVPKIYNSKNPFDWMDMISLQGKTNFFEKRVGEYQKAGVMAERTSKVFSLDAD 329

                  .
gi 1622961223 423 F 423
Cdd:PTZ00211  330 F 330
Ribonuc_red_sm pfam00268
Ribonucleotide reductase, small chain;
113-380 3.07e-157

Ribonucleotide reductase, small chain;


Pssm-ID: 425568 [Multi-domain]  Cd Length: 276  Bit Score: 444.64  E-value: 3.07e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 113 RFVIFPIQYPDIWKMYKQAQASFWTAEEVDLSKDLPHWNKLKADEKYFISHILAFFAASDGIVNENLVERFSQEVQVPEA 192
Cdd:pfam00268   1 RFNLNPIKYPEIWEFYKKLEANFWTPEEIPLSKDIKDWKKLSEDEREFIKRVLAFLALLDTLVNENLVERFSREVQTPEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 193 RCFYGFQILIENVHSEMYSLLIDTYIRDPKKREFLFNAIETMPYVKKKADWALRWIADRKSTFGERVVAFAAVEGIFFSG 272
Cdd:pfam00268  81 RAFYGFQAFMENIHSESYSYILDTLGKDPEEIDELFNWIETNPALQKKAEWILKWYQDFDSDFLERLVAFAILEGIFFYS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 273 SFAAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQYLV-------NKPSEERVREIIVDAVQIEQEFLTEALPVG 345
Cdd:pfam00268 161 GFAAILWLKRRGKMPGLAEIIELISRDEGLHGDFACLLFQHLKeenpeleTKELKEEVYDLIKEAVELEKEFLDDALPVG 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1622961223 346 LIGMNCILMKQYIEFVADRLLVELGFSKIFQAE-NP 380
Cdd:pfam00268 241 LLGMNAEDVKQYIEYVADRRLMNLGYEKLYNVEvNP 276
RNRR2 cd01049
Ribonucleotide Reductase, R2/beta subunit, ferritin-like diiron-binding domain; Ribonucleotide ...
114-389 6.90e-143

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: 408.94  E-value: 6.90e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 114 FVIFPIQYPDIWKMYKQAQASFWTAEEVDLSKDLPHWNKLKADEKYFISHILAFFAASDGIVNENLVERFSQEVQVPEAR 193
Cdd:cd01049     1 FNLNPIKYPWAWELYKKAEANFWTPEEIDLSKDLKDWEKLTEAERHFIKRVLAFLAALDSIVGENLVELFSRHVQIPEAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 194 CFYGFQILIENVHSEMYSLLIDTYIRDPkKREFLFNAIETMPYVKKKADWALRWIAD----RKSTFGERVVAFAAVEGIF 269
Cdd:cd01049    81 AFYGFQAFMENIHSESYSYILDTLGKDE-ERDELFEAIETDPALKKKADWILRWYDNlddnTKESFAERLVAFAILEGIF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 270 FSGSFAAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQYLVNK-------PSEERVREIIVDAVQIEQEFLTEAL 342
Cdd:cd01049   160 FYSGFAAIFWLARRGKMPGLAEIIELISRDESLHGDFACLLIRELLNEnpelfteEFKEEVYELIKEAVELEKEFARDLL 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1622961223 343 PVGLIGMNCILMKQYIEFVADRLLVELGFSKIF--QAENPFDFMENISL 389
Cdd:cd01049   240 PDGILGLNKEDMKQYIEYVANRRLENLGLEKLFnvEDKNPFDWMELISD 288
NrdB COG0208
Ribonucleotide reductase beta subunit, ferritin-like domain [Nucleotide transport and ...
109-415 1.12e-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: 340.99  E-value: 1.12e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 109 KSSRRFVIFPIQYPDIWKMYKQAQASFWTAEEVDLSKDLPHWNKLKADEKYFISHILAFFAASDGIVNENLVERFSQEVQ 188
Cdd:COG0208     9 LTTNRINWNPIKYPWAYELYKKQLANFWLPEEVPLSNDIKDWKKLSDDERHLIKRVLGFLTLLDSIQGNNLVLALYPHVT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 189 VPEARCFYGFQILIENVHSEMYSLLIDTYIRDPKKrefLFNAIETMPYVKKKADWALRWIADRKS-----TFGERVVAFA 263
Cdd:COG0208    89 APEVRAVLSRQAFMEAIHAKSYSYILETLGLDIDE---IFNWIEENPALQKKAEFILKYYDDLGTretkkDLLKSLVASV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 264 AVEGIFFSGSFAAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQYLVNKPSE-------ERVREIIVDAVQIEQE 336
Cdd:COG0208   166 FLEGIFFYSGFAYPLSLARRGKMKGTAEIIRLILRDESLHGNFGIYLINTIREENPElfteelkEEIYELLKEAVELEKE 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 337 FLTEALPVGLIGMNCILMKQYIEFVADRLLVELGFSKIFQ-AENPFDFMEN-ISLEGKTNFFEKRVSEYQRfAVMAETTD 414
Cdd:COG0208   246 YADDLFPDGILGLNAEDVKQYIRYIANKRLMNLGLEPLFEgDVNPFPWMSEgLDLNKKTDFFETRVTEYQK-GGVESTFD 324

                  .
gi 1622961223 415 N 415
Cdd:COG0208   325 E 325
nrdF PRK09614
ribonucleotide-diphosphate reductase subunit beta; Reviewed
118-417 1.16e-51

ribonucleotide-diphosphate reductase subunit beta; Reviewed


Pssm-ID: 236591 [Multi-domain]  Cd Length: 324  Bit Score: 176.17  E-value: 1.16e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 118 PIQYPDIWKMYKQAQASFWTAEEVDLSKDLPHWNKLKADEKYFISHILAFFAASDGIVNENLVERFSQEVQVPEARCFYG 197
Cdd:PRK09614   16 KIEDPWDYEAWKRLTANFWLPEEVPLSNDLKDWKKLSDEEKNLYTRVFGGLTLLDTLQNNNGMPNLMPDITTPEEEAVLA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 198 FQILIENVHSEMYSLLIDTyIRDPKKREFLFNAIETMPYVKKKADWALRWIADRKSTFGERVVAFAAV-EGIFFSGSFAA 276
Cdd:PRK09614   96 NIAFMEAVHAKSYSYIFST-LCSPEEIDEAFEWAEENPYLQKKADIIQDFYEPLKKKILRKAAVASVFlEGFLFYSGFYY 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 277 IFWLKKRGLMPGltfSNELIS---RDEGLHCDFACLMFQYLVNKPSE-------ERVREIIVDAVQIEQEFLTEALP-VG 345
Cdd:PRK09614  175 PLYLARQGKMTG---TAQIIRliiRDESLHGYYIGYLFQEGLEELPEleqeelkDEIYDLLYELYENEEAYTELLYDiVG 251
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622961223 346 LIGMncilMKQYIEFVADRLLVELGFSKIFQAENPFD--FMENISLEG--KTNFFEKRVSEYQRfAVMAETTDNVF 417
Cdd:PRK09614  252 LAED----VKKYIRYNANKRLMNLGLEPLFPEEEEVNpiWLNGLSNNAdeNHDFFEGKGTSYVK-GATEATEDDDW 322
PRK07209 PRK07209
ribonucleotide-diphosphate reductase subunit beta; Validated
116-404 2.94e-49

ribonucleotide-diphosphate reductase subunit beta; Validated


Pssm-ID: 235968  Cd Length: 369  Bit Score: 171.33  E-value: 2.94e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 116 IFPIQYPDIWKMYKQAQASFWTAEEVDLSKDLPHW---NKLKADEKYFISHILAFFAASDGIVNENLVERFSQEVQVPEA 192
Cdd:PRK07209   51 LVPFKYKWAWEKYLAGCANHWMPQEVNMSRDIALWkspNGLTEDERRIVKRNLGFFSTADSLVANNIVLAIYRHITNPEC 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 193 RCFYGFQILIENVHSEMYSLLIDTYIRDPKKrefLFNAIETMPYVKKKADWALRWI--------------ADRKstFGER 258
Cdd:PRK07209  131 RQYLLRQAFEEAIHTHAYQYIVESLGLDEGE---IFNMYHEVPSIRAKDEFLIPFTrsltdpnfktgtpeNDQK--LLRN 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 259 VVAFAAV-EGIFFSGSFAAIFWLKKRGLMPGLTFSNELISRDEGLHCDFAC-LMFQYLVNKPS------EERVREIIVDA 330
Cdd:PRK07209  206 LIAFYCImEGIFFYVGFTQILSLGRQNKMTGIAEQYQYILRDESMHLNFGIdLINQIKLENPHlwtaefQAEIRELIKEA 285
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622961223 331 VQIEQEFLTEALPVGLIGMNCILMKQYIEFVADRLLVELGFSKIF-QAENPFDFM-ENISLEGKTNFFEKRVSEYQ 404
Cdd:PRK07209  286 VELEYRYARDTMPRGVLGLNASMFKDYLRFIANRRLQQIGLKPQYpGTENPFPWMsEMIDLKKEKNFFETRVIEYQ 361
PRK12759 PRK12759
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional
118-404 4.16e-26

bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional


Pssm-ID: 139206 [Multi-domain]  Cd Length: 410  Bit Score: 108.96  E-value: 4.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 118 PIQYPDIWKMYKQAQASFWTAEEVDLSKDLPHWN--KLKADEKYFISHILAFFAASDGIVNENLVERFSQEVQVPEARCF 195
Cdd:PRK12759  102 PFNYPWAVDLTVKHEKAHWIEDEIDLSEDVTDWKngKITKVEKEYITNILRLFTQSDVAVGQNYYDQFIPLFKNNEIRNM 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 196 YGFQILIENVHSEMYSLLIDTY-IRDPKKREFLfnaieTMPYVKKKADWALRWIADRKSTFGERVVAFAAVEGIFFSGSF 274
Cdd:PRK12759  182 LGSFAAREGIHQRAYALLNDTLgLPDSEYHAFL-----EYKAMTDKIDFMMDADPTTRRGLGLCLAKTVFNEGVALFASF 256
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 275 AAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQ-------YLVNKPSEERVREIIVDAVQIEQEFLTEALPVGLI 347
Cdd:PRK12759  257 AMLLNFQRFGKMKGMGKVVEWSIRDESMHVEGNAALFRiycqenpYIVDNEFKKEIYLMASKAVELEDRFIELAYELGTI 336
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622961223 348 -GMNCILMKQYIEFVADRLLVELGFSKIFQAE-NPFDFMENIsLEG--KTNFFEKRVSEYQ 404
Cdd:PRK12759  337 eGLKADEVKQYIRHITDRRLNQLGLKEIYNIEkNPLTWLEWI-LNGadHTNFFENRVTEYE 396
nrdB PRK09101
ribonucleotide-diphosphate reductase subunit beta; Reviewed
135-386 5.17e-10

ribonucleotide-diphosphate reductase subunit beta; Reviewed


Pssm-ID: 181647  Cd Length: 376  Bit Score: 60.75  E-value: 5.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 135 FWTAEEVDLSKDLPHWNKLKADEKY-FISHiLAFFAASDGIVNENLVERFSQEVQVPEARCF---YGFQiliENVHSEMY 210
Cdd:PRK09101   48 FWRPEEVDVSRDRIDYQALPEHEKHiFISN-LKYQTLLDSIQGRSPNVALLPLVSIPELETWietWSFS---ETIHSRSY 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 211 SLLIDTYIRDPKKrefLFNAIETMPYVKKKA-DWA-----LRWIADRKSTFGER-----------------------VVA 261
Cdd:PRK09101  124 THIIRNIVNDPSV---VFDDIVTNEEILKRAkDISsyyddLIEMTSYYHLLGEGthtvngktvtvslrelkkklylcLMS 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 262 FAAVEGIFFSGSFAAIFWLKKRGLMPGLTFSNELISRDEGLHCDFAclmfQYLVN---------------KPSEERVREI 326
Cdd:PRK09101  201 VNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGT----QHMLNlmrsgkddpemaeiaEECKQECYDL 276
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622961223 327 IVDAVQIEQEFLTEALPVG-LIGMNCILMKQYIEFVADRLLVELGFSKIFQAE-NPFDFMEN 386
Cdd:PRK09101  277 FVQAAEQEKEWADYLFKDGsMIGLNKDILCQYVEYITNIRMQAVGLDLPFQTRsNPIPWINA 338
PRK13965 PRK13965
ribonucleotide-diphosphate reductase subunit beta; Provisional
123-378 3.23e-08

ribonucleotide-diphosphate reductase subunit beta; Provisional


Pssm-ID: 184425 [Multi-domain]  Cd Length: 335  Bit Score: 54.78  E-value: 3.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 123 DIWKMYKQaqaSFWTAEEVDLSKDLPHWNKLKADEKYFISHILAFFAASDGIvnENLVERFSqevQVPEARCFYGFQIL- 201
Cdd:PRK13965   37 EVWNRVTQ---NFWLPEKVPVSNDLNSWRSLGEDWQQLITRTFTGLTLLDTV--QATVGDVA---QIPHSQTDHEQVIYt 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 202 ----IENVHSEMYSLLIDTYIRDPKKREFLFNAIETmPYVKKKADWALRWIADRKSTfgERVVAFAAVEGIFFSGSFAAI 277
Cdd:PRK13965  109 nfafMVAIHARSYGTIFSTLCSSEQIEEAHEWVVST-ESLQRRARVLIPYYTGDDPL--KSKVAAAMMPGFLLYGGFYLP 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 278 FWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQYLVNKPSEER-------VREIIVDAVQIEQEFLTEaLPVGLIGMN 350
Cdd:PRK13965  186 FYLSARGKLPNTSDIIRLILRDKVIHNYYSGYKYQQKVARLSPEKqaemkafVFDLLYELIDLEKAYLRE-LYAGFDLAE 264
                         250       260
                  ....*....|....*....|....*...
gi 1622961223 351 CIlmKQYIEFVADRLLVELGFSKIFQAE 378
Cdd:PRK13965  265 DA--IRFSLYNAGKFLQNLGYESPFTEE 290
nrdF2 PRK13966
ribonucleotide-diphosphate reductase subunit beta; Provisional
126-375 4.13e-07

ribonucleotide-diphosphate reductase subunit beta; Provisional


Pssm-ID: 140022  Cd Length: 324  Bit Score: 51.64  E-value: 4.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 126 KMYKQAQASFWTAEEVDLSKDLPHWNKLKADEKYFISHILAFFAASDGIVNENLVERFSQEVQVPEARCFYGFQILIENV 205
Cdd:PRK13966   26 EVWDRLTGNFWLPEKVPVSNDIPSWGTLTAGEKQLTMRVFTGLTMLDTIQGTVGAVSLIPDALTPHEEAVLTNIAFMESV 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 206 HSEMYSLLIDTYIRDPKKREfLFNAIETMPYVKKKADWALRWIadRKSTFGERVVAFAAVEG-IFFSGSFAAIFWlKKRG 284
Cdd:PRK13966  106 HAKSYSQIFSTLCSTAEIDD-AFRWSEENRNLQRKAEIVLQYY--RGDEPLKRKVASTLLESfLFYSGFYLPMYW-SSRA 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 285 LMPGLTFSNELISRDEGLHCDFACLMFQY---LVNKPSEERVR----EIIVDAVQIEQEFLTEAL-PVGLIGMncilMKQ 356
Cdd:PRK13966  182 KLTNTADMIRLIIRDEAVHGYYIGYKFQRglaLVDDVTRAELKdytyELLFELYDNEVEYTQDLYdEVGLTED----VKK 257
                         250
                  ....*....|....*....
gi 1622961223 357 YIEFVADRLLVELGFSKIF 375
Cdd:PRK13966  258 FLRYNANKALMNLGYEALF 276
PRK08326 PRK08326
R2-like ligand-binding oxidase;
126-337 5.20e-07

R2-like ligand-binding oxidase;


Pssm-ID: 236242  Cd Length: 311  Bit Score: 51.15  E-value: 5.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 126 KMYKQAQASFWTAEEVDLSKDLPHWNKLKADEKYFISHILAFFAASDGIVNENLVE---------RFSQE-----VQVPE 191
Cdd:PRK08326   29 KLFAKGNAKFWNPADIDFSRDAEDWEKLSDEERDYATRLCAQFIAGEEAVTLDIQPlisamaaegRLEDEmyltqFAFEE 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 192 ARcfygfqilienvHSEMYSLLIDTYIRDPKKREFLfnaiETMPYVKK-------KADWALRwiADRKStfgERVVAFAA 264
Cdd:PRK08326  109 AK------------HTEAFRRWFDAVGVTEDLSVYT----DDNPSYRQifyeelpAALNRLS--TDPSP---ENQVRASV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 265 -----VEGIF-FSGSFAAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQYLVN------KPSEERVREIIVDAV- 331
Cdd:PRK08326  168 tynhvVEGVLaETGYYAWRKICVTRGILPGLQELVRRIGDDERRHIAWGTYTCRRLVAaddsnwDVFEERMNELLPLALg 247

                  ....*.
gi 1622961223 332 QIEQEF 337
Cdd:PRK08326  248 LIDEIF 253
nrdF1 PRK13967
ribonucleotide-diphosphate reductase subunit beta; Provisional
126-303 2.92e-06

ribonucleotide-diphosphate reductase subunit beta; Provisional


Pssm-ID: 140023  Cd Length: 322  Bit Score: 48.96  E-value: 2.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 126 KMYKQAQASFWTAEEVDLSKDLPHWNKLKADEKYFISHILAFFAASDGIVNENLVERFSQEVQVPEARCFYGFQILIENV 205
Cdd:PRK13967   24 QVWERLTGNFWLPEKIPLSNDLASWQTLSSTEQQTTIRVFTGLTLLDTAQATVGAVAMIDDAVTPHEEAVLTNMAFMESV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 206 HSEMYSLLIDTyIRDPKKREFLFNAIETMPYVKKKADWALRWIadRKSTFGERVVAFAAVEG-IFFSGSFAAIFWlKKRG 284
Cdd:PRK13967  104 HAKSYSSIFST-LCSTKQIDDAFDWSEQNPYLQRKAQIIVDYY--RGDDALKRKASSVMLESfLFYSGFYLPMYW-SSRG 179
                         170
                  ....*....|....*....
gi 1622961223 285 LMPGLTFSNELISRDEGLH 303
Cdd:PRK13967  180 KLTNTADLIRLIIRDEAVH 198
RNRR2_Rv0233_like cd07911
Ribonucleotide Reductase R2-like protein, Mn/Fe-binding domain; Rv0233 is a Mycobacterium ...
126-329 2.04e-04

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: 42.71  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 126 KMYKQAQA-SFWTAEEVDLSKDLPHWNKLKADEKYFISHILAFFAASDGIVNENLVE---------RFSQEVqvpearcf 195
Cdd:cd07911    11 KLFEKGKRkGFWNPADIDFSQDREDWEQLSEEERDLALRLCAGFIAGEEAVTLDLLPlmmamaaegRLEEEM-------- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622961223 196 YGFQILIENV-HSEMYSLLID---------TYIRDPKKREF---LFNAIEtmpyvKKKADWALRWIADRKSTFGERVVAF 262
Cdd:cd07911    83 YLTQFLFEEAkHTDFFRRWLDavgvsddlsDLHTAVYREPFyeaLPYAEL-----RLYLDASPAAQVRASVTYNMIVEGV 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622961223 263 AAVEGIFfsgSFAAIfwLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQYLVNkpSEERVREIIVD 329
Cdd:cd07911   158 LAETGYY---AWRTI--CEKRGILPGMQEGIRRLGDDESRHIAWGTFTCRRLVA--ADDANWDVFEE 217
 
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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