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Conserved domains on  [gi|612907271|gb|EZV18923|]
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anaerobic ribonucleoside-triphosphate reductase activating protein [Staphylococcus aureus 12S00881]

Protein Classification

4Fe-4S single cluster domain-containing protein( domain architecture ID 12135473)

4Fe-4S single cluster domain-containing protein binds iron-sulfur clusters

Gene Ontology:  GO:0051539
PubMed:  29601957

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
 22-161 8.79e-67

4Fe-4S single cluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


:

Pssm-ID: 433138 [Multi-domain]  Cd Length: 137  Bit Score: 200.09  E-value: 8.79e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907271   22 VDGEGVRCSVYVSGCPFNCVGCYNKASQKFRYGEKYTDEILAEILDDCDHDYISGLSLLGGEPFCNLDITLNLVKAFRAR 101
Cdd:pfam13353   1 VNGPGVRCSLFVSGCNHHCKGCFNPETWDFKYGKPFTEELEDEIIEDLAKPYIQGLTLSGGEPLLNAEALLELVKRVREE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907271  102 FGNtKTIWVWTGFLYEYLANDctERRELLSYIDVLVDGLFIQHLFKPDLPYKGSLNQRII 161
Cdd:pfam13353  81 CPE-KDIWLWTGYTFEELQSK--DQLELLKLIDVLVDGKFEQSLKDPSLRFRGSSNQRII 137
 
Name Accession Description Interval E-value
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
 22-161 8.79e-67

4Fe-4S single cluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 433138 [Multi-domain]  Cd Length: 137  Bit Score: 200.09  E-value: 8.79e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907271   22 VDGEGVRCSVYVSGCPFNCVGCYNKASQKFRYGEKYTDEILAEILDDCDHDYISGLSLLGGEPFCNLDITLNLVKAFRAR 101
Cdd:pfam13353   1 VNGPGVRCSLFVSGCNHHCKGCFNPETWDFKYGKPFTEELEDEIIEDLAKPYIQGLTLSGGEPLLNAEALLELVKRVREE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907271  102 FGNtKTIWVWTGFLYEYLANDctERRELLSYIDVLVDGLFIQHLFKPDLPYKGSLNQRII 161
Cdd:pfam13353  81 CPE-KDIWLWTGYTFEELQSK--DQLELLKLIDVLVDGKFEQSLKDPSLRFRGSSNQRII 137
NrdG TIGR02491
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
 12-163 2.13e-55

anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of the radical-SAM family (pfam04055) and utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487). The two components form an alpha-2/beta-2 heterodimer. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism, Protein fate, Protein modification and repair]


Pssm-ID: 274161 [Multi-domain]  Cd Length: 154  Bit Score: 171.76  E-value: 2.13e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907271   12 YIAKIESNSFVDGEGVRCSVYVSGCPFNCVGCYNKASQKFRYGEKYTDEILAEILDDC-DHDYISGLSLLGGEPF--CNL 88
Cdd:TIGR02491   1 NYMNIKPDDIVNGEGIRVSLFVAGCKHHCEGCFNKETWNFNGGKEFTEALEKEIIRDLnDNPLIDGLTLSGGDPLypRNV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612907271   89 DITLNLVKAFRARFGNtKTIWVWTGFLYEYLANDcTERRELLSYIDVLVDGLFIQHLFKPDLPYKGSLNQRIIDV 163
Cdd:TIGR02491  81 EELIELVKKIKAEFPE-KDIWLWTGYTWEEILED-EKHLEVLKYIDVLVDGKFELSKKDLKLKFRGSSNQRIIDL 153
nrdG PRK11121
anaerobic ribonucleoside-triphosphate reductase-activating protein;
22-160 3.17e-40

anaerobic ribonucleoside-triphosphate reductase-activating protein;


Pssm-ID: 236853  Cd Length: 154  Bit Score: 133.19  E-value: 3.17e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907271  22 VDGEGVRCSVYVSGCPFNCVGCYNKASQKFRYGEKYTDEILAEILDDCDHDYI--SGLSLLGGEPF--CNLDITLNLVKA 97
Cdd:PRK11121  12 VNGPGTRCTLFVSGCVHQCPGCYNKSTWRLNSGHPFTKEMEDQIIADLNDTRIkrQGLSLSGGDPLhpQNVPDILKLVQR 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612907271  98 FRARFGNtKTIWVWTGFLYEYLANdctERRELLSYIDVLVDGLFIQHLFKPDLPYKGSLNQRI 160
Cdd:PRK11121  92 VKAECPG-KDIWVWTGYKLDELNA---AQRQVVDLIDVLVDGKFVQDLADPSLIWRGSSNQVI 150
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
 10-138 1.93e-18

Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 79.46  E-value: 1.93e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907271  10 QGYIAKIESNSFVDGEG-VRCSVYVSGCPFNCVGCYNKASQKFR---YGEKYT-DEILAEILDDCDH-DYISGLSLLGGE 83
Cdd:COG1180    4 RGRIYGISPFSTVDGPGsIRLSVFTQGCNLRCPYCHNPEISQGRpdaAGRELSpEELVEEALKDRGFlDSCGGVTFSGGE 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 612907271  84 PFCNLDITLNLVKAFRARfgNTKTIWVWTGFL-YEYLandcterRELLSYID-VLVD 138
Cdd:COG1180   84 PTLQPEFLLDLAKLAKEL--GLHTALDTNGYIpEEAL-------EELLPYLDaVNID 131
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 35-153 3.81e-06

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 45.40  E-value: 3.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907271  35 GCPFNCVGCYNKASQKFRYGEKYTDEILAEILDDCDHDYISGLSLLGGEPFCNLDItLNLVKAFRARFGNTKTIWVWTGF 114
Cdd:cd01335    6 GCNLNCGFCSNPASKGRGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYPEL-AELLRRLKKELPGFEISIETNGT 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 612907271 115 LYEY-LANDCteRRELLSYIDVLVDGLFIQHLFKPDLPYK 153
Cdd:cd01335   85 LLTEeLLKEL--KELGLDGVGVSLDSGDEEVADKIRGSGE 122
 
Name Accession Description Interval E-value
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
 22-161 8.79e-67

4Fe-4S single cluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 433138 [Multi-domain]  Cd Length: 137  Bit Score: 200.09  E-value: 8.79e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907271   22 VDGEGVRCSVYVSGCPFNCVGCYNKASQKFRYGEKYTDEILAEILDDCDHDYISGLSLLGGEPFCNLDITLNLVKAFRAR 101
Cdd:pfam13353   1 VNGPGVRCSLFVSGCNHHCKGCFNPETWDFKYGKPFTEELEDEIIEDLAKPYIQGLTLSGGEPLLNAEALLELVKRVREE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907271  102 FGNtKTIWVWTGFLYEYLANDctERRELLSYIDVLVDGLFIQHLFKPDLPYKGSLNQRII 161
Cdd:pfam13353  81 CPE-KDIWLWTGYTFEELQSK--DQLELLKLIDVLVDGKFEQSLKDPSLRFRGSSNQRII 137
NrdG TIGR02491
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
 12-163 2.13e-55

anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of the radical-SAM family (pfam04055) and utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487). The two components form an alpha-2/beta-2 heterodimer. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism, Protein fate, Protein modification and repair]


Pssm-ID: 274161 [Multi-domain]  Cd Length: 154  Bit Score: 171.76  E-value: 2.13e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907271   12 YIAKIESNSFVDGEGVRCSVYVSGCPFNCVGCYNKASQKFRYGEKYTDEILAEILDDC-DHDYISGLSLLGGEPF--CNL 88
Cdd:TIGR02491   1 NYMNIKPDDIVNGEGIRVSLFVAGCKHHCEGCFNKETWNFNGGKEFTEALEKEIIRDLnDNPLIDGLTLSGGDPLypRNV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612907271   89 DITLNLVKAFRARFGNtKTIWVWTGFLYEYLANDcTERRELLSYIDVLVDGLFIQHLFKPDLPYKGSLNQRIIDV 163
Cdd:TIGR02491  81 EELIELVKKIKAEFPE-KDIWLWTGYTWEEILED-EKHLEVLKYIDVLVDGKFELSKKDLKLKFRGSSNQRIIDL 153
nrdG PRK11121
anaerobic ribonucleoside-triphosphate reductase-activating protein;
22-160 3.17e-40

anaerobic ribonucleoside-triphosphate reductase-activating protein;


Pssm-ID: 236853  Cd Length: 154  Bit Score: 133.19  E-value: 3.17e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907271  22 VDGEGVRCSVYVSGCPFNCVGCYNKASQKFRYGEKYTDEILAEILDDCDHDYI--SGLSLLGGEPF--CNLDITLNLVKA 97
Cdd:PRK11121  12 VNGPGTRCTLFVSGCVHQCPGCYNKSTWRLNSGHPFTKEMEDQIIADLNDTRIkrQGLSLSGGDPLhpQNVPDILKLVQR 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612907271  98 FRARFGNtKTIWVWTGFLYEYLANdctERRELLSYIDVLVDGLFIQHLFKPDLPYKGSLNQRI 160
Cdd:PRK11121  92 VKAECPG-KDIWVWTGYKLDELNA---AQRQVVDLIDVLVDGKFVQDLADPSLIWRGSSNQVI 150
Fer4_14 pfam13394
4Fe-4S single cluster domain;
31-139 8.29e-32

4Fe-4S single cluster domain;


Pssm-ID: 433171 [Multi-domain]  Cd Length: 115  Bit Score: 110.53  E-value: 8.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907271   31 VYVSGCPFNCVGCYNKASQKFRYGEKYTDEILAEILDDCDHDYI--SGLSLLGGEPFC--NLDITLNLVKAFRARFGnTK 106
Cdd:pfam13394   1 LFVSGCNHSCPGCDNKETWKFNYGEPFTEELEDQIIADLKDSYIkrQGLVLTGGEPLHpwNLPVLLKLLKRVKEEYP-SK 79

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 612907271  107 TIWVWTGFLY--EYLANDCTERRELLSYIDVLVDG 139
Cdd:pfam13394  80 DIWLETGYTLaiDFEYPDTEEQLFTLSVIDVLVDG 114
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
 10-138 1.93e-18

Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 79.46  E-value: 1.93e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907271  10 QGYIAKIESNSFVDGEG-VRCSVYVSGCPFNCVGCYNKASQKFR---YGEKYT-DEILAEILDDCDH-DYISGLSLLGGE 83
Cdd:COG1180    4 RGRIYGISPFSTVDGPGsIRLSVFTQGCNLRCPYCHNPEISQGRpdaAGRELSpEELVEEALKDRGFlDSCGGVTFSGGE 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 612907271  84 PFCNLDITLNLVKAFRARfgNTKTIWVWTGFL-YEYLandcterRELLSYID-VLVD 138
Cdd:COG1180   84 PTLQPEFLLDLAKLAKEL--GLHTALDTNGYIpEEAL-------EELLPYLDaVNID 131
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
 35-108 1.05e-06

Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation.


Pssm-ID: 427681 [Multi-domain]  Cd Length: 159  Bit Score: 46.37  E-value: 1.05e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612907271   35 GCPFNCVGCYNKASQKFRYGEKYTDEILAEILDDCDHDYISGLSLLGGEPFCNLDITLNLVKAFRARFGNTKTI 108
Cdd:pfam04055   4 GCNLRCTYCAFPSIRARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLELAEGIRI 77
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 35-153 3.81e-06

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 45.40  E-value: 3.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907271  35 GCPFNCVGCYNKASQKFRYGEKYTDEILAEILDDCDHDYISGLSLLGGEPFCNLDItLNLVKAFRARFGNTKTIWVWTGF 114
Cdd:cd01335    6 GCNLNCGFCSNPASKGRGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYPEL-AELLRRLKKELPGFEISIETNGT 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 612907271 115 LYEY-LANDCteRRELLSYIDVLVDGLFIQHLFKPDLPYK 153
Cdd:cd01335   85 LLTEeLLKEL--KELGLDGVGVSLDSGDEEVADKIRGSGE 122
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
 36-101 1.12e-05

Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, chromosome partitioning, Coenzyme transport and metabolism];


Pssm-ID: 440301 [Multi-domain]  Cd Length: 159  Bit Score: 43.35  E-value: 1.12e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612907271  36 CPFNCVGCYNKASQKFRygEKYTDEILAEILDDCDHDYISGLSLLGGEPFCNLDItLNLVKAFRAR 101
Cdd:COG0535   10 CNLRCKHCYADAGPKRP--GELSTEEAKRILDELAELGVKVVGLTGGEPLLRPDL-FELVEYAKEL 72
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
 24-101 9.00e-05

Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic radical activating enzyme NrdG/QueE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440367 [Multi-domain]  Cd Length: 205  Bit Score: 41.28  E-value: 9.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907271  24 GEGVRC---SVYV--SGCPFNCVGCYNKASQKFRYGEKYTDEILAEILDDCDHDYIsglSLLGGEPFCNLDITLnLVKAF 98
Cdd:COG0602   13 GEGALAgrpAVFVrlAGCNLRCSWCDTKYAWDGEGGKRMSAEEILEEVAALGARHV---VITGGEPLLQDDLAE-LLEAL 88


                 ...
gi 612907271  99 RAR 101
Cdd:COG0602   89 KDA 91
NrdG2 TIGR02495
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
 13-84 2.07e-04

anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of the radical-SAM family (pfam04055). It is often gene clustered with the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487) and presumably fulfills the identical function as NrdG, which utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in NrdD. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism, Protein fate, Protein modification and repair]


Pssm-ID: 274164 [Multi-domain]  Cd Length: 192  Bit Score: 40.04  E-value: 2.07e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612907271   13 IAKIESNSFVDGEG-VRCSVYVSGCPFNCVGCYNKASQKFRYGEKYTDEILAEILDDcDHDYISGLSLLGGEP 84
Cdd:TIGR02495   2 IAGLVPFSTVDYPGkLAFTIFLQGCNLKCPYCHNPLLIPRRGSGEIEVEELLEFLRR-RRGLLDGVVITGGEP 73
pflA PRK11145
pyruvate formate lyase 1-activating protein;
11-67 7.67e-03

pyruvate formate lyase 1-activating protein;


Pssm-ID: 182994 [Multi-domain]  Cd Length: 246  Bit Score: 35.77  E-value: 7.67e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 612907271  11 GYIAKIESNSFVDGEGVRCSVYVSGCPFNCVGCYNKASQKFRYGEKYT-DEILAEILD 67
Cdd:PRK11145   5 GRIHSFESCGTVDGPGIRFITFFQGCLMRCLYCHNRDTWDTHGGKEVTvEELMKEVVT 62
 
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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