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Conserved domains on  [gi|445990118|ref|WP_000067973|]
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MULTISPECIES: pyruvate formate lyase 1-activating protein [Salmonella]

Protein Classification

pyruvate formate lyase 1-activating protein( domain architecture ID 11485227)

pyruvate formate lyase 1-activating protein is a radical SAM protein that activates pyruvate formate-lyase 1 under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
pflA PRK11145
pyruvate formate lyase 1-activating protein;
22-265 0e+00

pyruvate formate lyase 1-activating protein;


:

Pssm-ID: 182994 [Multi-domain]  Cd Length: 246  Bit Score: 570.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118  22 VIGRIHSFESCGTVDGPGIRFITFFQGCLMRCLYCHNRDTWDTHGGKEITVEDLMKEVVTYRHFMNASGGGVTASGGEAI 101
Cdd:PRK11145   3 VIGRIHSFESCGTVDGPGIRFITFFQGCLMRCLYCHNRDTWDTHGGKEVTVEELMKEVVTYRHFMNASGGGVTASGGEAI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118 102 LQAEFVRDWFRACKKEGIHTCLDTNGFVRRYDPVIDELLDVTDLVMLDLKQMNDEIHQNLVGVSNHRTLEFAQYLSKKNV 181
Cdd:PRK11145  83 LQAEFVRDWFRACKKEGIHTCLDTNGFVRRYDPVIDELLDVTDLVMLDLKQMNDEIHQNLVGVSNHRTLEFARYLAKRNQ 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118 182 KVWIRYVVVPGWSDDDDSAHRLGEFTRDMGNVEKIELLPYHELGKHKWVAMGEEYKLDGVKPPKKETMERVKGILEQYGH 261
Cdd:PRK11145 163 KTWIRYVVVPGWTDDDDSAHRLGEFIKDMGNIEKIELLPYHELGKHKWEAMGEEYKLDGVKPPSKETMERVKGILEQYGH 242

                 ....
gi 445990118 262 KVMY 265
Cdd:PRK11145 243 KVMY 246
 
Name Accession Description Interval E-value
pflA PRK11145
pyruvate formate lyase 1-activating protein;
22-265 0e+00

pyruvate formate lyase 1-activating protein;


Pssm-ID: 182994 [Multi-domain]  Cd Length: 246  Bit Score: 570.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118  22 VIGRIHSFESCGTVDGPGIRFITFFQGCLMRCLYCHNRDTWDTHGGKEITVEDLMKEVVTYRHFMNASGGGVTASGGEAI 101
Cdd:PRK11145   3 VIGRIHSFESCGTVDGPGIRFITFFQGCLMRCLYCHNRDTWDTHGGKEVTVEELMKEVVTYRHFMNASGGGVTASGGEAI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118 102 LQAEFVRDWFRACKKEGIHTCLDTNGFVRRYDPVIDELLDVTDLVMLDLKQMNDEIHQNLVGVSNHRTLEFAQYLSKKNV 181
Cdd:PRK11145  83 LQAEFVRDWFRACKKEGIHTCLDTNGFVRRYDPVIDELLDVTDLVMLDLKQMNDEIHQNLVGVSNHRTLEFARYLAKRNQ 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118 182 KVWIRYVVVPGWSDDDDSAHRLGEFTRDMGNVEKIELLPYHELGKHKWVAMGEEYKLDGVKPPKKETMERVKGILEQYGH 261
Cdd:PRK11145 163 KTWIRYVVVPGWTDDDDSAHRLGEFIKDMGNIEKIELLPYHELGKHKWEAMGEEYKLDGVKPPSKETMERVKGILEQYGH 242

                 ....
gi 445990118 262 KVMY 265
Cdd:PRK11145 243 KVMY 246
PFLA TIGR02493
pyruvate formate-lyase 1-activating enzyme; An iron-sulfur protein with a radical-SAM domain ...
25-259 7.40e-146

pyruvate formate-lyase 1-activating enzyme; An iron-sulfur protein with a radical-SAM domain (pfam04055). A single glycine residue in EC 2.3.1.54, formate C-acetyltransferase (formate-pyruvate lyase), is oxidized to the corresponding radical by transfer of H from its CH2 to AdoMet with concomitant cleavage of the latter. The reaction requires Fe2+. The first stage is reduction of the AdoMet to give methionine and the 5'-deoxyadenosin-5-yl radical, which then abstracts a hydrogen radical from the glycine residue. [Energy metabolism, Anaerobic, Protein fate, Protein modification and repair]


Pssm-ID: 131546 [Multi-domain]  Cd Length: 235  Bit Score: 407.52  E-value: 7.40e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118   25 RIHSFESCGTVDGPGIRFITFFQGCLMRCLYCHNRDTWDTHGGKEITVEDLMKEVVTYRHFMNASGGGVTASGGEAILQA 104
Cdd:TIGR02493   1 RIHSTESMGTVDGPGIRFVVFMQGCPLRCQYCHNPDTWDLKGGTEVTPEELIKEVGSYKDFFKASGGGVTFSGGEPLLQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118  105 EFVRDWFRACKKEGIHTCLDTNGFVRRYDPVIDELLDVTDLVMLDLKQMNDEIHQNLVGVSNHRTLEFAQYLSKKNVKVW 184
Cdd:TIGR02493  81 EFLSELFKACKELGIHTCLDTSGFLGGCTEAADELLEYTDLVLLDIKHFNPEKYKKLTGVSLQPTLDFAKYLAKRNKPIW 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445990118  185 IRYVVVPGWSDDDDSAHRLGEFTRDMGNVEKIELLPYHELGKHKWVAMGEEYKLDGVKPPKKETMERVKGILEQY 259
Cdd:TIGR02493 161 IRYVLVPGYTDSEEDIEALAEFVKTLPNVERVEVLPYHQLGVYKWEALGIEYPLEGVKPPNKEQLERAAEIFKEY 235
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
20-262 2.93e-101

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 295.17  E-value: 2.93e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118  20 KPVIGRIHSFESCGTVDGPG-IRFITFFQGCLMRCLYCHNRDTWDTH---GGKEITVEDLMKEVVTYRHFMNaSGGGVTA 95
Cdd:COG1180    1 EEVRGRIYGISPFSTVDGPGsIRLSVFTQGCNLRCPYCHNPEISQGRpdaAGRELSPEELVEEALKDRGFLD-SCGGVTF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118  96 SGGEAILQAEFVRDWFRACKKEGIHTCLDTNGFVrrYDPVIDELLDVTDLVMLDLKQMNDEIHQNLVGVSNHRTLEFAQY 175
Cdd:COG1180   80 SGGEPTLQPEFLLDLAKLAKELGLHTALDTNGYI--PEEALEELLPYLDAVNIDLKAFDDEFYRKLTGVSLEPVLENLEL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118 176 LSKKNVKVWIRYVVVPGWSDDDDSAHRLGEFTRDMGNVEKIELLPYHELgkhkwvamgeeYKLDGVKPPKKETMERVKGI 255
Cdd:COG1180  158 LAESGVHVEIRTLVIPGLNDSEEELEAIARFIAELGDVIPVHLLPFHPL-----------YKLEDVPPPSPETLERAREI 226

                 ....*..
gi 445990118 256 LEQYGHK 262
Cdd:COG1180  227 AREYGLK 233
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
45-197 2.14e-19

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: 82.19  E-value: 2.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118   45 FFQGCLMRCLYCHNRDTWDTHGGKEITVEDLMKEVVTYRhfmNASGGGVTASGGEAILQAEFVRDWFRACKK---EGIHT 121
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKGRELSPEEILEEAKELK---RLGVEVVILGGGEPLLLPDLVELLERLLKLelaEGIRI 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445990118  122 CLDTNGFVRRYDpVIDELLDVT-DLVMLDLKQMNDEIHQNL-VGVSNHRTLEFAQYLSKKNVKV-WIRYVVVPGWSDDD 197
Cdd:pfam04055  78 TLETNGTLLDEE-LLELLKEAGlDRVSIGLESGDDEVLKLInRGHTFEEVLEALELLREAGIPVvTDNIVGLPGETDED 155
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
43-227 1.39e-10

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: 59.27  E-value: 1.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118  43 ITFFQGCLMRCLYCHNRdtWDTHGG-KEITVEDLMKEVVTYRHFMNASGggVTASGGEAILQAEFVRDWFRACK-KEGIH 120
Cdd:cd01335    1 LELTRGCNLNCGFCSNP--ASKGRGpESPPEIEEILDIVLEAKERGVEV--VILTGGEPLLYPELAELLRRLKKeLPGFE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118 121 TCLDTNGFVRRYDPV--IDELLDVTDLVMLDLKqmnDEIHQNLVGVSNH---RTLEFAQYLSKKNVKVWIRYVVVPGWSD 195
Cdd:cd01335   77 ISIETNGTLLTEELLkeLKELGLDGVGVSLDSG---DEEVADKIRGSGEsfkERLEALKELREAGLGLSTTLLVGLGDED 153
                        170       180       190
                 ....*....|....*....|....*....|..
gi 445990118 196 DDDSAhRLGEFTRDMGNVEKIELLPYHELGKH 227
Cdd:cd01335  154 EEDDL-EELELLAEFRSPDRVSLFRLLPEEGT 184
viperin_w_prok NF038283
viperin family antiviral radical SAM protein; Homologs of a viral defense radical SAM enzyme ...
49-137 8.15e-04

viperin family antiviral radical SAM protein; Homologs of a viral defense radical SAM enzyme found in Homo sapiens, viperin (RSAD2), occur in prokaryotes with a strong bias toward placement in phage defense islands, encoded next to CRISPR system and restriction enzyme genes. Further investigation shows members indeed perform the anti-viral function of synthesizing modified ribonucleotides such as ddhCTP, ddh-guanosine triphosphate (ddhGTP) and ddh-uridine triphosphate (ddhUTP). Those non-standard ribonucleotides can interfere with viral replication machinery.


Pssm-ID: 468450 [Multi-domain]  Cd Length: 280  Bit Score: 39.84  E-value: 8.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118  49 CLMRCLYC--HNRDTWDTHGGKEITVEDLMKEVVTYRHFMNASGGGVTASGGEAILQAEFVRDWFRACKKEGIHTCLDTN 126
Cdd:NF038283  12 CNYRCKYCfaKWNDVKSPRHHDKGHLEKLLEELAEFFKLLSYGFVRINFAGGEPLLYPDRLLDLIKLAKELGFKTSIITN 91
                         90
                 ....*....|....*..
gi 445990118 127 G------FVRRYDPVID 137
Cdd:NF038283  92 GsllteeFLEELAPYLD 108
 
Name Accession Description Interval E-value
pflA PRK11145
pyruvate formate lyase 1-activating protein;
22-265 0e+00

pyruvate formate lyase 1-activating protein;


Pssm-ID: 182994 [Multi-domain]  Cd Length: 246  Bit Score: 570.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118  22 VIGRIHSFESCGTVDGPGIRFITFFQGCLMRCLYCHNRDTWDTHGGKEITVEDLMKEVVTYRHFMNASGGGVTASGGEAI 101
Cdd:PRK11145   3 VIGRIHSFESCGTVDGPGIRFITFFQGCLMRCLYCHNRDTWDTHGGKEVTVEELMKEVVTYRHFMNASGGGVTASGGEAI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118 102 LQAEFVRDWFRACKKEGIHTCLDTNGFVRRYDPVIDELLDVTDLVMLDLKQMNDEIHQNLVGVSNHRTLEFAQYLSKKNV 181
Cdd:PRK11145  83 LQAEFVRDWFRACKKEGIHTCLDTNGFVRRYDPVIDELLDVTDLVMLDLKQMNDEIHQNLVGVSNHRTLEFARYLAKRNQ 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118 182 KVWIRYVVVPGWSDDDDSAHRLGEFTRDMGNVEKIELLPYHELGKHKWVAMGEEYKLDGVKPPKKETMERVKGILEQYGH 261
Cdd:PRK11145 163 KTWIRYVVVPGWTDDDDSAHRLGEFIKDMGNIEKIELLPYHELGKHKWEAMGEEYKLDGVKPPSKETMERVKGILEQYGH 242

                 ....
gi 445990118 262 KVMY 265
Cdd:PRK11145 243 KVMY 246
PFLA TIGR02493
pyruvate formate-lyase 1-activating enzyme; An iron-sulfur protein with a radical-SAM domain ...
25-259 7.40e-146

pyruvate formate-lyase 1-activating enzyme; An iron-sulfur protein with a radical-SAM domain (pfam04055). A single glycine residue in EC 2.3.1.54, formate C-acetyltransferase (formate-pyruvate lyase), is oxidized to the corresponding radical by transfer of H from its CH2 to AdoMet with concomitant cleavage of the latter. The reaction requires Fe2+. The first stage is reduction of the AdoMet to give methionine and the 5'-deoxyadenosin-5-yl radical, which then abstracts a hydrogen radical from the glycine residue. [Energy metabolism, Anaerobic, Protein fate, Protein modification and repair]


Pssm-ID: 131546 [Multi-domain]  Cd Length: 235  Bit Score: 407.52  E-value: 7.40e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118   25 RIHSFESCGTVDGPGIRFITFFQGCLMRCLYCHNRDTWDTHGGKEITVEDLMKEVVTYRHFMNASGGGVTASGGEAILQA 104
Cdd:TIGR02493   1 RIHSTESMGTVDGPGIRFVVFMQGCPLRCQYCHNPDTWDLKGGTEVTPEELIKEVGSYKDFFKASGGGVTFSGGEPLLQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118  105 EFVRDWFRACKKEGIHTCLDTNGFVRRYDPVIDELLDVTDLVMLDLKQMNDEIHQNLVGVSNHRTLEFAQYLSKKNVKVW 184
Cdd:TIGR02493  81 EFLSELFKACKELGIHTCLDTSGFLGGCTEAADELLEYTDLVLLDIKHFNPEKYKKLTGVSLQPTLDFAKYLAKRNKPIW 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445990118  185 IRYVVVPGWSDDDDSAHRLGEFTRDMGNVEKIELLPYHELGKHKWVAMGEEYKLDGVKPPKKETMERVKGILEQY 259
Cdd:TIGR02493 161 IRYVLVPGYTDSEEDIEALAEFVKTLPNVERVEVLPYHQLGVYKWEALGIEYPLEGVKPPNKEQLERAAEIFKEY 235
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
20-262 2.93e-101

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 295.17  E-value: 2.93e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118  20 KPVIGRIHSFESCGTVDGPG-IRFITFFQGCLMRCLYCHNRDTWDTH---GGKEITVEDLMKEVVTYRHFMNaSGGGVTA 95
Cdd:COG1180    1 EEVRGRIYGISPFSTVDGPGsIRLSVFTQGCNLRCPYCHNPEISQGRpdaAGRELSPEELVEEALKDRGFLD-SCGGVTF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118  96 SGGEAILQAEFVRDWFRACKKEGIHTCLDTNGFVrrYDPVIDELLDVTDLVMLDLKQMNDEIHQNLVGVSNHRTLEFAQY 175
Cdd:COG1180   80 SGGEPTLQPEFLLDLAKLAKELGLHTALDTNGYI--PEEALEELLPYLDAVNIDLKAFDDEFYRKLTGVSLEPVLENLEL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118 176 LSKKNVKVWIRYVVVPGWSDDDDSAHRLGEFTRDMGNVEKIELLPYHELgkhkwvamgeeYKLDGVKPPKKETMERVKGI 255
Cdd:COG1180  158 LAESGVHVEIRTLVIPGLNDSEEELEAIARFIAELGDVIPVHLLPFHPL-----------YKLEDVPPPSPETLERAREI 226

                 ....*..
gi 445990118 256 LEQYGHK 262
Cdd:COG1180  227 AREYGLK 233
PFLE_PFLC TIGR02494
glycyl-radical enzyme activating protein; This subset of the radical-SAM family (pfam04055) ...
36-260 4.04e-64

glycyl-radical enzyme activating protein; This subset of the radical-SAM family (pfam04055) includes a number of probable activating proteins acting on different enzymes all requiring an amino-acid-centered radical. The closest relatives to this family are the pyruvate-formate lyase activating enzyme (PflA, 1.97.1.4, TIGR02493) and the anaerobic ribonucleotide reductase activating enzyme (TIGR02491). Included within this subfamily are activators of hydroxyphenyl acetate decarboxylase (HdpA), benzylsuccinate synthase (BssD), gycerol dehydratase (DhaB2) as well as enzymes annotated in E. coli as activators of different isozymes of pyruvate-formate lyase (PFLC and PFLE) however, these appear to lack characterization and may activate enzymes with distinctive functions. Most of the sequence-level variability between these forms is concentrated within an N-terminal domain which follows a conserved group of three cysteines and contains a variable pattern of 0 to 8 additional cysteines.


Pssm-ID: 274163 [Multi-domain]  Cd Length: 295  Bit Score: 202.18  E-value: 4.04e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118   36 DGPGIRFITFFQGCLMRCLYCHNRDTWD----------------------------------------------THG--- 66
Cdd:TIGR02494  11 DGPGIRTTVFLKGCPLRCKWCSNPESQRkspellfkenrclgcgkcvevcpagtarlseladgrnriiirrekcTHCgkc 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118   67 ------------GKEITVEDLMKEVVTYRHFMNASGGGVTASGGEAILQAEFVRDWFRACKKEGIHTCLDTNGFVRRydP 134
Cdd:TIGR02494  91 teacpsgalsivGEEMTVEEVMRVVLRDSIFYRNSGGGVTLSGGEPLLQPEFALALLQACHERGIHTAVETSGFTPW--E 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118  135 VIDELLDVTDLVMLDLKQMNDEIHQNLVGVSNHRTLEFAQYLSKKNVKVWIRYVVVPGWSDDDDSAHRLGEFTRDMGN-V 213
Cdd:TIGR02494 169 TIEKVLPYVDLFLFDIKHLDDERHKEVTGVDNEPILENLEALAAAGKNVVIRIPVIPGFNDSEENIEAIAAFLRKLEPgV 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 445990118  214 EKIELLPYHELGKHKWVAMGEEYKLDGVKPPKKETMERVKGILEQYG 260
Cdd:TIGR02494 249 DEIDLLPYHRLGENKYRQLGREYPDSEIPDPAEEQLLELKEIFESKG 295
activase_YjjW TIGR04041
glycine radical enzyme activase, YjjW family; Members of this family are radical SAM enzymes, ...
22-260 1.53e-49

glycine radical enzyme activase, YjjW family; Members of this family are radical SAM enzymes, designated YjjW in E. coli, that are paired with and appear to activate a glycyl radical enzyme of unknown function, designated YjjI. This activase and its target are found in Clostridial species as well as E. coli and cousins. Members of this family may be misannotated as pyruvate formate lyase activating enzyme. [Protein fate, Protein modification and repair]


Pssm-ID: 274938 [Multi-domain]  Cd Length: 276  Bit Score: 164.34  E-value: 1.53e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118   22 VIGRIHSFeSCgtVDGPGIRFITFFQGCLMRCLYCHNRDTWDT------------------HGGK--------------- 68
Cdd:TIGR04041   3 LVNKIIPF-SC--VDGPGNRLAIFLQGCNFDCKYCHNPETINHcdhcgdcvagcpagalslVDGKvvwdkercigcdtci 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118   69 ------------EITVEDLMKEVVTYRHFMNasggGVTASGGEAILQAEFVRDWFRACKKEGIhTCL-DTNGFV--RRYd 133
Cdd:TIGR04041  80 kvcphqsspktkEYTVEELLDRIRKNMPFIR----GITVSGGECTLQLDFLTELFKAIKAAGL-TCFiDSNGSLdlTGW- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118  134 pviDELLDVTDLVMLDLKQMNDEIHQNLVGVSNHRTLEFAQYLSKKNVKVWIRYVVVPGWSDDDDSAHRLGEFTRDMGNV 213
Cdd:TIGR04041 154 ---PKLLPVLDGAMLDLKAWDSETHRWLTGRDNHRVLKNIRFLAELGKLYEVRLVHIPGLSDLEQEIDGLARFLGDLPSD 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 445990118  214 EKIELLPYHELGkhkwvaMGEEYKldGVKPPKKETMERVKGILEQYG 260
Cdd:TIGR04041 231 TRIKLIAFRHHG------VRGEAL--EWPSPTDEQMEELAEALIKRG 269
PRK10076 PRK10076
pyruvate formate lyase II activase; Provisional
67-263 1.92e-28

pyruvate formate lyase II activase; Provisional


Pssm-ID: 182224 [Multi-domain]  Cd Length: 213  Bit Score: 107.55  E-value: 1.92e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118  67 GKEITVEDLMKEVVTYRHFMNASGGGVTASGGEAILQAEFVRDWFRACKKEGIHTCLDTNGFVRRydpviDELLDVT--- 143
Cdd:PRK10076  16 GRDITLDALEREVMKDDIFFRTSGGGVTLSGGEVLMQAEFATRFLQRLRLWGVSCAIETAGDAPA-----SKLLPLAklc 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118 144 DLVMLDLKQMNDEIHQNLVGVSNHRTLEFAQYLSKKNVKVWIRYVVVPGWSDDDDSAHRLGEFTRDMGnVEKIELLPYHE 223
Cdd:PRK10076  91 DEVLFDLKIMDATQARDVVKMNLPRVLENLRLLVSEGVNVIPRLPLIPGFTLSRENMQQALDVLIPLG-IKQIHLLPFHQ 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 445990118 224 LGKHKWVAMGEEYKLDGVKPPKKETMERVKGILEQYGHKV 263
Cdd:PRK10076 170 YGEPKYRLLGKTWSMKEVPAPSSADVATMREMAERAGFQV 209
NrdG2 TIGR02495
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
25-198 4.83e-20

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: 85.11  E-value: 4.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118   25 RIHSFESCGTVDGPG-IRFITFFQGCLMRCLYCHNRDTWDTHGGKEITVEDLMKEVVTYRHFMNasggGVTASGGEAILQ 103
Cdd:TIGR02495   1 RIAGLVPFSTVDYPGkLAFTIFLQGCNLKCPYCHNPLLIPRRGSGEIEVEELLEFLRRRRGLLD----GVVITGGEPTLQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118  104 AEFVrDWFRACKKEGIHTCLDTNG-FVRRYDPVIDELLdvTDLVMLDLK---QMNDEIHQNLVGVSNHRTLEFAQYLSKK 179
Cdd:TIGR02495  77 AGLP-DFLREVRELGFEVKLDTNGsNPRRLEELLEEGL--VDYVAMDVKappEKYGELYGLEKNGAAKNILKSLEILLES 153
                         170
                  ....*....|....*....
gi 445990118  180 NVKVWIRYVVVPGWSDDDD 198
Cdd:TIGR02495 154 GIPFELRTTVVRGFLTEED 172
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
45-197 2.14e-19

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: 82.19  E-value: 2.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118   45 FFQGCLMRCLYCHNRDTWDTHGGKEITVEDLMKEVVTYRhfmNASGGGVTASGGEAILQAEFVRDWFRACKK---EGIHT 121
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKGRELSPEEILEEAKELK---RLGVEVVILGGGEPLLLPDLVELLERLLKLelaEGIRI 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445990118  122 CLDTNGFVRRYDpVIDELLDVT-DLVMLDLKQMNDEIHQNL-VGVSNHRTLEFAQYLSKKNVKV-WIRYVVVPGWSDDD 197
Cdd:pfam04055  78 TLETNGTLLDEE-LLELLKEAGlDRVSIGLESGDDEVLKLInRGHTFEEVLEALELLREAGIPVvTDNIVGLPGETDED 155
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
35-168 7.06e-19

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: 80.29  E-value: 7.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118   35 VDGPGIRFITFFQGCLMRCLYCHNRDTWDTHGGKEITVEdLMKEVVTYrhFMNASGGGVTASGGEAILQAEFVRDWFRAC 114
Cdd:pfam13353   1 VNGPGVRCSLFVSGCNHHCKGCFNPETWDFKYGKPFTEE-LEDEIIED--LAKPYIQGLTLSGGEPLLNAEALLELVKRV 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445990118  115 KKEGIH-TCLDTNGFvrRYD----PVIDELLDVTDlVMLDLKQMND--EIHQNLVGVSNHR 168
Cdd:pfam13353  78 REECPEkDIWLWTGY--TFEelqsKDQLELLKLID-VLVDGKFEQSlkDPSLRFRGSSNQR 135
NrdG TIGR02491
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
25-113 1.71e-13

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: 66.22  E-value: 1.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118   25 RIHSFESCGTVDGPGIRFITFFQGCLMRCLYCHNRDTWDTHGGKEITvEDLMKEVVtyRHFM-NASGGGVTASGGEAILQ 103
Cdd:TIGR02491   1 NYMNIKPDDIVNGEGIRVSLFVAGCKHHCEGCFNKETWNFNGGKEFT-EALEKEII--RDLNdNPLIDGLTLSGGDPLYP 77
                          90
                  ....*....|....*.
gi 445990118  104 A------EFVRdWFRA 113
Cdd:TIGR02491  78 RnveeliELVK-KIKA 92
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
43-227 1.39e-10

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: 59.27  E-value: 1.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118  43 ITFFQGCLMRCLYCHNRdtWDTHGG-KEITVEDLMKEVVTYRHFMNASGggVTASGGEAILQAEFVRDWFRACK-KEGIH 120
Cdd:cd01335    1 LELTRGCNLNCGFCSNP--ASKGRGpESPPEIEEILDIVLEAKERGVEV--VILTGGEPLLYPELAELLRRLKKeLPGFE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118 121 TCLDTNGFVRRYDPV--IDELLDVTDLVMLDLKqmnDEIHQNLVGVSNH---RTLEFAQYLSKKNVKVWIRYVVVPGWSD 195
Cdd:cd01335   77 ISIETNGTLLTEELLkeLKELGLDGVGVSLDSG---DEEVADKIRGSGEsfkERLEALKELREAGLGLSTTLLVGLGDED 153
                        170       180       190
                 ....*....|....*....|....*....|..
gi 445990118 196 DDDSAhRLGEFTRDMGNVEKIELLPYHELGKH 227
Cdd:cd01335  154 EEDDL-EELELLAEFRSPDRVSLFRLLPEEGT 184
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
46-151 3.26e-10

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: 58.23  E-value: 3.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118  46 FQGCLMRCLYChnrDT---WDTHGGKEITVEDLMKEVVTYRHFMnasgggVTASGGEAILQAEFvRDWFRACKKEGIHTC 122
Cdd:COG0602   27 LAGCNLRCSWC---DTkyaWDGEGGKRMSAEEILEEVAALGARH------VVITGGEPLLQDDL-AELLEALKDAGYEVA 96
                         90       100
                 ....*....|....*....|....*....
gi 445990118 123 LDTNGFVRRYDPVidelldvtDLVMLDLK 151
Cdd:COG0602   97 LETNGTLPIPAGI--------DWVTVSPK 117
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
49-263 1.70e-08

Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal structure and biogenesis]; Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440495 [Multi-domain]  Cd Length: 248  Bit Score: 53.66  E-value: 1.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118  49 CLMRCLYCH-NRDTWDTHGGKE-ITVEDLMKEVVTYRHFMNASGGG---VTASG-GEAILQAEFVR--DWFRacKKEGIH 120
Cdd:COG0731   34 CNFDCVYCQrGRTTDLTRERREfDDPEEILEELIEFLRKLPEEAREpdhITFSGsGEPTLYPNLGEliEEIK--KLRGIK 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118 121 TCLDTNGfVRRYDP-VIDELLDVtDLVMLDLKQMNDEIHQNLVGVsnHRTLEFAQYL-------SKKNVKVWIRYVVVPG 192
Cdd:COG0731  112 TALLTNG-SLLHRPeVREELLKA-DQVYPSLDAADEETFRKINRP--HPGLSWERIIeglelfrKLYKGRTVIETMLVKG 187
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445990118 193 WSDDDDSAHRLGEFTRDmGNVEKIEL-----LPyhelgkhkwvamgeeyKLDGVKPPKKETMERVKGILEQYGHKV 263
Cdd:COG0731  188 INDSEEELEAYAELIKR-INPDFVELktymrPP----------------ALSRVNMPSHEELEEFAERLAELGYEV 246
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
49-188 1.36e-07

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: 49.90  E-value: 1.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118  49 CLMRCLYCHNRdtWDTHGGKEITVED---LMKEVVTYRHFMnasgggVTASGGEAILQAEFvRDWFRACKKEGIHTCLDT 125
Cdd:COG0535   10 CNLRCKHCYAD--AGPKRPGELSTEEakrILDELAELGVKV------VGLTGGEPLLRPDL-FELVEYAKELGIRVNLST 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445990118 126 NGfVRRYDPVIDELLDV-TDLVMLDLKQMNDEIHQNLVGVSNH--RTLEFAQYLSKKNVKVWIRYV 188
Cdd:COG0535   81 NG-TLLTEELAERLAEAgLDHVTISLDGVDPETHDKIRGVPGAfdKVLEAIKLLKEAGIPVGINTV 145
Fer4_14 pfam13394
4Fe-4S single cluster domain;
45-99 6.96e-04

4Fe-4S single cluster domain;


Pssm-ID: 433171 [Multi-domain]  Cd Length: 115  Bit Score: 38.50  E-value: 6.96e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 445990118   45 FFQGCLMRCLYCHNRDTWDTHGGKEITvEDLMKEVVTYRHFMNASGGGVTASGGE 99
Cdd:pfam13394   2 FVSGCNHSCPGCDNKETWKFNYGEPFT-EELEDQIIADLKDSYIKRQGLVLTGGE 55
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
104-185 7.18e-04

Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 440290 [Multi-domain]  Cd Length: 301  Bit Score: 40.25  E-value: 7.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118 104 AEFVRDWFRACKKEGIHTCLDTN---GFVRRYDPVIDELLDVTDLVMldlkqMNDEIHQNLVGVSNHRtlEFAQYLSKKN 180
Cdd:COG0524  144 REALLAALEAARAAGVPVSLDPNyrpALWEPARELLRELLALVDILF-----PNEEEAELLTGETDPE--EAAAALLARG 216

                 ....*
gi 445990118 181 VKVWI 185
Cdd:COG0524  217 VKLVV 221
viperin_w_prok NF038283
viperin family antiviral radical SAM protein; Homologs of a viral defense radical SAM enzyme ...
49-137 8.15e-04

viperin family antiviral radical SAM protein; Homologs of a viral defense radical SAM enzyme found in Homo sapiens, viperin (RSAD2), occur in prokaryotes with a strong bias toward placement in phage defense islands, encoded next to CRISPR system and restriction enzyme genes. Further investigation shows members indeed perform the anti-viral function of synthesizing modified ribonucleotides such as ddhCTP, ddh-guanosine triphosphate (ddhGTP) and ddh-uridine triphosphate (ddhUTP). Those non-standard ribonucleotides can interfere with viral replication machinery.


Pssm-ID: 468450 [Multi-domain]  Cd Length: 280  Bit Score: 39.84  E-value: 8.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118  49 CLMRCLYC--HNRDTWDTHGGKEITVEDLMKEVVTYRHFMNASGGGVTASGGEAILQAEFVRDWFRACKKEGIHTCLDTN 126
Cdd:NF038283  12 CNYRCKYCfaKWNDVKSPRHHDKGHLEKLLEELAEFFKLLSYGFVRINFAGGEPLLYPDRLLDLIKLAKELGFKTSIITN 91
                         90
                 ....*....|....*..
gi 445990118 127 G------FVRRYDPVID 137
Cdd:NF038283  92 GsllteeFLEELAPYLD 108
nrdG PRK11121
anaerobic ribonucleoside-triphosphate reductase-activating protein;
27-73 1.47e-03

anaerobic ribonucleoside-triphosphate reductase-activating protein;


Pssm-ID: 236853  Cd Length: 154  Bit Score: 38.05  E-value: 1.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 445990118  27 HSFESCGTVDGPGIRFITFFQGCLMRCLYCHNRDTWDTHGGKEITVE 73
Cdd:PRK11121   4 HQYYPVDVVNGPGTRCTLFVSGCVHQCPGCYNKSTWRLNSGHPFTKE 50
RNR_activ_nrdG3 TIGR02826
anaerobic ribonucleoside-triphosphate reductase activating protein; Members of this family ...
46-125 9.88e-03

anaerobic ribonucleoside-triphosphate reductase activating protein; Members of this family represent a set of radical SAM enzymes related to, yet architecturally different from, the activating protein for the glycine radical-containing, oxygen-sensitive ribonucleoside-triphosphate reductase (RNR) as described in model TIGR02491. Members of this family are found paired with members of a similarly divergent set of anaerobic ribonucleoside-triphosphate reductases. Identification of this protein as an RNR activitating protein is partly from pairing with a candidate RNR. It is further supported by our finding that upstream of these operons are examples of a conserved regulatory element (described Rodionov and Gelfand) that is found in nearly all bacteria and that occurs specifically upstream of operons for all three classes of RNR genes. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]


Pssm-ID: 274317  Cd Length: 147  Bit Score: 35.79  E-value: 9.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990118   46 FQGCLMRCLYCHNRDTWDTHGGKEITVEDLMKEVVTYRHFMNAsgggVTASGGE----AILQ-AEFVRDwfrackKEGIH 120
Cdd:TIGR02826  22 ISGCPLGCPGCHSPELWHEDEGTPLTPEVLAQLLDKYRSLITC----VLFLGGEwepeALLSlLKYVKE------HAGLK 91

                  ....*
gi 445990118  121 TCLDT 125
Cdd:TIGR02826  92 VCLYT 96
 
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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