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Conserved domains on  [gi|639318366|ref|WP_024595150|]
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MULTISPECIES: viperin family antiviral radical SAM protein [unclassified Pseudoalteromonas]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
viperin_w_prok super family cl45735
viperin family antiviral radical SAM protein; Homologs of a viral defense radical SAM enzyme ...
6-291 2.01e-137

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.


The actual alignment was detected with superfamily member NF038283:

Pssm-ID: 468450 [Multi-domain]  Cd Length: 280  Bit Score: 389.99  E-value: 2.01e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366   6 ELVINFHMTEACNYRCGYCYGKWQDNTSatELHHSSESIQDLLLMLAEYFFSnnqirqgLGYQSVRINFAGGEPVMIGAR 85
Cdd:NF038283   1 ELVINWHLTEACNYRCKYCFAKWNDVKS--PRHHDKGHLEKLLEELAEFFKL-------LSYGFVRINFAGGEPLLYPDR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366  86 FISALLFAKSIGFNTSLITNEHFLSPAMLRRIAPHLDMLGLSFDTADYLIAQSIGRTDHKGEWFSPQKALTVTALYRQLN 165
Cdd:NF038283  72 LLDLIKLAKELGFKTSIITNGSLLTEEFLEELAPYLDWIGISIDSANEETNRKIGRVDRKGRVLSLEELLELIALIRQIN 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366 166 PQGKLKVNTVVNAFNFRENLNETIALLQPDKWKLLRALPVY--SDQLTISQEKYDSYVQKHKEHNNVIAIEDNCDMWESY 243
Cdd:NF038283 152 PNIKLKINTVVNRLNWDEDLSELIRELNPDRWKVLQVLPVVgqNDDLLISDEQFDAFVERHKALGSIIVAEDNDDMTGSY 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 639318366 244 LMINPESNFYQNSSSCQGLTLSPSILDIGVSKALNHVNFNIKAFASRY 291
Cdd:NF038283 232 LMIDPEGRFFQNSGGGKGYRYSEPILEVGVEEALSQINFDPEKFLSRY 279
 
Name Accession Description Interval E-value
viperin_w_prok NF038283
viperin family antiviral radical SAM protein; Homologs of a viral defense radical SAM enzyme ...
6-291 2.01e-137

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: 389.99  E-value: 2.01e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366   6 ELVINFHMTEACNYRCGYCYGKWQDNTSatELHHSSESIQDLLLMLAEYFFSnnqirqgLGYQSVRINFAGGEPVMIGAR 85
Cdd:NF038283   1 ELVINWHLTEACNYRCKYCFAKWNDVKS--PRHHDKGHLEKLLEELAEFFKL-------LSYGFVRINFAGGEPLLYPDR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366  86 FISALLFAKSIGFNTSLITNEHFLSPAMLRRIAPHLDMLGLSFDTADYLIAQSIGRTDHKGEWFSPQKALTVTALYRQLN 165
Cdd:NF038283  72 LLDLIKLAKELGFKTSIITNGSLLTEEFLEELAPYLDWIGISIDSANEETNRKIGRVDRKGRVLSLEELLELIALIRQIN 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366 166 PQGKLKVNTVVNAFNFRENLNETIALLQPDKWKLLRALPVY--SDQLTISQEKYDSYVQKHKEHNNVIAIEDNCDMWESY 243
Cdd:NF038283 152 PNIKLKINTVVNRLNWDEDLSELIRELNPDRWKVLQVLPVVgqNDDLLISDEQFDAFVERHKALGSIIVAEDNDDMTGSY 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 639318366 244 LMINPESNFYQNSSSCQGLTLSPSILDIGVSKALNHVNFNIKAFASRY 291
Cdd:NF038283 232 LMIDPEGRFFQNSGGGKGYRYSEPILEVGVEEALSQINFDPEKFLSRY 279
viperin TIGR04278
antiviral radical SAM protein viperin; Viperin (Virus Inhibitory Protein, ER-associated, ...
9-290 1.63e-25

antiviral radical SAM protein viperin; Viperin (Virus Inhibitory Protein, ER-associated, Iterferon-inducible) is a radical SAM enzyme found in human and other vertebrates. It is both induced by interferon and demonstrably active in blocking replication by several types of virus, apparently by modifying lipid chemistries in lipid droplets and membrane rafts.


Pssm-ID: 212001  Cd Length: 347  Bit Score: 104.04  E-value: 1.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366    9 INFHMTEACNYRCGYCYgkwqdNTSATELHHSSESIQDLLLMLAEyffsnnqirQGLGyqsvRINFAGGEPVMIG-ARFI 87
Cdd:TIGR04278  61 VNYHFTRQCNYKCGFCF-----HTAKTSFVLPLEEAKRGLRLLKE---------AGME----KINFSGGEPFLHDrGEFL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366   88 SALL-FAK--------SIGFNTSLITNEHFlspamlRRIAPHLDMLGLSFDTADYLIAQSIGRTD-HKGEWFSPQKALTV 157
Cdd:TIGR04278 123 GKLVqFCKeelqlpsvSIVSNGSLIRERWF------KKYGEYLDILAISCDSFDEQVNVLIGRGQgKKNHVENLQKLRNW 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366  158 TALYRQlnpqgKLKVNTVVNAFNFRENLNETIALLQPDKWKLLRALPV-----------YSDQLTISQEKYDSYVQKHKE 226
Cdd:TIGR04278 197 CRDYKV-----AFKINSVINRFNVEEDMREQIKALNPVRWKVFQCLLIegenagedalrEAERFVISDEEFEGFLERHKS 271
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 639318366  227 HNNVIAiEDNCDMWESYLMINPESNFYqnssSCQGLTLSP--SILDIGVSKALNHVNFNIKAFASR 290
Cdd:TIGR04278 272 VSCLVP-ESNQKMRDSYLILDEYMRFL----NCRNGRKDPskSILDVGVEEAIKFSGFDEKMFLKR 332
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
8-132 7.40e-14

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: 68.01  E-value: 7.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366   8 VINFHMTEACNYRCGYCYGkWQDNTSATELhhSSESIQDLLLMLAEYffsnnQIRQglgyqsvrINFAGGEPVMIgARFI 87
Cdd:COG0535    1 RLQIELTNRCNLRCKHCYA-DAGPKRPGEL--STEEAKRILDELAEL-----GVKV--------VGLTGGEPLLR-PDLF 63
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 639318366  88 SALLFAKSIGFNTSLITNEHFLSPAMLRRIAPH-LDMLGLSFDTAD 132
Cdd:COG0535   64 ELVEYAKELGIRVNLSTNGTLLTEELAERLAEAgLDHVTISLDGVD 109
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
14-225 1.24e-08

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: 54.26  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366  14 TEACNYRCGYCYGkWQDNTSATELHHSSESIQDLLLMLAEYFfsnnqirqglgyqSVRINFAGGEPVMIG--ARFISALL 91
Cdd:cd01335    4 TRGCNLNCGFCSN-PASKGRGPESPPEIEEILDIVLEAKERG-------------VEVVILTGGEPLLYPelAELLRRLK 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366  92 FAKSiGFNTSLITNEHFLSPAMLRRIAP-HLDMLGLSFDTADYLIAQsigrtDHKGEWFSPQKALtvTALYRQLNPQGKL 170
Cdd:cd01335   70 KELP-GFEISIETNGTLLTEELLKELKElGLDGVGVSLDSGDEEVAD-----KIRGSGESFKERL--EALKELREAGLGL 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 639318366 171 KVNTVV-NAFNFRENLNETIALLQPDKWKLLRALPVYSDQLTISQEKYDSYVQKHK 225
Cdd:cd01335  142 STTLLVgLGDEDEEDDLEELELLAEFRSPDRVSLFRLLPEEGTPLELAAPVVPAEK 197
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
13-142 4.11e-08

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: 51.76  E-value: 4.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366   13 MTEACNYRCGYCYGkwqdNTSATELHHSSESIQDLLLMLAEYffsnnqIRQGLGYqsvrINFAGGEPVM---IGARFISA 89
Cdd:pfam04055   1 ITRGCNLRCTYCAF----PSIRARGKGRELSPEEILEEAKEL------KRLGVEV----VILGGGEPLLlpdLVELLERL 66
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 639318366   90 LLFAKSIGFNTSLITNEHFLSPAMLRRIAPH-LDMLGLSFDTADYLIAQSIGRT 142
Cdd:pfam04055  67 LKLELAEGIRITLETNGTLLDEELLELLKEAgLDRVSIGLESGDDEVLKLINRG 120
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
13-149 2.58e-05

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 44.31  E-value: 2.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366    13 MTEACNYRCGYCYgkwQDNTSATELHHSSESIQDLLLMLAEYFFSNNQIRQglgyqsvrINFAGGEPVMIGARFISALL- 91
Cdd:smart00729   7 ITRGCPRRCTFCS---FPSLRGKLRSRYLEALVREIELLAEKGEKEGLVGT--------VFIGGGTPTLLSPEQLEELLe 75
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639318366    92 -----FAKSIGFNTSLITNEHFLSPAMLRRIAPH-LDMLGLSFDTADYLIAQSIGRTdHKGEWF 149
Cdd:smart00729  76 aireiLGLAKDVEITIETRPDTLTEELLEALKEAgVNRVSLGVQSGDDEVLKAINRG-HTVEDV 138
 
Name Accession Description Interval E-value
viperin_w_prok NF038283
viperin family antiviral radical SAM protein; Homologs of a viral defense radical SAM enzyme ...
6-291 2.01e-137

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: 389.99  E-value: 2.01e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366   6 ELVINFHMTEACNYRCGYCYGKWQDNTSatELHHSSESIQDLLLMLAEYFFSnnqirqgLGYQSVRINFAGGEPVMIGAR 85
Cdd:NF038283   1 ELVINWHLTEACNYRCKYCFAKWNDVKS--PRHHDKGHLEKLLEELAEFFKL-------LSYGFVRINFAGGEPLLYPDR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366  86 FISALLFAKSIGFNTSLITNEHFLSPAMLRRIAPHLDMLGLSFDTADYLIAQSIGRTDHKGEWFSPQKALTVTALYRQLN 165
Cdd:NF038283  72 LLDLIKLAKELGFKTSIITNGSLLTEEFLEELAPYLDWIGISIDSANEETNRKIGRVDRKGRVLSLEELLELIALIRQIN 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366 166 PQGKLKVNTVVNAFNFRENLNETIALLQPDKWKLLRALPVY--SDQLTISQEKYDSYVQKHKEHNNVIAIEDNCDMWESY 243
Cdd:NF038283 152 PNIKLKINTVVNRLNWDEDLSELIRELNPDRWKVLQVLPVVgqNDDLLISDEQFDAFVERHKALGSIIVAEDNDDMTGSY 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 639318366 244 LMINPESNFYQNSSSCQGLTLSPSILDIGVSKALNHVNFNIKAFASRY 291
Cdd:NF038283 232 LMIDPEGRFFQNSGGGKGYRYSEPILEVGVEEALSQINFDPEKFLSRY 279
viperin TIGR04278
antiviral radical SAM protein viperin; Viperin (Virus Inhibitory Protein, ER-associated, ...
9-290 1.63e-25

antiviral radical SAM protein viperin; Viperin (Virus Inhibitory Protein, ER-associated, Iterferon-inducible) is a radical SAM enzyme found in human and other vertebrates. It is both induced by interferon and demonstrably active in blocking replication by several types of virus, apparently by modifying lipid chemistries in lipid droplets and membrane rafts.


Pssm-ID: 212001  Cd Length: 347  Bit Score: 104.04  E-value: 1.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366    9 INFHMTEACNYRCGYCYgkwqdNTSATELHHSSESIQDLLLMLAEyffsnnqirQGLGyqsvRINFAGGEPVMIG-ARFI 87
Cdd:TIGR04278  61 VNYHFTRQCNYKCGFCF-----HTAKTSFVLPLEEAKRGLRLLKE---------AGME----KINFSGGEPFLHDrGEFL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366   88 SALL-FAK--------SIGFNTSLITNEHFlspamlRRIAPHLDMLGLSFDTADYLIAQSIGRTD-HKGEWFSPQKALTV 157
Cdd:TIGR04278 123 GKLVqFCKeelqlpsvSIVSNGSLIRERWF------KKYGEYLDILAISCDSFDEQVNVLIGRGQgKKNHVENLQKLRNW 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366  158 TALYRQlnpqgKLKVNTVVNAFNFRENLNETIALLQPDKWKLLRALPV-----------YSDQLTISQEKYDSYVQKHKE 226
Cdd:TIGR04278 197 CRDYKV-----AFKINSVINRFNVEEDMREQIKALNPVRWKVFQCLLIegenagedalrEAERFVISDEEFEGFLERHKS 271
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 639318366  227 HNNVIAiEDNCDMWESYLMINPESNFYqnssSCQGLTLSP--SILDIGVSKALNHVNFNIKAFASR 290
Cdd:TIGR04278 272 VSCLVP-ESNQKMRDSYLILDEYMRFL----NCRNGRKDPskSILDVGVEEAIKFSGFDEKMFLKR 332
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
8-132 7.40e-14

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: 68.01  E-value: 7.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366   8 VINFHMTEACNYRCGYCYGkWQDNTSATELhhSSESIQDLLLMLAEYffsnnQIRQglgyqsvrINFAGGEPVMIgARFI 87
Cdd:COG0535    1 RLQIELTNRCNLRCKHCYA-DAGPKRPGEL--STEEAKRILDELAEL-----GVKV--------VGLTGGEPLLR-PDLF 63
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 639318366  88 SALLFAKSIGFNTSLITNEHFLSPAMLRRIAPH-LDMLGLSFDTAD 132
Cdd:COG0535   64 ELVEYAKELGIRVNLSTNGTLLTEELAERLAEAgLDHVTISLDGVD 109
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
14-225 1.24e-08

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: 54.26  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366  14 TEACNYRCGYCYGkWQDNTSATELHHSSESIQDLLLMLAEYFfsnnqirqglgyqSVRINFAGGEPVMIG--ARFISALL 91
Cdd:cd01335    4 TRGCNLNCGFCSN-PASKGRGPESPPEIEEILDIVLEAKERG-------------VEVVILTGGEPLLYPelAELLRRLK 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366  92 FAKSiGFNTSLITNEHFLSPAMLRRIAP-HLDMLGLSFDTADYLIAQsigrtDHKGEWFSPQKALtvTALYRQLNPQGKL 170
Cdd:cd01335   70 KELP-GFEISIETNGTLLTEELLKELKElGLDGVGVSLDSGDEEVAD-----KIRGSGESFKERL--EALKELREAGLGL 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 639318366 171 KVNTVV-NAFNFRENLNETIALLQPDKWKLLRALPVYSDQLTISQEKYDSYVQKHK 225
Cdd:cd01335  142 STTLLVgLGDEDEEDDLEELELLAEFRSPDRVSLFRLLPEEGTPLELAAPVVPAEK 197
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
13-142 4.11e-08

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: 51.76  E-value: 4.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366   13 MTEACNYRCGYCYGkwqdNTSATELHHSSESIQDLLLMLAEYffsnnqIRQGLGYqsvrINFAGGEPVM---IGARFISA 89
Cdd:pfam04055   1 ITRGCNLRCTYCAF----PSIRARGKGRELSPEEILEEAKEL------KRLGVEV----VILGGGEPLLlpdLVELLERL 66
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 639318366   90 LLFAKSIGFNTSLITNEHFLSPAMLRRIAPH-LDMLGLSFDTADYLIAQSIGRT 142
Cdd:pfam04055  67 LKLELAEGIRITLETNGTLLDEELLELLKEAgLDRVSIGLESGDDEVLKLINRG 120
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
11-129 4.74e-07

Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 50.76  E-value: 4.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366  11 FHMTEACNYRCGYCYGKWQDNTSATELhhSSESIQDLLLMLAEYFFSnnqirqglgYQSVRINFAGGEPVMIGARFISAL 90
Cdd:COG0641    5 LKPTSRCNLRCSYCYYSEGDEGSRRRM--SEETAEKAIDFLIESSGP---------GKELTITFFGGEPLLNFDFIKEIV 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 639318366  91 LFAKSIG-----FNTSLITNEHFLSPAMLRRIAPHLDMLGLSFD 129
Cdd:COG0641   74 EYARKYAkkgkkIRFSIQTNGTLLDDEWIDFLKENGFSVGISLD 117
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
17-133 1.92e-06

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 48.26  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366  17 CNYRCGYCYgkwqdN--TSATELHHSSE--SIQDLLLMLAEYffsNNQIRQGLGyqsvrINFAGGEPVMIGARFISALLF 92
Cdd:COG1180   31 CNLRCPYCH-----NpeISQGRPDAAGRelSPEELVEEALKD---RGFLDSCGG-----VTFSGGEPTLQPEFLLDLAKL 97
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 639318366  93 AKSIGFNTSLITNeHFLSPAMLRRIAPHLDMLGL---SFDTADY 133
Cdd:COG1180   98 AKELGLHTALDTN-GYIPEEALEELLPYLDAVNIdlkAFDDEFY 140
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
13-149 2.58e-05

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 44.31  E-value: 2.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318366    13 MTEACNYRCGYCYgkwQDNTSATELHHSSESIQDLLLMLAEYFFSNNQIRQglgyqsvrINFAGGEPVMIGARFISALL- 91
Cdd:smart00729   7 ITRGCPRRCTFCS---FPSLRGKLRSRYLEALVREIELLAEKGEKEGLVGT--------VFIGGGTPTLLSPEQLEELLe 75
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639318366    92 -----FAKSIGFNTSLITNEHFLSPAMLRRIAPH-LDMLGLSFDTADYLIAQSIGRTdHKGEWF 149
Cdd:smart00729  76 aireiLGLAKDVEITIETRPDTLTEELLEALKEAgVNRVSLGVQSGDDEVLKAINRG-HTVEDV 138
rSAM_Cxxx_rpt TIGR04115
radical SAM peptide maturase, CXXX-repeat target family; Members of this radical SAM domain ...
9-81 6.14e-04

radical SAM peptide maturase, CXXX-repeat target family; Members of this radical SAM domain protein are predicted peptide maturases, similar to PqqE, AlbA, the mycofactocin radical SAM maturase, and many others that share the peptide modification radical SAM protein C-terminal additional 4Fe4S-binding domain (TIGR04085). Members co-occur with a protein of unknown function that may be a chaperone or immunity protein and with a peptide that may have twelve or more cysteines occurring regularly spaced every fourth residue. These Cys residues tend to be flanked by residues with small side chains that provide minimal steric hindrance to crosslink formation by the radical SAM enzyme as in the subtilosin A system.


Pssm-ID: 200366 [Multi-domain]  Cd Length: 359  Bit Score: 41.03  E-value: 6.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 639318366    9 INFHMTEACNYRCGYCY--GKWQDNTSATELhhsSESIQDLLLmlaeyffsNNqiRQGLGYQSVRINFAGGEPVM 81
Cdd:TIGR04115   4 ITFIVTDDCQLACKYCYqtGKNKNKRMSFET---AKKAVDYIL--------SG--NKGFGEPSVIWDFIGGEPLL 65
 
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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