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Conserved domains on  [gi|2065437490|pdb|7N7H|A]
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Chain A, VIPERIN-LIKE ENZYME

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
viperin super family cl28175
antiviral radical SAM protein viperin; Viperin (Virus Inhibitory Protein, ER-associated, ...
2-293 0e+00

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.


The actual alignment was detected with superfamily member TIGR04278:

Pssm-ID: 212001  Cd Length: 347  Bit Score: 620.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A          2 TVPVSVNYHFTRQCNYQCGFCFHTAKTSFVLPIEEAKKGLLMLMKAGMEKVNFSGGEPFLHDRGKFVGELVRYCKQELEL 81
Cdd:TIGR04278  56 TTPTSVNYHFTRQCNYKCGFCFHTAKTSFVLPLEEAKRGLRLLKEAGMEKINFSGGEPFLHDRGEFLGKLVQFCKEELQL 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A         82 PSVSIVSNGSLIRDNWFNKYGECLDILAISCDSFDEETNVLIGRRQKGKNHVEALRRVRDMCQQYKVAFKLNTVVNTYNK 161
Cdd:TIGR04278 136 PSVSIVSNGSLIRERWFKKYGEYLDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRNWCRDYKVAFKINSVINRFNV 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A        162 QEDMTSHIQELCPVRWKVFQCLVIAGENSGEDALRDAEQFLVSNHEFDQFISRHASLECLVPESNEKMQNSYLILDEYMR 241
Cdd:TIGR04278 216 EEDMREQIKALNPVRWKVFQCLLIEGENAGEDALREAERFVISDEEFEGFLERHKSVSCLVPESNQKMRDSYLILDEYMR 295
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
7N7H_A        242 FLDCTGGSKSPSKSILDVGVDQAMKFSGFDEKMFLKRGGKYVWSKADMKLDW 293
Cdd:TIGR04278 296 FLNCRNGRKDPSKSILDVGVEEAIKFSGFDEKMFLKRGGKYVWSKADMKLDW 347
 
Name Accession Description Interval E-value
viperin TIGR04278
antiviral radical SAM protein viperin; Viperin (Virus Inhibitory Protein, ER-associated, ...
2-293 0e+00

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: 620.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A          2 TVPVSVNYHFTRQCNYQCGFCFHTAKTSFVLPIEEAKKGLLMLMKAGMEKVNFSGGEPFLHDRGKFVGELVRYCKQELEL 81
Cdd:TIGR04278  56 TTPTSVNYHFTRQCNYKCGFCFHTAKTSFVLPLEEAKRGLRLLKEAGMEKINFSGGEPFLHDRGEFLGKLVQFCKEELQL 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A         82 PSVSIVSNGSLIRDNWFNKYGECLDILAISCDSFDEETNVLIGRRQKGKNHVEALRRVRDMCQQYKVAFKLNTVVNTYNK 161
Cdd:TIGR04278 136 PSVSIVSNGSLIRERWFKKYGEYLDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRNWCRDYKVAFKINSVINRFNV 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A        162 QEDMTSHIQELCPVRWKVFQCLVIAGENSGEDALRDAEQFLVSNHEFDQFISRHASLECLVPESNEKMQNSYLILDEYMR 241
Cdd:TIGR04278 216 EEDMREQIKALNPVRWKVFQCLLIEGENAGEDALREAERFVISDEEFEGFLERHKSVSCLVPESNQKMRDSYLILDEYMR 295
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
7N7H_A        242 FLDCTGGSKSPSKSILDVGVDQAMKFSGFDEKMFLKRGGKYVWSKADMKLDW 293
Cdd:TIGR04278 296 FLNCRNGRKDPSKSILDVGVEEAIKFSGFDEKMFLKRGGKYVWSKADMKLDW 347
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
10-165 3.03e-18

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: 80.84  E-value: 3.03e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A       10 HFTRQCNYQCGFCFHTAKTSFVLP----IEEAKKGLLMLMKAGMEKVNFSGGEPFLHDRgkfVGELVRYCKQELELPSVS 85
Cdd:cd01335   2 ELTRGCNLNCGFCSNPASKGRGPEsppeIEEILDIVLEAKERGVEVVILTGGEPLLYPE---LAELLRRLKKELPGFEIS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A       86 IVSNGSLIRDNWFNKYGE-CLDILAISCDSFDEETNVLIGRRQKGKNHV-EALRRVRDmcqqYKVAFKLNTVVNTYNKQE 163
Cdd:cd01335  79 IETNGTLLTEELLKELKElGLDGVGVSLDSGDEEVADKIRGSGESFKERlEALKELRE----AGLGLSTTLLVGLGDEDE 154

                ..
7N7H_A      164 DM 165
Cdd:cd01335 155 ED 156
Radical_SAM pfam04055
Radical SAM superfamily. Radical SAM proteins catalyze diverse reactions, including unusual ...
11-141 1.19e-14

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


Pssm-ID: 367788  Cd Length: 160  Bit Score: 69.86  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A         11 FTRQCNYQCGFCF----HTAKTSFVLPIEEAKKGLLMLM-KAGMEKVNFSGGEPFLHDrgKFVGELVRYCKQEL-ELPSV 84
Cdd:pfam04055   1 ITRGCNLRCTYCAfpsiRGRGKGRELSPEEILEEAKELKaRLGVEVVILGGGEPLLLP--DLVELLLRLLKLELaEGIRI 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
7N7H_A         85 SIVSNGSLIRDNWFNKYGEC-LDILAISCDSFDEETNVLIGRRQKGKNHVEALRRVRD 141
Cdd:pfam04055  79 TLETNGTLLDEELLELLKEAgLDRVSIGLESGDDEVLKLINRKHTFEEVLEAIELLRE 136
SkfB COG0535
Radical SAM superfamily enzyme, MoaA/NifB/PqqE/SkfB family [General function prediction only];
3-200 2.48e-11

Radical SAM superfamily enzyme, MoaA/NifB/PqqE/SkfB family [General function prediction only];


Pssm-ID: 223609 [Multi-domain]  Cd Length: 347  Bit Score: 63.11  E-value: 2.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A        3 VPVSVNYHFTRQCNYQCGFCFHTAKTSFV--LPIEEAKKGL-LMLMKAGMEKVNFSGGEPFLHDRgkfVGELVRYCKQEL 79
Cdd:COG0535  17 PPLVVGIELTNRCNLACKHCYAEAGKKLPgeLSTEEDLRVIdELAELGEIPVVIFTGGEPLLRPD---LLEIVEYARKKG 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A       80 ELPsVSIVSNGSLIRDNWFNKYGEC-LDILAISCDSFDEETNVLIgRRQKG--KNHVEALRRVRDmcqqYKVAFKLNTVV 156
Cdd:COG0535  94 GIR-VSLSTNGTLLTEEVLEKLKEAgLDYVSISLDGLDPETHDPI-RGVKGvfKRAVEAIKNLKE----AGILVVINTTV 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
7N7H_A      157 NTYNKQE--DMTSHIQELCPVRWKVFQCLVIAGENSGEDALRDAEQ 200
Cdd:COG0535 168 TKINYDElpEIADLAAELGVDELNVFPLIPVGRGEENLELDLTPEE 213
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
9-143 2.57e-11

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: 61.65  E-value: 2.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A           9 YHFTRQCNYQCGFC--FHTAKTSFVLPIEEAKKGLLMLMKAG-----MEKVNFSGGEPFLHDRGKFvGELVRYCKQELEL 81
Cdd:smart00729   5 YIITRGCPRRCTFCsfPSLRGKLRSRYLEALVREIELLAEKGekeglVGTVFIGGGTPTLLSPEQL-EELLEAIREILGL 83
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
7N7H_A          82 P---SVSIVSNGSLIRDNWFNKYGE-CLDILAISCDSFDEETNVLIGRRQKGKNHVEALRRVRDMC 143
Cdd:smart00729  84 AkdvEITIETRPDTLTEELLEALKEaGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAG 149
moaA PRK00164
GTP 3',8-cyclase MoaA;
5-156 1.38e-06

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 48.60  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A         5 VSVnyhfTRQCNYQCGFCFHTAKTSF-----VLPIEEakkgLLMLMKA----GMEKVNFSGGEPFLhdRGKFVgELVRYC 75
Cdd:PRK00164  21 ISV----TDRCNFRCTYCMPEGYLPFlpkeeLLSLEE----IERLVRAfvalGVRKVRLTGGEPLL--RKDLE-DIIAAL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A        76 KQELELPSVSIVSNGSLIR---DNWFnkygEC-LDILAISCDSFDEETNVLI---GRRQKGKNHVEALRRVRDmcqqYKV 148
Cdd:PRK00164  90 AALPGIRDLALTTNGYLLArraAALK----DAgLDRVNVSLDSLDPERFKAItgrDRLDQVLAGIDAALAAGL----TPV 161

                 ....*...
7N7H_A       149 afKLNTVV 156
Cdd:PRK00164 162 --KVNAVL 167
AlbA NF012164
subtilosin maturase AlbA; AlbA is a radical SAM/SPASM domain-containing protein responsible ...
3-120 5.57e-05

subtilosin maturase AlbA; AlbA is a radical SAM/SPASM domain-containing protein responsible for introducing thioether crosslinks during that maturation of bacteriocins such subtilosin A.


Pssm-ID: 333728 [Multi-domain]  Cd Length: 442  Bit Score: 44.25  E-value: 5.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A         3 VPVSVNYHFTRQCNYQCGFCF--HTAKTSFVLPIEEAKKGLLMLMKAGMEKVNFSGGEPFLHDRGKfvgELVRYCKQELE 80
Cdd:NF012164 111 MPLHATFELTHRCNLKCAHCYleSSPEALGTVSIEQFKKTADMLFDNGVLTCEITGGEIFVHPNAN---EILDYVCKKFK 187
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
7N7H_A        81 lpSVSIVSNGSLIRD---NWFNKYGECLdILAISCDSFDEETN 120
Cdd:NF012164 188 --KVAVLTNGTLMRKeslELLKAYKQKI-IVGISLDSVNSEVH 227
 
Name Accession Description Interval E-value
viperin TIGR04278
antiviral radical SAM protein viperin; Viperin (Virus Inhibitory Protein, ER-associated, ...
2-293 0e+00

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: 620.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A          2 TVPVSVNYHFTRQCNYQCGFCFHTAKTSFVLPIEEAKKGLLMLMKAGMEKVNFSGGEPFLHDRGKFVGELVRYCKQELEL 81
Cdd:TIGR04278  56 TTPTSVNYHFTRQCNYKCGFCFHTAKTSFVLPLEEAKRGLRLLKEAGMEKINFSGGEPFLHDRGEFLGKLVQFCKEELQL 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A         82 PSVSIVSNGSLIRDNWFNKYGECLDILAISCDSFDEETNVLIGRRQKGKNHVEALRRVRDMCQQYKVAFKLNTVVNTYNK 161
Cdd:TIGR04278 136 PSVSIVSNGSLIRERWFKKYGEYLDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRNWCRDYKVAFKINSVINRFNV 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A        162 QEDMTSHIQELCPVRWKVFQCLVIAGENSGEDALRDAEQFLVSNHEFDQFISRHASLECLVPESNEKMQNSYLILDEYMR 241
Cdd:TIGR04278 216 EEDMREQIKALNPVRWKVFQCLLIEGENAGEDALREAERFVISDEEFEGFLERHKSVSCLVPESNQKMRDSYLILDEYMR 295
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
7N7H_A        242 FLDCTGGSKSPSKSILDVGVDQAMKFSGFDEKMFLKRGGKYVWSKADMKLDW 293
Cdd:TIGR04278 296 FLNCRNGRKDPSKSILDVGVEEAIKFSGFDEKMFLKRGGKYVWSKADMKLDW 347
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
10-165 3.03e-18

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: 80.84  E-value: 3.03e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A       10 HFTRQCNYQCGFCFHTAKTSFVLP----IEEAKKGLLMLMKAGMEKVNFSGGEPFLHDRgkfVGELVRYCKQELELPSVS 85
Cdd:cd01335   2 ELTRGCNLNCGFCSNPASKGRGPEsppeIEEILDIVLEAKERGVEVVILTGGEPLLYPE---LAELLRRLKKELPGFEIS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A       86 IVSNGSLIRDNWFNKYGE-CLDILAISCDSFDEETNVLIGRRQKGKNHV-EALRRVRDmcqqYKVAFKLNTVVNTYNKQE 163
Cdd:cd01335  79 IETNGTLLTEELLKELKElGLDGVGVSLDSGDEEVADKIRGSGESFKERlEALKELRE----AGLGLSTTLLVGLGDEDE 154

                ..
7N7H_A      164 DM 165
Cdd:cd01335 155 ED 156
Radical_SAM pfam04055
Radical SAM superfamily. Radical SAM proteins catalyze diverse reactions, including unusual ...
11-141 1.19e-14

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


Pssm-ID: 367788  Cd Length: 160  Bit Score: 69.86  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A         11 FTRQCNYQCGFCF----HTAKTSFVLPIEEAKKGLLMLM-KAGMEKVNFSGGEPFLHDrgKFVGELVRYCKQEL-ELPSV 84
Cdd:pfam04055   1 ITRGCNLRCTYCAfpsiRGRGKGRELSPEEILEEAKELKaRLGVEVVILGGGEPLLLP--DLVELLLRLLKLELaEGIRI 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
7N7H_A         85 SIVSNGSLIRDNWFNKYGEC-LDILAISCDSFDEETNVLIGRRQKGKNHVEALRRVRD 141
Cdd:pfam04055  79 TLETNGTLLDEELLELLKEAgLDRVSIGLESGDDEVLKLINRKHTFEEVLEAIELLRE 136
SkfB COG0535
Radical SAM superfamily enzyme, MoaA/NifB/PqqE/SkfB family [General function prediction only];
3-200 2.48e-11

Radical SAM superfamily enzyme, MoaA/NifB/PqqE/SkfB family [General function prediction only];


Pssm-ID: 223609 [Multi-domain]  Cd Length: 347  Bit Score: 63.11  E-value: 2.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A        3 VPVSVNYHFTRQCNYQCGFCFHTAKTSFV--LPIEEAKKGL-LMLMKAGMEKVNFSGGEPFLHDRgkfVGELVRYCKQEL 79
Cdd:COG0535  17 PPLVVGIELTNRCNLACKHCYAEAGKKLPgeLSTEEDLRVIdELAELGEIPVVIFTGGEPLLRPD---LLEIVEYARKKG 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A       80 ELPsVSIVSNGSLIRDNWFNKYGEC-LDILAISCDSFDEETNVLIgRRQKG--KNHVEALRRVRDmcqqYKVAFKLNTVV 156
Cdd:COG0535  94 GIR-VSLSTNGTLLTEEVLEKLKEAgLDYVSISLDGLDPETHDPI-RGVKGvfKRAVEAIKNLKE----AGILVVINTTV 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
7N7H_A      157 NTYNKQE--DMTSHIQELCPVRWKVFQCLVIAGENSGEDALRDAEQ 200
Cdd:COG0535 168 TKINYDElpEIADLAAELGVDELNVFPLIPVGRGEENLELDLTPEE 213
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
9-143 2.57e-11

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: 61.65  E-value: 2.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A           9 YHFTRQCNYQCGFC--FHTAKTSFVLPIEEAKKGLLMLMKAG-----MEKVNFSGGEPFLHDRGKFvGELVRYCKQELEL 81
Cdd:smart00729   5 YIITRGCPRRCTFCsfPSLRGKLRSRYLEALVREIELLAEKGekeglVGTVFIGGGTPTLLSPEQL-EELLEAIREILGL 83
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
7N7H_A          82 P---SVSIVSNGSLIRDNWFNKYGE-CLDILAISCDSFDEETNVLIGRRQKGKNHVEALRRVRDMC 143
Cdd:smart00729  84 AkdvEITIETRPDTLTEELLEALKEaGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAG 149
MoaA COG2896
Molybdenum cofactor biosynthesis enzyme MoaA [Coenzyme transport and metabolism];
5-156 7.49e-09

Molybdenum cofactor biosynthesis enzyme MoaA [Coenzyme transport and metabolism];


Pssm-ID: 225449 [Multi-domain]  Cd Length: 322  Bit Score: 55.69  E-value: 7.49e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A        5 VSVNYhftrQCNYQCGFCFHTAKTSF-----VLPIEEakkgLLMLMKA----GMEKVNFSGGEPFLhdRgKFVGELVRYC 75
Cdd:COG2896  15 ISVTD----RCNFRCTYCMPEGPLAFlpkeeLLSLEE----IRRLVRAfaelGVEKVRLTGGEPLL--R-KDLDEIIARL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A       76 KQeLELPSVSIVSNGSLIRDnWFNKYGEC-LDILAISCDSFDEETNVLIGRRQKGKNHVEALRRVRDmcqqykVAF---K 151
Cdd:COG2896  84 AR-LGIRDLSLTTNGVLLAR-RAADLKEAgLDRVNVSLDSLDPEKFRKITGRDRLDRVLEGIDAAVE------AGLtpvK 155

                ....*
7N7H_A      152 LNTVV 156
Cdd:COG2896 156 LNTVL 160
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
5-156 5.49e-08

molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes molybdenum cofactor biosynthesis protein A, or MoaA, as found in bacteria. It does not include the family of probable functional equivalent proteins from the archaea. MoaA works together with MoaC to synthesize precursor Z from guanine. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 274250 [Multi-domain]  Cd Length: 334  Bit Score: 53.00  E-value: 5.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A          5 VSVnyhfTRQCNYQCGFCFHTAKTSFVLPieeaKKGLL----------MLMKAGMEKVNFSGGEPFLHdrgKFVGELVRY 74
Cdd:TIGR02666  14 ISV----TDRCNLRCVYCMPEGGGLDFLP----KEELLtfeeierlvrAFVGLGVRKVRLTGGEPLLR---KDLVELVAR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A         75 CKQELELPSVSIVSNGSLIRdnwfnKYGECL-----DILAISCDSFDEETNVLIGRRQKGKNHV-EALrrvrDMCQQYKV 148
Cdd:TIGR02666  83 LAALPGIEDIALTTNGLLLA-----RHAKDLkeaglKRVNVSLDSLDPERFAKITRRGGRLEQVlAGI----DAALAAGL 153

                  ....*....
7N7H_A        149 A-FKLNTVV 156
Cdd:TIGR02666 154 EpVKLNTVV 162
rSAM_NirJ2 TIGR04055
putative heme d1 biosynthesis radical SAM protein NirJ2; Members of this radical SAM protein ...
7-201 9.63e-08

putative heme d1 biosynthesis radical SAM protein NirJ2; Members of this radical SAM protein subfamily, designated NirJ2, occur in genomic contexts with a paralog NirJ1 and with other nitrite reductase operon genes associated with heme d1 biosynthesis, as in Heliobacillus mobilis and Heliophilum fasciatum. NirJ2 is presumed by bioinformatics analysis (Xiong, et al.) to be a heme d1 biosynthesis protein by context. This model has been redone (2014) to remove the branch (TIGR04545) that included DVU_0855, from a similar pathway for heme b biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274947 [Multi-domain]  Cd Length: 326  Bit Score: 52.42  E-value: 9.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A          7 VNYHFTRQCNYQCGFCFHTA--KTSFVLPIEEAKKGLLMLMKAGMEKVNFSGGEPFLHDRgkfVGELVRYCKqELELPSV 84
Cdd:TIGR04055   2 ISWNTTNKCNMYCDHCYRDAgvKAEGELSTEEGKKLIDEIAKAGFKIMIFSGGEPLMRPD---IFELIAYAT-SRGLRPV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A         85 sIVSNGSLIRDNWFNKYGEC-LDILAISCDSFDEETNVLIgRRQKG--KNHVEALRRvrdmCQQYKVAFKLNTVVNTYNK 161
Cdd:TIGR04055  78 -LGTNGTLITPEVARKLKKAgAMGMGISLDSLDPKKHDGF-RAYDGawQDAVEGMRN----CREAGLPFQIHTTVMDWNK 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
7N7H_A        162 QE--DMTSHIQELCPVRWKVFqCLVIAGE--NSGEDALRdAEQF 201
Cdd:TIGR04055 152 DEveDITDFAVELGAVAHHVF-FLVPTGRavNIEEESLR-AEQY 193
pseudo_SAM_Halo TIGR04347
pseudo-rSAM protein/SPASM domain protein; Members of this family all have a C-terminal SPASM ...
4-125 9.94e-07

pseudo-rSAM protein/SPASM domain protein; Members of this family all have a C-terminal SPASM domain (see model TIGR04085), a region usually found as a C-terminal second 4Fe-4S domain of radical SAM domain (see pfam04055) proteins. A majority of rSAM/SPASM proteins modify ribosomally produced peptides. In a few members of this family, the key Cys residues of the radical SAM domain have been lost, making this a pseudo-rSAM family. Members of this family are restricted so far to Haloarchaea, always occur next a member of family TIGR04031, and are often accompanied by another rSAM/SPASM domain protein. The function of this two or three gene cassette is unknown.


Pssm-ID: 275143 [Multi-domain]  Cd Length: 390  Bit Score: 49.44  E-value: 9.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A          4 PVSVnYHFTRQCNYQCGFCFHTAKTSFV---LPIEEAKKGLLMLMKAGMEKVNFSGGEPFLHDRgkfVGELVRYCKQELE 80
Cdd:TIGR04347  38 PVVV-WNTTRRCNLYCEHCYAGADTEAApgeLSTAEAKALLDDLADYGVPVILFSGGEPLVRDD---LEELVAYAADAGI 113
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
7N7H_A         81 LPSVSivSNGSLIRDNWFNKYGEC-LDILAISCDSFDEETNVLIGR 125
Cdd:TIGR04347 114 RPVLS--TNGTLLTEERAEALRDAgLDYAGVSVDGLPERNDEFRGK 157
moaA PRK00164
GTP 3',8-cyclase MoaA;
5-156 1.38e-06

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 48.60  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A         5 VSVnyhfTRQCNYQCGFCFHTAKTSF-----VLPIEEakkgLLMLMKA----GMEKVNFSGGEPFLhdRGKFVgELVRYC 75
Cdd:PRK00164  21 ISV----TDRCNFRCTYCMPEGYLPFlpkeeLLSLEE----IERLVRAfvalGVRKVRLTGGEPLL--RKDLE-DIIAAL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A        76 KQELELPSVSIVSNGSLIR---DNWFnkygEC-LDILAISCDSFDEETNVLI---GRRQKGKNHVEALRRVRDmcqqYKV 148
Cdd:PRK00164  90 AALPGIRDLALTTNGYLLArraAALK----DAgLDRVNVSLDSLDPERFKAItgrDRLDQVLAGIDAALAAGL----TPV 161

                 ....*...
7N7H_A       149 afKLNTVV 156
Cdd:PRK00164 162 --KVNAVL 167
moaA_archaeal TIGR02668
probable molybdenum cofactor biosynthesis protein A, archaeal; This model describes an ...
6-119 1.97e-06

probable molybdenum cofactor biosynthesis protein A, archaeal; This model describes an archaeal family related, and predicted to be functionally equivalent, to molybdenum cofactor biosynthesis protein A (MoaA) of bacteria (see TIGR02666). [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 274251 [Multi-domain]  Cd Length: 302  Bit Score: 48.07  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A          6 SVNYHFTRQCNYQCGFCF---HTAKTSFVLPIEEAKKGLLMLMKAGMEKVNFSGGEPFLhdRGKFVgELVRYCKQElELP 82
Cdd:TIGR02668  11 SLRISVTDRCNLSCFYCHmegEDRSGGNELSPEEIERIVRVASEFGVRKVKITGGEPLL--RKDLI-EIIRRIKDY-GIK 86
                          90       100       110
                  ....*....|....*....|....*....|....*...
7N7H_A         83 SVSIVSNGSLIRDnWFNKYGEC-LDILAISCDSFDEET 119
Cdd:TIGR02668  87 DVSMTTNGILLEK-LAKKLKEAgLDRVNVSLDTLDPEK 123
SCM_rSAM_ScmE TIGR04250
SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in ...
4-138 4.45e-06

SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in Syntrophobacter fumaroxidans MPOB, Chlorobium limicola DSM 245, Methanocella paludicola SANAE, and delta proteobacterium NaphS2 contains two PqqE-like radical SAM/SPASM domain proteins, a PqqD homolog, and a conserved hypothetical protein. These components suggest modification of a ribosomally produced peptide precursor, but the precursor has not been identified. Of the two PqqE homologs of the cassette, this family is the closer in sequence.


Pssm-ID: 211973 [Multi-domain]  Cd Length: 358  Bit Score: 47.16  E-value: 4.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A          4 PVSVNYHFTRQCNYQCGFCFH---TAKTSFVLPIEEAKKGLLMLMKAGMEKVNFSGGEPFLhdRGKFvGELVR-YCKQEL 79
Cdd:TIGR04250   2 PRSVDIDITGRCNLRCRYCSHfssAAETPTDLETAEWLRFFRELNRCSVLRVVLSGGEPFM--RSDF-REIIDgIVKNRM 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
7N7H_A         80 ELpsvSIVSNGSLIRDN---WFNKYGEClDILAISCDSFDEETNVLI---GRRQKGKNHVEALRR 138
Cdd:TIGR04250  79 RF---SILSNGTLITDAiasFLAATRRC-DYVQVSIDGSTPGTHDRLrgtGSFLQAVEGIELLRK 139
GeoRSP_rSAM TIGR04303
GeoRSP system radical SAM/SPASM protein; Members of this family are radical SAM/SPASM domain ...
1-163 5.10e-06

GeoRSP system radical SAM/SPASM protein; Members of this family are radical SAM/SPASM domain proteins from a cassette restricted to the genus Geobacter. Genes always found adjacent include a non-radical SAM protein with a closely related SPASM domain and a short stretch of N-terminal homology as well to this family, and also a PqqD-like protein. The three-gene cassette is designated GeoRSP for the genus Geobacter, this radical SAM protein, the SPASM domain protein, and the PqqD family protein.


Pssm-ID: 213916 [Multi-domain]  Cd Length: 325  Bit Score: 47.22  E-value: 5.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A          1 MTVPVSVNYHFTRQCNYQCGFCFHTAKTSFVLPIEEAKKGLLMLMKAGMEKVNFSGGEPFLHDRGKFVGELVRYCKQEle 80
Cdd:TIGR04303   1 LKAPLTINWAINNNCNFACRHCYSRGDTHEELPRDVLCACLGKVAAAGVFSVNFGGGEPLLRPDLLEIASCAAGSGMR-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A         81 lpsVSIVSNGSLI--------RDNWFNKYGecldilaISCDSFDEetnvLIGRRQKG--KNH---VEALRRVRDMcqqyK 147
Cdd:TIGR04303  79 ---VSMNSNGYLIdrdkaaalKDAGFSKVG-------ISIDSHLP----RVHDRFRGvdGSHgraVNALRHLAEA----G 140
                         170
                  ....*....|....*.
7N7H_A        148 VAFKLNTVVNTYNKQE 163
Cdd:TIGR04303 141 IKTSISTVICRINHTA 156
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
11-92 9.63e-06

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


Pssm-ID: 224101 [Multi-domain]  Cd Length: 260  Bit Score: 45.75  E-value: 9.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A       11 FTRQCNYQCGFC--FHTAKTSFVLPIEEAKKGLL---MLMKAGMEKVNFSGGEPFLHdrGKFVGELVRYCKqELELPsVS 85
Cdd:COG1180  41 FLQGCNLRCPYCqnPEISQRGREVSGEEVSPEVLvdkAFYSESGGGVTFSGGEPTLQ--AEFALDLLRAAK-ERGLH-VA 116

                ....*..
7N7H_A       86 IVSNGSL 92
Cdd:COG1180 117 LDTNGFL 123
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
12-156 1.32e-05

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 45.90  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A        12 TRQCNYQCGFCFHTA-----KTSFVLPIEEAKKGLLMLMKAGMEKVNFSGGEPFLHdrgKFVGELVRYCKQELELPSVSI 86
Cdd:PLN02951  65 TERCNLRCQYCMPEEgveltPKSHLLSQDEIVRLAGLFVAAGVDKIRLTGGEPTLR---KDIEDICLQLSSLKGLKTLAM 141
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7N7H_A        87 VSNG-SLIRDnwFNKYGEC-LDILAISCDSFDEETNVLIGRRqkgKNHVEALRRVRDMCQQYKVAFKLNTVV 156
Cdd:PLN02951 142 TTNGiTLSRK--LPRLKEAgLTSLNISLDTLVPAKFEFLTRR---KGHDRVLESIDTAIELGYNPVKVNCVV 208
rSAM_NirJ TIGR04051
heme d1 biosynthesis radical SAM protein NirJ; Heme d1 occurs in the cytochrome cd1 subunit of ...
4-145 1.76e-05

heme d1 biosynthesis radical SAM protein NirJ; Heme d1 occurs in the cytochrome cd1 subunit of nitrite reductase in species such as Pseudomonas stutzeri. NirJ is a radical SAM protein involved in its bioynthesis. In a number of species, distinct genes NirJ1 and NirJ2 are found in similar genomic regions; this model describe authentic NirJ from genomes with NirJ only. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 188566 [Multi-domain]  Cd Length: 354  Bit Score: 45.44  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A          4 PVsVNYHFTRQCNYQCGFCFHT-AKTSFV--LPIEEAKKGLLMLMKAGMEKVNFSGGEPFLHDRgkfVGELVRYCKQelE 80
Cdd:TIGR04051   2 PV-VIWNLIRRCNLTCKHCYSTsADIDFPgeLSTAEVLRVIDDLKAFGVPALILSGGEPLLRPD---IFEIAARARQ--L 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
7N7H_A         81 LPSVSIVSNGSLI-RDN-------WFNKYGECLDILAISCDSFdeetnvligRRQKGKnHVEALRRVRdMCQQ 145
Cdd:TIGR04051  76 GFYVALSTNGTLIdEGNiariaaaGFDYVGISIDGLEATHDRF---------RRLKGA-FDAALAGIR-LCKA 137
rSAM_skfB TIGR04403
sporulation killing factor system radical SAM maturase; Members of this family are a radical ...
3-153 4.17e-05

sporulation killing factor system radical SAM maturase; Members of this family are a radical SAM enzyme of post-translational modification of ribosomally translated peptides. In Bacillus subtilis, the enzyme SkfB creates a sactipeptide (sulfur-to-alpha-carbon) crosslink of Cys-4 to Met-12 of the mature form of sporulation killing factor (SkfA). In Paenibacillus larvae subsp. larvae B-3650, the Met is replaced by Leu, so the modification must be different. SkfB has 2 4Fe-4S clusters, one in its radical SAM domain (pfam04055) and one in a region that somewhat resembles the SPASM domain (TIGR04085).


Pssm-ID: 275196 [Multi-domain]  Cd Length: 402  Bit Score: 44.53  E-value: 4.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A          3 VPVSVNYHFTRQCNYQCGFCFhtAKTSFVLPIEEAKKGLLMLMKA----GMEKVNFSGGEPFLhdrGKFVGELVRYCKQE 78
Cdd:TIGR04403 102 LPISCTLQLTNACNLSCSFCY--ASSGKPYPEELATDQWIQVMQKlaavGVADVTLTGGEAKL---IKGFKEIVTVASSL 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A         79 LElpSVSIVSNGSlirdNWFNKYGECLDILA-----ISCDSFDEETNVLIGRRQKGKNHVEALRRVRDMCQQYKVAFKLN 153
Cdd:TIGR04403 177 FT--NVNVFSNGL----NWRDEEVELLSHLGnvsvqISIDGTPETHNLLRGRKGAFEESMNTIKRLAEANIPVIVAMTIN 250
AlbA NF012164
subtilosin maturase AlbA; AlbA is a radical SAM/SPASM domain-containing protein responsible ...
3-120 5.57e-05

subtilosin maturase AlbA; AlbA is a radical SAM/SPASM domain-containing protein responsible for introducing thioether crosslinks during that maturation of bacteriocins such subtilosin A.


Pssm-ID: 333728 [Multi-domain]  Cd Length: 442  Bit Score: 44.25  E-value: 5.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A         3 VPVSVNYHFTRQCNYQCGFCF--HTAKTSFVLPIEEAKKGLLMLMKAGMEKVNFSGGEPFLHDRGKfvgELVRYCKQELE 80
Cdd:NF012164 111 MPLHATFELTHRCNLKCAHCYleSSPEALGTVSIEQFKKTADMLFDNGVLTCEITGGEIFVHPNAN---EILDYVCKKFK 187
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
7N7H_A        81 lpSVSIVSNGSLIRD---NWFNKYGECLdILAISCDSFDEETN 120
Cdd:NF012164 188 --KVAVLTNGTLMRKeslELLKAYKQKI-IVGISLDSVNSEVH 227
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
14-214 6.05e-05

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


Pssm-ID: 223714 [Multi-domain]  Cd Length: 378  Bit Score: 43.97  E-value: 6.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A       14 QCNYQCGFCFHTAKTSF--VLPIEEAKKGLLMLMKA-GMEKVNFS--GGEPFLHdrGKFVGELVRYCKQELEL---PSVS 85
Cdd:COG0641  17 ECNLDCKYCFYLEKESLqrIMSDETLEEYVRQYIAAsNGDKVTFTwqGGEPLLA--GLDFYRKAVALQQKYANgktISNA 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A       86 IVSNGSLIRDNWFNKYGECLDILAISCDSfDEETNVLIGRRQKGKNHVEALRRVRDMCQQYKVAFKLNTVVNTYNKQ--E 163
Cdd:COG0641  95 LQTNGTLLNDEWAEFLAEHDFLIGISIDG-PEEIHDKYRVTKSGKGTFDRVMKGLELLQAHGVDFNTLTVVNRQNVLhpE 173
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
7N7H_A      164 DMTSHIQELcPVRWKVFQCLViaGENSGEDALRDaeqFLVSNHEFDQFISR 214
Cdd:COG0641 174 EIYHFLKSE-GSKFIQFIPLV--ESDNRGDSLLE---FSVTAEEYGQFLIA 218
rSAM_FibroRumin TIGR04136
radical SAM peptide maturase, FibroRumin system; Members of this protein family are radical ...
5-171 1.53e-04

radical SAM peptide maturase, FibroRumin system; Members of this protein family are radical SAM enzymes proposed to act on small, Cys-rich peptides encoded by tandem gene pairs. Members occur in enzymes Fibrobacter succinogenes subsp. succinogenes S85 (genes for their target peptides missed) and in Ruminococcus albus 8. This enzyme family is similar in sequence to the SCIFF (Six Cysteines in Forty-Five) system maturase (TIGR03974).


Pssm-ID: 200387 [Multi-domain]  Cd Length: 458  Bit Score: 42.64  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A          5 VSVNYH-FTRQCNYQCGFCF-----HTAKTSF---VLPIEEAKKGLLMLMK----AGMEKVN------FSGGEPFL-HDR 64
Cdd:TIGR04136  90 ISICYFiLSEQCNLACKYCFlgnndKEKRHNFakeLMSKEIADKAIEFFIKqleaSELDAEDnkaaiiFYGGEPLMnFET 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A         65 GKFVGELVRYCKQE---LELPSVSIVSNGSLIRDNWFNKYGECLDILAISCDSFDEETNVLigRRQKGKNHV-EALRRVR 140
Cdd:TIGR04136 170 LKYVAEKFNSLKSEekcLENAEFSMVSNGLLLSEERIIELRDLGVSIAISIDGCDEAANAM--RVDLAGNIVfPKILETL 247
                         170       180       190
                  ....*....|....*....|....*....|...
7N7H_A        141 DMCQQYKVAFKLNTVVN--TYNKQEDMTSHIQE 171
Cdd:TIGR04136 248 DIAKELGVNVSLSITLSeeTIKDQQDVIDLIDE 280
rSAM_PTO1314 TIGR03961
archaeal radical SAM protein, PTO1314 family; Members of this protein family average about 340 ...
15-117 4.24e-04

archaeal radical SAM protein, PTO1314 family; Members of this protein family average about 340 residues in length, with a radical SAM domain in the N-terminal 200 residues. The taxonomic distribution is restricted to non-methanogenic archaea, including Picrophilus torridus (locus PTO1314), Sulfolobus sp., Thermoplasma sp., Picrophilus torridus, and Metallosphaera sedula. The gene neighborhood is not conserved, and the function of this family is unknown. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 188476 [Multi-domain]  Cd Length: 332  Bit Score: 41.34  E-value: 4.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A         15 CNYQCGFC-FHTAKTSFVLPIEEAKKGLLMLMKAGMEKVNFSGGEPFLHDrgkfvgELVRYCKQELELPSVSIVSNGSLI 93
Cdd:TIGR03961  33 CNLRCEMCpFWRRKDEKLLSLEEEIKMMDALERAGVLFMGFEGGEPLLRR------DLPQILEESHKRFHTSLVTNGWLL 106
                          90       100
                  ....*....|....*....|....
7N7H_A         94 RDNwFNKYGECLDILAISCDSFDE 117
Cdd:TIGR03961 107 KDR-IKSISEYLDYLFVSIDGIGE 129
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
14-172 4.33e-04

Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal structure and biogenesis];


Pssm-ID: 223803 [Multi-domain]  Cd Length: 296  Bit Score: 41.13  E-value: 4.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A       14 QCNYQCGFC---FHTAKTS----FVLP--IEEAKKGLL-MLMKAGME--KVNFSG-GEPFLHDRgkfVGELVRYCKQELE 80
Cdd:COG0731  33 WCSYNCVYCwrgRTKKGTPerpeFIVEesILEELKLLLgYKGDEATEpdHVTISLsGEPTLYPN---LGELIEEIKKRGK 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A       81 LPSVsIVSNGSLirdnwfNKYGECL---DILAISCDSFDEETNVLIGRRQKGKNH---VEALRRVRDMCQQYKVAfkLNT 154
Cdd:COG0731 110 KTTF-LVTNGSL------PDVLEELklpDQLYVSLDAPDEKTFRRINRPHKKDSWekiLEGLEIFRSEYKGRTVI--RTT 180
                       170
                ....*....|....*...
7N7H_A      155 VVNTYNKQEDMTSHIQEL 172
Cdd:COG0731 181 LVKGINDDEEELEEYAEL 198
rSAM_Clo7bot TIGR04334
radical SAM/SPASM domain Clo7bot peptide maturase; In multiple strains of Clostridium ...
12-103 5.50e-04

radical SAM/SPASM domain Clo7bot peptide maturase; In multiple strains of Clostridium botulinum, this single radical SAM domain protein occurs next to a tandem array of seven homologous Cys-rich small peptides (see TIGR04333). Because this radical SAM enzyme contains the SPASM domain, associated with peptide modification, it is proposed to modify all seven C. botulinum targets, hence the name Clo7bot for this system. Suggested gene symbol is ctpM (Clostridial Tandem Peptide Maturase). [Protein fate, Protein modification and repair]


Pssm-ID: 213947 [Multi-domain]  Cd Length: 440  Bit Score: 41.00  E-value: 5.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A         12 TRQCNYQCGFCFHTAKTSFVlpIEEAKKGLL-MLMKAGMEKVNFS----GGEPFLHDRGKF--VGELVRYCKQELELPSV 84
Cdd:TIGR04334  97 TLSCNFACPYCYENPKSGIM--DKNVTDALIeMITEEAKKKKDINitwyGGEPLIAKNVVFdmSQKIIEICKKHNTNYSA 174
                          90
                  ....*....|....*....
7N7H_A         85 SIVSNGSLIRDNWFNKYGE 103
Cdd:TIGR04334 175 YIVTNGYLIDDVVISKLND 193
rSAM_pair_HxsC TIGR03977
His-Xaa-Ser system radical SAM maturase HxsC; This model describes the downstream member, HxsC, ...
12-95 6.96e-04

His-Xaa-Ser system radical SAM maturase HxsC; This model describes the downstream member, HxsC, of a pair of uncharacterized radical SAM proteins, regularly found in the context of a small protein with four or more repeats of the tripeptide His-Xaa-Ser (HXS). This enzyme appears to be part of a peptide modification system.


Pssm-ID: 274895  Cd Length: 292  Bit Score: 40.30  E-value: 6.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A         12 TRQCNYQCGFCFHTAK-TSFVLPIEEAKKgLLMLMKAGMEKVNFSGGEPFLHDRGKFvgELVRYCKQELELPSVSIVSNG 90
Cdd:TIGR03977  32 TERCNNYCLMCSQPPKkVDDSWLLDEALE-AIALFPENPRVLGITGGEPTLLGEGFF--RFLRFIKKKLPQTALHVLTNG 108

                  ....*
7N7H_A         91 SLIRD 95
Cdd:TIGR03977 109 RAFSD 113
PRK13361 PRK13361
GTP 3',8-cyclase MoaA;
5-156 7.63e-04

GTP 3',8-cyclase MoaA;


Pssm-ID: 237364 [Multi-domain]  Cd Length: 329  Bit Score: 40.39  E-value: 7.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A         5 VSVnyhfTRQCNYQCGFCFhTAKTSF-----VLPIEEakkgLLMLMKAGME----KVNFSGGEPFLHdRGkfVGELVRYC 75
Cdd:PRK13361  18 LSV----TDRCDFRCVYCM-SEDPCFlprdqVLSLEE----LAWLAQAFTElgvrKIRLTGGEPLVR-RG--CDQLVARL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A        76 KQELELPSVSIVSNGSLIRDNWFNKYGECLDILAISCDSFDEETNVLIGRRQKgknhveaLRRVRDMCQQYKVA----FK 151
Cdd:PRK13361  86 GKLPGLEELSLTTNGSRLARFAAELADAGLKRLNISLDTLRPELFAALTRNGR-------LERVIAGIDAAKAAgferIK 158

                 ....*
7N7H_A       152 LNTVV 156
Cdd:PRK13361 159 LNAVI 163
quino_hemo_SAM TIGR03906
quinohemoprotein amine dehydrogenase maturation protein; Members of this protein family are ...
12-99 8.13e-04

quinohemoprotein amine dehydrogenase maturation protein; Members of this protein family are radical SAM enzymes responsible for post-translational modifications to the gamma subunit of quinohemoprotein amine dehydrogenases. Ono, et al. () suggest that this protein is responsible for intrapeptidyl thioether cross-linking rather than cysteine tryptophylquinone biogenesis in the gamma subunit. [Protein fate, Protein modification and repair]


Pssm-ID: 274848 [Multi-domain]  Cd Length: 467  Bit Score: 40.53  E-value: 8.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A         12 TRQCNYQCGFCFH----TAKTSFVLPIEEAKKGLLMLMKAGMEK----VNFSGGEPFLhdRGKFVGELVRYCKQ------ 77
Cdd:TIGR03906 101 NTGCNLSCTYCYKedltTPSKGPKMSLETAKASVELLLAESGHRervnVVFFGGEPLT--NFPLIRAVVEYAEQraaaag 178
                          90       100
                  ....*....|....*....|....*.
7N7H_A         78 -ELELpsvSIVSNGSLIRD---NWFN 99
Cdd:TIGR03906 179 kQIEF---SLTTNATLLTEeivDFLN 201
Fer4_12 pfam13353
4Fe-4S single cluster domain. This family includes proteins containing domains which bind to ...
15-108 8.23e-04

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: 379137  Cd Length: 140  Bit Score: 38.70  E-value: 8.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A         15 CNYQCGFCFHTA----KTSFVLPIEEAKKGLLMLMKAGMEKVNFSGGEPFLHDRGKFVGELVRYCKQELELPSVsIVSNG 90
Cdd:pfam13353  15 CNHHCKGCFNPEtwdfKGGKPFTEELEDEIIEDLNDPYIQGLTLSGGEPLLPQNAEALLELVKRVREEFPEKDI-WLYTG 93
                          90       100
                  ....*....|....*....|..
7N7H_A         91 S----LIRDNWFNKYGECLDIL 108
Cdd:pfam13353  94 YtleeLLPEQETRELLSYIDVL 115
rSAM_ocin_clost TIGR04068
Cys-rich peptide radical SAM maturase CcpM; Members of this family are radical SAM enzymes ...
12-95 1.41e-03

Cys-rich peptide radical SAM maturase CcpM; Members of this family are radical SAM enzymes that occur next to clostridial Cys-rich predicted bacteriocin (or other class of ribosomal natural product) precursors (see families TIGR04065 and TIGR04067). They include a TIGR04085 C-terminal additional 4Fe4S cluster-binding domain that is associated with peptide modification by radical SAM enzymes, and they are proposed to be ribosomal natural product maturases. The gene symbol ccpM is assigned, for Clostridial Cys-rich Peptide Maturase. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274958 [Multi-domain]  Cd Length: 459  Bit Score: 39.59  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A         12 TRQCNYQCGFCFHTAK------TSFVLPIEEAKKGLLMLMK--AGMEKVNFS--GGEPFLhdRGKFVGELVRYCKQELEL 81
Cdd:TIGR04068  89 TQQCNLRCKYCAYSGSydnrvhSNKRMSIETAKKAIDFLIKhsEDTDELNLGfyGGEPLL--EFELIKECVEYAKEKAEG 166
                          90
                  ....*....|....*.
7N7H_A         82 PSV--SIVSNGSLIRD 95
Cdd:TIGR04068 167 KKInfNMTTNGTLLTE 182
pyrrolys_PylB TIGR03910
pyrrolysine biosynthesis radical SAM protein; This model describes a radical SAM protein, PylB, ...
10-106 1.51e-03

pyrrolysine biosynthesis radical SAM protein; This model describes a radical SAM protein, PylB, that is part of the three-gene cassette sufficient for the biosynthesis of pyrrolysine (the twenty-second amino acid) when expressed heterologously in E. coli. The pyrrolysine next is ligated to its own tRNA and incorporated at special UAG codons. [Amino acid biosynthesis, Other]


Pssm-ID: 188425 [Multi-domain]  Cd Length: 347  Bit Score: 39.35  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A         10 HFTRQCNYQCGFCFHTAKTSFV----LPIEEAKKGLLMLMKAGMEKVNFSGGE-PFLHDRGKF---VGELVRYCKQELEL 81
Cdd:TIGR03910  61 YFSTFCKNNCAFCYYRKSNHAIrryrKTREEIKAAARALADSGVHLIDLTMGEdPYYHNDPRGferLAELVRMVKEETGL 140
                          90       100       110
                  ....*....|....*....|....*....|...
7N7H_A         82 P---SVSIVSNGSLIR-----DNWFNKYGECLD 106
Cdd:TIGR03910 141 PvmiSPGVVDNETLKKlkeagANWYACYQETHD 173
rSAM_BlsE TIGR04466
cytosylglucuronate decarboxylase; BlsE, part of the blasticidin S biosynthetic pathway, is a ...
9-163 1.54e-03

cytosylglucuronate decarboxylase; BlsE, part of the blasticidin S biosynthetic pathway, is a radical SAM enzyme that performs a decarboxylation at C5 of the glucoside residue. MilG in mildiomycin biosynthesis is equivalent. This enzyme follows CGA synthase and makes the pyranoside core moiety of a class of peptidyl nucleoside antibiotics. [Cellular processes, Toxin production and resistance]


Pssm-ID: 275259 [Multi-domain]  Cd Length: 327  Bit Score: 39.46  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A          9 YHFTR---QCNYQCGFC-FHTAKTSFVLPIEEAKKGLLMLMKAGMEKVNFSGGEPFLHDRgkfVGELVRYCKQELElpSV 84
Cdd:TIGR04466   4 YLFIRileACNADCFMCeFALSRDTYRFSLEDFDELLPQAVEAGVGYVRFTGGEPLMHGE---VLELVREGTAAGM--KM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A         85 SIVSNGSLIrDNWFNKYGEC-LDILAISCDSFDEETNVlIGRRQKG--KNHVEALRRVRDMcqqyKVAFKLNTVVNTYNK 161
Cdd:TIGR04466  79 SLITNGMRL-PRMVDRLAEAgLAQVIVSLDGSSGETHD-VYRRSPGmfDRGLRGLRRASRL----GVLPRVNTVVGPHNY 152

                  ..
7N7H_A        162 QE 163
Cdd:TIGR04466 153 TQ 154
rSAM_ahbC_deAc TIGR04546
12,18-didecarboxysiroheme deacetylase; This model describes one of a pair of radical SAM ...
4-163 2.26e-03

12,18-didecarboxysiroheme deacetylase; This model describes one of a pair of radical SAM enzymes involved in the alternative heme biosynthesis (ahb) pathway for heme b biosynthesis from siroheme. This anaerobic pathway occurs in sulfate-reducing bacteria and methanogens. A very similar pair of radical SAM enzymes (TIGR04054, TIGR04055) is involved in heme d1 biosynthesis in species such as Heliobacillus mobilis and Heliophilum fasciatum. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 275339 [Multi-domain]  Cd Length: 390  Bit Score: 39.03  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A          4 PVSVnYHFTRQCNYQCGFCFHTAKT---SFVLPIEEAKKGLLMLMKAGMEKVNFSGGEPFLhdRGKFVgELVRYCKQElE 80
Cdd:TIGR04546  39 PVVV-WNMTRRCNLKCVHCYAHAQDeefKDEMSTEEGKALIDDLAAFGAPVLLFSGGEPLM--RKDLP-ELAAYAVSK-G 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A         81 LPSVsIVSNGSLIRDNWFNKYGEC-LDILAISCDSFdEETNvliGRRQKGKNHVEALRRVRDMCQQYKVAFKLNTVVNTY 159
Cdd:TIGR04546 114 MRAV-ISTNGTLITKEKARELKEVgLSYVGISLDGG-EEVH---DRFRGVPGAFDAALKGIENCREEGIKVGLRFTINKR 188

                  ....
7N7H_A        160 NKQE 163
Cdd:TIGR04546 189 NVAD 192
Fer4_14 pfam13394
4Fe-4S single cluster domain.
15-109 4.28e-03

4Fe-4S single cluster domain.


Pssm-ID: 379159  Cd Length: 115  Bit Score: 36.13  E-value: 4.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A         15 CNYQCGFCFHTAKTSF---VLPIEEAKKGLLMLMKAGMEKVN---FSGGEPFLHDRGKFVGELVRYCKQELELPSVSIVS 88
Cdd:pfam13394   6 CNHSCPGCYNKETWNFsygKPFTEELEDQIIDDLKDSYIKRQglvLTGGEPLHYLNLPVLLKLVKRVREEYPEKDIWLWT 85
                          90       100
                  ....*....|....*....|.
7N7H_A         89 NGSLIRDNWFNKYGECLDILA 109
Cdd:pfam13394  86 GYTLEIDFDFPDYKEQLFMLS 106
ThiH COG1060
2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzyme MqnC [Coenzyme transport and ...
2-78 4.90e-03

2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzyme MqnC [Coenzyme transport and metabolism];


Pssm-ID: 223988 [Multi-domain]  Cd Length: 370  Bit Score: 38.04  E-value: 4.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7N7H_A        2 TVPVSVNYH--FTRQCNYQCGFC-FHT---AKTSFVLPIEEAKKGLLMLMKAGMEKVNFSGGE-PFLhdRGKFVGELVRY 74
Cdd:COG1060  54 GVTYVVNRNinYTNICVNDCTFCaFYRkpgDPKAYTLSPEEILEEVREAVKRGITEVLIVGGEhPEL--SLEYYEELFRT 131

                ....
7N7H_A       75 CKQE 78
Cdd:COG1060 132 IKEE 135
COG5014 COG5014
Uncharacterized Fe-S cluster-containing protein, radical SAM superfamily [General function ...
15-61 5.02e-03

Uncharacterized Fe-S cluster-containing protein, radical SAM superfamily [General function prediction only];


Pssm-ID: 227347  Cd Length: 228  Bit Score: 37.55  E-value: 5.02e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
7N7H_A       15 CNYQCGFCFHTAKTSFVL-------PIEEAKKGLLMLMKAGMEKVNFSGGEPFL 61
Cdd:COG5014  51 CNLLCAYCWNYFRNLRPKragdflsPEEVAERLLEISKKRGCDLVRISGAEPIL 104
rSAM_Cxxx_rpt TIGR04115
radical SAM peptide maturase, CXXX-repeat target family; Members of this radical SAM domain ...
6-61 5.21e-03

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: 37.94  E-value: 5.21e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
7N7H_A          6 SVNYHFTRQCNYQCGFCFHTAKTSF-VLPIEEAKKGLLMLMKA----GMEKV--NFSGGEPFL 61
Cdd:TIGR04115   3 SITFIVTDDCQLACKYCYQTGKNKNkRMSFETAKKAVDYILSGnkgfGEPSViwDFIGGEPLL 65
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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