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Conserved domains on  [gi|499322109|ref|WP_011012601|]
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MULTISPECIES: tetraether lipid synthase Tes [Pyrococcus]

Protein Classification

radical SAM protein( domain architecture ID 11449413)

radical SAM protein generates radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity; contains a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster; transfers a single electron from the iron-sulfur cluster to SAM leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MoaA2 super family cl34384
C-terminal domain of the GTP 3',8'-cyclase MoaA, radical SAM superfamily (molybdenum cofactor ...
45-551 8.18e-176

C-terminal domain of the GTP 3',8'-cyclase MoaA, radical SAM superfamily (molybdenum cofactor biosynthesis) [Coenzyme transport and metabolism];


The actual alignment was detected with superfamily member COG1964:

Pssm-ID: 441567 [Multi-domain]  Cd Length: 473  Bit Score: 505.95  E-value: 8.18e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109  45 ANRGYGepLPHRTYSLCPESRRVVPAVVWEKDGMVWITKKCPE-GIITDLYSEDVDLYYRFLRWKFEDKKLFSVNVPnTG 123
Cdd:COG1964    1 KTRPYL--FYETTTSLCPECLKVVDAKIVEEDGKVYMEKRCPEhGEFRDLYWSDAEYYRRFEEYNKPGEGPLNFNTE-TE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 124 INCPFDCGLCARHRSHTNLLNIVLTNRCNLSCWYCFFYAREGePVYEPTLEQIRMMLRNAKKENPIgANAVQFTGGEPTL 203
Cdd:COG1964   78 YGCPYDCGLCPDHEQHTCLALIEVTNRCNLNCPICFANSGPG-YGYEPSLEEIEKMLDALVREEGE-PDVVQFSGGEPTV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 204 RDDLIEIIKIAKEEGYDHVQLNTDGIRLAFEPELVKKIREAG-VNTLYLSYDGMTP----QTNWKNHWEI-PLIFENVRK 277
Cdd:COG1964  156 HPDLFEILDLAKERPIKHVMINTNGIRIAKDPDFAERLAEAGpLFEVYLQFDGLSDepyrRLRGADLLEVkLKAIENLRK 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 278 AGgPGIVLVPTLIRNVNDHEAGAIINFGLNHlDIVRGVNFQPISLVGRVPKKERQRFRITIAGAIKKIEEQTNGAISRDD 357
Cdd:COG1964  236 AG-ISTTLVPTLVKGVNDHEIGDIIRFALQN-PCVRGVTFQPVAFAGRIPQFDPEEDRITLPDVRRLIEEQTDGLFTPED 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 358 WYPIPiagyiarffeaftgkhyymTSHYACGAATYVFldKEEKKVIPIPRFIDVEGFVEFLVEKAEEiERARFKGLAKLK 437
Cdd:COG1964  314 FYPVP-------------------CCHPHCGAMTYAL--KDGGKVIPLTRFIDVEGLLEGLANTIAF-EEDKALLKKSLP 371
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 438 aigetvfikfkQFYDEKYAPKGL--DVLGLIKNAFMHgnYDALGQFHTKTLFLGMMHFMDEYNYDVERVERCVIHYAMPD 515
Cdd:COG1964  372 -----------KLFSESKSPESIaeNLKDLLCCLPKG--VEALAELHENVFRIGIMHFMDAYNFDVERVKKCCIHYVTPD 438
                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 499322109 516 GRIVPFCTFNVIpeIYRDKVQRQFSYSWEEWKKLHP 551
Cdd:COG1964  439 GRIIPFCTYNLF--LYRDEVEEKFSKPLREWKARRK 472
 
Name Accession Description Interval E-value
MoaA2 COG1964
C-terminal domain of the GTP 3',8'-cyclase MoaA, radical SAM superfamily (molybdenum cofactor ...
45-551 8.18e-176

C-terminal domain of the GTP 3',8'-cyclase MoaA, radical SAM superfamily (molybdenum cofactor biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 441567 [Multi-domain]  Cd Length: 473  Bit Score: 505.95  E-value: 8.18e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109  45 ANRGYGepLPHRTYSLCPESRRVVPAVVWEKDGMVWITKKCPE-GIITDLYSEDVDLYYRFLRWKFEDKKLFSVNVPnTG 123
Cdd:COG1964    1 KTRPYL--FYETTTSLCPECLKVVDAKIVEEDGKVYMEKRCPEhGEFRDLYWSDAEYYRRFEEYNKPGEGPLNFNTE-TE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 124 INCPFDCGLCARHRSHTNLLNIVLTNRCNLSCWYCFFYAREGePVYEPTLEQIRMMLRNAKKENPIgANAVQFTGGEPTL 203
Cdd:COG1964   78 YGCPYDCGLCPDHEQHTCLALIEVTNRCNLNCPICFANSGPG-YGYEPSLEEIEKMLDALVREEGE-PDVVQFSGGEPTV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 204 RDDLIEIIKIAKEEGYDHVQLNTDGIRLAFEPELVKKIREAG-VNTLYLSYDGMTP----QTNWKNHWEI-PLIFENVRK 277
Cdd:COG1964  156 HPDLFEILDLAKERPIKHVMINTNGIRIAKDPDFAERLAEAGpLFEVYLQFDGLSDepyrRLRGADLLEVkLKAIENLRK 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 278 AGgPGIVLVPTLIRNVNDHEAGAIINFGLNHlDIVRGVNFQPISLVGRVPKKERQRFRITIAGAIKKIEEQTNGAISRDD 357
Cdd:COG1964  236 AG-ISTTLVPTLVKGVNDHEIGDIIRFALQN-PCVRGVTFQPVAFAGRIPQFDPEEDRITLPDVRRLIEEQTDGLFTPED 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 358 WYPIPiagyiarffeaftgkhyymTSHYACGAATYVFldKEEKKVIPIPRFIDVEGFVEFLVEKAEEiERARFKGLAKLK 437
Cdd:COG1964  314 FYPVP-------------------CCHPHCGAMTYAL--KDGGKVIPLTRFIDVEGLLEGLANTIAF-EEDKALLKKSLP 371
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 438 aigetvfikfkQFYDEKYAPKGL--DVLGLIKNAFMHgnYDALGQFHTKTLFLGMMHFMDEYNYDVERVERCVIHYAMPD 515
Cdd:COG1964  372 -----------KLFSESKSPESIaeNLKDLLCCLPKG--VEALAELHENVFRIGIMHFMDAYNFDVERVKKCCIHYVTPD 438
                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 499322109 516 GRIVPFCTFNVIpeIYRDKVQRQFSYSWEEWKKLHP 551
Cdd:COG1964  439 GRIIPFCTYNLF--LYRDEVEEKFSKPLREWKARRK 472
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
147-297 4.72e-23

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: 95.67  E-value: 4.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109  147 LTNRCNLSCWYCFFYA-REGEPVYEPTLEQIRMMLRNAKKenpIGANAVQFTGGEPTLRDDLIEIIKIAKEE---GYDHV 222
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSiRARGKGRELSPEEILEEAKELKR---LGVEVVILGGGEPLLLPDLVELLERLLKLelaEGIRI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109  223 QLNTDGIRLafEPELVKKIREAGVNTLYLSYDGMTPQ----TNWKNHWEIPL-IFENVRKAGGPGIVLVPTLIRNVNDHE 297
Cdd:pfam04055  78 TLETNGTLL--DEELLELLKEAGLDRVSIGLESGDDEvlklINRGHTFEEVLeALELLREAGIPVVTDNIVGLPGETDED 155
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
145-327 5.02e-20

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: 88.54  E-value: 5.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 145 IVLTNRCNLSCWYCFFYAREGEPVYEPTLEQIrmMLRNAKKENPIGANAVQFTGGEPTLRDDLIEIIKIAKEEGYD-HVQ 223
Cdd:cd01335    1 LELTRGCNLNCGFCSNPASKGRGPESPPEIEE--ILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGfEIS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 224 LNTDGIrlAFEPELVKKIREAGVNTLYLSYDGMTPQTNWKNH--WEIPL-IFENVRKAGGPGIVLVPTLI--RNVNDHEA 298
Cdd:cd01335   79 IETNGT--LLTEELLKELKELGLDGVGVSLDSGDEEVADKIRgsGESFKeRLEALKELREAGLGLSTTLLvgLGDEDEED 156
                        170       180
                 ....*....|....*....|....*....
gi 499322109 299 GAIINFGLNHLDIVRGVNFQPISLVGRVP 327
Cdd:cd01335  157 DLEELELLAEFRSPDRVSLFRLLPEEGTP 185
moaA PRK00164
GTP 3',8-cyclase MoaA;
143-308 1.91e-15

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 77.87  E-value: 1.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 143 LNIVLTNRCNLSCWYCFfyaREGEPVYEP-----TLEQIRMMLRNAKKEnpiGANAVQFTGGEPTLRDDLIEIIK-IAKE 216
Cdd:PRK00164  19 LRISVTDRCNFRCTYCM---PEGYLPFLPkeellSLEEIERLVRAFVAL---GVRKVRLTGGEPLLRKDLEDIIAaLAAL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 217 EGYDHVQLNTDGIRLAfepELVKKIREAGVNTLYLSYDGMTPQ-----TNWKNhweipliFENV-------RKAGgpgiv 284
Cdd:PRK00164  93 PGIRDLALTTNGYLLA---RRAAALKDAGLDRVNVSLDSLDPErfkaiTGRDR-------LDQVlagidaaLAAG----- 157
                        170       180
                 ....*....|....*....|....*....
gi 499322109 285 LVPT-----LIRNVNDHEAGAIINFGLNH 308
Cdd:PRK00164 158 LTPVkvnavLMKGVNDDEIPDLLEWAKDR 186
SCM_rSAM_ScmF TIGR04251
SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in ...
147-262 9.65e-09

SynChlorMet cassette radical SAM/SPASM protein ScmF; 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 more distant in sequence.


Pssm-ID: 211974 [Multi-domain]  Cd Length: 353  Bit Score: 57.54  E-value: 9.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109  147 LTNRCNLSCWYCFF---YAREGE--PVYEPTLeqIRMMLRNAKkenPIGANAVQFTGGEPTLRDDLIEIIKIAKEEGydh 221
Cdd:TIGR04251  10 LTEGCNLKCRHCWIdpkYQGEGEqhPSLDPSL--FRSIIRQAI---PLGLTSVKLTGGEPLLHPAIGEILECIGENN--- 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 499322109  222 VQLNTDGIRLAFEPELVKKIREAGVNTLYLSYDGMTPQT-NW 262
Cdd:TIGR04251  82 LQLSVETNGLLCTPQTARDLASCETPFVSVSLDGVDAAThDW 123
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
145-252 1.61e-07

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: 52.40  E-value: 1.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109   145 IVLTNRCNLSCWYCFFYAREGEPVYEP---TLEQIRMMLRNAKKENPIGANAvqFTGGEPTL--RDDLIEIIK-IAKEEG 218
Cdd:smart00729   5 YIITRGCPRRCTFCSFPSLRGKLRSRYleaLVREIELLAEKGEKEGLVGTVF--IGGGTPTLlsPEQLEELLEaIREILG 82
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 499322109   219 YDHVQLNTDGIRL-AFEPELVKKIREAGVNTLYLS 252
Cdd:smart00729  83 LAKDVEITIETRPdTLTEELLEALKEAGVNRVSLG 117
 
Name Accession Description Interval E-value
MoaA2 COG1964
C-terminal domain of the GTP 3',8'-cyclase MoaA, radical SAM superfamily (molybdenum cofactor ...
45-551 8.18e-176

C-terminal domain of the GTP 3',8'-cyclase MoaA, radical SAM superfamily (molybdenum cofactor biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 441567 [Multi-domain]  Cd Length: 473  Bit Score: 505.95  E-value: 8.18e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109  45 ANRGYGepLPHRTYSLCPESRRVVPAVVWEKDGMVWITKKCPE-GIITDLYSEDVDLYYRFLRWKFEDKKLFSVNVPnTG 123
Cdd:COG1964    1 KTRPYL--FYETTTSLCPECLKVVDAKIVEEDGKVYMEKRCPEhGEFRDLYWSDAEYYRRFEEYNKPGEGPLNFNTE-TE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 124 INCPFDCGLCARHRSHTNLLNIVLTNRCNLSCWYCFFYAREGePVYEPTLEQIRMMLRNAKKENPIgANAVQFTGGEPTL 203
Cdd:COG1964   78 YGCPYDCGLCPDHEQHTCLALIEVTNRCNLNCPICFANSGPG-YGYEPSLEEIEKMLDALVREEGE-PDVVQFSGGEPTV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 204 RDDLIEIIKIAKEEGYDHVQLNTDGIRLAFEPELVKKIREAG-VNTLYLSYDGMTP----QTNWKNHWEI-PLIFENVRK 277
Cdd:COG1964  156 HPDLFEILDLAKERPIKHVMINTNGIRIAKDPDFAERLAEAGpLFEVYLQFDGLSDepyrRLRGADLLEVkLKAIENLRK 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 278 AGgPGIVLVPTLIRNVNDHEAGAIINFGLNHlDIVRGVNFQPISLVGRVPKKERQRFRITIAGAIKKIEEQTNGAISRDD 357
Cdd:COG1964  236 AG-ISTTLVPTLVKGVNDHEIGDIIRFALQN-PCVRGVTFQPVAFAGRIPQFDPEEDRITLPDVRRLIEEQTDGLFTPED 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 358 WYPIPiagyiarffeaftgkhyymTSHYACGAATYVFldKEEKKVIPIPRFIDVEGFVEFLVEKAEEiERARFKGLAKLK 437
Cdd:COG1964  314 FYPVP-------------------CCHPHCGAMTYAL--KDGGKVIPLTRFIDVEGLLEGLANTIAF-EEDKALLKKSLP 371
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 438 aigetvfikfkQFYDEKYAPKGL--DVLGLIKNAFMHgnYDALGQFHTKTLFLGMMHFMDEYNYDVERVERCVIHYAMPD 515
Cdd:COG1964  372 -----------KLFSESKSPESIaeNLKDLLCCLPKG--VEALAELHENVFRIGIMHFMDAYNFDVERVKKCCIHYVTPD 438
                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 499322109 516 GRIVPFCTFNVIpeIYRDKVQRQFSYSWEEWKKLHP 551
Cdd:COG1964  439 GRIIPFCTYNLF--LYRDEVEEKFSKPLREWKARRK 472
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
142-261 1.34e-25

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: 103.06  E-value: 1.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 142 LLNIVLTNRCNLSCWYCFFYAREGEPvYEPTLEQIRMMLRNAKKenpIGANAVQFTGGEPTLRDDLIEIIKIAKEEGYdH 221
Cdd:COG0535    1 RLQIELTNRCNLRCKHCYADAGPKRP-GELSTEEAKRILDELAE---LGVKVVGLTGGEPLLRPDLFELVEYAKELGI-R 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 499322109 222 VQLNTDGIRLafEPELVKKIREAGVNTLYLSYDGMTPQTN 261
Cdd:COG0535   76 VNLSTNGTLL--TEELAERLAEAGLDHVTISLDGVDPETH 113
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
147-297 4.72e-23

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: 95.67  E-value: 4.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109  147 LTNRCNLSCWYCFFYA-REGEPVYEPTLEQIRMMLRNAKKenpIGANAVQFTGGEPTLRDDLIEIIKIAKEE---GYDHV 222
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSiRARGKGRELSPEEILEEAKELKR---LGVEVVILGGGEPLLLPDLVELLERLLKLelaEGIRI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109  223 QLNTDGIRLafEPELVKKIREAGVNTLYLSYDGMTPQ----TNWKNHWEIPL-IFENVRKAGGPGIVLVPTLIRNVNDHE 297
Cdd:pfam04055  78 TLETNGTLL--DEELLELLKEAGLDRVSIGLESGDDEvlklINRGHTFEEVLeALELLREAGIPVVTDNIVGLPGETDED 155
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
145-327 5.02e-20

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: 88.54  E-value: 5.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 145 IVLTNRCNLSCWYCFFYAREGEPVYEPTLEQIrmMLRNAKKENPIGANAVQFTGGEPTLRDDLIEIIKIAKEEGYD-HVQ 223
Cdd:cd01335    1 LELTRGCNLNCGFCSNPASKGRGPESPPEIEE--ILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGfEIS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 224 LNTDGIrlAFEPELVKKIREAGVNTLYLSYDGMTPQTNWKNH--WEIPL-IFENVRKAGGPGIVLVPTLI--RNVNDHEA 298
Cdd:cd01335   79 IETNGT--LLTEELLKELKELGLDGVGVSLDSGDEEVADKIRgsGESFKeRLEALKELREAGLGLSTTLLvgLGDEDEED 156
                        170       180
                 ....*....|....*....|....*....
gi 499322109 299 GAIINFGLNHLDIVRGVNFQPISLVGRVP 327
Cdd:cd01335  157 DLEELELLAEFRSPDRVSLFRLLPEEGTP 185
moaA PRK00164
GTP 3',8-cyclase MoaA;
143-308 1.91e-15

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 77.87  E-value: 1.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 143 LNIVLTNRCNLSCWYCFfyaREGEPVYEP-----TLEQIRMMLRNAKKEnpiGANAVQFTGGEPTLRDDLIEIIK-IAKE 216
Cdd:PRK00164  19 LRISVTDRCNFRCTYCM---PEGYLPFLPkeellSLEEIERLVRAFVAL---GVRKVRLTGGEPLLRKDLEDIIAaLAAL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 217 EGYDHVQLNTDGIRLAfepELVKKIREAGVNTLYLSYDGMTPQ-----TNWKNhweipliFENV-------RKAGgpgiv 284
Cdd:PRK00164  93 PGIRDLALTTNGYLLA---RRAAALKDAGLDRVNVSLDSLDPErfkaiTGRDR-------LDQVlagidaaLAAG----- 157
                        170       180
                 ....*....|....*....|....*....
gi 499322109 285 LVPT-----LIRNVNDHEAGAIINFGLNH 308
Cdd:PRK00164 158 LTPVkvnavLMKGVNDDEIPDLLEWAKDR 186
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
137-308 6.06e-15

GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and metabolism]; GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 442141 [Multi-domain]  Cd Length: 329  Bit Score: 76.25  E-value: 6.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 137 RSHTNLlNIVLTNRCNLSCWYCFfyaREGEPVYEP-----TLEQIRMMLRNAKKenpIGANAVQFTGGEPTLRDDLIEII 211
Cdd:COG2896   11 RPIDYL-RISVTDRCNFRCTYCM---PEEGYQFLPkeellSFEEIERLVRAFVE---LGVRKIRLTGGEPLLRKDLPELI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 212 K-IAKEEGYDHVQLNTDGIRLAfepELVKKIREAGVNTLYLSYDGMTPQ-----TNWKNhweipliFENV-------RKA 278
Cdd:COG2896   84 ArLAALPGIEDLALTTNGSLLA---RYAEALKAAGLDRVNVSLDSLDPErfrriTRRDD-------LDKVlagidaaLAA 153
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 499322109 279 GgpgivLVPT-----LIRNVNDHEAGAIINFGLNH 308
Cdd:COG2896  154 G-----LTPVkinavVMRGVNDDEILDLLEFAKER 183
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
137-322 6.09e-14

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 73.64  E-value: 6.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 137 RSHtNLLNIVLTNRCNLSCWYCFfyAREGEPVY-EPTLEQIRMMLRNAKKENPIGANAVQFTGGEPTLRDDLIEIIK-IA 214
Cdd:PLN02951  55 RRH-NYLRISLTERCNLRCQYCM--PEEGVELTpKSHLLSQDEIVRLAGLFVAAGVDKIRLTGGEPTLRKDIEDICLqLS 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 215 KEEGYDHVQLNTDGIRLAFE-PELVkkirEAGVNTLYLSYDGMTPQ-----TNWKNHWEiplIFENVRKAGGPGI--VLV 286
Cdd:PLN02951 132 SLKGLKTLAMTTNGITLSRKlPRLK----EAGLTSLNISLDTLVPAkfeflTRRKGHDR---VLESIDTAIELGYnpVKV 204
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 499322109 287 PTLI-RNVNDHEAgaiinfglnhLDIVRGVNFQPISL 322
Cdd:PLN02951 205 NCVVmRGFNDDEI----------CDFVELTRDKPINV 231
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
143-255 3.02e-10

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 61.93  E-value: 3.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 143 LNIVLTNRCNLSCWYCFFYAREGEPVY---EPTLEQ-IRMMLRNAKKENPIganAVQFTGGEPTLRDDLI-EIIKIAKEE 217
Cdd:COG0641    3 LVLKPTSRCNLRCSYCYYSEGDEGSRRrmsEETAEKaIDFLIESSGPGKEL---TITFFGGEPLLNFDFIkEIVEYARKY 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 499322109 218 GYDHVQLN----TDGIRLafEPELVKKIREAGVNTLyLSYDG 255
Cdd:COG0641   80 AKKGKKIRfsiqTNGTLL--DDEWIDFLKENGFSVG-ISLDG 118
COG2108 COG2108
Uncharacterized radical SAM domain-containing protein [Function unknown];
147-247 8.61e-09

Uncharacterized radical SAM domain-containing protein [Function unknown];


Pssm-ID: 441711 [Multi-domain]  Cd Length: 361  Bit Score: 57.67  E-value: 8.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 147 LTNRCNLSCWYCF----------FYAREgEPVYEPT--LEQIRMMlrnakkenpiGANAVQFTGGEPTLR-DDLIEIIKI 213
Cdd:COG2108   33 ITGLCNRNCFYCPlseerkgkdvIYANE-RPVESDEdvIEEARRM----------GALGAGITGGEPLLVlDRTLEYIRL 101
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 499322109 214 AKEE-GYD-HVQLNTDGIrlAFEPELVKKIREAGVN 247
Cdd:COG2108  102 LKEEfGPDhHIHLYTNGI--LADEDVLRKLADAGLD 135
SCM_rSAM_ScmF TIGR04251
SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in ...
147-262 9.65e-09

SynChlorMet cassette radical SAM/SPASM protein ScmF; 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 more distant in sequence.


Pssm-ID: 211974 [Multi-domain]  Cd Length: 353  Bit Score: 57.54  E-value: 9.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109  147 LTNRCNLSCWYCFF---YAREGE--PVYEPTLeqIRMMLRNAKkenPIGANAVQFTGGEPTLRDDLIEIIKIAKEEGydh 221
Cdd:TIGR04251  10 LTEGCNLKCRHCWIdpkYQGEGEqhPSLDPSL--FRSIIRQAI---PLGLTSVKLTGGEPLLHPAIGEILECIGENN--- 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 499322109  222 VQLNTDGIRLAFEPELVKKIREAGVNTLYLSYDGMTPQT-NW 262
Cdd:TIGR04251  82 LQLSVETNGLLCTPQTARDLASCETPFVSVSLDGVDAAThDW 123
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
151-228 7.31e-08

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: 53.22  E-value: 7.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 151 CNLSCWYC----FFYAREGEPVyepTLEQIrmmLRNAKKenpIGANAVQFTGGEPTLRDDLIEIIKIAKEEGYdHVQLNT 226
Cdd:COG0602   30 CNLRCSWCdtkyAWDGEGGKRM---SAEEI---LEEVAA---LGARHVVITGGEPLLQDDLAELLEALKDAGY-EVALET 99

                 ..
gi 499322109 227 DG 228
Cdd:COG0602  100 NG 101
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
145-252 1.61e-07

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: 52.40  E-value: 1.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109   145 IVLTNRCNLSCWYCFFYAREGEPVYEP---TLEQIRMMLRNAKKENPIGANAvqFTGGEPTL--RDDLIEIIK-IAKEEG 218
Cdd:smart00729   5 YIITRGCPRRCTFCSFPSLRGKLRSRYleaLVREIELLAEKGEKEGLVGTVF--IGGGTPTLlsPEQLEELLEaIREILG 82
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 499322109   219 YDHVQLNTDGIRL-AFEPELVKKIREAGVNTLYLS 252
Cdd:smart00729  83 LAKDVEITIETRPdTLTEELLEALKEAGVNRVSLG 117
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
151-319 2.94e-07

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 51.72  E-value: 2.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 151 CNLSCWYC----FFYAREGEPVYEPTLEQI-RMMLRNAKKENPIGanAVQFTGGEPTL-RDDLIEIIKIAKEEGYdHVQL 224
Cdd:COG1180   31 CNLRCPYChnpeISQGRPDAAGRELSPEELvEEALKDRGFLDSCG--GVTFSGGEPTLqPEFLLDLAKLAKELGL-HTAL 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 225 NTDGIrlaFEPELVKKIREA--GVNtlylsYD--GMTPQTnwknHWEI-----PLIFENVRKAGGPGI------VLVPTL 289
Cdd:COG1180  108 DTNGY---IPEEALEELLPYldAVN-----IDlkAFDDEF----YRKLtgvslEPVLENLELLAESGVhveirtLVIPGL 175
                        170       180       190
                 ....*....|....*....|....*....|
gi 499322109 290 irNVNDHEAGAIINFgLNHLDIVRGVNFQP 319
Cdd:COG1180  176 --NDSEEELEAIARF-IAELGDVIPVHLLP 202
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
149-297 1.47e-06

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: 49.80  E-value: 1.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 149 NRCNLSCWYC-----FFYAREGEPVYEPtlEQIRMMLRNAKKENPIGA---NAVQFTG-GEPTLRDDLIEIIKIAKEEGY 219
Cdd:COG0731   32 KTCNFDCVYCqrgrtTDLTRERREFDDP--EEILEELIEFLRKLPEEArepDHITFSGsGEPTLYPNLGELIEEIKKLRG 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 220 DHVQLNTDGIRLaFEPELVKKIREAGVntLYLSYDGMTPQTnWK--NHWEIPLIFENV-------RKAGGPGIVLVPTLI 290
Cdd:COG0731  110 IKTALLTNGSLL-HRPEVREELLKADQ--VYPSLDAADEET-FRkiNRPHPGLSWERIieglelfRKLYKGRTVIETMLV 185

                 ....*..
gi 499322109 291 RNVNDHE 297
Cdd:COG0731  186 KGINDSE 192
COG2100 COG2100
Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function ...
140-306 1.68e-06

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


Pssm-ID: 441703 [Multi-domain]  Cd Length: 344  Bit Score: 50.29  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 140 TNLLNIVLTNRCNLSCWYCFFYA------REGEPVYEPtlEQIRMMLRNAKKENPIGANAVQFTGGEPTLRDDLIEIIKI 213
Cdd:COG2100   35 TNVLQVRPTTGCNLNCIFCSVDAgphsrtRQAEYIVDP--EYLVEWFEKVARFKGKGVEAHIDGVGEPLLYPYIVELVKG 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 214 AKE-EGYDHVQLNTDGIRLAFEpeLVKKIREAGVNTLYLSYDGMTPQ-------TNWKNHWEIPLIFENVRKAGGPGIVL 285
Cdd:COG2100  113 LKEiKGVKVVSMQTNGTLLSEK--LIDELEEAGLDRINLSIDTLDPEkakklagTKWYDVEKVLELAEYIARETKIDLLI 190
                        170       180
                 ....*....|....*....|.
gi 499322109 286 VPTLIRNVNDHEAGAIINFGL 306
Cdd:COG2100  191 APVWLPGINDEDIPKIIEWAL 211
SCM_rSAM_ScmE TIGR04250
SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in ...
143-212 7.80e-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: 48.31  E-value: 7.80e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499322109  143 LNIVLTNRCNLSCWYCFFYAREGEPVYE-PTLEQIRMMlrnaKKENPIGANAVQFTGGEPTLRDDLIEIIK 212
Cdd:TIGR04250   5 VDIDITGRCNLRCRYCSHFSSAAETPTDlETAEWLRFF----RELNRCSVLRVVLSGGEPFMRSDFREIID 71
ThiH COG1060
2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme ...
144-249 1.93e-05

2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme transport and metabolism]; 2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440680 [Multi-domain]  Cd Length: 351  Bit Score: 47.05  E-value: 1.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 144 NIVLTNRCNLSCWYCFFYAREGEPV-YEPTLEQIRMMLRNAKKEnpiGANAVQFTGGE-PTLR-DDLIEIIKIAKEEgYD 220
Cdd:COG1060   54 PINLTNVCVNGCKFCAFSRDNGDIDrYTLSPEEILEEAEEAKAL---GATEILLVGGEhPDLPlEYYLDLLRAIKER-FP 129
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 499322109 221 HVQ---LNTDGIRLAFE------PELVKKIREAGVNTL 249
Cdd:COG1060  130 NIHihaLSPEEIAHLARasglsvEEVLERLKEAGLDSL 167
NrdG2 TIGR02495
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
145-256 2.77e-05

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: 45.05  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109  145 IVLTNRCNLSCWYCF---FYAREGEPVYEptLEQIRMMLRNAKKEnpigANAVQFTGGEPTLRDDLIEIIKIAKEEGYDh 221
Cdd:TIGR02495  20 TIFLQGCNLKCPYCHnplLIPRRGSGEIE--VEELLEFLRRRRGL----LDGVVITGGEPTLQAGLPDFLREVRELGFE- 92
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 499322109  222 VQLNTDGIRlafePELVKKIREAGvntlYLSYDGM 256
Cdd:TIGR02495  93 VKLDTNGSN----PRRLEELLEEG----LVDYVAM 119
TM0948 COG5014
Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General ...
151-260 8.12e-05

Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General function prediction only];


Pssm-ID: 444038  Cd Length: 261  Bit Score: 44.59  E-value: 8.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109 151 CNLSCWYC------FFYAREGEpVYEPtlEQIRMMLRNAKKENpiGANAVQFTGGEPTL-RDDLIEIIKIAKEEGYDHVq 223
Cdd:COG5014   50 CNLRCGFCwswrfrDFPLTIGK-FYSP--EEVAERLIEIARER--GYRQVRLSGGEPTIgFEHLLKVLELFSERGLTFI- 123
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 499322109 224 LNTDGIRLAFEPELVKKIREAGVNTLYLSYDGMTPQT 260
Cdd:COG5014  124 LETNGILIGYDRELARELASFRNIVVRVSIKGCTPEE 160
geopep_mat_rSAM TIGR04280
putative geopeptide radical SAM maturase; This family is the radical SAM/SPASM domain putative ...
135-211 3.28e-03

putative geopeptide radical SAM maturase; This family is the radical SAM/SPASM domain putative peptide maturase for geopeptide, described by model TIGR04229. The SPASM domain (see model TIGR04085) frequently marks peptide-modifying radical SAM enzymes.


Pssm-ID: 275100 [Multi-domain]  Cd Length: 428  Bit Score: 40.08  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109  135 RHRSHTNLLnIVLTNRCNLSCWYCF---FyaREGEPVYEPTLEQ-IRMMLRN--AKKENPiganAVQFTGGEPTLRDDLI 208
Cdd:TIGR04280  79 RERRHFAAI-VVLNLDCNLACPYCFegpF--RGKRYMDDATADLlVSYLVRErlAQGRDV----SLDFYGGEPLLSLDLI 151

                  ...
gi 499322109  209 EII 211
Cdd:TIGR04280 152 RRI 154
sulfatase_rSAM TIGR03942
anaerobic sulfatase-maturating enzyme; Members of this protein family are radical SAM family ...
150-204 5.06e-03

anaerobic sulfatase-maturating enzyme; Members of this protein family are radical SAM family enzymes, maturases that prepare the oxygen-sensitive radical required in the active site of anaerobic sulfatases. This maturase role has led to many misleading legacy annotations suggesting that this enzyme maturase is instead a sulfatase regulatory protein. All members of the seed alignment are radical SAM enzymes encoded next to or near an anaerobic sulfatase. Note that a single genome may encode more than one sulfatase/maturase pair. [Protein fate, Protein modification and repair]


Pssm-ID: 188457 [Multi-domain]  Cd Length: 363  Bit Score: 39.52  E-value: 5.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109  150 RCNLSCWYCFFY---AREGEPVYEPTLEQIRMMLRNAKKENPigANAVQFT--GGEPTLR 204
Cdd:TIGR03942  10 KCNLDCDYCFYLekeDLYPKPKPKMSDETLETFIKQYIASQD--GPEVNFAwqGGEPTLA 67
F420_cofH TIGR03551
7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofH subunit; This enzyme, together with ...
144-249 5.27e-03

7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofH subunit; This enzyme, together with CofG, complete the biosynthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, the chromophore of coenzyme F420. The chromophore is also used in cyanobacteria DNA photolyases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 132590 [Multi-domain]  Cd Length: 343  Bit Score: 39.18  E-value: 5.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499322109  144 NIVLTNRCNLSCWYCFFYAREGEP-VYEPTLEQIRMMLRNAKKenpIGANAVQFTGG-EPTLRDDL-IEIIKIAKEEGYD 220
Cdd:TIGR03551  42 NINFTNVCYGGCGFCAFRKRKGDAdAYLLSLEEIAERAAEAWK---AGATEVCIQGGiHPDLDGDFyLDILRAVKEEVPG 118
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 499322109  221 -HVQlntdgirlAFEP---------------ELVKKIREAGVNTL 249
Cdd:TIGR03551 119 mHIH--------AFSPmevyygarnsglsveEALKRLKEAGLDSM 155
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
151-218 9.71e-03

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: 36.77  E-value: 9.71e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499322109  151 CNLSCWYCFFYA----REGEPVYEPTLEQIrmmLRNAKKENPIGanaVQFTGGEPTL-RDDLIEIIKIAKEEG 218
Cdd:pfam13353  15 CNHHCKGCFNPEtwdfKYGKPFTEELEDEI---IEDLAKPYIQG---LTLSGGEPLLnAEALLELVKRVREEC 81
 
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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