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Conserved domains on  [gi|1937240315|ref|WP_195909930|]
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bifunctional tRNA (adenosine(37)-C2)-methyltransferase TrmG/ribosomal RNA large subunit methyltransferase RlmN [secondary endosymbiont of Ctenarytaina eucalypti]

Protein Classification

radical SAM family protein( domain architecture ID 139618)

radical SAM family protein may generate 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

Gene Ontology:  GO:0003824|GO:0051539|GO:1904047
SCOP:  3000308

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
Radical_SAM super family cl18962
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
5-366 0e+00

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.


The actual alignment was detected with superfamily member PRK11194:

Pssm-ID: 450244  Cd Length: 372  Bit Score: 734.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315   5 QKKLNLLDMNRQKMRDFFLSLGEPLFRADQVMRWIYHYYCDDFDKMTNIKKYLRTKLKVLAEIRAPAIVHEQRSSDGTIK 84
Cdd:PRK11194    3 EKKINLLDLNRQQMREFFAELGEKPFRADQVMKWIYHYGCDDFDEMTNINKVLREKLKEVAEIRAPEVAEEQRSSDGTIK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315  85 WAIRVGEQKVEMVYIPEENRGTLCLSSQVGCSLQCTFCSTAQRGFNRNLQVSEIIGQVWRAANIIGKSKVTGRCSITNIV 164
Cdd:PRK11194   83 WAIAVGDQRVETVYIPEDDRATLCVSSQVGCALECKFCSTAQQGFNRNLRVSEIIGQVWRAAKIIGAAKVTGQRPITNVV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 165 MMGMGEPLLNLSNVVPAMEIMLDDCGFGLSKRHVTLSTAGVVPALDKLGDMIDVGLAISLHAPNDTIRDKLVPINRKYNI 244
Cdd:PRK11194  163 MMGMGEPLLNLNNVVPAMEIMLDDFGFGLSKRRVTLSTSGVVPALDKLGDMIDVALAISLHAPNDELRDEIVPINKKYNI 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 245 DTLLSAVRRYLHKTRANHGRVTVEYVMLHYINDDTEHAHQLAACLKETPCKINLIPWNPFPDAPYKRSSNSRVNRFAQVM 324
Cdd:PRK11194  243 ETFLAAVRRYLEKSNANQGRVTVEYVMLDHVNDGTEHAHQLAELLKDTPCKINLIPWNPFPGAPYGRSSNSRIDRFSKVL 322
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1937240315 325 IGYGFTTIVRKIRGDDINAACGQLTGEVIDRTKRTTRNCIQG 366
Cdd:PRK11194  323 MEYGFTVIVRKTRGDDIDAACGQLAGDVIDRTKRTLKKRMQG 364
 
Name Accession Description Interval E-value
PRK11194 PRK11194
ribosomal RNA large subunit methyltransferase N; Provisional
5-366 0e+00

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 183031  Cd Length: 372  Bit Score: 734.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315   5 QKKLNLLDMNRQKMRDFFLSLGEPLFRADQVMRWIYHYYCDDFDKMTNIKKYLRTKLKVLAEIRAPAIVHEQRSSDGTIK 84
Cdd:PRK11194    3 EKKINLLDLNRQQMREFFAELGEKPFRADQVMKWIYHYGCDDFDEMTNINKVLREKLKEVAEIRAPEVAEEQRSSDGTIK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315  85 WAIRVGEQKVEMVYIPEENRGTLCLSSQVGCSLQCTFCSTAQRGFNRNLQVSEIIGQVWRAANIIGKSKVTGRCSITNIV 164
Cdd:PRK11194   83 WAIAVGDQRVETVYIPEDDRATLCVSSQVGCALECKFCSTAQQGFNRNLRVSEIIGQVWRAAKIIGAAKVTGQRPITNVV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 165 MMGMGEPLLNLSNVVPAMEIMLDDCGFGLSKRHVTLSTAGVVPALDKLGDMIDVGLAISLHAPNDTIRDKLVPINRKYNI 244
Cdd:PRK11194  163 MMGMGEPLLNLNNVVPAMEIMLDDFGFGLSKRRVTLSTSGVVPALDKLGDMIDVALAISLHAPNDELRDEIVPINKKYNI 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 245 DTLLSAVRRYLHKTRANHGRVTVEYVMLHYINDDTEHAHQLAACLKETPCKINLIPWNPFPDAPYKRSSNSRVNRFAQVM 324
Cdd:PRK11194  243 ETFLAAVRRYLEKSNANQGRVTVEYVMLDHVNDGTEHAHQLAELLKDTPCKINLIPWNPFPGAPYGRSSNSRIDRFSKVL 322
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1937240315 325 IGYGFTTIVRKIRGDDINAACGQLTGEVIDRTKRTTRNCIQG 366
Cdd:PRK11194  323 MEYGFTVIVRKTRGDDIDAACGQLAGDVIDRTKRTLKKRMQG 364
RlmN COG0820
Adenine C2-methylase RlmN of 23S rRNA A2503 and tRNA A37 [Translation, ribosomal structure and ...
10-352 0e+00

Adenine C2-methylase RlmN of 23S rRNA A2503 and tRNA A37 [Translation, ribosomal structure and biogenesis]; Adenine C2-methylase RlmN of 23S rRNA A2503 and tRNA A37 is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440582  Cd Length: 338  Bit Score: 551.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315  10 LLDMNRQKMRDFFLSLGEPLFRADQVMRWIYHYYCDDFDKMTNIKKYLRTKLKVLAEIRAPAIVHEQRSSDGTIKWAIRV 89
Cdd:COG0820     1 LLGLTLEELEEFLAELGEKPFRAKQIFRWLYQKGVTDFDEMTNLPKALREKLAENFEIGLLEVVREQVSADGTRKYLFRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315  90 GE-QKVEMVYIPEENRGTLCLSSQVGCSLQCTFCSTAQRGFNRNLQVSEIIGQVWRAANIIGKskvTGRcSITNIVMMGM 168
Cdd:COG0820    81 ADgNLVETVLIPYEDRGTLCVSSQVGCAMGCSFCATGKQGLVRNLTAGEIVGQVLLARRDLRE---GGR-RVTNIVFMGM 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 169 GEPLLNLSNVVPAMEIMLDDCGFGLSKRHVTLSTAGVVPALDKLGDM-IDVGLAISLHAPNDTIRDKLVPINRKYNIDTL 247
Cdd:COG0820   157 GEPLLNYDNVLKAIRILNDPEGLGISARRITVSTSGLVPGIRRLADEgLPVNLAVSLHAPNDELRDELMPINKKYPLEEL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 248 LSAVRRYLHKTRanhGRVTVEYVMLHYINDDTEHAHQLAACLKETPCKINLIPWNPFPDAPYKRSSNSRVNRFAQVMIGY 327
Cdd:COG0820   237 LEACRRYPEKTG---RRITFEYVLLKGVNDSPEDARELARLLKGLPCKVNLIPFNPVPGSPYKRPSPERIEAFADILEKA 313
                         330       340
                  ....*....|....*....|....*
gi 1937240315 328 GFTTIVRKIRGDDINAACGQLTGEV 352
Cdd:COG0820   314 GIPVTVRRSRGDDIDAACGQLRAKV 338
rRNA_mod_RlmN TIGR00048
23S rRNA (adenine(2503)-C(2))-methyltransferase; Members of this family are RlmN, a 23S rRNA ...
7-359 0e+00

23S rRNA (adenine(2503)-C(2))-methyltransferase; Members of this family are RlmN, a 23S rRNA m2A2503 methyltransferase in the radical SAM enzyme family. Closely related is Cfr, a Staphylococcus sciuri plasmid-borne homolog to this family, Cfr, has been identified as essential to transferrable resistance to chloramphenicol and florfenicol. Cfr methylates 23S RNA at a different site. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 272874  Cd Length: 355  Bit Score: 535.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315   7 KLNLLDMNRQKMRDFFLSLGEPLFRADQVMRWIYHYYCDDFDKMTNIKKYLRTKLKVLAEIRAPAIVHEQRSSDGTIKWA 86
Cdd:TIGR00048   6 KPSLLDLTLQELRQWLKDLGEKPFRAKQIMKWLYHKGCDSFDDMTNLSKVLREKLNEVFEIRTPEIAHEQRSSDGTIKYL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315  87 IRVGE-QKVEMVYIPEENRGTLCLSSQVGCSLQCTFCSTAQRGFNRNLQVSEIIGQVWRAANIIGkskVTGRcSITNIVM 165
Cdd:TIGR00048  86 FALGDgQTIETVLIPEDDRATVCVSSQVGCALGCTFCATAKGGFNRNLEASEIIGQVLRVQKIVG---ETGE-RVSNVVF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 166 MGMGEPLLNLSNVVPAMEIMLDDCGFGLSKRHVTLSTAGVVPALDKLGD-MIDVGLAISLHAPNDTIRDKLVPINRKYNI 244
Cdd:TIGR00048 162 MGMGEPLLNLNEVVKAMEIMNDDFGFGISKRRITISTSGVVPKIDKLADkMLQVALAISLHAPNDEIRSSLMPINKKYNI 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 245 DTLLSAVRRYLHKTRAnhgRVTVEYVMLHYINDDTEHAHQLAACLKETPCKINLIPWNPFPDAPYKRSSNSRVNRFAQVM 324
Cdd:TIGR00048 242 ETLLAAVRRYLEKTGR---RVTFEYVLLDGVNDQVEHAEELAELLKGTKCKVNLIPWNPFPEADYGRPSNSQIDRFAKVL 318
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1937240315 325 IGYGFTTIVRKIRGDDINAACGQL-TGEVIDRTKRT 359
Cdd:TIGR00048 319 MSYGFTVTIRKSRGDDIDAACGQLrAKDVIDRTKRT 354
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
112-278 7.02e-15

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: 71.79  E-value: 7.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 112 QVGCSLQCTFC---STAQRGFNRNLQVSEIIGQVWRAANIIgkskvtgrcsiTNIVMMGMGEPLLNLSNVVPAMEIMLDD 188
Cdd:pfam04055   2 TRGCNLRCTYCafpSIRARGKGRELSPEEILEEAKELKRLG-----------VEVVILGGGEPLLLPDLVELLERLLKLE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 189 cgfGLSKRHVTLSTAGVVP---ALDKLGDMIDVGLAISLHAPNDTIRDklvPINRKYNIDTLLSAVRRYLhktRANHGRV 265
Cdd:pfam04055  71 ---LAEGIRITLETNGTLLdeeLLELLKEAGLDRVSIGLESGDDEVLK---LINRGHTFEEVLEALELLR---EAGIPVV 141
                         170
                  ....*....|...
gi 1937240315 266 TVEYVMLHYINDD 278
Cdd:pfam04055 142 TDNIVGLPGETDE 154
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
114-314 1.96e-07

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: 51.18  E-value: 1.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 114 GCSLQCTFCS---TAQRGFNRNLQVSEIIGQVWRAANIIGKskvtgrcsitnIVMMGMGEPLLNLsNVVPAMEIMLDDCG 190
Cdd:cd01335     6 GCNLNCGFCSnpaSKGRGPESPPEIEEILDIVLEAKERGVE-----------VVILTGGEPLLYP-ELAELLRRLKKELP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 191 fglsKRHVTLSTAGVVP---ALDKLGDMIDVGLAISLHAPNDTIRDKLvpINRKYNIDTLLSAVRRYLHKTRanhgRVTV 267
Cdd:cd01335    74 ----GFEISIETNGTLLteeLLKELKELGLDGVGVSLDSGDEEVADKI--RGSGESFKERLEALKELREAGL----GLST 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1937240315 268 EYVMLHYIN---DDTEHAHQLAAclKETPCKINLIPWNPFPDAPYKRSSN 314
Cdd:cd01335   144 TLLVGLGDEdeeDDLEELELLAE--FRSPDRVSLFRLLPEEGTPLELAAP 191
 
Name Accession Description Interval E-value
PRK11194 PRK11194
ribosomal RNA large subunit methyltransferase N; Provisional
5-366 0e+00

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 183031  Cd Length: 372  Bit Score: 734.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315   5 QKKLNLLDMNRQKMRDFFLSLGEPLFRADQVMRWIYHYYCDDFDKMTNIKKYLRTKLKVLAEIRAPAIVHEQRSSDGTIK 84
Cdd:PRK11194    3 EKKINLLDLNRQQMREFFAELGEKPFRADQVMKWIYHYGCDDFDEMTNINKVLREKLKEVAEIRAPEVAEEQRSSDGTIK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315  85 WAIRVGEQKVEMVYIPEENRGTLCLSSQVGCSLQCTFCSTAQRGFNRNLQVSEIIGQVWRAANIIGKSKVTGRCSITNIV 164
Cdd:PRK11194   83 WAIAVGDQRVETVYIPEDDRATLCVSSQVGCALECKFCSTAQQGFNRNLRVSEIIGQVWRAAKIIGAAKVTGQRPITNVV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 165 MMGMGEPLLNLSNVVPAMEIMLDDCGFGLSKRHVTLSTAGVVPALDKLGDMIDVGLAISLHAPNDTIRDKLVPINRKYNI 244
Cdd:PRK11194  163 MMGMGEPLLNLNNVVPAMEIMLDDFGFGLSKRRVTLSTSGVVPALDKLGDMIDVALAISLHAPNDELRDEIVPINKKYNI 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 245 DTLLSAVRRYLHKTRANHGRVTVEYVMLHYINDDTEHAHQLAACLKETPCKINLIPWNPFPDAPYKRSSNSRVNRFAQVM 324
Cdd:PRK11194  243 ETFLAAVRRYLEKSNANQGRVTVEYVMLDHVNDGTEHAHQLAELLKDTPCKINLIPWNPFPGAPYGRSSNSRIDRFSKVL 322
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1937240315 325 IGYGFTTIVRKIRGDDINAACGQLTGEVIDRTKRTTRNCIQG 366
Cdd:PRK11194  323 MEYGFTVIVRKTRGDDIDAACGQLAGDVIDRTKRTLKKRMQG 364
RlmN COG0820
Adenine C2-methylase RlmN of 23S rRNA A2503 and tRNA A37 [Translation, ribosomal structure and ...
10-352 0e+00

Adenine C2-methylase RlmN of 23S rRNA A2503 and tRNA A37 [Translation, ribosomal structure and biogenesis]; Adenine C2-methylase RlmN of 23S rRNA A2503 and tRNA A37 is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440582  Cd Length: 338  Bit Score: 551.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315  10 LLDMNRQKMRDFFLSLGEPLFRADQVMRWIYHYYCDDFDKMTNIKKYLRTKLKVLAEIRAPAIVHEQRSSDGTIKWAIRV 89
Cdd:COG0820     1 LLGLTLEELEEFLAELGEKPFRAKQIFRWLYQKGVTDFDEMTNLPKALREKLAENFEIGLLEVVREQVSADGTRKYLFRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315  90 GE-QKVEMVYIPEENRGTLCLSSQVGCSLQCTFCSTAQRGFNRNLQVSEIIGQVWRAANIIGKskvTGRcSITNIVMMGM 168
Cdd:COG0820    81 ADgNLVETVLIPYEDRGTLCVSSQVGCAMGCSFCATGKQGLVRNLTAGEIVGQVLLARRDLRE---GGR-RVTNIVFMGM 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 169 GEPLLNLSNVVPAMEIMLDDCGFGLSKRHVTLSTAGVVPALDKLGDM-IDVGLAISLHAPNDTIRDKLVPINRKYNIDTL 247
Cdd:COG0820   157 GEPLLNYDNVLKAIRILNDPEGLGISARRITVSTSGLVPGIRRLADEgLPVNLAVSLHAPNDELRDELMPINKKYPLEEL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 248 LSAVRRYLHKTRanhGRVTVEYVMLHYINDDTEHAHQLAACLKETPCKINLIPWNPFPDAPYKRSSNSRVNRFAQVMIGY 327
Cdd:COG0820   237 LEACRRYPEKTG---RRITFEYVLLKGVNDSPEDARELARLLKGLPCKVNLIPFNPVPGSPYKRPSPERIEAFADILEKA 313
                         330       340
                  ....*....|....*....|....*
gi 1937240315 328 GFTTIVRKIRGDDINAACGQLTGEV 352
Cdd:COG0820   314 GIPVTVRRSRGDDIDAACGQLRAKV 338
rRNA_mod_RlmN TIGR00048
23S rRNA (adenine(2503)-C(2))-methyltransferase; Members of this family are RlmN, a 23S rRNA ...
7-359 0e+00

23S rRNA (adenine(2503)-C(2))-methyltransferase; Members of this family are RlmN, a 23S rRNA m2A2503 methyltransferase in the radical SAM enzyme family. Closely related is Cfr, a Staphylococcus sciuri plasmid-borne homolog to this family, Cfr, has been identified as essential to transferrable resistance to chloramphenicol and florfenicol. Cfr methylates 23S RNA at a different site. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 272874  Cd Length: 355  Bit Score: 535.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315   7 KLNLLDMNRQKMRDFFLSLGEPLFRADQVMRWIYHYYCDDFDKMTNIKKYLRTKLKVLAEIRAPAIVHEQRSSDGTIKWA 86
Cdd:TIGR00048   6 KPSLLDLTLQELRQWLKDLGEKPFRAKQIMKWLYHKGCDSFDDMTNLSKVLREKLNEVFEIRTPEIAHEQRSSDGTIKYL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315  87 IRVGE-QKVEMVYIPEENRGTLCLSSQVGCSLQCTFCSTAQRGFNRNLQVSEIIGQVWRAANIIGkskVTGRcSITNIVM 165
Cdd:TIGR00048  86 FALGDgQTIETVLIPEDDRATVCVSSQVGCALGCTFCATAKGGFNRNLEASEIIGQVLRVQKIVG---ETGE-RVSNVVF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 166 MGMGEPLLNLSNVVPAMEIMLDDCGFGLSKRHVTLSTAGVVPALDKLGD-MIDVGLAISLHAPNDTIRDKLVPINRKYNI 244
Cdd:TIGR00048 162 MGMGEPLLNLNEVVKAMEIMNDDFGFGISKRRITISTSGVVPKIDKLADkMLQVALAISLHAPNDEIRSSLMPINKKYNI 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 245 DTLLSAVRRYLHKTRAnhgRVTVEYVMLHYINDDTEHAHQLAACLKETPCKINLIPWNPFPDAPYKRSSNSRVNRFAQVM 324
Cdd:TIGR00048 242 ETLLAAVRRYLEKTGR---RVTFEYVLLDGVNDQVEHAEELAELLKGTKCKVNLIPWNPFPEADYGRPSNSQIDRFAKVL 318
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1937240315 325 IGYGFTTIVRKIRGDDINAACGQL-TGEVIDRTKRT 359
Cdd:TIGR00048 319 MSYGFTVTIRKSRGDDIDAACGQLrAKDVIDRTKRT 354
PRK14461 PRK14461
ribosomal RNA large subunit methyltransferase N; Provisional
9-352 1.76e-86

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 237718  Cd Length: 371  Bit Score: 266.75  E-value: 1.76e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315   9 NLLDMNRQKMRDFFLSLGEPLFRADQVMRWIYHYYCDDFDKMTNIKKYLRTKLKVLAEIRAPAIVHEQRSSDG-TIKWAI 87
Cdd:PRK14461    9 NLYDLNLAELTELLTAWGQPAFRARQLYRHLYVNLADSVLAMTDLPLALRERLTAELPLSTLRLEQVQIGDNGlTRKALF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315  88 RV-GEQKVEMVYIPEENRGTLCLSSQVGCSLQCTFCSTAQRGFNRNLQVSEIIGQV-W------RAANIIGKSKVTGRCS 159
Cdd:PRK14461   89 RLpDGAVVETVLMIYPDRATVCVSTQAGCGMGCVFCATGTLGLLRNLSSGEIVAQViWasrelrAMGAAISKRHAGPVGR 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 160 ITNIVMMGMGEPLLNLSNVVPAMEIMLDDCGFGLSKRHVTLSTAGVVPALDKLGD-MIDVGLAISLHAPNDTIRDKLVPI 238
Cdd:PRK14461  169 VTNLVFMGMGEPFANYDRWWQAVERLHDPQGFNLGARSMTVSTVGLVKGIRRLANeRLPINLAISLHAPDDALRSELMPV 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 239 NRKYNIDTLLSAVRRYLHKTranHGRVTVEYVMLHYINDDTEHAHQLAACLK-ETP-----CKINLIPWNPFPDAPYKRS 312
Cdd:PRK14461  249 NRRYPIADLMAATRDYIAKT---RRRVSFEYVLLQGKNDHPEQAAALARLLRgEAPpgpllVHVNLIPWNPVPGTPLGRS 325
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1937240315 313 SNSRVNRFAQVMIGYGFTTIVRKIRGDDINAACGQLTGEV 352
Cdd:PRK14461  326 ERERVTTFQRILTDYGIPCTVRVERGVEIAAACGQLAGRH 365
PRK14453 PRK14453
chloramphenicol/florfenicol resistance protein; Provisional
17-351 8.09e-63

chloramphenicol/florfenicol resistance protein; Provisional


Pssm-ID: 184685  Cd Length: 347  Bit Score: 204.98  E-value: 8.09e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315  17 KMRDFFLSLGEPLFRADQVMRWIYHYYCDDFDKMTNIKKYLRtklKVLAEIRAPAI-----VHEQRSSDGT-IKWAIRVG 90
Cdd:PRK14453    9 KMKQILSNLKLPDYRYEQITKAIFKQRIDNFEDMHILPKALR---ESLINEFGKNVlsvipVFEQDSKQVTkVLFELTDG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315  91 EQ--KVEMVYipEENRGTLCLSSQVGCSLQCTFCSTAQRGFNRNLQVSEIIGQVWRAaniigksKVTGRcSITNIVMMGM 168
Cdd:PRK14453   86 ERieAVGLKY--KQGWESFCISSQCGCGFGCRFCATGSIGLKRNLTADEITDQLLYF-------YLNGH-RLDSISFMGM 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 169 GEPLLNlSNVVPAMEIMLDDCGFGLSKRHVTLSTAGVVPALDKL-GDMIDVGLAISLHAPNDTIRDKLVPINRKYNIDTL 247
Cdd:PRK14453  156 GEALAN-PELFDALKILTDPNLFGLSQRRITISTIGIIPGIQRLtQEFPQVNLTFSLHSPFESQRSELMPINKRFPLNEV 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 248 LSAVRRYLHKTRAnhgRVTVEYVMLHYINDDTEHAHQLAACLKETPC-----KINLIPWNPFPDAP--YKRSSNSRVNRF 320
Cdd:PRK14453  235 MKTLDEHIRHTGR---KVYIAYIMLEGVNDSKEHAEAVVGLLRNRGSwehlyHVNLIPYNSTDKTPfkFQSSSAGQIKQF 311
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1937240315 321 AQVMIGYGFTTIVRKIRGDDINAACGQLTGE 351
Cdd:PRK14453  312 CSTLKSAGISVTVRTQFGSDISAACGQLYGN 342
PRK14470 PRK14470
ribosomal RNA large subunit methyltransferase N; Provisional
52-348 5.23e-47

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 172945  Cd Length: 336  Bit Score: 163.18  E-value: 5.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315  52 NIKKYLRTKLKVLAEIRAPAIVHEQRSSDGTIKWAIRVGE-QKVEMVYIP-EENRGTLCLSSQVGCSLQCTFCSTAQRGF 129
Cdd:PRK14470   42 NVRRSVLDEVDALATPGELRLVERVDAKDGFRKYLFELPDgLRVEAVRIPlFDTHHVVCLSSQAGCALGCAFCATGKLGL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 130 NRNLQVSEIIGQVWRAaniigksKVTGRCSITNIVMMGMGEPLLNLSNVVPAMEIMLDDCGFGLSKRHVTLSTAGVVPAL 209
Cdd:PRK14470  122 DRSLRSWEIVAQLLAV-------RADSERPITGVVFMGQGEPFLNYDEVLRAAYALCDPAGARIDGRRISISTAGVVPMI 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 210 DK-LGDMIDVGLAISLHAPNDTIRDKLVPINRKYNIDTLLSAVRRYlhktRANHGRVTVEYVMLHYINDDTEHAHQLAAC 288
Cdd:PRK14470  195 RRyTAEGHKFRLCISLNAAIPWKRRALMPIEQGFPLDELVEAIREH----AALRGRVTLEYVMISGVNVGEEDAAALGRL 270
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937240315 289 LKETPCKINLIPWNPfPDAPYKRSSNSRVNRF----AQVMIGygfTTIVRKIR-GDDINAACGQL 348
Cdd:PRK14470  271 LAGIPVRLNPIAVND-ATGRYRPPDEDEWNAFrdalARELPG---TPVVRRYSgGQDEHAACGML 331
PRK14464 PRK14464
RNA methyltransferase;
57-361 5.62e-39

RNA methyltransferase;


Pssm-ID: 184691  Cd Length: 344  Bit Score: 142.17  E-value: 5.62e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315  57 LRTKLKVL-AEIRAPAIVH-EQRSSDGTIKWAIRVGE-QKVEMVYIPeenRGTLCLSSQVGCSLQCTFCSTAQRGFNRNL 133
Cdd:PRK14464   48 LREALPALeAELDGLARLRsEHPGEDGSARLLVELADgQMVESVLLP---RDGLCVSTQVGCAVGCVFCMTGRSGLLRQL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 134 QVSEIIGQVWRAaniigkskvTGRCSITNIVMMGMGEPLLNLSNVVPAMEIMLDDCGFGlsKRHVTLSTAGVVPALDKLG 213
Cdd:PRK14464  125 GSAEIVAQVVLA---------RRRRAVKKVVFMGMGEPAHNLDNVLEAIDLLGTEGGIG--HKNLVFSTVGDPRVFERLP 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 214 DM-IDVGLAISLHAPNDTIRDKLVPINRKYNIDTLLSAVRRYlhkTRANHGRVTVEYVMLHYINDDTEHAHQLAACLKET 292
Cdd:PRK14464  194 QQrVKPALALSLHTTRAELRARLLPRAPRIAPEELVELGEAY---ARATGYPIQYQWTLLEGVNDSDEEMDGIVRLLKGK 270
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937240315 293 PCKINLIPWNPFPDAPYKRSSNSRVNRFAQVMIGYGFTTIVRKIRGDDINAACGQLTGEVIDRTKRTTR 361
Cdd:PRK14464  271 YAVMNLIPYNSVDGDAYRRPSGERIVAMARYLHRRGVLTKVRNSAGQDVDGGCGQLRARAAKAAAVRRI 339
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
112-278 7.02e-15

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: 71.79  E-value: 7.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 112 QVGCSLQCTFC---STAQRGFNRNLQVSEIIGQVWRAANIIgkskvtgrcsiTNIVMMGMGEPLLNLSNVVPAMEIMLDD 188
Cdd:pfam04055   2 TRGCNLRCTYCafpSIRARGKGRELSPEEILEEAKELKRLG-----------VEVVILGGGEPLLLPDLVELLERLLKLE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 189 cgfGLSKRHVTLSTAGVVP---ALDKLGDMIDVGLAISLHAPNDTIRDklvPINRKYNIDTLLSAVRRYLhktRANHGRV 265
Cdd:pfam04055  71 ---LAEGIRITLETNGTLLdeeLLELLKEAGLDRVSIGLESGDDEVLK---LINRGHTFEEVLEALELLR---EAGIPVV 141
                         170
                  ....*....|...
gi 1937240315 266 TVEYVMLHYINDD 278
Cdd:pfam04055 142 TDNIVGLPGETDE 154
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
114-314 1.96e-07

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: 51.18  E-value: 1.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 114 GCSLQCTFCS---TAQRGFNRNLQVSEIIGQVWRAANIIGKskvtgrcsitnIVMMGMGEPLLNLsNVVPAMEIMLDDCG 190
Cdd:cd01335     6 GCNLNCGFCSnpaSKGRGPESPPEIEEILDIVLEAKERGVE-----------VVILTGGEPLLYP-ELAELLRRLKKELP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 191 fglsKRHVTLSTAGVVP---ALDKLGDMIDVGLAISLHAPNDTIRDKLvpINRKYNIDTLLSAVRRYLHKTRanhgRVTV 267
Cdd:cd01335    74 ----GFEISIETNGTLLteeLLKELKELGLDGVGVSLDSGDEEVADKI--RGSGESFKERLEALKELREAGL----GLST 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1937240315 268 EYVMLHYIN---DDTEHAHQLAAclKETPCKINLIPWNPFPDAPYKRSSN 314
Cdd:cd01335   144 TLLVGLGDEdeeDDLEELELLAE--FRSPDRVSLFRLLPEEGTPLELAAP 191
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
113-333 3.85e-04

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 41.71  E-value: 3.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 113 VGCSLQCTFCS---TAQRGFNRNLQ---VSEIIGQVWRAANIIGKSK---VTGrcsitnivmmgmGEPLLNlsnvvpaME 183
Cdd:COG1180    29 QGCNLRCPYCHnpeISQGRPDAAGRelsPEELVEEALKDRGFLDSCGgvtFSG------------GEPTLQ-------PE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 184 IMLDdcgfgLSKR------HVTLSTAGVVP--ALDKLGDMIDvGLAISLHAPNDTIRDKLVPINRKYNIDTLlsavrRYL 255
Cdd:COG1180    90 FLLD-----LAKLakelglHTALDTNGYIPeeALEELLPYLD-AVNIDLKAFDDEFYRKLTGVSLEPVLENL-----ELL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937240315 256 HKTRANhgrVTVEYVMLHYINDDTEHAHQLAACLKETPckiNLIPW--NPF-PDAPYKRS---SNSRVNRFAQVMIGYGF 329
Cdd:COG1180   159 AESGVH---VEIRTLVIPGLNDSEEELEAIARFIAELG---DVIPVhlLPFhPLYKLEDVpppSPETLERAREIAREYGL 232

                  ....
gi 1937240315 330 TTIV 333
Cdd:COG1180   233 KYVY 236
 
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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