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Conserved domains on  [gi|1486688785|ref|WP_120177226|]
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radical SAM protein [Sutterella megalosphaeroides]

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 ...
21-356 1.87e-119

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 PRK14464:

Pssm-ID: 450244  Cd Length: 344  Bit Score: 348.64  E-value: 1.87e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785  21 LPALREALARRGAKPEHVRRILLAWmgLAPWAADAKCR-----YPAALTRALPEVRALLESIGRV--ECSDAE-TAKLLL 92
Cdd:PRK14464    3 IQDLRQRLRALGAKPCHEGRILRAW--LQGLPLDTRRQraedfLPLALREALPALEAELDGLARLrsEHPGEDgSARLLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785  93 AMRAGDFVEAVLLPREGLCVSTQVGCAVGCRFCMTGRSGLVRQLGSLEILAQVREGLRRMPtLAKIKFMGMGEPSHNLRA 172
Cdd:PRK14464   81 ELADGQMVESVLLPRDGLCVSTQVGCAVGCVFCMTGRSGLLRQLGSAEIVAQVVLARRRRA-VKKVVFMGMGEPAHNLDN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 173 VLEVLEFLGSAEGLGfaHKALTVSTVGDERLFEALERSPVKPALALSLHTTNDTIRRELLPRAARIPVEKLLDSALRYGD 252
Cdd:PRK14464  160 VLEAIDLLGTEGGIG--HKNLVFSTVGDPRVFERLPQQRVKPALALSLHTTRAELRARLLPRAPRIAPEELVELGEAYAR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 253 LAKFPVQIEWTLLSGVNDGLDEAARLAGLLKGRRAMVNYIDLNAVEGSDFRPVPEERAQELITVLRRSGTVATLRKSAAR 332
Cdd:PRK14464  238 ATGYPIQYQWTLLEGVNDSDEEMDGIVRLLKGKYAVMNLIPYNSVDGDAYRRPSGERIVAMARYLHRRGVLTKVRNSAGQ 317
                         330       340
                  ....*....|....*....|....
gi 1486688785 333 TVEGGCGQLRAVRLAGATRSSAKA 356
Cdd:PRK14464  318 DVDGGCGQLRARAAKAAAVRRIRR 341
 
Name Accession Description Interval E-value
PRK14464 PRK14464
RNA methyltransferase;
21-356 1.87e-119

RNA methyltransferase;


Pssm-ID: 184691  Cd Length: 344  Bit Score: 348.64  E-value: 1.87e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785  21 LPALREALARRGAKPEHVRRILLAWmgLAPWAADAKCR-----YPAALTRALPEVRALLESIGRV--ECSDAE-TAKLLL 92
Cdd:PRK14464    3 IQDLRQRLRALGAKPCHEGRILRAW--LQGLPLDTRRQraedfLPLALREALPALEAELDGLARLrsEHPGEDgSARLLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785  93 AMRAGDFVEAVLLPREGLCVSTQVGCAVGCRFCMTGRSGLVRQLGSLEILAQVREGLRRMPtLAKIKFMGMGEPSHNLRA 172
Cdd:PRK14464   81 ELADGQMVESVLLPRDGLCVSTQVGCAVGCVFCMTGRSGLLRQLGSAEIVAQVVLARRRRA-VKKVVFMGMGEPAHNLDN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 173 VLEVLEFLGSAEGLGfaHKALTVSTVGDERLFEALERSPVKPALALSLHTTNDTIRRELLPRAARIPVEKLLDSALRYGD 252
Cdd:PRK14464  160 VLEAIDLLGTEGGIG--HKNLVFSTVGDPRVFERLPQQRVKPALALSLHTTRAELRARLLPRAPRIAPEELVELGEAYAR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 253 LAKFPVQIEWTLLSGVNDGLDEAARLAGLLKGRRAMVNYIDLNAVEGSDFRPVPEERAQELITVLRRSGTVATLRKSAAR 332
Cdd:PRK14464  238 ATGYPIQYQWTLLEGVNDSDEEMDGIVRLLKGKYAVMNLIPYNSVDGDAYRRPSGERIVAMARYLHRRGVLTKVRNSAGQ 317
                         330       340
                  ....*....|....*....|....
gi 1486688785 333 TVEGGCGQLRAVRLAGATRSSAKA 356
Cdd:PRK14464  318 DVDGGCGQLRARAAKAAAVRRIRR 341
RlmN COG0820
Adenine C2-methylase RlmN of 23S rRNA A2503 and tRNA A37 [Translation, ribosomal structure and ...
20-343 5.33e-110

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: 324.29  E-value: 5.33e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785  20 TLPALREALARRGAKPEHVRRILlAWM---GLAPWaaDAKCRYPAALTRALPEvRALLES--IGRVECSDAETAKLLLAM 94
Cdd:COG0820     5 TLEELEEFLAELGEKPFRAKQIF-RWLyqkGVTDF--DEMTNLPKALREKLAE-NFEIGLleVVREQVSADGTRKYLFRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785  95 RAGDFVEAVLLP---REGLCVSTQVGCAVGCRFCMTGRSGLVRQLGSLEILAQVREGLRRMPT----LAKIKFMGMGEPS 167
Cdd:COG0820    81 ADGNLVETVLIPyedRGTLCVSSQVGCAMGCSFCATGKQGLVRNLTAGEIVGQVLLARRDLREggrrVTNIVFMGMGEPL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 168 HNLRAVLEVLEFLGSAEGLGFAHKALTVSTVGDERLFEALERSPVKPALALSLHTTNDTIRRELLPRAARIPVEKLLDSA 247
Cdd:COG0820   161 LNYDNVLKAIRILNDPEGLGISARRITVSTSGLVPGIRRLADEGLPVNLAVSLHAPNDELRDELMPINKKYPLEELLEAC 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 248 LRYGDLAKFPVQIEWTLLSGVNDGLDEAARLAGLLKGRRAMVNYIDLNAVEGSDFRPVPEERAQELITVLRRSGTVATLR 327
Cdd:COG0820   241 RRYPEKTGRRITFEYVLLKGVNDSPEDARELARLLKGLPCKVNLIPFNPVPGSPYKRPSPERIEAFADILEKAGIPVTVR 320
                         330
                  ....*....|....*.
gi 1486688785 328 KSAARTVEGGCGQLRA 343
Cdd:COG0820   321 RSRGDDIDAACGQLRA 336
rRNA_mod_RlmN TIGR00048
23S rRNA (adenine(2503)-C(2))-methyltransferase; Members of this family are RlmN, a 23S rRNA ...
20-354 2.09e-63

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: 205.82  E-value: 2.09e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785  20 TLPALREALARRGAKPEHVRRILLawmglapWAADAKCRYPAALT------RALPEVRALLESIGRVECSDAE--TAKLL 91
Cdd:TIGR00048  13 TLQELRQWLKDLGEKPFRAKQIMK-------WLYHKGCDSFDDMTnlskvlREKLNEVFEIRTPEIAHEQRSSdgTIKYL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785  92 LAMRAGDFVEAVLLP---REGLCVSTQVGCAVGCRFCMTGRSGLVRQLGSLEILAQV-------REGLRRmptLAKIKFM 161
Cdd:TIGR00048  86 FALGDGQTIETVLIPeddRATVCVSSQVGCALGCTFCATAKGGFNRNLEASEIIGQVlrvqkivGETGER---VSNVVFM 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 162 GMGEPSHNLRAVLEVLEFLGSAEGLGFAHKALTVSTVGDERLFEALERSPVKPALALSLHTTNDTIRRELLPRAARIPVE 241
Cdd:TIGR00048 163 GMGEPLLNLNEVVKAMEIMNDDFGFGISKRRITISTSGVVPKIDKLADKMLQVALAISLHAPNDEIRSSLMPINKKYNIE 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 242 KLLDSALRYGDLAKFPVQIEWTLLSGVNDGLDEAARLAGLLKGRRAMVNYIDLNAVEGSDFRPVPEERAQELITVLRRSG 321
Cdd:TIGR00048 243 TLLAAVRRYLEKTGRRVTFEYVLLDGVNDQVEHAEELAELLKGTKCKVNLIPWNPFPEADYGRPSNSQIDRFAKVLMSYG 322
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1486688785 322 TVATLRKSAARTVEGGCGQLRAVRLAGATRSSA 354
Cdd:TIGR00048 323 FTVTIRKSRGDDIDAACGQLRAKDVIDRTKRTL 355
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
114-270 3.76e-11

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: 61.00  E-value: 3.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 114 TQVGCAVGCRFCMTGRSGLVRQLGSL---EILAQVREgLRRMPTlaKIKFMGMGEPSHNLRAVLEVLEFLGSAEGLGFAH 190
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKGRELspeEILEEAKE-LKRLGV--EVVILGGGEPLLLPDLVELLERLLKLELAEGIRI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 191 KALTVSTVGDERLFEALERSPVKpALALSLHTTNDTIRRellPRAARIPVEKLLDSALRYGDLAKFPVQIEWTLLSGVND 270
Cdd:pfam04055  78 TLETNGTLLDEELLELLKEAGLD-RVSIGLESGDDEVLK---LINRGHTFEEVLEALELLREAGIPVVTDNIVGLPGETD 153
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
117-319 2.34e-04

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: 41.94  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 117 GCAVGCRFCMTGRSGLVRQLGSLEILAQVREGLRRMPTLAKIKFMGMGEPSHNLRAVLEVLEFLGSAEGLGFAhkALTVS 196
Cdd:cd01335     6 GCNLNCGFCSNPASKGRGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGFEIS--IETNG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 197 TVGDERLFEALERSPVKpALALSLHTTNDTIRRELlpRAARIPVEKLLDSALRYGDlAKFPVQIEWTLLSGVNDGLDEAA 276
Cdd:cd01335    84 TLLTEELLKELKELGLD-GVGVSLDSGDEEVADKI--RGSGESFKERLEALKELRE-AGLGLSTTLLVGLGDEDEEDDLE 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1486688785 277 RLAGLLK-GRRAMVNYIDLNAVEGS-DFRPVPEERAQELITVLRR 319
Cdd:cd01335   160 ELELLAEfRSPDRVSLFRLLPEEGTpLELAAPVVPAEKLLRLIAA 204
 
Name Accession Description Interval E-value
PRK14464 PRK14464
RNA methyltransferase;
21-356 1.87e-119

RNA methyltransferase;


Pssm-ID: 184691  Cd Length: 344  Bit Score: 348.64  E-value: 1.87e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785  21 LPALREALARRGAKPEHVRRILLAWmgLAPWAADAKCR-----YPAALTRALPEVRALLESIGRV--ECSDAE-TAKLLL 92
Cdd:PRK14464    3 IQDLRQRLRALGAKPCHEGRILRAW--LQGLPLDTRRQraedfLPLALREALPALEAELDGLARLrsEHPGEDgSARLLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785  93 AMRAGDFVEAVLLPREGLCVSTQVGCAVGCRFCMTGRSGLVRQLGSLEILAQVREGLRRMPtLAKIKFMGMGEPSHNLRA 172
Cdd:PRK14464   81 ELADGQMVESVLLPRDGLCVSTQVGCAVGCVFCMTGRSGLLRQLGSAEIVAQVVLARRRRA-VKKVVFMGMGEPAHNLDN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 173 VLEVLEFLGSAEGLGfaHKALTVSTVGDERLFEALERSPVKPALALSLHTTNDTIRRELLPRAARIPVEKLLDSALRYGD 252
Cdd:PRK14464  160 VLEAIDLLGTEGGIG--HKNLVFSTVGDPRVFERLPQQRVKPALALSLHTTRAELRARLLPRAPRIAPEELVELGEAYAR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 253 LAKFPVQIEWTLLSGVNDGLDEAARLAGLLKGRRAMVNYIDLNAVEGSDFRPVPEERAQELITVLRRSGTVATLRKSAAR 332
Cdd:PRK14464  238 ATGYPIQYQWTLLEGVNDSDEEMDGIVRLLKGKYAVMNLIPYNSVDGDAYRRPSGERIVAMARYLHRRGVLTKVRNSAGQ 317
                         330       340
                  ....*....|....*....|....
gi 1486688785 333 TVEGGCGQLRAVRLAGATRSSAKA 356
Cdd:PRK14464  318 DVDGGCGQLRARAAKAAAVRRIRR 341
RlmN COG0820
Adenine C2-methylase RlmN of 23S rRNA A2503 and tRNA A37 [Translation, ribosomal structure and ...
20-343 5.33e-110

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: 324.29  E-value: 5.33e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785  20 TLPALREALARRGAKPEHVRRILlAWM---GLAPWaaDAKCRYPAALTRALPEvRALLES--IGRVECSDAETAKLLLAM 94
Cdd:COG0820     5 TLEELEEFLAELGEKPFRAKQIF-RWLyqkGVTDF--DEMTNLPKALREKLAE-NFEIGLleVVREQVSADGTRKYLFRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785  95 RAGDFVEAVLLP---REGLCVSTQVGCAVGCRFCMTGRSGLVRQLGSLEILAQVREGLRRMPT----LAKIKFMGMGEPS 167
Cdd:COG0820    81 ADGNLVETVLIPyedRGTLCVSSQVGCAMGCSFCATGKQGLVRNLTAGEIVGQVLLARRDLREggrrVTNIVFMGMGEPL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 168 HNLRAVLEVLEFLGSAEGLGFAHKALTVSTVGDERLFEALERSPVKPALALSLHTTNDTIRRELLPRAARIPVEKLLDSA 247
Cdd:COG0820   161 LNYDNVLKAIRILNDPEGLGISARRITVSTSGLVPGIRRLADEGLPVNLAVSLHAPNDELRDELMPINKKYPLEELLEAC 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 248 LRYGDLAKFPVQIEWTLLSGVNDGLDEAARLAGLLKGRRAMVNYIDLNAVEGSDFRPVPEERAQELITVLRRSGTVATLR 327
Cdd:COG0820   241 RRYPEKTGRRITFEYVLLKGVNDSPEDARELARLLKGLPCKVNLIPFNPVPGSPYKRPSPERIEAFADILEKAGIPVTVR 320
                         330
                  ....*....|....*.
gi 1486688785 328 KSAARTVEGGCGQLRA 343
Cdd:COG0820   321 RSRGDDIDAACGQLRA 336
rRNA_mod_RlmN TIGR00048
23S rRNA (adenine(2503)-C(2))-methyltransferase; Members of this family are RlmN, a 23S rRNA ...
20-354 2.09e-63

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: 205.82  E-value: 2.09e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785  20 TLPALREALARRGAKPEHVRRILLawmglapWAADAKCRYPAALT------RALPEVRALLESIGRVECSDAE--TAKLL 91
Cdd:TIGR00048  13 TLQELRQWLKDLGEKPFRAKQIMK-------WLYHKGCDSFDDMTnlskvlREKLNEVFEIRTPEIAHEQRSSdgTIKYL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785  92 LAMRAGDFVEAVLLP---REGLCVSTQVGCAVGCRFCMTGRSGLVRQLGSLEILAQV-------REGLRRmptLAKIKFM 161
Cdd:TIGR00048  86 FALGDGQTIETVLIPeddRATVCVSSQVGCALGCTFCATAKGGFNRNLEASEIIGQVlrvqkivGETGER---VSNVVFM 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 162 GMGEPSHNLRAVLEVLEFLGSAEGLGFAHKALTVSTVGDERLFEALERSPVKPALALSLHTTNDTIRRELLPRAARIPVE 241
Cdd:TIGR00048 163 GMGEPLLNLNEVVKAMEIMNDDFGFGISKRRITISTSGVVPKIDKLADKMLQVALAISLHAPNDEIRSSLMPINKKYNIE 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 242 KLLDSALRYGDLAKFPVQIEWTLLSGVNDGLDEAARLAGLLKGRRAMVNYIDLNAVEGSDFRPVPEERAQELITVLRRSG 321
Cdd:TIGR00048 243 TLLAAVRRYLEKTGRRVTFEYVLLDGVNDQVEHAEELAELLKGTKCKVNLIPWNPFPEADYGRPSNSQIDRFAKVLMSYG 322
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1486688785 322 TVATLRKSAARTVEGGCGQLRAVRLAGATRSSA 354
Cdd:TIGR00048 323 FTVTIRKSRGDDIDAACGQLRAKDVIDRTKRTL 355
PRK11194 PRK11194
ribosomal RNA large subunit methyltransferase N; Provisional
93-341 4.57e-44

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 183031  Cd Length: 372  Bit Score: 155.65  E-value: 4.57e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785  93 AMRAGD-FVEAVLLP---REGLCVSTQVGCAVGCRFCMTGRSGLVRQLGSLEILAQV----------REGLRRMPTlaKI 158
Cdd:PRK11194   84 AIAVGDqRVETVYIPeddRATLCVSSQVGCALECKFCSTAQQGFNRNLRVSEIIGQVwraakiigaaKVTGQRPIT--NV 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 159 KFMGMGEPSHNLRAVLEVLEFLGSAEGLGFAHKALTVSTVGderLFEALE--RSPVKPALALSLHTTNDTIRRELLPRAA 236
Cdd:PRK11194  162 VMMGMGEPLLNLNNVVPAMEIMLDDFGFGLSKRRVTLSTSG---VVPALDklGDMIDVALAISLHAPNDELRDEIVPINK 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 237 RIPVEKLLDSALRYgdLAKF-----PVQIEWTLLSGVNDGLDEAARLAGLLKGRRAMVNYIDLNAVEGSDFRPVPEERAQ 311
Cdd:PRK11194  239 KYNIETFLAAVRRY--LEKSnanqgRVTVEYVMLDHVNDGTEHAHQLAELLKDTPCKINLIPWNPFPGAPYGRSSNSRID 316
                         250       260       270
                  ....*....|....*....|....*....|
gi 1486688785 312 ELITVLRRSGTVATLRKSAARTVEGGCGQL 341
Cdd:PRK11194  317 RFSKVLMEYGFTVIVRKTRGDDIDAACGQL 346
PRK14461 PRK14461
ribosomal RNA large subunit methyltransferase N; Provisional
60-343 5.03e-40

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 237718  Cd Length: 371  Bit Score: 145.03  E-value: 5.03e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785  60 PAALTRALP-EVRALLESIGRVECSDAE-TAKLLLAMRAGDFVEAVLL---PREGLCVSTQVGCAVGCRFCMTGRSGLVR 134
Cdd:PRK14461   54 PLALRERLTaELPLSTLRLEQVQIGDNGlTRKALFRLPDGAVVETVLMiypDRATVCVSTQAGCGMGCVFCATGTLGLLR 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 135 QLGSLEILAQV----REgLRRM----------PT--LAKIKFMGMGEPSHNLRAVLEVLEFLGSAEGLGFAHKALTVSTV 198
Cdd:PRK14461  134 NLSSGEIVAQViwasRE-LRAMgaaiskrhagPVgrVTNLVFMGMGEPFANYDRWWQAVERLHDPQGFNLGARSMTVSTV 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 199 ----GDERLfeALERSPVKpaLALSLHTTNDTIRRELLPRAARIPVEKLLDSALRYGDLAKFPVQIEWTLLSGVNDGLDE 274
Cdd:PRK14461  213 glvkGIRRL--ANERLPIN--LAISLHAPDDALRSELMPVNRRYPIADLMAATRDYIAKTRRRVSFEYVLLQGKNDHPEQ 288
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1486688785 275 AARLAGLLKGRRAM------VNYIDLNAVEGSDFRPVPEERAQELITVLRRSGTVATLRKSAARTVEGGCGQLRA 343
Cdd:PRK14461  289 AAALARLLRGEAPPgpllvhVNLIPWNPVPGTPLGRSERERVTTFQRILTDYGIPCTVRVERGVEIAAACGQLAG 363
PRK14453 PRK14453
chloramphenicol/florfenicol resistance protein; Provisional
76-341 3.77e-37

chloramphenicol/florfenicol resistance protein; Provisional


Pssm-ID: 184685  Cd Length: 347  Bit Score: 136.80  E-value: 3.77e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785  76 SIGRVECSDAETA-KLLLAMRAGDFVEAVLLPR----EGLCVSTQVGCAVGCRFCMTGRSGLVRQLGSLEILAQVREGLR 150
Cdd:PRK14453   63 SVIPVFEQDSKQVtKVLFELTDGERIEAVGLKYkqgwESFCISSQCGCGFGCRFCATGSIGLKRNLTADEITDQLLYFYL 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 151 RMPTLAKIKFMGMGEPSHNLRaVLEVLEFLGSAEGLGFAHKALTVSTVGDERLFEALERSPVKPALALSLHTTNDTIRRE 230
Cdd:PRK14453  143 NGHRLDSISFMGMGEALANPE-LFDALKILTDPNLFGLSQRRITISTIGIIPGIQRLTQEFPQVNLTFSLHSPFESQRSE 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 231 LLPRAARIPVEKLLDSALRYGDLAKFPVQIEWTLLSGVNDGLDEAARLAGLLKGRRAM-----VNYIDLNAVEGS--DFR 303
Cdd:PRK14453  222 LMPINKRFPLNEVMKTLDEHIRHTGRKVYIAYIMLEGVNDSKEHAEAVVGLLRNRGSWehlyhVNLIPYNSTDKTpfKFQ 301
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1486688785 304 PVPEERAQELITVLRRSGTVATLRKSAARTVEGGCGQL 341
Cdd:PRK14453  302 SSSAGQIKQFCSTLKSAGISVTVRTQFGSDISAACGQL 339
PRK14470 PRK14470
ribosomal RNA large subunit methyltransferase N; Provisional
24-345 3.47e-36

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 172945  Cd Length: 336  Bit Score: 133.90  E-value: 3.47e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785  24 LREALARRGAKPEHVRRILLAWMGLAPWAADAKcrypAALTRALPEVRALLE--SIGRVECSDAETA--KLLLAMRAGDF 99
Cdd:PRK14470    9 SRALARPAGISLEDARRITGAVIGRGAPLRSAR----NVRRSVLDEVDALATpgELRLVERVDAKDGfrKYLFELPDGLR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 100 VEAVLLP----REGLCVSTQVGCAVGCRFCMTGRSGLVRQLGSLEILAQ---VREGLRRmpTLAKIKFMGMGEPSHNLRA 172
Cdd:PRK14470   85 VEAVRIPlfdtHHVVCLSSQAGCALGCAFCATGKLGLDRSLRSWEIVAQllaVRADSER--PITGVVFMGQGEPFLNYDE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 173 VLEVLEFLGSAEGLGFAHKALTVSTVGDERLFEALERSPVKPALALSLHTTNDTIRRELLPRAARIPVEKLLDSALRYGD 252
Cdd:PRK14470  163 VLRAAYALCDPAGARIDGRRISISTAGVVPMIRRYTAEGHKFRLCISLNAAIPWKRRALMPIEQGFPLDELVEAIREHAA 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 253 LaKFPVQIEWTLLSGVNDGLDEAARLAGLLKGRRAMVNYIDLNAVEGSdFRPVPEERAQELITVLRRS--GTVATLRKSA 330
Cdd:PRK14470  243 L-RGRVTLEYVMISGVNVGEEDAAALGRLLAGIPVRLNPIAVNDATGR-YRPPDEDEWNAFRDALARElpGTPVVRRYSG 320
                         330
                  ....*....|....*
gi 1486688785 331 ARTVEGGCGQLRAVR 345
Cdd:PRK14470  321 GQDEHAACGMLASRR 335
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
114-270 3.76e-11

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: 61.00  E-value: 3.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 114 TQVGCAVGCRFCMTGRSGLVRQLGSL---EILAQVREgLRRMPTlaKIKFMGMGEPSHNLRAVLEVLEFLGSAEGLGFAH 190
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKGRELspeEILEEAKE-LKRLGV--EVVILGGGEPLLLPDLVELLERLLKLELAEGIRI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 191 KALTVSTVGDERLFEALERSPVKpALALSLHTTNDTIRRellPRAARIPVEKLLDSALRYGDLAKFPVQIEWTLLSGVND 270
Cdd:pfam04055  78 TLETNGTLLDEELLELLKEAGLD-RVSIGLESGDDEVLK---LINRGHTFEEVLEALELLREAGIPVVTDNIVGLPGETD 153
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
140-313 7.06e-05

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: 43.64  E-value: 7.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 140 EILAQVREGLRRMPTLAK----IKFMGMGEPSHNLRavL-EVLEFLGSAEGLgfahkalTV------STVGDERLFEALE 208
Cdd:COG0731    61 EILEELIEFLRKLPEEARepdhITFSGSGEPTLYPN--LgELIEEIKKLRGI-------KTalltngSLLHRPEVREELL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 209 RSPVkpaLALSLHTTNDTIRRELLPRAARIPVEKLLDSALRYGDLAKFPVQIEWTLLSGVNDGLDEAARLAGLLKgrRAM 288
Cdd:COG0731   132 KADQ---VYPSLDAADEETFRKINRPHPGLSWERIIEGLELFRKLYKGRTVIETMLVKGINDSEEELEAYAELIK--RIN 206
                         170       180
                  ....*....|....*....|....*
gi 1486688785 289 VNYIDLNAVegsdFRPVPEERAQEL 313
Cdd:COG0731   207 PDFVELKTY----MRPPALSRVNMP 227
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
117-319 2.34e-04

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: 41.94  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 117 GCAVGCRFCMTGRSGLVRQLGSLEILAQVREGLRRMPTLAKIKFMGMGEPSHNLRAVLEVLEFLGSAEGLGFAhkALTVS 196
Cdd:cd01335     6 GCNLNCGFCSNPASKGRGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGFEIS--IETNG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486688785 197 TVGDERLFEALERSPVKpALALSLHTTNDTIRRELlpRAARIPVEKLLDSALRYGDlAKFPVQIEWTLLSGVNDGLDEAA 276
Cdd:cd01335    84 TLLTEELLKELKELGLD-GVGVSLDSGDEEVADKI--RGSGESFKERLEALKELRE-AGLGLSTTLLVGLGDEDEEDDLE 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1486688785 277 RLAGLLK-GRRAMVNYIDLNAVEGS-DFRPVPEERAQELITVLRR 319
Cdd:cd01335   160 ELELLAEfRSPDRVSLFRLLPEEGTpLELAAPVVPAEKLLRLIAA 204
 
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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