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Conserved domains on  [gi|504510524|ref|WP_014697626|]
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23S rRNA (adenine(2503)-C(2))-methyltransferase RlmN [Bifidobacterium animalis]

Protein Classification

23S rRNA (adenine(2503)-C(2))-methyltransferase RlmN( domain architecture ID 11435290)

23S rRNA (adenine(2503)-C(2))-methyltransferase RlmN is a dual-specificity RNA methyltransferase that specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RlmN COG0820
Adenine C2-methylase RlmN of 23S rRNA A2503 and tRNA A37 [Translation, ribosomal structure and ...
47-395 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: 533.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524  47 FADLTDDERIAKAKELGLPKFRVRQLANHYYGHFDADAGNFTDFPAGKRDEVAREFFPTLIREVTRQVADDGqTIKTLWE 126
Cdd:COG0820    1 LLGLTLEELEEFLAELGEKPFRAKQIFRWLYQKGVTDFDEMTNLPKALREKLAENFEIGLLEVVREQVSADG-TRKYLFR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 127 LFDGSKIESVLMRYPNRTTLCISSQVGCGMGCPFCATGQLGLTRNMSTGEILEQVRIAAAMMERGEvaggpGRLSNVVFM 206
Cdd:COG0820   80 LADGNLVETVLIPYEDRGTLCVSSQVGCAMGCSFCATGKQGLVRNLTAGEIVGQVLLARRDLREGG-----RRVTNIVFM 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 207 GMGEPMGNYRAIVSAVRQISAmpPEGFGISARNITVSTVGVVPGIRRLAQEGMPVRLAVSLHAPNNALRDELVPMNRRFN 286
Cdd:COG0820  155 GMGEPLLNYDNVLKAIRILND--PEGLGISARRITVSTSGLVPGIRRLADEGLPVNLAVSLHAPNDELRDELMPINKKYP 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 287 VDEVLDAAHDYYLASKRRVSIEYALMRGINDQEVHARQLANRLNHYGdnwAHVNPIPLNPIEGSKWTASKPEDERRFLEI 366
Cdd:COG0820  233 LEELLEACRRYPEKTGRRITFEYVLLKGVNDSPEDARELARLLKGLP---CKVNLIPFNPVPGSPYKRPSPERIEAFADI 309
                        330       340
                 ....*....|....*....|....*....
gi 504510524 367 LHNAGITATLRDTRGQDIDGACGQLAAKT 395
Cdd:COG0820  310 LEKAGIPVTVRRSRGDDIDAACGQLRAKV 338
 
Name Accession Description Interval E-value
RlmN COG0820
Adenine C2-methylase RlmN of 23S rRNA A2503 and tRNA A37 [Translation, ribosomal structure and ...
47-395 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: 533.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524  47 FADLTDDERIAKAKELGLPKFRVRQLANHYYGHFDADAGNFTDFPAGKRDEVAREFFPTLIREVTRQVADDGqTIKTLWE 126
Cdd:COG0820    1 LLGLTLEELEEFLAELGEKPFRAKQIFRWLYQKGVTDFDEMTNLPKALREKLAENFEIGLLEVVREQVSADG-TRKYLFR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 127 LFDGSKIESVLMRYPNRTTLCISSQVGCGMGCPFCATGQLGLTRNMSTGEILEQVRIAAAMMERGEvaggpGRLSNVVFM 206
Cdd:COG0820   80 LADGNLVETVLIPYEDRGTLCVSSQVGCAMGCSFCATGKQGLVRNLTAGEIVGQVLLARRDLREGG-----RRVTNIVFM 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 207 GMGEPMGNYRAIVSAVRQISAmpPEGFGISARNITVSTVGVVPGIRRLAQEGMPVRLAVSLHAPNNALRDELVPMNRRFN 286
Cdd:COG0820  155 GMGEPLLNYDNVLKAIRILND--PEGLGISARRITVSTSGLVPGIRRLADEGLPVNLAVSLHAPNDELRDELMPINKKYP 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 287 VDEVLDAAHDYYLASKRRVSIEYALMRGINDQEVHARQLANRLNHYGdnwAHVNPIPLNPIEGSKWTASKPEDERRFLEI 366
Cdd:COG0820  233 LEELLEACRRYPEKTGRRITFEYVLLKGVNDSPEDARELARLLKGLP---CKVNLIPFNPVPGSPYKRPSPERIEAFADI 309
                        330       340
                 ....*....|....*....|....*....
gi 504510524 367 LHNAGITATLRDTRGQDIDGACGQLAAKT 395
Cdd:COG0820  310 LEKAGIPVTVRRSRGDDIDAACGQLRAKV 338
PRK14461 PRK14461
ribosomal RNA large subunit methyltransferase N; Provisional
49-395 4.55e-112

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 237718  Cd Length: 371  Bit Score: 332.62  E-value: 4.55e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524  49 DLTDDERIAKAKELGLPKFRVRQLANHYYGHFDADAGNFTDFPAGKRDEVAREFFPTLIREVTRQVADDGQTIKTLWELF 128
Cdd:PRK14461  12 DLNLAELTELLTAWGQPAFRARQLYRHLYVNLADSVLAMTDLPLALRERLTAELPLSTLRLEQVQIGDNGLTRKALFRLP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 129 DGSKIESVLMRYPNRTTLCISSQVGCGMGCPFCATGQLGLTRNMSTGEILEQVRIAAAMM-----ERGEVAGGP-GRLSN 202
Cdd:PRK14461  92 DGAVVETVLMIYPDRATVCVSTQAGCGMGCVFCATGTLGLLRNLSSGEIVAQVIWASRELramgaAISKRHAGPvGRVTN 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 203 VVFMGMGEPMGNYRAIVSAVRQISamPPEGFGISARNITVSTVGVVPGIRRLAQEGMPVRLAVSLHAPNNALRDELVPMN 282
Cdd:PRK14461 172 LVFMGMGEPFANYDRWWQAVERLH--DPQGFNLGARSMTVSTVGLVKGIRRLANERLPINLAISLHAPDDALRSELMPVN 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 283 RRFNVDEVLDAAHDYYLASKRRVSIEYALMRGINDQEVHARQLANRLNH---YGDNWAHVNPIPLNPIEGSKWTASKPED 359
Cdd:PRK14461 250 RRYPIADLMAATRDYIAKTRRRVSFEYVLLQGKNDHPEQAAALARLLRGeapPGPLLVHVNLIPWNPVPGTPLGRSERER 329
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 504510524 360 ERRFLEILHNAGITATLRDTRGQDIDGACGQLAAKT 395
Cdd:PRK14461 330 VTTFQRILTDYGIPCTVRVERGVEIAAACGQLAGRH 365
rRNA_mod_RlmN TIGR00048
23S rRNA (adenine(2503)-C(2))-methyltransferase; Members of this family are RlmN, a 23S rRNA ...
38-394 5.51e-105

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: 314.06  E-value: 5.51e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524   38 ARRGKPPVHfaDLTDDERIAKAKELGLPKFRVRQLANHYYGHFDADAGNFTDFPAGKRDEVAREFFPTLIREVTRQVADD 117
Cdd:TIGR00048   2 AKDGKPSLL--DLTLQELRQWLKDLGEKPFRAKQIMKWLYHKGCDSFDDMTNLSKVLREKLNEVFEIRTPEIAHEQRSSD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524  118 GqTIKTLWELFDGSKIESVLMRYPNRTTLCISSQVGCGMGCPFCATGQLGLTRNMSTGEILEQV-RIAAAMMERGEvagg 196
Cdd:TIGR00048  80 G-TIKYLFALGDGQTIETVLIPEDDRATVCVSSQVGCALGCTFCATAKGGFNRNLEASEIIGQVlRVQKIVGETGE---- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524  197 pgRLSNVVFMGMGEPMGNYRAIVSAVRQISAMppEGFGISARNITVSTVGVVPGIRRLAQEGMPVRLAVSLHAPNNALRD 276
Cdd:TIGR00048 155 --RVSNVVFMGMGEPLLNLNEVVKAMEIMNDD--FGFGISKRRITISTSGVVPKIDKLADKMLQVALAISLHAPNDEIRS 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524  277 ELVPMNRRFNVDEVLDAAHDYYLASKRRVSIEYALMRGINDQEVHARQLANRLNhygDNWAHVNPIPLNPIEGSKWTASK 356
Cdd:TIGR00048 231 SLMPINKKYNIETLLAAVRRYLEKTGRRVTFEYVLLDGVNDQVEHAEELAELLK---GTKCKVNLIPWNPFPEADYGRPS 307
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 504510524  357 PEDERRFLEILHNAGITATLRDTRGQDIDGACGQLAAK 394
Cdd:TIGR00048 308 NSQIDRFAKVLMSYGFTVTIRKSRGDDIDAACGQLRAK 345
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
151-320 2.56e-14

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: 70.25  E-value: 2.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524  151 QVGCGMGCPFCA---TGQLGLTRNMSTGEILEQVRIAAAMMergevaggpgrlSNVVFMGMGEPMGNYRAIVSAVRQISA 227
Cdd:pfam04055   2 TRGCNLRCTYCAfpsIRARGKGRELSPEEILEEAKELKRLG------------VEVVILGGGEPLLLPDLVELLERLLKL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524  228 MPPEGFGIsarniTVSTVGVVPG---IRRLAQEGMpVRLAVSLHAPNNALRDelvPMNRRFNVDEVLDAAHDYYLASKRR 304
Cdd:pfam04055  70 ELAEGIRI-----TLETNGTLLDeelLELLKEAGL-DRVSIGLESGDDEVLK---LINRGHTFEEVLEALELLREAGIPV 140
                         170
                  ....*....|....*.
gi 504510524  305 VSIEYALMRGINDQEV 320
Cdd:pfam04055 141 VTDNIVGLPGETDEDL 156
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
153-367 3.58e-11

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: 61.97  E-value: 3.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 153 GCGMGCPFCATGQLGLTRNMSTGEILEQVRIAAAMMERGEVaggpgrlsnVVFMGMGEPMGNYRaIVSAVRQISAMPPeG 232
Cdd:cd01335    6 GCNLNCGFCSNPASKGRGPESPPEIEEILDIVLEAKERGVE---------VVILTGGEPLLYPE-LAELLRRLKKELP-G 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 233 FGISarnITVSTVGVVPG-IRRLAQEGmPVRLAVSLHAPNNALRDELVpmNRRFNVDEVLDAAHdYYLASKRRVSIEYAL 311
Cdd:cd01335   75 FEIS---IETNGTLLTEElLKELKELG-LDGVGVSLDSGDEEVADKIR--GSGESFKERLEALK-ELREAGLGLSTTLLV 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504510524 312 MRGINDQEVHARQLANRLNHYGDNWAHVNpiPLNPIEGS-KWTASKPEDERRFLEIL 367
Cdd:cd01335  148 GLGDEDEEDDLEELELLAEFRSPDRVSLF--RLLPEEGTpLELAAPVVPAEKLLRLI 202
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
153-367 6.79e-05

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


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 43.54  E-value: 6.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524   153 GCGMGCPFCATGQL-GLTRNMSTGEILEQVRIAAAmmergevAGGPGRLSNVVFMGMGEPMGN----YRAIVSAVRQISA 227
Cdd:smart00729  10 GCPRRCTFCSFPSLrGKLRSRYLEALVREIELLAE-------KGEKEGLVGTVFIGGGTPTLLspeqLEELLEAIREILG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524   228 MPPEgfgisaRNITVSTvgvVPG------IRRLAQEGMpVRLAVSLHAPNNALRDElvpMNRRFNVDEVLDAAHdyYLAS 301
Cdd:smart00729  83 LAKD------VEITIET---RPDtlteelLEALKEAGV-NRVSLGVQSGDDEVLKA---INRGHTVEDVLEAVE--LLRE 147
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504510524   302 KRRVSIEYALMRGINDQ-EVHARQLANRLNHYGDNWAHVNpiPLNPIEGS----KWTASKPEDERRFLEIL 367
Cdd:smart00729 148 AGPIKVSTDLIVGLPGEtEEDFEETLKLLKELGPDRVSIF--PLSPRPGTplakMYKRLKPPTKEERAELL 216
 
Name Accession Description Interval E-value
RlmN COG0820
Adenine C2-methylase RlmN of 23S rRNA A2503 and tRNA A37 [Translation, ribosomal structure and ...
47-395 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: 533.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524  47 FADLTDDERIAKAKELGLPKFRVRQLANHYYGHFDADAGNFTDFPAGKRDEVAREFFPTLIREVTRQVADDGqTIKTLWE 126
Cdd:COG0820    1 LLGLTLEELEEFLAELGEKPFRAKQIFRWLYQKGVTDFDEMTNLPKALREKLAENFEIGLLEVVREQVSADG-TRKYLFR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 127 LFDGSKIESVLMRYPNRTTLCISSQVGCGMGCPFCATGQLGLTRNMSTGEILEQVRIAAAMMERGEvaggpGRLSNVVFM 206
Cdd:COG0820   80 LADGNLVETVLIPYEDRGTLCVSSQVGCAMGCSFCATGKQGLVRNLTAGEIVGQVLLARRDLREGG-----RRVTNIVFM 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 207 GMGEPMGNYRAIVSAVRQISAmpPEGFGISARNITVSTVGVVPGIRRLAQEGMPVRLAVSLHAPNNALRDELVPMNRRFN 286
Cdd:COG0820  155 GMGEPLLNYDNVLKAIRILND--PEGLGISARRITVSTSGLVPGIRRLADEGLPVNLAVSLHAPNDELRDELMPINKKYP 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 287 VDEVLDAAHDYYLASKRRVSIEYALMRGINDQEVHARQLANRLNHYGdnwAHVNPIPLNPIEGSKWTASKPEDERRFLEI 366
Cdd:COG0820  233 LEELLEACRRYPEKTGRRITFEYVLLKGVNDSPEDARELARLLKGLP---CKVNLIPFNPVPGSPYKRPSPERIEAFADI 309
                        330       340
                 ....*....|....*....|....*....
gi 504510524 367 LHNAGITATLRDTRGQDIDGACGQLAAKT 395
Cdd:COG0820  310 LEKAGIPVTVRRSRGDDIDAACGQLRAKV 338
PRK14461 PRK14461
ribosomal RNA large subunit methyltransferase N; Provisional
49-395 4.55e-112

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 237718  Cd Length: 371  Bit Score: 332.62  E-value: 4.55e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524  49 DLTDDERIAKAKELGLPKFRVRQLANHYYGHFDADAGNFTDFPAGKRDEVAREFFPTLIREVTRQVADDGQTIKTLWELF 128
Cdd:PRK14461  12 DLNLAELTELLTAWGQPAFRARQLYRHLYVNLADSVLAMTDLPLALRERLTAELPLSTLRLEQVQIGDNGLTRKALFRLP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 129 DGSKIESVLMRYPNRTTLCISSQVGCGMGCPFCATGQLGLTRNMSTGEILEQVRIAAAMM-----ERGEVAGGP-GRLSN 202
Cdd:PRK14461  92 DGAVVETVLMIYPDRATVCVSTQAGCGMGCVFCATGTLGLLRNLSSGEIVAQVIWASRELramgaAISKRHAGPvGRVTN 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 203 VVFMGMGEPMGNYRAIVSAVRQISamPPEGFGISARNITVSTVGVVPGIRRLAQEGMPVRLAVSLHAPNNALRDELVPMN 282
Cdd:PRK14461 172 LVFMGMGEPFANYDRWWQAVERLH--DPQGFNLGARSMTVSTVGLVKGIRRLANERLPINLAISLHAPDDALRSELMPVN 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 283 RRFNVDEVLDAAHDYYLASKRRVSIEYALMRGINDQEVHARQLANRLNH---YGDNWAHVNPIPLNPIEGSKWTASKPED 359
Cdd:PRK14461 250 RRYPIADLMAATRDYIAKTRRRVSFEYVLLQGKNDHPEQAAALARLLRGeapPGPLLVHVNLIPWNPVPGTPLGRSERER 329
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 504510524 360 ERRFLEILHNAGITATLRDTRGQDIDGACGQLAAKT 395
Cdd:PRK14461 330 VTTFQRILTDYGIPCTVRVERGVEIAAACGQLAGRH 365
rRNA_mod_RlmN TIGR00048
23S rRNA (adenine(2503)-C(2))-methyltransferase; Members of this family are RlmN, a 23S rRNA ...
38-394 5.51e-105

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: 314.06  E-value: 5.51e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524   38 ARRGKPPVHfaDLTDDERIAKAKELGLPKFRVRQLANHYYGHFDADAGNFTDFPAGKRDEVAREFFPTLIREVTRQVADD 117
Cdd:TIGR00048   2 AKDGKPSLL--DLTLQELRQWLKDLGEKPFRAKQIMKWLYHKGCDSFDDMTNLSKVLREKLNEVFEIRTPEIAHEQRSSD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524  118 GqTIKTLWELFDGSKIESVLMRYPNRTTLCISSQVGCGMGCPFCATGQLGLTRNMSTGEILEQV-RIAAAMMERGEvagg 196
Cdd:TIGR00048  80 G-TIKYLFALGDGQTIETVLIPEDDRATVCVSSQVGCALGCTFCATAKGGFNRNLEASEIIGQVlRVQKIVGETGE---- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524  197 pgRLSNVVFMGMGEPMGNYRAIVSAVRQISAMppEGFGISARNITVSTVGVVPGIRRLAQEGMPVRLAVSLHAPNNALRD 276
Cdd:TIGR00048 155 --RVSNVVFMGMGEPLLNLNEVVKAMEIMNDD--FGFGISKRRITISTSGVVPKIDKLADKMLQVALAISLHAPNDEIRS 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524  277 ELVPMNRRFNVDEVLDAAHDYYLASKRRVSIEYALMRGINDQEVHARQLANRLNhygDNWAHVNPIPLNPIEGSKWTASK 356
Cdd:TIGR00048 231 SLMPINKKYNIETLLAAVRRYLEKTGRRVTFEYVLLDGVNDQVEHAEELAELLK---GTKCKVNLIPWNPFPEADYGRPS 307
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 504510524  357 PEDERRFLEILHNAGITATLRDTRGQDIDGACGQLAAK 394
Cdd:TIGR00048 308 NSQIDRFAKVLMSYGFTVTIRKSRGDDIDAACGQLRAK 345
PRK11194 PRK11194
ribosomal RNA large subunit methyltransferase N; Provisional
60-392 4.96e-81

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 183031  Cd Length: 372  Bit Score: 253.10  E-value: 4.96e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524  60 KELGLPKFRVRQLANHYYgHFDADagNF---TDFPAGKRDEVAREffpTLIR--EVT-RQVADDGqTIKtlWEL-FDGSK 132
Cdd:PRK11194  21 AELGEKPFRADQVMKWIY-HYGCD--DFdemTNINKVLREKLKEV---AEIRapEVAeEQRSSDG-TIK--WAIaVGDQR 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 133 IESVLMRYPNRTTLCISSQVGCGMGCPFCATGQLGLTRNMSTGEILEQV-RIAAAMMERGEVAGGPgrLSNVVFMGMGEP 211
Cdd:PRK11194  92 VETVYIPEDDRATLCVSSQVGCALECKFCSTAQQGFNRNLRVSEIIGQVwRAAKIIGAAKVTGQRP--ITNVVMMGMGEP 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 212 MGNYRAIVSAVRQIsaMPPEGFGISARNITVSTVGVVPGIRRLAqEGMPVRLAVSLHAPNNALRDELVPMNRRFNVDEVL 291
Cdd:PRK11194 170 LLNLNNVVPAMEIM--LDDFGFGLSKRRVTLSTSGVVPALDKLG-DMIDVALAISLHAPNDELRDEIVPINKKYNIETFL 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 292 DAAHDYYLASKR---RVSIEYALMRGINDQEVHARQLANRLNhygDNWAHVNPIPLNPIEGSKWtaSKPEDER--RFLEI 366
Cdd:PRK11194 247 AAVRRYLEKSNAnqgRVTVEYVMLDHVNDGTEHAHQLAELLK---DTPCKINLIPWNPFPGAPY--GRSSNSRidRFSKV 321
                        330       340
                 ....*....|....*....|....*.
gi 504510524 367 LHNAGITATLRDTRGQDIDGACGQLA 392
Cdd:PRK11194 322 LMEYGFTVIVRKTRGDDIDAACGQLA 347
PRK14453 PRK14453
chloramphenicol/florfenicol resistance protein; Provisional
54-391 1.17e-80

chloramphenicol/florfenicol resistance protein; Provisional


Pssm-ID: 184685  Cd Length: 347  Bit Score: 251.20  E-value: 1.17e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524  54 ERIAK-AKELGLPKFRVRQLAN----HYYGHFDAdagnFTDFPAGKRDEVAREFFPTLIREVTRQVADDGQTIKTLWELF 128
Cdd:PRK14453   8 GKMKQiLSNLKLPDYRYEQITKaifkQRIDNFED----MHILPKALRESLINEFGKNVLSVIPVFEQDSKQVTKVLFELT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 129 DGSKIESVLMRYPNR-TTLCISSQVGCGMGCPFCATGQLGLTRNMSTGEILEQVriaAAMMERGEvaggpgRLSNVVFMG 207
Cdd:PRK14453  84 DGERIEAVGLKYKQGwESFCISSQCGCGFGCRFCATGSIGLKRNLTADEITDQL---LYFYLNGH------RLDSISFMG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 208 MGEPMGNyRAIVSAVRQISamPPEGFGISARNITVSTVGVVPGIRRLAQEGMPVRLAVSLHAPNNALRDELVPMNRRFNV 287
Cdd:PRK14453 155 MGEALAN-PELFDALKILT--DPNLFGLSQRRITISTIGIIPGIQRLTQEFPQVNLTFSLHSPFESQRSELMPINKRFPL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 288 DEVLDAAHDYYLASKRRVSIEYALMRGINDQEVHARQLANRLNHYGdNWA---HVNPIPLNPIEGS--KWTASKPEDERR 362
Cdd:PRK14453 232 NEVMKTLDEHIRHTGRKVYIAYIMLEGVNDSKEHAEAVVGLLRNRG-SWEhlyHVNLIPYNSTDKTpfKFQSSSAGQIKQ 310
                        330       340
                 ....*....|....*....|....*....
gi 504510524 363 FLEILHNAGITATLRDTRGQDIDGACGQL 391
Cdd:PRK14453 311 FCSTLKSAGISVTVRTQFGSDISAACGQL 339
PRK14470 PRK14470
ribosomal RNA large subunit methyltransferase N; Provisional
96-395 5.17e-51

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 172945  Cd Length: 336  Bit Score: 174.35  E-value: 5.17e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524  96 DEVAREFFPTLIREVTRQVADDGqTIKTLWELFDGSKIESVLMR-YPNRTTLCISSQVGCGMGCPFCATGQLGLTRNMST 174
Cdd:PRK14470  49 DEVDALATPGELRLVERVDAKDG-FRKYLFELPDGLRVEAVRIPlFDTHHVVCLSSQAGCALGCAFCATGKLGLDRSLRS 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 175 GEILEQVRIAAAMMERGevaggpgrLSNVVFMGMGEPMGNYRAIVSAVRQISAmpPEGFGISARNITVSTVGVVPGIRRL 254
Cdd:PRK14470 128 WEIVAQLLAVRADSERP--------ITGVVFMGQGEPFLNYDEVLRAAYALCD--PAGARIDGRRISISTAGVVPMIRRY 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 255 AQEGMPVRLAVSLHAPNNALRDELVPMNRRFNVDEVLDAAHDYYlASKRRVSIEYALMRGINDQEVHARQLANRLNHYGd 334
Cdd:PRK14470 198 TAEGHKFRLCISLNAAIPWKRRALMPIEQGFPLDELVEAIREHA-ALRGRVTLEYVMISGVNVGEEDAAALGRLLAGIP- 275
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504510524 335 nwAHVNPIPLNPIEGsKWTASKPEDERRFLEILHNA--GITATLRDTRGQDIDGACGQLAAKT 395
Cdd:PRK14470 276 --VRLNPIAVNDATG-RYRPPDEDEWNAFRDALARElpGTPVVRRYSGGQDEHAACGMLASRR 335
PRK14464 PRK14464
RNA methyltransferase;
41-395 3.20e-50

RNA methyltransferase;


Pssm-ID: 184691  Cd Length: 344  Bit Score: 172.22  E-value: 3.20e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524  41 GKPPVHfadltdDERIAKAKELGLPKFRVRQLANHYyghfdadagnftdFPAGKRDEVAR--EFFPTLIREVTRQVADDG 118
Cdd:PRK14464  14 GAKPCH------EGRILRAWLQGLPLDTRRQRAEDF-------------LPLALREALPAleAELDGLARLRSEHPGEDG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 119 QTiKTLWELFDGSKIESVLMryPnRTTLCISSQVGCGMGCPFCATGQLGLTRNMSTGEILEQVriAAAMMERgevaggpg 198
Cdd:PRK14464  75 SA-RLLVELADGQMVESVLL--P-RDGLCVSTQVGCAVGCVFCMTGRSGLLRQLGSAEIVAQV--VLARRRR-------- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 199 RLSNVVFMGMGEPMGNYRAIVSAvrqISAMPPEGfGISARNITVSTVGVVPGIRRLAQEGMPVRLAVSLHAPNNALRDEL 278
Cdd:PRK14464 141 AVKKVVFMGMGEPAHNLDNVLEA---IDLLGTEG-GIGHKNLVFSTVGDPRVFERLPQQRVKPALALSLHTTRAELRARL 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 279 VPMNRRFNVDEVLDAAHDYYLASKRRVSIEYALMRGIND--QEVHA--RQLANRlnhygdnWAHVNPIPLNPIEGSKWta 354
Cdd:PRK14464 217 LPRAPRIAPEELVELGEAYARATGYPIQYQWTLLEGVNDsdEEMDGivRLLKGK-------YAVMNLIPYNSVDGDAY-- 287
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 504510524 355 SKPEDER--RFLEILHNAGITATLRDTRGQDIDGACGQLAAKT 395
Cdd:PRK14464 288 RRPSGERivAMARYLHRRGVLTKVRNSAGQDVDGGCGQLRARA 330
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
151-320 2.56e-14

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: 70.25  E-value: 2.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524  151 QVGCGMGCPFCA---TGQLGLTRNMSTGEILEQVRIAAAMMergevaggpgrlSNVVFMGMGEPMGNYRAIVSAVRQISA 227
Cdd:pfam04055   2 TRGCNLRCTYCAfpsIRARGKGRELSPEEILEEAKELKRLG------------VEVVILGGGEPLLLPDLVELLERLLKL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524  228 MPPEGFGIsarniTVSTVGVVPG---IRRLAQEGMpVRLAVSLHAPNNALRDelvPMNRRFNVDEVLDAAHDYYLASKRR 304
Cdd:pfam04055  70 ELAEGIRI-----TLETNGTLLDeelLELLKEAGL-DRVSIGLESGDDEVLK---LINRGHTFEEVLEALELLREAGIPV 140
                         170
                  ....*....|....*.
gi 504510524  305 VSIEYALMRGINDQEV 320
Cdd:pfam04055 141 VTDNIVGLPGETDEDL 156
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
153-367 3.58e-11

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: 61.97  E-value: 3.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 153 GCGMGCPFCATGQLGLTRNMSTGEILEQVRIAAAMMERGEVaggpgrlsnVVFMGMGEPMGNYRaIVSAVRQISAMPPeG 232
Cdd:cd01335    6 GCNLNCGFCSNPASKGRGPESPPEIEEILDIVLEAKERGVE---------VVILTGGEPLLYPE-LAELLRRLKKELP-G 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 233 FGISarnITVSTVGVVPG-IRRLAQEGmPVRLAVSLHAPNNALRDELVpmNRRFNVDEVLDAAHdYYLASKRRVSIEYAL 311
Cdd:cd01335   75 FEIS---IETNGTLLTEElLKELKELG-LDGVGVSLDSGDEEVADKIR--GSGESFKERLEALK-ELREAGLGLSTTLLV 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504510524 312 MRGINDQEVHARQLANRLNHYGDNWAHVNpiPLNPIEGS-KWTASKPEDERRFLEIL 367
Cdd:cd01335  148 GLGDEDEEDDLEELELLAEFRSPDRVSLF--RLLPEEGTpLELAAPVVPAEKLLRLI 202
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
153-367 6.79e-05

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


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 43.54  E-value: 6.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524   153 GCGMGCPFCATGQL-GLTRNMSTGEILEQVRIAAAmmergevAGGPGRLSNVVFMGMGEPMGN----YRAIVSAVRQISA 227
Cdd:smart00729  10 GCPRRCTFCSFPSLrGKLRSRYLEALVREIELLAE-------KGEKEGLVGTVFIGGGTPTLLspeqLEELLEAIREILG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524   228 MPPEgfgisaRNITVSTvgvVPG------IRRLAQEGMpVRLAVSLHAPNNALRDElvpMNRRFNVDEVLDAAHdyYLAS 301
Cdd:smart00729  83 LAKD------VEITIET---RPDtlteelLEALKEAGV-NRVSLGVQSGDDEVLKA---INRGHTVEDVLEAVE--LLRE 147
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504510524   302 KRRVSIEYALMRGINDQ-EVHARQLANRLNHYGDNWAHVNpiPLNPIEGS----KWTASKPEDERRFLEIL 367
Cdd:smart00729 148 AGPIKVSTDLIVGLPGEtEEDFEETLKLLKELGPDRVSIF--PLSPRPGTplakMYKRLKPPTKEERAELL 216
moaA PRK00164
GTP 3',8-cyclase MoaA;
158-320 2.98e-04

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 42.44  E-value: 2.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 158 CPFC--ATGQLGLTRN--MSTGEIleqVRIAAAMMERG--EVaggpgRLSnvvfmGmGEPMgnYRA-IVSAVRQISAMPP 230
Cdd:PRK00164  31 CTYCmpEGYLPFLPKEelLSLEEI---ERLVRAFVALGvrKV-----RLT-----G-GEPL--LRKdLEDIIAALAALPG 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 231 EgfgisaRNITVSTVGVvpGIRRLAQE----GMPvRLAVSLHApnnaLRDELV-PMNRRFNVDEVL---DAAHDYYLAsk 302
Cdd:PRK00164  95 I------RDLALTTNGY--LLARRAAAlkdaGLD-RVNVSLDS----LDPERFkAITGRDRLDQVLagiDAALAAGLT-- 159
                        170
                 ....*....|....*...
gi 504510524 303 rRVSIEYALMRGINDQEV 320
Cdd:PRK00164 160 -PVKVNAVLMKGVNDDEI 176
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
144-356 3.50e-04

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 42.43  E-value: 3.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 144 TTLCISSQVGCGMGCPFCATGQ-LGLTRN---MSTGEIleqVRIAAAMmergeVAGGPG--RLSNvvfmgmGEPMGNyRA 217
Cdd:PLN02951  58 NYLRISLTERCNLRCQYCMPEEgVELTPKshlLSQDEI---VRLAGLF-----VAAGVDkiRLTG------GEPTLR-KD 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510524 218 IVSAVRQISAMPpegfgiSARNITVSTVGVV--PGIRRLAQEGMpVRLAVSLhapnnalrDELVP-----MNRRFNVDEV 290
Cdd:PLN02951 123 IEDICLQLSSLK------GLKTLAMTTNGITlsRKLPRLKEAGL-TSLNISL--------DTLVPakfefLTRRKGHDRV 187
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504510524 291 LDAAHDYYLASKRRVSIEYALMRGINDQEVhaRQLANRLNHYGDNwahVNPIPLNPIEGSKWTASK 356
Cdd:PLN02951 188 LESIDTAIELGYNPVKVNCVVMRGFNDDEI--CDFVELTRDKPIN---VRFIEFMPFDGNVWNVKK 248
 
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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