NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1085021386|gb|OGS28304|]
View 

23S rRNA (adenine(2503)-C(2))-methyltransferase [Elusimicrobia bacterium RIFCSPHIGHO2_02_FULL_61_10]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
1-340 9.33e-155

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: 437.54  E-value: 9.33e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386   1 MDLKKLSIFLKENGIPAFRLNQVRDAVYKNFAASWDEVTVLPAAMRERLRHGIYIHSVEILETQVSKkrD-AIKFSFVLK 79
Cdd:COG0820     4 LTLEELEEFLAELGEKPFRAKQIFRWLYQKGVTDFDEMTNLPKALREKLAENFEIGLLEVVREQVSA--DgTRKYLFRLA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386  80 DGLKVEAVLLKLlSDKWSICLSTQVGCPVRCPFCATGKKGLKRNLSPDEITDQYLAAAHYLKTKDEqKIGSVIFMGMGEP 159
Cdd:COG0820    82 DGNLVETVLIPY-EDRGTLCVSSQVGCAMGCSFCATGKQGLVRNLTAGEIVGQVLLARRDLREGGR-RVTNIVFMGMGEP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 160 FLNYDSVAEAVRTIADPELIGLGQRHISVSTAGHVPGIRRFAKDFPQCNLAVSLHAAEDALRSDLVPLNRTYPLSQLAKA 239
Cdd:COG0820   160 LLNYDNVLKAIRILNDPEGLGISARRITVSTSGLVPGIRRLADEGLPVNLAVSLHAPNDELRDELMPINKKYPLEELLEA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 240 LKDYITSTKRRVFIEYVLFEGINNSRTQVARLNAWLRtvaaPKYFVVNIIPYNRT-GSPYKAPTRDRIKLFGELLEAAGI 318
Cdd:COG0820   240 CRRYPEKTGRRITFEYVLLKGVNDSPEDARELARLLK----GLPCKVNLIPFNPVpGSPYKRPSPERIEAFADILEKAGI 315
                         330       340
                  ....*....|....*....|..
gi 1085021386 319 EVTIRKSMGEDIEGACGQLAGK 340
Cdd:COG0820   316 PVTVRRSRGDDIDAACGQLRAK 337
 
Name Accession Description Interval E-value
RlmN COG0820
Adenine C2-methylase RlmN of 23S rRNA A2503 and tRNA A37 [Translation, ribosomal structure and ...
1-340 9.33e-155

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: 437.54  E-value: 9.33e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386   1 MDLKKLSIFLKENGIPAFRLNQVRDAVYKNFAASWDEVTVLPAAMRERLRHGIYIHSVEILETQVSKkrD-AIKFSFVLK 79
Cdd:COG0820     4 LTLEELEEFLAELGEKPFRAKQIFRWLYQKGVTDFDEMTNLPKALREKLAENFEIGLLEVVREQVSA--DgTRKYLFRLA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386  80 DGLKVEAVLLKLlSDKWSICLSTQVGCPVRCPFCATGKKGLKRNLSPDEITDQYLAAAHYLKTKDEqKIGSVIFMGMGEP 159
Cdd:COG0820    82 DGNLVETVLIPY-EDRGTLCVSSQVGCAMGCSFCATGKQGLVRNLTAGEIVGQVLLARRDLREGGR-RVTNIVFMGMGEP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 160 FLNYDSVAEAVRTIADPELIGLGQRHISVSTAGHVPGIRRFAKDFPQCNLAVSLHAAEDALRSDLVPLNRTYPLSQLAKA 239
Cdd:COG0820   160 LLNYDNVLKAIRILNDPEGLGISARRITVSTSGLVPGIRRLADEGLPVNLAVSLHAPNDELRDELMPINKKYPLEELLEA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 240 LKDYITSTKRRVFIEYVLFEGINNSRTQVARLNAWLRtvaaPKYFVVNIIPYNRT-GSPYKAPTRDRIKLFGELLEAAGI 318
Cdd:COG0820   240 CRRYPEKTGRRITFEYVLLKGVNDSPEDARELARLLK----GLPCKVNLIPFNPVpGSPYKRPSPERIEAFADILEKAGI 315
                         330       340
                  ....*....|....*....|..
gi 1085021386 319 EVTIRKSMGEDIEGACGQLAGK 340
Cdd:COG0820   316 PVTVRRSRGDDIDAACGQLRAK 337
rRNA_mod_RlmN TIGR00048
23S rRNA (adenine(2503)-C(2))-methyltransferase; Members of this family are RlmN, a 23S rRNA ...
1-340 1.53e-98

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: 295.19  E-value: 1.53e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386   1 MDLKKLSIFLKENGIPAFRLNQVRDAVYKNFAASWDEVTVLPAAMRERLRHGIYIHSVEILETQVSKKrDAIKFSFVLKD 80
Cdd:TIGR00048  12 LTLQELRQWLKDLGEKPFRAKQIMKWLYHKGCDSFDDMTNLSKVLREKLNEVFEIRTPEIAHEQRSSD-GTIKYLFALGD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386  81 GLKVEAVLLKLlSDKWSICLSTQVGCPVRCPFCATGKKGLKRNLSPDEITDQYLAAAHYLKTKDEqKIGSVIFMGMGEPF 160
Cdd:TIGR00048  91 GQTIETVLIPE-DDRATVCVSSQVGCALGCTFCATAKGGFNRNLEASEIIGQVLRVQKIVGETGE-RVSNVVFMGMGEPL 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 161 LNYDSVAEAVRTIADPELIGLGQRHISVSTAGHVPGIRRFAKDFPQCNLAVSLHAAEDALRSDLVPLNRTYPLSQLAKAL 240
Cdd:TIGR00048 169 LNLNEVVKAMEIMNDDFGFGISKRRITISTSGVVPKIDKLADKMLQVALAISLHAPNDEIRSSLMPINKKYNIETLLAAV 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 241 KDYITSTKRRVFIEYVLFEGINNSRTQVARLNAWLRTVAAPkyfvVNIIPYN-RTGSPYKAPTRDRIKLFGELLEAAGIE 319
Cdd:TIGR00048 249 RRYLEKTGRRVTFEYVLLDGVNDQVEHAEELAELLKGTKCK----VNLIPWNpFPEADYGRPSNSQIDRFAKVLMSYGFT 324
                         330       340
                  ....*....|....*....|.
gi 1085021386 320 VTIRKSMGEDIEGACGQLAGK 340
Cdd:TIGR00048 325 VTIRKSRGDDIDAACGQLRAK 345
PRK14461 PRK14461
ribosomal RNA large subunit methyltransferase N; Provisional
1-339 2.07e-96

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 237718  Cd Length: 371  Bit Score: 290.25  E-value: 2.07e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386   1 MDLKKLSIFLKENGIPAFRLNQVRDAVYKNFAASWDEVTVLPAAMRERLRHGIYIHSVEILETQVSKKRDAIKFSFVLKD 80
Cdd:PRK14461   13 LNLAELTELLTAWGQPAFRARQLYRHLYVNLADSVLAMTDLPLALRERLTAELPLSTLRLEQVQIGDNGLTRKALFRLPD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386  81 GLKVEAVLLkLLSDKWSICLSTQVGCPVRCPFCATGKKGLKRNLSPDEITDQYLAAAHYLK----TKDEQKIGSV----- 151
Cdd:PRK14461   93 GAVVETVLM-IYPDRATVCVSTQAGCGMGCVFCATGTLGLLRNLSSGEIVAQVIWASRELRamgaAISKRHAGPVgrvtn 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 152 -IFMGMGEPFLNYDSVAEAVRTIADPELIGLGQRHISVSTAGHVPGIRRFAKDFPQCNLAVSLHAAEDALRSDLVPLNRT 230
Cdd:PRK14461  172 lVFMGMGEPFANYDRWWQAVERLHDPQGFNLGARSMTVSTVGLVKGIRRLANERLPINLAISLHAPDDALRSELMPVNRR 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 231 YPLSQLAKALKDYITSTKRRVFIEYVLFEGINNSRTQVARLNAWLRTVA--APKYFVVNIIPYNRT-GSPYKAPTRDRIK 307
Cdd:PRK14461  252 YPIADLMAATRDYIAKTRRRVSFEYVLLQGKNDHPEQAAALARLLRGEAppGPLLVHVNLIPWNPVpGTPLGRSERERVT 331
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1085021386 308 LFGELLEAAGIEVTIRKSMGEDIEGACGQLAG 339
Cdd:PRK14461  332 TFQRILTDYGIPCTVRVERGVEIAAACGQLAG 363
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
102-262 2.36e-12

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: 64.08  E-value: 2.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 102 TQVGCPVRCPFCATGKK---GLKRNLSPDEITDQYLAAAHYLKtkdeqkigSVIFMGMGEPFLNYDSVAEAVRTIadpEL 178
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIrarGKGRELSPEEILEEAKELKRLGV--------EVVILGGGEPLLLPDLVELLERLL---KL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 179 IGLGQRHISVSTAGHVPGIRRFA--KDFPQCNLAVSLHAAEDALRSdlvPLNRTYPLSQLAKALKDYITSTKRRVFIEYV 256
Cdd:pfam04055  70 ELAEGIRITLETNGTLLDEELLEllKEAGLDRVSIGLESGDDEVLK---LINRGHTFEEVLEALELLREAGIPVVTDNIV 146

                  ....*.
gi 1085021386 257 LFEGIN 262
Cdd:pfam04055 147 GLPGET 152
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
105-306 3.92e-09

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: 55.80  E-value: 3.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 105 GCPVRCPFCATGKKGLKRNLSPDEITDQYLAAAhylktKDEQKIGSVIFMGMGEPFLNYDsVAEAVRTIADpeliGLGQR 184
Cdd:cd01335     6 GCNLNCGFCSNPASKGRGPESPPEIEEILDIVL-----EAKERGVEVVILTGGEPLLYPE-LAELLRRLKK----ELPGF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 185 HISVSTAGHVPGIRRFA--KDFPQCNLAVSLHAAEDALRSDLVPLNRTYPLS-QLAKALKDYITSTKRRVFIEyvLFEGI 261
Cdd:cd01335    76 EISIETNGTLLTEELLKelKELGLDGVGVSLDSGDEEVADKIRGSGESFKERlEALKELREAGLGLSTTLLVG--LGDED 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1085021386 262 NNSRTQVARLNAWLRTVAAPKYFVVNIIPYNRTGSPYKAPTRDRI 306
Cdd:cd01335   154 EEDDLEELELLAEFRSPDRVSLFRLLPEEGTPLELAAPVVPAEKL 198
 
Name Accession Description Interval E-value
RlmN COG0820
Adenine C2-methylase RlmN of 23S rRNA A2503 and tRNA A37 [Translation, ribosomal structure and ...
1-340 9.33e-155

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: 437.54  E-value: 9.33e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386   1 MDLKKLSIFLKENGIPAFRLNQVRDAVYKNFAASWDEVTVLPAAMRERLRHGIYIHSVEILETQVSKkrD-AIKFSFVLK 79
Cdd:COG0820     4 LTLEELEEFLAELGEKPFRAKQIFRWLYQKGVTDFDEMTNLPKALREKLAENFEIGLLEVVREQVSA--DgTRKYLFRLA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386  80 DGLKVEAVLLKLlSDKWSICLSTQVGCPVRCPFCATGKKGLKRNLSPDEITDQYLAAAHYLKTKDEqKIGSVIFMGMGEP 159
Cdd:COG0820    82 DGNLVETVLIPY-EDRGTLCVSSQVGCAMGCSFCATGKQGLVRNLTAGEIVGQVLLARRDLREGGR-RVTNIVFMGMGEP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 160 FLNYDSVAEAVRTIADPELIGLGQRHISVSTAGHVPGIRRFAKDFPQCNLAVSLHAAEDALRSDLVPLNRTYPLSQLAKA 239
Cdd:COG0820   160 LLNYDNVLKAIRILNDPEGLGISARRITVSTSGLVPGIRRLADEGLPVNLAVSLHAPNDELRDELMPINKKYPLEELLEA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 240 LKDYITSTKRRVFIEYVLFEGINNSRTQVARLNAWLRtvaaPKYFVVNIIPYNRT-GSPYKAPTRDRIKLFGELLEAAGI 318
Cdd:COG0820   240 CRRYPEKTGRRITFEYVLLKGVNDSPEDARELARLLK----GLPCKVNLIPFNPVpGSPYKRPSPERIEAFADILEKAGI 315
                         330       340
                  ....*....|....*....|..
gi 1085021386 319 EVTIRKSMGEDIEGACGQLAGK 340
Cdd:COG0820   316 PVTVRRSRGDDIDAACGQLRAK 337
rRNA_mod_RlmN TIGR00048
23S rRNA (adenine(2503)-C(2))-methyltransferase; Members of this family are RlmN, a 23S rRNA ...
1-340 1.53e-98

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: 295.19  E-value: 1.53e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386   1 MDLKKLSIFLKENGIPAFRLNQVRDAVYKNFAASWDEVTVLPAAMRERLRHGIYIHSVEILETQVSKKrDAIKFSFVLKD 80
Cdd:TIGR00048  12 LTLQELRQWLKDLGEKPFRAKQIMKWLYHKGCDSFDDMTNLSKVLREKLNEVFEIRTPEIAHEQRSSD-GTIKYLFALGD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386  81 GLKVEAVLLKLlSDKWSICLSTQVGCPVRCPFCATGKKGLKRNLSPDEITDQYLAAAHYLKTKDEqKIGSVIFMGMGEPF 160
Cdd:TIGR00048  91 GQTIETVLIPE-DDRATVCVSSQVGCALGCTFCATAKGGFNRNLEASEIIGQVLRVQKIVGETGE-RVSNVVFMGMGEPL 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 161 LNYDSVAEAVRTIADPELIGLGQRHISVSTAGHVPGIRRFAKDFPQCNLAVSLHAAEDALRSDLVPLNRTYPLSQLAKAL 240
Cdd:TIGR00048 169 LNLNEVVKAMEIMNDDFGFGISKRRITISTSGVVPKIDKLADKMLQVALAISLHAPNDEIRSSLMPINKKYNIETLLAAV 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 241 KDYITSTKRRVFIEYVLFEGINNSRTQVARLNAWLRTVAAPkyfvVNIIPYN-RTGSPYKAPTRDRIKLFGELLEAAGIE 319
Cdd:TIGR00048 249 RRYLEKTGRRVTFEYVLLDGVNDQVEHAEELAELLKGTKCK----VNLIPWNpFPEADYGRPSNSQIDRFAKVLMSYGFT 324
                         330       340
                  ....*....|....*....|.
gi 1085021386 320 VTIRKSMGEDIEGACGQLAGK 340
Cdd:TIGR00048 325 VTIRKSRGDDIDAACGQLRAK 345
PRK14461 PRK14461
ribosomal RNA large subunit methyltransferase N; Provisional
1-339 2.07e-96

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 237718  Cd Length: 371  Bit Score: 290.25  E-value: 2.07e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386   1 MDLKKLSIFLKENGIPAFRLNQVRDAVYKNFAASWDEVTVLPAAMRERLRHGIYIHSVEILETQVSKKRDAIKFSFVLKD 80
Cdd:PRK14461   13 LNLAELTELLTAWGQPAFRARQLYRHLYVNLADSVLAMTDLPLALRERLTAELPLSTLRLEQVQIGDNGLTRKALFRLPD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386  81 GLKVEAVLLkLLSDKWSICLSTQVGCPVRCPFCATGKKGLKRNLSPDEITDQYLAAAHYLK----TKDEQKIGSV----- 151
Cdd:PRK14461   93 GAVVETVLM-IYPDRATVCVSTQAGCGMGCVFCATGTLGLLRNLSSGEIVAQVIWASRELRamgaAISKRHAGPVgrvtn 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 152 -IFMGMGEPFLNYDSVAEAVRTIADPELIGLGQRHISVSTAGHVPGIRRFAKDFPQCNLAVSLHAAEDALRSDLVPLNRT 230
Cdd:PRK14461  172 lVFMGMGEPFANYDRWWQAVERLHDPQGFNLGARSMTVSTVGLVKGIRRLANERLPINLAISLHAPDDALRSELMPVNRR 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 231 YPLSQLAKALKDYITSTKRRVFIEYVLFEGINNSRTQVARLNAWLRTVA--APKYFVVNIIPYNRT-GSPYKAPTRDRIK 307
Cdd:PRK14461  252 YPIADLMAATRDYIAKTRRRVSFEYVLLQGKNDHPEQAAALARLLRGEAppGPLLVHVNLIPWNPVpGTPLGRSERERVT 331
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1085021386 308 LFGELLEAAGIEVTIRKSMGEDIEGACGQLAG 339
Cdd:PRK14461  332 TFQRILTDYGIPCTVRVERGVEIAAACGQLAG 363
PRK14453 PRK14453
chloramphenicol/florfenicol resistance protein; Provisional
5-339 9.39e-95

chloramphenicol/florfenicol resistance protein; Provisional


Pssm-ID: 184685  Cd Length: 347  Bit Score: 285.49  E-value: 9.39e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386   5 KLSIFLKENGIPAFRLNQVRDAVYKNFAASWDEVTVLPAAMRERL--RHGIYIHSVEILETQVSKKRDAIKFSfvLKDGL 82
Cdd:PRK14453    9 KMKQILSNLKLPDYRYEQITKAIFKQRIDNFEDMHILPKALRESLinEFGKNVLSVIPVFEQDSKQVTKVLFE--LTDGE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386  83 KVEAVLLKLLSDKWSICLSTQVGCPVRCPFCATGKKGLKRNLSPDEITDQYLaaahYLKTKDeQKIGSVIFMGMGEPFLN 162
Cdd:PRK14453   87 RIEAVGLKYKQGWESFCISSQCGCGFGCRFCATGSIGLKRNLTADEITDQLL----YFYLNG-HRLDSISFMGMGEALAN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 163 yDSVAEAVRTIADPELIGLGQRHISVSTAGHVPGIRRFAKDFPQCNLAVSLHAAEDALRSDLVPLNRTYPLSQLAKALKD 242
Cdd:PRK14453  162 -PELFDALKILTDPNLFGLSQRRITISTIGIIPGIQRLTQEFPQVNLTFSLHSPFESQRSELMPINKRFPLNEVMKTLDE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 243 YITSTKRRVFIEYVLFEGINNSRTQVARLNAWLRTVAA-PKYFVVNIIPYNRT-GSP--YKAPTRDRIKLFGELLEAAGI 318
Cdd:PRK14453  241 HIRHTGRKVYIAYIMLEGVNDSKEHAEAVVGLLRNRGSwEHLYHVNLIPYNSTdKTPfkFQSSSAGQIKQFCSTLKSAGI 320
                         330       340
                  ....*....|....*....|.
gi 1085021386 319 EVTIRKSMGEDIEGACGQLAG 339
Cdd:PRK14453  321 SVTVRTQFGSDISAACGQLYG 341
PRK11194 PRK11194
ribosomal RNA large subunit methyltransferase N; Provisional
1-339 3.38e-74

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 183031  Cd Length: 372  Bit Score: 233.46  E-value: 3.38e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386   1 MDLKKLSIFLKENGIPAFRLNQVRDAVYKNFAASWDEVTVLPAAMRERLRHGIYIHSVEILETQVSKKrDAIKFSFVLKD 80
Cdd:PRK11194   11 LNRQQMREFFAELGEKPFRADQVMKWIYHYGCDDFDEMTNINKVLREKLKEVAEIRAPEVAEEQRSSD-GTIKWAIAVGD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386  81 GlKVEAVLLKLlSDKWSICLSTQVGCPVRCPFCATGKKGLKRNLSPDEITDQYLAAAHYL---KTKDEQKIGSVIFMGMG 157
Cdd:PRK11194   90 Q-RVETVYIPE-DDRATLCVSSQVGCALECKFCSTAQQGFNRNLRVSEIIGQVWRAAKIIgaaKVTGQRPITNVVMMGMG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 158 EPFLNYDSVAEAVRTIADPELIGLGQRHISVSTAGHVPGIRRFaKDFPQCNLAVSLHAAEDALRSDLVPLNRTYPLSQLA 237
Cdd:PRK11194  168 EPLLNLNNVVPAMEIMLDDFGFGLSKRRVTLSTSGVVPALDKL-GDMIDVALAISLHAPNDELRDEIVPINKKYNIETFL 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 238 KALKDYITSTKR---RVFIEYVLFEGINNSRTQVARLNAWLRTVAAPkyfvVNIIPYNR-TGSPYKAPTRDRIKLFGELL 313
Cdd:PRK11194  247 AAVRRYLEKSNAnqgRVTVEYVMLDHVNDGTEHAHQLAELLKDTPCK----INLIPWNPfPGAPYGRSSNSRIDRFSKVL 322
                         330       340
                  ....*....|....*....|....*.
gi 1085021386 314 EAAGIEVTIRKSMGEDIEGACGQLAG 339
Cdd:PRK11194  323 MEYGFTVIVRKTRGDDIDAACGQLAG 348
PRK14470 PRK14470
ribosomal RNA large subunit methyltransferase N; Provisional
62-340 3.06e-60

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 172945  Cd Length: 336  Bit Score: 196.30  E-value: 3.06e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386  62 ETQVSKKRDA----IKFSFVLKDGLKVEAVLLKLLSDKWSICLSTQVGCPVRCPFCATGKKGLKRNLSPDEITDQYLAaa 137
Cdd:PRK14470   59 ELRLVERVDAkdgfRKYLFELPDGLRVEAVRIPLFDTHHVVCLSSQAGCALGCAFCATGKLGLDRSLRSWEIVAQLLA-- 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 138 hyLKTKDEQKIGSVIFMGMGEPFLNYDSVAEAVRTIADPELIGLGQRHISVSTAGHVPGIRRFAKDFPQCNLAVSLHAAE 217
Cdd:PRK14470  137 --VRADSERPITGVVFMGQGEPFLNYDEVLRAAYALCDPAGARIDGRRISISTAGVVPMIRRYTAEGHKFRLCISLNAAI 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 218 DALRSDLVPLNRTYPLSQLAKALKDYiTSTKRRVFIEYVLFEGINNSRTQVARLNAWLRTVAAPkyfvVNIIPYNRTGSP 297
Cdd:PRK14470  215 PWKRRALMPIEQGFPLDELVEAIREH-AALRGRVTLEYVMISGVNVGEEDAAALGRLLAGIPVR----LNPIAVNDATGR 289
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1085021386 298 YKAPTRDRIKLFGELL--EAAGIEVTIRKSMGEDIEGACGQLAGK 340
Cdd:PRK14470  290 YRPPDEDEWNAFRDALarELPGTPVVRRYSGGQDEHAACGMLASR 334
PRK14464 PRK14464
RNA methyltransferase;
78-337 1.38e-46

RNA methyltransferase;


Pssm-ID: 184691  Cd Length: 344  Bit Score: 161.05  E-value: 1.38e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386  78 LKDGLKVEAVLLKllsdKWSICLSTQVGCPVRCPFCATGKKGLKRNLSPDEITDQYLAAahylktKDEQKIGSVIFMGMG 157
Cdd:PRK14464   82 LADGQMVESVLLP----RDGLCVSTQVGCAVGCVFCMTGRSGLLRQLGSAEIVAQVVLA------RRRRAVKKVVFMGMG 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 158 EPFLNYDSVAEAVrtiadpELIG----LGQRHISVSTAGHvpgiRRFAKDFPQCN----LAVSLHAAEDALRSDLVPLNR 229
Cdd:PRK14464  152 EPAHNLDNVLEAI------DLLGteggIGHKNLVFSTVGD----PRVFERLPQQRvkpaLALSLHTTRAELRARLLPRAP 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 230 TYPLSQLAKALKDYITSTKRRVFIEYVLFEGINNSRtqvARLNAWLRTVAApKYFVVNIIPYNRT-GSPYKAPTRDRIKL 308
Cdd:PRK14464  222 RIAPEELVELGEAYARATGYPIQYQWTLLEGVNDSD---EEMDGIVRLLKG-KYAVMNLIPYNSVdGDAYRRPSGERIVA 297
                         250       260
                  ....*....|....*....|....*....
gi 1085021386 309 FGELLEAAGIEVTIRKSMGEDIEGACGQL 337
Cdd:PRK14464  298 MARYLHRRGVLTKVRNSAGQDVDGGCGQL 326
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
102-262 2.36e-12

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: 64.08  E-value: 2.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 102 TQVGCPVRCPFCATGKK---GLKRNLSPDEITDQYLAAAHYLKtkdeqkigSVIFMGMGEPFLNYDSVAEAVRTIadpEL 178
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIrarGKGRELSPEEILEEAKELKRLGV--------EVVILGGGEPLLLPDLVELLERLL---KL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 179 IGLGQRHISVSTAGHVPGIRRFA--KDFPQCNLAVSLHAAEDALRSdlvPLNRTYPLSQLAKALKDYITSTKRRVFIEYV 256
Cdd:pfam04055  70 ELAEGIRITLETNGTLLDEELLEllKEAGLDRVSIGLESGDDEVLK---LINRGHTFEEVLEALELLREAGIPVVTDNIV 146

                  ....*.
gi 1085021386 257 LFEGIN 262
Cdd:pfam04055 147 GLPGET 152
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
105-306 3.92e-09

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: 55.80  E-value: 3.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 105 GCPVRCPFCATGKKGLKRNLSPDEITDQYLAAAhylktKDEQKIGSVIFMGMGEPFLNYDsVAEAVRTIADpeliGLGQR 184
Cdd:cd01335     6 GCNLNCGFCSNPASKGRGPESPPEIEEILDIVL-----EAKERGVEVVILTGGEPLLYPE-LAELLRRLKK----ELPGF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 185 HISVSTAGHVPGIRRFA--KDFPQCNLAVSLHAAEDALRSDLVPLNRTYPLS-QLAKALKDYITSTKRRVFIEyvLFEGI 261
Cdd:cd01335    76 EISIETNGTLLTEELLKelKELGLDGVGVSLDSGDEEVADKIRGSGESFKERlEALKELREAGLGLSTTLLVG--LGDED 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1085021386 262 NNSRTQVARLNAWLRTVAAPKYFVVNIIPYNRTGSPYKAPTRDRI 306
Cdd:cd01335   154 EEDDLEELELLAEFRSPDRVSLFRLLPEEGTPLELAAPVVPAEKL 198
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
97-327 1.46e-07

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 51.72  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386  97 SICLS--TQvGCPVRCPFC------ATGKKGLKRNLSPDEITDQYLAAAHYLktkdeQKIGSVIFMGmGEPFLNYDSVAE 168
Cdd:COG1180    21 SIRLSvfTQ-GCNLRCPYChnpeisQGRPDAAGRELSPEELVEEALKDRGFL-----DSCGGVTFSG-GEPTLQPEFLLD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 169 AVRTIADpelIGLgqrHISVSTAGHVPgIRRFAKDFPQCNL-AVSLHAAEDALRSDL--VPLNRTYplsQLAKALKDyit 245
Cdd:COG1180    94 LAKLAKE---LGL---HTALDTNGYIP-EEALEELLPYLDAvNIDLKAFDDEFYRKLtgVSLEPVL---ENLELLAE--- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 246 stkRRVFIE--YVLFEGINNSRTQVARLNAWLRTVAAPKyfVVNIIPYNRTG--SPYKAPTRDRIKLFGELLEAAGIE-V 320
Cdd:COG1180   161 ---SGVHVEirTLVIPGLNDSEEELEAIARFIAELGDVI--PVHLLPFHPLYklEDVPPPSPETLERAREIAREYGLKyV 235

                  ....*..
gi 1085021386 321 TIRKSMG 327
Cdd:COG1180   236 YIGNVPG 242
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
106-221 4.82e-04

Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, chromosome partitioning, Coenzyme transport and metabolism];


Pssm-ID: 440301 [Multi-domain]  Cd Length: 159  Bit Score: 40.27  E-value: 4.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 106 CPVRCPFC-ATGKKGLKRNLSPDEItDQYLAAAHylktkdEQKIGSVIFMGmGEPFLNYDsVAEAVRTIADpelIGLgqr 184
Cdd:COG0535    10 CNLRCKHCyADAGPKRPGELSTEEA-KRILDELA------ELGVKVVGLTG-GEPLLRPD-LFELVEYAKE---LGI--- 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1085021386 185 HISVSTAGHvpGI-RRFAKDFPQCNL---AVSLHAAE----DALR 221
Cdd:COG0535    75 RVNLSTNGT--LLtEELAERLAEAGLdhvTISLDGVDpethDKIR 117
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
105-195 5.45e-03

Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic radical activating enzyme NrdG/QueE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440367 [Multi-domain]  Cd Length: 205  Bit Score: 37.42  E-value: 5.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085021386 105 GCPVRCPFCAT-----GKKGlkRNLSPDEITDQYLAAAHYlktkdeqkigSVIFMGmGEPFLnYDSVAEAVRtiadpELI 179
Cdd:COG0602    29 GCNLRCSWCDTkyawdGEGG--KRMSAEEILEEVAALGAR----------HVVITG-GEPLL-QDDLAELLE-----ALK 89
                          90
                  ....*....|....*.
gi 1085021386 180 GLGqRHISVSTAGHVP 195
Cdd:COG0602    90 DAG-YEVALETNGTLP 104
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH