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Conserved domains on  [gi|999186210|emb|CZP45146|]
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Ribosomal RNA large subunit methyltransferase N [Legionella pneumophila]

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 ...
8-349 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: 613.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210   8 LLNYNYSQLRELLIGWDEKPFRAQQLFQWIHQVGIRDFAQMTNLGKVLRNKLSQLACIDLPEIVACQKSADGTHKWLLKL 87
Cdd:COG0820    1 LLGLTLEELEEFLAELGEKPFRAKQIFRWLYQKGVTDFDEMTNLPKALREKLAENFEIGLLEVVREQVSADGTRKYLFRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210  88 ECGNCIETVFIPEANRGTLCVSSQVGCALNCSFCSTAKQGFNRNLSTAEIIGQVWLAARELsdnnGTHDKKITNVVMMGM 167
Cdd:COG0820   81 ADGNLVETVLIPYEDRGTLCVSSQVGCAMGCSFCATGKQGLVRNLTAGEIVGQVLLARRDL----REGGRRVTNIVFMGM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210 168 GEPLLNFDNVVSAMNIMMDDLAYGLSKRRVTLSTSGVLPEMERL-REVSPVALAVSLHAPTDELRNELVPINKKYPLSQL 246
Cdd:COG0820  157 GEPLLNYDNVLKAIRILNDPEGLGISARRITVSTSGLVPGIRRLaDEGLPVNLAVSLHAPNDELRDELMPINKKYPLEEL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210 247 ISLCKRYFKDEPRRkVTFEYVMLKGVNDQPEHASQLIKLLHNVPAKVNLIPFNPFPLTQYQRSSRETIDAFRDKLMKHGI 326
Cdd:COG0820  237 LEACRRYPEKTGRR-ITFEYVLLKGVNDSPEDARELARLLKGLPCKVNLIPFNPVPGSPYKRPSPERIEAFADILEKAGI 315
                        330       340
                 ....*....|....*....|...
gi 999186210 327 NTITRKTRGDDIDAACGQLAGEV 349
Cdd:COG0820  316 PVTVRRSRGDDIDAACGQLRAKV 338
 
Name Accession Description Interval E-value
RlmN COG0820
Adenine C2-methylase RlmN of 23S rRNA A2503 and tRNA A37 [Translation, ribosomal structure and ...
8-349 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: 613.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210   8 LLNYNYSQLRELLIGWDEKPFRAQQLFQWIHQVGIRDFAQMTNLGKVLRNKLSQLACIDLPEIVACQKSADGTHKWLLKL 87
Cdd:COG0820    1 LLGLTLEELEEFLAELGEKPFRAKQIFRWLYQKGVTDFDEMTNLPKALREKLAENFEIGLLEVVREQVSADGTRKYLFRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210  88 ECGNCIETVFIPEANRGTLCVSSQVGCALNCSFCSTAKQGFNRNLSTAEIIGQVWLAARELsdnnGTHDKKITNVVMMGM 167
Cdd:COG0820   81 ADGNLVETVLIPYEDRGTLCVSSQVGCAMGCSFCATGKQGLVRNLTAGEIVGQVLLARRDL----REGGRRVTNIVFMGM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210 168 GEPLLNFDNVVSAMNIMMDDLAYGLSKRRVTLSTSGVLPEMERL-REVSPVALAVSLHAPTDELRNELVPINKKYPLSQL 246
Cdd:COG0820  157 GEPLLNYDNVLKAIRILNDPEGLGISARRITVSTSGLVPGIRRLaDEGLPVNLAVSLHAPNDELRDELMPINKKYPLEEL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210 247 ISLCKRYFKDEPRRkVTFEYVMLKGVNDQPEHASQLIKLLHNVPAKVNLIPFNPFPLTQYQRSSRETIDAFRDKLMKHGI 326
Cdd:COG0820  237 LEACRRYPEKTGRR-ITFEYVLLKGVNDSPEDARELARLLKGLPCKVNLIPFNPVPGSPYKRPSPERIEAFADILEKAGI 315
                        330       340
                 ....*....|....*....|...
gi 999186210 327 NTITRKTRGDDIDAACGQLAGEV 349
Cdd:COG0820  316 PVTVRRSRGDDIDAACGQLRAKV 338
PRK11194 PRK11194
ribosomal RNA large subunit methyltransferase N; Provisional
1-361 0e+00

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 183031  Cd Length: 372  Bit Score: 545.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210   1 MDQQKVNLLNYNYSQLRELLIGWDEKPFRAQQLFQWIHQVGIRDFAQMTNLGKVLRNKLSQLACIDLPEIVACQKSADGT 80
Cdd:PRK11194   1 MKEKKINLLDLNRQQMREFFAELGEKPFRADQVMKWIYHYGCDDFDEMTNINKVLREKLKEVAEIRAPEVAEEQRSSDGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210  81 HKWLLKLEcGNCIETVFIPEANRGTLCVSSQVGCALNCSFCSTAKQGFNRNLSTAEIIGQVWLAARELSDNNGTHDKKIT 160
Cdd:PRK11194  81 IKWAIAVG-DQRVETVYIPEDDRATLCVSSQVGCALECKFCSTAQQGFNRNLRVSEIIGQVWRAAKIIGAAKVTGQRPIT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210 161 NVVMMGMGEPLLNFDNVVSAMNIMMDDLAYGLSKRRVTLSTSGVLPEMERLREVSPVALAVSLHAPTDELRNELVPINKK 240
Cdd:PRK11194 160 NVVMMGMGEPLLNLNNVVPAMEIMLDDFGFGLSKRRVTLSTSGVVPALDKLGDMIDVALAISLHAPNDELRDEIVPINKK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210 241 YPLSQLISLCKRYF--KDEPRRKVTFEYVMLKGVNDQPEHASQLIKLLHNVPAKVNLIPFNPFPLTQYQRSSRETIDAFR 318
Cdd:PRK11194 240 YNIETFLAAVRRYLekSNANQGRVTVEYVMLDHVNDGTEHAHQLAELLKDTPCKINLIPWNPFPGAPYGRSSNSRIDRFS 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 999186210 319 DKLMKHGINTITRKTRGDDIDAACGQLAGEVKDKTSRSQRWQK 361
Cdd:PRK11194 320 KVLMEYGFTVIVRKTRGDDIDAACGQLAGDVIDRTKRTLKKRM 362
rRNA_mod_RlmN TIGR00048
23S rRNA (adenine(2503)-C(2))-methyltransferase; Members of this family are RlmN, a 23S rRNA ...
5-356 8.23e-166

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: 467.76  E-value: 8.23e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210    5 KVNLLNYNYSQLRELLIGWDEKPFRAQQLFQWIHQVGIRDFAQMTNLGKVLRNKLSQLACIDLPEIVACQKSADGTHKWL 84
Cdd:TIGR00048   6 KPSLLDLTLQELRQWLKDLGEKPFRAKQIMKWLYHKGCDSFDDMTNLSKVLREKLNEVFEIRTPEIAHEQRSSDGTIKYL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210   85 LKLECGNCIETVFIPEANRGTLCVSSQVGCALNCSFCSTAKQGFNRNLSTAEIIGQVWLAARelsDNNGTHDkKITNVVM 164
Cdd:TIGR00048  86 FALGDGQTIETVLIPEDDRATVCVSSQVGCALGCTFCATAKGGFNRNLEASEIIGQVLRVQK---IVGETGE-RVSNVVF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210  165 MGMGEPLLNFDNVVSAMNIMMDDLAYGLSKRRVTLSTSGVLPEMERLREVS-PVALAVSLHAPTDELRNELVPINKKYPL 243
Cdd:TIGR00048 162 MGMGEPLLNLNEVVKAMEIMNDDFGFGISKRRITISTSGVVPKIDKLADKMlQVALAISLHAPNDEIRSSLMPINKKYNI 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210  244 SQLISLCKRYFkDEPRRKVTFEYVMLKGVNDQPEHASQLIKLLHNVPAKVNLIPFNPFPLTQYQRSSRETIDAFRDKLMK 323
Cdd:TIGR00048 242 ETLLAAVRRYL-EKTGRRVTFEYVLLDGVNDQVEHAEELAELLKGTKCKVNLIPWNPFPEADYGRPSNSQIDRFAKVLMS 320
                         330       340       350
                  ....*....|....*....|....*....|....
gi 999186210  324 HGINTITRKTRGDDIDAACGQL-AGEVKDKTSRS 356
Cdd:TIGR00048 321 YGFTVTIRKSRGDDIDAACGQLrAKDVIDRTKRT 354
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
111-275 1.52e-18

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: 81.80  E-value: 1.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210  111 QVGCALNCSFCSTAKQGFN---RNLSTAEIIGQVWLAARelsdnngthdkKITNVVMMGMGEPLLNFDNVVSAMNIMMDD 187
Cdd:pfam04055   2 TRGCNLRCTYCAFPSIRARgkgRELSPEEILEEAKELKR-----------LGVEVVILGGGEPLLLPDLVELLERLLKLE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210  188 LAYGlskRRVTLSTSGVLPE---MERLREVSPVALAVSLHAPTDELRNelvPINKKYPLSQLISLCKRyFKDEPRRKVTF 264
Cdd:pfam04055  71 LAEG---IRITLETNGTLLDeelLELLKEAGLDRVSIGLESGDDEVLK---LINRGHTFEEVLEALEL-LREAGIPVVTD 143
                         170
                  ....*....|.
gi 999186210  265 EYVMLKGVNDQ 275
Cdd:pfam04055 144 NIVGLPGETDE 154
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
113-313 8.48e-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: 60.81  E-value: 8.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210 113 GCALNCSFCSTAKQGFNRNLSTAEIIGQVwLAARELSdnngthdKKITNVVMMGMGEPLLNFDNvvsaMNIMMdDLAYGL 192
Cdd:cd01335    6 GCNLNCGFCSNPASKGRGPESPPEIEEIL-DIVLEAK-------ERGVEVVILTGGEPLLYPEL----AELLR-RLKKEL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210 193 SKRRVTLSTSGVLPE---MERLREVSPVALAVSLHAPTDELRNELvpINKKYPLSQLISLCKRyfKDEPRRKVTFEYVML 269
Cdd:cd01335   73 PGFEISIETNGTLLTeelLKELKELGLDGVGVSLDSGDEEVADKI--RGSGESFKERLEALKE--LREAGLGLSTTLLVG 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 999186210 270 KGVNDQPEHAsQLIKLLHNV--PAKVNLIPFNPFPLTQYQRSSRET 313
Cdd:cd01335  149 LGDEDEEDDL-EELELLAEFrsPDRVSLFRLLPEEGTPLELAAPVV 193
 
Name Accession Description Interval E-value
RlmN COG0820
Adenine C2-methylase RlmN of 23S rRNA A2503 and tRNA A37 [Translation, ribosomal structure and ...
8-349 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: 613.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210   8 LLNYNYSQLRELLIGWDEKPFRAQQLFQWIHQVGIRDFAQMTNLGKVLRNKLSQLACIDLPEIVACQKSADGTHKWLLKL 87
Cdd:COG0820    1 LLGLTLEELEEFLAELGEKPFRAKQIFRWLYQKGVTDFDEMTNLPKALREKLAENFEIGLLEVVREQVSADGTRKYLFRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210  88 ECGNCIETVFIPEANRGTLCVSSQVGCALNCSFCSTAKQGFNRNLSTAEIIGQVWLAARELsdnnGTHDKKITNVVMMGM 167
Cdd:COG0820   81 ADGNLVETVLIPYEDRGTLCVSSQVGCAMGCSFCATGKQGLVRNLTAGEIVGQVLLARRDL----REGGRRVTNIVFMGM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210 168 GEPLLNFDNVVSAMNIMMDDLAYGLSKRRVTLSTSGVLPEMERL-REVSPVALAVSLHAPTDELRNELVPINKKYPLSQL 246
Cdd:COG0820  157 GEPLLNYDNVLKAIRILNDPEGLGISARRITVSTSGLVPGIRRLaDEGLPVNLAVSLHAPNDELRDELMPINKKYPLEEL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210 247 ISLCKRYFKDEPRRkVTFEYVMLKGVNDQPEHASQLIKLLHNVPAKVNLIPFNPFPLTQYQRSSRETIDAFRDKLMKHGI 326
Cdd:COG0820  237 LEACRRYPEKTGRR-ITFEYVLLKGVNDSPEDARELARLLKGLPCKVNLIPFNPVPGSPYKRPSPERIEAFADILEKAGI 315
                        330       340
                 ....*....|....*....|...
gi 999186210 327 NTITRKTRGDDIDAACGQLAGEV 349
Cdd:COG0820  316 PVTVRRSRGDDIDAACGQLRAKV 338
PRK11194 PRK11194
ribosomal RNA large subunit methyltransferase N; Provisional
1-361 0e+00

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 183031  Cd Length: 372  Bit Score: 545.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210   1 MDQQKVNLLNYNYSQLRELLIGWDEKPFRAQQLFQWIHQVGIRDFAQMTNLGKVLRNKLSQLACIDLPEIVACQKSADGT 80
Cdd:PRK11194   1 MKEKKINLLDLNRQQMREFFAELGEKPFRADQVMKWIYHYGCDDFDEMTNINKVLREKLKEVAEIRAPEVAEEQRSSDGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210  81 HKWLLKLEcGNCIETVFIPEANRGTLCVSSQVGCALNCSFCSTAKQGFNRNLSTAEIIGQVWLAARELSDNNGTHDKKIT 160
Cdd:PRK11194  81 IKWAIAVG-DQRVETVYIPEDDRATLCVSSQVGCALECKFCSTAQQGFNRNLRVSEIIGQVWRAAKIIGAAKVTGQRPIT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210 161 NVVMMGMGEPLLNFDNVVSAMNIMMDDLAYGLSKRRVTLSTSGVLPEMERLREVSPVALAVSLHAPTDELRNELVPINKK 240
Cdd:PRK11194 160 NVVMMGMGEPLLNLNNVVPAMEIMLDDFGFGLSKRRVTLSTSGVVPALDKLGDMIDVALAISLHAPNDELRDEIVPINKK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210 241 YPLSQLISLCKRYF--KDEPRRKVTFEYVMLKGVNDQPEHASQLIKLLHNVPAKVNLIPFNPFPLTQYQRSSRETIDAFR 318
Cdd:PRK11194 240 YNIETFLAAVRRYLekSNANQGRVTVEYVMLDHVNDGTEHAHQLAELLKDTPCKINLIPWNPFPGAPYGRSSNSRIDRFS 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 999186210 319 DKLMKHGINTITRKTRGDDIDAACGQLAGEVKDKTSRSQRWQK 361
Cdd:PRK11194 320 KVLMEYGFTVIVRKTRGDDIDAACGQLAGDVIDRTKRTLKKRM 362
rRNA_mod_RlmN TIGR00048
23S rRNA (adenine(2503)-C(2))-methyltransferase; Members of this family are RlmN, a 23S rRNA ...
5-356 8.23e-166

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: 467.76  E-value: 8.23e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210    5 KVNLLNYNYSQLRELLIGWDEKPFRAQQLFQWIHQVGIRDFAQMTNLGKVLRNKLSQLACIDLPEIVACQKSADGTHKWL 84
Cdd:TIGR00048   6 KPSLLDLTLQELRQWLKDLGEKPFRAKQIMKWLYHKGCDSFDDMTNLSKVLREKLNEVFEIRTPEIAHEQRSSDGTIKYL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210   85 LKLECGNCIETVFIPEANRGTLCVSSQVGCALNCSFCSTAKQGFNRNLSTAEIIGQVWLAARelsDNNGTHDkKITNVVM 164
Cdd:TIGR00048  86 FALGDGQTIETVLIPEDDRATVCVSSQVGCALGCTFCATAKGGFNRNLEASEIIGQVLRVQK---IVGETGE-RVSNVVF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210  165 MGMGEPLLNFDNVVSAMNIMMDDLAYGLSKRRVTLSTSGVLPEMERLREVS-PVALAVSLHAPTDELRNELVPINKKYPL 243
Cdd:TIGR00048 162 MGMGEPLLNLNEVVKAMEIMNDDFGFGISKRRITISTSGVVPKIDKLADKMlQVALAISLHAPNDEIRSSLMPINKKYNI 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210  244 SQLISLCKRYFkDEPRRKVTFEYVMLKGVNDQPEHASQLIKLLHNVPAKVNLIPFNPFPLTQYQRSSRETIDAFRDKLMK 323
Cdd:TIGR00048 242 ETLLAAVRRYL-EKTGRRVTFEYVLLDGVNDQVEHAEELAELLKGTKCKVNLIPWNPFPEADYGRPSNSQIDRFAKVLMS 320
                         330       340       350
                  ....*....|....*....|....*....|....
gi 999186210  324 HGINTITRKTRGDDIDAACGQL-AGEVKDKTSRS 356
Cdd:TIGR00048 321 YGFTVTIRKSRGDDIDAACGQLrAKDVIDRTKRT 354
PRK14461 PRK14461
ribosomal RNA large subunit methyltransferase N; Provisional
7-349 1.07e-97

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 237718  Cd Length: 371  Bit Score: 295.26  E-value: 1.07e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210   7 NLLNYNYSQLRELLIGWDEKPFRAQQLFQWIHQVGIRDFAQMTNLGKVLRNKLSQLACIDLPEIVACQKSADG-THKWLL 85
Cdd:PRK14461   9 NLYDLNLAELTELLTAWGQPAFRARQLYRHLYVNLADSVLAMTDLPLALRERLTAELPLSTLRLEQVQIGDNGlTRKALF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210  86 KLECGNCIETVFIPEANRGTLCVSSQVGCALNCSFCSTAKQGFNRNLSTAEIIGQVWLAARELSDNNGTHDK-------K 158
Cdd:PRK14461  89 RLPDGAVVETVLMIYPDRATVCVSTQAGCGMGCVFCATGTLGLLRNLSSGEIVAQVIWASRELRAMGAAISKrhagpvgR 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210 159 ITNVVMMGMGEPLLNFDNVVSAMNIMMDDLAYGLSKRRVTLSTSGVLPEMERL-REVSPVALAVSLHAPTDELRNELVPI 237
Cdd:PRK14461 169 VTNLVFMGMGEPFANYDRWWQAVERLHDPQGFNLGARSMTVSTVGLVKGIRRLaNERLPINLAISLHAPDDALRSELMPV 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210 238 NKKYPLSQLISlCKRYFKDEPRRKVTFEYVMLKGVNDQPEHASQLIKLLHNVPAK------VNLIPFNPFPLTQYQRSSR 311
Cdd:PRK14461 249 NRRYPIADLMA-ATRDYIAKTRRRVSFEYVLLQGKNDHPEQAAALARLLRGEAPPgpllvhVNLIPWNPVPGTPLGRSER 327
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 999186210 312 ETIDAFRDKLMKHGINTITRKTRGDDIDAACGQLAGEV 349
Cdd:PRK14461 328 ERVTTFQRILTDYGIPCTVRVERGVEIAAACGQLAGRH 365
PRK14453 PRK14453
chloramphenicol/florfenicol resistance protein; Provisional
13-348 6.78e-74

chloramphenicol/florfenicol resistance protein; Provisional


Pssm-ID: 184685  Cd Length: 347  Bit Score: 233.48  E-value: 6.78e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210  13 YSQLRELLIGWDEKPFRAQQLFQWIHQVGIRDFAQMTNLGKVLRNKL-----SQLACIdlpEIVACQKSADGThKWLLKL 87
Cdd:PRK14453   7 YGKMKQILSNLKLPDYRYEQITKAIFKQRIDNFEDMHILPKALRESLinefgKNVLSV---IPVFEQDSKQVT-KVLFEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210  88 ECGNCIETVFIP-EANRGTLCVSSQVGCALNCSFCSTAKQGFNRNLSTAEIIGQVwLAARelsdnngTHDKKITNVVMMG 166
Cdd:PRK14453  83 TDGERIEAVGLKyKQGWESFCISSQCGCGFGCRFCATGSIGLKRNLTADEITDQL-LYFY-------LNGHRLDSISFMG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210 167 MGEPLLNfDNVVSAMNIMMDDLAYGLSKRRVTLSTSGVLPEMERL-REVSPVALAVSLHAPTDELRNELVPINKKYPLSQ 245
Cdd:PRK14453 155 MGEALAN-PELFDALKILTDPNLFGLSQRRITISTIGIIPGIQRLtQEFPQVNLTFSLHSPFESQRSELMPINKRFPLNE 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210 246 LISLCKRYFKdEPRRKVTFEYVMLKGVNDQPEHASQLIKLLHNVPA-----KVNLIPFNPFPLT--QYQRSSRETIDAFR 318
Cdd:PRK14453 234 VMKTLDEHIR-HTGRKVYIAYIMLEGVNDSKEHAEAVVGLLRNRGSwehlyHVNLIPYNSTDKTpfKFQSSSAGQIKQFC 312
                        330       340       350
                 ....*....|....*....|....*....|
gi 999186210 319 DKLMKHGINTITRKTRGDDIDAACGQLAGE 348
Cdd:PRK14453 313 STLKSAGISVTVRTQFGSDISAACGQLYGN 342
PRK14470 PRK14470
ribosomal RNA large subunit methyltransferase N; Provisional
46-346 2.21e-65

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 172945  Cd Length: 336  Bit Score: 211.33  E-value: 2.21e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210  46 AQMTNLGKVLRNKLSQL-ACIDLPE--IVACQKSADGTHKWLLKLECGNCIETVFIPEAN-RGTLCVSSQVGCALNCSFC 121
Cdd:PRK14470  35 APLRSARNVRRSVLDEVdALATPGElrLVERVDAKDGFRKYLFELPDGLRVEAVRIPLFDtHHVVCLSSQAGCALGCAFC 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210 122 STAKQGFNRNLSTAEIIGQVwLAARELSdnngthDKKITNVVMMGMGEPLLNFDNVVSAMNIMMDDLAYGLSKRRVTLST 201
Cdd:PRK14470 115 ATGKLGLDRSLRSWEIVAQL-LAVRADS------ERPITGVVFMGQGEPFLNYDEVLRAAYALCDPAGARIDGRRISIST 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210 202 SGVLPEMER-LREVSPVALAVSLHAPTDELRNELVPINKKYPLSQLISLCKRYfkDEPRRKVTFEYVMLKGVNDQPEHAS 280
Cdd:PRK14470 188 AGVVPMIRRyTAEGHKFRLCISLNAAIPWKRRALMPIEQGFPLDELVEAIREH--AALRGRVTLEYVMISGVNVGEEDAA 265
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 999186210 281 QLIKLLHNVPAKVNLIPFNPfPLTQYQRSSRETIDAFRDKLMKH--GINTITRKTRGDDIDAACGQLA 346
Cdd:PRK14470 266 ALGRLLAGIPVRLNPIAVND-ATGRYRPPDEDEWNAFRDALARElpGTPVVRRYSGGQDEHAACGMLA 332
PRK14464 PRK14464
RNA methyltransferase;
77-358 1.62e-57

RNA methyltransferase;


Pssm-ID: 184691  Cd Length: 344  Bit Score: 191.09  E-value: 1.62e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210  77 ADGTHKWLLKLECGNCIETVFIPeanRGTLCVSSQVGCALNCSFCSTAKQGFNRNLSTAEIIGQVWLAARElsdnngthd 156
Cdd:PRK14464  72 EDGSARLLVELADGQMVESVLLP---RDGLCVSTQVGCAVGCVFCMTGRSGLLRQLGSAEIVAQVVLARRR--------- 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210 157 KKITNVVMMGMGEPLLNFDNVVSAMNIMmdDLAYGLSKRRVTLSTSGVLPEMERL--REVSPvALAVSLHAPTDELRNEL 234
Cdd:PRK14464 140 RAVKKVVFMGMGEPAHNLDNVLEAIDLL--GTEGGIGHKNLVFSTVGDPRVFERLpqQRVKP-ALALSLHTTRAELRARL 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210 235 VPINKKYPLSQLISLCKRYFK--DEPrrkVTFEYVMLKGVNDQPEHASQLIKLLHNVPAKVNLIPFNPFPLTQYQRSSRE 312
Cdd:PRK14464 217 LPRAPRIAPEELVELGEAYARatGYP---IQYQWTLLEGVNDSDEEMDGIVRLLKGKYAVMNLIPYNSVDGDAYRRPSGE 293
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 999186210 313 TIDAFRDKLMKHGINTITRKTRGDDIDAACGQL-AGEVKDKTSRSQR 358
Cdd:PRK14464 294 RIVAMARYLHRRGVLTKVRNSAGQDVDGGCGQLrARAAKAAAVRRIR 340
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
111-275 1.52e-18

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: 81.80  E-value: 1.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210  111 QVGCALNCSFCSTAKQGFN---RNLSTAEIIGQVWLAARelsdnngthdkKITNVVMMGMGEPLLNFDNVVSAMNIMMDD 187
Cdd:pfam04055   2 TRGCNLRCTYCAFPSIRARgkgRELSPEEILEEAKELKR-----------LGVEVVILGGGEPLLLPDLVELLERLLKLE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210  188 LAYGlskRRVTLSTSGVLPE---MERLREVSPVALAVSLHAPTDELRNelvPINKKYPLSQLISLCKRyFKDEPRRKVTF 264
Cdd:pfam04055  71 LAEG---IRITLETNGTLLDeelLELLKEAGLDRVSIGLESGDDEVLK---LINRGHTFEEVLEALEL-LREAGIPVVTD 143
                         170
                  ....*....|.
gi 999186210  265 EYVMLKGVNDQ 275
Cdd:pfam04055 144 NIVGLPGETDE 154
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
113-313 8.48e-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: 60.81  E-value: 8.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210 113 GCALNCSFCSTAKQGFNRNLSTAEIIGQVwLAARELSdnngthdKKITNVVMMGMGEPLLNFDNvvsaMNIMMdDLAYGL 192
Cdd:cd01335    6 GCNLNCGFCSNPASKGRGPESPPEIEEIL-DIVLEAK-------ERGVEVVILTGGEPLLYPEL----AELLR-RLKKEL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210 193 SKRRVTLSTSGVLPE---MERLREVSPVALAVSLHAPTDELRNELvpINKKYPLSQLISLCKRyfKDEPRRKVTFEYVML 269
Cdd:cd01335   73 PGFEISIETNGTLLTeelLKELKELGLDGVGVSLDSGDEEVADKI--RGSGESFKERLEALKE--LREAGLGLSTTLLVG 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 999186210 270 KGVNDQPEHAsQLIKLLHNV--PAKVNLIPFNPFPLTQYQRSSRET 313
Cdd:cd01335  149 LGDEDEEDDL-EELELLAEFrsPDRVSLFRLLPEEGTPLELAAPVV 193
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
114-330 3.90e-07

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: 50.58  E-value: 3.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210 114 CALNCSFCstakQ-GFNRNL--------STAEIIGQVwlaaRELSDNNGTHDKKITNVVMMGMGEPLLNfdnvvsamnIM 184
Cdd:COG0731   34 CNFDCVYC----QrGRTTDLtrerrefdDPEEILEEL----IEFLRKLPEEAREPDHITFSGSGEPTLY---------PN 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210 185 MDDLAYGLSKRR------VT----LSTSGVLPEMERLREVSPvalavSLHAPTDELRNELVPINKKYPLSQLI-SLCKry 253
Cdd:COG0731   97 LGELIEEIKKLRgiktalLTngslLHRPEVREELLKADQVYP-----SLDAADEETFRKINRPHPGLSWERIIeGLEL-- 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 999186210 254 FKDEPRRKVTFEYVMLKGVNDQPEHASQLIKLLHNV-PAKVNL-IPFNPFPLTQYQRSSRETIDAFRDKLMKHGINTIT 330
Cdd:COG0731  170 FRKLYKGRTVIETMLVKGINDSEEELEAYAELIKRInPDFVELkTYMRPPALSRVNMPSHEELEEFAERLAELGYEVVS 248
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
114-229 1.25e-05

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: 44.89  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999186210 114 CALNCSFC-STAKQGFNRNLSTAEIIGqvwlAARELSDNNgthdkkiTNVVMMGMGEPLLNFDnvvsamniMMDDLAYGL 192
Cdd:COG0535   10 CNLRCKHCyADAGPKRPGELSTEEAKR----ILDELAELG-------VKVVGLTGGEPLLRPD--------LFELVEYAK 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 999186210 193 SKR-RVTLSTSGVL--PEM-ERLREVSPVALAVSLHAPTDE 229
Cdd:COG0535   71 ELGiRVNLSTNGTLltEELaERLAEAGLDHVTISLDGVDPE 111
 
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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