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Conserved domains on  [gi|488615634|ref|WP_002552483|]
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MULTISPECIES: 23S rRNA (adenine(2503)-C(2))-methyltransferase RlmN [Pseudomonas]

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 ...
10-352 0e+00

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


:

Pssm-ID: 440582  Cd Length: 338  Bit Score: 600.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634  10 LLGLTQQEMEKFFDSIGEKRFRAGQVMKWIHHFGVDDFDAMTNVSKALREKLKACAEVRGPEVVSEDISSDGTRKWVVRV 89
Cdd:COG0820    1 LLGLTLEELEEFLAELGEKPFRAKQIFRWLYQKGVTDFDEMTNLPKALREKLAENFEIGLLEVVREQVSADGTRKYLFRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634  90 ESGSCVETVYIPQGKRGTLCVSSQAGCALDCSFCSTGKQGFNSNLTAAEVIGQVWIANKSFGSvpatVDRAITNVVMMGM 169
Cdd:COG0820   81 ADGNLVETVLIPYEDRGTLCVSSQVGCAMGCSFCATGKQGLVRNLTAGEIVGQVLLARRDLRE----GGRRVTNIVFMGM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 170 GEPLLNFDNVIAAMHLMMDDLGYGISKRRVTLSTSGVVPMIDELSKH-IDVSLALSLHAPNDALRNQLVPINKKYPLQML 248
Cdd:COG0820  157 GEPLLNYDNVLKAIRILNDPEGLGISARRITVSTSGLVPGIRRLADEgLPVNLAVSLHAPNDELRDELMPINKKYPLEEL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 249 LDSCRRYMSSLGeKRVlTIEYTMLKDINDKVEHAVEMIELLKDTPCKINLIPFNPFPHSGYERPSNNAIRRFQDLLHQAG 328
Cdd:COG0820  237 LEACRRYPEKTG-RRI-TFEYVLLKGVNDSPEDARELARLLKGLPCKVNLIPFNPVPGSPYKRPSPERIEAFADILEKAG 314
                        330       340
                 ....*....|....*....|....
gi 488615634 329 YNVTVRTTRGEDIDAACGQLVGQV 352
Cdd:COG0820  315 IPVTVRRSRGDDIDAACGQLRAKV 338
 
Name Accession Description Interval E-value
RlmN COG0820
Adenine C2-methylase RlmN of 23S rRNA A2503 and tRNA A37 [Translation, ribosomal structure and ...
10-352 0e+00

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


Pssm-ID: 440582  Cd Length: 338  Bit Score: 600.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634  10 LLGLTQQEMEKFFDSIGEKRFRAGQVMKWIHHFGVDDFDAMTNVSKALREKLKACAEVRGPEVVSEDISSDGTRKWVVRV 89
Cdd:COG0820    1 LLGLTLEELEEFLAELGEKPFRAKQIFRWLYQKGVTDFDEMTNLPKALREKLAENFEIGLLEVVREQVSADGTRKYLFRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634  90 ESGSCVETVYIPQGKRGTLCVSSQAGCALDCSFCSTGKQGFNSNLTAAEVIGQVWIANKSFGSvpatVDRAITNVVMMGM 169
Cdd:COG0820   81 ADGNLVETVLIPYEDRGTLCVSSQVGCAMGCSFCATGKQGLVRNLTAGEIVGQVLLARRDLRE----GGRRVTNIVFMGM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 170 GEPLLNFDNVIAAMHLMMDDLGYGISKRRVTLSTSGVVPMIDELSKH-IDVSLALSLHAPNDALRNQLVPINKKYPLQML 248
Cdd:COG0820  157 GEPLLNYDNVLKAIRILNDPEGLGISARRITVSTSGLVPGIRRLADEgLPVNLAVSLHAPNDELRDELMPINKKYPLEEL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 249 LDSCRRYMSSLGeKRVlTIEYTMLKDINDKVEHAVEMIELLKDTPCKINLIPFNPFPHSGYERPSNNAIRRFQDLLHQAG 328
Cdd:COG0820  237 LEACRRYPEKTG-RRI-TFEYVLLKGVNDSPEDARELARLLKGLPCKVNLIPFNPVPGSPYKRPSPERIEAFADILEKAG 314
                        330       340
                 ....*....|....*....|....
gi 488615634 329 YNVTVRTTRGEDIDAACGQLVGQV 352
Cdd:COG0820  315 IPVTVRRSRGDDIDAACGQLRAKV 338
PRK11194 PRK11194
ribosomal RNA large subunit methyltransferase N; Provisional
3-359 0e+00

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 183031  Cd Length: 372  Bit Score: 592.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634   3 ASTGKTNLLGLTQQEMEKFFDSIGEKRFRAGQVMKWIHHFGVDDFDAMTNVSKALREKLKACAEVRGPEVVSEDISSDGT 82
Cdd:PRK11194   1 MKEKKINLLDLNRQQMREFFAELGEKPFRADQVMKWIYHYGCDDFDEMTNINKVLREKLKEVAEIRAPEVAEEQRSSDGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634  83 RKWVVRVEsGSCVETVYIPQGKRGTLCVSSQAGCALDCSFCSTGKQGFNSNLTAAEVIGQVWIANKSFGSVPATVDRAIT 162
Cdd:PRK11194  81 IKWAIAVG-DQRVETVYIPEDDRATLCVSSQVGCALECKFCSTAQQGFNRNLRVSEIIGQVWRAAKIIGAAKVTGQRPIT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 163 NVVMMGMGEPLLNFDNVIAAMHLMMDDLGYGISKRRVTLSTSGVVPMIDELSKHIDVSLALSLHAPNDALRNQLVPINKK 242
Cdd:PRK11194 160 NVVMMGMGEPLLNLNNVVPAMEIMLDDFGFGLSKRRVTLSTSGVVPALDKLGDMIDVALAISLHAPNDELRDEIVPINKK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 243 YPLQMLLDSCRRYM--SSLGEKRVlTIEYTMLKDINDKVEHAVEMIELLKDTPCKINLIPFNPFPHSGYERPSNNAIRRF 320
Cdd:PRK11194 240 YNIETFLAAVRRYLekSNANQGRV-TVEYVMLDHVNDGTEHAHQLAELLKDTPCKINLIPWNPFPGAPYGRSSNSRIDRF 318
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 488615634 321 QDLLHQAGYNVTVRTTRGEDIDAACGQLVGQVMDRTRRS 359
Cdd:PRK11194 319 SKVLMEYGFTVIVRKTRGDDIDAACGQLAGDVIDRTKRT 357
rRNA_mod_RlmN TIGR00048
23S rRNA (adenine(2503)-C(2))-methyltransferase; Members of this family are RlmN, a 23S rRNA ...
3-359 1.39e-172

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: 485.09  E-value: 1.39e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634    3 ASTGKTNLLGLTQQEMEKFFDSIGEKRFRAGQVMKWIHHFGVDDFDAMTNVSKALREKLKACAEVRGPEVVSEDISSDGT 82
Cdd:TIGR00048   2 AKDGKPSLLDLTLQELRQWLKDLGEKPFRAKQIMKWLYHKGCDSFDDMTNLSKVLREKLNEVFEIRTPEIAHEQRSSDGT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634   83 RKWVVRVESGSCVETVYIPQGKRGTLCVSSQAGCALDCSFCSTGKQGFNSNLTAAEVIGQVWIANKSFGsvpaTVDRAIT 162
Cdd:TIGR00048  82 IKYLFALGDGQTIETVLIPEDDRATVCVSSQVGCALGCTFCATAKGGFNRNLEASEIIGQVLRVQKIVG----ETGERVS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634  163 NVVMMGMGEPLLNFDNVIAAMHLMMDDLGYGISKRRVTLSTSGVVPMIDELS-KHIDVSLALSLHAPNDALRNQLVPINK 241
Cdd:TIGR00048 158 NVVFMGMGEPLLNLNEVVKAMEIMNDDFGFGISKRRITISTSGVVPKIDKLAdKMLQVALAISLHAPNDEIRSSLMPINK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634  242 KYPLQMLLDSCRRYMSSLGeKRVlTIEYTMLKDINDKVEHAVEMIELLKDTPCKINLIPFNPFPHSGYERPSNNAIRRFQ 321
Cdd:TIGR00048 238 KYNIETLLAAVRRYLEKTG-RRV-TFEYVLLDGVNDQVEHAEELAELLKGTKCKVNLIPWNPFPEADYGRPSNSQIDRFA 315
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 488615634  322 DLLHQAGYNVTVRTTRGEDIDAACGQL-VGQVMDRTRRS 359
Cdd:TIGR00048 316 KVLMSYGFTVTIRKSRGDDIDAACGQLrAKDVIDRTKRT 354
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
115-278 1.27e-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: 71.02  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634  115 GCALDCSFCSTGKQGFNSN---LTAAEVIGQVWIAnksfgsvpatvDRAITNVVMMGMGEPLLNFDNVIAAMHLMMDDLG 191
Cdd:pfam04055   4 GCNLRCTYCAFPSIRARGKgreLSPEEILEEAKEL-----------KRLGVEVVILGGGEPLLLPDLVELLERLLKLELA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634  192 YGIskrRVTLSTSGVVP---MIDELSKHIDVSLALSLHAPNDALRNqlvPINKKYPLQMLLDSCRRyMSSLGeKRVLTIE 268
Cdd:pfam04055  73 EGI---RITLETNGTLLdeeLLELLKEAGLDRVSIGLESGDDEVLK---LINRGHTFEEVLEALEL-LREAG-IPVVTDN 144
                         170
                  ....*....|
gi 488615634  269 YTMLKDINDK 278
Cdd:pfam04055 145 IVGLPGETDE 154
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
115-316 3.16e-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: 56.19  E-value: 3.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 115 GCALDCSFCSTGKQ---GFNSNLTAAEVIGQVWIANKSFGSvpatvdraitnVVMMGMGEPLLNFDNVIAAMHlmmddLG 191
Cdd:cd01335    6 GCNLNCGFCSNPASkgrGPESPPEIEEILDIVLEAKERGVE-----------VVILTGGEPLLYPELAELLRR-----LK 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 192 YGISKRRVTLSTSGVVPM---IDELSKHIDVSLALSLHAPNDALRNQLvpINKKYPLQMLLDSCRRYMSSlgeKRVLTIE 268
Cdd:cd01335   70 KELPGFEISIETNGTLLTeelLKELKELGLDGVGVSLDSGDEEVADKI--RGSGESFKERLEALKELREA---GLGLSTT 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 488615634 269 YTMLKDINDKVEHAVEMIELLK-DTPCKINLIPFNPFPHSGYERPSNNA 316
Cdd:cd01335  145 LLVGLGDEDEEDDLEELELLAEfRSPDRVSLFRLLPEEGTPLELAAPVV 193
 
Name Accession Description Interval E-value
RlmN COG0820
Adenine C2-methylase RlmN of 23S rRNA A2503 and tRNA A37 [Translation, ribosomal structure and ...
10-352 0e+00

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


Pssm-ID: 440582  Cd Length: 338  Bit Score: 600.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634  10 LLGLTQQEMEKFFDSIGEKRFRAGQVMKWIHHFGVDDFDAMTNVSKALREKLKACAEVRGPEVVSEDISSDGTRKWVVRV 89
Cdd:COG0820    1 LLGLTLEELEEFLAELGEKPFRAKQIFRWLYQKGVTDFDEMTNLPKALREKLAENFEIGLLEVVREQVSADGTRKYLFRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634  90 ESGSCVETVYIPQGKRGTLCVSSQAGCALDCSFCSTGKQGFNSNLTAAEVIGQVWIANKSFGSvpatVDRAITNVVMMGM 169
Cdd:COG0820   81 ADGNLVETVLIPYEDRGTLCVSSQVGCAMGCSFCATGKQGLVRNLTAGEIVGQVLLARRDLRE----GGRRVTNIVFMGM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 170 GEPLLNFDNVIAAMHLMMDDLGYGISKRRVTLSTSGVVPMIDELSKH-IDVSLALSLHAPNDALRNQLVPINKKYPLQML 248
Cdd:COG0820  157 GEPLLNYDNVLKAIRILNDPEGLGISARRITVSTSGLVPGIRRLADEgLPVNLAVSLHAPNDELRDELMPINKKYPLEEL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 249 LDSCRRYMSSLGeKRVlTIEYTMLKDINDKVEHAVEMIELLKDTPCKINLIPFNPFPHSGYERPSNNAIRRFQDLLHQAG 328
Cdd:COG0820  237 LEACRRYPEKTG-RRI-TFEYVLLKGVNDSPEDARELARLLKGLPCKVNLIPFNPVPGSPYKRPSPERIEAFADILEKAG 314
                        330       340
                 ....*....|....*....|....
gi 488615634 329 YNVTVRTTRGEDIDAACGQLVGQV 352
Cdd:COG0820  315 IPVTVRRSRGDDIDAACGQLRAKV 338
PRK11194 PRK11194
ribosomal RNA large subunit methyltransferase N; Provisional
3-359 0e+00

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 183031  Cd Length: 372  Bit Score: 592.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634   3 ASTGKTNLLGLTQQEMEKFFDSIGEKRFRAGQVMKWIHHFGVDDFDAMTNVSKALREKLKACAEVRGPEVVSEDISSDGT 82
Cdd:PRK11194   1 MKEKKINLLDLNRQQMREFFAELGEKPFRADQVMKWIYHYGCDDFDEMTNINKVLREKLKEVAEIRAPEVAEEQRSSDGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634  83 RKWVVRVEsGSCVETVYIPQGKRGTLCVSSQAGCALDCSFCSTGKQGFNSNLTAAEVIGQVWIANKSFGSVPATVDRAIT 162
Cdd:PRK11194  81 IKWAIAVG-DQRVETVYIPEDDRATLCVSSQVGCALECKFCSTAQQGFNRNLRVSEIIGQVWRAAKIIGAAKVTGQRPIT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 163 NVVMMGMGEPLLNFDNVIAAMHLMMDDLGYGISKRRVTLSTSGVVPMIDELSKHIDVSLALSLHAPNDALRNQLVPINKK 242
Cdd:PRK11194 160 NVVMMGMGEPLLNLNNVVPAMEIMLDDFGFGLSKRRVTLSTSGVVPALDKLGDMIDVALAISLHAPNDELRDEIVPINKK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 243 YPLQMLLDSCRRYM--SSLGEKRVlTIEYTMLKDINDKVEHAVEMIELLKDTPCKINLIPFNPFPHSGYERPSNNAIRRF 320
Cdd:PRK11194 240 YNIETFLAAVRRYLekSNANQGRV-TVEYVMLDHVNDGTEHAHQLAELLKDTPCKINLIPWNPFPGAPYGRSSNSRIDRF 318
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 488615634 321 QDLLHQAGYNVTVRTTRGEDIDAACGQLVGQVMDRTRRS 359
Cdd:PRK11194 319 SKVLMEYGFTVIVRKTRGDDIDAACGQLAGDVIDRTKRT 357
rRNA_mod_RlmN TIGR00048
23S rRNA (adenine(2503)-C(2))-methyltransferase; Members of this family are RlmN, a 23S rRNA ...
3-359 1.39e-172

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: 485.09  E-value: 1.39e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634    3 ASTGKTNLLGLTQQEMEKFFDSIGEKRFRAGQVMKWIHHFGVDDFDAMTNVSKALREKLKACAEVRGPEVVSEDISSDGT 82
Cdd:TIGR00048   2 AKDGKPSLLDLTLQELRQWLKDLGEKPFRAKQIMKWLYHKGCDSFDDMTNLSKVLREKLNEVFEIRTPEIAHEQRSSDGT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634   83 RKWVVRVESGSCVETVYIPQGKRGTLCVSSQAGCALDCSFCSTGKQGFNSNLTAAEVIGQVWIANKSFGsvpaTVDRAIT 162
Cdd:TIGR00048  82 IKYLFALGDGQTIETVLIPEDDRATVCVSSQVGCALGCTFCATAKGGFNRNLEASEIIGQVLRVQKIVG----ETGERVS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634  163 NVVMMGMGEPLLNFDNVIAAMHLMMDDLGYGISKRRVTLSTSGVVPMIDELS-KHIDVSLALSLHAPNDALRNQLVPINK 241
Cdd:TIGR00048 158 NVVFMGMGEPLLNLNEVVKAMEIMNDDFGFGISKRRITISTSGVVPKIDKLAdKMLQVALAISLHAPNDEIRSSLMPINK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634  242 KYPLQMLLDSCRRYMSSLGeKRVlTIEYTMLKDINDKVEHAVEMIELLKDTPCKINLIPFNPFPHSGYERPSNNAIRRFQ 321
Cdd:TIGR00048 238 KYNIETLLAAVRRYLEKTG-RRV-TFEYVLLDGVNDQVEHAEELAELLKGTKCKVNLIPWNPFPEADYGRPSNSQIDRFA 315
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 488615634  322 DLLHQAGYNVTVRTTRGEDIDAACGQL-VGQVMDRTRRS 359
Cdd:TIGR00048 316 KVLMSYGFTVTIRKSRGDDIDAACGQLrAKDVIDRTKRT 354
PRK14461 PRK14461
ribosomal RNA large subunit methyltransferase N; Provisional
9-352 5.01e-85

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 237718  Cd Length: 371  Bit Score: 262.90  E-value: 5.01e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634   9 NLLGLTQQEMEKFFDSIGEKRFRAGQVMKWIHHFGVDDFDAMTNVSKALREKLKACAEVRGPEVVSEDISSDG-TRKWVV 87
Cdd:PRK14461   9 NLYDLNLAELTELLTAWGQPAFRARQLYRHLYVNLADSVLAMTDLPLALRERLTAELPLSTLRLEQVQIGDNGlTRKALF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634  88 RVESGSCVETVYIPQGKRGTLCVSSQAGCALDCSFCSTGKQGFNSNLTAAEVIGQV-WIAN--KSFGSVPA-----TVDR 159
Cdd:PRK14461  89 RLPDGAVVETVLMIYPDRATVCVSTQAGCGMGCVFCATGTLGLLRNLSSGEIVAQViWASRelRAMGAAISkrhagPVGR 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 160 aITNVVMMGMGEPLLNFDNVIAAMHLMMDDLGYGISKRRVTLSTSGVVPMIDELS-KHIDVSLALSLHAPNDALRNQLVP 238
Cdd:PRK14461 169 -VTNLVFMGMGEPFANYDRWWQAVERLHDPQGFNLGARSMTVSTVGLVKGIRRLAnERLPINLAISLHAPDDALRSELMP 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 239 INKKYPLQMLLDSCRRYMSSLGekRVLTIEYTMLKDINDKVEHAVEMIELLKDTP------CKINLIPFNPFPHSGYERP 312
Cdd:PRK14461 248 VNRRYPIADLMAATRDYIAKTR--RRVSFEYVLLQGKNDHPEQAAALARLLRGEAppgpllVHVNLIPWNPVPGTPLGRS 325
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 488615634 313 SNNAIRRFQDLLHQAGYNVTVRTTRGEDIDAACGQLVGQV 352
Cdd:PRK14461 326 ERERVTTFQRILTDYGIPCTVRVERGVEIAAACGQLAGRH 365
PRK14453 PRK14453
chloramphenicol/florfenicol resistance protein; Provisional
18-351 1.59e-69

chloramphenicol/florfenicol resistance protein; Provisional


Pssm-ID: 184685  Cd Length: 347  Bit Score: 222.31  E-value: 1.59e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634  18 MEKFFDSIGEKRFRAGQVMKWIHHFGVDDFDAMTNVSKALREKLkacAEVRGPEVVS----EDISSDGTRKWVVRVESGS 93
Cdd:PRK14453  10 MKQILSNLKLPDYRYEQITKAIFKQRIDNFEDMHILPKALRESL---INEFGKNVLSvipvFEQDSKQVTKVLFELTDGE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634  94 CVETVYIpQGKRG--TLCVSSQAGCALDCSFCSTGKQGFNSNLTAAEVIGQV---WIANKSFGSVPatvdraitnvvMMG 168
Cdd:PRK14453  87 RIEAVGL-KYKQGweSFCISSQCGCGFGCRFCATGSIGLKRNLTADEITDQLlyfYLNGHRLDSIS-----------FMG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 169 MGEPLLNfDNVIAAMHLMMDDLGYGISKRRVTLSTSGVVPMIDELSKHI-DVSLALSLHAPNDALRNQLVPINKKYPLQM 247
Cdd:PRK14453 155 MGEALAN-PELFDALKILTDPNLFGLSQRRITISTIGIIPGIQRLTQEFpQVNLTFSLHSPFESQRSELMPINKRFPLNE 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 248 LLDSCRRYMSSLGEKrvLTIEYTMLKDINDKVEHAVEMIELLKDTPC-----KINLIPFNPF---PHSgYERPSNNAIRR 319
Cdd:PRK14453 234 VMKTLDEHIRHTGRK--VYIAYIMLEGVNDSKEHAEAVVGLLRNRGSwehlyHVNLIPYNSTdktPFK-FQSSSAGQIKQ 310
                        330       340       350
                 ....*....|....*....|....*....|..
gi 488615634 320 FQDLLHQAGYNVTVRTTRGEDIDAACGQLVGQ 351
Cdd:PRK14453 311 FCSTLKSAGISVTVRTQFGSDISAACGQLYGN 342
PRK14470 PRK14470
ribosomal RNA large subunit methyltransferase N; Provisional
52-348 2.18e-55

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 172945  Cd Length: 336  Bit Score: 185.13  E-value: 2.18e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634  52 NVSKALREKLKACAEVRGPEVVSEDISSDGTRKWVVRVESGSCVETVYIPQ-GKRGTLCVSSQAGCALDCSFCSTGKQGF 130
Cdd:PRK14470  42 NVRRSVLDEVDALATPGELRLVERVDAKDGFRKYLFELPDGLRVEAVRIPLfDTHHVVCLSSQAGCALGCAFCATGKLGL 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 131 NSNLTAAEVIGQVWianksfgSVPATVDRAITNVVMMGMGEPLLNFDNVIAAMHLMMDDLGYGISKRRVTLSTSGVVPMI 210
Cdd:PRK14470 122 DRSLRSWEIVAQLL-------AVRADSERPITGVVFMGQGEPFLNYDEVLRAAYALCDPAGARIDGRRISISTAGVVPMI 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 211 DELSK--HiDVSLALSLHAPNDALRNQLVPINKKYPLQMLLDSCRRYMSSLGekRVlTIEYTMLKDINDKVEHAVEMIEL 288
Cdd:PRK14470 195 RRYTAegH-KFRLCISLNAAIPWKRRALMPIEQGFPLDELVEAIREHAALRG--RV-TLEYVMISGVNVGEEDAAALGRL 270
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488615634 289 LKDTPCKINLIPFNPfPHSGYERPSNNAIRRFQDLLHQA--GYNVTVRTTRGEDIDAACGQL 348
Cdd:PRK14470 271 LAGIPVRLNPIAVND-ATGRYRPPDEDEWNAFRDALARElpGTPVVRRYSGGQDEHAACGML 331
PRK14464 PRK14464
RNA methyltransferase;
56-361 7.91e-55

RNA methyltransferase;


Pssm-ID: 184691  Cd Length: 344  Bit Score: 183.77  E-value: 7.91e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634  56 ALREKLKAC-AEVRG-PEVVSEDISSDGTRKWVVRVESGSCVETVYIPqgkRGTLCVSSQAGCALDCSFCSTGKQGFNSN 133
Cdd:PRK14464  47 ALREALPALeAELDGlARLRSEHPGEDGSARLLVELADGQMVESVLLP---RDGLCVSTQVGCAVGCVFCMTGRSGLLRQ 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 134 LTAAEVIGQVWIANKSfgsvpatvdRAITNVVMMGMGEPLLNFDNVIAAMHLmmddLGY--GISKRRVTLSTSGVVPMID 211
Cdd:PRK14464 124 LGSAEIVAQVVLARRR---------RAVKKVVFMGMGEPAHNLDNVLEAIDL----LGTegGIGHKNLVFSTVGDPRVFE 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 212 ELSKH-IDVSLALSLHAPNDALRNQLVPINKKYPLQMLLDSCRRYMSSLGekrvLTIEY--TMLKDINDKVEHAVEMIEL 288
Cdd:PRK14464 191 RLPQQrVKPALALSLHTTRAELRARLLPRAPRIAPEELVELGEAYARATG----YPIQYqwTLLEGVNDSDEEMDGIVRL 266
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488615634 289 LKDTPCKINLIPFNPFPHSGYERPSNNAIRRFQDLLHQAGYNVTVRTTRGEDIDAACGQLVGQVMD--RTRRSER 361
Cdd:PRK14464 267 LKGKYAVMNLIPYNSVDGDAYRRPSGERIVAMARYLHRRGVLTKVRNSAGQDVDGGCGQLRARAAKaaAVRRIRR 341
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
115-278 1.27e-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: 71.02  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634  115 GCALDCSFCSTGKQGFNSN---LTAAEVIGQVWIAnksfgsvpatvDRAITNVVMMGMGEPLLNFDNVIAAMHLMMDDLG 191
Cdd:pfam04055   4 GCNLRCTYCAFPSIRARGKgreLSPEEILEEAKEL-----------KRLGVEVVILGGGEPLLLPDLVELLERLLKLELA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634  192 YGIskrRVTLSTSGVVP---MIDELSKHIDVSLALSLHAPNDALRNqlvPINKKYPLQMLLDSCRRyMSSLGeKRVLTIE 268
Cdd:pfam04055  73 EGI---RITLETNGTLLdeeLLELLKEAGLDRVSIGLESGDDEVLK---LINRGHTFEEVLEALEL-LREAG-IPVVTDN 144
                         170
                  ....*....|
gi 488615634  269 YTMLKDINDK 278
Cdd:pfam04055 145 IVGLPGETDE 154
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
115-316 3.16e-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: 56.19  E-value: 3.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 115 GCALDCSFCSTGKQ---GFNSNLTAAEVIGQVWIANKSFGSvpatvdraitnVVMMGMGEPLLNFDNVIAAMHlmmddLG 191
Cdd:cd01335    6 GCNLNCGFCSNPASkgrGPESPPEIEEILDIVLEAKERGVE-----------VVILTGGEPLLYPELAELLRR-----LK 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 192 YGISKRRVTLSTSGVVPM---IDELSKHIDVSLALSLHAPNDALRNQLvpINKKYPLQMLLDSCRRYMSSlgeKRVLTIE 268
Cdd:cd01335   70 KELPGFEISIETNGTLLTeelLKELKELGLDGVGVSLDSGDEEVADKI--RGSGESFKERLEALKELREA---GLGLSTT 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 488615634 269 YTMLKDINDKVEHAVEMIELLK-DTPCKINLIPFNPFPHSGYERPSNNA 316
Cdd:cd01335  145 LLVGLGDEDEEDDLEELELLAEfRSPDRVSLFRLLPEEGTPLELAAPVV 193
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
114-338 6.31e-07

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 50.18  E-value: 6.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 114 AGCALDCSFC------STGKQGFNSNLTAAEVIGQVwIANKSF----GSVpatvdrAITnvvmmgMGEPLLNFDNVIAAM 183
Cdd:COG1180   29 QGCNLRCPYChnpeisQGRPDAAGRELSPEELVEEA-LKDRGFldscGGV------TFS------GGEPTLQPEFLLDLA 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 184 HLMMDdlgYGIskrRVTLSTSGVVP--MIDELSKHIDVsLALSLHAPNDALRNQLVpinkKYPLQMLLDSCRRymssLGE 261
Cdd:COG1180   96 KLAKE---LGL---HTALDTNGYIPeeALEELLPYLDA-VNIDLKAFDDEFYRKLT----GVSLEPVLENLEL----LAE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 262 KRV-LTIEYTMLKDINDKVEHAVEMIELLKDTPC--KINLIPFNP-FPHSGYERPSNNAIRRFQDLLHQAG-YNVTVRTT 336
Cdd:COG1180  161 SGVhVEIRTLVIPGLNDSEEELEAIARFIAELGDviPVHLLPFHPlYKLEDVPPPSPETLERAREIAREYGlKYVYIGNV 240

                 ..
gi 488615634 337 RG 338
Cdd:COG1180  241 PG 242
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
168-331 1.60e-03

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: 39.79  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 168 GMGEPLL--NFDNVIAAMHlmmddlgygiSKRRVTLS--TSGVVP----MIDELSKhIDVsLALSLHAPNDALRNQLVPI 239
Cdd:COG0731   87 GSGEPTLypNLGELIEEIK----------KLRGIKTAllTNGSLLhrpeVREELLK-ADQ-VYPSLDAADEETFRKINRP 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 240 NKKYPLQMLLDSCRRyMSSLGEKRvLTIEYTMLKDINDKVEHAVEMIELLKDT-PCKINL-IPFNPFPHSGYERPSNNAI 317
Cdd:COG0731  155 HPGLSWERIIEGLEL-FRKLYKGR-TVIETMLVKGINDSEEELEAYAELIKRInPDFVELkTYMRPPALSRVNMPSHEEL 232
                        170
                 ....*....|....
gi 488615634 318 RRFQDLLHQAGYNV 331
Cdd:COG0731  233 EEFAERLAELGYEV 246
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
114-218 4.48e-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: 38.19  E-value: 4.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615634 114 AGCALDCSFCST-----GKQGfnSNLTAAEVIGQVwianKSFGsvpatvdraITNVVMMGmGEPLL--NFDNVIAAMHlm 186
Cdd:COG0602   28 AGCNLRCSWCDTkyawdGEGG--KRMSAEEILEEV----AALG---------ARHVVITG-GEPLLqdDLAELLEALK-- 89
                         90       100       110
                 ....*....|....*....|....*....|..
gi 488615634 187 mdDLGYgiskrRVTLSTSGVVPmideLSKHID 218
Cdd:COG0602   90 --DAGY-----EVALETNGTLP----IPAGID 110
 
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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