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Conserved domains on  [gi|510806669|ref|WP_016181429|]
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MULTISPECIES: 23S rRNA (adenine(2503)-C(2))-methyltransferase RlmN [Enterococcus]

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 ...
6-348 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: 585.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669   6 IYGLRREELVEWFLEHGEKKFRATQVWEWLYRSRVSEFSEMSNLSKQTIALLEENFIINPLKQLVVQEASDGTVKYLFEL 85
Cdd:COG0820    1 LLGLTLEELEEFLAELGEKPFRAKQIFRWLYQKGVTDFDEMTNLPKALREKLAENFEIGLLEVVREQVSADGTRKYLFRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669  86 PDHLMIETVLMRQEYGLSVCVTTQVGCNIGCTFCASGLLKKQRDLTAGEIVAQIMLVQHYFDEcgEDERVSHVVVMGIGE 165
Cdd:COG0820   81 ADGNLVETVLIPYEDRGTLCVSSQVGCAMGCSFCATGKQGLVRNLTAGEIVGQVLLARRDLRE--GGRRVTNIVFMGMGE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 166 PFDNYNNVMNFLHVINDDKGMAIGARHITVSTSGLVPKIKKFAENGLQVNLAISLHAPNNEVRSSIMRINRSFPIEKLME 245
Cdd:COG0820  159 PLLNYDNVLKAIRILNDPEGLGISARRITVSTSGLVPGIRRLADEGLPVNLAVSLHAPNDELRDELMPINKKYPLEELLE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 246 AVDYYIEETNRRVTFEYIMLSGVNDRPDHAQQLADLMKNkkKLVYVNLIPYNPVSEHDqYSRSSKADVLRFYDVLKKNGI 325
Cdd:COG0820  239 ACRRYPEKTGRRITFEYVLLKGVNDSPEDARELARLLKG--LPCKVNLIPFNPVPGSP-YKRPSPERIEAFADILEKAGI 315
                        330       340
                 ....*....|....*....|...
gi 510806669 326 NCVIRKEHGTDIDAACGQLRSKQ 348
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 ...
6-348 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: 585.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669   6 IYGLRREELVEWFLEHGEKKFRATQVWEWLYRSRVSEFSEMSNLSKQTIALLEENFIINPLKQLVVQEASDGTVKYLFEL 85
Cdd:COG0820    1 LLGLTLEELEEFLAELGEKPFRAKQIFRWLYQKGVTDFDEMTNLPKALREKLAENFEIGLLEVVREQVSADGTRKYLFRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669  86 PDHLMIETVLMRQEYGLSVCVTTQVGCNIGCTFCASGLLKKQRDLTAGEIVAQIMLVQHYFDEcgEDERVSHVVVMGIGE 165
Cdd:COG0820   81 ADGNLVETVLIPYEDRGTLCVSSQVGCAMGCSFCATGKQGLVRNLTAGEIVGQVLLARRDLRE--GGRRVTNIVFMGMGE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 166 PFDNYNNVMNFLHVINDDKGMAIGARHITVSTSGLVPKIKKFAENGLQVNLAISLHAPNNEVRSSIMRINRSFPIEKLME 245
Cdd:COG0820  159 PLLNYDNVLKAIRILNDPEGLGISARRITVSTSGLVPGIRRLADEGLPVNLAVSLHAPNDELRDELMPINKKYPLEELLE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 246 AVDYYIEETNRRVTFEYIMLSGVNDRPDHAQQLADLMKNkkKLVYVNLIPYNPVSEHDqYSRSSKADVLRFYDVLKKNGI 325
Cdd:COG0820  239 ACRRYPEKTGRRITFEYVLLKGVNDSPEDARELARLLKG--LPCKVNLIPFNPVPGSP-YKRPSPERIEAFADILEKAGI 315
                        330       340
                 ....*....|....*....|...
gi 510806669 326 NCVIRKEHGTDIDAACGQLRSKQ 348
Cdd:COG0820  316 PVTVRRSRGDDIDAACGQLRAKV 338
rRNA_mod_RlmN TIGR00048
23S rRNA (adenine(2503)-C(2))-methyltransferase; Members of this family are RlmN, a 23S rRNA ...
2-353 1.25e-156

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: 443.49  E-value: 1.25e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669    2 EKPSIYGLRREELVEWFLEHGEKKFRATQVWEWLYRSRVSEFSEMSNLSKQTIALLEENFIINPLKQLVVQEASDGTVKY 81
Cdd:TIGR00048   5 GKPSLLDLTLQELRQWLKDLGEKPFRAKQIMKWLYHKGCDSFDDMTNLSKVLREKLNEVFEIRTPEIAHEQRSSDGTIKY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669   82 LFELPDHLMIETVLMRQEYGLSVCVTTQVGCNIGCTFCASGLLKKQRDLTAGEIVAQIMLVQHYFDECGEdeRVSHVVVM 161
Cdd:TIGR00048  85 LFALGDGQTIETVLIPEDDRATVCVSSQVGCALGCTFCATAKGGFNRNLEASEIIGQVLRVQKIVGETGE--RVSNVVFM 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669  162 GIGEPFDNYNNVMNFLHVINDDKGMAIGARHITVSTSGLVPKIKKFAENGLQVNLAISLHAPNNEVRSSIMRINRSFPIE 241
Cdd:TIGR00048 163 GMGEPLLNLNEVVKAMEIMNDDFGFGISKRRITISTSGVVPKIDKLADKMLQVALAISLHAPNDEIRSSLMPINKKYNIE 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669  242 KLMEAVDYYIEETNRRVTFEYIMLSGVNDRPDHAQQLADLMKNKKklVYVNLIPYNPVSEHDqYSRSSKADVLRFYDVLK 321
Cdd:TIGR00048 243 TLLAAVRRYLEKTGRRVTFEYVLLDGVNDQVEHAEELAELLKGTK--CKVNLIPWNPFPEAD-YGRPSNSQIDRFAKVLM 319
                         330       340       350
                  ....*....|....*....|....*....|..
gi 510806669  322 KNGINCVIRKEHGTDIDAACGQLRSKQMKKAT 353
Cdd:TIGR00048 320 SYGFTVTIRKSRGDDIDAACGQLRAKDVIDRT 351
PRK14461 PRK14461
ribosomal RNA large subunit methyltransferase N; Provisional
1-344 5.90e-104

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 237718  Cd Length: 371  Bit Score: 310.28  E-value: 5.90e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669   1 MEKPSIYGLRREELVEWFLEHGEKKFRATQVWEWLYRSRVSEFSEMSNLSKQTIALLEENFIINPLKQLVVQEASDG-TV 79
Cdd:PRK14461   5 MEQRNLYDLNLAELTELLTAWGQPAFRARQLYRHLYVNLADSVLAMTDLPLALRERLTAELPLSTLRLEQVQIGDNGlTR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669  80 KYLFELPDHLMIETVLMRQEYGLSVCVTTQVGCNIGCTFCASGLLKKQRDLTAGEIVAQIMLVQHYF---------DECG 150
Cdd:PRK14461  85 KALFRLPDGAVVETVLMIYPDRATVCVSTQAGCGMGCVFCATGTLGLLRNLSSGEIVAQVIWASRELramgaaiskRHAG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 151 EDERVSHVVVMGIGEPFDNYNNVMNFLHVINDDKGMAIGARHITVSTSGLVPKIKKFAENGLQVNLAISLHAPNNEVRSS 230
Cdd:PRK14461 165 PVGRVTNLVFMGMGEPFANYDRWWQAVERLHDPQGFNLGARSMTVSTVGLVKGIRRLANERLPINLAISLHAPDDALRSE 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 231 IMRINRSFPIEKLMEAVDYYIEETNRRVTFEYIMLSGVNDRPDHAQQLADLMKNKKK----LVYVNLIPYNPVSeHDQYS 306
Cdd:PRK14461 245 LMPVNRRYPIADLMAATRDYIAKTRRRVSFEYVLLQGKNDHPEQAAALARLLRGEAPpgplLVHVNLIPWNPVP-GTPLG 323
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 510806669 307 RSSKADVLRFYDVLKKNGINCVIRKEHGTDIDAACGQL 344
Cdd:PRK14461 324 RSERERVTTFQRILTDYGIPCTVRVERGVEIAAACGQL 361
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
108-270 6.50e-16

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: 74.10  E-value: 6.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669  108 TQVGCNIGCTFCA---SGLLKKQRDLTAGEIVAQIMLVQhyfdecgedERVSHVVVMGIGEPFDNYNNVMNFLHVINDDk 184
Cdd:pfam04055   1 ITRGCNLRCTYCAfpsIRARGKGRELSPEEILEEAKELK---------RLGVEVVILGGGEPLLLPDLVELLERLLKLE- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669  185 gmAIGARHITVSTSGLVP---KIKKFAENGLqVNLAISLHAPNNEVRssiMRINRSFPIEKLMEAVDYYIEETNRRVTFE 261
Cdd:pfam04055  71 --LAEGIRITLETNGTLLdeeLLELLKEAGL-DRVSIGLESGDDEVL---KLINRGHTFEEVLEALELLREAGIPVVTDN 144

                  ....*....
gi 510806669  262 YIMLSGVND 270
Cdd:pfam04055 145 IVGLPGETD 153
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
111-299 3.03e-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: 3.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 111 GCNIGCTFCASGLLKKQRDLTAGEIVAQIMLVQhyfdecGEDERVSHVVVMGIGEPFDNYNNVMNFLHVINDDKGMaiga 190
Cdd:cd01335    6 GCNLNCGFCSNPASKGRGPESPPEIEEILDIVL------EAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGF---- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 191 rHITVSTSGLVPK---IKKFAENGLqVNLAISLHAPNNEVRSSIMRINRSFpiEKLMEAVDYYiEETNRRVTFEYIMLSG 267
Cdd:cd01335   76 -EISIETNGTLLTeelLKELKELGL-DGVGVSLDSGDEEVADKIRGSGESF--KERLEALKEL-REAGLGLSTTLLVGLG 150
                        170       180       190
                 ....*....|....*....|....*....|..
gi 510806669 268 VNDRPDHAQQLADLmKNKKKLVYVNLIPYNPV 299
Cdd:cd01335  151 DEDEEDDLEELELL-AEFRSPDRVSLFRLLPE 181
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
106-317 7.04e-05

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


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 43.54  E-value: 7.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669   106 VTTQVGCNIGCTFCA-SGLLKKQRDLTAGEIVAQIMLVqhyfDECGEDERVSHVVVMGIGEPFDN-YNNVMNFLHVIN-- 181
Cdd:smart00729   5 YIITRGCPRRCTFCSfPSLRGKLRSRYLEALVREIELL----AEKGEKEGLVGTVFIGGGTPTLLsPEQLEELLEAIRei 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669   182 ----DDKGMAIGARHITVSTSglvpKIKKFAENGLQVnLAISLHAPNNEVRSsimRINRSFPIEKLMEAVDYYIEETNRR 257
Cdd:smart00729  81 lglaKDVEITIETRPDTLTEE----LLEALKEAGVNR-VSLGVQSGDDEVLK---AINRGHTVEDVLEAVELLREAGPIK 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510806669   258 VTFeYIM--LSGVNDrpDHAQQLADLMKnKKKLVYVNLIPYNPV------SEHDQYSRSSKADVLRFY 317
Cdd:smart00729 153 VST-DLIvgLPGETE--EDFEETLKLLK-ELGPDRVSIFPLSPRpgtplaKMYKRLKPPTKEERAELL 216
 
Name Accession Description Interval E-value
RlmN COG0820
Adenine C2-methylase RlmN of 23S rRNA A2503 and tRNA A37 [Translation, ribosomal structure and ...
6-348 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: 585.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669   6 IYGLRREELVEWFLEHGEKKFRATQVWEWLYRSRVSEFSEMSNLSKQTIALLEENFIINPLKQLVVQEASDGTVKYLFEL 85
Cdd:COG0820    1 LLGLTLEELEEFLAELGEKPFRAKQIFRWLYQKGVTDFDEMTNLPKALREKLAENFEIGLLEVVREQVSADGTRKYLFRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669  86 PDHLMIETVLMRQEYGLSVCVTTQVGCNIGCTFCASGLLKKQRDLTAGEIVAQIMLVQHYFDEcgEDERVSHVVVMGIGE 165
Cdd:COG0820   81 ADGNLVETVLIPYEDRGTLCVSSQVGCAMGCSFCATGKQGLVRNLTAGEIVGQVLLARRDLRE--GGRRVTNIVFMGMGE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 166 PFDNYNNVMNFLHVINDDKGMAIGARHITVSTSGLVPKIKKFAENGLQVNLAISLHAPNNEVRSSIMRINRSFPIEKLME 245
Cdd:COG0820  159 PLLNYDNVLKAIRILNDPEGLGISARRITVSTSGLVPGIRRLADEGLPVNLAVSLHAPNDELRDELMPINKKYPLEELLE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 246 AVDYYIEETNRRVTFEYIMLSGVNDRPDHAQQLADLMKNkkKLVYVNLIPYNPVSEHDqYSRSSKADVLRFYDVLKKNGI 325
Cdd:COG0820  239 ACRRYPEKTGRRITFEYVLLKGVNDSPEDARELARLLKG--LPCKVNLIPFNPVPGSP-YKRPSPERIEAFADILEKAGI 315
                        330       340
                 ....*....|....*....|...
gi 510806669 326 NCVIRKEHGTDIDAACGQLRSKQ 348
Cdd:COG0820  316 PVTVRRSRGDDIDAACGQLRAKV 338
rRNA_mod_RlmN TIGR00048
23S rRNA (adenine(2503)-C(2))-methyltransferase; Members of this family are RlmN, a 23S rRNA ...
2-353 1.25e-156

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: 443.49  E-value: 1.25e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669    2 EKPSIYGLRREELVEWFLEHGEKKFRATQVWEWLYRSRVSEFSEMSNLSKQTIALLEENFIINPLKQLVVQEASDGTVKY 81
Cdd:TIGR00048   5 GKPSLLDLTLQELRQWLKDLGEKPFRAKQIMKWLYHKGCDSFDDMTNLSKVLREKLNEVFEIRTPEIAHEQRSSDGTIKY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669   82 LFELPDHLMIETVLMRQEYGLSVCVTTQVGCNIGCTFCASGLLKKQRDLTAGEIVAQIMLVQHYFDECGEdeRVSHVVVM 161
Cdd:TIGR00048  85 LFALGDGQTIETVLIPEDDRATVCVSSQVGCALGCTFCATAKGGFNRNLEASEIIGQVLRVQKIVGETGE--RVSNVVFM 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669  162 GIGEPFDNYNNVMNFLHVINDDKGMAIGARHITVSTSGLVPKIKKFAENGLQVNLAISLHAPNNEVRSSIMRINRSFPIE 241
Cdd:TIGR00048 163 GMGEPLLNLNEVVKAMEIMNDDFGFGISKRRITISTSGVVPKIDKLADKMLQVALAISLHAPNDEIRSSLMPINKKYNIE 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669  242 KLMEAVDYYIEETNRRVTFEYIMLSGVNDRPDHAQQLADLMKNKKklVYVNLIPYNPVSEHDqYSRSSKADVLRFYDVLK 321
Cdd:TIGR00048 243 TLLAAVRRYLEKTGRRVTFEYVLLDGVNDQVEHAEELAELLKGTK--CKVNLIPWNPFPEAD-YGRPSNSQIDRFAKVLM 319
                         330       340       350
                  ....*....|....*....|....*....|..
gi 510806669  322 KNGINCVIRKEHGTDIDAACGQLRSKQMKKAT 353
Cdd:TIGR00048 320 SYGFTVTIRKSRGDDIDAACGQLRAKDVIDRT 351
PRK14461 PRK14461
ribosomal RNA large subunit methyltransferase N; Provisional
1-344 5.90e-104

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 237718  Cd Length: 371  Bit Score: 310.28  E-value: 5.90e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669   1 MEKPSIYGLRREELVEWFLEHGEKKFRATQVWEWLYRSRVSEFSEMSNLSKQTIALLEENFIINPLKQLVVQEASDG-TV 79
Cdd:PRK14461   5 MEQRNLYDLNLAELTELLTAWGQPAFRARQLYRHLYVNLADSVLAMTDLPLALRERLTAELPLSTLRLEQVQIGDNGlTR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669  80 KYLFELPDHLMIETVLMRQEYGLSVCVTTQVGCNIGCTFCASGLLKKQRDLTAGEIVAQIMLVQHYF---------DECG 150
Cdd:PRK14461  85 KALFRLPDGAVVETVLMIYPDRATVCVSTQAGCGMGCVFCATGTLGLLRNLSSGEIVAQVIWASRELramgaaiskRHAG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 151 EDERVSHVVVMGIGEPFDNYNNVMNFLHVINDDKGMAIGARHITVSTSGLVPKIKKFAENGLQVNLAISLHAPNNEVRSS 230
Cdd:PRK14461 165 PVGRVTNLVFMGMGEPFANYDRWWQAVERLHDPQGFNLGARSMTVSTVGLVKGIRRLANERLPINLAISLHAPDDALRSE 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 231 IMRINRSFPIEKLMEAVDYYIEETNRRVTFEYIMLSGVNDRPDHAQQLADLMKNKKK----LVYVNLIPYNPVSeHDQYS 306
Cdd:PRK14461 245 LMPVNRRYPIADLMAATRDYIAKTRRRVSFEYVLLQGKNDHPEQAAALARLLRGEAPpgplLVHVNLIPWNPVP-GTPLG 323
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 510806669 307 RSSKADVLRFYDVLKKNGINCVIRKEHGTDIDAACGQL 344
Cdd:PRK14461 324 RSERERVTTFQRILTDYGIPCTVRVERGVEIAAACGQL 361
PRK11194 PRK11194
ribosomal RNA large subunit methyltransferase N; Provisional
2-351 6.07e-102

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 183031  Cd Length: 372  Bit Score: 305.11  E-value: 6.07e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669   2 EKPSIYGLRREELVEWFLEHGEKKFRATQVWEWLYRSRVSEFSEMSNLSKQTIALLEENFIINPLKQLVVQEASDGTVKY 81
Cdd:PRK11194   4 KKINLLDLNRQQMREFFAELGEKPFRADQVMKWIYHYGCDDFDEMTNINKVLREKLKEVAEIRAPEVAEEQRSSDGTIKW 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669  82 LFELPDHlMIETVLMRQEYGLSVCVTTQVGCNIGCTFCASGLLKKQRDLTAGEIVAQIMLVQHYFDECGEDER--VSHVV 159
Cdd:PRK11194  84 AIAVGDQ-RVETVYIPEDDRATLCVSSQVGCALECKFCSTAQQGFNRNLRVSEIIGQVWRAAKIIGAAKVTGQrpITNVV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 160 VMGIGEPFDNYNNVMNFLHVINDDKGMAIGARHITVSTSGLVPKIKKFAENgLQVNLAISLHAPNNEVRSSIMRINRSFP 239
Cdd:PRK11194 163 MMGMGEPLLNLNNVVPAMEIMLDDFGFGLSKRRVTLSTSGVVPALDKLGDM-IDVALAISLHAPNDELRDEIVPINKKYN 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 240 IEKLMEAVDYYIEETNR---RVTFEYIMLSGVNDRPDHAQQLADLMKNKKklVYVNLIPYNPVSEHDqYSRSSKADVLRF 316
Cdd:PRK11194 242 IETFLAAVRRYLEKSNAnqgRVTVEYVMLDHVNDGTEHAHQLAELLKDTP--CKINLIPWNPFPGAP-YGRSSNSRIDRF 318
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 510806669 317 YDVLKKNGINCVIRKEHGTDIDAACGQL------RSKQMKK 351
Cdd:PRK11194 319 SKVLMEYGFTVIVRKTRGDDIDAACGQLagdvidRTKRTLK 359
PRK14453 PRK14453
chloramphenicol/florfenicol resistance protein; Provisional
23-344 5.51e-89

chloramphenicol/florfenicol resistance protein; Provisional


Pssm-ID: 184685  Cd Length: 347  Bit Score: 271.23  E-value: 5.51e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669  23 EKKFRATQVWEWLYRSRVSEFSEMSNLSKQTIALLEENF-----IINPLKQLVVQEASdgtvKYLFELPDHLMIETVLMR 97
Cdd:PRK14453  19 LPDYRYEQITKAIFKQRIDNFEDMHILPKALRESLINEFgknvlSVIPVFEQDSKQVT----KVLFELTDGERIEAVGLK 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669  98 QEYGL-SVCVTTQVGCNIGCTFCASGLLKKQRDLTAGEIVAQIMlvqhYFDECGEdeRVSHVVVMGIGEPFDNyNNVMNF 176
Cdd:PRK14453  95 YKQGWeSFCISSQCGCGFGCRFCATGSIGLKRNLTADEITDQLL----YFYLNGH--RLDSISFMGMGEALAN-PELFDA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 177 LHVINDDKGMAIGARHITVSTSGLVPKIKKFAENGLQVNLAISLHAPNNEVRSSIMRINRSFPIEKLMEAVDYYIEETNR 256
Cdd:PRK14453 168 LKILTDPNLFGLSQRRITISTIGIIPGIQRLTQEFPQVNLTFSLHSPFESQRSELMPINKRFPLNEVMKTLDEHIRHTGR 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 257 RVTFEYIMLSGVNDRPDHAQQLADLMKNKKK---LVYVNLIPYNP-VSEHDQYSRSSKADVLRFYDVLKKNGINCVIRKE 332
Cdd:PRK14453 248 KVYIAYIMLEGVNDSKEHAEAVVGLLRNRGSwehLYHVNLIPYNStDKTPFKFQSSSAGQIKQFCSTLKSAGISVTVRTQ 327
                        330
                 ....*....|..
gi 510806669 333 HGTDIDAACGQL 344
Cdd:PRK14453 328 FGSDISAACGQL 339
PRK14470 PRK14470
ribosomal RNA large subunit methyltransferase N; Provisional
66-348 2.38e-54

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 172945  Cd Length: 336  Bit Score: 181.67  E-value: 2.38e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669  66 LKQLVVQEASDGTVKYLFELPDHLMIETV---LMRQEYglSVCVTTQVGCNIGCTFCASGLLKKQRDLTAGEIVAQIMLV 142
Cdd:PRK14470  60 LRLVERVDAKDGFRKYLFELPDGLRVEAVripLFDTHH--VVCLSSQAGCALGCAFCATGKLGLDRSLRSWEIVAQLLAV 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 143 QhyfdecGEDER-VSHVVVMGIGEPFDNYNNVMNFLHVINDDKGMAIGARHITVSTSGLVPKIKKFAENGLQVNLAISLH 221
Cdd:PRK14470 138 R------ADSERpITGVVFMGQGEPFLNYDEVLRAAYALCDPAGARIDGRRISISTAGVVPMIRRYTAEGHKFRLCISLN 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 222 APNNEVRSSIMRINRSFPIEKLMEAVDYYiEETNRRVTFEYIMLSGVNDRPDHAQQLADLMKNKKklVYVNLIPYNPVSe 301
Cdd:PRK14470 212 AAIPWKRRALMPIEQGFPLDELVEAIREH-AALRGRVTLEYVMISGVNVGEEDAAALGRLLAGIP--VRLNPIAVNDAT- 287
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 510806669 302 hDQYSRSSKADVLRFYDVLKKN--GINCVIRKEHGTDIDAACGQLRSKQ 348
Cdd:PRK14470 288 -GRYRPPDEDEWNAFRDALARElpGTPVVRRYSGGQDEHAACGMLASRR 335
PRK14464 PRK14464
RNA methyltransferase;
74-354 4.88e-46

RNA methyltransferase;


Pssm-ID: 184691  Cd Length: 344  Bit Score: 160.28  E-value: 4.88e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669  74 ASDGTVKYLFELPDHLMIETVLMRQEyGLsvCVTTQVGCNIGCTFCA---SGLLkkqRDLTAGEIVAQIMLVQHYfdecg 150
Cdd:PRK14464  71 GEDGSARLLVELADGQMVESVLLPRD-GL--CVSTQVGCAVGCVFCMtgrSGLL---RQLGSAEIVAQVVLARRR----- 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 151 edERVSHVVVMGIGEPFDNYNNVMNFLHVINDDKGmaIGARHITVSTSGLVPKIKKFAENGLQVNLAISLHAPNNEVRSS 230
Cdd:PRK14464 140 --RAVKKVVFMGMGEPAHNLDNVLEAIDLLGTEGG--IGHKNLVFSTVGDPRVFERLPQQRVKPALALSLHTTRAELRAR 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 231 IMRINRSFPIEKLMEAVDYYIEETNRRVTFEYIMLSGVNDRPDHAQQLADLMKNKKKLvyVNLIPYNPVsEHDQYSRSSK 310
Cdd:PRK14464 216 LLPRAPRIAPEELVELGEAYARATGYPIQYQWTLLEGVNDSDEEMDGIVRLLKGKYAV--MNLIPYNSV-DGDAYRRPSG 292
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 510806669 311 ADVLRFYDVLKKNGINCVIRKEHGTDIDAACGQLRSKQMKKATV 354
Cdd:PRK14464 293 ERIVAMARYLHRRGVLTKVRNSAGQDVDGGCGQLRARAAKAAAV 336
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
108-270 6.50e-16

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: 74.10  E-value: 6.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669  108 TQVGCNIGCTFCA---SGLLKKQRDLTAGEIVAQIMLVQhyfdecgedERVSHVVVMGIGEPFDNYNNVMNFLHVINDDk 184
Cdd:pfam04055   1 ITRGCNLRCTYCAfpsIRARGKGRELSPEEILEEAKELK---------RLGVEVVILGGGEPLLLPDLVELLERLLKLE- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669  185 gmAIGARHITVSTSGLVP---KIKKFAENGLqVNLAISLHAPNNEVRssiMRINRSFPIEKLMEAVDYYIEETNRRVTFE 261
Cdd:pfam04055  71 --LAEGIRITLETNGTLLdeeLLELLKEAGL-DRVSIGLESGDDEVL---KLINRGHTFEEVLEALELLREAGIPVVTDN 144

                  ....*....
gi 510806669  262 YIMLSGVND 270
Cdd:pfam04055 145 IVGLPGETD 153
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
110-334 6.79e-10

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 58.66  E-value: 6.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 110 VGCNIGCTFCA------SGLLKKQRDLTAGEIVAQIMLVQHYFDECGedervsHVVVMGiGEPFDNYNNVMNFLHVIndd 183
Cdd:COG1180   29 QGCNLRCPYCHnpeisqGRPDAAGRELSPEELVEEALKDRGFLDSCG------GVTFSG-GEPTLQPEFLLDLAKLA--- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 184 KGMAIgarHITVSTSGLVPK--IKKFAENglqVNL-AISLHAPNNEVRSSIMRInrsfPIEKLMEAVDYyIEETNRRVTF 260
Cdd:COG1180   99 KELGL---HTALDTNGYIPEeaLEELLPY---LDAvNIDLKAFDDEFYRKLTGV----SLEPVLENLEL-LAESGVHVEI 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510806669 261 EYIMLSGVNDRPDHAQQLADLMKNKKKLVYVNLIPYNPVSEHDQYSRSSKADVLRFYDVLKKNGI-NCVIRKEHG 334
Cdd:COG1180  168 RTLVIPGLNDSEEELEAIARFIAELGDVIPVHLLPFHPLYKLEDVPPPSPETLERAREIAREYGLkYVYIGNVPG 242
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
111-299 3.03e-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: 3.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 111 GCNIGCTFCASGLLKKQRDLTAGEIVAQIMLVQhyfdecGEDERVSHVVVMGIGEPFDNYNNVMNFLHVINDDKGMaiga 190
Cdd:cd01335    6 GCNLNCGFCSNPASKGRGPESPPEIEEILDIVL------EAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGF---- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 191 rHITVSTSGLVPK---IKKFAENGLqVNLAISLHAPNNEVRSSIMRINRSFpiEKLMEAVDYYiEETNRRVTFEYIMLSG 267
Cdd:cd01335   76 -EISIETNGTLLTeelLKELKELGL-DGVGVSLDSGDEEVADKIRGSGESF--KERLEALKEL-REAGLGLSTTLLVGLG 150
                        170       180       190
                 ....*....|....*....|....*....|..
gi 510806669 268 VNDRPDHAQQLADLmKNKKKLVYVNLIPYNPV 299
Cdd:cd01335  151 DEDEEDDLEELELL-AEFRSPDRVSLFRLLPE 181
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
112-253 6.72e-08

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: 51.44  E-value: 6.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 112 CNIGCTFC-ASGLLKKQRDLTAGEIvaqimlvQHYFDECgEDERVSHVVVMGiGEPFDNyNNVMNFLHVINdDKGMaiga 190
Cdd:COG0535   10 CNLRCKHCyADAGPKRPGELSTEEA-------KRILDEL-AELGVKVVGLTG-GEPLLR-PDLFELVEYAK-ELGI---- 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510806669 191 rHITVSTSGLV---PKIKKFAENGLQVnLAISLHAPNNEVRSSIMRINRSFpiEKLMEAVDYYIEE 253
Cdd:COG0535   75 -RVNLSTNGTLlteELAERLAEAGLDH-VTISLDGVDPETHDKIRGVPGAF--DKVLEAIKLLKEA 136
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
106-317 7.04e-05

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


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 43.54  E-value: 7.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669   106 VTTQVGCNIGCTFCA-SGLLKKQRDLTAGEIVAQIMLVqhyfDECGEDERVSHVVVMGIGEPFDN-YNNVMNFLHVIN-- 181
Cdd:smart00729   5 YIITRGCPRRCTFCSfPSLRGKLRSRYLEALVREIELL----AEKGEKEGLVGTVFIGGGTPTLLsPEQLEELLEAIRei 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669   182 ----DDKGMAIGARHITVSTSglvpKIKKFAENGLQVnLAISLHAPNNEVRSsimRINRSFPIEKLMEAVDYYIEETNRR 257
Cdd:smart00729  81 lglaKDVEITIETRPDTLTEE----LLEALKEAGVNR-VSLGVQSGDDEVLK---AINRGHTVEDVLEAVELLREAGPIK 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510806669   258 VTFeYIM--LSGVNDrpDHAQQLADLMKnKKKLVYVNLIPYNPV------SEHDQYSRSSKADVLRFY 317
Cdd:smart00729 153 VST-DLIvgLPGETE--EDFEETLKLLK-ELGPDRVSIFPLSPRpgtplaKMYKRLKPPTKEERAELL 216
YgiQ COG1032
Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];
95-333 4.31e-04

Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];


Pssm-ID: 440655 [Multi-domain]  Cd Length: 394  Bit Score: 41.86  E-value: 4.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669  95 LMRQEYGLSVCVTTQVGCNIGCTFCASGLL--KKQRDLTAGEIVAQI-MLVQHYfdecgedeRVSHVVVMGiGEPFDNYN 171
Cdd:COG1032  167 LDLEAYHRRASIETSRGCPFGCSFCSISALygRKVRYRSPESVVEEIeELVKRY--------GIREIFFVD-DNFNVDKK 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 172 NVMNFLHVINdDKGMAIGArHITVSTSGLVPK-IKKFAENGL-QVNLAISlhAPNNEVRSsimRINRSFPIEKLMEAVDy 249
Cdd:COG1032  238 RLKELLEELI-ERGLNVSF-PSEVRVDLLDEElLELLKKAGCrGLFIGIE--SGSQRVLK---AMNKGITVEDILEAVR- 309
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 250 YIEETNRRVTFeYIMLSGVNDRPDHAQQLADLMK-NKKKLVYVN-LIPYnPVSEhdqysrsskadvlrFYDVLKKNGINC 327
Cdd:COG1032  310 LLKKAGIRVKL-YFIIGLPGETEEDIEETIEFIKeLGPDQAQVSiFTPL-PGTP--------------LYEELEKEGRLY 373

                 ....*.
gi 510806669 328 VIRKEH 333
Cdd:COG1032  374 DWEKYE 379
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
111-295 6.12e-04

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: 40.51  E-value: 6.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 111 GCNIGCTFC--------ASGllkkqRDLTAGEIVAQImlvqhyfdecgEDERVSHVVVMGiGEPF--DNYNNVMNFLHvi 180
Cdd:COG0602   29 GCNLRCSWCdtkyawdgEGG-----KRMSAEEILEEV-----------AALGARHVVITG-GEPLlqDDLAELLEALK-- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 181 ndDKGMaigarHITVSTSGLVPK----------IKKFAENGLQVNLA-ISLHAPNNEVRssimrinrsFPI---EKLMEA 246
Cdd:COG0602   90 --DAGY-----EVALETNGTLPIpagidwvtvsPKLPSSGEEEDNREnLEVLRRADELK---------FVVadeTDLEEA 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 510806669 247 VDyYIEETNRRVTFeYIMLSGVNDRPDHAQQLADLMKNKKKlvyVNLIP 295
Cdd:COG0602  154 EE-LLARLDFRCPV-YLQPVWGNKLEENTELLAEWCLAHPN---VRLSP 197
COG2100 COG2100
Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function ...
111-270 1.02e-03

Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function prediction only];


Pssm-ID: 441703 [Multi-domain]  Cd Length: 344  Bit Score: 40.66  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 111 GCNIGCTFCA--SGLLKKQRdlTAGEIVAQIMLVQHYFDECGEDERVSHVVVMGIGEPFdNYNNVMNFLHVINDDKGMAI 188
Cdd:COG2100   45 GCNLNCIFCSvdAGPHSRTR--QAEYIVDPEYLVEWFEKVARFKGKGVEAHIDGVGEPL-LYPYIVELVKGLKEIKGVKV 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 189 garhITVSTSGLV---PKIKKFAENGL-QVNLAI-SLhapnNEVRSSIMRINRSFPIEKLMEAVDYYIEETNRRVTFEYI 263
Cdd:COG2100  122 ----VSMQTNGTLlseKLIDELEEAGLdRINLSIdTL----DPEKAKKLAGTKWYDVEKVLELAEYIARETKIDLLIAPV 193

                 ....*..
gi 510806669 264 MLSGVND 270
Cdd:COG2100  194 WLPGIND 200
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
218-329 3.39e-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: 38.63  E-value: 3.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669 218 ISLHAPNNEvrsSIMRINR---SFPIEKLMEAVDYYIEETNRRVTFEYIMLSGVNDRPDHAQQLADLMKN-KKKLVYVNL 293
Cdd:COG0731  138 PSLDAADEE---TFRKINRphpGLSWERIIEGLELFRKLYKGRTVIETMLVKGINDSEEELEAYAELIKRiNPDFVELKT 214
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 510806669 294 IPYNPVSEHDQysRSSKADVLRFYDVLKKNGINCVI 329
Cdd:COG0731  215 YMRPPALSRVN--MPSHEELEEFAERLAELGYEVVS 248
MiaB-like-C TIGR01579
MiaB-like tRNA modifying enzyme; This clade of sequences is closely related to MiaB, a ...
106-248 7.53e-03

MiaB-like tRNA modifying enzyme; This clade of sequences is closely related to MiaB, a modifier of isopentenylated adenosine-37 of certain eukaryotic and bacterial tRNAs (see TIGR01574). Sequence alignments suggest that this equivalog performs the same chemical transformation as MiaB, perhaps on a different (or differently modified) tRNA base substrate. This clade is a member of a subfamily (TIGR00089) and spans low GC Gram positive bacteria, alpha and epsilon proteobacteria, Campylobacter, Porphyromonas, Aquifex, Thermotoga, Chlamydia, Treponema and Fusobacterium. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273704 [Multi-domain]  Cd Length: 414  Bit Score: 38.12  E-value: 7.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806669  106 VTTQVGCNIGCTFCASGLLK-KQRDLTAGEIVAQI-MLVQHYFDEcgedervshVVVMGI-----GEPFDNYNNVMNFLH 178
Cdd:TIGR01579 142 IKVQDGCNFFCSYCIIPFARgRSRSVPMEAILKQVkILVAKGYKE---------IVLTGVnlgsyGDDLKNGTSLAKLLE 212
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510806669  179 VIN---DDKGMAIGARHITVSTSGLVPKIKKfaENGLQVNLAISLHAPNNEVrssIMRINRSFPIEKLMEAVD 248
Cdd:TIGR01579 213 QILqipGIKRIRLSSIDPEDIDEELLEAIAS--EKRLCPHLHLSLQSGSDRV---LKRMRRKYTRDDFLKLVN 280
 
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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