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Conserved domains on  [gi|1655118514|ref|WP_137603864|]
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23S rRNA (adenine(2503)-C(2))-methyltransferase RlmN [Enterococcus dongliensis]

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: 586.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514   6 IYGLRREELVEWFLEHGEKKFRATQVWEWLYRSRVTEFAQMSNLSKQTIALLEENFIINPLKQLVVQEASDGTVKYLFEL 85
Cdd:COG0820     1 LLGLTLEELEEFLAELGEKPFRAKQIFRWLYQKGVTDFDEMTNLPKALREKLAENFEIGLLEVVREQVSADGTRKYLFRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514  86 PDHLMIETVLMRQEYGLSVCVTTQVGCNIGCTFCASGLLKKQRDLTAGEIVAQIMLVQHYFDERGEeeRVSHIVVMGIGE 165
Cdd:COG0820    81 ADGNLVETVLIPYEDRGTLCVSSQVGCAMGCSFCATGKQGLVRNLTAGEIVGQVLLARRDLREGGR--RVTNIVFMGMGE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 166 PFDNYNNVMDFLHVINDDKGMAIGARHITVSTSGLVPKIKKFAENGLQVNLAISLHAPNNEIRSSIMRINRSFPIEKLMG 245
Cdd:COG0820   159 PLLNYDNVLKAIRILNDPEGLGISARRITVSTSGLVPGIRRLADEGLPVNLAVSLHAPNDELRDELMPINKKYPLEELLE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 246 AVDYYIEETNRRVTFEYIMLSGVNDQPEHAQQLADLMKDkkKLVYVNLIPYNPVSEHDqYSRSSKAAVLRFYDVLKKNGI 325
Cdd:COG0820   239 ACRRYPEKTGRRITFEYVLLKGVNDSPEDARELARLLKG--LPCKVNLIPFNPVPGSP-YKRPSPERIEAFADILEKAGI 315
                         330       340
                  ....*....|....*....|...
gi 1655118514 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: 586.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514   6 IYGLRREELVEWFLEHGEKKFRATQVWEWLYRSRVTEFAQMSNLSKQTIALLEENFIINPLKQLVVQEASDGTVKYLFEL 85
Cdd:COG0820     1 LLGLTLEELEEFLAELGEKPFRAKQIFRWLYQKGVTDFDEMTNLPKALREKLAENFEIGLLEVVREQVSADGTRKYLFRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514  86 PDHLMIETVLMRQEYGLSVCVTTQVGCNIGCTFCASGLLKKQRDLTAGEIVAQIMLVQHYFDERGEeeRVSHIVVMGIGE 165
Cdd:COG0820    81 ADGNLVETVLIPYEDRGTLCVSSQVGCAMGCSFCATGKQGLVRNLTAGEIVGQVLLARRDLREGGR--RVTNIVFMGMGE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 166 PFDNYNNVMDFLHVINDDKGMAIGARHITVSTSGLVPKIKKFAENGLQVNLAISLHAPNNEIRSSIMRINRSFPIEKLMG 245
Cdd:COG0820   159 PLLNYDNVLKAIRILNDPEGLGISARRITVSTSGLVPGIRRLADEGLPVNLAVSLHAPNDELRDELMPINKKYPLEELLE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 246 AVDYYIEETNRRVTFEYIMLSGVNDQPEHAQQLADLMKDkkKLVYVNLIPYNPVSEHDqYSRSSKAAVLRFYDVLKKNGI 325
Cdd:COG0820   239 ACRRYPEKTGRRITFEYVLLKGVNDSPEDARELARLLKG--LPCKVNLIPFNPVPGSP-YKRPSPERIEAFADILEKAGI 315
                         330       340
                  ....*....|....*....|...
gi 1655118514 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 ...
2-348 3.90e-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: 442.33  E-value: 3.90e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514   2 ERPSIYGLRREELVEWFLEHGEKKFRATQVWEWLYRSRVTEFAQMSNLSKQTIALLEENFIINPLKQLVVQEASDGTVKY 81
Cdd:TIGR00048   5 GKPSLLDLTLQELRQWLKDLGEKPFRAKQIMKWLYHKGCDSFDDMTNLSKVLREKLNEVFEIRTPEIAHEQRSSDGTIKY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514  82 LFELPDHLMIETVLMRQEYGLSVCVTTQVGCNIGCTFCASGLLKKQRDLTAGEIVAQIMLVQHYFDERGEeeRVSHIVVM 161
Cdd:TIGR00048  85 LFALGDGQTIETVLIPEDDRATVCVSSQVGCALGCTFCATAKGGFNRNLEASEIIGQVLRVQKIVGETGE--RVSNVVFM 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 162 GIGEPFDNYNNVMDFLHVINDDKGMAIGARHITVSTSGLVPKIKKFAENGLQVNLAISLHAPNNEIRSSIMRINRSFPIE 241
Cdd:TIGR00048 163 GMGEPLLNLNEVVKAMEIMNDDFGFGISKRRITISTSGVVPKIDKLADKMLQVALAISLHAPNDEIRSSLMPINKKYNIE 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 242 KLMGAVDYYIEETNRRVTFEYIMLSGVNDQPEHAQQLADLMKDKKklVYVNLIPYNPVSEHDqYSRSSKAAVLRFYDVLK 321
Cdd:TIGR00048 243 TLLAAVRRYLEKTGRRVTFEYVLLDGVNDQVEHAEELAELLKGTK--CKVNLIPWNPFPEAD-YGRPSNSQIDRFAKVLM 319
                         330       340
                  ....*....|....*....|....*..
gi 1655118514 322 KNGINCVIRKEHGTDIDAACGQLRSKQ 348
Cdd:TIGR00048 320 SYGFTVTIRKSRGDDIDAACGQLRAKD 346
PRK14461 PRK14461
ribosomal RNA large subunit methyltransferase N; Provisional
1-344 3.78e-105

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 237718  Cd Length: 371  Bit Score: 313.36  E-value: 3.78e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514   1 MERPSIYGLRREELVEWFLEHGEKKFRATQVWEWLYRSRVTEFAQMSNLSKQTIALLEENFIINPLKQLVVQEASDG-TV 79
Cdd:PRK14461    5 MEQRNLYDLNLAELTELLTAWGQPAFRARQLYRHLYVNLADSVLAMTDLPLALRERLTAELPLSTLRLEQVQIGDNGlTR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514  80 KYLFELPDHLMIETVLMRQEYGLSVCVTTQVGCNIGCTFCASGLLKKQRDLTAGEIVAQIMLVQHYF---------DERG 150
Cdd:PRK14461   85 KALFRLPDGAVVETVLMIYPDRATVCVSTQAGCGMGCVFCATGTLGLLRNLSSGEIVAQVIWASRELramgaaiskRHAG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 151 EEERVSHIVVMGIGEPFDNYNNVMDFLHVINDDKGMAIGARHITVSTSGLVPKIKKFAENGLQVNLAISLHAPNNEIRSS 230
Cdd:PRK14461  165 PVGRVTNLVFMGMGEPFANYDRWWQAVERLHDPQGFNLGARSMTVSTVGLVKGIRRLANERLPINLAISLHAPDDALRSE 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 231 IMRINRSFPIEKLMGAVDYYIEETNRRVTFEYIMLSGVNDQPEHAQQLADLMKDKKK----LVYVNLIPYNPVSeHDQYS 306
Cdd:PRK14461  245 LMPVNRRYPIADLMAATRDYIAKTRRRVSFEYVLLQGKNDHPEQAAALARLLRGEAPpgplLVHVNLIPWNPVP-GTPLG 323
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1655118514 307 RSSKAAVLRFYDVLKKNGINCVIRKEHGTDIDAACGQL 344
Cdd:PRK14461  324 RSERERVTTFQRILTDYGIPCTVRVERGVEIAAACGQL 361
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
108-271 1.94e-15

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: 72.94  E-value: 1.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 108 TQVGCNIGCTFCA---SGLLKKQRDLTAGEIVAQImlvqhyfdERGEEERVSHIVVMGiGEPFDNYNNVMDFLHVINDDk 184
Cdd:pfam04055   1 ITRGCNLRCTYCAfpsIRARGKGRELSPEEILEEA--------KELKRLGVEVVILGG-GEPLLLPDLVELLERLLKLE- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 185 gmAIGARHITVSTSGLVP---KIKKFAENGLqVNLAISLHAPNNEIRssiMRINRSFPIEKLMGAVDYYIEETNRRVTFE 261
Cdd:pfam04055  71 --LAEGIRITLETNGTLLdeeLLELLKEAGL-DRVSIGLESGDDEVL---KLINRGHTFEEVLEALELLREAGIPVVTDN 144
                         170
                  ....*....|
gi 1655118514 262 YIMLSGVNDQ 271
Cdd:pfam04055 145 IVGLPGETDE 154
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
111-299 7.35e-08

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: 52.34  E-value: 7.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 111 GCNIGCTFCASGLLKKQRDLTAGEIVAQIMLVqhyfdeRGEEERVSHIVVMGIGEPFDNYNNVMDFLHVINDDKGMaiga 190
Cdd:cd01335     6 GCNLNCGFCSNPASKGRGPESPPEIEEILDIV------LEAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGF---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 191 rHITVSTSGLVPK---IKKFAENGLqVNLAISLHAPNNEIRSSIMRINRSF-----PIEKLMgavdyyieETNRRVTFEY 262
Cdd:cd01335    76 -EISIETNGTLLTeelLKELKELGL-DGVGVSLDSGDEEVADKIRGSGESFkerleALKELR--------EAGLGLSTTL 145
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1655118514 263 IMLSGVNDQPEHAQQLADLmKDKKKLVYVNLIPYNPV 299
Cdd:cd01335   146 LVGLGDEDEEDDLEELELL-AEFRSPDRVSLFRLLPE 181
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
106-317 1.13e-04

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: 42.77  E-value: 1.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514  106 VTTQVGCNIGCTFCA-SGLLKKQRDLTAGEIVAQIMLVqhyfDERGEEERVSHIVVMGIGEPFDN-YNNVMDFLHVIN-- 181
Cdd:smart00729   5 YIITRGCPRRCTFCSfPSLRGKLRSRYLEALVREIELL----AEKGEKEGLVGTVFIGGGTPTLLsPEQLEELLEAIRei 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514  182 ----DDKGMAIGARHITVSTSglvpKIKKFAENGLQVnLAISLHAPNNEIRSsimRINRSFPIEKLMGAVDyYIEETNRR 257
Cdd:smart00729  81 lglaKDVEITIETRPDTLTEE----LLEALKEAGVNR-VSLGVQSGDDEVLK---AINRGHTVEDVLEAVE-LLREAGPI 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655118514  258 VTFEYIMLsGVNDQ-PEHAQQLADLMKDkKKLVYVNLIPYNPV------SEHDQYSRSSKAAVLRFY 317
Cdd:smart00729 152 KVSTDLIV-GLPGEtEEDFEETLKLLKE-LGPDRVSIFPLSPRpgtplaKMYKRLKPPTKEERAELL 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: 586.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514   6 IYGLRREELVEWFLEHGEKKFRATQVWEWLYRSRVTEFAQMSNLSKQTIALLEENFIINPLKQLVVQEASDGTVKYLFEL 85
Cdd:COG0820     1 LLGLTLEELEEFLAELGEKPFRAKQIFRWLYQKGVTDFDEMTNLPKALREKLAENFEIGLLEVVREQVSADGTRKYLFRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514  86 PDHLMIETVLMRQEYGLSVCVTTQVGCNIGCTFCASGLLKKQRDLTAGEIVAQIMLVQHYFDERGEeeRVSHIVVMGIGE 165
Cdd:COG0820    81 ADGNLVETVLIPYEDRGTLCVSSQVGCAMGCSFCATGKQGLVRNLTAGEIVGQVLLARRDLREGGR--RVTNIVFMGMGE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 166 PFDNYNNVMDFLHVINDDKGMAIGARHITVSTSGLVPKIKKFAENGLQVNLAISLHAPNNEIRSSIMRINRSFPIEKLMG 245
Cdd:COG0820   159 PLLNYDNVLKAIRILNDPEGLGISARRITVSTSGLVPGIRRLADEGLPVNLAVSLHAPNDELRDELMPINKKYPLEELLE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 246 AVDYYIEETNRRVTFEYIMLSGVNDQPEHAQQLADLMKDkkKLVYVNLIPYNPVSEHDqYSRSSKAAVLRFYDVLKKNGI 325
Cdd:COG0820   239 ACRRYPEKTGRRITFEYVLLKGVNDSPEDARELARLLKG--LPCKVNLIPFNPVPGSP-YKRPSPERIEAFADILEKAGI 315
                         330       340
                  ....*....|....*....|...
gi 1655118514 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 ...
2-348 3.90e-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: 442.33  E-value: 3.90e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514   2 ERPSIYGLRREELVEWFLEHGEKKFRATQVWEWLYRSRVTEFAQMSNLSKQTIALLEENFIINPLKQLVVQEASDGTVKY 81
Cdd:TIGR00048   5 GKPSLLDLTLQELRQWLKDLGEKPFRAKQIMKWLYHKGCDSFDDMTNLSKVLREKLNEVFEIRTPEIAHEQRSSDGTIKY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514  82 LFELPDHLMIETVLMRQEYGLSVCVTTQVGCNIGCTFCASGLLKKQRDLTAGEIVAQIMLVQHYFDERGEeeRVSHIVVM 161
Cdd:TIGR00048  85 LFALGDGQTIETVLIPEDDRATVCVSSQVGCALGCTFCATAKGGFNRNLEASEIIGQVLRVQKIVGETGE--RVSNVVFM 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 162 GIGEPFDNYNNVMDFLHVINDDKGMAIGARHITVSTSGLVPKIKKFAENGLQVNLAISLHAPNNEIRSSIMRINRSFPIE 241
Cdd:TIGR00048 163 GMGEPLLNLNEVVKAMEIMNDDFGFGISKRRITISTSGVVPKIDKLADKMLQVALAISLHAPNDEIRSSLMPINKKYNIE 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 242 KLMGAVDYYIEETNRRVTFEYIMLSGVNDQPEHAQQLADLMKDKKklVYVNLIPYNPVSEHDqYSRSSKAAVLRFYDVLK 321
Cdd:TIGR00048 243 TLLAAVRRYLEKTGRRVTFEYVLLDGVNDQVEHAEELAELLKGTK--CKVNLIPWNPFPEAD-YGRPSNSQIDRFAKVLM 319
                         330       340
                  ....*....|....*....|....*..
gi 1655118514 322 KNGINCVIRKEHGTDIDAACGQLRSKQ 348
Cdd:TIGR00048 320 SYGFTVTIRKSRGDDIDAACGQLRAKD 346
PRK14461 PRK14461
ribosomal RNA large subunit methyltransferase N; Provisional
1-344 3.78e-105

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 237718  Cd Length: 371  Bit Score: 313.36  E-value: 3.78e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514   1 MERPSIYGLRREELVEWFLEHGEKKFRATQVWEWLYRSRVTEFAQMSNLSKQTIALLEENFIINPLKQLVVQEASDG-TV 79
Cdd:PRK14461    5 MEQRNLYDLNLAELTELLTAWGQPAFRARQLYRHLYVNLADSVLAMTDLPLALRERLTAELPLSTLRLEQVQIGDNGlTR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514  80 KYLFELPDHLMIETVLMRQEYGLSVCVTTQVGCNIGCTFCASGLLKKQRDLTAGEIVAQIMLVQHYF---------DERG 150
Cdd:PRK14461   85 KALFRLPDGAVVETVLMIYPDRATVCVSTQAGCGMGCVFCATGTLGLLRNLSSGEIVAQVIWASRELramgaaiskRHAG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 151 EEERVSHIVVMGIGEPFDNYNNVMDFLHVINDDKGMAIGARHITVSTSGLVPKIKKFAENGLQVNLAISLHAPNNEIRSS 230
Cdd:PRK14461  165 PVGRVTNLVFMGMGEPFANYDRWWQAVERLHDPQGFNLGARSMTVSTVGLVKGIRRLANERLPINLAISLHAPDDALRSE 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 231 IMRINRSFPIEKLMGAVDYYIEETNRRVTFEYIMLSGVNDQPEHAQQLADLMKDKKK----LVYVNLIPYNPVSeHDQYS 306
Cdd:PRK14461  245 LMPVNRRYPIADLMAATRDYIAKTRRRVSFEYVLLQGKNDHPEQAAALARLLRGEAPpgplLVHVNLIPWNPVP-GTPLG 323
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1655118514 307 RSSKAAVLRFYDVLKKNGINCVIRKEHGTDIDAACGQL 344
Cdd:PRK14461  324 RSERERVTTFQRILTDYGIPCTVRVERGVEIAAACGQL 361
PRK11194 PRK11194
ribosomal RNA large subunit methyltransferase N; Provisional
9-351 6.55e-102

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 183031  Cd Length: 372  Bit Score: 305.11  E-value: 6.55e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514   9 LRREELVEWFLEHGEKKFRATQVWEWLYRSRVTEFAQMSNLSKQTIALLEENFIINPLKQLVVQEASDGTVKYLFELPDH 88
Cdd:PRK11194   11 LNRQQMREFFAELGEKPFRADQVMKWIYHYGCDDFDEMTNINKVLREKLKEVAEIRAPEVAEEQRSSDGTIKWAIAVGDQ 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514  89 lMIETVLMRQEYGLSVCVTTQVGCNIGCTFCASGLLKKQRDLTAGEIVAQIMLVQHYFDERGEEER--VSHIVVMGIGEP 166
Cdd:PRK11194   91 -RVETVYIPEDDRATLCVSSQVGCALECKFCSTAQQGFNRNLRVSEIIGQVWRAAKIIGAAKVTGQrpITNVVMMGMGEP 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 167 FDNYNNVMDFLHVINDDKGMAIGARHITVSTSGLVPKIKKFAENgLQVNLAISLHAPNNEIRSSIMRINRSFPIEKLMGA 246
Cdd:PRK11194  170 LLNLNNVVPAMEIMLDDFGFGLSKRRVTLSTSGVVPALDKLGDM-IDVALAISLHAPNDELRDEIVPINKKYNIETFLAA 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 247 VDYYIEETNR---RVTFEYIMLSGVNDQPEHAQQLADLMKDKKklVYVNLIPYNPVSEHDqYSRSSKAAVLRFYDVLKKN 323
Cdd:PRK11194  249 VRRYLEKSNAnqgRVTVEYVMLDHVNDGTEHAHQLAELLKDTP--CKINLIPWNPFPGAP-YGRSSNSRIDRFSKVLMEY 325
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1655118514 324 GINCVIRKEHGTDIDAACGQL------RSKQMKK 351
Cdd:PRK11194  326 GFTVIVRKTRGDDIDAACGQLagdvidRTKRTLK 359
PRK14453 PRK14453
chloramphenicol/florfenicol resistance protein; Provisional
23-344 2.29e-89

chloramphenicol/florfenicol resistance protein; Provisional


Pssm-ID: 184685  Cd Length: 347  Bit Score: 272.00  E-value: 2.29e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514  23 EKKFRATQVWEWLYRSRVTEFAQMSNLSKQTIALLEENF-----IINPLKQLVVQEASdgtvKYLFELPDHLMIETVLMR 97
Cdd:PRK14453   19 LPDYRYEQITKAIFKQRIDNFEDMHILPKALRESLINEFgknvlSVIPVFEQDSKQVT----KVLFELTDGERIEAVGLK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514  98 QEYGL-SVCVTTQVGCNIGCTFCASGLLKKQRDLTAGEIVAQIMlvqhYFDERGEeeRVSHIVVMGIGEPFDNyNNVMDF 176
Cdd:PRK14453   95 YKQGWeSFCISSQCGCGFGCRFCATGSIGLKRNLTADEITDQLL----YFYLNGH--RLDSISFMGMGEALAN-PELFDA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 177 LHVINDDKGMAIGARHITVSTSGLVPKIKKFAENGLQVNLAISLHAPNNEIRSSIMRINRSFPIEKLMGAVDYYIEETNR 256
Cdd:PRK14453  168 LKILTDPNLFGLSQRRITISTIGIIPGIQRLTQEFPQVNLTFSLHSPFESQRSELMPINKRFPLNEVMKTLDEHIRHTGR 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 257 RVTFEYIMLSGVNDQPEHAQQLADLMKDKKK---LVYVNLIPYNP-VSEHDQYSRSSKAAVLRFYDVLKKNGINCVIRKE 332
Cdd:PRK14453  248 KVYIAYIMLEGVNDSKEHAEAVVGLLRNRGSwehLYHVNLIPYNStDKTPFKFQSSSAGQIKQFCSTLKSAGISVTVRTQ 327
                         330
                  ....*....|..
gi 1655118514 333 HGTDIDAACGQL 344
Cdd:PRK14453  328 FGSDISAACGQL 339
PRK14470 PRK14470
ribosomal RNA large subunit methyltransferase N; Provisional
66-348 2.71e-54

ribosomal RNA large subunit methyltransferase N; Provisional


Pssm-ID: 172945  Cd Length: 336  Bit Score: 181.67  E-value: 2.71e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514  66 LKQLVVQEASDGTVKYLFELPDHLMIETV---LMRQEYglSVCVTTQVGCNIGCTFCASGLLKKQRDLTAGEIVAQIMLV 142
Cdd:PRK14470   60 LRLVERVDAKDGFRKYLFELPDGLRVEAVripLFDTHH--VVCLSSQAGCALGCAFCATGKLGLDRSLRSWEIVAQLLAV 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 143 qhyfdeRGEEER-VSHIVVMGIGEPFDNYNNVMDFLHVINDDKGMAIGARHITVSTSGLVPKIKKFAENGLQVNLAISLH 221
Cdd:PRK14470  138 ------RADSERpITGVVFMGQGEPFLNYDEVLRAAYALCDPAGARIDGRRISISTAGVVPMIRRYTAEGHKFRLCISLN 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 222 APNNEIRSSIMRINRSFPIEKLMGAVDYYiEETNRRVTFEYIMLSGVNDQPEHAQQLADLMKDKKklVYVNLIPYNPVSe 301
Cdd:PRK14470  212 AAIPWKRRALMPIEQGFPLDELVEAIREH-AALRGRVTLEYVMISGVNVGEEDAAALGRLLAGIP--VRLNPIAVNDAT- 287
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1655118514 302 hDQYSRSSKAAVLRFYDVLKKN--GINCVIRKEHGTDIDAACGQLRSKQ 348
Cdd:PRK14470  288 -GRYRPPDEDEWNAFRDALARElpGTPVVRRYSGGQDEHAACGMLASRR 335
PRK14464 PRK14464
RNA methyltransferase;
74-354 1.00e-45

RNA methyltransferase;


Pssm-ID: 184691  Cd Length: 344  Bit Score: 159.12  E-value: 1.00e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514  74 ASDGTVKYLFELPDHLMIETVLMRQEyGLsvCVTTQVGCNIGCTFCA---SGLLkkqRDLTAGEIVAQIMLVQHYfderg 150
Cdd:PRK14464   71 GEDGSARLLVELADGQMVESVLLPRD-GL--CVSTQVGCAVGCVFCMtgrSGLL---RQLGSAEIVAQVVLARRR----- 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 151 eeERVSHIVVMGIGEPFDNYNNVMDFLHVINDDKGmaIGARHITVSTSGLVPKIKKFAENGLQVNLAISLHAPNNEIRSS 230
Cdd:PRK14464  140 --RAVKKVVFMGMGEPAHNLDNVLEAIDLLGTEGG--IGHKNLVFSTVGDPRVFERLPQQRVKPALALSLHTTRAELRAR 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 231 IMRINRSFPIEKLMGAVDYYIEETNRRVTFEYIMLSGVNDQPEHAQQLADLMKDKKKLvyVNLIPYNPVsEHDQYSRSSK 310
Cdd:PRK14464  216 LLPRAPRIAPEELVELGEAYARATGYPIQYQWTLLEGVNDSDEEMDGIVRLLKGKYAV--MNLIPYNSV-DGDAYRRPSG 292
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1655118514 311 AAVLRFYDVLKKNGINCVIRKEHGTDIDAACGQLRSKQMKKAAV 354
Cdd:PRK14464  293 ERIVAMARYLHRRGVLTKVRNSAGQDVDGGCGQLRARAAKAAAV 336
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
108-271 1.94e-15

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: 72.94  E-value: 1.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 108 TQVGCNIGCTFCA---SGLLKKQRDLTAGEIVAQImlvqhyfdERGEEERVSHIVVMGiGEPFDNYNNVMDFLHVINDDk 184
Cdd:pfam04055   1 ITRGCNLRCTYCAfpsIRARGKGRELSPEEILEEA--------KELKRLGVEVVILGG-GEPLLLPDLVELLERLLKLE- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 185 gmAIGARHITVSTSGLVP---KIKKFAENGLqVNLAISLHAPNNEIRssiMRINRSFPIEKLMGAVDYYIEETNRRVTFE 261
Cdd:pfam04055  71 --LAEGIRITLETNGTLLdeeLLELLKEAGL-DRVSIGLESGDDEVL---KLINRGHTFEEVLEALELLREAGIPVVTDN 144
                         170
                  ....*....|
gi 1655118514 262 YIMLSGVNDQ 271
Cdd:pfam04055 145 IVGLPGETDE 154
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
110-334 3.43e-09

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 56.73  E-value: 3.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 110 VGCNIGCTFCA------SGLLKKQRDLTAGEIVAQIMLVQHYFDERGeeervsHIVVMGiGEPFDNYNNVMDFLHVIndd 183
Cdd:COG1180    29 QGCNLRCPYCHnpeisqGRPDAAGRELSPEELVEEALKDRGFLDSCG------GVTFSG-GEPTLQPEFLLDLAKLA--- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 184 KGMAIgarHITVSTSGLVPK--IKKFAENglqVNL-AISLHAPNNE-----IRSSIMRINRSfpIEklmgavdyYIEETN 255
Cdd:COG1180    99 KELGL---HTALDTNGYIPEeaLEELLPY---LDAvNIDLKAFDDEfyrklTGVSLEPVLEN--LE--------LLAESG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 256 RRVTFEYIMLSGVNDQPEHAQQLADLMKDKKKLVYVNLIPYNPVSEHDQYSRSSKAAVLRFYDVLKKNGI-NCVIRKEHG 334
Cdd:COG1180   163 VHVEIRTLVIPGLNDSEEELEAIARFIAELGDVIPVHLLPFHPLYKLEDVPPPSPETLERAREIAREYGLkYVYIGNVPG 242
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
112-253 7.05e-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: 7.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 112 CNIGCTFC-ASGLLKKQRDLTAGEIVAQImlvqhyfdERGEEERVSHIVVMGiGEPFDNyNNVMDFLHVINdDKGMaiga 190
Cdd:COG0535    10 CNLRCKHCyADAGPKRPGELSTEEAKRIL--------DELAELGVKVVGLTG-GEPLLR-PDLFELVEYAK-ELGI---- 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655118514 191 rHITVSTSGLV---PKIKKFAENGLQVnLAISLHAPNNEIRSSIMRINRSFpiEKLMGAVDYYIEE 253
Cdd:COG0535    75 -RVNLSTNGTLlteELAERLAEAGLDH-VTISLDGVDPETHDKIRGVPGAF--DKVLEAIKLLKEA 136
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
111-299 7.35e-08

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: 52.34  E-value: 7.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 111 GCNIGCTFCASGLLKKQRDLTAGEIVAQIMLVqhyfdeRGEEERVSHIVVMGIGEPFDNYNNVMDFLHVINDDKGMaiga 190
Cdd:cd01335     6 GCNLNCGFCSNPASKGRGPESPPEIEEILDIV------LEAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGF---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 191 rHITVSTSGLVPK---IKKFAENGLqVNLAISLHAPNNEIRSSIMRINRSF-----PIEKLMgavdyyieETNRRVTFEY 262
Cdd:cd01335    76 -EISIETNGTLLTeelLKELKELGL-DGVGVSLDSGDEEVADKIRGSGESFkerleALKELR--------EAGLGLSTTL 145
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1655118514 263 IMLSGVNDQPEHAQQLADLmKDKKKLVYVNLIPYNPV 299
Cdd:cd01335   146 LVGLGDEDEEDDLEELELL-AEFRSPDRVSLFRLLPE 181
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
106-317 1.13e-04

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: 42.77  E-value: 1.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514  106 VTTQVGCNIGCTFCA-SGLLKKQRDLTAGEIVAQIMLVqhyfDERGEEERVSHIVVMGIGEPFDN-YNNVMDFLHVIN-- 181
Cdd:smart00729   5 YIITRGCPRRCTFCSfPSLRGKLRSRYLEALVREIELL----AEKGEKEGLVGTVFIGGGTPTLLsPEQLEELLEAIRei 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514  182 ----DDKGMAIGARHITVSTSglvpKIKKFAENGLQVnLAISLHAPNNEIRSsimRINRSFPIEKLMGAVDyYIEETNRR 257
Cdd:smart00729  81 lglaKDVEITIETRPDTLTEE----LLEALKEAGVNR-VSLGVQSGDDEVLK---AINRGHTVEDVLEAVE-LLREAGPI 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655118514  258 VTFEYIMLsGVNDQ-PEHAQQLADLMKDkKKLVYVNLIPYNPV------SEHDQYSRSSKAAVLRFY 317
Cdd:smart00729 152 KVSTDLIV-GLPGEtEEDFEETLKLLKE-LGPDRVSIFPLSPRpgtplaKMYKRLKPPTKEERAELL 216
YgiQ COG1032
Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];
95-333 1.28e-03

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


Pssm-ID: 440655 [Multi-domain]  Cd Length: 394  Bit Score: 40.31  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514  95 LMRQEYGLSVCVTTQVGCNIGCTFCASGLL--KKQRDLTAGEIVAQI-MLVQHYfdergeeeRVSHIVVMGiGEPFDNYN 171
Cdd:COG1032   167 LDLEAYHRRASIETSRGCPFGCSFCSISALygRKVRYRSPESVVEEIeELVKRY--------GIREIFFVD-DNFNVDKK 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 172 NVMDFLHVINdDKGMAIGArHITVSTSGLVPK-IKKFAENGL-QVNLAISlhAPNNEIRSsimRINRSFPIEKLMGAVDy 249
Cdd:COG1032   238 RLKELLEELI-ERGLNVSF-PSEVRVDLLDEElLELLKKAGCrGLFIGIE--SGSQRVLK---AMNKGITVEDILEAVR- 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 250 YIEETNRRVTFeYIMLSGVNDQPEHAQQLADLMKD-KKKLVYVN-LIPYnPVSEhdqysrsskaavlrFYDVLKKNGINC 327
Cdd:COG1032   310 LLKKAGIRVKL-YFIIGLPGETEEDIEETIEFIKElGPDQAQVSiFTPL-PGTP--------------LYEELEKEGRLY 373

                  ....*.
gi 1655118514 328 VIRKEH 333
Cdd:COG1032   374 DWEKYE 379
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
111-295 1.50e-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: 39.35  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 111 GCNIGCTFC--------ASGllkkqRDLTAGEIVAQImlvqhyfdergEEERVSHIVVMGiGEPF--DNYNNVMDFLHvi 180
Cdd:COG0602    29 GCNLRCSWCdtkyawdgEGG-----KRMSAEEILEEV-----------AALGARHVVITG-GEPLlqDDLAELLEALK-- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655118514 181 ndDKGMaigarHITVSTSGLVPK----------IKKFAENGLQVNLA-ISLHAPNNEIRssimrinrsFPIeklMGAVDY 249
Cdd:COG0602    90 --DAGY-----EVALETNGTLPIpagidwvtvsPKLPSSGEEEDNREnLEVLRRADELK---------FVV---ADETDL 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1655118514 250 -YIEETNRRVTFE---YIMLSGVNDQPEHAQQLADLMKDKKKlvyVNLIP 295
Cdd:COG0602   151 eEAEELLARLDFRcpvYLQPVWGNKLEENTELLAEWCLAHPN---VRLSP 197
Fer4_14 pfam13394
4Fe-4S single cluster domain;
111-172 9.51e-03

4Fe-4S single cluster domain;


Pssm-ID: 433171 [Multi-domain]  Cd Length: 115  Bit Score: 35.80  E-value: 9.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655118514 111 GCNIGCTFCasgLLKKQRDLTAGEIVAQIMLVQHYFDERGEEERVSHIVVMGiGEPFDNYNN 172
Cdd:pfam13394   5 GCNHSCPGC---DNKETWKFNYGEPFTEELEDQIIADLKDSYIKRQGLVLTG-GEPLHPWNL 62
 
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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