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Conserved domains on  [gi|2417049477|ref|WP_269457050|]
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peptide chain release factor N(5)-glutamine methyltransferase [Brevefilum fermentans]

Protein Classification

N5-glutamine methyltransferase family protein( domain architecture ID 11458394)

N5-glutamine methyltransferase family protein such as peptide chain release factor N(5)-glutamine methyltransferase, which modifies the glutamine residue in the universally conserved glycylglycylglutamine (GGQ) motif of peptide chain release factor, resulting in almost complete loss of release activity

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:0003676|GO:0032259|GO:1904047
PubMed:  12826405|12504684|12741815
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 2-264 7.24e-96

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


:

Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 282.81  E-value: 7.24e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477   2 AQADCEAPGQISLVLLQHVLKQSKSWVLSHSEYRLTPQEHEALQESLDHFLKGVPLPYILGYWEFFGRTFQLTPDVLIPR 81
Cdd:COG2890    15 AAAGVDSARLEAELLLAHVLGLDRADLLLHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFYGLEFKVDPGVLIPR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  82 PETEMLVEFALQHAQGLHSCRIIDIGTGSGCIAISLAAELPEATVFGVDLSMAALRIAQKNARYHNLPH-IHFIQADLLS 160
Cdd:COG2890    95 PETEELVELALALLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLGLEDrVRFLQGDLFE 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477 161 SFST--QFDLICANLPYIPTRTLDALP--VSRWEPRLALDGGQSGMETIRRLLVQAKTRMAPNSVLLLEVestlGASTLA 236
Cdd:COG2890   175 PLPGdgRFDLIVSNPPYIPEDEIALLPpeVRDHEPRLALDGGEDGLDFYRRIIAQAPRLLKPGGWLLLEI----GEDQGE 250

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2417049477 237 SAQEVFPNA-YHQ--LVPDLTGLDRMIKIQL 264
Cdd:COG2890   251 AVRALLEAAgFADveTHKDLAGRDRVVVARR 281
 
Name Accession Description Interval E-value
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 2-264 7.24e-96

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 282.81  E-value: 7.24e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477   2 AQADCEAPGQISLVLLQHVLKQSKSWVLSHSEYRLTPQEHEALQESLDHFLKGVPLPYILGYWEFFGRTFQLTPDVLIPR 81
Cdd:COG2890    15 AAAGVDSARLEAELLLAHVLGLDRADLLLHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFYGLEFKVDPGVLIPR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  82 PETEMLVEFALQHAQGLHSCRIIDIGTGSGCIAISLAAELPEATVFGVDLSMAALRIAQKNARYHNLPH-IHFIQADLLS 160
Cdd:COG2890    95 PETEELVELALALLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLGLEDrVRFLQGDLFE 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477 161 SFST--QFDLICANLPYIPTRTLDALP--VSRWEPRLALDGGQSGMETIRRLLVQAKTRMAPNSVLLLEVestlGASTLA 236
Cdd:COG2890   175 PLPGdgRFDLIVSNPPYIPEDEIALLPpeVRDHEPRLALDGGEDGLDFYRRIIAQAPRLLKPGGWLLLEI----GEDQGE 250

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2417049477 237 SAQEVFPNA-YHQ--LVPDLTGLDRMIKIQL 264
Cdd:COG2890   251 AVRALLEAAgFADveTHKDLAGRDRVVVARR 281
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 2-264 1.28e-93

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 277.04  E-value: 1.28e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477   2 AQADCEAPGQISLVLLQHVLKQSKSWVLSHSEYRLTPQEHEALQESLDHFLKGVPLPYILGYWEFFGRTFQLTPDVLIPR 81
Cdd:PRK09328   11 ATARLASPRLDAELLLAHVLGLSRTDLLLNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFWGLDFKVSPGVLIPR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  82 PETEMLVEFALQHAQGLHSCRIIDIGTGSGCIAISLAAELPEATVFGVDLSMAALRIAQKNARYHNLPHIHFIQADLLSS 161
Cdd:PRK09328   91 PETEELVEWALEALLLKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGLGARVEFLQGDWFEP 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477 162 FST-QFDLICANLPYIPTRTLDALP--VSRWEPRLALDGGQSGMETIRRLLVQAKTRMAPNSVLLLEVestlGASTLASA 238
Cdd:PRK09328  171 LPGgRFDLIVSNPPYIPEADIHLLQpeVRDHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGWLLLEI----GYDQGEAV 246

                         250       260
                  ....*....|....*....|....*....
gi 2417049477 239 QEVF-PNAYHQL--VPDLTGLDRMIKIQL 264
Cdd:PRK09328  247 RALLaAAGFADVetRKDLAGRDRVVLGRR 275
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 15-260 2.45e-91

protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein family are HemK (PrmC), a protein once thought to be involved in heme biosynthesis but now recognized to be a protein-glutamine methyltransferase that modifies the peptide chain release factors. All members of the seed alignment are encoded next to the release factor 1 gene (prfA) and confirmed by phylogenetic analysis. SIMBAL analysis (manuscript in prep.) shows the motif [LIV]PRx[DE]TE (in Escherichia coli, IPRPDTE) confers specificity for the release factors rather than for ribosomal protein L3. [Protein fate, Protein modification and repair]


Pssm-ID: 274634 [Multi-domain]  Cd Length: 250  Bit Score: 270.11  E-value: 2.45e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  15 VLLQHVLKQSKSWVLSHSEYRLTPQEHEALQESLDHFLKGVPLPYILGYWEFFGRTFQLTPDVLIPRPETEMLVEFALQH 94
Cdd:TIGR03534   4 LLLAHVLGKDRAQLLLHPEDELTPEELAAFDALLARRAAGEPVAYILGEREFYGLDFKVSPGVLIPRPETEELVEAALER 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  95 AQGLHscRIIDIGTGSGCIAISLAAELPEATVFGVDLSMAALRIAQKNARYHNLPHIHFIQADLLSSF-STQFDLICANL 173
Cdd:TIGR03534  84 LKKGP--RVLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKNARRLGLENVEFLQGDWFEPLpSGKFDLIVSNP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477 174 PYIPTRTLDALP--VSRWEPRLALDGGQSGMETIRRLLVQAKTRMAPNSVLLLEVESTLGASTLASAQEvFPNAYHQLVP 251
Cdd:TIGR03534 162 PYIPEADIHLLDpeVRDFEPRLALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFEA-AGFADVETRK 240


                  ....*....
gi 2417049477 252 DLTGLDRMI 260
Cdd:TIGR03534 241 DLAGKDRVV 249
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 89-235 1.18e-16

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 75.32  E-value: 1.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  89 EFALQHAQGLHSCRIIDIGTGSGCIAISLAAELPEATVFGVDLSMAALRIAQKNARYHNLPHIHFIQADLLSSFST-QFD 167
Cdd:pfam05175  21 RLLLEHLPKDLSGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGLENGEVVASDVYSGVEDgKFD 100

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2417049477 168 LICANLPYiptrtldalpvsrweprlaLDGGQSGMETIRRLLVQAKTRMAPNSVLLLEVESTLGASTL 235
Cdd:pfam05175 101 LIISNPPF-------------------HAGLATTYNVAQRFIADAKRHLRPGGELWIVANRFLGYPPL 149
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 102-227 2.86e-11

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 58.98  E-value: 2.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477 102 RIIDIGTGSGCIAISLAaELPEATVFGVDLSMAALRIAQKNARYHNLPHIHFIQADLLSSFS---TQFDLICANLPYipt 178
Cdd:cd02440     1 RVLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeadESFDVIISDPPL--- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2417049477 179 rtldalpvsrweprlaldggQSGMETIRRLLVQAKTRMAPNSVLLLEVE 227
Cdd:cd02440    77 --------------------HHLVEDLARFLEEARRLLKPGGVLVLTLV 105
 
Name Accession Description Interval E-value
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 2-264 7.24e-96

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 282.81  E-value: 7.24e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477   2 AQADCEAPGQISLVLLQHVLKQSKSWVLSHSEYRLTPQEHEALQESLDHFLKGVPLPYILGYWEFFGRTFQLTPDVLIPR 81
Cdd:COG2890    15 AAAGVDSARLEAELLLAHVLGLDRADLLLHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFYGLEFKVDPGVLIPR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  82 PETEMLVEFALQHAQGLHSCRIIDIGTGSGCIAISLAAELPEATVFGVDLSMAALRIAQKNARYHNLPH-IHFIQADLLS 160
Cdd:COG2890    95 PETEELVELALALLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLGLEDrVRFLQGDLFE 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477 161 SFST--QFDLICANLPYIPTRTLDALP--VSRWEPRLALDGGQSGMETIRRLLVQAKTRMAPNSVLLLEVestlGASTLA 236
Cdd:COG2890   175 PLPGdgRFDLIVSNPPYIPEDEIALLPpeVRDHEPRLALDGGEDGLDFYRRIIAQAPRLLKPGGWLLLEI----GEDQGE 250

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2417049477 237 SAQEVFPNA-YHQ--LVPDLTGLDRMIKIQL 264
Cdd:COG2890   251 AVRALLEAAgFADveTHKDLAGRDRVVVARR 281
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 2-264 1.28e-93

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 277.04  E-value: 1.28e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477   2 AQADCEAPGQISLVLLQHVLKQSKSWVLSHSEYRLTPQEHEALQESLDHFLKGVPLPYILGYWEFFGRTFQLTPDVLIPR 81
Cdd:PRK09328   11 ATARLASPRLDAELLLAHVLGLSRTDLLLNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFWGLDFKVSPGVLIPR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  82 PETEMLVEFALQHAQGLHSCRIIDIGTGSGCIAISLAAELPEATVFGVDLSMAALRIAQKNARYHNLPHIHFIQADLLSS 161
Cdd:PRK09328   91 PETEELVEWALEALLLKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGLGARVEFLQGDWFEP 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477 162 FST-QFDLICANLPYIPTRTLDALP--VSRWEPRLALDGGQSGMETIRRLLVQAKTRMAPNSVLLLEVestlGASTLASA 238
Cdd:PRK09328  171 LPGgRFDLIVSNPPYIPEADIHLLQpeVRDHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGWLLLEI----GYDQGEAV 246

                         250       260
                  ....*....|....*....|....*....
gi 2417049477 239 QEVF-PNAYHQL--VPDLTGLDRMIKIQL 264
Cdd:PRK09328  247 RALLaAAGFADVetRKDLAGRDRVVLGRR 275
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 15-260 2.45e-91

protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein family are HemK (PrmC), a protein once thought to be involved in heme biosynthesis but now recognized to be a protein-glutamine methyltransferase that modifies the peptide chain release factors. All members of the seed alignment are encoded next to the release factor 1 gene (prfA) and confirmed by phylogenetic analysis. SIMBAL analysis (manuscript in prep.) shows the motif [LIV]PRx[DE]TE (in Escherichia coli, IPRPDTE) confers specificity for the release factors rather than for ribosomal protein L3. [Protein fate, Protein modification and repair]


Pssm-ID: 274634 [Multi-domain]  Cd Length: 250  Bit Score: 270.11  E-value: 2.45e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  15 VLLQHVLKQSKSWVLSHSEYRLTPQEHEALQESLDHFLKGVPLPYILGYWEFFGRTFQLTPDVLIPRPETEMLVEFALQH 94
Cdd:TIGR03534   4 LLLAHVLGKDRAQLLLHPEDELTPEELAAFDALLARRAAGEPVAYILGEREFYGLDFKVSPGVLIPRPETEELVEAALER 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  95 AQGLHscRIIDIGTGSGCIAISLAAELPEATVFGVDLSMAALRIAQKNARYHNLPHIHFIQADLLSSF-STQFDLICANL 173
Cdd:TIGR03534  84 LKKGP--RVLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKNARRLGLENVEFLQGDWFEPLpSGKFDLIVSNP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477 174 PYIPTRTLDALP--VSRWEPRLALDGGQSGMETIRRLLVQAKTRMAPNSVLLLEVESTLGASTLASAQEvFPNAYHQLVP 251
Cdd:TIGR03534 162 PYIPEADIHLLDpeVRDFEPRLALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFEA-AGFADVETRK 240


                  ....*....
gi 2417049477 252 DLTGLDRMI 260
Cdd:TIGR03534 241 DLAGKDRVV 249
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 7-258 1.01e-66

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 208.75  E-value: 1.01e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477   7 EAPGQISLVLLQHVLKQSKSWVLSHSEYRLTPQEHEALQESLDHFLKGVPLPYILGYWEFFGRTFQLTPDVLIPRPETEM 86
Cdd:TIGR00536  21 ENPWLEALLLLEHDLGRERDLLLAFLTEELTPDEKERIFRLVLRRVKGVPVAYLLGSKEFYGLEFFVNEHVLIPRPETEE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  87 LVEFAL-QHAQGLHSCRIIDIGTGSGCIAISLAAELPEATVFGVDLSMAALRIAQKNARYHNLPH-IHFIQADLLSSF-S 163
Cdd:TIGR00536 101 LVEKALaSLISQPPILHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQLEHrVEFIQSNLFEPLaG 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477 164 TQFDLICANLPYIPTRTLDALP-VSRWEPRLALDGGQSGMETIRRLLVQAKTRMAPNSVLLLEVestlGASTLASAQEV- 241
Cdd:TIGR00536 181 QKIDIIVSNPPYIDEEDLADLPnVVRFEPLLALVGGDDGLNILRQIIELAPDYLKPNGFLVCEI----GNWQQKSLKELl 256

                         250       260
                  ....*....|....*....|
gi 2417049477 242 -FPNAYH--QLVPDLTGLDR 258
Cdd:TIGR00536 257 rIKFTWYdvENGRDLNGKER 276
L3_gln_methyl TIGR03533
protein-(glutamine-N5) methyltransferase, ribosomal protein L3-specific; Members of this ...
 35-226 3.15e-39

protein-(glutamine-N5) methyltransferase, ribosomal protein L3-specific; Members of this protein family methylate ribosomal protein L3 on a glutamine side chain. This family is related to HemK, a protein-glutamine methyltranferase for peptide chain release factors. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 274633 [Multi-domain]  Cd Length: 284  Bit Score: 138.03  E-value: 3.15e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  35 RLTPQEHEALqesLDHFLKGV----PLPYILGYWEFFGRTFQLTPDVLIPR-PETEMLVE-FA-LQHAQGLHscRIIDIG 107
Cdd:TIGR03533  55 RLTPSEKERI---LELIERRIeeriPVAYLTNEAWFAGLEFYVDERVLIPRsPIAELIEDgFApWLEPEPVK--RILDLC 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477 108 TGSGCIAISLAAELPEATVFGVDLSMAALRIAQKNARYHNLPH-IHFIQADLLSSFSTQ-FDLICANLPYIPTRTLDALP 185
Cdd:TIGR03533 130 TGSGCIAIACAYAFPEAEVDAVDISPDALAVAEINIERHGLEDrVTLIQSDLFAALPGRkYDLIVSNPPYVDAEDMADLP 209

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2417049477 186 VS-RWEPRLALDGGQSGMETIRRLLVQAKTRMAPNSVLLLEV 226
Cdd:TIGR03533 210 AEyHHEPELALASGEDGLDLVRRILAEAADHLNENGVLVVEV 251
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
 9-266 3.22e-38

bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) methyltransferase; Reviewed


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 140.00  E-value: 3.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477   9 PGQISLVLLQHVLKQSKSWVLSHSEYRLTPQEHEALQESLDHFLKGVPLPYILGYWEFFGRTFQLTPDVLIPRPETEMLV 88
Cdd:PRK01544   24 PQLEARILLQHVINKPIEYLLINLDEQLNEAEIEAFEKLLERRLKHEPIAYITGVKEFYSREFIVNKHVLIPRSDTEVLV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  89 EFALQHAQG---------LHSC---------------RIIDIGTGSGCIAISLAAELPEATVFGVDLSMAALRIAQKNA- 143
Cdd:PRK01544  104 DVVFQCHSResgnpekkqLNPCfrgndissncndkflNILELGTGSGCIAISLLCELPNANVIATDISLDAIEVAKSNAi 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477 144 RYHNLPHIHFIQADLLSSFSTQ-FDLICANLPYIPT--RTLDALPVSRWEPRLALDGGQSGMETIRRLLVQAKTRMAPNS 220
Cdd:PRK01544  184 KYEVTDRIQIIHSNWFENIEKQkFDFIVSNPPYISHseKSEMAIETINYEPSIALFAEEDGLQAYFIIAENAKQFLKPNG 263

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2417049477 221 VLLLEVestlGASTLASAQEVFPN-AYH--QLVPDLTGLDRMIKIQLIS 266
Cdd:PRK01544  264 KIILEI----GFKQEEAVTQIFLDhGYNieSVYKDLQGHSRVILISPIN 308
PRK14966 PRK14966
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; ...
 9-259 1.17e-31

unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; Provisional


Pssm-ID: 184930 [Multi-domain]  Cd Length: 423  Bit Score: 120.96  E-value: 1.17e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477   9 PGQISLVLLQHVLKQSKSWVLSHSEYRLTPQEHEALQESLDHFLKGVPLPYILGYWEFFGRTFQLTPDVLIPRPETEMLV 88
Cdd:PRK14966  163 PKNEARMLLQYASEYTRVQLLTRGGEEMPDEVRQRADRLAQRRLNGEPVAYILGVREFYGRRFAVNPNVLIPRPETEHLV 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  89 EFALqhAQGLHSCRIIDIGTGSGCIAISLAAELPEATVFGVDLSMAALRIAQKNA----RYHNLPHIHFIQADLLSsfST 164
Cdd:PRK14966  243 EAVL--ARLPENGRVWDLGTGSGAVAVTVALERPDAFVRASDISPPALETARKNAadlgARVEFAHGSWFDTDMPS--EG 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477 165 QFDLICANLPYIPT--RTLDALPVsRWEPRLALDGGQSGMETIRRLLVQAKTRMAPNSVLLLEVESTLGASTLASAQEvf 242
Cdd:PRK14966  319 KWDIIVSNPPYIENgdKHLLQGDL-RFEPQIALTDFSDGLSCIRTLAQGAPDRLAEGGFLLLEHGFDQGAAVRGVLAE-- 395

                         250
                  ....*....|....*....
gi 2417049477 243 pNAYH--QLVPDLTGLDRM 259
Cdd:PRK14966  396 -NGFSgvETLPDLAGLDRV 413
PrmC_rel_meth TIGR03704
putative protein-(glutamine-N5) methyltransferase, unknown substrate-specific; This protein ...
 37-238 1.02e-28

putative protein-(glutamine-N5) methyltransferase, unknown substrate-specific; This protein family is closely related to two different families of protein-(glutamine-N5) methyltransferase. The first is PrmB, which modifies ribosomal protein L3 in some bacteria. The second is PrmC (HemK), which modifies peptide chain release factors 1 and 2 in most bacteria and also in eukaryotes. The glutamine side chain-binding motif NPPY shared by PrmB and PrmC is N[VAT]PY in this family. The protein substrate is unknown. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 274733 [Multi-domain]  Cd Length: 251  Bit Score: 109.49  E-value: 1.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  37 TPQEheaLQESLDHFLKGVPLPYILGYWEFFGRTFQLTPDVLIPRPETEMLVEFALQHAQGLHSCR-IIDIGTGSGCIAI 115
Cdd:TIGR03704  26 TPGE---LAAMVDRRVAGLPLEHVLGWAEFCGLRIAVDPGVFVPRRRTEFLVDEAAALARPRSGTLvVVDLCCGSGAVGA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477 116 SLAAELPEATVFGVDLSMAALRIAQKNARYHNlPHIHfiQADLLSSFSTQF----DLICANLPYIPTRTLDALP--VSRW 189
Cdd:TIGR03704 103 ALAAALDGIELHAADIDPAAVRCARRNLADAG-GTVH--EGDLYDALPTALrgrvDILAANAPYVPTDAIALMPpeARDH 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2417049477 190 EPRLALDGGQSGMETIRRLLVQAKTRMAPNSVLLLEV---ESTLGASTLASA 238
Cdd:TIGR03704 180 EPRVALDGGADGLDVLRRVAAGAPDWLAPGGHLLVETserQAPLAVEAFARA 231
PRK14968 PRK14968
putative methyltransferase; Provisional
 73-262 4.63e-25

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 98.05  E-value: 4.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  73 LTPDVLIPRPETEMLVEFALQHAQGlhscRIIDIGTGSGCIAISLAAElpEATVFGVDLSMAALRIAQKNARYHNL--PH 150
Cdd:PRK14968    1 LNDEVYEPAEDSFLLAENAVDKKGD----RVLEVGTGSGIVAIVAAKN--GKKVVGVDINPYAVECAKCNAKLNNIrnNG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477 151 IHFIQADLLSSFS-TQFDLICANLPYIPTRTLDALPvsRWEpRLALDGGQSGMETIRRLLVQAKTRMAPNSVLLLevest 229
Cdd:PRK14968   75 VEVIRSDLFEPFRgDKFDVILFNPPYLPTEEEEEWD--DWL-NYALSGGKDGREVIDRFLDEVGRYLKPGGRILL----- 146

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2417049477 230 lgastlasaqevfpnayhqLVPDLTGLDRMIKI 262
Cdd:PRK14968  147 -------------------LQSSLTGEDEVLEY 160
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 84-224 8.72e-19

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 81.77  E-value: 8.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  84 TEMLVEFALQHAQGlhscRIIDIGTGSGCIAISLAAELPEATVFGVDLSMAALRIAQKNARYHNLPHIHFIQADLLSSFS 163
Cdd:COG2813    38 TRLLLEHLPEPLGG----RVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAANGLENVEVLWSDGLSGVP 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2417049477 164 T-QFDLICANLPYiptRTldalpvsrweprlaldGGQSGMETIRRLLVQAKTRMAPNSVLLL 224
Cdd:COG2813   114 DgSFDLILSNPPF---HA----------------GRAVDKEVAHALIADAARHLRPGGELWL 156
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 89-235 1.18e-16

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 75.32  E-value: 1.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  89 EFALQHAQGLHSCRIIDIGTGSGCIAISLAAELPEATVFGVDLSMAALRIAQKNARYHNLPHIHFIQADLLSSFST-QFD 167
Cdd:pfam05175  21 RLLLEHLPKDLSGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGLENGEVVASDVYSGVEDgKFD 100

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2417049477 168 LICANLPYiptrtldalpvsrweprlaLDGGQSGMETIRRLLVQAKTRMAPNSVLLLEVESTLGASTL 235
Cdd:pfam05175 101 LIISNPPF-------------------HAGLATTYNVAQRFIADAKRHLRPGGELWIVANRFLGYPPL 149
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 102-230 1.16e-15

HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 72.97  E-value: 1.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477 102 RIIDIGTGSGCIAISLAAELpeATVFGVDLSMAALRIAQKNARYHNLpHIHFIQADLLSSFSTQFDLICANLPYIPTRtl 181
Cdd:TIGR00537  22 DVLEIGAGTGLVAIRLKGKG--KCILTTDINPFAVKELRENAKLNNV-GLDVVMTDLFKGVRGKFDVILFNPPYLPLE-- 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2417049477 182 DALPVSRWePRLALDGGQSGMETIRRLLVQAKTRMAPNSVLLLeVESTL 230
Cdd:TIGR00537  97 DDLRRGDW-LDVAIDGGKDGRKVIDRFLDELPEILKEGGRVQL-IQSSL 143
PRK14967 PRK14967
putative methyltransferase; Provisional
 74-230 1.70e-15

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 73.55  E-value: 1.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  74 TPDVLIPRPETEMLVEFAlqHAQGL-HSCRIIDIGTGSGCIAISlAAELPEATVFGVDLSMAALRIAQKNARYHNLPhIH 152
Cdd:PRK14967   12 APGVYRPQEDTQLLADAL--AAEGLgPGRRVLDLCTGSGALAVA-AAAAGAGSVTAVDISRRAVRSARLNALLAGVD-VD 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2417049477 153 FIQADLLSSFSTQ-FDLICANLPYIPTrTLDALPVSrwEPRLALDGGQSGMETIRRLLVQAKTRMAPNSVLLLeVESTL 230
Cdd:PRK14967   88 VRRGDWARAVEFRpFDVVVSNPPYVPA-PPDAPPSR--GPARAWDAGPDGRAVLDRLCDAAPALLAPGGSLLL-VQSEL 162
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
102-177 1.49e-13

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 64.84  E-value: 1.49e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2417049477 102 RIIDIGTGSGCIAISLAAELPEATVFGVDLSMAALRIAQKnaryhNLPHIHFIQADLLS-SFSTQFDLICAN--LPYIP 177
Cdd:COG4106     4 RVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARA-----RLPNVRFVVADLRDlDPPEPFDLVVSNaaLHWLP 77
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 103-184 2.41e-13

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 64.12  E-value: 2.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477 103 IIDIGTGSGCIAISLAAELpEATVFGVDLSMAALRIAQKNARYHNlPHIHFIQADL--LSSFSTQFDLICAN--LPYIPT 178
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERAAEAG-LNVEFVQGDAedLPFPDGSFDLVVSSgvLHHLPD 78


                  ....*.
gi 2417049477 179 RTLDAL 184
Cdd:pfam13649  79 PDLEAA 84
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 102-175 1.38e-12

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 65.55  E-value: 1.38e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2417049477 102 RIIDIGTGSGCIAISLAAELPEATVFGVDLSMAALRIAQKNARYHNL-PHIHFIQADLLSSFST----QFDLICANLPY 175
Cdd:COG4123    40 RVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLeDRITVIHGDLKEFAAElppgSFDLVVSNPPY 118
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 102-227 2.86e-11

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 58.98  E-value: 2.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477 102 RIIDIGTGSGCIAISLAaELPEATVFGVDLSMAALRIAQKNARYHNLPHIHFIQADLLSSFS---TQFDLICANLPYipt 178
Cdd:cd02440     1 RVLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeadESFDVIISDPPL--- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2417049477 179 rtldalpvsrweprlaldggQSGMETIRRLLVQAKTRMAPNSVLLLEVE 227
Cdd:cd02440    77 --------------------HHLVEDLARFLEEARRLLKPGGVLVLTLV 105
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 101-172 4.04e-11

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 59.74  E-value: 4.04e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2417049477 101 CRIIDIGTGSGCIAISLAAEL-PEATVFGVDLSMAALRIAQKNARYHNLPHIHFIQAD---LLSSFSTQ-FDLICAN 172
Cdd:pfam13847   5 MRVLDLGCGTGHLSFELAEELgPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDieeLPELLEDDkFDVVISN 81
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 87-177 2.24e-10

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 56.95  E-value: 2.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  87 LVEFALQHAqgLHSCRIIDIGTGSGCIAISLAAElpEATVFGVDLSMAALRIAQKNARYHNlphIHFIQADL--LSSFST 164
Cdd:COG2227    14 LAALLARLL--PAGGRVLDVGCGTGRLALALARR--GADVTGVDISPEALEIARERAAELN---VDFVQGDLedLPLEDG 86

                          90
                  ....*....|....*
gi 2417049477 165 QFDLICAN--LPYIP 177
Cdd:COG2227    87 SFDLVICSevLEHLP 101
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
101-224 2.67e-10

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 59.42  E-value: 2.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477 101 CRIIDIGTGSGCIAIsLAAELPEATVFGVDLSMAALRIAQKNARYHNLPH-IHFIQADLLSsfSTQFDLICANLpyiptr 179
Cdd:COG2264   150 KTVLDVGCGSGILAI-AAAKLGAKRVLAVDIDPVAVEAARENAELNGVEDrIEVVLGDLLE--DGPYDLVVANI------ 220

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2417049477 180 tldalpvsrweprLAldggqsgmETIRRLLVQAKTRMAPNSVLLL 224
Cdd:COG2264   221 -------------LA--------NPLIELAPDLAALLKPGGYLIL 244
PrmC_N pfam17827
PrmC N-terminal domain; This entry corresponds to the N-terminal alpha helical domain of the ...
 2-62 2.83e-09

PrmC N-terminal domain; This entry corresponds to the N-terminal alpha helical domain of the HemK protein. HemK is a methyltransferase enzyme that carries out the methylation of the N5 nitrogen of the glutamine found in the conserved GGQ motif of class-1 release factors.


Pssm-ID: 436073 [Multi-domain]  Cd Length: 71  Bit Score: 52.48  E-value: 2.83e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2417049477   2 AQADCEAPGQISLVLLQHVLKQSKSWVLSHSEYRLTPQEHEALQESLDHFLKGVPLPYILG 62
Cdd:pfam17827  11 KEAGIESPRLDAELLLAHVLGLDRTDLLLHPEEELSEEELERFEELLERRAAGEPLQYILG 71
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 99-172 4.44e-09

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 54.92  E-value: 4.44e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2417049477  99 HSCRIIDIGTGSGCIAISLAAeLPEATVFGVDLSMAALRIAQKNARYHNLPHIHFIQADLLSS---FSTQFDLICAN 172
Cdd:COG0500    26 KGGRVLDLGCGTGRNLLALAA-RFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAELdplPAESFDLVVAF 101
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 102-173 6.71e-09

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 53.46  E-value: 6.71e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2417049477 102 RIIDIGTGSGCIAISLAAElpEATVFGVDLSMAALRIAQKNARYHNLpHIHFIQADLLS-SFSTQ-FDLICANL 173
Cdd:COG2226    25 RVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAEDlPFPDGsFDLVISSF 95
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 104-172 7.92e-09

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 51.98  E-value: 7.92e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2417049477 104 IDIGTGSGCIAISLAAELPEATVFGVDLSMAALRIAQKN---ARYHNLPHIHFIQADLLSSFSTQFDLICAN 172
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERlaaLGLLNAVRVELFQLDLGELDPGSFDVVVAS 72
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
85-177 2.41e-08

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 52.69  E-value: 2.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  85 EMLVEFALQHAQGLHSCRIIDIGTGSGCIAISLAAElpEATVFGVDLSMAALRIAQKNARYhnlphIHFIQADL--LSSF 162
Cdd:COG4976    32 ALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPR--GYRLTGVDLSEEMLAKAREKGVY-----DRLLVADLadLAEP 104

                          90
                  ....*....|....*..
gi 2417049477 163 STQFDLICAN--LPYIP 177
Cdd:COG4976   105 DGRFDLIVAAdvLTYLG 121
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 85-169 4.18e-08

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 51.47  E-value: 4.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  85 EMLVEFALQHAQGLHSCRIIDIGTGSGCIAISLAAELpEATVFGVDLSMAALRIAQKNARYHNLPH-IHFIQADLLS-SF 162
Cdd:COG2230    37 EAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAEAGLADrVEVRLADYRDlPA 115


                  ....*..
gi 2417049477 163 STQFDLI 169
Cdd:COG2230   116 DGQFDAI 122
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 82-172 1.12e-07

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 51.88  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  82 PETEMLVEFALQHAQGLHScrIIDIGTGSGCIAISlAAELPEATVFGVDLSMAALRIAQKNARYHNLPHIhfIQADLLSS 161
Cdd:pfam06325 146 PTTKLCLEALERLVKPGES--VLDVGCGSGILAIA-ALKLGAKKVVGVDIDPVAVRAAKENAELNGVEAR--LEVYLPGD 220

                          90
                  ....*....|..
gi 2417049477 162 -FSTQFDLICAN 172
Cdd:pfam06325 221 lPKEKADVVVAN 232
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
98-224 2.63e-07

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 50.54  E-value: 2.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  98 LHSCRIIDIGTGSGCIAIsLAAELPEATVFGVDLSMAALRIAQKNARYHNLP-HIHFIQADLlssfstQFDLICANLpyi 176
Cdd:PRK00517  118 LPGKTVLDVGCGSGILAI-AAAKLGAKKVLAVDIDPQAVEAARENAELNGVElNVYLPQGDL------KADVIVANI--- 187

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2417049477 177 ptrtldalpvsrweprLAldggqsgmETIRRLLVQAKTRMAPNSVLLL 224
Cdd:PRK00517  188 ----------------LA--------NPLLELAPDLARLLKPGGRLIL 211
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 102-184 4.17e-07

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 48.79  E-value: 4.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477 102 RIIDIGTGSGCIAIslAAELPEATVFGVDLSMAALRIAQKNARYHNLPHIHFIQAD--LLSSFSTQFDLICANLPY---- 175
Cdd:COG1041    29 TVLDPFCGTGTILI--EAGLLGRRVIGSDIDPKMVEGARENLEHYGYEDADVIRGDarDLPLADESVDAIVTDPPYgrss 106

                          90
                  ....*....|
gi 2417049477 176 -IPTRTLDAL 184
Cdd:COG1041   107 kISGEELLEL 116
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 102-173 5.55e-07

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 49.21  E-value: 5.55e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2417049477 102 RIIDIGTGSGCIAISLAAELPEATVFGVDLSMAALRIAQKnaryHNLPHIHFIQADL--LSSFSTQFDLICANL 173
Cdd:TIGR02072  37 SVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKT----KLSENVQFICGDAekLPLEDSSFDLIVSNL 106
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 81-172 1.37e-06

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 48.40  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  81 RPETEMLVEFALQHAQglhscRIIDIGTGSGCIAISLAAELPEATVFGVDLSMAALRIAQKNaryhnLPHIHFIQADLLS 160
Cdd:PRK01683   18 RPARDLLARVPLENPR-----YVVDLGCGPGNSTELLVERWPAARITGIDSSPAMLAEARSR-----LPDCQFVEADIAS 87

                          90
                  ....*....|...
gi 2417049477 161 SFSTQ-FDLICAN 172
Cdd:PRK01683   88 WQPPQaLDLIFAN 100
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 102-187 1.59e-06

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 47.84  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477 102 RIIDIGTGSGCIAISLAAELPE-ATVFGVDLSMAALRIAQKNARYHNL-PHIHFIQADllssfstqfdliCANLPYiPTR 179
Cdd:PRK00216   54 KVLDLACGTGDLAIALAKAVGKtGEVVGLDFSEGMLAVGREKLRDLGLsGNVEFVQGD------------AEALPF-PDN 120


                  ....*...
gi 2417049477 180 TLDALPVS 187
Cdd:PRK00216  121 SFDAVTIA 128
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 102-224 7.80e-06

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 44.24  E-value: 7.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477 102 RIIDIGTGSGCIAISLAAELPEATVFGVDLSMAALRIAQKNARYHNLPHIHFIQADllssfstqfdlicanlpyiptrTL 181
Cdd:TIGR02469  22 VLWDIGAGTGSVTIEAARLVPNGRVYAIERNPEALDLIERNLRRFGVSNIVIVEGD----------------------AP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2417049477 182 DALPVSRWEPRLALDGGQSGMetIRRLLVQAKTRMAPNSVLLL 224
Cdd:TIGR02469  80 EAPEALLPDPDAVFVGGSGGL--LQEILEAVERRLRPGGRIVL 120
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 102-157 8.54e-06

Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 46.31  E-value: 8.54e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2417049477 102 RIIDIGTGSGCIAISLAAELPEATVFGVDLSMAALRIAQKNARYHNLPHIHFIQAD 157
Cdd:COG2242   250 VLWDIGAGSGSVSIEAARLAPGGRVYAIERDPERAALIRANARRFGVPNVEVVEGE 305
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 102-175 1.20e-05

Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 44.65  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477 102 RIIDIGTGSGCIAISLA-----------AELPEATVFGVDLSMAALRIAQKNARYHNLPH-IHFIQADL--LSSFSTQFD 167
Cdd:pfam01170  31 PLLDPMCGSGTILIEAAlmganiapgkfDARVRAPLYGSDIDRRMVQGARLNAENAGVGDlIEFVQADAadLPLLEGSVD 110


                  ....*...
gi 2417049477 168 LICANLPY 175
Cdd:pfam01170 111 VIVTNPPY 118
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 104-173 1.52e-05

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 42.65  E-value: 1.52e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2417049477 104 IDIGTGSGCIAISLAAELPEatVFGVDLSMAALRIAQKNARyhnLPHIHFIQADLLS-SF-STQFDLICANL 173
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR--VTGVDISPEMLELAREKAP---REGLTFVVGDAEDlPFpDNSFDLVLSSE 67
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
97-156 3.74e-05

decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;


Pssm-ID: 181354  Cd Length: 187  Bit Score: 43.45  E-value: 3.74e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2417049477  97 GLHSCR-IIDIGTGSGCIAISLAAELPEATVFGVDLSMAALRIAQKNARYHNLPHIHFIQA 156
Cdd:PRK08287   28 ELHRAKhLIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKENRQRFGCGNIDIIPG 88
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
71-175 4.02e-05

Adenine-specific DNA N6-methylase [Replication, recombination and repair];


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 44.17  E-value: 4.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  71 FQLTPDVLIprpeteMLVEFALQHAQGLHSCRIIDIGTGSGCIAISLAAELP-EATVFGVDLSMAALRIAQKNARYHNLP 149
Cdd:COG0827    93 HQMTPDAIG------LLIGYLVEKFTKKEGLRILDPAVGTGNLLTTVLNQLKkKVNAYGVEVDDLLIRLAAVLANLQGHP 166

                          90       100
                  ....*....|....*....|....*..
gi 2417049477 150 hIHFIQADLLSSFST-QFDLICANLPY 175
Cdd:COG0827   167 -VELFHQDALQPLLIdPVDVVISDLPV 192
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 91-169 1.34e-04

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 42.21  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  91 ALQHAQGLHScrIIDIGTGSGCIAISLAAELPE---ATVFGVDLSMAALRIAQKnaRYHNlphIHFIQAdllSSF----- 162
Cdd:PRK11088   79 AERLDEKATA--LLDIGCGEGYYTHALADALPEittMQLFGLDISKVAIKYAAK--RYPQ---VTFCVA---SSHrlpfa 148


                  ....*..
gi 2417049477 163 STQFDLI 169
Cdd:PRK11088  149 DQSLDAI 155
PRK08317 PRK08317
hypothetical protein; Provisional
 102-171 2.01e-04

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 41.85  E-value: 2.01e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2417049477 102 RIIDIGTGSGCIAISLAAEL-PEATVFGVDLSMAALRIAqKNARYHNLPHIHFIQADLLSS-FSTQ-FDLICA 171
Cdd:PRK08317   22 RVLDVGCGPGNDARELARRVgPEGRVVGIDRSEAMLALA-KERAAGLGPNVEFVRGDADGLpFPDGsFDAVRS 93
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
80-175 5.33e-04

Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 40.56  E-value: 5.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  80 PRPETEMLVEFALQHaqglHSCRIIDIGTGSGCIAISLAAELPEA--------TVFGVDLSMAALRIAQKNARYHNLPHI 151
Cdd:COG0286    28 PREVVRLMVELLDPK----PGETVYDPACGSGGFLVEAAEYLKEHggderkklSLYGQEINPTTYRLAKMNLLLHGIGDP 103

                          90       100
                  ....*....|....*....|....*..
gi 2417049477 152 HFIQADLLSS---FSTQFDLICANLPY 175
Cdd:COG0286   104 NIELGDTLSNdgdELEKFDVVLANPPF 130
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 102-169 9.64e-04

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 39.76  E-value: 9.64e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2417049477 102 RIIDIGTGSGCIAISLAAEL-PEATVFGVDLSMAALRIAQKNARYHNLPH-IHFIQADLLSSFS-TQFDLI 169
Cdd:COG2519    94 RVLEAGTGSGALTLALARAVgPEGKVYSYERREDFAEIARKNLERFGLPDnVELKLGDIREGIDeGDVDAV 164
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
102-168 2.20e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 38.48  E-value: 2.20e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2417049477 102 RIIDIGTGSGCIAIsLAAELPEATVFGVDLSMAALRIAQKNARYHNLPH-IHFIQADllssfSTQFDL 168
Cdd:COG4076    38 VVLDIGTGSGLLSM-LAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDrITVINAD-----ATDLDL 99
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 124-169 2.48e-03

23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 38.62  E-value: 2.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2417049477 124 ATVFGVDLSMAALRIAQKNARYHNLPHIH-FIQAD---LLSSFST---QFDLI 169
Cdd:COG1092   240 KSVTSVDLSATALEWAKENAALNGLDDRHeFVQADafdWLRELARegeRFDLI 292
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 102-198 3.74e-03

tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442010 [Multi-domain]  Cd Length: 333  Bit Score: 38.30  E-value: 3.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477 102 RIIDIGTGSGCIAISLAAELPeATVFGVDLSMAALRIAQKNARYHNLPH-IHFIQAD---LLSSFSTQFDLICANLPYip 177
Cdd:COG2520   183 RVLDMFAGVGPFSIPIAKRSG-AKVVAIDINPDAVEYLKENIRLNKVEDrVTPILGDareVAPELEGKADRIIMNLPH-- 259

                          90       100
                  ....*....|....*....|.
gi 2417049477 178 tRTLDALPVSRwepRLALDGG 198
Cdd:COG2520   260 -SADEFLDAAL---RALKPGG 276
PRK15001 PRK15001
23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;
90-175 4.19e-03

23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;


Pssm-ID: 184963 [Multi-domain]  Cd Length: 378  Bit Score: 38.08  E-value: 4.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  90 FALQHAQGLHSCRIIDIGTGSGCIAISLAAELPEATVFGVDLSMAALRIAQKNARYhNLPHI----HFIQADLLSSFST- 164
Cdd:PRK15001  219 FFMQHLPENLEGEIVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVET-NMPEAldrcEFMINNALSGVEPf 297

                          90
                  ....*....|.
gi 2417049477 165 QFDLICANLPY 175
Cdd:PRK15001  298 RFNAVLCNPPF 308
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 102-184 8.02e-03

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 36.25  E-value: 8.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477 102 RIIDIGTGSGCIAISLAAELPeaTVFGVDLSMAALRIAQKNARYHNLPHIHFIQADLLSSFSTQFDLICaNLPYiPTRTL 181
Cdd:pfam13489  25 RVLDFGCGTGIFLRLLRAQGF--SVTGVDPSPIAIERALLNVRFDQFDEQEAAVPAGKFDVIVAREVLE-HVPD-PPALL 100


                  ...
gi 2417049477 182 DAL 184
Cdd:pfam13489 101 RQI 103
rsmG_gidB TIGR00138
16S rRNA (guanine(527)-N(7))-methyltransferase RsmG; RsmG was previously called GidB ...
 67-199 9.55e-03

16S rRNA (guanine(527)-N(7))-methyltransferase RsmG; RsmG was previously called GidB (glucose-inhibited division protein B). It is present and a single copy in nearly all complete eubacterial genomes. It is missing only from some obligate intracellular species of various lineages (Chlamydiae, Ehrlichia, Wolbachia, Anaplasma, Buchnera, etc.). RsmG shows a methytransferase fold in its the crystal structure, and acts as a 7-methylguanosine (m(7)G) methyltransferase, apparently specific to 16S rRNA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 272928  Cd Length: 181  Bit Score: 36.08  E-value: 9.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2417049477  67 FGRTFQLTPDVLIPRPETEMLVEfALQHAQGLHSCRIIDIGTGSGCIAISLAAELPEATVFGVD--------LSMAALRI 138
Cdd:TIGR00138  11 WNQRFNLTSIKTPEEIWQRHILD-SLALLPYLDGKRVIDIGSGAGFPGIPLAIARPELKLTLLEsnhkkvafLREVKAEL 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2417049477 139 aqknaryhNLPHIHFIQADLLSSFST-QFDLICAnlpyiptRTLDALPV-SRWEPRLALDGGQ 199
Cdd:TIGR00138  90 --------GLNNVEIVNGRAEDYQHEeQFDIITS-------RALASLNVlLELTLNLLKVGGY 137
 
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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