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Conserved domains on  [gi|767923520|ref|XP_011532116|]
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MTRF1L release factor glutamine methyltransferase isoform X7 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RF_mod_PrmC super family cl37287
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 1-219 1.13e-59

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]


The actual alignment was detected with superfamily member TIGR03534:

Pssm-ID: 274634 [Multi-domain]  Cd Length: 250  Bit Score: 188.83  E-value: 1.13e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520    1 MPVQYILGEWDFQGLSLRMVPPVFIPRPETEelvewvleevaqrsHAVGS-----PGSPLILEVGCGSGAISLSLLSQLP 75
Cdd:TIGR03534  44 EPVAYILGEREFYGLDFKVSPGVLIPRPETE--------------ELVEAalerlKKGPRVLDLGTGSGAIALALAKERP 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520   76 QSRVIAVDKREAAISLTHENAQRLRLqDRIWIIHLDMTSerswtHLPWGPMDLIVSNPPYVFHQDMEQLAPEIRSYEDPA 155
Cdd:TIGR03534 110 DARVTAVDISPEALAVARKNARRLGL-ENVEFLQGDWFE-----PLPSGKFDLIVSNPPYIPEADIHLLDPEVRDFEPRL 183

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767923520  156 ALDGGEEGMDIITHILALAPRLLKDSGSIFLEVDPRHPELVSSWLQSRPdlyLNLVAVRRDFCG 219
Cdd:TIGR03534 184 ALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFEAAG---FADVETRKDLAG 244
 
Name Accession Description Interval E-value
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 1-219 1.13e-59

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: 188.83  E-value: 1.13e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520    1 MPVQYILGEWDFQGLSLRMVPPVFIPRPETEelvewvleevaqrsHAVGS-----PGSPLILEVGCGSGAISLSLLSQLP 75
Cdd:TIGR03534  44 EPVAYILGEREFYGLDFKVSPGVLIPRPETE--------------ELVEAalerlKKGPRVLDLGTGSGAIALALAKERP 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520   76 QSRVIAVDKREAAISLTHENAQRLRLqDRIWIIHLDMTSerswtHLPWGPMDLIVSNPPYVFHQDMEQLAPEIRSYEDPA 155
Cdd:TIGR03534 110 DARVTAVDISPEALAVARKNARRLGL-ENVEFLQGDWFE-----PLPSGKFDLIVSNPPYIPEADIHLLDPEVRDFEPRL 183

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767923520  156 ALDGGEEGMDIITHILALAPRLLKDSGSIFLEVDPRHPELVSSWLQSRPdlyLNLVAVRRDFCG 219
Cdd:TIGR03534 184 ALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFEAAG---FADVETRKDLAG 244
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 1-219 1.32e-59

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 189.59  E-value: 1.32e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520   1 MPVQYILGEWDFQGLSLRMVPPVFIPRPETEELVewvleevAQRSHAVGSPGSPLILEVGCGSGAISLSLLSQLPQSRVI 80
Cdd:COG2890   68 EPLAYILGEAEFYGLEFKVDPGVLIPRPETEELV-------ELALALLPAGAPPRVLDLGTGSGAIALALAKERPDARVT 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520  81 AVDKREAAISLTHENAQRLRLQDRIWIIHLDMTSErswthLPW-GPMDLIVSNPPYVFHQDMEQLAPEIRSYEDPAALDG 159
Cdd:COG2890  141 AVDISPDALAVARRNAERLGLEDRVRFLQGDLFEP-----LPGdGRFDLIVSNPPYIPEDEIALLPPEVRDHEPRLALDG 215

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520 160 GEEGMDIITHILALAPRLLKDSGSIFLEVDPRHPELVSSWLQSRPdlyLNLVAVRRDFCG 219
Cdd:COG2890  216 GEDGLDFYRRIIAQAPRLLKPGGWLLLEIGEDQGEAVRALLEAAG---FADVETHKDLAG 272
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 1-216 9.62e-56

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 179.59  E-value: 9.62e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520   1 MPVQYILGEWDFQGLSLRMVPPVFIPRPETEELVEWVLEEVAQRSHAVgspgsplILEVGCGSGAISLSLLSQLPQSRVI 80
Cdd:PRK09328  64 EPLQYILGEAEFWGLDFKVSPGVLIPRPETEELVEWALEALLLKEPLR-------VLDLGTGSGAIALALAKERPDAEVT 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520  81 AVDKREAAISLTHENAQRLrLQDRIWIIHLDMtsersWTHLPWGPMDLIVSNPPYVFHQDMEQLAPEIRSYEDPAALDGG 160
Cdd:PRK09328 137 AVDISPEALAVARRNAKHG-LGARVEFLQGDW-----FEPLPGGRFDLIVSNPPYIPEADIHLLQPEVRDHEPHLALFGG 210

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767923520 161 EEGMDIITHILALAPRLLKDSGSIFLEVDPRHPELVSSWLqsRPDLYLNlVAVRRD 216
Cdd:PRK09328 211 EDGLDFYRRIIEQAPRYLKPGGWLLLEIGYDQGEAVRALL--AAAGFAD-VETRKD 263
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 56-186 6.03e-14

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: 67.62  E-value: 6.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520   56 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLqDRIWIIHLDMTSErswthLPWGPMDLIVSNPPy 135
Cdd:pfam05175  35 VLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGL-ENGEVVASDVYSG-----VEDGKFDLIISNPP- 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767923520  136 vFHQdmeqlapeirsyedpaaldGGEEGMDIITHILALAPRLLKDSGSIFL 186
Cdd:pfam05175 108 -FHA-------------------GLATTYNVAQRFIADAKRHLRPGGELWI 138
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 56-149 2.64e-09

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: 53.20  E-value: 2.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520  56 ILEVGCGSGAISLSLLSQlPQSRVIAVDKREAAISLThENAQRLRLQDRIWIIHLDMtseRSWTHLPWGPMDLIVSNPPY 135
Cdd:cd02440    2 VLDLGCGTGALALALASG-PGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDA---EELPPEADESFDVIISDPPL 76

                         90
                 ....*....|....*
gi 767923520 136 V-FHQDMEQLAPEIR 149
Cdd:cd02440   77 HhLVEDLARFLEEAR 91
rADc smart00650
Ribosomal RNA adenine dimethylases;
45-135 5.81e-05

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 42.50  E-value: 5.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520    45 SHAVGSPGSPlILEVGCGSGAISLSLLSQLpqSRVIAV--DKREAAISlthenAQRLRLQDRIWIIHLDMTSerswTHLP 122
Cdd:smart00650   7 RAANLRPGDT-VLEIGPGKGALTEELLERA--KRVTAIeiDPRLAPRL-----REKFAAADNLTVIHGDALK----FDLP 74

                           90
                   ....*....|...
gi 767923520   123 WGPMDLIVSNPPY 135
Cdd:smart00650  75 KLQPYKVVGNLPY 87
 
Name Accession Description Interval E-value
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 1-219 1.13e-59

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: 188.83  E-value: 1.13e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520    1 MPVQYILGEWDFQGLSLRMVPPVFIPRPETEelvewvleevaqrsHAVGS-----PGSPLILEVGCGSGAISLSLLSQLP 75
Cdd:TIGR03534  44 EPVAYILGEREFYGLDFKVSPGVLIPRPETE--------------ELVEAalerlKKGPRVLDLGTGSGAIALALAKERP 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520   76 QSRVIAVDKREAAISLTHENAQRLRLqDRIWIIHLDMTSerswtHLPWGPMDLIVSNPPYVFHQDMEQLAPEIRSYEDPA 155
Cdd:TIGR03534 110 DARVTAVDISPEALAVARKNARRLGL-ENVEFLQGDWFE-----PLPSGKFDLIVSNPPYIPEADIHLLDPEVRDFEPRL 183

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767923520  156 ALDGGEEGMDIITHILALAPRLLKDSGSIFLEVDPRHPELVSSWLQSRPdlyLNLVAVRRDFCG 219
Cdd:TIGR03534 184 ALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFEAAG---FADVETRKDLAG 244
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 1-219 1.32e-59

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 189.59  E-value: 1.32e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520   1 MPVQYILGEWDFQGLSLRMVPPVFIPRPETEELVewvleevAQRSHAVGSPGSPLILEVGCGSGAISLSLLSQLPQSRVI 80
Cdd:COG2890   68 EPLAYILGEAEFYGLEFKVDPGVLIPRPETEELV-------ELALALLPAGAPPRVLDLGTGSGAIALALAKERPDARVT 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520  81 AVDKREAAISLTHENAQRLRLQDRIWIIHLDMTSErswthLPW-GPMDLIVSNPPYVFHQDMEQLAPEIRSYEDPAALDG 159
Cdd:COG2890  141 AVDISPDALAVARRNAERLGLEDRVRFLQGDLFEP-----LPGdGRFDLIVSNPPYIPEDEIALLPPEVRDHEPRLALDG 215

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520 160 GEEGMDIITHILALAPRLLKDSGSIFLEVDPRHPELVSSWLQSRPdlyLNLVAVRRDFCG 219
Cdd:COG2890  216 GEDGLDFYRRIIAQAPRLLKPGGWLLLEIGEDQGEAVRALLEAAG---FADVETHKDLAG 272
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 1-216 9.62e-56

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 179.59  E-value: 9.62e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520   1 MPVQYILGEWDFQGLSLRMVPPVFIPRPETEELVEWVLEEVAQRSHAVgspgsplILEVGCGSGAISLSLLSQLPQSRVI 80
Cdd:PRK09328  64 EPLQYILGEAEFWGLDFKVSPGVLIPRPETEELVEWALEALLLKEPLR-------VLDLGTGSGAIALALAKERPDAEVT 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520  81 AVDKREAAISLTHENAQRLrLQDRIWIIHLDMtsersWTHLPWGPMDLIVSNPPYVFHQDMEQLAPEIRSYEDPAALDGG 160
Cdd:PRK09328 137 AVDISPEALAVARRNAKHG-LGARVEFLQGDW-----FEPLPGGRFDLIVSNPPYIPEADIHLLQPEVRDHEPHLALFGG 210

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767923520 161 EEGMDIITHILALAPRLLKDSGSIFLEVDPRHPELVSSWLqsRPDLYLNlVAVRRD 216
Cdd:PRK09328 211 EDGLDFYRRIIEQAPRYLKPGGWLLLEIGYDQGEAVRALL--AAAGFAD-VETRKD 263
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 2-188 6.95e-41

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: 141.72  E-value: 6.95e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520    2 PVQYILGEWDFQGLSLRMVPPVFIPRPETEELVEWVLEEVAQRSHAVGspgsplILEVGCGSGAISLSLLSQLPQSRVIA 81
Cdd:TIGR00536  70 PVAYLLGSKEFYGLEFFVNEHVLIPRPETEELVEKALASLISQPPILH------ILDLGTGSGCIALALAYEFPNAEVIA 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520   82 VDKREAAISLTHENAQRLRLQDRIWIIHLDMtsersWTHLPWGPMDLIVSNPPYVFHQDMEQLAPEIRsYEDPAALDGGE 161
Cdd:TIGR00536 144 VDISPDALAVAEENAEKNQLEHRVEFIQSNL-----FEPLAGQKIDIIVSNPPYIDEEDLADLPNVVR-FEPLLALVGGD 217

                         170       180
                  ....*....|....*....|....*..
gi 767923520  162 EGMDIITHILALAPRLLKDSGSIFLEV 188
Cdd:TIGR00536 218 DGLNILRQIIELAPDYLKPNGFLVCEI 244
L3_gln_methyl TIGR03533
protein-(glutamine-N5) methyltransferase, ribosomal protein L3-specific; Members of this ...
 56-188 2.85e-26

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: 103.36  E-value: 2.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520   56 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLQDRIWIIHLDMTSErswthLPWGPMDLIVSNPPY 135
Cdd:TIGR03533 125 ILDLCTGSGCIAIACAYAFPEAEVDAVDISPDALAVAEINIERHGLEDRVTLIQSDLFAA-----LPGRKYDLIVSNPPY 199

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767923520  136 VFHQDMEQLAPEIRsYEDPAALDGGEEGMDIITHILALAPRLLKDSGSIFLEV 188
Cdd:TIGR03533 200 VDAEDMADLPAEYH-HEPELALASGEDGLDLVRRILAEAADHLNENGVLVVEV 251
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
 2-197 1.07e-23

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


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 99.17  E-value: 1.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520   2 PVQYILGEWDFQGLSLRMVPPVFIPRPETEELVEWVLEEVAQRSHAV-------GSPGSPL----------ILEVGCGSG 64
Cdd:PRK01544  71 PIAYITGVKEFYSREFIVNKHVLIPRSDTEVLVDVVFQCHSRESGNPekkqlnpCFRGNDIssncndkflnILELGTGSG 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520  65 AISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLQDRIWIIHLDmtsersW-THLPWGPMDLIVSNPPYVFHQDMEQ 143
Cdd:PRK01544 151 CIAISLLCELPNANVIATDISLDAIEVAKSNAIKYEVTDRIQIIHSN------WfENIEKQKFDFIVSNPPYISHSEKSE 224

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767923520 144 LAPEIRSYEDPAALDGGEEGMDIITHILALAPRLLKDSGSIFLEVDPRHPELVS 197
Cdd:PRK01544 225 MAIETINYEPSIALFAEEDGLQAYFIIAENAKQFLKPNGKIILEIGFKQEEAVT 278
PrmC_rel_meth TIGR03704
putative protein-(glutamine-N5) methyltransferase, unknown substrate-specific; This protein ...
 1-191 6.42e-20

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: 85.61  E-value: 6.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520    1 MPVQYILGEWDFQGLSLRMVPPVFIPRPETEELVEWVLeevaqrSHAVGSPGSPLILEVGCGSGAISLSLLSQLPQSRVI 80
Cdd:TIGR03704  41 LPLEHVLGWAEFCGLRIAVDPGVFVPRRRTEFLVDEAA------ALARPRSGTLVVVDLCCGSGAVGAALAAALDGIELH 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520   81 AVDKREAAISLTHENaqrlrLQDRIWIIHLDMTSERSWTHLPwGPMDLIVSNPPYVFHQDMEQLAPEIRSYEDPAALDGG 160
Cdd:TIGR03704 115 AADIDPAAVRCARRN-----LADAGGTVHEGDLYDALPTALR-GRVDILAANAPYVPTDAIALMPPEARDHEPRVALDGG 188

                         170       180       190
                  ....*....|....*....|....*....|.
gi 767923520  161 EEGMDIITHILALAPRLLKDSGSIFLEVDPR 191
Cdd:TIGR03704 189 ADGLDVLRRVAAGAPDWLAPGGHLLVETSER 219
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 56-186 6.68e-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: 81.39  E-value: 6.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520  56 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLQDrIWIIHLDMTSerswtHLPWGPMDLIVSNPPy 135
Cdd:COG2813   53 VLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAANGLEN-VEVLWSDGLS-----GVPDGSFDLILSNPP- 125

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767923520 136 vFHQdmeqlapeirsyedpaaldGGEEGMDIITHILALAPRLLKDSGSIFL 186
Cdd:COG2813  126 -FHA-------------------GRAVDKEVAHALIADAARHLRPGGELWL 156
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 56-186 6.85e-19

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: 82.50  E-value: 6.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520  56 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLQDRIWIIHLDMtseRSWT-HLPWGPMDLIVSNPP 134
Cdd:COG4123   41 VLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDL---KEFAaELPPGSFDLVVSNPP 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767923520 135 YvFHQDMEQLAP-EIRS---YEDPAALDggeegmdiitHILALAPRLLKDSGSIFL 186
Cdd:COG4123  118 Y-FKAGSGRKSPdEARAiarHEDALTLE----------DLIRAAARLLKPGGRFAL 162
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 56-186 6.03e-14

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: 67.62  E-value: 6.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520   56 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLqDRIWIIHLDMTSErswthLPWGPMDLIVSNPPy 135
Cdd:pfam05175  35 VLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGL-ENGEVVASDVYSG-----VEDGKFDLIISNPP- 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767923520  136 vFHQdmeqlapeirsyedpaaldGGEEGMDIITHILALAPRLLKDSGSIFL 186
Cdd:pfam05175 108 -FHA-------------------GLATTYNVAQRFIADAKRHLRPGGELWI 138
PRK14966 PRK14966
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; ...
 2-187 2.27e-13

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


Pssm-ID: 184930 [Multi-domain]  Cd Length: 423  Bit Score: 68.95  E-value: 2.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520   2 PVQYILGEWDFQGLSLRMVPPVFIPRPETEELVEWVLEEVaqrshavgsPGSPLILEVGCGSGAISLSLLSQLPQSRVIA 81
Cdd:PRK14966 210 PVAYILGVREFYGRRFAVNPNVLIPRPETEHLVEAVLARL---------PENGRVWDLGTGSGAVAVTVALERPDAFVRA 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520  82 VDKREAAISLTHENA----QRLRLQDRIWiIHLDMTSERSWthlpwgpmDLIVSNPPYVFHQDMEQLAPEIRsYEDPAAL 157
Cdd:PRK14966 281 SDISPPALETARKNAadlgARVEFAHGSW-FDTDMPSEGKW--------DIIVSNPPYIENGDKHLLQGDLR-FEPQIAL 350

                        170       180       190
                 ....*....|....*....|....*....|
gi 767923520 158 DGGEEGMDIITHILALAPRLLKDSGSIFLE 187
Cdd:PRK14966 351 TDFSDGLSCIRTLAQGAPDRLAEGGFLLLE 380
PRK14968 PRK14968
putative methyltransferase; Provisional
 56-198 1.35e-12

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 64.15  E-value: 1.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520  56 ILEVGCGSGAISLSLLSQlpQSRVIAVDKREAAISLTHENAQRLRLQDR-IWIIHLDMTSE-RSwthlpwGPMDLIVSNP 133
Cdd:PRK14968  27 VLEVGTGSGIVAIVAAKN--GKKVVGVDINPYAVECAKCNAKLNNIRNNgVEVIRSDLFEPfRG------DKFDVILFNP 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767923520 134 PYVFHQDMEqlapEIRSYEDpAALDGGEEGMDIITHILALAPRLLKDSGSIFLevdprhpeLVSS 198
Cdd:PRK14968  99 PYLPTEEEE----EWDDWLN-YALSGGKDGREVIDRFLDEVGRYLKPGGRILL--------LQSS 150
PRK14967 PRK14967
putative methyltransferase; Provisional
 46-186 8.20e-12

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 62.76  E-value: 8.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520  46 HAVGSPGSPLILEVGCGSGAISLSLlSQLPQSRVIAVDKREAAISLTHENAQRLRLqdRIWIIHLDMTserswTHLPWGP 125
Cdd:PRK14967  30 AAEGLGPGRRVLDLCTGSGALAVAA-AAAGAGSVTAVDISRRAVRSARLNALLAGV--DVDVRRGDWA-----RAVEFRP 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767923520 126 MDLIVSNPPYVFHqdmeqlAPEIRSYEDPA-ALDGGEEGMDIITHILALAPRLLKDSGSIFL 186
Cdd:PRK14967 102 FDVVVSNPPYVPA------PPDAPPSRGPArAWDAGPDGRAVLDRLCDAAPALLAPGGSLLL 157
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 56-149 1.01e-10

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 56.80  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520   56 ILEVGCGSGAISLsLLSQLPQSRVIAVDKREAAISLTHENAQRLRLqdRIWIIHLDMTSerswTHLPWGPMDLIVSNppY 135
Cdd:pfam13649   1 VLDLGCGTGRLTL-ALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAED----LPFPDGSFDLVVSS--G 71

                          90
                  ....*....|....*...
gi 767923520  136 VFH----QDMEQLAPEIR 149
Cdd:pfam13649  72 VLHhlpdPDLEAALREIA 89
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 56-103 2.68e-10

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: 56.57  E-value: 2.68e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 767923520   56 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLQD 103
Cdd:TIGR02469  23 LWDIGAGTGSVTIEAARLVPNGRVYAIERNPEALDLIERNLRRFGVSN 70
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
56-150 5.79e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 54.83  E-value: 5.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520  56 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRlqdriwIIHLDMtseRSWThlPWGPMDLIVSNppY 135
Cdd:COG4106    5 VLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLPNVR------FVVADL---RDLD--PPEPFDLVVSN--A 71

                         90
                 ....*....|....*..
gi 767923520 136 VFH--QDMEQLAPEIRS 150
Cdd:COG4106   72 ALHwlPDHAALLARLAA 88
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 51-196 5.86e-10

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 57.23  E-value: 5.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520  51 PGSPLILEVGCGSGAiSLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLqDRIWIIHLDMTserSWTHLPWGPMDLIV 130
Cdd:COG0500   25 PKGGRVLDLGCGTGR-NLLALAARFGGRVIGIDLSPEAIALARARAAKAGL-GNVEFLVADLA---ELDPLPAESFDLVV 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767923520 131 SNppYVFHqdmeqlapeirsYEDPAALdggeegmdiiTHILALAPRLLKDSGSIFLEVDPRHPELV 196
Cdd:COG0500  100 AF--GVLH------------HLPPEER----------EALLRELARALKPGGVLLLSASDAAAALS 141
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 56-149 2.64e-09

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: 53.20  E-value: 2.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520  56 ILEVGCGSGAISLSLLSQlPQSRVIAVDKREAAISLThENAQRLRLQDRIWIIHLDMtseRSWTHLPWGPMDLIVSNPPY 135
Cdd:cd02440    2 VLDLGCGTGALALALASG-PGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDA---EELPPEADESFDVIISDPPL 76

                         90
                 ....*....|....*
gi 767923520 136 V-FHQDMEQLAPEIR 149
Cdd:cd02440   77 HhLVEDLARFLEEAR 91
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 51-103 9.62e-09

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: 55.17  E-value: 9.62e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767923520  51 PGSpLILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLQD 103
Cdd:COG2242  247 PGD-VLWDIGAGSGSVSIEAARLAPGGRVYAIERDPERAALIRANARRFGVPN 298
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 56-202 1.63e-07

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: 49.22  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520  56 ILEVGCGSGAISLSLLSQlpQSRVIAVDKREAAISLTHENAQRLRLqdRIWIIHLDMtserswTHLPW--GPMDLIVSNp 133
Cdd:COG2226   26 VLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGL--NVEFVVGDA------EDLPFpdGSFDLVISS- 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767923520 134 pYVFH--QDMEQLAPEIRsyedpaaldggeegmdiithilalapRLLKDSGS-IFLEVDPRHPELVSSWLQS 202
Cdd:COG2226   95 -FVLHhlPDPERALAEIA--------------------------RVLKPGGRlVVVDFSPPDLAELEELLAE 139
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 51-110 3.18e-07

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: 49.77  E-value: 3.18e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767923520  51 PGSpLILEVGCGSGAISLSLLSQL-PQSRVIAVDKREAAISLTHENAQRLRLQDRiWIIHL 110
Cdd:COG2519   91 PGA-RVLEAGTGSGALTLALARAVgPEGKVYSYERREDFAEIARKNLERFGLPDN-VELKL 149
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 56-186 1.84e-06

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: 46.77  E-value: 1.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520   56 ILEVGCGSGAISLSLLSQlpQSRVIAVDKREAAISLTHENAQRLRLQDRIWIIHLDMTSErswthlpwGPMDLIVSNPPY 135
Cdd:TIGR00537  23 VLEIGAGTGLVAIRLKGK--GKCILTTDINPFAVKELRENAKLNNVGLDVVMTDLFKGVR--------GKFDVILFNPPY 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767923520  136 VFHQDMEQlapeIRSYEDpAALDGGEEGMDIITHILALAPRLLKDSGSIFL 186
Cdd:TIGR00537  93 LPLEDDLR----RGDWLD-VAIDGGKDGRKVIDRFLDELPEILKEGGRVQL 138
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 56-131 3.62e-06

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 45.69  E-value: 3.62e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767923520  56 ILEVGCGSGAISLSLLSQLpQSRVIAVDKREAAISLTHENAQRLRLQDRIWIIHLDMtserswTHLPW-GPMDLIVS 131
Cdd:COG2230   55 VLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADY------RDLPAdGQFDAIVS 124
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 56-188 7.49e-06

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: 44.24  E-value: 7.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520  56 ILEVGCGSGAISLSLLSQlpQSRVIAVDKREAAIslthENAQRLRLQDRIWIIHLDMTSerswTHLPWGPMDLIVSNppY 135
Cdd:COG2227   28 VLDVGCGTGRLALALARR--GADVTGVDISPEAL----EIARERAAELNVDFVQGDLED----LPLEDGSFDLVICS--E 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767923520 136 VFHqdmeqlapeirSYEDPAALdggeegmdiithiLALAPRLLKDSGSIFLEV 188
Cdd:COG2227   96 VLE-----------HLPDPAAL-------------LRELARLLKPGGLLLLST 124
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 56-132 7.96e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 44.72  E-value: 7.96e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767923520   56 ILEVGCGSGAISLSLLSQL-PQSRVIAVDKREAAISLTHENAQRLRLqDRIWIIHLDMTSERswTHLPWGPMDLIVSN 132
Cdd:pfam13847   7 VLDLGCGTGHLSFELAEELgPNAEVVGIDISEEAIEKARENAQKLGF-DNVEFEQGDIEELP--ELLEDDKFDVVISN 81
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 56-108 1.18e-05

cobalt-precorrin-6Y C(15)-methyltransferase; Provisional


Pssm-ID: 234740  Cd Length: 198  Bit Score: 44.79  E-value: 1.18e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767923520  56 ILEVGCGSGAISL--SLLSQlPQSRVIAVDKREAAISLTHENAQRLRLQDRIWII 108
Cdd:PRK00377  44 ILDIGCGTGSVTVeaSLLVG-ETGKVYAVDKDEKAINLTRRNAEKFGVLNNIVLI 97
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 57-149 1.26e-05

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 42.74  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520   57 LEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLQDRIW--IIHLDMTSerswthLPWGPMDLIVSNpp 134
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVRveLFQLDLGE------LDPGSFDVVVAS-- 72

                          90
                  ....*....|....*..
gi 767923520  135 YVFH--QDMEQLAPEIR 149
Cdd:pfam08242  73 NVLHhlADPRAVLRNIR 89
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
56-102 1.57e-05

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


Pssm-ID: 181354  Cd Length: 187  Bit Score: 44.22  E-value: 1.57e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 767923520  56 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLQ 102
Cdd:PRK08287  35 LIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKENRQRFGCG 81
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
47-185 3.77e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 43.49  E-value: 3.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520  47 AVGSPGSpLILEVGCGSGAISLsLLSQLPQSRVIAVDKREAAISLTHENAQRLRLQDRIWIIHLDmtserSWTHLPWGPM 126
Cdd:COG4076   31 RVVKPGD-VVLDIGTGSGLLSM-LAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINAD-----ATDLDLPEKA 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767923520 127 DLIVSnppyvfhqdmEQLapeirsyeDPAALDggEEGMDIITHILAlapRLLKDSGSIF 185
Cdd:COG4076  104 DVIIS----------EML--------DTALLD--EGQVPILNHARK---RLLKPGGRII 139
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
55-134 4.66e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 42.97  E-value: 4.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520  55 LILEVGCGSGAisLSLLSQLPQ-SRVIAVDKREAAISLTHENAqrLRLQDRIWIIHLDMTSERswthlPWGPMDLIVSNP 133
Cdd:COG2263   48 TVLDLGCGTGM--LAIGAALLGaKKVVGVDIDPEALEIARENA--ERLGVRVDFIRADVTRIP-----LGGSVDTVVMNP 118


                 .
gi 767923520 134 P 134
Cdd:COG2263  119 P 119
rADc smart00650
Ribosomal RNA adenine dimethylases;
45-135 5.81e-05

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 42.50  E-value: 5.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520    45 SHAVGSPGSPlILEVGCGSGAISLSLLSQLpqSRVIAV--DKREAAISlthenAQRLRLQDRIWIIHLDMTSerswTHLP 122
Cdd:smart00650   7 RAANLRPGDT-VLEIGPGKGALTEELLERA--KRVTAIeiDPRLAPRL-----REKFAAADNLTVIHGDALK----FDLP 74

                           90
                   ....*....|...
gi 767923520   123 WGPMDLIVSNPPY 135
Cdd:smart00650  75 KLQPYKVVGNLPY 87
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 57-149 6.44e-05

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 40.73  E-value: 6.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520   57 LEVGCGSGAISLSLLSQLPqsRVIAVDKREAAISLTHENAQRLRLQdriwIIHLDMtserswTHLPW--GPMDLIVSNpp 134
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMLELAREKAPREGLT----FVVGDA------EDLPFpdNSFDLVLSS-- 66

                          90
                  ....*....|....*..
gi 767923520  135 YVFH--QDMEQLAPEIR 149
Cdd:pfam08241  67 EVLHhvEDPERALREIA 83
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 75-135 9.58e-05

23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA G2445 N2-methylase RlmL is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 439886 [Multi-domain]  Cd Length: 369  Bit Score: 42.78  E-value: 9.58e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767923520  75 PQSRVIAVDKREAAISLTHENAQRLRLQDRIWIIHLDMtserSWTHLPWGPmDLIVSNPPY 135
Cdd:COG0116  249 PPLPIFGSDIDPRAIEAARENAERAGVADLIEFEQADF----RDLEPPAEP-GLIITNPPY 304
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
56-132 1.01e-04

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 42.47  E-value: 1.01e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767923520  56 ILEVGCGSG--AIsLSLLsqLPQSRVIAVDKREAAISLTHENAQRLRLQDRIWIIHLDMTSErswthlpwGPMDLIVSN 132
Cdd:COG2264  152 VLDVGCGSGilAI-AAAK--LGAKRVLAVDIDPVAVEAARENAELNGVEDRIEVVLGDLLED--------GPYDLVVAN 219
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
56-142 1.82e-04

16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 41.85  E-value: 1.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520  56 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLQDRiwIIHLDMTSERSwthlpwGPMDLIVSNPPy 135
Cdd:PRK09489 200 VLDVGCGAGVLSAVLARHSPKIRLTLSDVSAAALESSRATLAANGLEGE--VFASNVFSDIK------GRFDMIISNPP- 270


                 ....*..
gi 767923520 136 vFHQDME 142
Cdd:PRK09489 271 -FHDGIQ 276
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 56-132 3.05e-04

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: 40.73  E-value: 3.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520   56 ILEVGCGSGAISLSLLSQLPQSRVIAVDkreaaISLT-HENAQRLRLQDRIWiIHLDMtserswTHLPWGP--MDLIVSN 132
Cdd:TIGR02072  38 VLDIGCGTGYLTRALLKRFPQAEFIALD-----ISAGmLAQAKTKLSENVQF-ICGDA------EKLPLEDssFDLIVSN 105
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 47-184 3.24e-04

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: 40.32  E-value: 3.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520  47 AVGSPGSpLILEVGCGSGAISL--SLLSqlpqSRVIAVDKREAAISLTHENAQRLRLQDrIWIIHLDMTSerswTHLPWG 124
Cdd:COG1041   22 AGAKEGD-TVLDPFCGTGTILIeaGLLG----RRVIGSDIDPKMVEGARENLEHYGYED-ADVIRGDARD----LPLADE 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520 125 PMDLIVSNPPYVfhqdmeqlapeirsyedPAALDGGEEGMDIITHILALAPRLLKDSGSI 184
Cdd:COG1041   92 SVDAIVTDPPYG-----------------RSSKISGEELLELYEKALEEAARVLKPGGRV 134
PRK15001 PRK15001
23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;
56-97 7.17e-04

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


Pssm-ID: 184963 [Multi-domain]  Cd Length: 378  Bit Score: 40.40  E-value: 7.17e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 767923520  56 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQ 97
Cdd:PRK15001 232 IVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVE 273
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 51-135 8.13e-04

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: 39.26  E-value: 8.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520   51 PGSPlILEVGCGSGAISL-----------SLLSQLPQSRVIAVDKREAAISLTHENAQRLRLQDRIWIIHLDMTSerswT 119
Cdd:pfam01170  28 PGDP-LLDPMCGSGTILIeaalmganiapGKFDARVRAPLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAAD----L 102

                          90
                  ....*....|....*.
gi 767923520  120 HLPWGPMDLIVSNPPY 135
Cdd:pfam01170 103 PLLEGSVDVIVTNPPY 118
Methyltransf_15 pfam09445
RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as ...
 55-135 2.17e-03

RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as Schizosaccharomyces pombe Tgs1 and Giardia lamblia Tgs2 catalyze methylation of the exocyclic N2 amine of 7-methylguanosine.


Pssm-ID: 370496  Cd Length: 165  Bit Score: 37.70  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520   55 LILEVGCGSGAISLSLLSQLPqsRVIAVDKREAAISLTHENAQRLRLQDRIWIIHLDMTSERSWTHLPWGPMDLIVSNPP 134
Cdd:pfam09445   3 RILDVFCGGGGNTIQFANVFD--SVISIDINLEHLACAQHNAEVYGVSDRIWLIHGDWFELLAKLKFEKIKYDCVFASPP 80


                  .
gi 767923520  135 Y 135
Cdd:pfam09445  81 W 81
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 56-132 4.41e-03

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: 37.63  E-value: 4.41e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767923520   56 ILEVGCGSG--AISLSLLSqlpQSRVIAVDKREAAISLTHENAQRLRLQDRiwiIHLDMTSErswthLPWGPMDLIVSN 132
Cdd:pfam06325 165 VLDVGCGSGilAIAALKLG---AKKVVGVDIDPVAVRAAKENAELNGVEAR---LEVYLPGD-----LPKEKADVVVAN 232
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
56-135 5.20e-03

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 37.19  E-value: 5.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520  56 ILEVGCGSGAISLSLLSQLPQSRVIAVDKReaaisLTHENAQRLRLQDRIWIIHLDMtserswTHLPWGPMDLIVSNPPY 135
Cdd:PRK14896  33 VLEIGPGKGALTDELAKRAKKVYAIELDPR-----LAEFLRDDEIAAGNVEIIEGDA------LKVDLPEFNKVVSNLPY 101
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
56-192 7.63e-03

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


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 36.85  E-value: 7.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520  56 ILEVGCGSGAISLSLLSQLP-QSRVIAVDKREAAISLTHENAQRLRLQdrIWIIHLDmtserSWTHLPWGPMDLIVSNPP 134
Cdd:COG0827  119 ILDPAVGTGNLLTTVLNQLKkKVNAYGVEVDDLLIRLAAVLANLQGHP--VELFHQD-----ALQPLLIDPVDVVISDLP 191

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767923520 135 YVFHQDmeqlapEIRSYEDPAALDggeEGMDIITHIL---ALapRLLKDSGSIFLEVdPRH 192
Cdd:COG0827  192 VGYYPN------DERAKRFKLKAD---EGHSYAHHLFieqSL--NYLKPGGYLFFLV-PSN 240
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
 50-104 9.13e-03

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


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 35.62  E-value: 9.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767923520   50 SPGSPLILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLQDR 104
Cdd:pfam13679  23 ENGPITIVDHGAGKGYLGFILYYLKYGVRVYGIDTRAELVEKANALAQKLGFNKR 77
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 56-134 9.60e-03

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 36.69  E-value: 9.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923520  56 ILEVGCGSGAISLSLLSQlpQSRVIAVDKREAAISLTHENAQRLRLqDRIWIIHLDMtsERSWTHLPWGPM-DLIVSNPP 134
Cdd:COG2265  237 VLDLYCGVGTFALPLARR--AKKVIGVEIVPEAVEDARENARLNGL-KNVEFVAGDL--EEVLPELLWGGRpDVVVLDPP 311
 
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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