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Conserved domains on  [gi|767923514|ref|XP_011532114|]
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MTRF1L release factor glutamine methyltransferase isoform X4 [Homo sapiens]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11458394)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor, such as Schizosaccharomyces pombe eRF1 methyltransferase catalytic subunit mtq2 that methylates eRF1 on Gln-182

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 ...
 43-274 1.48e-48

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


:

Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 163.01  E-value: 1.48e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514  43 ELVSHWTGVFEKRGIPEARESSEYIVAHVLGAKTFQSLrpALWTQPLTSQQLQCIRELSSRRLQRMPVQYILGEWDFQGL 122
Cdd:COG2890    5 ELLRWAAARLAAAGVDSARLEAELLLAHVLGLDRADLL--LHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFYGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514 123 SLRMVPPVFIPRPETeelvewvLEEVAQRSHAVGSPGSPLILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHEN 202
Cdd:COG2890   83 EFKVDPGVLIPRPET-------EELVELALALLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514 203 AQ------------------------------------------------SYEDPAALDGGEEGMDIITHILALAPRLLK 234
Cdd:COG2890  156 AErlgledrvrflqgdlfeplpgdgrfdlivsnppyipedeiallppevrDHEPRLALDGGEDGLDFYRRIIAQAPRLLK 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 767923514 235 DSGSIFLEVDPRHPELVSSWLQSRPdlyLNLVAVRRDFCG 274
Cdd:COG2890  236 PGGWLLLEIGEDQGEAVRALLEAAG---FADVETHKDLAG 272
 
Name Accession Description Interval E-value
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 43-274 1.48e-48

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 163.01  E-value: 1.48e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514  43 ELVSHWTGVFEKRGIPEARESSEYIVAHVLGAKTFQSLrpALWTQPLTSQQLQCIRELSSRRLQRMPVQYILGEWDFQGL 122
Cdd:COG2890    5 ELLRWAAARLAAAGVDSARLEAELLLAHVLGLDRADLL--LHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFYGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514 123 SLRMVPPVFIPRPETeelvewvLEEVAQRSHAVGSPGSPLILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHEN 202
Cdd:COG2890   83 EFKVDPGVLIPRPET-------EELVELALALLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514 203 AQ------------------------------------------------SYEDPAALDGGEEGMDIITHILALAPRLLK 234
Cdd:COG2890  156 AErlgledrvrflqgdlfeplpgdgrfdlivsnppyipedeiallppevrDHEPRLALDGGEDGLDFYRRIIAQAPRLLK 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 767923514 235 DSGSIFLEVDPRHPELVSSWLQSRPdlyLNLVAVRRDFCG 274
Cdd:COG2890  236 PGGWLLLEIGEDQGEAVRALLEAAG---FADVETHKDLAG 272
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 63-274 2.59e-44

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: 151.08  E-value: 2.59e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514   63 SSEYIVAHVLGaKTFQSLRpALWTQPLTSQQLQCIRELSSRRLQRMPVQYILGEWDFQGLSLRMVPPVFIPRPETEelve 142
Cdd:TIGR03534   1 DAELLLAHVLG-KDRAQLL-LHPEDELTPEELAAFDALLARRAAGEPVAYILGEREFYGLDFKVSPGVLIPRPETE---- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514  143 wvleevaqrsHAVGS-----PGSPLILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQS------------ 205
Cdd:TIGR03534  75 ----------ELVEAalerlKKGPRVLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKNARRlglenveflqgd 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514  206 ----------------------------------YEDPAALDGGEEGMDIITHILALAPRLLKDSGSIFLEVDPRHPELV 251
Cdd:TIGR03534 145 wfeplpsgkfdlivsnppyipeadihlldpevrdFEPRLALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAV 224

                         250       260
                  ....*....|....*....|...
gi 767923514  252 SSWLQSRPdlyLNLVAVRRDFCG 274
Cdd:TIGR03534 225 RALFEAAG---FADVETRKDLAG 244
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 59-271 8.25e-43

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 148.00  E-value: 8.25e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514  59 EARESSEYIVAHVLGaKTFQSLRpALWTQPLTSQQLQCIRELSSRRLQRMPVQYILGEWDFQGLSLRMVPPVFIPRPETE 138
Cdd:PRK09328  17 SPRLDAELLLAHVLG-LSRTDLL-LNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFWGLDFKVSPGVLIPRPETE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514 139 ELVEWVLEEVAQRSHAVgspgsplILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQS------------- 205
Cdd:PRK09328  95 ELVEWALEALLLKEPLR-------VLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHglgarveflqgdw 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514 206 ---------------------------------YEDPAALDGGEEGMDIITHILALAPRLLKDSGSIFLEVDPRHPELVS 252
Cdd:PRK09328 168 feplpggrfdlivsnppyipeadihllqpevrdHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGWLLLEIGYDQGEAVR 247

                        250
                 ....*....|....*....
gi 767923514 253 SWLqsRPDLYLNlVAVRRD 271
Cdd:PRK09328 248 ALL--AAAGFAD-VETRKD 263
PrmC_N pfam17827
PrmC N-terminal domain; This entry corresponds to the N-terminal alpha helical domain of the ...
 43-115 8.10e-14

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: 65.19  E-value: 8.10e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767923514   43 ELVSHWTGVFEKRGIPEARESSEYIVAHVLGAKTFQSLrpALWTQPLTSQQLQCIRELSSRRLQRMPVQYILG 115
Cdd:pfam17827   1 EALRWASSRLKEAGIESPRLDAELLLAHVLGLDRTDLL--LHPEEELSEEELERFEELLERRAAGEPLQYILG 71
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 163-243 1.16e-04

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: 40.88  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514 163 ILEVGCGSGAISLSLLSQlPQSRVIAVDKREAAISLTHENAQSYEDP----------AALDGGEEGMDIIT--------- 223
Cdd:cd02440    2 VLDLGCGTGALALALASG-PGARVTGVDISPVALELARKAAAALLADnvevlkgdaeELPPEADESFDVIIsdpplhhlv 80

                         90       100
                 ....*....|....*....|....
gi 767923514 224 ----HILALAPRLLKDSGSIFLEV 243
Cdd:cd02440   81 edlaRFLEEARRLLKPGGVLVLTL 104
 
Name Accession Description Interval E-value
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 43-274 1.48e-48

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 163.01  E-value: 1.48e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514  43 ELVSHWTGVFEKRGIPEARESSEYIVAHVLGAKTFQSLrpALWTQPLTSQQLQCIRELSSRRLQRMPVQYILGEWDFQGL 122
Cdd:COG2890    5 ELLRWAAARLAAAGVDSARLEAELLLAHVLGLDRADLL--LHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFYGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514 123 SLRMVPPVFIPRPETeelvewvLEEVAQRSHAVGSPGSPLILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHEN 202
Cdd:COG2890   83 EFKVDPGVLIPRPET-------EELVELALALLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514 203 AQ------------------------------------------------SYEDPAALDGGEEGMDIITHILALAPRLLK 234
Cdd:COG2890  156 AErlgledrvrflqgdlfeplpgdgrfdlivsnppyipedeiallppevrDHEPRLALDGGEDGLDFYRRIIAQAPRLLK 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 767923514 235 DSGSIFLEVDPRHPELVSSWLQSRPdlyLNLVAVRRDFCG 274
Cdd:COG2890  236 PGGWLLLEIGEDQGEAVRALLEAAG---FADVETHKDLAG 272
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 63-274 2.59e-44

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: 151.08  E-value: 2.59e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514   63 SSEYIVAHVLGaKTFQSLRpALWTQPLTSQQLQCIRELSSRRLQRMPVQYILGEWDFQGLSLRMVPPVFIPRPETEelve 142
Cdd:TIGR03534   1 DAELLLAHVLG-KDRAQLL-LHPEDELTPEELAAFDALLARRAAGEPVAYILGEREFYGLDFKVSPGVLIPRPETE---- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514  143 wvleevaqrsHAVGS-----PGSPLILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQS------------ 205
Cdd:TIGR03534  75 ----------ELVEAalerlKKGPRVLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKNARRlglenveflqgd 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514  206 ----------------------------------YEDPAALDGGEEGMDIITHILALAPRLLKDSGSIFLEVDPRHPELV 251
Cdd:TIGR03534 145 wfeplpsgkfdlivsnppyipeadihlldpevrdFEPRLALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAV 224

                         250       260
                  ....*....|....*....|...
gi 767923514  252 SSWLQSRPdlyLNLVAVRRDFCG 274
Cdd:TIGR03534 225 RALFEAAG---FADVETRKDLAG 244
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 59-271 8.25e-43

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 148.00  E-value: 8.25e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514  59 EARESSEYIVAHVLGaKTFQSLRpALWTQPLTSQQLQCIRELSSRRLQRMPVQYILGEWDFQGLSLRMVPPVFIPRPETE 138
Cdd:PRK09328  17 SPRLDAELLLAHVLG-LSRTDLL-LNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFWGLDFKVSPGVLIPRPETE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514 139 ELVEWVLEEVAQRSHAVgspgsplILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQS------------- 205
Cdd:PRK09328  95 ELVEWALEALLLKEPLR-------VLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHglgarveflqgdw 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514 206 ---------------------------------YEDPAALDGGEEGMDIITHILALAPRLLKDSGSIFLEVDPRHPELVS 252
Cdd:PRK09328 168 feplpggrfdlivsnppyipeadihllqpevrdHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGWLLLEIGYDQGEAVR 247

                        250
                 ....*....|....*....
gi 767923514 253 SWLqsRPDLYLNlVAVRRD 271
Cdd:PRK09328 248 ALL--AAAGFAD-VETRKD 263
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 64-243 1.47e-26

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: 105.51  E-value: 1.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514   64 SEYIVAHVLGAKTFQSLrpALWTQPLTSQQLQCIRELSSRRLQRMPVQYILGEWDFQGLSLRMVPPVFIPRPETeelvew 143
Cdd:TIGR00536  27 ALLLLEHDLGRERDLLL--AFLTEELTPDEKERIFRLVLRRVKGVPVAYLLGSKEFYGLEFFVNEHVLIPRPET------ 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514  144 vlEEVAQRSHAVGSPGSPL--ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENA------------QSY--- 206
Cdd:TIGR00536  99 --EELVEKALASLISQPPIlhILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAeknqlehrvefiQSNlfe 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767923514  207 -------------------EDPA------------ALDGGEEGMDIITHILALAPRLLKDSGSIFLEV 243
Cdd:TIGR00536 177 plagqkidiivsnppyideEDLAdlpnvvrfepllALVGGDDGLNILRQIIELAPDYLKPNGFLVCEI 244
PrmC_N pfam17827
PrmC N-terminal domain; This entry corresponds to the N-terminal alpha helical domain of the ...
 43-115 8.10e-14

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: 65.19  E-value: 8.10e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767923514   43 ELVSHWTGVFEKRGIPEARESSEYIVAHVLGAKTFQSLrpALWTQPLTSQQLQCIRELSSRRLQRMPVQYILG 115
Cdd:pfam17827   1 EALRWASSRLKEAGIESPRLDAELLLAHVLGLDRTDLL--LHPEEELSEEELERFEELLERRAAGEPLQYILG 71
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
 89-207 7.09e-10

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


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 59.49  E-value: 7.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514  89 LTSQQLQCIRELSSRRLQRMPVQYILGEWDFQGLSLRMVPPVFIPRPETEELVEWVLEEVAQRSHAV-------GSPGSP 161
Cdd:PRK01544  51 LNEAEIEAFEKLLERRLKHEPIAYITGVKEFYSREFIVNKHVLIPRSDTEVLVDVVFQCHSRESGNPekkqlnpCFRGND 130

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767923514 162 L----------ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQSYE 207
Cdd:PRK01544 131 IssncndkflnILELGTGSGCIAISLLCELPNANVIATDISLDAIEVAKSNAIKYE 186
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 163-241 2.28e-09

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: 55.97  E-value: 2.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514 163 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQ-------------SYEDPAAL------------DGGEE 217
Cdd:COG2813   53 VLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAanglenvevlwsdGLSGVPDGsfdlilsnppfhAGRAV 132

                         90       100
                 ....*....|....*....|....
gi 767923514 218 GMDIITHILALAPRLLKDSGSIFL 241
Cdd:COG2813  133 DKEVAHALIADAARHLRPGGELWL 156
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 163-241 8.97e-09

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: 52.72  E-value: 8.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514  163 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQSY----------EDPAALD-----------GGEEGMdi 221
Cdd:TIGR02469  23 LWDIGAGTGSVTIEAARLVPNGRVYAIERNPEALDLIERNLRRFgvsnivivegDAPEAPEallpdpdavfvGGSGGL-- 100

                          90       100
                  ....*....|....*....|
gi 767923514  222 ITHILALAPRLLKDSGSIFL 241
Cdd:TIGR02469 101 LQEILEAVERRLRPGGRIVL 120
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 158-214 8.79e-07

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: 49.78  E-value: 8.79e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767923514 158 PGSpLILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQSY----------EDPAALDG 214
Cdd:COG2242  247 PGD-VLWDIGAGSGSVSIEAARLAPGGRVYAIERDPERAALIRANARRFgvpnvevvegEAPEALAD 312
PRK14968 PRK14968
putative methyltransferase; Provisional
 163-253 8.83e-07

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 48.36  E-value: 8.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514 163 ILEVGCGSGAISLSLLSQlpQSRVIAVDKREAAISLTHENAQS------------------------------------- 205
Cdd:PRK14968  27 VLEVGTGSGIVAIVAAKN--GKKVVGVDINPYAVECAKCNAKLnnirnngvevirsdlfepfrgdkfdvilfnppylpte 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767923514 206 ----YEDPA--ALDGGEEGMDIITHILALAPRLLKDSGSIFLevdprhpeLVSS 253
Cdd:PRK14968 105 eeeeWDDWLnyALSGGKDGREVIDRFLDEVGRYLKPGGRILL--------LQSS 150
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 158-251 3.17e-06

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 46.83  E-value: 3.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514 158 PGSPLILEVGCGSGAiSLSLLSQLPQSRVIAVDKREAAISLTHENAQ------------SYEDPAALDggEEGMDIIT-- 223
Cdd:COG0500   25 PKGGRVLDLGCGTGR-NLLALAARFGGRVIGIDLSPEAIALARARAAkaglgnveflvaDLAELDPLP--AESFDLVVaf 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767923514 224 ------------HILALAPRLLKDSGSIFLEVDPRHPELV 251
Cdd:COG0500  102 gvlhhlppeereALLRELARALKPGGVLLLSASDAAAALS 141
PRK14966 PRK14966
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; ...
 100-203 4.32e-06

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


Pssm-ID: 184930 [Multi-domain]  Cd Length: 423  Bit Score: 47.77  E-value: 4.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514 100 LSSRRLQRMPVQYILGEWDFQGLSLRMVPPVFIPRPETEELVEWVLEEVaqrshavgsPGSPLILEVGCGSGAISLSLLS 179
Cdd:PRK14966 201 LAQRRLNGEPVAYILGVREFYGRRFAVNPNVLIPRPETEHLVEAVLARL---------PENGRVWDLGTGSGAVAVTVAL 271

                         90       100
                 ....*....|....*....|....
gi 767923514 180 QLPQSRVIAVDKREAAISLTHENA 203
Cdd:PRK14966 272 ERPDAFVRASDISPPALETARKNA 295
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 163-204 5.02e-06

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: 46.68  E-value: 5.02e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 767923514 163 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQ 204
Cdd:COG4123   41 VLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVA 82
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 163-228 8.11e-06

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 43.71  E-value: 8.11e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767923514  163 ILEVGCGSGAISLsLLSQLPQSRVIAVDKREAAISLTHENAQSYE--------DPAALDGGEEGMDIITHILAL 228
Cdd:pfam13649   1 VLDLGCGTGRLTL-ALARRGGARVTGVDLSPEMLERARERAAEAGlnvefvqgDAEDLPFPDGSFDLVVSSGVL 73
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 163-243 9.85e-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: 9.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514 163 ILEVGCGSGAISLSLLSQlpQSRVIAVDKREAAISLTHENAQSYE------DPAALDGGEEGMDIIT------HI----- 225
Cdd:COG2227   28 VLDVGCGTGRLALALARR--GADVTGVDISPEALEIARERAAELNvdfvqgDLEDLPLEDGSFDLVIcsevleHLpdpaa 105

                         90
                 ....*....|....*....
gi 767923514 226 -LALAPRLLKDSGSIFLEV 243
Cdd:COG2227  106 lLRELARLLKPGGLLLLST 124
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
163-196 3.32e-05

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 42.12  E-value: 3.32e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 767923514 163 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAI 196
Cdd:COG4106    5 VLDLGCGTGRLTALLAERFPGARVTGVDLSPEML 38
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 163-241 4.44e-05

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: 42.96  E-value: 4.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514  163 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQS-------------YED--PAALD----------GGEE 217
Cdd:pfam05175  35 VLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAAnglengevvasdvYSGveDGKFDliisnppfhaGLAT 114

                          90       100
                  ....*....|....*....|....
gi 767923514  218 GMDIITHILALAPRLLKDSGSIFL 241
Cdd:pfam05175 115 TYNVAQRFIADAKRHLRPGGELWI 138
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 163-257 1.10e-04

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: 41.52  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514 163 ILEVGCGSGAISLSLLSQlpQSRVIAVDKREAAISLTHENAQSYE--------DPAALDGGEEGMDIITHILAL--AP-- 230
Cdd:COG2226   26 VLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGlnvefvvgDAEDLPFPDGSFDLVISSFVLhhLPdp 103

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767923514 231 --------RLLKDSGS-IFLEVDPRHPELVSSWLQS 257
Cdd:COG2226  104 eralaeiaRVLKPGGRlVVVDFSPPDLAELEELLAE 139
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 163-243 1.16e-04

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: 40.88  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514 163 ILEVGCGSGAISLSLLSQlPQSRVIAVDKREAAISLTHENAQSYEDP----------AALDGGEEGMDIIT--------- 223
Cdd:cd02440    2 VLDLGCGTGALALALASG-PGARVTGVDISPVALELARKAAAALLADnvevlkgdaeELPPEADESFDVIIsdpplhhlv 80

                         90       100
                 ....*....|....*....|....
gi 767923514 224 ----HILALAPRLLKDSGSIFLEV 243
Cdd:cd02440   81 edlaRFLEEARRLLKPGGVLVLTL 104
PRK15001 PRK15001
23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;
163-216 1.30e-04

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


Pssm-ID: 184963 [Multi-domain]  Cd Length: 378  Bit Score: 43.09  E-value: 1.30e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767923514 163 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQSyEDPAALDGGE 216
Cdd:PRK15001 232 IVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVET-NMPEALDRCE 284
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 158-193 1.99e-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: 42.07  E-value: 1.99e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 767923514 158 PGSpLILEVGCGSGAISLSLLSQL-PQSRVIAVDKRE 193
Cdd:COG2519   91 PGA-RVLEAGTGSGALTLALARAVgPEGKVYSYERRE 126
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 163-243 3.32e-04

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 40.94  E-value: 3.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514 163 ILEVGCGSGAISL--SLLSQlPQSRVIAVDKREAAISLTHENAQSY-----------EDPAALD-------------GGE 216
Cdd:PRK00377  44 ILDIGCGTGSVTVeaSLLVG-ETGKVYAVDKDEKAINLTRRNAEKFgvlnnivlikgEAPEILFtinekfdrifiggGSE 122

                         90       100
                 ....*....|....*....|....*..
gi 767923514 217 EgmdiITHILALAPRLLKDSGSIFLEV 243
Cdd:PRK00377 123 K----LKEIISASWEIIKKGGRIVIDA 145
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
163-204 3.62e-04

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


Pssm-ID: 181354  Cd Length: 187  Bit Score: 40.76  E-value: 3.62e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 767923514 163 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQ 204
Cdd:PRK08287  35 LIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKENRQ 76
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 163-205 4.18e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 40.09  E-value: 4.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 767923514  163 ILEVGCGSGAISLSLLSQL-PQSRVIAVDKREAAISLTHENAQS 205
Cdd:pfam13847   7 VLDLGCGTGHLSFELAEELgPNAEVVGIDISEEAIEKARENAQK 50
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 164-228 6.06e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 38.50  E-value: 6.06e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767923514  164 LEVGCGSGAISLSLLSQLPQSRVIAVD----------KREAAISLTHENAQSYEDPAALDGGEEGMDIITHILAL 228
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDispaaleaarERLAALGLLNAVRVELFQLDLGELDPGSFDVVVASNVL 75
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
163-241 7.22e-04

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 40.14  E-value: 7.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514 163 ILEVGCGSG--AISLSLLSqlpQSRVIAVDKREAAISLTHENAQ--SYEDPAALDGGEEGMDIIT-HILA-----LAP-- 230
Cdd:PRK00517 123 VLDVGCGSGilAIAAAKLG---AKKVLAVDIDPQAVEAARENAElnGVELNVYLPQGDLKADVIVaNILAnplleLAPdl 199

                         90
                 ....*....|..
gi 767923514 231 -RLLKDSGSIFL 241
Cdd:PRK00517 200 aRLLKPGGRLIL 211
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
154-256 3.31e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 38.09  E-value: 3.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923514 154 AVGSPGSpLILEVGCGSGAISLsLLSQLPQSRVIAVD---------KREAA-------ISLTHENAQSYEDPAALD---- 213
Cdd:COG4076   31 RVVKPGD-VVLDIGTGSGLLSM-LAARAGAKKVYAVEvnpdiaavaRRIIAanglsdrITVINADATDLDLPEKADviis 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767923514 214 ------GGEEGM-DIITHILAlapRLLKDSGSIFlevdprhPELVSSWLQ 256
Cdd:COG4076  109 emldtaLLDEGQvPILNHARK---RLLKPGGRII-------PERITNAAQ 148
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 163-190 5.19e-03

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: 37.65  E-value: 5.19e-03
                          10        20
                  ....*....|....*....|....*...
gi 767923514  163 ILEVGCGSGAISLSLLSQLPQSRVIAVD 190
Cdd:TIGR02072  38 VLDIGCGTGYLTRALLKRFPQAEFIALD 65
 
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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