NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|564365382|ref|XP_006243790|]
View 

MTRF1L release factor glutamine methyltransferase isoform X1 [Rattus norvegicus]

Protein Classification

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

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 45-338 3.66e-77

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


:

Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 238.13  E-value: 3.66e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382  45 IVNHWTRVFEERGIPEARESSEYIVAHVLGAKTFQSLrpALWTKPLTPQQLECIQELCNHRLQRMPVQYILGEWDFQGLN 124
Cdd:COG2890    6 LLRWAAARLAAAGVDSARLEAELLLAHVLGLDRADLL--LHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFYGLE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 125 LKMAPPVFIPRPETEELVEWVLEevaqrppAVRAQDGPLILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENA 204
Cdd:COG2890   84 FKVDPGVLIPRPETEELVELALA-------LLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 205 QRLQLQDRIRIIHLDITSEgccthLLPWGPMDLVVSNPPYIFRKDMEQLAPEIRSYEDLVALDGGDEGMDIITHILTLAP 284
Cdd:COG2890  157 ERLGLEDRVRFLQGDLFEP-----LPGDGRFDLIVSNPPYIPEDEIALLPPEVRDHEPRLALDGGEDGLDFYRRIIAQAP 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564365382 285 WLLNASGSIFLEVDPRHPELVSSWLQSQPdlhLSLVGVREDFCGRPRFLHVQKS 338
Cdd:COG2890  232 RLLKPGGWLLLEIGEDQGEAVRALLEAAG---FADVETHKDLAGRDRVVVARRP 282
 
Name Accession Description Interval E-value
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 45-338 3.66e-77

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 238.13  E-value: 3.66e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382  45 IVNHWTRVFEERGIPEARESSEYIVAHVLGAKTFQSLrpALWTKPLTPQQLECIQELCNHRLQRMPVQYILGEWDFQGLN 124
Cdd:COG2890    6 LLRWAAARLAAAGVDSARLEAELLLAHVLGLDRADLL--LHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFYGLE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 125 LKMAPPVFIPRPETEELVEWVLEevaqrppAVRAQDGPLILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENA 204
Cdd:COG2890   84 FKVDPGVLIPRPETEELVELALA-------LLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 205 QRLQLQDRIRIIHLDITSEgccthLLPWGPMDLVVSNPPYIFRKDMEQLAPEIRSYEDLVALDGGDEGMDIITHILTLAP 284
Cdd:COG2890  157 ERLGLEDRVRFLQGDLFEP-----LPGDGRFDLIVSNPPYIPEDEIALLPPEVRDHEPRLALDGGEDGLDFYRRIIAQAP 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564365382 285 WLLNASGSIFLEVDPRHPELVSSWLQSQPdlhLSLVGVREDFCGRPRFLHVQKS 338
Cdd:COG2890  232 RLLKPGGWLLLEIGEDQGEAVRALLEAAG---FADVETHKDLAGRDRVVVARRP 282
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 64-333 8.11e-69

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: 215.41  E-value: 8.11e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382   64 SSEYIVAHVLGaKTFQSLRpALWTKPLTPQQLECIQELCNHRLQRMPVQYILGEWDFQGLNLKMAPPVFIPRPETEELve 143
Cdd:TIGR03534   1 DAELLLAHVLG-KDRAQLL-LHPEDELTPEELAAFDALLARRAAGEPVAYILGEREFYGLDFKVSPGVLIPRPETEEL-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382  144 wvleevaqrppaV-----RAQDGPLILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLqDRIRIIHL 218
Cdd:TIGR03534  77 ------------VeaaleRLKKGPRVLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKNARRLGL-ENVEFLQG 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382  219 DITSEgccthlLPWGPMDLVVSNPPYIFRKDMEQLAPEIRSYEDLVALDGGDEGMDIITHILTLAPWLLNASGSIFLEVD 298
Cdd:TIGR03534 144 DWFEP------LPSGKFDLIVSNPPYIPEADIHLLDPEVRDFEPRLALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIG 217

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 564365382  299 PRHPELVSSWLQSQPdlhLSLVGVREDFCGRPRFL 333
Cdd:TIGR03534 218 YDQGEAVRALFEAAG---FADVETRKDLAGKDRVV 249
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 60-337 1.51e-67

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 213.10  E-value: 1.51e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382  60 EARESSEYIVAHVLGaKTFQSLRpALWTKPLTPQQLECIQELCNHRLQRMPVQYILGEWDFQGLNLKMAPPVFIPRPETE 139
Cdd:PRK09328  17 SPRLDAELLLAHVLG-LSRTDLL-LNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFWGLDFKVSPGVLIPRPETE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 140 ELVEWVLEEVAQRPPAVraqdgplILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLqLQDRIRIIHLD 219
Cdd:PRK09328  95 ELVEWALEALLLKEPLR-------VLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHG-LGARVEFLQGD 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 220 ITSEgccthlLPWGPMDLVVSNPPYIFRKDMEQLAPEIRSYEDLVALDGGDEGMDIITHILTLAPWLLNASGSIFLEVDP 299
Cdd:PRK09328 167 WFEP------LPGGRFDLIVSNPPYIPEADIHLLQPEVRDHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGWLLLEIGY 240

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 564365382 300 RHPELVSSWLQSQpdlHLSLVGVREDFCGRPRFLHVQK 337
Cdd:PRK09328 241 DQGEAVRALLAAA---GFADVETRKDLAGRDRVVLGRR 275
PrmC_N pfam17827
PrmC N-terminal domain; This entry corresponds to the N-terminal alpha helical domain of the ...
 45-116 2.95e-13

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: 64.04  E-value: 2.95e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564365382   45 IVNHWTRVFEERGIPEARESSEYIVAHVLG-AKTFQSLRPalwTKPLTPQQLECIQELCNHRLQRMPVQYILG 116
Cdd:pfam17827   2 ALRWASSRLKEAGIESPRLDAELLLAHVLGlDRTDLLLHP---EEELSEEELERFEELLERRAAGEPLQYILG 71
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 164-258 2.96e-10

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: 56.67  E-value: 2.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 164 ILEVGCGSGAIALSLLSQlPKTQVIAVDKEEAAVSLTLENAQRLqLQDRIRIIHLDITSEgcctHLLPWGPMDLVVSNPP 243
Cdd:cd02440    2 VLDLGCGTGALALALASG-PGARVTGVDISPVALELARKAAAAL-LADNVEVLKGDAEEL----PPEADESFDVIISDPP 75

                         90
                 ....*....|....*.
gi 564365382 244 YIFRK-DMEQLAPEIR 258
Cdd:cd02440   76 LHHLVeDLARFLEEAR 91
rADc smart00650
Ribosomal RNA adenine dimethylases;
155-252 2.59e-05

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 44.04  E-value: 2.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382   155 AVRAQDGPLILEVGCGSGAIALSLLSQLPKtqVIAVDKEEAAVSLTlenAQRLQLQDRIRIIHLDItsegCCTHLLPWGP 234
Cdd:smart00650   8 AANLRPGDTVLEIGPGKGALTEELLERAKR--VTAIEIDPRLAPRL---REKFAAADNLTVIHGDA----LKFDLPKLQP 78

                           90       100
                   ....*....|....*....|...
gi 564365382   235 mDLVVSNPPY-----IFRKDMEQ 252
Cdd:smart00650  79 -YKVVGNLPYnistpILFKLLEE 100
 
Name Accession Description Interval E-value
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 45-338 3.66e-77

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 238.13  E-value: 3.66e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382  45 IVNHWTRVFEERGIPEARESSEYIVAHVLGAKTFQSLrpALWTKPLTPQQLECIQELCNHRLQRMPVQYILGEWDFQGLN 124
Cdd:COG2890    6 LLRWAAARLAAAGVDSARLEAELLLAHVLGLDRADLL--LHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFYGLE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 125 LKMAPPVFIPRPETEELVEWVLEevaqrppAVRAQDGPLILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENA 204
Cdd:COG2890   84 FKVDPGVLIPRPETEELVELALA-------LLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 205 QRLQLQDRIRIIHLDITSEgccthLLPWGPMDLVVSNPPYIFRKDMEQLAPEIRSYEDLVALDGGDEGMDIITHILTLAP 284
Cdd:COG2890  157 ERLGLEDRVRFLQGDLFEP-----LPGDGRFDLIVSNPPYIPEDEIALLPPEVRDHEPRLALDGGEDGLDFYRRIIAQAP 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564365382 285 WLLNASGSIFLEVDPRHPELVSSWLQSQPdlhLSLVGVREDFCGRPRFLHVQKS 338
Cdd:COG2890  232 RLLKPGGWLLLEIGEDQGEAVRALLEAAG---FADVETHKDLAGRDRVVVARRP 282
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 64-333 8.11e-69

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: 215.41  E-value: 8.11e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382   64 SSEYIVAHVLGaKTFQSLRpALWTKPLTPQQLECIQELCNHRLQRMPVQYILGEWDFQGLNLKMAPPVFIPRPETEELve 143
Cdd:TIGR03534   1 DAELLLAHVLG-KDRAQLL-LHPEDELTPEELAAFDALLARRAAGEPVAYILGEREFYGLDFKVSPGVLIPRPETEEL-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382  144 wvleevaqrppaV-----RAQDGPLILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLqDRIRIIHL 218
Cdd:TIGR03534  77 ------------VeaaleRLKKGPRVLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKNARRLGL-ENVEFLQG 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382  219 DITSEgccthlLPWGPMDLVVSNPPYIFRKDMEQLAPEIRSYEDLVALDGGDEGMDIITHILTLAPWLLNASGSIFLEVD 298
Cdd:TIGR03534 144 DWFEP------LPSGKFDLIVSNPPYIPEADIHLLDPEVRDFEPRLALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIG 217

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 564365382  299 PRHPELVSSWLQSQPdlhLSLVGVREDFCGRPRFL 333
Cdd:TIGR03534 218 YDQGEAVRALFEAAG---FADVETRKDLAGKDRVV 249
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 60-337 1.51e-67

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 213.10  E-value: 1.51e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382  60 EARESSEYIVAHVLGaKTFQSLRpALWTKPLTPQQLECIQELCNHRLQRMPVQYILGEWDFQGLNLKMAPPVFIPRPETE 139
Cdd:PRK09328  17 SPRLDAELLLAHVLG-LSRTDLL-LNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFWGLDFKVSPGVLIPRPETE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 140 ELVEWVLEEVAQRPPAVraqdgplILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLqLQDRIRIIHLD 219
Cdd:PRK09328  95 ELVEWALEALLLKEPLR-------VLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHG-LGARVEFLQGD 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 220 ITSEgccthlLPWGPMDLVVSNPPYIFRKDMEQLAPEIRSYEDLVALDGGDEGMDIITHILTLAPWLLNASGSIFLEVDP 299
Cdd:PRK09328 167 WFEP------LPGGRFDLIVSNPPYIPEADIHLLQPEVRDHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGWLLLEIGY 240

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 564365382 300 RHPELVSSWLQSQpdlHLSLVGVREDFCGRPRFLHVQK 337
Cdd:PRK09328 241 DQGEAVRALLAAA---GFADVETRKDLAGRDRVVLGRR 275
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 65-297 1.40e-49

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: 167.14  E-value: 1.40e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382   65 SEYIVAHVLGAKTFQSLrpALWTKPLTPQQLECIQELCNHRLQRMPVQYILGEWDFQGLNLKMAPPVFIPRPETEELVEW 144
Cdd:TIGR00536  27 ALLLLEHDLGRERDLLL--AFLTEELTPDEKERIFRLVLRRVKGVPVAYLLGSKEFYGLEFFVNEHVLIPRPETEELVEK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382  145 VLEEVAQRPPAVRaqdgplILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLQDRIRIIHLDITSEg 224
Cdd:TIGR00536 105 ALASLISQPPILH------ILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQLEHRVEFIQSNLFEP- 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564365382  225 ccthlLPWGPMDLVVSNPPYIFRKDMEQLAPEIRsYEDLVALDGGDEGMDIITHILTLAPWLLNASGSIFLEV 297
Cdd:TIGR00536 178 -----LAGQKIDIIVSNPPYIDEEDLADLPNVVR-FEPLLALVGGDDGLNILRQIIELAPDYLKPNGFLVCEI 244
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
 88-306 4.84e-23

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


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 99.55  E-value: 4.84e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382  88 KPLTPQQLECIQELCNHRLQRMPVQYILGEWDFQGLNLKMAPPVFIPRPETE-------ELVEWVLEEVAQRPPAVRAQD 160
Cdd:PRK01544  49 EQLNEAEIEAFEKLLERRLKHEPIAYITGVKEFYSREFIVNKHVLIPRSDTEvlvdvvfQCHSRESGNPEKKQLNPCFRG 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 161 GPL----------ILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLQDRIRIIHLDITSEgccthlL 230
Cdd:PRK01544 129 NDIssncndkflnILELGTGSGCIAISLLCELPNANVIATDISLDAIEVAKSNAIKYEVTDRIQIIHSNWFEN------I 202

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564365382 231 PWGPMDLVVSNPPYIFRKDMEQLAPEIRSYEDLVALDGGDEGMDIITHILTLAPWLLNASGSIFLEVDPRHPELVS 306
Cdd:PRK01544 203 EKQKFDFIVSNPPYISHSEKSEMAIETINYEPSIALFAEEDGLQAYFIIAENAKQFLKPNGKIILEIGFKQEEAVT 278
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 155-244 1.37e-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: 86.35  E-value: 1.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 155 AVRAQDGPLILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLQDRIRIIHLDITSegcCTHLLPWGP 234
Cdd:COG4123   32 FAPVKKGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKE---FAAELPPGS 108

                         90
                 ....*....|
gi 564365382 235 MDLVVSNPPY 244
Cdd:COG4123  109 FDLVVSNPPY 118
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 164-295 1.98e-17

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: 79.08  E-value: 1.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 164 ILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLQDrIRIIHLDITSEgccthlLPWGPMDLVVSNPP 243
Cdd:COG2813   53 VLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAANGLEN-VEVLWSDGLSG------VPDGSFDLILSNPP 125

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564365382 244 yiFRkdmeqlapeirsyedlvalDGGDEGMDIITHILTLAPWLLNASGSIFL 295
Cdd:COG2813  126 --FH-------------------AGRAVDKEVAHALIADAARHLRPGGELWL 156
PrmC_N pfam17827
PrmC N-terminal domain; This entry corresponds to the N-terminal alpha helical domain of the ...
 45-116 2.95e-13

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: 64.04  E-value: 2.95e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564365382   45 IVNHWTRVFEERGIPEARESSEYIVAHVLG-AKTFQSLRPalwTKPLTPQQLECIQELCNHRLQRMPVQYILG 116
Cdd:pfam17827   2 ALRWASSRLKEAGIESPRLDAELLLAHVLGlDRTDLLLHP---EEELSEEELERFEELLERRAAGEPLQYILG 71
PRK14966 PRK14966
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; ...
 101-296 7.18e-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: 7.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 101 LCNHRLQRMPVQYILGEWDFQGLNLKMAPPVFIPRPETeelVEWVLEEVAQRPPAVRAQDgplileVGCGSGAIALSLLS 180
Cdd:PRK14966 201 LAQRRLNGEPVAYILGVREFYGRRFAVNPNVLIPRPET---EHLVEAVLARLPENGRVWD------LGTGSGAVAVTVAL 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 181 QLPKTQVIAVDKEEAAVSLTLENAQrlQLQDRIRIIH-----LDITSEGccthllPWgpmDLVVSNPPYIFRKDMEQLAP 255
Cdd:PRK14966 272 ERPDAFVRASDISPPALETARKNAA--DLGARVEFAHgswfdTDMPSEG------KW---DIIVSNPPYIENGDKHLLQG 340

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 564365382 256 EIRsYEDLVALDGGDEGMDIITHILTLAPWLLNASGSIFLE 296
Cdd:PRK14966 341 DLR-FEPQIALTDFSDGLSCIRTLAQGAPDRLAEGGFLLLE 380
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 164-295 1.46e-12

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: 64.92  E-value: 1.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382  164 ILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLqDRIRIIHLDITSEgccthlLPWGPMDLVVSNPP 243
Cdd:pfam05175  35 VLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGL-ENGEVVASDVYSG------VEDGKFDLIISNPP 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564365382  244 yiFRkdmeqlapeirsyedlvalDGGDEGMDIITHILTLAPWLLNASGSIFL 295
Cdd:pfam05175 108 --FH-------------------AGLATTYNVAQRFIADAKRHLRPGGELWI 138
PRK14968 PRK14968
putative methyltransferase; Provisional
 155-307 1.94e-11

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 62.22  E-value: 1.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 155 AVRAQDGPLILEVGCGSGAIALSLLSQLPKtqVIAVDKEEAAVSLTLENAQRLQLQDR-IRIIHLDITSegCCTHllpwG 233
Cdd:PRK14968  18 NAVDKKGDRVLEVGTGSGIVAIVAAKNGKK--VVGVDINPYAVECAKCNAKLNNIRNNgVEVIRSDLFE--PFRG----D 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564365382 234 PMDLVVSNPPYIFRKDMEqlapEIRSYEDLvALDGGDEGMDIITHILTLAPWLLNASGSIFLevdprhpeLVSS 307
Cdd:PRK14968  90 KFDVILFNPPYLPTEEEE----EWDDWLNY-ALSGGKDGREVIDRFLDEVGRYLKPGGRILL--------LQSS 150
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 157-216 1.97e-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: 57.72  E-value: 1.97e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382  157 RAQDGPLILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLqDRIRII 216
Cdd:TIGR02469  16 RLRPGDVLWDIGAGTGSVTIEAARLVPNGRVYAIERNPEALDLIERNLRRFGV-SNIVIV 74
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 164-258 2.96e-10

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: 56.67  E-value: 2.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 164 ILEVGCGSGAIALSLLSQlPKTQVIAVDKEEAAVSLTLENAQRLqLQDRIRIIHLDITSEgcctHLLPWGPMDLVVSNPP 243
Cdd:cd02440    2 VLDLGCGTGALALALASG-PGARVTGVDISPVALELARKAAAAL-LADNVEVLKGDAEEL----PPEADESFDVIISDPP 75

                         90
                 ....*....|....*.
gi 564365382 244 YIFRK-DMEQLAPEIR 258
Cdd:cd02440   76 LHHLVeDLARFLEEAR 91
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 164-258 1.96e-09

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 54.11  E-value: 1.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382  164 ILEVGCGSGAIALsLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLqdRIRIIHLDItsegccTHL-LPWGPMDLVVSNP 242
Cdd:pfam13649   1 VLDLGCGTGRLTL-ALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDA------EDLpFPDGSFDLVVSSG 71

                          90
                  ....*....|....*...
gi 564365382  243 P--YIFRKDMEQLAPEIR 258
Cdd:pfam13649  72 VlhHLPDPDLEAALREIA 89
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
164-241 9.24e-09

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 52.13  E-value: 9.24e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564365382 164 ILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAvsltLENAQrlQLQDRIRIIHLDItsegccTHLLPWGPMDLVVSN 241
Cdd:COG4106    5 VLDLGCGTGRLTALLAERFPGARVTGVDLSPEM----LARAR--ARLPNVRFVVADL------RDLDPPEPFDLVVSN 70
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 156-217 1.69e-08

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: 55.56  E-value: 1.69e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 156 VRA--------QDGPLILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLqDRIRIIH 217
Cdd:COG2242  235 VRAltlaklalRPGDVLWDIGAGSGSVSIEAARLAPGGRVYAIERDPERAALIRANARRFGV-PNVEVVE 303
PRK14967 PRK14967
putative methyltransferase; Provisional
 161-295 7.83e-08

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 52.36  E-value: 7.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 161 GPLILEVGCGSGAIALSLlSQLPKTQVIAVDKEEAAVSLTLENAqrLQLQDRIRIIHLDITSEgccthlLPWGPMDLVVS 240
Cdd:PRK14967  37 GRRVLDLCTGSGALAVAA-AAAGAGSVTAVDISRRAVRSARLNA--LLAGVDVDVRRGDWARA------VEFRPFDVVVS 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564365382 241 NPPYIFRKDMeqlAPEIRSYEDlvALDGGDEGMDIITHILTLAPWLLNASGSIFL 295
Cdd:PRK14967 108 NPPYVPAPPD---APPSRGPAR--AWDAGPDGRAVLDRLCDAAPALLAPGGSLLL 157
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
164-260 9.42e-08

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 52.48  E-value: 9.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 164 ILEVGCGSG--AIALSLLsqlPKTQVIAVDKEEAAVSLTLENAQRLQLQDRIRIIHLDITSEgccthllpwGPMDLVVSN 241
Cdd:COG2264  152 VLDVGCGSGilAIAAAKL---GAKRVLAVDIDPVAVEAARENAELNGVEDRIEVVLGDLLED---------GPYDLVVAN 219

                         90
                 ....*....|....*....
gi 564365382 242 ppyIFRKDMEQLAPEIRSY 260
Cdd:COG2264  220 ---ILANPLIELAPDLAAL 235
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
160-243 1.02e-07

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 51.44  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 160 DGPLILEVGCGSG--AIALSLLSqlPKtQVIAVDKEEAAVSLTLENAQRLQlqDRIRIIHLDITsegcctHLLPWGPMDL 237
Cdd:COG2263   45 EGKTVLDLGCGTGmlAIGAALLG--AK-KVVGVDIDPEALEIARENAERLG--VRVDFIRADVT------RIPLGGSVDT 113


                 ....*.
gi 564365382 238 VVSNPP 243
Cdd:COG2263  114 VVMNPP 119
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 164-241 3.73e-07

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 48.95  E-value: 3.73e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564365382  164 ILEVGCGSGAIALSLLSQL-PKTQVIAVDKEEAAVSLTLENAQRLQLqDRIRIIHLDITSEGCcthLLPWGPMDLVVSN 241
Cdd:pfam13847   7 VLDLGCGTGHLSFELAEELgPNAEVVGIDISEEAIEKARENAQKLGF-DNVEFEQGDIEELPE---LLEDDKFDVVISN 81
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 155-240 4.10e-07

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 49.16  E-value: 4.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 155 AVRAQDGPLILEVGCGSGAIALSLLSQLpKTQVIAVDKEEAAVSLTLENAQRLQLQDRIRIIHLDItsegccTHLLPWGP 234
Cdd:COG2230   46 KLGLKPGMRVLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADY------RDLPADGQ 118


                 ....*.
gi 564365382 235 MDLVVS 240
Cdd:COG2230  119 FDAIVS 124
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 157-241 6.30e-07

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 49.14  E-value: 6.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 157 RAQDGPLILEVGCGSGAIALsLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLqDRIRIIHLDITSegccTHLLPWGPMD 236
Cdd:COG0500   23 RLPKGGRVLDLGCGTGRNLL-ALAARFGGRVIGIDLSPEAIALARARAAKAGL-GNVEFLVADLAE----LDPLPAESFD 96


                 ....*
gi 564365382 237 LVVSN 241
Cdd:COG0500   97 LVVAF 101
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 164-239 8.85e-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: 49.39  E-value: 8.85e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564365382 164 ILEVGCGSGAIALSLLSQL-PKTQVIAVDKEEAAVSLTLENAQRLQLQDRIRIIHLDItSEGccthlLPWGPMDLVV 239
Cdd:COG2519   95 VLEAGTGSGALTLALARAVgPEGKVYSYERREDFAEIARKNLERFGLPDNVELKLGDI-REG-----IDEGDVDAVF 165
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 155-314 1.46e-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: 47.93  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382  155 AVRAQDGPLILEVGCGSGAIALSLLSQLPKtqVIAVDKEEAAVSLTLENAQRLQLQdrIRIIHLDItSEGCCthllpwGP 234
Cdd:TIGR00537  14 NLRELKPDDVLEIGAGTGLVAIRLKGKGKC--ILTTDINPFAVKELRENAKLNNVG--LDVVMTDL-FKGVR------GK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382  235 MDLVVSNPPYIFRKDMEQlapeIRSYEDlVALDGGDEGMDIITHILTLAPWLLNASGSIflevdprhpELVSSWLQSQPD 314
Cdd:TIGR00537  83 FDVILFNPPYLPLEDDLR----RGDWLD-VAIDGGKDGRKVIDRFLDELPEILKEGGRV---------QLIQSSLNGEPD 148
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 155-258 3.22e-06

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: 46.14  E-value: 3.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 155 AVRAQDGPLILEVGCGSGAIALSLLSQlpKTQVIAVDKEEAAVSLTLENAQRLQLqdRIRIIHLDITSegccthlLPW-- 232
Cdd:COG2226   17 ALGLRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAED-------LPFpd 85

                         90       100
                 ....*....|....*....|....*.
gi 564365382 233 GPMDLVVSNPPYIFRKDMEQLAPEIR 258
Cdd:COG2226   86 GSFDLVISSFVLHHLPDPERALAEIA 111
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 157-216 3.40e-06

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 47.10  E-value: 3.40e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564365382 157 RAQDGPLILEVGCGSGAIAL--SLLSQlPKTQVIAVDKEEAAVSLTLENAQRLQLQDRIRII 216
Cdd:PRK00377  37 RLRKGDMILDIGCGTGSVTVeaSLLVG-ETGKVYAVDKDEKAINLTRRNAEKFGVLNNIVLI 97
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 165-241 6.76e-06

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 44.28  E-value: 6.76e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564365382  165 LEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLE--NAQRLQLQDRIRIIHLDITSegccthlLPWGPMDLVVSN 241
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARErlAALGLLNAVRVELFQLDLGE-------LDPGSFDVVVAS 72
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
164-216 1.76e-05

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


Pssm-ID: 181354  Cd Length: 187  Bit Score: 44.61  E-value: 1.76e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564365382 164 ILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLQDrIRII 216
Cdd:PRK08287  35 LIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKENRQRFGCGN-IDII 86
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 157-257 2.31e-05

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


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 44.27  E-value: 2.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382  157 RAQDGPLILEVGCGSGAIAL-----------SLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLQDRIRIIHLDITSegc 225
Cdd:pfam01170  25 GWKPGDPLLDPMCGSGTILIeaalmganiapGKFDARVRAPLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAAD--- 101

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 564365382  226 cthlLPW--GPMDLVVSNPPYIFR----KDMEQLAPEI 257
Cdd:pfam01170 102 ----LPLleGSVDVIVTNPPYGIRlgskGALEALYPEF 135
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
155-240 2.53e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 45.03  E-value: 2.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 155 AVRAQDGP--LILEVGCGSGAIALsLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLQDRIRIIHLDItsegccTHLLPW 232
Cdd:COG4076   28 AIERVVKPgdVVLDIGTGSGLLSM-LAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADA------TDLDLP 100


                 ....*...
gi 564365382 233 GPMDLVVS 240
Cdd:COG4076  101 EKADVIIS 108
rADc smart00650
Ribosomal RNA adenine dimethylases;
155-252 2.59e-05

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 44.04  E-value: 2.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382   155 AVRAQDGPLILEVGCGSGAIALSLLSQLPKtqVIAVDKEEAAVSLTlenAQRLQLQDRIRIIHLDItsegCCTHLLPWGP 234
Cdd:smart00650   8 AANLRPGDTVLEIGPGKGALTEELLERAKR--VTAIEIDPRLAPRL---REKFAAADNLTVIHGDA----LKFDLPKLQP 78

                           90       100
                   ....*....|....*....|...
gi 564365382   235 mDLVVSNPPY-----IFRKDMEQ 252
Cdd:smart00650  79 -YKVVGNLPYnistpILFKLLEE 100
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 157-241 2.83e-05

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: 43.08  E-value: 2.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 157 RAQDGPLILEVGCGSGAIALSLLSQlpKTQVIAVDKEEAAvsltLENAQRLQLQDRIRIIHLDITsegccTHLLPWGPMD 236
Cdd:COG2227   21 LLPAGGRVLDVGCGTGRLALALARR--GADVTGVDISPEA----LEIARERAAELNVDFVQGDLE-----DLPLEDGSFD 89


                 ....*
gi 564365382 237 LVVSN 241
Cdd:COG2227   90 LVICS 94
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 175-244 3.34e-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: 45.09  E-value: 3.34e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 175 ALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLQDRIRIIHLDITsegcctHLLPWGPMDLVVSNPPY 244
Cdd:COG0116  241 AEARIKRDPPLPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFR------DLEPPAEPGLIITNPPY 304
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
164-260 1.62e-04

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


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 43.01  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 164 ILEVGCGSGAIALSLLSQLP-KTQVIAVDKEEAAVSLTLENAQRLQLQdrIRIIHLDITsegcctHLLPWGPMDLVVSNP 242
Cdd:COG0827  119 ILDPAVGTGNLLTTVLNQLKkKVNAYGVEVDDLLIRLAAVLANLQGHP--VELFHQDAL------QPLLIDPVDVVISDL 190

                         90       100
                 ....*....|....*....|....
gi 564365382 243 PYIF------RKDMEQLAPEIRSY 260
Cdd:COG0827  191 PVGYypnderAKRFKLKADEGHSY 214
TrmB COG0220
tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 ...
 158-220 1.69e-04

tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 N7-methylase TrmB is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439990  Cd Length: 204  Bit Score: 42.05  E-value: 1.69e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564365382 158 AQDGPLILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLqDRIRIIHLDI 220
Cdd:COG0220   30 GNDAPLVLEIGFGKGEFLVELAAANPDINFIGIEVHEPGVAKALKKAEEEGL-TNVRLLRGDA 91
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 155-243 3.77e-04

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: 42.09  E-value: 3.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 155 AVRAQDGPLILEVGCGSGAIALSLLSQlpKTQVIAVDKEEAAVSLTLENAQRLQLqDRIRIIHLDitSEGCCTHLLPWGP 234
Cdd:COG2265  228 WLDLTGGERVLDLYCGVGTFALPLARR--AKKVIGVEIVPEAVEDARENARLNGL-KNVEFVAGD--LEEVLPELLWGGR 302


                 ....*....
gi 564365382 235 MDLVVSNPP 243
Cdd:COG2265  303 PDVVVLDPP 311
Methyltransf_4 pfam02390
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ...
 160-221 4.82e-04

Putative methyltransferase; This is a family of putative methyltransferases. The aligned region contains the GXGXG S-AdoMet binding site suggesting a putative methyltransferase activity.


Pssm-ID: 367068  Cd Length: 173  Bit Score: 40.35  E-value: 4.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564365382  160 DGPLILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLQDrIRIIHLDIT 221
Cdd:pfam02390   1 DAPVFLEIGCGMGGFLVAMAKANPDKNFIGIEIRVPGVAKALKKIDALGLQN-LRILCGNAL 61
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 159-241 4.88e-04

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: 41.48  E-value: 4.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382  159 QDGPLILEVGCGSG--AIALSLLSQLPktqVIAVDKEEAAVSLTLENAQRLQLQDRiriIHLDITSEgccthlLPWGPMD 236
Cdd:pfam06325 160 KPGESVLDVGCGSGilAIAALKLGAKK---VVGVDIDPVAVRAAKENAELNGVEAR---LEVYLPGD------LPKEKAD 227


                  ....*
gi 564365382  237 LVVSN 241
Cdd:pfam06325 228 VVVAN 232
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 165-241 5.74e-04

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 38.41  E-value: 5.74e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564365382  165 LEVGCGSGAIALSLLSQLPktQVIAVDKEEAAvsltLENAQRLQLQDRIRIIHLDITSegccthlLPW--GPMDLVVSN 241
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEM----LELAREKAPREGLTFVVGDAED-------LPFpdNSFDLVLSS 66
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
164-215 6.33e-04

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 40.91  E-value: 6.33e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564365382 164 ILEVGCGSG--AIALSLLSqlpKTQVIAVDKEEAAVSLTLENAQRLQLQDRIRI 215
Cdd:PRK00517 123 VLDVGCGSGilAIAAAKLG---AKKVLAVDIDPQAVEAARENAELNGVELNVYL 173
trmB PRK00121
tRNA (guanine-N(7)-)-methyltransferase; Reviewed
 159-221 3.34e-03

tRNA (guanine-N(7)-)-methyltransferase; Reviewed


Pssm-ID: 234649  Cd Length: 202  Bit Score: 38.22  E-value: 3.34e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564365382 159 QDGPLILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLqDRIRIIHLDIT 221
Cdd:PRK00121  39 NDAPIHLEIGFGKGEFLVEMAKANPDINFIGIEVHEPGVGKALKKIEEEGL-TNLRLLCGDAV 100
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 157-257 4.19e-03

ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an S-adenosyl-L-methionine-dependent methyltransferase required for the modification of ribosomal protein L11. This protein is found in bacteria and (with a probable transit peptide) in Arabidopsis. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273061  Cd Length: 288  Bit Score: 38.28  E-value: 4.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382  157 RAQDGPLILEVGCGSGAIALSLLsQLPKTQVIAVDKEEAAVSLTLENAQRLQLQDRIRII--HLDITSEgccthllpwGP 234
Cdd:TIGR00406 156 LDLKDKNVIDVGCGSGILSIAAL-KLGAAKVVGIDIDPLAVESARKNAELNQVSDRLQVKliYLEQPIE---------GK 225

                          90       100
                  ....*....|....*....|...
gi 564365382  235 MDLVVSNppyIFRKDMEQLAPEI 257
Cdd:TIGR00406 226 ADVIVAN---ILAEVIKELYPQF 245
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 181-244 5.18e-03

bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2))-methyltransferase RlmL;


Pssm-ID: 236981 [Multi-domain]  Cd Length: 702  Bit Score: 38.63  E-value: 5.18e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564365382 181 QLPKTQVIAVDKEEAAVSLTLENAQRLQLQDRIRIIHLDITSegcCTHLLPWGPMDLVVSNPPY 244
Cdd:PRK11783 253 AELPSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVAD---LKNPLPKGPTGLVISNPPY 313
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
164-244 5.20e-03

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


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 38.38  E-value: 5.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 164 ILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAvsltLENAQRLQLQDRI--RIIHLDITSEgccthllPWGPMDLVVSN 241
Cdd:PRK09489 200 VLDVGCGAGVLSAVLARHSPKIRLTLSDVSAAA----LESSRATLAANGLegEVFASNVFSD-------IKGRFDMIISN 268


                 ...
gi 564365382 242 PPY 244
Cdd:PRK09489 269 PPF 271
PRK15001 PRK15001
23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;
164-205 5.44e-03

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


Pssm-ID: 184963 [Multi-domain]  Cd Length: 378  Bit Score: 38.47  E-value: 5.44e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 564365382 164 ILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQ 205
Cdd:PRK15001 232 IVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVE 273
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
164-244 5.83e-03

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 37.96  E-value: 5.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 164 ILEVGCGSGAIALSLLSQLPKTQVIAVDKeeaavslTLEN--AQRLQLQDRIRIIHLDITSegccthlLPWGPMDLVVSN 241
Cdd:PRK14896  33 VLEIGPGKGALTDELAKRAKKVYAIELDP-------RLAEflRDDEIAAGNVEIIEGDALK-------VDLPEFNKVVSN 98


                 ...
gi 564365382 242 PPY 244
Cdd:PRK14896  99 LPY 101
PRK07402 PRK07402
precorrin-6Y C5,15-methyltransferase subunit CbiT;
155-211 8.62e-03

precorrin-6Y C5,15-methyltransferase subunit CbiT;


Pssm-ID: 180961  Cd Length: 196  Bit Score: 36.90  E-value: 8.62e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564365382 155 AVRAQDGPLILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLQD 211
Cdd:PRK07402  35 QLRLEPDSVLWDIGAGTGTIPVEAGLLCPKGRVIAIERDEEVVNLIRRNCDRFGVKN 91
PTZ00338 PTZ00338
dimethyladenosine transferase-like protein; Provisional
 155-244 8.67e-03

dimethyladenosine transferase-like protein; Provisional


Pssm-ID: 240367 [Multi-domain]  Cd Length: 294  Bit Score: 37.29  E-value: 8.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365382 155 AVRAQDgpLILEVGCGSGAIALSLLsQLPKtQVIAVDKEEAAVSLTLENAQRLQLQDRIRIIHLDitsegCCTHLLPwgP 234
Cdd:PTZ00338  33 AIKPTD--TVLEIGPGTGNLTEKLL-QLAK-KVIAIEIDPRMVAELKKRFQNSPLASKLEVIEGD-----ALKTEFP--Y 101

                         90
                 ....*....|
gi 564365382 235 MDLVVSNPPY 244
Cdd:PTZ00338 102 FDVCVANVPY 111
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 169-244 8.94e-03

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


Pssm-ID: 442010 [Multi-domain]  Cd Length: 333  Bit Score: 37.53  E-value: 8.94e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564365382 169 CGSGAIALSLLSQLPKTqVIAVDKEEAAVSLTLENAQRLQLQDRIRIIHLDitsegcCTHLLPW--GPMDLVVSNPPY 244
Cdd:COG2520  189 AGVGPFSIPIAKRSGAK-VVAIDINPDAVEYLKENIRLNKVEDRVTPILGD------AREVAPEleGKADRIIMNLPH 259
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH