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Conserved domains on  [gi|1907200076|ref|XP_036011144|]
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MTRF1L release factor glutamine methyltransferase isoform X3 [Mus musculus]

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 ...
 1-230 2.88e-62

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


:

Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 195.75  E-value: 2.88e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076   1 MPVQYILGEWDFQGLSLKMVPPVFIPRPETEELVewvleevAQRPHAVRAQDGPLILEVGCGSGAITLSLLSQLPKSRVV 80
Cdd:COG2890    68 EPLAYILGEAEFYGLEFKVDPGVLIPRPETEELV-------ELALALLPAGAPPRVLDLGTGSGAIALALAKERPDARVT 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  81 AVDKEEAAVSLTHENAQRLQLQDRIRIIHLDITSEgccthLLPWSPLDLVVSNPPYIFRKDMEQLAPEICSYEDLVALDG 160
Cdd:COG2890   141 AVDISPDALAVARRNAERLGLEDRVRFLQGDLFEP-----LPGDGRFDLIVSNPPYIPEDEIALLPPEVRDHEPRLALDG 215

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076 161 GDEGMDIITHILTLAPQLLNASGSIFLEVDPRHPELVSSWLQSHPdlhLSLVGVREDFCGRPRFLHVQKS 230
Cdd:COG2890   216 GEDGLDFYRRIIAQAPRLLKPGGWLLLEIGEDQGEAVRALLEAAG---FADVETHKDLAGRDRVVVARRP 282
 
Name Accession Description Interval E-value
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 1-230 2.88e-62

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 195.75  E-value: 2.88e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076   1 MPVQYILGEWDFQGLSLKMVPPVFIPRPETEELVewvleevAQRPHAVRAQDGPLILEVGCGSGAITLSLLSQLPKSRVV 80
Cdd:COG2890    68 EPLAYILGEAEFYGLEFKVDPGVLIPRPETEELV-------ELALALLPAGAPPRVLDLGTGSGAIALALAKERPDARVT 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  81 AVDKEEAAVSLTHENAQRLQLQDRIRIIHLDITSEgccthLLPWSPLDLVVSNPPYIFRKDMEQLAPEICSYEDLVALDG 160
Cdd:COG2890   141 AVDISPDALAVARRNAERLGLEDRVRFLQGDLFEP-----LPGDGRFDLIVSNPPYIPEDEIALLPPEVRDHEPRLALDG 215

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076 161 GDEGMDIITHILTLAPQLLNASGSIFLEVDPRHPELVSSWLQSHPdlhLSLVGVREDFCGRPRFLHVQKS 230
Cdd:COG2890   216 GEDGLDFYRRIIAQAPRLLKPGGWLLLEIGEDQGEAVRALLEAAG---FADVETHKDLAGRDRVVVARRP 282
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 1-225 4.18e-60

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: 189.22  E-value: 4.18e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076   1 MPVQYILGEWDFQGLSLKMVPPVFIPRPETEelvewvleevaqrpHAV-----RAQDGPLILEVGCGSGAITLSLLSQLP 75
Cdd:TIGR03534  44 EPVAYILGEREFYGLDFKVSPGVLIPRPETE--------------ELVeaaleRLKKGPRVLDLGTGSGAIALALAKERP 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  76 KSRVVAVDKEEAAVSLTHENAQRLQLqDRIRIIHLDITSEgccthlLPWSPLDLVVSNPPYIFRKDMEQLAPEICSYEDL 155
Cdd:TIGR03534 110 DARVTAVDISPEALAVARKNARRLGL-ENVEFLQGDWFEP------LPSGKFDLIVSNPPYIPEADIHLLDPEVRDFEPR 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076 156 VALDGGDEGMDIITHILTLAPQLLNASGSIFLEVDPRHPELVSSWLQSHPdlhLSLVGVREDFCGRPRFL 225
Cdd:TIGR03534 183 LALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFEAAG---FADVETRKDLAGKDRVV 249
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 1-229 1.28e-56

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 181.13  E-value: 1.28e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076   1 MPVQYILGEWDFQGLSLKMVPPVFIPRPETEELVEWVLEEVAQRPHAVraqdgplILEVGCGSGAITLSLLSQLPKSRVV 80
Cdd:PRK09328   64 EPLQYILGEAEFWGLDFKVSPGVLIPRPETEELVEWALEALLLKEPLR-------VLDLGTGSGAIALALAKERPDAEVT 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  81 AVDKEEAAVSLTHENAQRLqLQDRIRIIHLDITSEgccthlLPWSPLDLVVSNPPYIFRKDMEQLAPEICSYEDLVALDG 160
Cdd:PRK09328  137 AVDISPEALAVARRNAKHG-LGARVEFLQGDWFEP------LPGGRFDLIVSNPPYIPEADIHLLQPEVRDHEPHLALFG 209

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200076 161 GDEGMDIITHILTLAPQLLNASGSIFLEVDPRHPELVSSWLQSHpdlHLSLVGVREDFCGRPRFLHVQK 229
Cdd:PRK09328  210 GEDGLDFYRRIIEQAPRYLKPGGWLLLEIGYDQGEAVRALLAAA---GFADVETRKDLAGRDRVVLGRR 275
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 56-187 1.75e-13

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: 66.07  E-value: 1.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  56 ILEVGCGSGAITLSLLSQLPKSRVVAVDKEEAAVSLTHENAQRLQLqDRIRIIHLDITSEgccthlLPWSPLDLVVSNPP 135
Cdd:pfam05175  35 VLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGL-ENGEVVASDVYSG------VEDGKFDLIISNPP 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907200076 136 yiFRkdmeqlapeicsyedlvalDGGDEGMDIITHILTLAPQLLNASGSIFL 187
Cdd:pfam05175 108 --FH-------------------AGLATTYNVAQRFIADAKRHLRPGGELWI 138
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 56-141 1.11e-08

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: 51.28  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  56 ILEVGCGSGAITLSLLSQLPKsRVVAVDKEEAAVSLTHENAQRLqLQDRIRIIHLDITSEgcctHLLPWSPLDLVVSNPP 135
Cdd:cd02440     2 VLDLGCGTGALALALASGPGA-RVTGVDISPVALELARKAAAAL-LADNVEVLKGDAEEL----PPEADESFDVIISDPP 75


                  ....*.
gi 1907200076 136 YIFRKD 141
Cdd:cd02440    76 LHHLVE 81
rADc smart00650
Ribosomal RNA adenine dimethylases;
47-144 1.10e-07

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 49.82  E-value: 1.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076   47 AVRAQDGPLILEVGCGSGAITLSLLSQLpkSRVVAVDKEEAAVSLTHEnaqRLQLQDRIRIIHLDItsegcCTHLLPWSP 126
Cdd:smart00650   8 AANLRPGDTVLEIGPGKGALTEELLERA--KRVTAIEIDPRLAPRLRE---KFAAADNLTVIHGDA-----LKFDLPKLQ 77

                           90       100
                   ....*....|....*....|...
gi 1907200076  127 LDLVVSNPPY-----IFRKDMEQ 144
Cdd:smart00650  78 PYKVVGNLPYnistpILFKLLEE 100
 
Name Accession Description Interval E-value
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 1-230 2.88e-62

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 195.75  E-value: 2.88e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076   1 MPVQYILGEWDFQGLSLKMVPPVFIPRPETEELVewvleevAQRPHAVRAQDGPLILEVGCGSGAITLSLLSQLPKSRVV 80
Cdd:COG2890    68 EPLAYILGEAEFYGLEFKVDPGVLIPRPETEELV-------ELALALLPAGAPPRVLDLGTGSGAIALALAKERPDARVT 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  81 AVDKEEAAVSLTHENAQRLQLQDRIRIIHLDITSEgccthLLPWSPLDLVVSNPPYIFRKDMEQLAPEICSYEDLVALDG 160
Cdd:COG2890   141 AVDISPDALAVARRNAERLGLEDRVRFLQGDLFEP-----LPGDGRFDLIVSNPPYIPEDEIALLPPEVRDHEPRLALDG 215

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076 161 GDEGMDIITHILTLAPQLLNASGSIFLEVDPRHPELVSSWLQSHPdlhLSLVGVREDFCGRPRFLHVQKS 230
Cdd:COG2890   216 GEDGLDFYRRIIAQAPRLLKPGGWLLLEIGEDQGEAVRALLEAAG---FADVETHKDLAGRDRVVVARRP 282
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 1-225 4.18e-60

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: 189.22  E-value: 4.18e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076   1 MPVQYILGEWDFQGLSLKMVPPVFIPRPETEelvewvleevaqrpHAV-----RAQDGPLILEVGCGSGAITLSLLSQLP 75
Cdd:TIGR03534  44 EPVAYILGEREFYGLDFKVSPGVLIPRPETE--------------ELVeaaleRLKKGPRVLDLGTGSGAIALALAKERP 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  76 KSRVVAVDKEEAAVSLTHENAQRLQLqDRIRIIHLDITSEgccthlLPWSPLDLVVSNPPYIFRKDMEQLAPEICSYEDL 155
Cdd:TIGR03534 110 DARVTAVDISPEALAVARKNARRLGL-ENVEFLQGDWFEP------LPSGKFDLIVSNPPYIPEADIHLLDPEVRDFEPR 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076 156 VALDGGDEGMDIITHILTLAPQLLNASGSIFLEVDPRHPELVSSWLQSHPdlhLSLVGVREDFCGRPRFL 225
Cdd:TIGR03534 183 LALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFEAAG---FADVETRKDLAGKDRVV 249
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 1-229 1.28e-56

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 181.13  E-value: 1.28e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076   1 MPVQYILGEWDFQGLSLKMVPPVFIPRPETEELVEWVLEEVAQRPHAVraqdgplILEVGCGSGAITLSLLSQLPKSRVV 80
Cdd:PRK09328   64 EPLQYILGEAEFWGLDFKVSPGVLIPRPETEELVEWALEALLLKEPLR-------VLDLGTGSGAIALALAKERPDAEVT 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  81 AVDKEEAAVSLTHENAQRLqLQDRIRIIHLDITSEgccthlLPWSPLDLVVSNPPYIFRKDMEQLAPEICSYEDLVALDG 160
Cdd:PRK09328  137 AVDISPEALAVARRNAKHG-LGARVEFLQGDWFEP------LPGGRFDLIVSNPPYIPEADIHLLQPEVRDHEPHLALFG 209

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200076 161 GDEGMDIITHILTLAPQLLNASGSIFLEVDPRHPELVSSWLQSHpdlHLSLVGVREDFCGRPRFLHVQK 229
Cdd:PRK09328  210 GEDGLDFYRRIIEQAPRYLKPGGWLLLEIGYDQGEAVRALLAAA---GFADVETRKDLAGRDRVVLGRR 275
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 2-189 1.18e-41

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


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 142.88  E-value: 1.18e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076   2 PVQYILGEWDFQGLSLKMVPPVFIPRPETEELVEWVLEEVAQRPHAVRaqdgplILEVGCGSGAITLSLLSQLPKSRVVA 81
Cdd:TIGR00536  70 PVAYLLGSKEFYGLEFFVNEHVLIPRPETEELVEKALASLISQPPILH------ILDLGTGSGCIALALAYEFPNAEVIA 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  82 VDKEEAAVSLTHENAQRLQLQDRIRIIHLDITSEgccthlLPWSPLDLVVSNPPYIFRKDMEQLaPEICSYEDLVALDGG 161
Cdd:TIGR00536 144 VDISPDALAVAEENAEKNQLEHRVEFIQSNLFEP------LAGQKIDIIVSNPPYIDEEDLADL-PNVVRFEPLLALVGG 216

                         170       180
                  ....*....|....*....|....*...
gi 1907200076 162 DEGMDIITHILTLAPQLLNASGSIFLEV 189
Cdd:TIGR00536 217 DDGLNILRQIIELAPDYLKPNGFLVCEI 244
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
 2-204 3.04e-21

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


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 91.47  E-value: 3.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076   2 PVQYILGEWDFQGLSLKMVPPVFIPRPET--------EELVEWVLEEVAQRPHAVrAQDGPL----------ILEVGCGS 63
Cdd:PRK01544   71 PIAYITGVKEFYSREFIVNKHVLIPRSDTevlvdvvfQCHSRESGNPEKKQLNPC-FRGNDIssncndkflnILELGTGS 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  64 GAITLSLLSQLPKSRVVAVDKEEAAVSLTHENAQRLQLQDRIRIIHLDITSEgccthlLPWSPLDLVVSNPPYIFRKDME 143
Cdd:PRK01544  150 GCIAISLLCELPNANVIATDISLDAIEVAKSNAIKYEVTDRIQIIHSNWFEN------IEKQKFDFIVSNPPYISHSEKS 223

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907200076 144 QLAPEICSYEDLVALDGGDEGMDIITHILTLAPQLLNASGSIFLEVDPRHPELVSSWLQSH 204
Cdd:PRK01544  224 EMAIETINYEPSIALFAEEDGLQAYFIIAENAKQFLKPNGKIILEIGFKQEEAVTQIFLDH 284
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 46-157 3.82e-20

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: 85.58  E-value: 3.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  46 HAVRAQDGPLILEVGCGSGAITLSLLSQLPKSRVVAVDKEEAAVSLTHENAQRLQLQDRIRIIHLDITSegcCTHLLPWS 125
Cdd:COG4123    31 AFAPVKKGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKE---FAAELPPG 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907200076 126 PLDLVVSNPPYiFRKDMEQLAP----------EICSYEDLVA 157
Cdd:COG4123   108 SFDLVVSNPPY-FKAGSGRKSPdearaiarheDALTLEDLIR 148
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 56-187 4.33e-18

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: 78.69  E-value: 4.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  56 ILEVGCGSGAITLSLLSQLPKSRVVAVDKEEAAVSLTHENAQRLQLQDrIRIIHLDITSEgccthlLPWSPLDLVVSNPP 135
Cdd:COG2813    53 VLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAANGLEN-VEVLWSDGLSG------VPDGSFDLILSNPP 125

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907200076 136 yiFRkdmeqlapeicsyedlvalDGGDEGMDIITHILTLAPQLLNASGSIFL 187
Cdd:COG2813   126 --FH-------------------AGRAVDKEVAHALIADAARHLRPGGELWL 156
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 56-187 1.75e-13

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: 66.07  E-value: 1.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  56 ILEVGCGSGAITLSLLSQLPKSRVVAVDKEEAAVSLTHENAQRLQLqDRIRIIHLDITSEgccthlLPWSPLDLVVSNPP 135
Cdd:pfam05175  35 VLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGL-ENGEVVASDVYSG------VEDGKFDLIISNPP 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907200076 136 yiFRkdmeqlapeicsyedlvalDGGDEGMDIITHILTLAPQLLNASGSIFL 187
Cdd:pfam05175 108 --FH-------------------AGLATTYNVAQRFIADAKRHLRPGGELWI 138
PRK14966 PRK14966
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; ...
 2-188 2.26e-13

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


Pssm-ID: 184930 [Multi-domain]  Cd Length: 423  Bit Score: 68.57  E-value: 2.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076   2 PVQYILGEWDFQGLSLKMVPPVFIPRPETeelVEWVLEEVAQRPHAVRAQDgplileVGCGSGAITLSLLSQLPKSRVVA 81
Cdd:PRK14966  210 PVAYILGVREFYGRRFAVNPNVLIPRPET---EHLVEAVLARLPENGRVWD------LGTGSGAVAVTVALERPDAFVRA 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  82 VDKEEAAVSLTHENAQrlQLQDRIRIIH-----LDITSEGccthllPWsplDLVVSNPPYIFRKDmEQLAPEICSYEDLV 156
Cdd:PRK14966  281 SDISPPALETARKNAA--DLGARVEFAHgswfdTDMPSEG------KW---DIIVSNPPYIENGD-KHLLQGDLRFEPQI 348

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1907200076 157 ALDGGDEGMDIITHILTLAPQLLNASGSIFLE 188
Cdd:PRK14966  349 ALTDFSDGLSCIRTLAQGAPDRLAEGGFLLLE 380
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 49-108 1.33e-11

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: 59.65  E-value: 1.33e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  49 RAQDGPLILEVGCGSGAITLSLLSQLPKSRVVAVDKEEAAVSLTHENAQRLQLqDRIRII 108
Cdd:TIGR02469  16 RLRPGDVLWDIGAGTGSVTIEAARLVPNGRVYAIERNPEALDLIERNLRRFGV-SNIVIV 74
PRK14968 PRK14968
putative methyltransferase; Provisional
 47-199 8.90e-11

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 59.14  E-value: 8.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  47 AVRAQDGPLILEVGCGSGAITLSLLSQlpKSRVVAVDKEEAAVSLTHENAQRLQLQDR-IRIIHLDITSegCCTHllpwS 125
Cdd:PRK14968   18 NAVDKKGDRVLEVGTGSGIVAIVAAKN--GKKVVGVDINPYAVECAKCNAKLNNIRNNgVEVIRSDLFE--PFRG----D 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907200076 126 PLDLVVSNPPYIFRKDMEqlapEICSYEDLvALDGGDEGMDIITHILTLAPQLLNASGSIFLevdprhpeLVSS 199
Cdd:PRK14968   90 KFDVILFNPPYLPTEEEE----EWDDWLNY-ALSGGKDGREVIDRFLDEVGRYLKPGGRILL--------LQSS 150
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
56-133 1.37e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 56.37  E-value: 1.37e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907200076  56 ILEVGCGSGAITLSLLSQLPKSRVVAVDKEEAAVslthENAQrlQLQDRIRIIHLDItsegccTHLLPWSPLDLVVSN 133
Cdd:COG4106     5 VLDLGCGTGRLTALLAERFPGARVTGVDLSPEML----ARAR--ARLPNVRFVVADL------RDLDPPEPFDLVVSN 70
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 56-149 3.79e-09

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 52.18  E-value: 3.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  56 ILEVGCGSGAITLsLLSQLPKSRVVAVDKEEAAVSLTHENAQRLQLqdRIRIIHLDItsegccTHL-LPWSPLDLVVSNP 134
Cdd:pfam13649   1 VLDLGCGTGRLTL-ALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDA------EDLpFPDGSFDLVVSSG 71

                          90
                  ....*....|....*..
gi 1907200076 135 P--YIFRKDMEQLAPEI 149
Cdd:pfam13649  72 VlhHLPDPDLEAALREI 88
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 48-109 5.02e-09

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


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 55.56  E-value: 5.02e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  48 VRA--------QDGPLILEVGCGSGAITLSLLSQLPKSRVVAVDKEEAAVSLTHENAQRLQLqDRIRIIH 109
Cdd:COG2242   235 VRAltlaklalRPGDVLWDIGAGSGSVSIEAARLAPGGRVYAIERDPERAALIRANARRFGV-PNVEVVE 303
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 56-141 1.11e-08

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: 51.28  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  56 ILEVGCGSGAITLSLLSQLPKsRVVAVDKEEAAVSLTHENAQRLqLQDRIRIIHLDITSEgcctHLLPWSPLDLVVSNPP 135
Cdd:cd02440     2 VLDLGCGTGALALALASGPGA-RVTGVDISPVALELARKAAAAL-LADNVEVLKGDAEEL----PPEADESFDVIISDPP 75


                  ....*.
gi 1907200076 136 YIFRKD 141
Cdd:cd02440    76 LHHLVE 81
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 49-108 1.96e-08

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 52.49  E-value: 1.96e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907200076  49 RAQDGPLILEVGCGSGAITL--SLLSQlPKSRVVAVDKEEAAVSLTHENAQRLQLQDRIRII 108
Cdd:PRK00377   37 RLRKGDMILDIGCGTGSVTVeaSLLVG-ETGKVYAVDKDEKAINLTRRNAEKFGVLNNIVLI 97
PRK14967 PRK14967
putative methyltransferase; Provisional
 53-187 2.83e-08

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 52.36  E-value: 2.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  53 GPLILEVGCGSGAITLSLlSQLPKSRVVAVDKEEAAVSLTHENAqrLQLQDRIRIIHLDITSEgccthlLPWSPLDLVVS 132
Cdd:PRK14967   37 GRRVLDLCTGSGALAVAA-AAAGAGSVTAVDISRRAVRSARLNA--LLAGVDVDVRRGDWARA------VEFRPFDVVVS 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907200076 133 NPPYIFRKDMEqlAPeicSYEDLVALDGGDEGMDIITHILTLAPQLLNASGSIFL 187
Cdd:PRK14967  108 NPPYVPAPPDA--PP---SRGPARAWDAGPDGRAVLDRLCDAAPALLAPGGSLLL 157
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
56-152 6.46e-08

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 51.71  E-value: 6.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  56 ILEVGCGSG--AItLSLLsqLPKSRVVAVDKEEAAVSLTHENAQRLQLQDRIRIIHLDITSEGccthllpwsPLDLVVSN 133
Cdd:COG2264   152 VLDVGCGSGilAI-AAAK--LGAKRVLAVDIDPVAVEAARENAELNGVEDRIEVVLGDLLEDG---------PYDLVVAN 219

                          90
                  ....*....|....*....
gi 1907200076 134 ppyIFRKDMEQLAPEICSY 152
Cdd:COG2264   220 ---ILANPLIELAPDLAAL 235
rADc smart00650
Ribosomal RNA adenine dimethylases;
47-144 1.10e-07

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 49.82  E-value: 1.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076   47 AVRAQDGPLILEVGCGSGAITLSLLSQLpkSRVVAVDKEEAAVSLTHEnaqRLQLQDRIRIIHLDItsegcCTHLLPWSP 126
Cdd:smart00650   8 AANLRPGDTVLEIGPGKGALTEELLERA--KRVTAIEIDPRLAPRLRE---KFAAADNLTVIHGDA-----LKFDLPKLQ 77

                           90       100
                   ....*....|....*....|...
gi 1907200076  127 LDLVVSNPPY-----IFRKDMEQ 144
Cdd:smart00650  78 PYKVVGNLPYnistpILFKLLEE 100
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 56-133 1.44e-07

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 49.34  E-value: 1.44e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200076  56 ILEVGCGSGAITLSLLSQL-PKSRVVAVDKEEAAVSLTHENAQRLQLqDRIRIIHLDITSEGCcthLLPWSPLDLVVSN 133
Cdd:pfam13847   7 VLDLGCGTGHLSFELAEELgPNAEVVGIDISEEAIEKARENAQKLGF-DNVEFEQGDIEELPE---LLEDDKFDVVISN 81
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
52-135 1.57e-07

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 49.90  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  52 DGPLILEVGCGSGaiTLSLLSQLP-KSRVVAVDKEEAAVSLTHENAQRLQlqDRIRIIHLDITsegcctHLLPWSPLDLV 130
Cdd:COG2263    45 EGKTVLDLGCGTG--MLAIGAALLgAKKVVGVDIDPEALEIARENAERLG--VRVDFIRADVT------RIPLGGSVDTV 114


                  ....*
gi 1907200076 131 VSNPP 135
Cdd:COG2263   115 VMNPP 119
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 56-131 6.11e-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: 48.62  E-value: 6.11e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907200076  56 ILEVGCGSGAITLSLLSQL-PKSRVVAVDKEEAAVSLTHENAQRLQLQDRIRIIHLDItSEGccthlLPWSPLDLVV 131
Cdd:COG2519    95 VLEAGTGSGALTLALARAVgPEGKVYSYERREDFAEIARKNLERFGLPDNVELKLGDI-REG-----IDEGDVDAVF 165
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 49-133 7.79e-07

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 47.99  E-value: 7.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  49 RAQDGPLILEVGCGSGAITLsLLSQLPKSRVVAVDKEEAAVSLTHENAQRLQLqDRIRIIHLDITSegccTHLLPWSPLD 128
Cdd:COG0500    23 RLPKGGRVLDLGCGTGRNLL-ALAARFGGRVIGIDLSPEAIALARARAAKAGL-GNVEFLVADLAE----LDPLPAESFD 96


                  ....*
gi 1907200076 129 LVVSN 133
Cdd:COG0500    97 LVVAF 101
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 47-133 8.05e-07

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


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 46.91  E-value: 8.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  47 AVRAQDGPLILEVGCGSGAITLSLLSQlpKSRVVAVDKEEAAVSLTHENAQRLQLqdRIRIIHLDITSegccthlLPWSP 126
Cdd:COG2226    17 ALGLRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAED-------LPFPD 85


                  ....*....
gi 1907200076 127 --LDLVVSN 133
Cdd:COG2226    86 gsFDLVISS 94
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 47-187 1.62e-06

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


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 46.77  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  47 AVRAQDGPLILEVGCGSGAITLSLLSQLPKsrVVAVDKEEAAVSLTHENAQRLQLQdrIRIIHLDITS--EGccthllpw 124
Cdd:TIGR00537  14 NLRELKPDDVLEIGAGTGLVAIRLKGKGKC--ILTTDINPFAVKELRENAKLNNVG--LDVVMTDLFKgvRG-------- 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907200076 125 sPLDLVVSNPPYIFRKDMEQlapeICSYEDlVALDGGDEGMDIITHILTLAPQLLNASGSIFL 187
Cdd:TIGR00537  82 -KFDVILFNPPYLPLEDDLR----RGDWLD-VAIDGGKDGRKVIDRFLDELPEILKEGGRVQL 138
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 47-132 2.95e-06

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 45.69  E-value: 2.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  47 AVRAQDGPLILEVGCGSGAiTLSLLSQLPKSRVVAVDKEEAAVSLTHENAQRLQLQDRIRIIHLDItsegccTHLLPWSP 126
Cdd:COG2230    46 KLGLKPGMRVLDIGCGWGG-LALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADY------RDLPADGQ 118


                  ....*.
gi 1907200076 127 LDLVVS 132
Cdd:COG2230   119 FDAIVS 124
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 57-133 7.74e-06

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 43.13  E-value: 7.74e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200076  57 LEVGCGSGAITLSLLSQLPKSRVVAVDKEEAAVSL--THENAQRLQLQDRIRIIHLDITSegccthlLPWSPLDLVVSN 133
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAarERLAALGLLNAVRVELFQLDLGE-------LDPGSFDVVVAS 72
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
56-108 8.11e-06

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


Pssm-ID: 181354  Cd Length: 187  Bit Score: 44.99  E-value: 8.11e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907200076  56 ILEVGCGSGAITLSLLSQLPKSRVVAVDKEEAAVSLTHENAQRLQLQDrIRII 108
Cdd:PRK08287   35 LIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKENRQRFGCGN-IDII 86
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
56-136 1.07e-05

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 45.28  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  56 ILEVGCGSGAITLSLLSQLPKSRVVAVDKeeaavSLTHENAQRLQLQDRIRIIHLDITSegccthlLPWSPLDLVVSNPP 135
Cdd:PRK14896   33 VLEIGPGKGALTDELAKRAKKVYAIELDP-----RLAEFLRDDEIAAGNVEIIEGDALK-------VDLPEFNKVVSNLP 100


                  .
gi 1907200076 136 Y 136
Cdd:PRK14896  101 Y 101
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
47-132 2.65e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 43.87  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  47 AVRAQDGP--LILEVGCGSGAitLSLL-SQLPKSRVVAVDKEEAAVSLTHENAQRLQLQDRIRIIHLDItsegccTHLLP 123
Cdd:COG4076    28 AIERVVKPgdVVLDIGTGSGL--LSMLaARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADA------TDLDL 99


                  ....*....
gi 1907200076 124 WSPLDLVVS 132
Cdd:COG4076   100 PEKADVIIS 108
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 49-133 1.23e-04

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: 40.39  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  49 RAQDGPLILEVGCGSGAITLSLLSQlpKSRVVAVDKEEAAVslthENAQRLQLQDRIRIIHLDITSegccthlLPWSP-- 126
Cdd:COG2227    21 LLPAGGRVLDVGCGTGRLALALARR--GADVTGVDISPEAL----EIARERAAELNVDFVQGDLED-------LPLEDgs 87


                  ....*..
gi 1907200076 127 LDLVVSN 133
Cdd:COG2227    88 FDLVICS 94
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 75-136 1.70e-04

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


Pssm-ID: 439886 [Multi-domain]  Cd Length: 369  Bit Score: 42.01  E-value: 1.70e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907200076  75 PKSRVVAVDKEEAAVSLTHENAQRLQLQDRIRIIHLDITsegcctHLLPWSPLDLVVSNPPY 136
Cdd:COG0116   249 PPLPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFR------DLEPPAEPGLIITNPPY 304
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 51-151 2.69e-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: 41.10  E-value: 2.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  51 QDGPLILEVGCGSG--AITLSLLSqlpKSRVVAVDKEEAAVSLTHENAQRLQLQDRiriIHLDITSEgccthlLPWSPLD 128
Cdd:pfam06325 160 KPGESVLDVGCGSGilAIAALKLG---AKKVVGVDIDPVAVRAAKENAELNGVEAR---LEVYLPGD------LPKEKAD 227

                          90       100
                  ....*....|....*....|...
gi 1907200076 129 LVVSNppyIFRKDMEQLAPEICS 151
Cdd:pfam06325 228 VVVAN---ILADPLIELAPDIYA 247
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 47-136 3.40e-04

16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) [Translation, ribosomal structure and biogenesis]; 16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439801 [Multi-domain]  Cd Length: 270  Bit Score: 40.88  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  47 AVRAQDGPLILEVGCGSGAITLSLLSQLPksRVVAVDKEEAAVSLTHEnaqRLQLQDRIRIIHLDITSegccthlLPWSP 126
Cdd:COG0030    32 AAGITPGDTVLEIGPGLGALTRALLERAA--RVTAVEIDRRLAAILRE---TFAAYPNLTVIEGDALK-------VDLPA 99

                          90
                  ....*....|....*
gi 1907200076 127 LDL-----VVSNPPY 136
Cdd:COG0030   100 LAAgeplkVVGNLPY 114
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 47-135 3.48e-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: 40.93  E-value: 3.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  47 AVRAQDGPLILEVGCGSGAITLSLLSQlpKSRVVAVDKEEAAVSLTHENAQRLQLqDRIRIIHLDitSEGCCTHLLPWSP 126
Cdd:COG2265   228 WLDLTGGERVLDLYCGVGTFALPLARR--AKKVIGVEIVPEAVEDARENARLNGL-KNVEFVAGD--LEEVLPELLWGGR 302


                  ....*....
gi 1907200076 127 LDLVVSNPP 135
Cdd:COG2265   303 PDVVVLDPP 311
PTZ00338 PTZ00338
dimethyladenosine transferase-like protein; Provisional
 47-136 3.66e-04

dimethyladenosine transferase-like protein; Provisional


Pssm-ID: 240367 [Multi-domain]  Cd Length: 294  Bit Score: 40.76  E-value: 3.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  47 AVRAQDgpLILEVGCGSGAITLSLlsqLPKSR-VVAVDKEEAAVSLTHENAQRLQLQDRIRIIHLDitsegCCTHLLPws 125
Cdd:PTZ00338   33 AIKPTD--TVLEIGPGTGNLTEKL---LQLAKkVIAIEIDPRMVAELKKRFQNSPLASKLEVIEGD-----ALKTEFP-- 100

                          90
                  ....*....|.
gi 1907200076 126 PLDLVVSNPPY 136
Cdd:PTZ00338  101 YFDVCVANVPY 111
TrmB COG0220
tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 ...
 45-112 4.62e-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: 40.12  E-value: 4.62e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907200076  45 PHAVRAQDGPLILEVGCGSGAITLSLLSQLPKSRVVAVDKEEAAVSLTHENAQRLQLqDRIRIIHLDI 112
Cdd:COG0220    25 WAELFGNDAPLVLEIGFGKGEFLVELAAANPDINFIGIEVHEPGVAKALKKAEEEGL-TNVRLLRGDA 91
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 49-149 4.86e-04

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


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 39.65  E-value: 4.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  49 RAQDGPLILEVGCGSGAITL-----------SLLSQLPKSRVVAVDKEEAAVSLTHENAQRLQLQDRIRIIHLDITSegc 117
Cdd:pfam01170  25 GWKPGDPLLDPMCGSGTILIeaalmganiapGKFDARVRAPLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAAD--- 101

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907200076 118 cthlLPW--SPLDLVVSNPPYIFR----KDMEQLAPEI 149
Cdd:pfam01170 102 ----LPLleGSVDVIVTNPPYGIRlgskGALEALYPEF 135
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 56-133 5.53e-04

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


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 39.96  E-value: 5.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  56 ILEVGCGSGAITLSLLSQLPKSRVVAVD--KEEAAVSLTHENAQRLqlqdrirIIHLDItsegcCTHLLPWSPLDLVVSN 133
Cdd:TIGR02072  38 VLDIGCGTGYLTRALLKRFPQAEFIALDisAGMLAQAKTKLSENVQ-------FICGDA-----EKLPLEDSSFDLIVSN 105
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 73-136 9.81e-04

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: 39.79  E-value: 9.81e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907200076  73 QLPKSRVVAVDKEEAAVSLTHENAQRLQLQDRIRIIHLDITSegcCTHLLPWSPLDLVVSNPPY 136
Cdd:PRK11783  253 AELPSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVAD---LKNPLPKGPTGLVISNPPY 313
PRK15001 PRK15001
23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;
56-97 9.99e-04

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


Pssm-ID: 184963 [Multi-domain]  Cd Length: 378  Bit Score: 39.63  E-value: 9.99e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1907200076  56 ILEVGCGSGAITLSLLSQLPKSRVVAVDKEEAAVSLTHENAQ 97
Cdd:PRK15001  232 IVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVE 273
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 57-133 2.06e-03

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 36.49  E-value: 2.06e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200076  57 LEVGCGSGAITLSLLSQLPksRVVAVDKEEAAVSLTHENAQRLQLQdrirIIHLDITSegccthlLPWSP--LDLVVSN 133
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMLELAREKAPREGLT----FVVGDAED-------LPFPDnsFDLVLSS 66
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
56-152 2.28e-03

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


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 38.39  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  56 ILEVGCGSGAITLSLLSQLP-KSRVVAVDKEEAAVSLTHENAQRLQLQdrIRIIHLDITSegccTHLLPwsPLDLVVSNP 134
Cdd:COG0827   119 ILDPAVGTGNLLTTVLNQLKkKVNAYGVEVDDLLIRLAAVLANLQGHP--VELFHQDALQ----PLLID--PVDVVISDL 190

                          90       100
                  ....*....|....*....|....
gi 1907200076 135 PYIF------RKDMEQLAPEICSY 152
Cdd:COG0827   191 PVGYypnderAKRFKLKADEGHSY 214
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 49-149 4.49e-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: 37.51  E-value: 4.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  49 RAQDGPLILEVGCGSGAITLSLLsQLPKSRVVAVDKEEAAVSLTHENAQRLQLQDRIRII--HLDITSEGccthllpwsP 126
Cdd:TIGR00406 156 LDLKDKNVIDVGCGSGILSIAAL-KLGAAKVVGIDIDPLAVESARKNAELNQVSDRLQVKliYLEQPIEG---------K 225

                          90       100
                  ....*....|....*....|...
gi 1907200076 127 LDLVVSNppyIFRKDMEQLAPEI 149
Cdd:TIGR00406 226 ADVIVAN---ILAEVIKELYPQF 245
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
56-152 4.77e-03

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 37.05  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200076  56 ILEVGCGSG--AITLSLLSQlpkSRVVAVDKEEAAVSLTHENAQRLQLQDRIRIIHLDitsegccthllpwSPLDLVVSN 133
Cdd:PRK00517  123 VLDVGCGSGilAIAAAKLGA---KKVLAVDIDPQAVEAARENAELNGVELNVYLPQGD-------------LKADVIVAN 186

                          90
                  ....*....|....*....
gi 1907200076 134 ppyIFRKDMEQLAPEICSY 152
Cdd:PRK00517  187 ---ILANPLLELAPDLARL 202
PRK10901 PRK10901
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
50-106 7.45e-03

16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;


Pssm-ID: 236790 [Multi-domain]  Cd Length: 427  Bit Score: 37.09  E-value: 7.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907200076  50 AQDGPLILEVGCGSGAITLSLLSQLPKSRVVAVDKEEAAVSLTHENAQRLQLQDRIR 106
Cdd:PRK10901  242 PQNGERVLDACAAPGGKTAHILELAPQAQVVALDIDAQRLERVRENLQRLGLKATVI 298
Methyltransf_4 pfam02390
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ...
 52-113 8.08e-03

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: 36.11  E-value: 8.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907200076  52 DGPLILEVGCGSGAITLSLLSQLPKSRVVAVDKEEAAVSLTHENAQRLQLQDrIRIIHLDIT 113
Cdd:pfam02390   1 DAPVFLEIGCGMGGFLVAMAKANPDKNFIGIEIRVPGVAKALKKIDALGLQN-LRILCGNAL 61
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 61-111 8.18e-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: 36.76  E-value: 8.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907200076  61 CGSGAITLsLLSQLPKSRVVAVDKEEAAVSLTHENAQRLQLQDRIRIIHLD 111
Cdd:COG2520   189 AGVGPFSI-PIAKRSGAKVVAIDINPDAVEYLKENIRLNKVEDRVTPILGD 238
 
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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