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Conserved domains on  [gi|1958795565|ref|XP_038937144|]
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MTRF1L release factor glutamine methyltransferase isoform X2 [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

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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 2.04e-63

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


:

Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 198.84  E-value: 2.04e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565   1 MPVQYILGEWDFQGLNLKMAPPVFIPRPETEELVEWVLEevaqrppAVRAQDGPLILEVGCGSGAIALSLLSQLPKTQVI 80
Cdd:COG2890    68 EPLAYILGEAEFYGLEFKVDPGVLIPRPETEELVELALA-------LLPAGAPPRVLDLGTGSGAIALALAKERPDARVT 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  81 AVDKEEAAVSLTLENAQRLQLQDRIRIIHLDITSEgccthLLPWGPMDLVVSNPPYIFRKDMEQLAPEIRSYEDLVALDG 160
Cdd:COG2890   141 AVDISPDALAVARRNAERLGLEDRVRFLQGDLFEP-----LPGDGRFDLIVSNPPYIPEDEIALLPPEVRDHEPRLALDG 215

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565 161 GDEGMDIITHILTLAPWLLNASGSIFLEVDPRHPELVSSWLQSQPdlhLSLVGVREDFCGRPRFLHVQKS 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 2.04e-63

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 198.84  E-value: 2.04e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565   1 MPVQYILGEWDFQGLNLKMAPPVFIPRPETEELVEWVLEevaqrppAVRAQDGPLILEVGCGSGAIALSLLSQLPKTQVI 80
Cdd:COG2890    68 EPLAYILGEAEFYGLEFKVDPGVLIPRPETEELVELALA-------LLPAGAPPRVLDLGTGSGAIALALAKERPDARVT 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  81 AVDKEEAAVSLTLENAQRLQLQDRIRIIHLDITSEgccthLLPWGPMDLVVSNPPYIFRKDMEQLAPEIRSYEDLVALDG 160
Cdd:COG2890   141 AVDISPDALAVARRNAERLGLEDRVRFLQGDLFEP-----LPGDGRFDLIVSNPPYIPEDEIALLPPEVRDHEPRLALDG 215

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565 161 GDEGMDIITHILTLAPWLLNASGSIFLEVDPRHPELVSSWLQSQPdlhLSLVGVREDFCGRPRFLHVQKS 230
Cdd:COG2890   216 GEDGLDFYRRIIAQAPRLLKPGGWLLLEIGEDQGEAVRALLEAAG---FADVETHKDLAGRDRVVVARRP 282
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 1-225 1.39e-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: 190.37  E-value: 1.39e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565   1 MPVQYILGEWDFQGLNLKMAPPVFIPRPETEELvewvleevaqrppaV-----RAQDGPLILEVGCGSGAIALSLLSQLP 75
Cdd:TIGR03534  44 EPVAYILGEREFYGLDFKVSPGVLIPRPETEEL--------------VeaaleRLKKGPRVLDLGTGSGAIALALAKERP 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  76 KTQVIAVDKEEAAVSLTLENAQRLQLqDRIRIIHLDITSEgccthlLPWGPMDLVVSNPPYIFRKDMEQLAPEIRSYEDL 155
Cdd:TIGR03534 110 DARVTAVDISPEALAVARKNARRLGL-ENVEFLQGDWFEP------LPSGKFDLIVSNPPYIPEADIHLLDPEVRDFEPR 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565 156 VALDGGDEGMDIITHILTLAPWLLNASGSIFLEVDPRHPELVSSWLQSQPdlhLSLVGVREDFCGRPRFL 225
Cdd:TIGR03534 183 LALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFEAAG---FADVETRKDLAGKDRVV 249
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 1-229 6.67e-58

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 184.60  E-value: 6.67e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565   1 MPVQYILGEWDFQGLNLKMAPPVFIPRPETEELVEWVLEEVAQRPPAVraqdgplILEVGCGSGAIALSLLSQLPKTQVI 80
Cdd:PRK09328   64 EPLQYILGEAEFWGLDFKVSPGVLIPRPETEELVEWALEALLLKEPLR-------VLDLGTGSGAIALALAKERPDAEVT 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  81 AVDKEEAAVSLTLENAQRLqLQDRIRIIHLDITSEgccthlLPWGPMDLVVSNPPYIFRKDMEQLAPEIRSYEDLVALDG 160
Cdd:PRK09328  137 AVDISPEALAVARRNAKHG-LGARVEFLQGDWFEP------LPGGRFDLIVSNPPYIPEADIHLLQPEVRDHEPHLALFG 209

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958795565 161 GDEGMDIITHILTLAPWLLNASGSIFLEVDPRHPELVSSWLQSQpdlHLSLVGVREDFCGRPRFLHVQK 229
Cdd:PRK09328  210 GEDGLDFYRRIIEQAPRYLKPGGWLLLEIGYDQGEAVRALLAAA---GFADVETRKDLAGRDRVVLGRR 275
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 56-187 4.35e-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: 64.92  E-value: 4.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  56 ILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLqDRIRIIHLDITSEgccthlLPWGPMDLVVSNPP 135
Cdd:pfam05175  35 VLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGL-ENGEVVASDVYSG------VEDGKFDLIISNPP 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958795565 136 yiFRkdmeqlapeirsyedlvalDGGDEGMDIITHILTLAPWLLNASGSIFL 187
Cdd:pfam05175 108 --FH-------------------AGLATTYNVAQRFIADAKRHLRPGGELWI 138
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 56-150 9.00e-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: 54.36  E-value: 9.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  56 ILEVGCGSGAIALSLLSQlPKTQVIAVDKEEAAVSLTLENAQRLqLQDRIRIIHLDITSEgcctHLLPWGPMDLVVSNPP 135
Cdd:cd02440     2 VLDLGCGTGALALALASG-PGARVTGVDISPVALELARKAAAAL-LADNVEVLKGDAEEL----PPEADESFDVIISDPP 75

                          90
                  ....*....|....*.
gi 1958795565 136 YIFRK-DMEQLAPEIR 150
Cdd:cd02440    76 LHHLVeDLARFLEEAR 91
rADc smart00650
Ribosomal RNA adenine dimethylases;
47-144 3.63e-05

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 42.88  E-value: 3.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565   47 AVRAQDGPLILEVGCGSGAIALSLLSQLPKtqVIAVDKEEAAVSLTlenAQRLQLQDRIRIIHLDItsegCCTHLLPWGP 126
Cdd:smart00650   8 AANLRPGDTVLEIGPGKGALTEELLERAKR--VTAIEIDPRLAPRL---REKFAAADNLTVIHGDA----LKFDLPKLQP 78

                           90       100
                   ....*....|....*....|...
gi 1958795565  127 mDLVVSNPPY-----IFRKDMEQ 144
Cdd:smart00650  79 -YKVVGNLPYnistpILFKLLEE 100
 
Name Accession Description Interval E-value
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 1-230 2.04e-63

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 198.84  E-value: 2.04e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565   1 MPVQYILGEWDFQGLNLKMAPPVFIPRPETEELVEWVLEevaqrppAVRAQDGPLILEVGCGSGAIALSLLSQLPKTQVI 80
Cdd:COG2890    68 EPLAYILGEAEFYGLEFKVDPGVLIPRPETEELVELALA-------LLPAGAPPRVLDLGTGSGAIALALAKERPDARVT 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  81 AVDKEEAAVSLTLENAQRLQLQDRIRIIHLDITSEgccthLLPWGPMDLVVSNPPYIFRKDMEQLAPEIRSYEDLVALDG 160
Cdd:COG2890   141 AVDISPDALAVARRNAERLGLEDRVRFLQGDLFEP-----LPGDGRFDLIVSNPPYIPEDEIALLPPEVRDHEPRLALDG 215

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565 161 GDEGMDIITHILTLAPWLLNASGSIFLEVDPRHPELVSSWLQSQPdlhLSLVGVREDFCGRPRFLHVQKS 230
Cdd:COG2890   216 GEDGLDFYRRIIAQAPRLLKPGGWLLLEIGEDQGEAVRALLEAAG---FADVETHKDLAGRDRVVVARRP 282
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 1-225 1.39e-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: 190.37  E-value: 1.39e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565   1 MPVQYILGEWDFQGLNLKMAPPVFIPRPETEELvewvleevaqrppaV-----RAQDGPLILEVGCGSGAIALSLLSQLP 75
Cdd:TIGR03534  44 EPVAYILGEREFYGLDFKVSPGVLIPRPETEEL--------------VeaaleRLKKGPRVLDLGTGSGAIALALAKERP 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  76 KTQVIAVDKEEAAVSLTLENAQRLQLqDRIRIIHLDITSEgccthlLPWGPMDLVVSNPPYIFRKDMEQLAPEIRSYEDL 155
Cdd:TIGR03534 110 DARVTAVDISPEALAVARKNARRLGL-ENVEFLQGDWFEP------LPSGKFDLIVSNPPYIPEADIHLLDPEVRDFEPR 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565 156 VALDGGDEGMDIITHILTLAPWLLNASGSIFLEVDPRHPELVSSWLQSQPdlhLSLVGVREDFCGRPRFL 225
Cdd:TIGR03534 183 LALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFEAAG---FADVETRKDLAGKDRVV 249
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 1-229 6.67e-58

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 184.60  E-value: 6.67e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565   1 MPVQYILGEWDFQGLNLKMAPPVFIPRPETEELVEWVLEEVAQRPPAVraqdgplILEVGCGSGAIALSLLSQLPKTQVI 80
Cdd:PRK09328   64 EPLQYILGEAEFWGLDFKVSPGVLIPRPETEELVEWALEALLLKEPLR-------VLDLGTGSGAIALALAKERPDAEVT 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  81 AVDKEEAAVSLTLENAQRLqLQDRIRIIHLDITSEgccthlLPWGPMDLVVSNPPYIFRKDMEQLAPEIRSYEDLVALDG 160
Cdd:PRK09328  137 AVDISPEALAVARRNAKHG-LGARVEFLQGDWFEP------LPGGRFDLIVSNPPYIPEADIHLLQPEVRDHEPHLALFG 209

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958795565 161 GDEGMDIITHILTLAPWLLNASGSIFLEVDPRHPELVSSWLQSQpdlHLSLVGVREDFCGRPRFLHVQK 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 3.97e-43

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: 146.73  E-value: 3.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565   2 PVQYILGEWDFQGLNLKMAPPVFIPRPETEELVEWVLEEVAQRPPAVRaqdgplILEVGCGSGAIALSLLSQLPKTQVIA 81
Cdd:TIGR00536  70 PVAYLLGSKEFYGLEFFVNEHVLIPRPETEELVEKALASLISQPPILH------ILDLGTGSGCIALALAYEFPNAEVIA 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  82 VDKEEAAVSLTLENAQRLQLQDRIRIIHLDITSEgccthlLPWGPMDLVVSNPPYIFRKDMEQLAPEIRsYEDLVALDGG 161
Cdd:TIGR00536 144 VDISPDALAVAEENAEKNQLEHRVEFIQSNLFEP------LAGQKIDIIVSNPPYIDEEDLADLPNVVR-FEPLLALVGG 216

                         170       180
                  ....*....|....*....|....*...
gi 1958795565 162 DEGMDIITHILTLAPWLLNASGSIFLEV 189
Cdd:TIGR00536 217 DDGLNILRQIIELAPDYLKPNGFLVCEI 244
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
 2-198 5.17e-21

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


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 90.69  E-value: 5.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565   2 PVQYILGEWDFQGLNLKMAPPVFIPRPET-------EELVEWVLEEVAQRPPAVRAQDGPL----------ILEVGCGSG 64
Cdd:PRK01544   71 PIAYITGVKEFYSREFIVNKHVLIPRSDTevlvdvvFQCHSRESGNPEKKQLNPCFRGNDIssncndkflnILELGTGSG 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  65 AIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLQDRIRIIHLDITSEgccthlLPWGPMDLVVSNPPYIFRKDMEQ 144
Cdd:PRK01544  151 CIAISLLCELPNANVIATDISLDAIEVAKSNAIKYEVTDRIQIIHSNWFEN------IEKQKFDFIVSNPPYISHSEKSE 224

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958795565 145 LAPEIRSYEDLVALDGGDEGMDIITHILTLAPWLLNASGSIFLEVDPRHPELVS 198
Cdd:PRK01544  225 MAIETINYEPSIALFAEEDGLQAYFIIAENAKQFLKPNGKIILEIGFKQEEAVT 278
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 47-136 5.00e-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: 85.20  E-value: 5.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  47 AVRAQDGPLILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLQDRIRIIHLDITSegcCTHLLPWGP 126
Cdd:COG4123    32 FAPVKKGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKE---FAAELPPGS 108

                          90
                  ....*....|
gi 1958795565 127 MDLVVSNPPY 136
Cdd:COG4123   109 FDLVVSNPPY 118
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 56-187 6.29e-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: 78.31  E-value: 6.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  56 ILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLQDrIRIIHLDITSEgccthlLPWGPMDLVVSNPP 135
Cdd:COG2813    53 VLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAANGLEN-VEVLWSDGLSG------VPDGSFDLILSNPP 125

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958795565 136 yiFRkdmeqlapeirsyedlvalDGGDEGMDIITHILTLAPWLLNASGSIFL 187
Cdd:COG2813   126 --FH-------------------AGRAVDKEVAHALIADAARHLRPGGELWL 156
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 56-187 4.35e-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: 64.92  E-value: 4.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  56 ILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLqDRIRIIHLDITSEgccthlLPWGPMDLVVSNPP 135
Cdd:pfam05175  35 VLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGL-ENGEVVASDVYSG------VEDGKFDLIISNPP 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958795565 136 yiFRkdmeqlapeirsyedlvalDGGDEGMDIITHILTLAPWLLNASGSIFL 187
Cdd:pfam05175 108 --FH-------------------AGLATTYNVAQRFIADAKRHLRPGGELWI 138
PRK14966 PRK14966
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; ...
 2-188 8.82e-13

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


Pssm-ID: 184930 [Multi-domain]  Cd Length: 423  Bit Score: 66.64  E-value: 8.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565   2 PVQYILGEWDFQGLNLKMAPPVFIPRPETeelVEWVLEEVAQRPPAVRAQDgplileVGCGSGAIALSLLSQLPKTQVIA 81
Cdd:PRK14966  210 PVAYILGVREFYGRRFAVNPNVLIPRPET---EHLVEAVLARLPENGRVWD------LGTGSGAVAVTVALERPDAFVRA 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  82 VDKEEAAVSLTLENAQrlQLQDRIRIIH-----LDITSEGccthllPWgpmDLVVSNPPYIFRKDMEQLAPEIRsYEDLV 156
Cdd:PRK14966  281 SDISPPALETARKNAA--DLGARVEFAHgswfdTDMPSEG------KW---DIIVSNPPYIENGDKHLLQGDLR-FEPQI 348

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1958795565 157 ALDGGDEGMDIITHILTLAPWLLNASGSIFLE 188
Cdd:PRK14966  349 ALTDFSDGLSCIRTLAQGAPDRLAEGGFLLLE 380
PRK14968 PRK14968
putative methyltransferase; Provisional
 47-199 6.29e-12

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 62.22  E-value: 6.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  47 AVRAQDGPLILEVGCGSGAIALSLLSQLPKtqVIAVDKEEAAVSLTLENAQRLQLQDR-IRIIHLDITSegCCTHllpwG 125
Cdd:PRK14968   18 NAVDKKGDRVLEVGTGSGIVAIVAAKNGKK--VVGVDINPYAVECAKCNAKLNNIRNNgVEVIRSDLFE--PFRG----D 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958795565 126 PMDLVVSNPPYIFRKDMEqlapEIRSYEDLvALDGGDEGMDIITHILTLAPWLLNASGSIFLevdprhpeLVSS 199
Cdd:PRK14968   90 KFDVILFNPPYLPTEEEE----EWDDWLNY-ALSGGKDGREVIDRFLDEVGRYLKPGGRILL--------LQSS 150
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 49-108 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: 56.57  E-value: 1.97e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  49 RAQDGPLILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLqDRIRII 108
Cdd:TIGR02469  16 RLRPGDVLWDIGAGTGSVTIEAARLVPNGRVYAIERNPEALDLIERNLRRFGV-SNIVIV 74
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 56-150 9.00e-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: 54.36  E-value: 9.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  56 ILEVGCGSGAIALSLLSQlPKTQVIAVDKEEAAVSLTLENAQRLqLQDRIRIIHLDITSEgcctHLLPWGPMDLVVSNPP 135
Cdd:cd02440     2 VLDLGCGTGALALALASG-PGARVTGVDISPVALELARKAAAAL-LADNVEVLKGDAEEL----PPEADESFDVIISDPP 75

                          90
                  ....*....|....*.
gi 1958795565 136 YIFRK-DMEQLAPEIR 150
Cdd:cd02440    76 LHHLVeDLARFLEEAR 91
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 56-150 2.52e-09

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 52.95  E-value: 2.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  56 ILEVGCGSGAIALsLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLqdRIRIIHLDItsegccTHL-LPWGPMDLVVSNP 134
Cdd:pfam13649   1 VLDLGCGTGRLTL-ALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDA------EDLpFPDGSFDLVVSSG 71

                          90
                  ....*....|....*...
gi 1958795565 135 P--YIFRKDMEQLAPEIR 150
Cdd:pfam13649  72 VlhHLPDPDLEAALREIA 89
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
56-133 9.75e-09

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 51.36  E-value: 9.75e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958795565  56 ILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAvsltLENAQrlQLQDRIRIIHLDItsegccTHLLPWGPMDLVVSN 133
Cdd:COG4106     5 VLDLGCGTGRLTALLAERFPGARVTGVDLSPEM----LARAR--ARLPNVRFVVADL------RDLDPPEPFDLVVSN 70
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 48-109 9.82e-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: 54.79  E-value: 9.82e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  48 VRA--------QDGPLILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLqDRIRIIH 109
Cdd:COG2242   235 VRAltlaklalRPGDVLWDIGAGSGSVSIEAARLAPGGRVYAIERDPERAALIRANARRFGV-PNVEVVE 303
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
56-152 6.11e-08

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 52.10  E-value: 6.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  56 ILEVGCGSG--AIALSLLsqlPKTQVIAVDKEEAAVSLTLENAQRLQLQDRIRIIHLDITSEgccthllpwGPMDLVVSN 133
Cdd:COG2264   152 VLDVGCGSGilAIAAAKL---GAKRVLAVDIDPVAVEAARENAELNGVEDRIEVVLGDLLED---------GPYDLVVAN 219

                          90
                  ....*....|....*....
gi 1958795565 134 ppyIFRKDMEQLAPEIRSY 152
Cdd:COG2264   220 ---ILANPLIELAPDLAAL 235
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
52-135 6.17e-08

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 51.06  E-value: 6.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  52 DGPLILEVGCGSG--AIALSLLSqlPKtQVIAVDKEEAAVSLTLENAQRLQlqDRIRIIHLDITsegcctHLLPWGPMDL 129
Cdd:COG2263    45 EGKTVLDLGCGTGmlAIGAALLG--AK-KVVGVDIDPEALEIARENAERLG--VRVDFIRADVT------RIPLGGSVDT 113


                  ....*.
gi 1958795565 130 VVSNPP 135
Cdd:COG2263   114 VVMNPP 119
PRK14967 PRK14967
putative methyltransferase; Provisional
 53-187 6.35e-08

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 51.59  E-value: 6.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  53 GPLILEVGCGSGAIALSLlSQLPKTQVIAVDKEEAAVSLTLENAqrLQLQDRIRIIHLDITSEgccthlLPWGPMDLVVS 132
Cdd:PRK14967   37 GRRVLDLCTGSGALAVAA-AAAGAGSVTAVDISRRAVRSARLNA--LLAGVDVDVRRGDWARA------VEFRPFDVVVS 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958795565 133 NPPYIFRKDMeqlAPEIRSYEDlvALDGGDEGMDIITHILTLAPWLLNASGSIFL 187
Cdd:PRK14967  108 NPPYVPAPPD---APPSRGPAR--AWDAGPDGRAVLDRLCDAAPALLAPGGSLLL 157
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 56-133 2.40e-07

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 48.57  E-value: 2.40e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958795565  56 ILEVGCGSGAIALSLLSQL-PKTQVIAVDKEEAAVSLTLENAQRLQLqDRIRIIHLDITSEGCcthLLPWGPMDLVVSN 133
Cdd:pfam13847   7 VLDLGCGTGHLSFELAEELgPNAEVVGIDISEEAIEKARENAQKLGF-DNVEFEQGDIEELPE---LLEDDKFDVVISN 81
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 47-132 2.79e-07

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 48.77  E-value: 2.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  47 AVRAQDGPLILEVGCGSGAIALSLLSQLpKTQVIAVDKEEAAVSLTLENAQRLQLQDRIRIIHLDItsegccTHLLPWGP 126
Cdd:COG2230    46 KLGLKPGMRVLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADY------RDLPADGQ 118


                  ....*.
gi 1958795565 127 MDLVVS 132
Cdd:COG2230   119 FDAIVS 124
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 56-131 4.47e-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: 49.00  E-value: 4.47e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958795565  56 ILEVGCGSGAIALSLLSQL-PKTQVIAVDKEEAAVSLTLENAQRLQLQDRIRIIHLDItSEGccthlLPWGPMDLVV 131
Cdd:COG2519    95 VLEAGTGSGALTLALARAVgPEGKVYSYERREDFAEIARKNLERFGLPDNVELKLGDI-REG-----IDEGDVDAVF 165
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 49-133 6.55e-07

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 48.37  E-value: 6.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  49 RAQDGPLILEVGCGSGAIALsLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLqDRIRIIHLDITSegccTHLLPWGPMD 128
Cdd:COG0500    23 RLPKGGRVLDLGCGTGRNLL-ALAARFGGRVIGIDLSPEAIALARARAAKAGL-GNVEFLVADLAE----LDPLPAESFD 96


                  ....*
gi 1958795565 129 LVVSN 133
Cdd:COG0500    97 LVVAF 101
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 47-206 7.20e-07

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: 7.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  47 AVRAQDGPLILEVGCGSGAIALSLLSQLPKtqVIAVDKEEAAVSLTLENAQRLQLQdrIRIIHLDItSEGCCthllpwGP 126
Cdd:TIGR00537  14 NLRELKPDDVLEIGAGTGLVAIRLKGKGKC--ILTTDINPFAVKELRENAKLNNVG--LDVVMTDL-FKGVR------GK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565 127 MDLVVSNPPYIFRKDMEQlapeIRSYEDlVALDGGDEGMDIITHILTLAPWLLNASGSIflevdprhpELVSSWLQSQPD 206
Cdd:TIGR00537  83 FDVILFNPPYLPLEDDLR----RGDWLD-VAIDGGKDGRKVIDRFLDELPEILKEGGRV---------QLIQSSLNGEPD 148
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 49-108 1.66e-06

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 47.10  E-value: 1.66e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958795565  49 RAQDGPLILEVGCGSGAIAL--SLLSQlPKTQVIAVDKEEAAVSLTLENAQRLQLQDRIRII 108
Cdd:PRK00377   37 RLRKGDMILDIGCGTGSVTVeaSLLVG-ETGKVYAVDKDEKAINLTRRNAEKFGVLNNIVLI 97
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 47-150 4.76e-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: 44.98  E-value: 4.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  47 AVRAQDGPLILEVGCGSGAIALSLLSQlpKTQVIAVDKEEAAVSLTLENAQRLQLqdRIRIIHLDITSegccthlLPW-- 124
Cdd:COG2226    17 ALGLRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAED-------LPFpd 85

                          90       100
                  ....*....|....*....|....*.
gi 1958795565 125 GPMDLVVSNPPYIFRKDMEQLAPEIR 150
Cdd:COG2226    86 GSFDLVISSFVLHHLPDPERALAEIA 111
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 49-149 1.03e-05

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


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 44.65  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  49 RAQDGPLILEVGCGSGAIAL-----------SLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLQDRIRIIHLDITSegc 117
Cdd:pfam01170  25 GWKPGDPLLDPMCGSGTILIeaalmganiapGKFDARVRAPLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAAD--- 101

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958795565 118 cthlLPW--GPMDLVVSNPPYIFR----KDMEQLAPEI 149
Cdd:pfam01170 102 ----LPLleGSVDVIVTNPPYGIRlgskGALEALYPEF 135
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
56-108 1.21e-05

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


Pssm-ID: 181354  Cd Length: 187  Bit Score: 44.61  E-value: 1.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958795565  56 ILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLQDrIRII 108
Cdd:PRK08287   35 LIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKENRQRFGCGN-IDII 86
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 67-136 1.29e-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: 1.29e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  67 ALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLQDRIRIIHLDITsegcctHLLPWGPMDLVVSNPPY 136
Cdd:COG0116   241 AEARIKRDPPLPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFR------DLEPPAEPGLIITNPPY 304
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 57-133 1.48e-05

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 42.35  E-value: 1.48e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958795565  57 LEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLE--NAQRLQLQDRIRIIHLDITSegccthlLPWGPMDLVVSN 133
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARErlAALGLLNAVRVELFQLDLGE-------LDPGSFDVVVAS 72
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
47-132 3.26e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 43.49  E-value: 3.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  47 AVRAQDGP--LILEVGCGSGAIALsLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLQDRIRIIHLDItsegccTHLLPW 124
Cdd:COG4076    28 AIERVVKPgdVVLDIGTGSGLLSM-LAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADA------TDLDLP 100


                  ....*...
gi 1958795565 125 GPMDLVVS 132
Cdd:COG4076   101 EKADVIIS 108
rADc smart00650
Ribosomal RNA adenine dimethylases;
47-144 3.63e-05

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 42.88  E-value: 3.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565   47 AVRAQDGPLILEVGCGSGAIALSLLSQLPKtqVIAVDKEEAAVSLTlenAQRLQLQDRIRIIHLDItsegCCTHLLPWGP 126
Cdd:smart00650   8 AANLRPGDTVLEIGPGKGALTEELLERAKR--VTAIEIDPRLAPRL---REKFAAADNLTVIHGDA----LKFDLPKLQP 78

                           90       100
                   ....*....|....*....|...
gi 1958795565  127 mDLVVSNPPY-----IFRKDMEQ 144
Cdd:smart00650  79 -YKVVGNLPYnistpILFKLLEE 100
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 49-133 3.99e-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: 41.93  E-value: 3.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  49 RAQDGPLILEVGCGSGAIALSLLSQlpKTQVIAVDKEEAAvsltLENAQRLQLQDRIRIIHLDITsegccTHLLPWGPMD 128
Cdd:COG2227    21 LLPAGGRVLDVGCGTGRLALALARR--GADVTGVDISPEA----LEIARERAAELNVDFVQGDLE-----DLPLEDGSFD 89


                  ....*
gi 1958795565 129 LVVSN 133
Cdd:COG2227    90 LVICS 94
TrmB COG0220
tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 ...
 50-112 7.97e-05

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: 7.97e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958795565  50 AQDGPLILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLqDRIRIIHLDI 112
Cdd:COG0220    30 GNDAPLVLEIGFGKGEFLVELAAANPDINFIGIEVHEPGVAKALKKAEEEGL-TNVRLLRGDA 91
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
56-152 1.61e-04

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


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 41.86  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  56 ILEVGCGSGAIALSLLSQLP-KTQVIAVDKEEAAVSLTLENAQRLQLQdrIRIIHLDITsegcctHLLPWGPMDLVVSNP 134
Cdd:COG0827   119 ILDPAVGTGNLLTTVLNQLKkKVNAYGVEVDDLLIRLAAVLANLQGHP--VELFHQDAL------QPLLIDPVDVVISDL 190

                          90       100
                  ....*....|....*....|....
gi 1958795565 135 PYIF------RKDMEQLAPEIRSY 152
Cdd:COG0827   191 PVGYypnderAKRFKLKADEGHSY 214
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 47-135 2.74e-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: 41.32  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  47 AVRAQDGPLILEVGCGSGAIALSLLSQlpKTQVIAVDKEEAAVSLTLENAQRLQLqDRIRIIHLDitSEGCCTHLLPWGP 126
Cdd:COG2265   228 WLDLTGGERVLDLYCGVGTFALPLARR--AKKVIGVEIVPEAVEDARENARLNGL-KNVEFVAGD--LEEVLPELLWGGR 302


                  ....*....
gi 1958795565 127 MDLVVSNPP 135
Cdd:COG2265   303 PDVVVLDPP 311
Methyltransf_4 pfam02390
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ...
 52-113 3.10e-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: 39.97  E-value: 3.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958795565  52 DGPLILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLQDrIRIIHLDIT 113
Cdd:pfam02390   1 DAPVFLEIGCGMGGFLVAMAKANPDKNFIGIEIRVPGVAKALKKIDALGLQN-LRILCGNAL 61
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 51-133 3.18e-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: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  51 QDGPLILEVGCGSG--AIALSLLSQLPktqVIAVDKEEAAVSLTLENAQRLQLQDRiriIHLDITSEgccthlLPWGPMD 128
Cdd:pfam06325 160 KPGESVLDVGCGSGilAIAALKLGAKK---VVGVDIDPVAVRAAKENAELNGVEAR---LEVYLPGD------LPKEKAD 227


                  ....*
gi 1958795565 129 LVVSN 133
Cdd:pfam06325 228 VVVAN 232
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
56-107 4.12e-04

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 40.52  E-value: 4.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958795565  56 ILEVGCGSG--AIALSLLSQlpkTQVIAVDKEEAAVSLTLENAQRLQLQDRIRI 107
Cdd:PRK00517  123 VLDVGCGSGilAIAAAKLGA---KKVLAVDIDPQAVEAARENAELNGVELNVYL 173
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 57-133 1.20e-03

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 36.87  E-value: 1.20e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958795565  57 LEVGCGSGAIALSLLSQLPktQVIAVDKEEAAvsltLENAQRLQLQDRIRIIHLDITSegccthlLPW--GPMDLVVSN 133
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEM----LELAREKAPREGLTFVVGDAED-------LPFpdNSFDLVLSS 66
trmB PRK00121
tRNA (guanine-N(7)-)-methyltransferase; Reviewed
 51-113 1.62e-03

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


Pssm-ID: 234649  Cd Length: 202  Bit Score: 38.22  E-value: 1.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958795565  51 QDGPLILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLQDrIRIIHLDIT 113
Cdd:PRK00121   39 NDAPIHLEIGFGKGEFLVEMAKANPDINFIGIEVHEPGVGKALKKIEEEGLTN-LRLLCGDAV 100
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 73-136 2.31e-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: 2.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958795565  73 QLPKTQVIAVDKEEAAVSLTLENAQRLQLQDRIRIIHLDITSegcCTHLLPWGPMDLVVSNPPY 136
Cdd:PRK11783  253 AELPSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVAD---LKNPLPKGPTGLVISNPPY 313
PRK15001 PRK15001
23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;
56-97 2.66e-03

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


Pssm-ID: 184963 [Multi-domain]  Cd Length: 378  Bit Score: 38.47  E-value: 2.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958795565  56 ILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQ 97
Cdd:PRK15001  232 IVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVE 273
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
56-136 2.90e-03

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


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 38.00  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  56 ILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAvsltLENAQRLQLQDRI--RIIHLDITSEgccthllPWGPMDLVVSN 133
Cdd:PRK09489  200 VLDVGCGAGVLSAVLARHSPKIRLTLSDVSAAA----LESSRATLAANGLegEVFASNVFSD-------IKGRFDMIISN 268


                  ...
gi 1958795565 134 PPY 136
Cdd:PRK09489  269 PPF 271
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 49-149 2.98e-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: 37.89  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  49 RAQDGPLILEVGCGSGAIALSLLsQLPKTQVIAVDKEEAAVSLTLENAQRLQLQDRIRII--HLDITSEgccthllpwGP 126
Cdd:TIGR00406 156 LDLKDKNVIDVGCGSGILSIAAL-KLGAAKVVGIDIDPLAVESARKNAELNQVSDRLQVKliYLEQPIE---------GK 225

                          90       100
                  ....*....|....*....|...
gi 1958795565 127 MDLVVSNppyIFRKDMEQLAPEI 149
Cdd:TIGR00406 226 ADVIVAN---ILAEVIKELYPQF 245
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
56-136 3.61e-03

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 37.57  E-value: 3.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  56 ILEVGCGSGAIALSLLSQLPKTQVIAVDKeeaavslTLEN--AQRLQLQDRIRIIHLDITSegccthlLPWGPMDLVVSN 133
Cdd:PRK14896   33 VLEIGPGKGALTDELAKRAKKVYAIELDP-------RLAEflRDDEIAAGNVEIIEGDALK-------VDLPEFNKVVSN 98


                  ...
gi 1958795565 134 PPY 136
Cdd:PRK14896   99 LPY 101
PTZ00338 PTZ00338
dimethyladenosine transferase-like protein; Provisional
 47-136 4.40e-03

dimethyladenosine transferase-like protein; Provisional


Pssm-ID: 240367 [Multi-domain]  Cd Length: 294  Bit Score: 37.29  E-value: 4.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795565  47 AVRAQDgpLILEVGCGSGAIALSLLsQLPKtQVIAVDKEEAAVSLTLENAQRLQLQDRIRIIHLDitsegCCTHLLPwgP 126
Cdd:PTZ00338   33 AIKPTD--TVLEIGPGTGNLTEKLL-QLAK-KVIAIEIDPRMVAELKKRFQNSPLASKLEVIEGD-----ALKTEFP--Y 101

                          90
                  ....*....|
gi 1958795565 127 MDLVVSNPPY 136
Cdd:PTZ00338  102 FDVCVANVPY 111
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 61-136 5.20e-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: 37.15  E-value: 5.20e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958795565  61 CGSGAIALSLLSQLPKTqVIAVDKEEAAVSLTLENAQRLQLQDRIRIIHLDitsegcCTHLLPW--GPMDLVVSNPPY 136
Cdd:COG2520   189 AGVGPFSIPIAKRSGAK-VVAIDINPDAVEYLKENIRLNKVEDRVTPILGD------AREVAPEleGKADRIIMNLPH 259
PRK07402 PRK07402
precorrin-6Y C5,15-methyltransferase subunit CbiT;
47-103 5.73e-03

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


Pssm-ID: 180961  Cd Length: 196  Bit Score: 36.51  E-value: 5.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958795565  47 AVRAQDGPLILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLQD 103
Cdd:PRK07402   35 QLRLEPDSVLWDIGAGTGTIPVEAGLLCPKGRVIAIERDEEVVNLIRRNCDRFGVKN 91
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
 56-114 9.03e-03

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


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 35.24  E-value: 9.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958795565  56 ILEVGCGSGAIALSLLSQLPKTQVIAVDKEEAAVSLTLENAQRLQLQDRIRIIHLDITS 114
Cdd:pfam13679  29 IVDHGAGKGYLGFILYYLKYGVRVYGIDTRAELVEKANALAQKLGFNKRMSFLEGTIAG 87
 
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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