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Conserved domains on  [gi|2829611|sp|P74003|]
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RecName: Full=Release factor glutamine methyltransferase; Short=RF MTase; AltName: Full=M.Ssp6803HemKP; AltName: Full=N5-glutamine methyltransferase PrmC; AltName: Full=Protein-(glutamine-N5) MTase PrmC; AltName: Full=Protein-glutamine N-methyltransferase PrmC

Protein Classification

peptide chain release factor N(5)-glutamine methyltransferase( domain architecture ID 11489222)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
6-299 1.97e-131

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: 374.38  E-value: 1.97e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611      6 VSGEEFARWYATARQMAIAHgiETGELNWLLQGWTDLDRLTLRLQDFAHREIALQEtWENIQRGWRRRVEEkYPVQYLLG 85
Cdd:TIGR00536   1 MTIQEFLRWASSALSRAIAR--ENPWLEALLLLEHDLGRERDLLLAFLTEELTPDE-KERIFRLVLRRVKG-VPVAYLLG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611     86 QTQWRDFVIKVTDDVLIPRPETELIidiVQHEHSALSPSNCADHWVDLGTGSGAIALGLAATFPQALVHAVDCSGSALAI 165
Cdd:TIGR00536  77 SKEFYGLEFFVNEHVLIPRPETEEL---VEKALASLISQPPILHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611    166 ARENAQLNQFGDRIQFHQGYWWEPLEHLkgQVQGMVSNPPYIPQRELAQLqPEVIKHEPLLALDGGPDGLQAVEQLIRRS 245
Cdd:TIGR00536 154 AEENAEKNQLEHRVEFIQSNLFEPLAGQ--KIDIIVSNPPYIDEEDLADL-PNVVRFEPLLALVGGDDGLNILRQIIELA 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2829611    246 PTYLKPGGFWLVEIMTGQAPMVAELLRASGAYQDIQIHRDLASIERFVSARTLS 299
Cdd:TIGR00536 231 PDYLKPNGFLVCEIGNWQQKSLKELLRIKFTWYDVENGRDLNGKERVVLGFYHS 284
 
Name Accession Description Interval E-value
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
6-299 1.97e-131

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: 374.38  E-value: 1.97e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611      6 VSGEEFARWYATARQMAIAHgiETGELNWLLQGWTDLDRLTLRLQDFAHREIALQEtWENIQRGWRRRVEEkYPVQYLLG 85
Cdd:TIGR00536   1 MTIQEFLRWASSALSRAIAR--ENPWLEALLLLEHDLGRERDLLLAFLTEELTPDE-KERIFRLVLRRVKG-VPVAYLLG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611     86 QTQWRDFVIKVTDDVLIPRPETELIidiVQHEHSALSPSNCADHWVDLGTGSGAIALGLAATFPQALVHAVDCSGSALAI 165
Cdd:TIGR00536  77 SKEFYGLEFFVNEHVLIPRPETEEL---VEKALASLISQPPILHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611    166 ARENAQLNQFGDRIQFHQGYWWEPLEHLkgQVQGMVSNPPYIPQRELAQLqPEVIKHEPLLALDGGPDGLQAVEQLIRRS 245
Cdd:TIGR00536 154 AEENAEKNQLEHRVEFIQSNLFEPLAGQ--KIDIIVSNPPYIDEEDLADL-PNVVRFEPLLALVGGDDGLNILRQIIELA 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2829611    246 PTYLKPGGFWLVEIMTGQAPMVAELLRASGAYQDIQIHRDLASIERFVSARTLS 299
Cdd:TIGR00536 231 PDYLKPNGFLVCEIGNWQQKSLKELLRIKFTWYDVENGRDLNGKERVVLGFYHS 284
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
12-296 2.13e-104

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 305.92  E-value: 2.13e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611   12 ARWYATARQMAIAHGIETGEL--NWLLQGWTDLDRLTLRLqdFAHREIAlQETWENIQRGWRRRvEEKYPVQYLLGQTQW 89
Cdd:COG2890   4 RELLRWAAARLAAAGVDSARLeaELLLAHVLGLDRADLLL--HPDRPLT-EEELARLEALVARR-AAGEPLAYILGEAEF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611   90 RDFVIKVTDDVLIPRPETELIIDIVQHEHSALSPSncadHWVDLGTGSGAIALGLAATFPQALVHAVDCSGSALAIAREN 169
Cdd:COG2890  80 YGLEFKVDPGVLIPRPETEELVELALALLPAGAPP----RVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRN 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611  170 AQLNQFGDRIQFHQGYWWEPLEHlKGQVQGMVSNPPYIPQRELAQLQPEVIKHEPLLALDGGPDGLQAVEQLIRRSPTYL 249
Cdd:COG2890 156 AERLGLEDRVRFLQGDLFEPLPG-DGRFDLIVSNPPYIPEDEIALLPPEVRDHEPRLALDGGEDGLDFYRRIIAQAPRLL 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 2829611  250 KPGGFWLVEIMTGQAPMVAELLRASGaYQDIQIHRDLASIERFVSAR 296
Cdd:COG2890 235 KPGGWLLLEIGEDQGEAVRALLEAAG-FADVETHKDLAGRDRVVVAR 280
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
30-296 1.44e-91

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 272.81  E-value: 1.44e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611    30 GELNWLLQGWTDLDRLTLRLQdfaHREIALQETWENIQRGWRRRVEeKYPVQYLLGQTQWRDFVIKVTDDVLIPRPETEL 109
Cdd:PRK09328  20 LDAELLLAHVLGLSRTDLLLN---PEEELTPEELERFRALVARRAA-GEPLQYILGEAEFWGLDFKVSPGVLIPRPETEE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611   110 IIDIVQHEHSALSPsncaDHWVDLGTGSGAIALGLAATFPQALVHAVDCSGSALAIARENAQLNQfGDRIQFHQGYWWEP 189
Cdd:PRK09328  96 LVEWALEALLLKEP----LRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGL-GARVEFLQGDWFEP 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611   190 LEhlKGQVQGMVSNPPYIPQRELAQLQPEVIKHEPLLALDGGPDGLQAVEQLIRRSPTYLKPGGFWLVEIMTGQAPMVAE 269
Cdd:PRK09328 171 LP--GGRFDLIVSNPPYIPEADIHLLQPEVRDHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGWLLLEIGYDQGEAVRA 248
                        250       260
                 ....*....|....*....|....*..
gi 2829611   270 LLRASGaYQDIQIHRDLASIERFVSAR 296
Cdd:PRK09328 249 LLAAAG-FADVETRKDLAGRDRVVLGR 274
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
131-257 8.66e-14

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 68.00  E-value: 8.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611    131 VDLGTGSGAIALGLAATFPQALVHAVDCSGSALAIARENAQLNQFgDRIQFHQGYWWEPLEhlKGQVQGMVSNPPYipqr 210
Cdd:pfam05175  36 LDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGL-ENGEVVASDVYSGVE--DGKFDLIISNPPF---- 108
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2829611    211 elaqlqpevikHEpllaldGGPDGLQAVEQLIRRSPTYLKPGG-FWLV 257
Cdd:pfam05175 109 -----------HA------GLATTYNVAQRFIADAKRHLRPGGeLWIV 139
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
131-221 6.02e-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: 50.12  E-value: 6.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611  131 VDLGTGSGAIALGLAAtFPQALVHAVDCSGSALAIARENAqLNQFGDRIQFHQGYWWEPLEHLKGQVQGMVSNPPYIPqr 210
Cdd:cd02440   3 LDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAA-AALLADNVEVLKGDAEELPPEADESFDVIISDPPLHH-- 78
                        90
                ....*....|.
gi 2829611  211 eLAQLQPEVIK 221
Cdd:cd02440  79 -LVEDLARFLE 88
 
Name Accession Description Interval E-value
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
6-299 1.97e-131

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: 374.38  E-value: 1.97e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611      6 VSGEEFARWYATARQMAIAHgiETGELNWLLQGWTDLDRLTLRLQDFAHREIALQEtWENIQRGWRRRVEEkYPVQYLLG 85
Cdd:TIGR00536   1 MTIQEFLRWASSALSRAIAR--ENPWLEALLLLEHDLGRERDLLLAFLTEELTPDE-KERIFRLVLRRVKG-VPVAYLLG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611     86 QTQWRDFVIKVTDDVLIPRPETELIidiVQHEHSALSPSNCADHWVDLGTGSGAIALGLAATFPQALVHAVDCSGSALAI 165
Cdd:TIGR00536  77 SKEFYGLEFFVNEHVLIPRPETEEL---VEKALASLISQPPILHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611    166 ARENAQLNQFGDRIQFHQGYWWEPLEHLkgQVQGMVSNPPYIPQRELAQLqPEVIKHEPLLALDGGPDGLQAVEQLIRRS 245
Cdd:TIGR00536 154 AEENAEKNQLEHRVEFIQSNLFEPLAGQ--KIDIIVSNPPYIDEEDLADL-PNVVRFEPLLALVGGDDGLNILRQIIELA 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2829611    246 PTYLKPGGFWLVEIMTGQAPMVAELLRASGAYQDIQIHRDLASIERFVSARTLS 299
Cdd:TIGR00536 231 PDYLKPNGFLVCEIGNWQQKSLKELLRIKFTWYDVENGRDLNGKERVVLGFYHS 284
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
12-296 2.13e-104

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 305.92  E-value: 2.13e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611   12 ARWYATARQMAIAHGIETGEL--NWLLQGWTDLDRLTLRLqdFAHREIAlQETWENIQRGWRRRvEEKYPVQYLLGQTQW 89
Cdd:COG2890   4 RELLRWAAARLAAAGVDSARLeaELLLAHVLGLDRADLLL--HPDRPLT-EEELARLEALVARR-AAGEPLAYILGEAEF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611   90 RDFVIKVTDDVLIPRPETELIIDIVQHEHSALSPSncadHWVDLGTGSGAIALGLAATFPQALVHAVDCSGSALAIAREN 169
Cdd:COG2890  80 YGLEFKVDPGVLIPRPETEELVELALALLPAGAPP----RVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRN 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611  170 AQLNQFGDRIQFHQGYWWEPLEHlKGQVQGMVSNPPYIPQRELAQLQPEVIKHEPLLALDGGPDGLQAVEQLIRRSPTYL 249
Cdd:COG2890 156 AERLGLEDRVRFLQGDLFEPLPG-DGRFDLIVSNPPYIPEDEIALLPPEVRDHEPRLALDGGEDGLDFYRRIIAQAPRLL 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 2829611  250 KPGGFWLVEIMTGQAPMVAELLRASGaYQDIQIHRDLASIERFVSAR 296
Cdd:COG2890 235 KPGGWLLLEIGEDQGEAVRALLEAAG-FADVETHKDLAGRDRVVVAR 280
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
30-296 1.44e-91

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 272.81  E-value: 1.44e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611    30 GELNWLLQGWTDLDRLTLRLQdfaHREIALQETWENIQRGWRRRVEeKYPVQYLLGQTQWRDFVIKVTDDVLIPRPETEL 109
Cdd:PRK09328  20 LDAELLLAHVLGLSRTDLLLN---PEEELTPEELERFRALVARRAA-GEPLQYILGEAEFWGLDFKVSPGVLIPRPETEE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611   110 IIDIVQHEHSALSPsncaDHWVDLGTGSGAIALGLAATFPQALVHAVDCSGSALAIARENAQLNQfGDRIQFHQGYWWEP 189
Cdd:PRK09328  96 LVEWALEALLLKEP----LRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGL-GARVEFLQGDWFEP 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611   190 LEhlKGQVQGMVSNPPYIPQRELAQLQPEVIKHEPLLALDGGPDGLQAVEQLIRRSPTYLKPGGFWLVEIMTGQAPMVAE 269
Cdd:PRK09328 171 LP--GGRFDLIVSNPPYIPEADIHLLQPEVRDHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGWLLLEIGYDQGEAVRA 248
                        250       260
                 ....*....|....*....|....*..
gi 2829611   270 LLRASGaYQDIQIHRDLASIERFVSAR 296
Cdd:PRK09328 249 LLAAAG-FADVETRKDLAGRDRVVLGR 274
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
34-294 3.94e-77

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: 235.44  E-value: 3.94e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611     34 WLLQGWTDLDRLTLrlqdFAHREIAL-QETWENIQRGWRRRvEEKYPVQYLLGQTQWRDFVIKVTDDVLIPRPETELIID 112
Cdd:TIGR03534   4 LLLAHVLGKDRAQL----LLHPEDELtPEELAAFDALLARR-AAGEPVAYILGEREFYGLDFKVSPGVLIPRPETEELVE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611    113 ivqhehSALSPSNCADHWVDLGTGSGAIALGLAATFPQALVHAVDCSGSALAIARENAQLNQFgDRIQFHQGYWWEPLeh 192
Cdd:TIGR03534  79 ------AALERLKKGPRVLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKNARRLGL-ENVEFLQGDWFEPL-- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611    193 LKGQVQGMVSNPPYIPQRELAQLQPEVIKHEPLLALDGGPDGLQAVEQLIRRSPTYLKPGGFWLVEIMTGQAPMVAELLR 272
Cdd:TIGR03534 150 PSGKFDLIVSNPPYIPEADIHLLDPEVRDFEPRLALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFE 229
                         250       260
                  ....*....|....*....|..
gi 2829611    273 ASGaYQDIQIHRDLASIERFVS 294
Cdd:TIGR03534 230 AAG-FADVETRKDLAGKDRVVL 250
L3_gln_methyl TIGR03533
protein-(glutamine-N5) methyltransferase, ribosomal protein L3-specific; Members of this ...
71-259 6.42e-40

protein-(glutamine-N5) methyltransferase, ribosomal protein L3-specific; Members of this protein family methylate ribosomal protein L3 on a glutamine side chain. This family is related to HemK, a protein-glutamine methyltranferase for peptide chain release factors. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 274633 [Multi-domain]  Cd Length: 284  Bit Score: 140.73  E-value: 6.42e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611     71 RRRVEEKYPVQYLLGQTQWRDFVIKVTDDVLIPR-PETELIID----IVQHE--HSALspsncadhwvDLGTGSGAIALG 143
Cdd:TIGR03533  69 ERRIEERIPVAYLTNEAWFAGLEFYVDERVLIPRsPIAELIEDgfapWLEPEpvKRIL----------DLCTGSGCIAIA 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611    144 LAATFPQALVHAVDCSGSALAIARENAQLNQFGDRIQFHQGYWWEPLEHLKGQVqgMVSNPPYIPQRELAQLQPEvIKHE 223
Cdd:TIGR03533 139 CAYAFPEAEVDAVDISPDALAVAEINIERHGLEDRVTLIQSDLFAALPGRKYDL--IVSNPPYVDAEDMADLPAE-YHHE 215
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2829611    224 PLLALDGGPDGLQAVEQLIRRSPTYLKPGGFWLVEI 259
Cdd:TIGR03533 216 PELALASGEDGLDLVRRILAEAADHLNENGVLVVEV 251
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
72-293 5.91e-34

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


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 129.21  E-value: 5.91e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611    72 RRVEEKyPVQYLLGQTQW--RDFVikVTDDVLIPRPETELIIDIVQHEHSALS-------PSNCA-------------DH 129
Cdd:PRK01544  65 RRLKHE-PIAYITGVKEFysREFI--VNKHVLIPRSDTEVLVDVVFQCHSRESgnpekkqLNPCFrgndissncndkfLN 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611   130 WVDLGTGSGAIALGLAATFPQALVHAVDCSGSALAIARENAQLNQFGDRIQFHQGYWWEPLEHLKGQVqgMVSNPPYIPQ 209
Cdd:PRK01544 142 ILELGTGSGCIAISLLCELPNANVIATDISLDAIEVAKSNAIKYEVTDRIQIIHSNWFENIEKQKFDF--IVSNPPYISH 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611   210 RELAQLQPEVIKHEPLLALDGGPDGLQAVEQLIRRSPTYLKPGGFWLVEIMTGQAPMVAELLRASGaYQDIQIHRDLASI 289
Cdd:PRK01544 220 SEKSEMAIETINYEPSIALFAEEDGLQAYFIIAENAKQFLKPNGKIILEIGFKQEEAVTQIFLDHG-YNIESVYKDLQGH 298

                 ....
gi 2829611   290 ERFV 293
Cdd:PRK01544 299 SRVI 302
PrmC_rel_meth TIGR03704
putative protein-(glutamine-N5) methyltransferase, unknown substrate-specific; This protein ...
52-275 6.83e-33

putative protein-(glutamine-N5) methyltransferase, unknown substrate-specific; This protein family is closely related to two different families of protein-(glutamine-N5) methyltransferase. The first is PrmB, which modifies ribosomal protein L3 in some bacteria. The second is PrmC (HemK), which modifies peptide chain release factors 1 and 2 in most bacteria and also in eukaryotes. The glutamine side chain-binding motif NPPY shared by PrmB and PrmC is N[VAT]PY in this family. The protein substrate is unknown. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 274733 [Multi-domain]  Cd Length: 251  Bit Score: 121.43  E-value: 6.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611     52 FAHREIAL----QETWENIQRGWRRRVEeKYPVQYLLGQTQWRDFVIKVTDDVLIPRPETELIIDIVQHEHSALSPSNCA 127
Cdd:TIGR03704  12 FAEDEAALlvdaARTPGELAAMVDRRVA-GLPLEHVLGWAEFCGLRIAVDPGVFVPRRRTEFLVDEAAALARPRSGTLVV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611    128 dhwVDLGTGSGAIALGLAATFPQALVHAVDCSGSALAIARENaqLNQFGDRIqfHQGYWWEPL-EHLKGQVQGMVSNPPY 206
Cdd:TIGR03704  91 ---VDLCCGSGAVGAALAAALDGIELHAADIDPAAVRCARRN--LADAGGTV--HEGDLYDALpTALRGRVDILAANAPY 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2829611    207 IPQRELAQLQPEVIKHEPLLALDGGPDGLQAVEQLIRRSPTYLKPGGFWLVEIMTGQAPMVAELLRASG 275
Cdd:TIGR03704 164 VPTDAIALMPPEARDHEPRVALDGGADGLDVLRRVAAGAPDWLAPGGHLLVETSERQAPLAVEAFARAG 232
PRK14966 PRK14966
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; ...
61-291 1.44e-27

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


Pssm-ID: 184930 [Multi-domain]  Cd Length: 423  Bit Score: 110.56  E-value: 1.44e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611    61 ETWENIQRGWRRRVEEKyPVQYLLGqtqWRDFV---IKVTDDVLIPRPETELIIDIVQhehsALSPSNcADHWvDLGTGS 137
Cdd:PRK14966 193 EVRQRADRLAQRRLNGE-PVAYILG---VREFYgrrFAVNPNVLIPRPETEHLVEAVL----ARLPEN-GRVW-DLGTGS 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611   138 GAIALGLAATFPQALVHAVDCSGSALAIARENAQlnQFGDRIQFHQGYWWEPLEHLKGQVQGMVSNPPYIPQRElAQLQP 217
Cdd:PRK14966 263 GAVAVTVALERPDAFVRASDISPPALETARKNAA--DLGARVEFAHGSWFDTDMPSEGKWDIIVSNPPYIENGD-KHLLQ 339
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2829611   218 EVIKHEPLLALDGGPDGLQAVEQLIRRSPTYLKPGGFWLVEIMTGQAPMVAELLRASGaYQDIQIHRDLASIER 291
Cdd:PRK14966 340 GDLRFEPQIALTDFSDGLSCIRTLAQGAPDRLAEGGFLLLEHGFDQGAAVRGVLAENG-FSGVETLPDLAGLDR 412
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
127-257 5.89e-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: 79.85  E-value: 5.89e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611  127 ADHWVDLGTGSGAIALGLAATFPQALVHAVDCSGSALAIARENAQLNQFgDRIQFHQGYWWEPLEHlkGQVQGMVSNPPY 206
Cdd:COG2813  50 GGRVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAANGL-ENVEVLWSDGLSGVPD--GSFDLILSNPPF 126
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 2829611  207 ipqrelaqlqpevikHepllalDGGPDGLQAVEQLIRRSPTYLKPGG-FWLV 257
Cdd:COG2813 127 ---------------H------AGRAVDKEVAHALIADAARHLRPGGeLWLV 157
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
131-257 1.36e-17

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: 79.80  E-value: 1.36e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611  131 VDLGTGSGAIALGLAATFPQALVHAVDCSGSALAIARENAQLNQFGDRIQFHQGYWWEPLEHLKGQ----VqgmVSNPPY 206
Cdd:COG4123  42 LDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAAELPPGsfdlV---VSNPPY 118
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2829611  207 ----------IPQRELAqlqpeviKHEPLLALdggpdglqavEQLIRRSPTYLKPGG-FWLV 257
Cdd:COG4123 119 fkagsgrkspDEARAIA-------RHEDALTL----------EDLIRAAARLLKPGGrFALI 163
PRK14967 PRK14967
putative methyltransferase; Provisional
97-257 1.38e-14

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 71.24  E-value: 1.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611    97 TDDVLIPRPETELIIDIVQHEHsaLSPSNCAdhwVDLGTGSGAIALGlAATFPQALVHAVDCSGSALAIARENAQLNqfG 176
Cdd:PRK14967  12 APGVYRPQEDTQLLADALAAEG--LGPGRRV---LDLCTGSGALAVA-AAAAGAGSVTAVDISRRAVRSARLNALLA--G 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611   177 DRIQFHQGYWWEPLEHLKGQVqgMVSNPPYIPQRELAqlqpeVIKHEPLLALDGGPDGLQAVEQLIRRSPTYLKPGGFWL 256
Cdd:PRK14967  84 VDVDVRRGDWARAVEFRPFDV--VVSNPPYVPAPPDA-----PPSRGPARAWDAGPDGRAVLDRLCDAAPALLAPGGSLL 156

                 .
gi 2829611   257 V 257
Cdd:PRK14967 157 L 157
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
131-257 8.66e-14

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 68.00  E-value: 8.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611    131 VDLGTGSGAIALGLAATFPQALVHAVDCSGSALAIARENAQLNQFgDRIQFHQGYWWEPLEhlKGQVQGMVSNPPYipqr 210
Cdd:pfam05175  36 LDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGL-ENGEVVASDVYSGVE--DGKFDLIISNPPF---- 108
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2829611    211 elaqlqpevikHEpllaldGGPDGLQAVEQLIRRSPTYLKPGG-FWLV 257
Cdd:pfam05175 109 -----------HA------GLATTYNVAQRFIADAKRHLRPGGeLWIV 139
PRK14968 PRK14968
putative methyltransferase; Provisional
98-253 3.05e-12

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 64.15  E-value: 3.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611    98 DDVLIPRPETELIIDIVQhehsalspSNCADHWVDLGTGSG--AIALGLAATFpqalVHAVDCSGSALAIARENAQLNQF 175
Cdd:PRK14968   3 DEVYEPAEDSFLLAENAV--------DKKGDRVLEVGTGSGivAIVAAKNGKK----VVGVDINPYAVECAKCNAKLNNI 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611   176 GDR-IQFHQGYWWEPLEHLKGQVqgMVSNPPYIPQRelaqlqPEVIKHEPL-LALDGGPDGLQAVEQLIRRSPTYLKPGG 253
Cdd:PRK14968  71 RNNgVEVIRSDLFEPFRGDKFDV--ILFNPPYLPTE------EEEEWDDWLnYALSGGKDGREVIDRFLDEVGRYLKPGG 142
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
128-253 3.84e-11

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: 60.64  E-value: 3.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611    128 DHWVDLGTGSGAIALGLAATfpQALVHAVDCSGSALAIARENAQLNQFGdrIQFHQGYWWEPLEhlkGQVQGMVSNPPYI 207
Cdd:TIGR00537  21 DDVLEIGAGTGLVAIRLKGK--GKCILTTDINPFAVKELRENAKLNNVG--LDVVMTDLFKGVR---GKFDVILFNPPYL 93
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2829611    208 PQRElaqlqPEVIKHEPLLALDGGPDGLQAVEQLIRRSPTYLKPGG 253
Cdd:TIGR00537  94 PLED-----DLRRGDWLDVAIDGGKDGRKVIDRFLDELPEILKEGG 134
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
132-275 3.06e-08

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 53.64  E-value: 3.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611  132 DLGTGSG--AIAlglAATFPQALVHAVDCSGSALAIARENAQLNQFGDRIQFHQGywwePLEHlKGQVQGMVSNppyIpq 209
Cdd:COG2264 154 DVGCGSGilAIA---AAKLGAKRVLAVDIDPVAVEAARENAELNGVEDRIEVVLG----DLLE-DGPYDLVVAN---I-- 220
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2829611  210 reLAqlqpevikhEPLLALdggpdglqaVEQLIRRsptyLKPGGFWLVE-IMTGQAPMVAELLRASG 275
Cdd:COG2264 221 --LA---------NPLIEL---------APDLAAL----LKPGGYLILSgILEEQADEVLAAYEAAG 263
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
131-221 6.02e-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: 50.12  E-value: 6.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611  131 VDLGTGSGAIALGLAAtFPQALVHAVDCSGSALAIARENAqLNQFGDRIQFHQGYWWEPLEHLKGQVQGMVSNPPYIPqr 210
Cdd:cd02440   3 LDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAA-AALLADNVEVLKGDAEELPPEADESFDVIISDPPLHH-- 78
                        90
                ....*....|.
gi 2829611  211 eLAQLQPEVIK 221
Cdd:cd02440  79 -LVEDLARFLE 88
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
132-273 9.84e-08

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: 52.27  E-value: 9.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611    132 DLGTGSGAIALGlAATFPQALVHAVDCSGSALAIARENAQLNQFGDRIQFHQgywwePLEHLKGQVQGMVSNppyipqre 211
Cdd:pfam06325 167 DVGCGSGILAIA-ALKLGAKKVVGVDIDPVAVRAAKENAELNGVEARLEVYL-----PGDLPKEKADVVVAN-------- 232
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2829611    212 laqlqpevIKHEPLLALdggpdglqaVEQLIRRsptyLKPGG-FWLVEIMTGQAPMVAELLRA 273
Cdd:pfam06325 233 --------ILADPLIEL---------APDIYAL----VKPGGyLILSGILKEQAQMVAEAYSQ 274
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
132-184 2.07e-07

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 48.33  E-value: 2.07e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2829611    132 DLGTGSGAIALGLAATFpQALVHAVDCSGSALAIARENAQlnQFGDRIQFHQG 184
Cdd:pfam13649   3 DLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERAA--EAGLNVEFVQG 52
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
153-184 1.40e-06

23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 49.02  E-value: 1.40e-06
                        10        20        30
                ....*....|....*....|....*....|..
gi 2829611  153 VHAVDCSGSALAIARENAQLNQFGDRIQFHQG 184
Cdd:COG1092 242 VTSVDLSATALEWAKENAALNGLDDRHEFVQA 273
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
131-196 1.68e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 47.03  E-value: 1.68e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2829611    131 VDLGTGSGAIALGLAATF-PQALVHAVDCSGSALAIARENAQLNQFgDRIQFHQGYWWEPLEHLKGQ 196
Cdd:pfam13847   8 LDLGCGTGHLSFELAEELgPNAEVVGIDISEEAIEKARENAQKLGF-DNVEFEQGDIEELPELLEDD 73
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
127-184 3.01e-06

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 44.81  E-value: 3.01e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 2829611  127 ADHWVDLGTGSGAIALGLAATFPQALVHAVDCSGSALAIARENAqlnqfgDRIQFHQG 184
Cdd:COG4106   2 PRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARL------PNVRFVVA 53
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
128-184 6.73e-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: 6.73e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 2829611  128 DHWVDLGTGSGAIALGLAATfpQALVHAVDCSGSALAIARENAQlnQFGDRIQFHQG 184
Cdd:COG2226  24 ARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAA--EAGLNVEFVVG 76
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
136-206 2.32e-05

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


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 44.27  E-value: 2.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611    136 GSGAIAL-----------GLAATFPQALVHAVDCSGSALAIARENAQLNQFGDRIQFHQgywWE--PLEHLKGQVQGMVS 202
Cdd:pfam01170  38 GSGTILIeaalmganiapGKFDARVRAPLYGSDIDRRMVQGARLNAENAGVGDLIEFVQ---ADaaDLPLLEGSVDVIVT 114

                  ....
gi 2829611    203 NPPY 206
Cdd:pfam01170 115 NPPY 118
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
131-184 2.48e-05

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: 45.17  E-value: 2.48e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 2829611  131 VDLGTGSGAIALGLAATFPQalVHAVDCSGSALAIARENAQLNQFgDRIQFHQG 184
Cdd:COG2265 238 LDLYCGVGTFALPLARRAKK--VIGVEIVPEAVEDARENARLNGL-KNVEFVAG 288
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
131-188 3.23e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 44.26  E-value: 3.23e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 2829611  131 VDLGTGSGAIALgLAATFPQALVHAVDCSGSALAIARENAQLNQFGDRIQFHQGYWWE 188
Cdd:COG4076  40 LDIGTGSGLLSM-LAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATD 96
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
132-253 5.20e-05

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


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 44.16  E-value: 5.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611   132 DLGTGSGAIALGLAATFPQALVHAVDCSGSALAIARENAQLNQFGDRIQFHQGYwweplEHLKGQVQGMVSNPPYipqre 211
Cdd:PRK09489 202 DVGCGAGVLSAVLARHSPKIRLTLSDVSAAALESSRATLAANGLEGEVFASNVF-----SDIKGRFDMIISNPPF----- 271
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 2829611   212 laqlqpevikHepllalDGGPDGLQAVEQLIRRSPTYLKPGG 253
Cdd:PRK09489 272 ----------H------DGIQTSLDAAQTLIRGAVRHLNSGG 297
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
129-259 1.46e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 41.83  E-value: 1.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611  129 HWVDLGTGSGAIALGLAATFpQALVHAVDCSGSALAIARENAQLNQFGdRIQFHQGYWWEPLEHLKGQVQGMVSNppyip 208
Cdd:COG0500  29 RVLDLGCGTGRNLLALAARF-GGRVIGIDLSPEAIALARARAAKAGLG-NVEFLVADLAELDPLPAESFDLVVAF----- 101
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 2829611  209 qrelaqlqpEVIKHEPllaldggPDGLQAVEQLIRRsptYLKPGGFWLVEI 259
Cdd:COG0500 102 ---------GVLHHLP-------PEEREALLRELAR---ALKPGGVLLLSA 133
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
119-193 1.47e-04

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: 42.85  E-value: 1.47e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2829611  119 SALSPSNcADHWVDLGTGSGAIALGLAATFPQALVHAVDCSGSALAIARENAQlnQFG-DRIQFHQGYWWEPLEHL 193
Cdd:COG2242 241 AKLALRP-GDVLWDIGAGSGSVSIEAARLAPGGRVYAIERDPERAALIRANAR--RFGvPNVEVVEGEAPEALADL 313
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
131-205 1.50e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 41.81  E-value: 1.50e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2829611  131 VDLGTGSGAIALGlAATFPQALVHAVDCSGSALAIARENAqlNQFGDRIQFHQGYWWEPleHLKGQVQGMVSNPP 205
Cdd:COG2263  50 LDLGCGTGMLAIG-AALLGAKKVVGVDIDPEALEIARENA--ERLGVRVDFIRADVTRI--PLGGSVDTVVMNPP 119
PRK15001 PRK15001
23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;
123-212 1.59e-04

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


Pssm-ID: 184963 [Multi-domain]  Cd Length: 378  Bit Score: 42.71  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611   123 PSNCADHWVDLGTGSGAIALGLAATFPQALVHAVDCSGSALAIARENAQLN--QFGDRIQFHQGYWWEPLEHLKgqVQGM 200
Cdd:PRK15001 225 PENLEGEIVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNmpEALDRCEFMINNALSGVEPFR--FNAV 302
                         90
                 ....*....|..
gi 2829611   201 VSNPPYIPQREL 212
Cdd:PRK15001 303 LCNPPFHQQHAL 314
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
131-258 3.80e-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: 39.62  E-value: 3.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611  131 VDLGTGSGAIALGLAATFpqALVHAVDCSGSALAIARENAQlnqfGDRIQFHQGYwWEPLEHLKGQVQGMVSNppyipqr 210
Cdd:COG2227  29 LDVGCGTGRLALALARRG--ADVTGVDISPEALEIARERAA----ELNVDFVQGD-LEDLPLEDGSFDLVICS------- 94
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 2829611  211 elaqlqpEVIKHepllaldggpdgLQAVEQLIRRSPTYLKPGGFWLVE 258
Cdd:COG2227  95 -------EVLEH------------LPDPAALLRELARLLKPGGLLLLS 123
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
132-184 4.78e-04

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 39.91  E-value: 4.78e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 2829611  132 DLGTGSGAIALGLAATFpQALVHAVDCSGSALAIARENAQLNQFGDRIQFHQG 184
Cdd:COG2230  57 DIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLA 108
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
141-206 1.07e-03

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: 40.08  E-value: 1.07e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2829611  141 ALGLAATFPQALVHAVDCSGSALAIARENAQLNQFGDRIQFHQGywwePLEHLKGQVQG--MVSNPPY 206
Cdd:COG0116 241 AEARIKRDPPLPIFGSDIDPRAIEAARENAERAGVADLIEFEQA----DFRDLEPPAEPglIITNPPY 304
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
131-184 1.42e-03

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 37.26  E-value: 1.42e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2829611    131 VDLGTGSGAIALGLAATFPQalVHAVDCSGSALAIARENAQlnqfGDRIQFHQG 184
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR--VTGVDISPEMLELAREKAP----REGLTFVVG 48
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
132-275 1.52e-03

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 39.36  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611   132 DLGTGSG--AI-ALGLAATFpqalVHAVDCSGSALAIARENAQLNQFGDRIQFHQGywweplehlKGQVQGMVSNppyIp 208
Cdd:PRK00517 125 DVGCGSGilAIaAAKLGAKK----VLAVDIDPQAVEAARENAELNGVELNVYLPQG---------DLKADVIVAN---I- 187
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2829611   209 qreLAqlqpevikhEPLLALdggpdglqaVEQLIRRsptyLKPGGfWLveIMTG----QAPMVAELLRASG 275
Cdd:PRK00517 188 ---LA---------NPLLEL---------APDLARL----LKPGG-RL--ILSGileeQADEVLEAYEEAG 230
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
131-184 2.63e-03

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 36.58  E-value: 2.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2829611    131 VDLGTGSGAIALGLAATFPQALVHAVDCSGSALAIARE--NAQLNQFGDRIQFHQG 184
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARErlAALGLLNAVRVELFQL 56
PrmC_N pfam17827
PrmC N-terminal domain; This entry corresponds to the N-terminal alpha helical domain of the ...
14-85 2.67e-03

PrmC N-terminal domain; This entry corresponds to the N-terminal alpha helical domain of the HemK protein. HemK is a methyltransferase enzyme that carries out the methylation of the N5 nitrogen of the glutamine found in the conserved GGQ motif of class-1 release factors.


Pssm-ID: 436073 [Multi-domain]  Cd Length: 71  Bit Score: 35.92  E-value: 2.67e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2829611     14 WYATARQMAIAHGIETGELN--WLLQGWTDLDRLTLrlqdFAHREIAL-QETWENIQRGWRRRVEeKYPVQYLLG 85
Cdd:pfam17827   2 ALRWASSRLKEAGIESPRLDaeLLLAHVLGLDRTDL----LLHPEEELsEEELERFEELLERRAA-GEPLQYILG 71
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
127-185 2.81e-03

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


Pssm-ID: 181354  Cd Length: 187  Bit Score: 38.06  E-value: 2.81e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829611   127 ADHWVDLGTGSGAIALGLAATFPQALVHAVDCSGSALAIARENAQlnQFG-DRIQFHQGY 185
Cdd:PRK08287  32 AKHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKENRQ--RFGcGNIDIIPGE 89
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
131-191 8.39e-03

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 36.54  E-value: 8.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2829611    131 VDLGTGSGAIALGLAATFPQALVHAVDCSGsALAIARENAQLNQFGDRIQFHQGYWWEPLE 191
Cdd:pfam10294  51 LELGSGTGLVGIAVALLLPGASVTITDLEE-ALELLKKNIELNALSSKVVVKVLDWGENLP 110
 
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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