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Conserved domains on  [gi|616915685|gb|KAH06834|]
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protein-(glutamine-N5) methyltransferase, release factor-specific [Staphylococcus aureus VET1738S]

Protein Classification

peptide chain release factor N(5)-glutamine methyltransferase( domain architecture ID 11497022)

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
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 25-275 3.21e-97

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: 285.52  E-value: 3.21e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685   25 AEWLMLDVFQWTRTDFVVHMHDDMPKAMIMKFDLALQRMLLGEPIQYIVGFASFYGRTFDVNSNCLIPRPETEEVMLHFL 104
Cdd:TIGR03534   2 AELLLAHVLGKDRAQLLLHPEDELTPEELAAFDALLARRAAGEPVAYILGEREFYGLDFKVSPGVLIPRPETEELVEAAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685  105 QQLEDDATIVDIGTGSGVLAITLKCEKPDLNVIATDISLEAMNMARNNAEKHQ-SQIQFLTGDALKPLikEGIKLNGLIS 183
Cdd:TIGR03534  82 ERLKKGPRVLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKNARRLGlENVEFLQGDWFEPL--PSGKFDLIVS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685  184 NPPYIDEKDMVTMSPTVTRFEPHQALFADNHGYAIYESIIEDLPHVMEKGSPVVFEIGYNQGEALKSiILNKFPDKKIDI 263
Cdd:TIGR03534 160 NPPYIPEADIHLLDPEVRDFEPRLALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRA-LFEAAGFADVET 238

                         250
                  ....*....|..
gi 616915685  264 IKDINGHDRIVS 275
Cdd:TIGR03534 239 RKDLAGKDRVVL 250
 
Name Accession Description Interval E-value
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 25-275 3.21e-97

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: 285.52  E-value: 3.21e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685   25 AEWLMLDVFQWTRTDFVVHMHDDMPKAMIMKFDLALQRMLLGEPIQYIVGFASFYGRTFDVNSNCLIPRPETEEVMLHFL 104
Cdd:TIGR03534   2 AELLLAHVLGKDRAQLLLHPEDELTPEELAAFDALLARRAAGEPVAYILGEREFYGLDFKVSPGVLIPRPETEELVEAAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685  105 QQLEDDATIVDIGTGSGVLAITLKCEKPDLNVIATDISLEAMNMARNNAEKHQ-SQIQFLTGDALKPLikEGIKLNGLIS 183
Cdd:TIGR03534  82 ERLKKGPRVLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKNARRLGlENVEFLQGDWFEPL--PSGKFDLIVS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685  184 NPPYIDEKDMVTMSPTVTRFEPHQALFADNHGYAIYESIIEDLPHVMEKGSPVVFEIGYNQGEALKSiILNKFPDKKIDI 263
Cdd:TIGR03534 160 NPPYIPEADIHLLDPEVRDFEPRLALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRA-LFEAAGFADVET 238

                         250
                  ....*....|..
gi 616915685  264 IKDINGHDRIVS 275
Cdd:TIGR03534 239 RKDLAGKDRVVL 250
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 1-278 5.75e-95

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 280.89  E-value: 5.75e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685   1 MVNYKEKLDEAihlTQQKGFEQTRAEWLMLDVFQWTRTDFVVHMHDDMPKAMIMKFDLALQRMLLGEPIQYIVGFASFYG 80
Cdd:PRK09328   1 MMTIAEALREA---TARLASPRLDAELLLAHVLGLSRTDLLLNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFWG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685  81 RTFDVNSNCLIPRPETEEVMLHFLQQLEDD--ATIVDIGTGSGVLAITLKCEKPDLNVIATDISLEAMNMARNNAEKH-Q 157
Cdd:PRK09328  78 LDFKVSPGVLIPRPETEELVEWALEALLLKepLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGlG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685 158 SQIQFLTGDALKPLikEGIKLNGLISNPPYIDEKDMVTMSPTVTRFEPHQALFADNHGYAIYESIIEDLPHVMEKGSPVV 237
Cdd:PRK09328 158 ARVEFLQGDWFEPL--PGGRFDLIVSNPPYIPEADIHLLQPEVRDHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGWLL 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 616915685 238 FEIGYNQGEALKSiILNKFPDKKIDIIKDINGHDRIVSFKW 278
Cdd:PRK09328 236 LEIGYDQGEAVRA-LLAAAGFADVETRKDLAGRDRVVLGRR 275
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 3-278 1.93e-89

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 267.02  E-value: 1.93e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685   3 NYKEKLDEAIHLTQQKGFEQTR--AEWLMLDVFQWTRTDFVVHMHDDMPKAMIMKFDLALQRMLLGEPIQYIVGFASFYG 80
Cdd:COG2890    2 TIRELLRWAAARLAAAGVDSARleAELLLAHVLGLDRADLLLHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFYG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685  81 RTFDVNSNCLIPRPETEEVMLHFLQQLEDDA--TIVDIGTGSGVLAITLKCEKPDLNVIATDISLEAMNMARNNAEKHQ- 157
Cdd:COG2890   82 LEFKVDPGVLIPRPETEELVELALALLPAGAppRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLGl 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685 158 -SQIQFLTGDALKPLIKEGiKLNGLISNPPYIDEKDMVTMSPTVTRFEPHQALFADNHGYAIYESIIEDLPHVMEKGSPV 236
Cdd:COG2890  162 eDRVRFLQGDLFEPLPGDG-RFDLIVSNPPYIPEDEIALLPPEVRDHEPRLALDGGEDGLDFYRRIIAQAPRLLKPGGWL 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 616915685 237 VFEIGYNQGEALKSiILNKFPDKKIDIIKDINGHDRIVSFKW 278
Cdd:COG2890  241 LLEIGEDQGEAVRA-LLEAAGFADVETHKDLAGRDRVVVARR 281
PrmC_N pfam17827
PrmC N-terminal domain; This entry corresponds to the N-terminal alpha helical domain of the ...
 8-74 7.87e-16

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: 70.20  E-value: 7.87e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616915685    8 LDEAIHLTQQKGFEQTR--AEWLMLDVFQWTRTDFVVHMHDDMPKAMIMKFDLALQRMLLGEPIQYIVG 74
Cdd:pfam17827   3 LRWASSRLKEAGIESPRldAELLLAHVLGLDRTDLLLHPEEELSEEELERFEELLERRAAGEPLQYILG 71
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 112-192 1.02e-09

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: 54.74  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685 112 TIVDIGTGSGVLAITLKcEKPDLNVIATDISLEAMNMAR-NNAEKHQSQIQFLTGDALKPLIKEGIKLNGLISNPPYIDE 190
Cdd:cd02440    1 RVLDLGCGTGALALALA-SGPGARVTGVDISPVALELARkAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLHHL 79


                 ..
gi 616915685 191 KD 192
Cdd:cd02440   80 VE 81
 
Name Accession Description Interval E-value
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 25-275 3.21e-97

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: 285.52  E-value: 3.21e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685   25 AEWLMLDVFQWTRTDFVVHMHDDMPKAMIMKFDLALQRMLLGEPIQYIVGFASFYGRTFDVNSNCLIPRPETEEVMLHFL 104
Cdd:TIGR03534   2 AELLLAHVLGKDRAQLLLHPEDELTPEELAAFDALLARRAAGEPVAYILGEREFYGLDFKVSPGVLIPRPETEELVEAAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685  105 QQLEDDATIVDIGTGSGVLAITLKCEKPDLNVIATDISLEAMNMARNNAEKHQ-SQIQFLTGDALKPLikEGIKLNGLIS 183
Cdd:TIGR03534  82 ERLKKGPRVLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKNARRLGlENVEFLQGDWFEPL--PSGKFDLIVS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685  184 NPPYIDEKDMVTMSPTVTRFEPHQALFADNHGYAIYESIIEDLPHVMEKGSPVVFEIGYNQGEALKSiILNKFPDKKIDI 263
Cdd:TIGR03534 160 NPPYIPEADIHLLDPEVRDFEPRLALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRA-LFEAAGFADVET 238

                         250
                  ....*....|..
gi 616915685  264 IKDINGHDRIVS 275
Cdd:TIGR03534 239 RKDLAGKDRVVL 250
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 1-278 5.75e-95

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 280.89  E-value: 5.75e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685   1 MVNYKEKLDEAihlTQQKGFEQTRAEWLMLDVFQWTRTDFVVHMHDDMPKAMIMKFDLALQRMLLGEPIQYIVGFASFYG 80
Cdd:PRK09328   1 MMTIAEALREA---TARLASPRLDAELLLAHVLGLSRTDLLLNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFWG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685  81 RTFDVNSNCLIPRPETEEVMLHFLQQLEDD--ATIVDIGTGSGVLAITLKCEKPDLNVIATDISLEAMNMARNNAEKH-Q 157
Cdd:PRK09328  78 LDFKVSPGVLIPRPETEELVEWALEALLLKepLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGlG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685 158 SQIQFLTGDALKPLikEGIKLNGLISNPPYIDEKDMVTMSPTVTRFEPHQALFADNHGYAIYESIIEDLPHVMEKGSPVV 237
Cdd:PRK09328 158 ARVEFLQGDWFEPL--PGGRFDLIVSNPPYIPEADIHLLQPEVRDHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGWLL 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 616915685 238 FEIGYNQGEALKSiILNKFPDKKIDIIKDINGHDRIVSFKW 278
Cdd:PRK09328 236 LEIGYDQGEAVRA-LLAAAGFADVETRKDLAGRDRVVLGRR 275
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 3-278 1.93e-89

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 267.02  E-value: 1.93e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685   3 NYKEKLDEAIHLTQQKGFEQTR--AEWLMLDVFQWTRTDFVVHMHDDMPKAMIMKFDLALQRMLLGEPIQYIVGFASFYG 80
Cdd:COG2890    2 TIRELLRWAAARLAAAGVDSARleAELLLAHVLGLDRADLLLHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFYG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685  81 RTFDVNSNCLIPRPETEEVMLHFLQQLEDDA--TIVDIGTGSGVLAITLKCEKPDLNVIATDISLEAMNMARNNAEKHQ- 157
Cdd:COG2890   82 LEFKVDPGVLIPRPETEELVELALALLPAGAppRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLGl 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685 158 -SQIQFLTGDALKPLIKEGiKLNGLISNPPYIDEKDMVTMSPTVTRFEPHQALFADNHGYAIYESIIEDLPHVMEKGSPV 236
Cdd:COG2890  162 eDRVRFLQGDLFEPLPGDG-RFDLIVSNPPYIPEDEIALLPPEVRDHEPRLALDGGEDGLDFYRRIIAQAPRLLKPGGWL 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 616915685 237 VFEIGYNQGEALKSiILNKFPDKKIDIIKDINGHDRIVSFKW 278
Cdd:COG2890  241 LLEIGEDQGEAVRA-LLEAAGFADVETHKDLAGRDRVVVARR 281
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 3-278 5.30e-56

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: 181.78  E-value: 5.30e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685    3 NYKEKLDEAIhltQQKGFEQTR---AEWLMLDVFQWTRTDFVVHMHDDMPKAMIMKFDLALQRMLLGEPIQYIVGFASFY 79
Cdd:TIGR00536   5 EFLRWASSAL---SRAIARENPwleALLLLEHDLGRERDLLLAFLTEELTPDEKERIFRLVLRRVKGVPVAYLLGSKEFY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685   80 GRTFDVNSNCLIPRPETEEVMLHFLQQLEDDAT---IVDIGTGSGVLAITLKCEKPDLNVIATDISLEAMNMARNNAEKH 156
Cdd:TIGR00536  82 GLEFFVNEHVLIPRPETEELVEKALASLISQPPilhILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685  157 Q--SQIQFLTGDALKPLikEGIKLNGLISNPPYIDEKDMVTMsPTVTRFEPHQALFADNHGYAIYESIIEDLPHVMEKGS 234
Cdd:TIGR00536 162 QleHRVEFIQSNLFEPL--AGQKIDIIVSNPPYIDEEDLADL-PNVVRFEPLLALVGGDDGLNILRQIIELAPDYLKPNG 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 616915685  235 PVVFEIGYNQGEALKSIILNKFPDKKIDIIKDINGHDRIVSFKW 278
Cdd:TIGR00536 239 FLVCEIGNWQQKSLKELLRIKFTWYDVENGRDLNGKERVVLGFY 282
PRK14966 PRK14966
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; ...
 5-252 1.23e-41

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


Pssm-ID: 184930 [Multi-domain]  Cd Length: 423  Bit Score: 147.92  E-value: 1.23e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685   5 KEKLDEAIHLTQqkgFEQTRAEWLMLDVFQWTRTDFVVHMHDDMPKAMIMKFDLALQRMLLGEPIQYIVGFASFYGRTFD 84
Cdd:PRK14966 150 KMTFDEWLGLSK---LPKNEARMLLQYASEYTRVQLLTRGGEEMPDEVRQRADRLAQRRLNGEPVAYILGVREFYGRRFA 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685  85 VNSNCLIPRPETEEVMLHFLQQLEDDATIVDIGTGSGVLAITLKCEKPDLNVIATDISLEAMNMARNNAEKHQSQIQFLT 164
Cdd:PRK14966 227 VNPNVLIPRPETEHLVEAVLARLPENGRVWDLGTGSGAVAVTVALERPDAFVRASDISPPALETARKNAADLGARVEFAH 306

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685 165 GDALKPLIKEGIKLNGLISNPPYIDEKDMvTMSPTVTRFEPHQALFADNHGYAIYESIIEDLPHVMEKGSPVVFEIGYNQ 244
Cdd:PRK14966 307 GSWFDTDMPSEGKWDIIVSNPPYIENGDK-HLLQGDLRFEPQIALTDFSDGLSCIRTLAQGAPDRLAEGGFLLLEHGFDQ 385


                 ....*...
gi 616915685 245 GEALKSII 252
Cdd:PRK14966 386 GAAVRGVL 393
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
 40-254 1.33e-38

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


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 141.54  E-value: 1.33e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685  40 FVVHMHDDMPKAMIMKFDLALQRMLLGEPIQYIVGFASFYGRTFDVNSNCLIPRPETE---EVMLHFL---------QQL 107
Cdd:PRK01544  43 LLINLDEQLNEAEIEAFEKLLERRLKHEPIAYITGVKEFYSREFIVNKHVLIPRSDTEvlvDVVFQCHsresgnpekKQL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685 108 EDDAT--------------IVDIGTGSGVLAITLKCEKPDLNVIATDISLEAMNMARNNAEKHQ--SQIQFLTGDALKPL 171
Cdd:PRK01544 123 NPCFRgndissncndkflnILELGTGSGCIAISLLCELPNANVIATDISLDAIEVAKSNAIKYEvtDRIQIIHSNWFENI 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685 172 IKEgiKLNGLISNPPYIDEKDMVTMSPTVTRFEPHQALFADNHGYAIYESIIEDLPHVMEKGSPVVFEIGYNQGEALKSI 251
Cdd:PRK01544 203 EKQ--KFDFIVSNPPYISHSEKSEMAIETINYEPSIALFAEEDGLQAYFIIAENAKQFLKPNGKIILEIGFKQEEAVTQI 280


                 ...
gi 616915685 252 ILN 254
Cdd:PRK01544 281 FLD 283
L3_gln_methyl TIGR03533
protein-(glutamine-N5) methyltransferase, ribosomal protein L3-specific; Members of this ...
 68-248 1.05e-23

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: 97.20  E-value: 1.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685   68 PIQYIVGFASFYGRTFDVNSNCLIPRPETEEVMLHFLQQL---EDDATIVDIGTGSGVLAITLKCEKPDLNVIATDISLE 144
Cdd:TIGR03533  77 PVAYLTNEAWFAGLEFYVDERVLIPRSPIAELIEDGFAPWlepEPVKRILDLCTGSGCIAIACAYAFPEAEVDAVDISPD 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685  145 AMNMARNNAEKH--QSQIQFLTGDALKPLikEGIKLNGLISNPPYIDEKDMVTMsPTVTRFEPHQALFADNHGYAIYESI 222
Cdd:TIGR03533 157 ALAVAEINIERHglEDRVTLIQSDLFAAL--PGRKYDLIVSNPPYVDAEDMADL-PAEYHHEPELALASGEDGLDLVRRI 233

                         170       180
                  ....*....|....*....|....*.
gi 616915685  223 IEDLPHVMEKGSPVVFEIGYNQgEAL 248
Cdd:TIGR03533 234 LAEAADHLNENGVLVVEVGNSM-EAL 258
PrmC_N pfam17827
PrmC N-terminal domain; This entry corresponds to the N-terminal alpha helical domain of the ...
 8-74 7.87e-16

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: 70.20  E-value: 7.87e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616915685    8 LDEAIHLTQQKGFEQTR--AEWLMLDVFQWTRTDFVVHMHDDMPKAMIMKFDLALQRMLLGEPIQYIVG 74
Cdd:pfam17827   3 LRWASSRLKEAGIESPRldAELLLAHVLGLDRTDLLLHPEEELSEEELERFEELLERRAAGEPLQYILG 71
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 103-187 4.28e-14

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: 69.06  E-value: 4.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685 103 FLQQLEDDA--TIVDIGTGSGVLAITLKCEKPDLNVIATDISLEAMNMARNNAEKHQ-SQIQFLTGDALKPLikEGIKLN 179
Cdd:COG2813   41 LLEHLPEPLggRVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAANGlENVEVLWSDGLSGV--PDGSFD 118


                 ....*...
gi 616915685 180 GLISNPPY 187
Cdd:COG2813  119 LILSNPPF 126
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 103-186 1.03e-10

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: 59.14  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685  103 FLQQLEDDAT--IVDIGTGSGVLAITLKCEKPDLNVIATDISLEAMNMARNNAEKHQ-SQIQFLTGDALKPLiKEGiKLN 179
Cdd:pfam05175  23 LLEHLPKDLSgkVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGlENGEVVASDVYSGV-EDG-KFD 100


                  ....*..
gi 616915685  180 GLISNPP 186
Cdd:pfam05175 101 LIISNPP 107
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 112-192 1.02e-09

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: 54.74  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685 112 TIVDIGTGSGVLAITLKcEKPDLNVIATDISLEAMNMAR-NNAEKHQSQIQFLTGDALKPLIKEGIKLNGLISNPPYIDE 190
Cdd:cd02440    1 RVLDLGCGTGALALALA-SGPGARVTGVDISPVALELARkAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLHHL 79


                 ..
gi 616915685 191 KD 192
Cdd:cd02440   80 VE 81
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 113-169 9.03e-09

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 51.80  E-value: 9.03e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 616915685  113 IVDIGTGSGVLAITLkCEKPDLNVIATDISLEAMNMARNNAEKHQSQIQFLTGDALK 169
Cdd:pfam13649   1 VLDLGCGTGRLTLAL-ARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAED 56
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 107-218 1.21e-08

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: 54.38  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685 107 LEDDATIVDIGTGSGVLAITLKCEKPDLNVIATDISLEAMNMARNNAE--KHQSQIQFLTGD--ALKPLIKEGiKLNGLI 182
Cdd:COG4123   35 VKKGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVAlnGLEDRITVIHGDlkEFAAELPPG-SFDLVV 113

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 616915685 183 SNPPYidekdmvtmsptvtrFEPHQALFADNHGYAI 218
Cdd:COG4123  114 SNPPY---------------FKAGSGRKSPDEARAI 134
PRK14968 PRK14968
putative methyltransferase; Provisional
 108-188 2.83e-08

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 52.59  E-value: 2.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685 108 EDDATIVDIGTGSGVLAITLKceKPDLNVIATDISLEAMNMARNNAEKHQ---SQIQFLTGDALKPLikEGIKLNGLISN 184
Cdd:PRK14968  22 KKGDRVLEVGTGSGIVAIVAA--KNGKKVVGVDINPYAVECAKCNAKLNNirnNGVEVIRSDLFEPF--RGDKFDVILFN 97


                 ....
gi 616915685 185 PPYI 188
Cdd:PRK14968  98 PPYL 101
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 102-211 6.42e-08

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: 50.76  E-value: 6.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685 102 HFLQQL--EDDATIVDIGTGSGVLAITLKceKPDLNVIATDISLEAMNMARNNAEKHQSQIQFLTGDAlkplikegikln 179
Cdd:COG2226   13 ALLAALglRPGARVLDLGCGTGRLALALA--ERGARVTGVDISPEMLELARERAAEAGLNVEFVVGDA------------ 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 616915685 180 gliSNPPYIDEK-DMVTMSPTVTRFEPHQALFA 211
Cdd:COG2226   79 ---EDLPFPDGSfDLVISSFVLHHLPDPERALA 108
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 104-171 6.92e-08

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 51.46  E-value: 6.92e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616915685 104 LQQLEDDATIVDIGTGSGVLAITLkCEKPDLNVIATDISLEAMNMARNNAEK-HQSQIQFLTGDALKPL 171
Cdd:COG0500   21 LERLPKGGRVLDLGCGTGRNLLAL-AARFGGRVIGIDLSPEAIALARARAAKaGLGNVEFLVADLAELD 88
PRK15001 PRK15001
23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;
103-187 5.78e-07

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


Pssm-ID: 184963 [Multi-domain]  Cd Length: 378  Bit Score: 50.03  E-value: 5.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685 103 FLQQLED--DATIVDIGTGSGVLAITLKCEKPDLNVIATDISLEAMNMARNNAEKHQSQI----QFLTGDALKPLikEGI 176
Cdd:PRK15001 220 FMQHLPEnlEGEIVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNMPEAldrcEFMINNALSGV--EPF 297

                         90
                 ....*....|.
gi 616915685 177 KLNGLISNPPY 187
Cdd:PRK15001 298 RFNAVLCNPPF 308
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
104-170 5.99e-07

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 49.79  E-value: 5.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685 104 LQQLED----DATIVDIGTGSGVLAIT-LKcekpdL---NVIATDI---SLEAmnmARNNAEKHQ--SQIQFLTGDALKP 170
Cdd:COG2264  139 LEALEKllkpGKTVLDVGCGSGILAIAaAK-----LgakRVLAVDIdpvAVEA---ARENAELNGveDRIEVVLGDLLED 210
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
100-186 1.70e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 47.59  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685 100 MLHFLQQLED--DATIVDIGTGSGVLAI---TLKCEKpdlnVIATDISLEAMNMARNNAEKHQSQIQFLTGDALKPLIKE 174
Cdd:COG2263   34 LLHLAYLRGDieGKTVLDLGCGTGMLAIgaaLLGAKK----VVGVDIDPEALEIARENAERLGVRVDFIRADVTRIPLGG 109

                         90
                 ....*....|..
gi 616915685 175 GIKLngLISNPP 186
Cdd:COG2263  110 SVDT--VVMNPP 119
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
104-154 1.96e-06

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 47.84  E-value: 1.96e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 616915685 104 LQQLED----DATIVDIGTGSGVLAIT---LKCEKpdlnVIATDISLEAMNMARNNAE 154
Cdd:PRK00517 110 LEALEKlvlpGKTVLDVGCGSGILAIAaakLGAKK----VLAVDIDPQAVEAARENAE 163
PRK14967 PRK14967
putative methyltransferase; Provisional
 111-233 8.69e-06

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 45.81  E-value: 8.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685 111 ATIVDIGTGSGVLAITlKCEKPDLNVIATDISLEAMNMARNNAEKHQSQIQFLTGDALKPLikEGIKLNGLISNPPYIDe 190
Cdd:PRK14967  38 RRVLDLCTGSGALAVA-AAAAGAGSVTAVDISRRAVRSARLNALLAGVDVDVRRGDWARAV--EFRPFDVVVSNPPYVP- 113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 616915685 191 kdmvTMSPTVTRFEPHQALFADNHGYAIYESIIEDLPHVMEKG 233
Cdd:PRK14967 114 ----APPDAPPSRGPARAWDAGPDGRAVLDRLCDAAPALLAPG 152
Methyltransf_18 pfam12847
Methyltransferase domain; Protein in this family function as methyltransferases.
 105-171 2.63e-05

Methyltransferase domain; Protein in this family function as methyltransferases.


Pssm-ID: 463730  Cd Length: 151  Bit Score: 43.19  E-value: 2.63e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616915685  105 QQLEDDATIVDIGTGSGVLAITL----KCEKpdlnVIATDISLEAMNMARNNAEKH--QSQIQFLTGDALKPL 171
Cdd:pfam12847  10 SLVPPGSRVADIGTDHAYLPIYLvkngIAPK----AIASDINEGPLEKARENIEKYglEDRIEVRLGDGLEVL 78
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 131-194 3.04e-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: 44.71  E-value: 3.04e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616915685 131 KPDLNVIATDISLEAMNMARNNAEKH--QSQIQFLTGDA--LKPLIKEGIklngLISNPPY---IDEKDMV 194
Cdd:COG0116  248 DPPLPIFGSDIDPRAIEAARENAERAgvADLIEFEQADFrdLEPPAEPGL----IITNPPYgerLGEEEEL 314
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 106-167 4.69e-05

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 42.61  E-value: 4.69e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616915685 106 QLEDDATIVDIGTGSGVLAITLkCEKPDLNVIATDISLEAMNMARNNAEKH--QSQIQFLTGDA 167
Cdd:COG2230   48 GLKPGMRVLDIGCGWGGLALYL-ARRYGVRVTGVTLSPEQLEYARERAAEAglADRVEVRLADY 110
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 97-168 4.81e-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: 4.81e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616915685  97 EEVMLHFLQQ-LEDDATIVDIGTGSGVLAITLKCEkpDLNVIATDISLEAMNMARNNAEKHqsQIQFLTGDAL 168
Cdd:COG2227   11 DRRLAALLARlLPAGGRVLDVGCGTGRLALALARR--GADVTGVDISPEALEIARERAAEL--NVDFVQGDLE 79
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
110-167 6.44e-05

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 40.96  E-value: 6.44e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 616915685 110 DATIVDIGTGSGVLAITLKCEKPDLNVIATDISLEAMNMARnnaeKHQSQIQFLTGDA 167
Cdd:COG4106    2 PRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARAR----ARLPNVRFVVADL 55
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 107-169 1.56e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 41.25  E-value: 1.56e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616915685  107 LEDDATIVDIGTGSGVLAITLKCE-KPDLNVIATDISLEAMNMARNNAEKHQSQ-IQFLTGDALK 169
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEElGPNAEVVGIDISEEAIEKARENAQKLGFDnVEFEQGDIEE 65
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 105-169 1.68e-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: 42.25  E-value: 1.68e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616915685  105 QQLEDDATIVDIGTGSGVLAIT---LKCEKpdlnVIATDISLEAMNMARNNAEKHQ--SQIQ-FLTGDALK 169
Cdd:pfam06325 157 RLVKPGESVLDVGCGSGILAIAalkLGAKK----VVGVDIDPVAVRAAKENAELNGveARLEvYLPGDLPK 223
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 94-186 3.81e-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: 3.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685  94 PETEEVM----LHFLQqLEDDATIVDIGTGSGVLAITL--KCEKpdlnVIATDISLEAMNMARNNAEKHQ-SQIQFLTGD 166
Cdd:COG2265  215 PEQAEALyaaaLEWLD-LTGGERVLDLYCGVGTFALPLarRAKK----VIGVEIVPEAVEDARENARLNGlKNVEFVAGD 289

                         90       100
                 ....*....|....*....|..
gi 616915685 167 ALKPLIKE--GIKLNGLISNPP 186
Cdd:COG2265  290 LEEVLPELlwGGRPDVVVLDPP 311
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 106-173 4.32e-04

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: 39.24  E-value: 4.32e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616915685  106 QLEDDATIVDIGTGSGVLAITLKCEKPDLNVIATDISLEAMNMARNNAEKHQ-SQIQFLTGDALKPLIK 173
Cdd:TIGR02469  16 RLRPGDVLWDIGAGTGSVTIEAARLVPNGRVYAIERNPEALDLIERNLRRFGvSNIVIVEGDAPEAPEA 84
PRK08317 PRK08317
hypothetical protein; Provisional
 106-167 7.65e-04

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 39.92  E-value: 7.65e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616915685 106 QLEDDATIVDIGTGSGVLAITLKCE-KPDLNVIATDISlEAM-NMARNNAEKHQSQIQFLTGDA 167
Cdd:PRK08317  16 AVQPGDRVLDVGCGPGNDARELARRvGPEGRVVGIDRS-EAMlALAKERAAGLGPNVEFVRGDA 78
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 114-190 1.16e-03

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 37.35  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685  114 VDIGTGSGVLAITLKCEKPDLNVIATDISLEAMNMARNN-AEKHQSQIQFLTGDALKPLIKEGIK-----LNGLISNPPY 187
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERlAALGLLNAVRVELFQLDLGELDPGSfdvvvASNVLHHLAD 80


                  ...
gi 616915685  188 IDE 190
Cdd:pfam08242  81 PRA 83
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
98-187 2.07e-03

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


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 39.16  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915685  98 EVMLHFLQQL--EDDATIVDIGTGSGVLAITLkcekpdLNVIATDISLEAM-------NMARNNAEKHQSQIQFLTGDAL 168
Cdd:COG0827  102 LLIGYLVEKFtkKEGLRILDPAVGTGNLLTTV------LNQLKKKVNAYGVevddlliRLAAVLANLQGHPVELFHQDAL 175

                         90
                 ....*....|....*....
gi 616915685 169 KPLIKEgiKLNGLISNPPY 187
Cdd:COG0827  176 QPLLID--PVDVVISDLPV 192
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 106-171 2.94e-03

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: 38.61  E-value: 2.94e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616915685 106 QLEDDATIVDIGTGSGVLAITLKCEKPDLNVIATDISLEAMNMARNNAEKHQ-SQIQFLTGDALKPL 171
Cdd:COG2242  244 ALRPGDVLWDIGAGSGSVSIEAARLAPGGRVYAIERDPERAALIRANARRFGvPNVEVVEGEAPEAL 310
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 112-169 6.18e-03

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 37.05  E-value: 6.18e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616915685 112 TIVDIGTGSGVLAITL-KCEKPDLNVIATDISLEAMNMARnnaEKHQSQ-----IQFLTGDALK 169
Cdd:PRK00216  54 KVLDLACGTGDLAIALaKAVGKTGEVVGLDFSEGMLAVGR---EKLRDLglsgnVEFVQGDAEA 114
 
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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