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Conserved domains on  [gi|7705409|ref|NP_057257|]
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MTRF1L release factor glutamine methyltransferase isoform 1 [Homo sapiens]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11458394)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor, such as Schizosaccharomyces pombe eRF1 methyltransferase catalytic subunit mtq2 that methylates eRF1 on Gln-182

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 43-336 6.71e-77

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


:

Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 237.36  E-value: 6.71e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409   43 ELVSHWTGVFEKRGIPEARESSEYIVAHVLGAKTFQSLrpALWTQPLTSQQLQCIRELSSRRLQRMPVQYILGEWDFQGL 122
Cdd:COG2890   5 ELLRWAAARLAAAGVDSARLEAELLLAHVLGLDRADLL--LHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFYGL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409  123 SLRMVPPVFIPRPETeelvewvLEEVAQRSHAVGSPGSPLILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHEN 202
Cdd:COG2890  83 EFKVDPGVLIPRPET-------EELVELALALLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRN 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409  203 AQRLRLQDRIWIIHLDMTSErswthLPW-GPMDLIVSNPPYVFHQDMEQLAPEIRSYEDPAALDGGEEGMDIITHILALA 281
Cdd:COG2890 156 AERLGLEDRVRFLQGDLFEP-----LPGdGRFDLIVSNPPYIPEDEIALLPPEVRDHEPRLALDGGEDGLDFYRRIIAQA 230

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 7705409  282 PRLLKDSGSIFLEVDPRHPELVSSWLQSRPdlyLNLVAVRRDFCGRPRFLHIRRS 336
Cdd:COG2890 231 PRLLKPGGWLLLEIGEDQGEAVRALLEAAG---FADVETHKDLAGRDRVVVARRP 282
 
Name Accession Description Interval E-value
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 43-336 6.71e-77

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 237.36  E-value: 6.71e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409   43 ELVSHWTGVFEKRGIPEARESSEYIVAHVLGAKTFQSLrpALWTQPLTSQQLQCIRELSSRRLQRMPVQYILGEWDFQGL 122
Cdd:COG2890   5 ELLRWAAARLAAAGVDSARLEAELLLAHVLGLDRADLL--LHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFYGL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409  123 SLRMVPPVFIPRPETeelvewvLEEVAQRSHAVGSPGSPLILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHEN 202
Cdd:COG2890  83 EFKVDPGVLIPRPET-------EELVELALALLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRN 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409  203 AQRLRLQDRIWIIHLDMTSErswthLPW-GPMDLIVSNPPYVFHQDMEQLAPEIRSYEDPAALDGGEEGMDIITHILALA 281
Cdd:COG2890 156 AERLGLEDRVRFLQGDLFEP-----LPGdGRFDLIVSNPPYIPEDEIALLPPEVRDHEPRLALDGGEDGLDFYRRIIAQA 230

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 7705409  282 PRLLKDSGSIFLEVDPRHPELVSSWLQSRPdlyLNLVAVRRDFCGRPRFLHIRRS 336
Cdd:COG2890 231 PRLLKPGGWLLLEIGEDQGEAVRALLEAAG---FADVETHKDLAGRDRVVVARRP 282
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 63-331 3.30e-70

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: 218.88  E-value: 3.30e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409     63 SSEYIVAHVLGaKTFQSLRpALWTQPLTSQQLQCIRELSSRRLQRMPVQYILGEWDFQGLSLRMVPPVFIPRPETEelve 142
Cdd:TIGR03534   1 DAELLLAHVLG-KDRAQLL-LHPEDELTPEELAAFDALLARRAAGEPVAYILGEREFYGLDFKVSPGVLIPRPETE---- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409    143 wvleevaqrsHAVGS-----PGSPLILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLqDRIWIIHL 217
Cdd:TIGR03534  75 ----------ELVEAalerlKKGPRVLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKNARRLGL-ENVEFLQG 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409    218 DMTSerswtHLPWGPMDLIVSNPPYVFHQDMEQLAPEIRSYEDPAALDGGEEGMDIITHILALAPRLLKDSGSIFLEVDP 297
Cdd:TIGR03534 144 DWFE-----PLPSGKFDLIVSNPPYIPEADIHLLDPEVRDFEPRLALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGY 218

                         250       260       270
                  ....*....|....*....|....*....|....
gi 7705409    298 RHPELVSSWLQSRPdlyLNLVAVRRDFCGRPRFL 331
Cdd:TIGR03534 219 DQGEAVRALFEAAG---FADVETRKDLAGKDRVV 249
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 59-335 9.22e-69

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 216.18  E-value: 9.22e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409    59 EARESSEYIVAHVLGaKTFQSLRpALWTQPLTSQQLQCIRELSSRRLQRMPVQYILGEWDFQGLSLRMVPPVFIPRPETE 138
Cdd:PRK09328  17 SPRLDAELLLAHVLG-LSRTDLL-LNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFWGLDFKVSPGVLIPRPETE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409   139 ELVEWVLEEVAQRSHAVgspgsplILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRlRLQDRIWIIHLD 218
Cdd:PRK09328  95 ELVEWALEALLLKEPLR-------VLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKH-GLGARVEFLQGD 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409   219 MtsersWTHLPWGPMDLIVSNPPYVFHQDMEQLAPEIRSYEDPAALDGGEEGMDIITHILALAPRLLKDSGSIFLEVDPR 298
Cdd:PRK09328 167 W-----FEPLPGGRFDLIVSNPPYIPEADIHLLQPEVRDHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGWLLLEIGYD 241

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 7705409   299 HPELVSSWLqsRPDLYLNlVAVRRDFCGRPRFLHIRR 335
Cdd:PRK09328 242 QGEAVRALL--AAAGFAD-VETRKDLAGRDRVVLGRR 275
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 163-293 1.68e-13

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


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 67.62  E-value: 1.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409    163 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLqDRIWIIHLDMTSErswthLPWGPMDLIVSNPPy 242
Cdd:pfam05175  35 VLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGL-ENGEVVASDVYSG-----VEDGKFDLIISNPP- 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 7705409    243 vFHQdmeqlapeirsyedpaaldGGEEGMDIITHILALAPRLLKDSGSIFL 293
Cdd:pfam05175 108 -FHA-------------------GLATTYNVAQRFIADAKRHLRPGGELWI 138
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 163-256 2.04e-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: 54.36  E-value: 2.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409  163 ILEVGCGSGAISLSLLSQlPQSRVIAVDKREAAISLThENAQRLRLQDRIWIIHLDMtseRSWTHLPWGPMDLIVSNPPY 242
Cdd:cd02440   2 VLDLGCGTGALALALASG-PGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDA---EELPPEADESFDVIISDPPL 76

                        90
                ....*....|....*
gi 7705409  243 V-FHQDMEQLAPEIR 256
Cdd:cd02440  77 HhLVEDLARFLEEAR 91
rADc smart00650
Ribosomal RNA adenine dimethylases;
152-242 6.86e-05

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 42.88  E-value: 6.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409     152 SHAVGSPGSPlILEVGCGSGAISLSLLSQLpqSRVIAV--DKREAAISlthenAQRLRLQDRIWIIHLDMTSerswTHLP 229
Cdd:smart00650   7 RAANLRPGDT-VLEIGPGKGALTEELLERA--KRVTAIeiDPRLAPRL-----REKFAAADNLTVIHGDALK----FDLP 74

                           90
                   ....*....|...
gi 7705409     230 WGPMDLIVSNPPY 242
Cdd:smart00650  75 KLQPYKVVGNLPY 87
 
Name Accession Description Interval E-value
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 43-336 6.71e-77

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 237.36  E-value: 6.71e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409   43 ELVSHWTGVFEKRGIPEARESSEYIVAHVLGAKTFQSLrpALWTQPLTSQQLQCIRELSSRRLQRMPVQYILGEWDFQGL 122
Cdd:COG2890   5 ELLRWAAARLAAAGVDSARLEAELLLAHVLGLDRADLL--LHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFYGL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409  123 SLRMVPPVFIPRPETeelvewvLEEVAQRSHAVGSPGSPLILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHEN 202
Cdd:COG2890  83 EFKVDPGVLIPRPET-------EELVELALALLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRN 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409  203 AQRLRLQDRIWIIHLDMTSErswthLPW-GPMDLIVSNPPYVFHQDMEQLAPEIRSYEDPAALDGGEEGMDIITHILALA 281
Cdd:COG2890 156 AERLGLEDRVRFLQGDLFEP-----LPGdGRFDLIVSNPPYIPEDEIALLPPEVRDHEPRLALDGGEDGLDFYRRIIAQA 230

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 7705409  282 PRLLKDSGSIFLEVDPRHPELVSSWLQSRPdlyLNLVAVRRDFCGRPRFLHIRRS 336
Cdd:COG2890 231 PRLLKPGGWLLLEIGEDQGEAVRALLEAAG---FADVETHKDLAGRDRVVVARRP 282
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 63-331 3.30e-70

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: 218.88  E-value: 3.30e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409     63 SSEYIVAHVLGaKTFQSLRpALWTQPLTSQQLQCIRELSSRRLQRMPVQYILGEWDFQGLSLRMVPPVFIPRPETEelve 142
Cdd:TIGR03534   1 DAELLLAHVLG-KDRAQLL-LHPEDELTPEELAAFDALLARRAAGEPVAYILGEREFYGLDFKVSPGVLIPRPETE---- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409    143 wvleevaqrsHAVGS-----PGSPLILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLqDRIWIIHL 217
Cdd:TIGR03534  75 ----------ELVEAalerlKKGPRVLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKNARRLGL-ENVEFLQG 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409    218 DMTSerswtHLPWGPMDLIVSNPPYVFHQDMEQLAPEIRSYEDPAALDGGEEGMDIITHILALAPRLLKDSGSIFLEVDP 297
Cdd:TIGR03534 144 DWFE-----PLPSGKFDLIVSNPPYIPEADIHLLDPEVRDFEPRLALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGY 218

                         250       260       270
                  ....*....|....*....|....*....|....
gi 7705409    298 RHPELVSSWLQSRPdlyLNLVAVRRDFCGRPRFL 331
Cdd:TIGR03534 219 DQGEAVRALFEAAG---FADVETRKDLAGKDRVV 249
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 59-335 9.22e-69

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 216.18  E-value: 9.22e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409    59 EARESSEYIVAHVLGaKTFQSLRpALWTQPLTSQQLQCIRELSSRRLQRMPVQYILGEWDFQGLSLRMVPPVFIPRPETE 138
Cdd:PRK09328  17 SPRLDAELLLAHVLG-LSRTDLL-LNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFWGLDFKVSPGVLIPRPETE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409   139 ELVEWVLEEVAQRSHAVgspgsplILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRlRLQDRIWIIHLD 218
Cdd:PRK09328  95 ELVEWALEALLLKEPLR-------VLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKH-GLGARVEFLQGD 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409   219 MtsersWTHLPWGPMDLIVSNPPYVFHQDMEQLAPEIRSYEDPAALDGGEEGMDIITHILALAPRLLKDSGSIFLEVDPR 298
Cdd:PRK09328 167 W-----FEPLPGGRFDLIVSNPPYIPEADIHLLQPEVRDHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGWLLLEIGYD 241

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 7705409   299 HPELVSSWLqsRPDLYLNlVAVRRDFCGRPRFLHIRR 335
Cdd:PRK09328 242 QGEAVRALL--AAAGFAD-VETRKDLAGRDRVVLGRR 275
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 64-295 7.68e-46

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: 157.51  E-value: 7.68e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409     64 SEYIVAHVLGAKTFQSLrpALWTQPLTSQQLQCIRELSSRRLQRMPVQYILGEWDFQGLSLRMVPPVFIPRPETeelvew 143
Cdd:TIGR00536  27 ALLLLEHDLGRERDLLL--AFLTEELTPDEKERIFRLVLRRVKGVPVAYLLGSKEFYGLEFFVNEHVLIPRPET------ 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409    144 vlEEVAQRSHAVGSPGSPL--ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLQDRIWIIHLDMts 221
Cdd:TIGR00536  99 --EELVEKALASLISQPPIlhILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQLEHRVEFIQSNL-- 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7705409    222 ersWTHLPWGPMDLIVSNPPYVFHQDMEQLAPEIRsYEDPAALDGGEEGMDIITHILALAPRLLKDSGSIFLEV 295
Cdd:TIGR00536 175 ---FEPLAGQKIDIIVSNPPYIDEEDLADLPNVVR-FEPLLALVGGDDGLNILRQIIELAPDYLKPNGFLVCEI 244
L3_gln_methyl TIGR03533
protein-(glutamine-N5) methyltransferase, ribosomal protein L3-specific; Members of this ...
 82-295 5.57e-30

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: 115.30  E-value: 5.57e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409     82 PALWTQPLTSQQLQCIRELSSRRL-QRMPVQYILGEWDFQGLSLRMVPPVFIPRpeteelvewvleevaqrshavgSPGS 160
Cdd:TIGR03533  49 EPFLDARLTPSEKERILELIERRIeERIPVAYLTNEAWFAGLEFYVDERVLIPR----------------------SPIA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409    161 PLI----------------LEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLQDRIWIIHLDMTSErs 224
Cdd:TIGR03533 107 ELIedgfapwlepepvkriLDLCTGSGCIAIACAYAFPEAEVDAVDISPDALAVAEINIERHGLEDRVTLIQSDLFAA-- 184

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7705409    225 wthLPWGPMDLIVSNPPYVFHQDMEQLAPEIRsYEDPAALDGGEEGMDIITHILALAPRLLKDSGSIFLEV 295
Cdd:TIGR03533 185 ---LPGRKYDLIVSNPPYVDAEDMADLPAEYH-HEPELALASGEDGLDLVRRILAEAADHLNENGVLVVEV 251
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
 89-333 7.18e-26

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


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 107.64  E-value: 7.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409    89 LTSQQLQCIRELSSRRLQRMPVQYILGEWDFQGLSLRMVPPVFIPRPETEELVEWVLEEVAQRSHAV-------GSPGSP 161
Cdd:PRK01544  51 LNEAEIEAFEKLLERRLKHEPIAYITGVKEFYSREFIVNKHVLIPRSDTEVLVDVVFQCHSRESGNPekkqlnpCFRGND 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409   162 L----------ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLQDRIWIIHLDmtsersW-THLPW 230
Cdd:PRK01544 131 IssncndkflnILELGTGSGCIAISLLCELPNANVIATDISLDAIEVAKSNAIKYEVTDRIQIIHSN------WfENIEK 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409   231 GPMDLIVSNPPYVFHQDMEQLAPEIRSYEDPAALDGGEEGMDIITHILALAPRLLKDSGSIFLEVDPRHPELVSswlQSR 310
Cdd:PRK01544 205 QKFDFIVSNPPYISHSEKSEMAIETINYEPSIALFAEEDGLQAYFIIAENAKQFLKPNGKIILEIGFKQEEAVT---QIF 281

                        250       260
                 ....*....|....*....|...
gi 7705409   311 PDLYLNLVAVRRDFCGRPRFLHI 333
Cdd:PRK01544 282 LDHGYNIESVYKDLQGHSRVILI 304
PrmC_rel_meth TIGR03704
putative protein-(glutamine-N5) methyltransferase, unknown substrate-specific; This protein ...
 97-298 1.54e-20

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: 89.07  E-value: 1.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409     97 IRELSSRRLQRMPVQYILGEWDFQGLSLRMVPPVFIPRPETEELVEWVLeevaqrSHAVGSPGSPLILEVGCGSGAISLS 176
Cdd:TIGR03704  30 LAAMVDRRVAGLPLEHVLGWAEFCGLRIAVDPGVFVPRRRTEFLVDEAA------ALARPRSGTLVVVDLCCGSGAVGAA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409    177 LLSQLPQSRVIAVDKREAAISLTHENaqrlrLQDRIWIIHLDMTSERSWTHLPwGPMDLIVSNPPYVFHQDMEQLAPEIR 256
Cdd:TIGR03704 104 LAAALDGIELHAADIDPAAVRCARRN-----LADAGGTVHEGDLYDALPTALR-GRVDILAANAPYVPTDAIALMPPEAR 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 7705409    257 SYEDPAALDGGEEGMDIITHILALAPRLLKDSGSIFLEVDPR 298
Cdd:TIGR03704 178 DHEPRVALDGGADGLDVLRRVAAGAPDWLAPGGHLLVETSER 219
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 163-293 3.93e-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: 81.00  E-value: 3.93e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409  163 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLQDrIWIIHLDMTSerswtHLPWGPMDLIVSNPPy 242
Cdd:COG2813  53 VLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAANGLEN-VEVLWSDGLS-----GVPDGSFDLILSNPP- 125

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 7705409  243 vFHQdmeqlapeirsyedpaaldGGEEGMDIITHILALAPRLLKDSGSIFL 293
Cdd:COG2813 126 -FHA-------------------GRAVDKEVAHALIADAARHLRPGGELWL 156
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 163-293 4.94e-18

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: 81.73  E-value: 4.94e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409  163 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLQDRIWIIHLDMtseRSWT-HLPWGPMDLIVSNPP 241
Cdd:COG4123  41 VLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDL---KEFAaELPPGSFDLVVSNPP 117

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7705409  242 YvFHQDMEQLAP-EIRS---YEDPAALDggeegmdiitHILALAPRLLKDSGSIFL 293
Cdd:COG4123 118 Y-FKAGSGRKSPdEARAiarHEDALTLE----------DLIRAAARLLKPGGRFAL 162
PRK14966 PRK14966
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; ...
 100-294 3.20e-14

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


Pssm-ID: 184930 [Multi-domain]  Cd Length: 423  Bit Score: 73.19  E-value: 3.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409   100 LSSRRLQRMPVQYILGEWDFQGLSLRMVPPVFIPRPETEELVEWVLEEVaqrshavgsPGSPLILEVGCGSGAISLSLLS 179
Cdd:PRK14966 201 LAQRRLNGEPVAYILGVREFYGRRFAVNPNVLIPRPETEHLVEAVLARL---------PENGRVWDLGTGSGAVAVTVAL 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409   180 QLPQSRVIAVDKREAAISLTHENA----QRLRLQDRIWiIHLDMTSERSWthlpwgpmDLIVSNPPYVFHQDMEQLAPEI 255
Cdd:PRK14966 272 ERPDAFVRASDISPPALETARKNAadlgARVEFAHGSW-FDTDMPSEGKW--------DIIVSNPPYIENGDKHLLQGDL 342

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 7705409   256 RsYEDPAALDGGEEGMDIITHILALAPRLLKDSGSIFLE 294
Cdd:PRK14966 343 R-FEPQIALTDFSDGLSCIRTLAQGAPDRLAEGGFLLLE 380
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 163-293 1.68e-13

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


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 67.62  E-value: 1.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409    163 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLqDRIWIIHLDMTSErswthLPWGPMDLIVSNPPy 242
Cdd:pfam05175  35 VLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGL-ENGEVVASDVYSG-----VEDGKFDLIISNPP- 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 7705409    243 vFHQdmeqlapeirsyedpaaldGGEEGMDIITHILALAPRLLKDSGSIFL 293
Cdd:pfam05175 108 -FHA-------------------GLATTYNVAQRFIADAKRHLRPGGELWI 138
PrmC_N pfam17827
PrmC N-terminal domain; This entry corresponds to the N-terminal alpha helical domain of the ...
 43-115 1.99e-13

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


Pssm-ID: 436073 [Multi-domain]  Cd Length: 71  Bit Score: 64.42  E-value: 1.99e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7705409     43 ELVSHWTGVFEKRGIPEARESSEYIVAHVLGAKTFQSLrpALWTQPLTSQQLQCIRELSSRRLQRMPVQYILG 115
Cdd:pfam17827   1 EALRWASSRLKEAGIESPRLDAELLLAHVLGLDRTDLL--LHPEEELSEEELERFEELLERRAAGEPLQYILG 71
PRK14968 PRK14968
putative methyltransferase; Provisional
 163-305 3.45e-12

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 64.15  E-value: 3.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409   163 ILEVGCGSGAISLSLLSQlpQSRVIAVDKREAAISLTHENAQRLRLQDR-IWIIHLDMTSE-RSwthlpwGPMDLIVSNP 240
Cdd:PRK14968  27 VLEVGTGSGIVAIVAAKN--GKKVVGVDINPYAVECAKCNAKLNNIRNNgVEVIRSDLFEPfRG------DKFDVILFNP 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7705409   241 PYVFHQDMEqlapEIRSYEDpAALDGGEEGMDIITHILALAPRLLKDSGSIFLevdprhpeLVSS 305
Cdd:PRK14968  99 PYLPTEEEE----EWDDWLN-YALSGGKDGREVIDRFLDEVGRYLKPGGRILL--------LQSS 150
PRK14967 PRK14967
putative methyltransferase; Provisional
 153-293 5.07e-11

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 61.61  E-value: 5.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409   153 HAVGSPGSPLILEVGCGSGAISLSLlSQLPQSRVIAVDKREAAISLTHENAQRLRLqdRIWIIHLDMTserswTHLPWGP 232
Cdd:PRK14967  30 AAEGLGPGRRVLDLCTGSGALAVAA-AAAGAGSVTAVDISRRAVRSARLNALLAGV--DVDVRRGDWA-----RAVEFRP 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7705409   233 MDLIVSNPPYVFHqdmeqlAPEIRSYEDPA-ALDGGEEGMDIITHILALAPRLLKDSGSIFL 293
Cdd:PRK14967 102 FDVVVSNPPYVPA------PPDAPPSRGPArAWDAGPDGRAVLDRLCDAAPALLAPGGSLLL 157
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 163-256 1.44e-10

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 57.19  E-value: 1.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409    163 ILEVGCGSGAISLsLLSQLPQSRVIAVDKREAAISLTHENAQRLRLqdRIWIIHLDMTSerswTHLPWGPMDLIVSNppY 242
Cdd:pfam13649   1 VLDLGCGTGRLTL-ALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAED----LPFPDGSFDLVVSS--G 71

                          90
                  ....*....|....*...
gi 7705409    243 VFH----QDMEQLAPEIR 256
Cdd:pfam13649  72 VLHhlpdPDLEAALREIA 89
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 163-210 5.49e-10

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 56.57  E-value: 5.49e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 7705409    163 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLQD 210
Cdd:TIGR02469  23 LWDIGAGTGSVTIEAARLVPNGRVYAIERNPEALDLIERNLRRFGVSN 70
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 158-303 1.74e-09

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 56.85  E-value: 1.74e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409  158 PGSPLILEVGCGSGAiSLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLqDRIWIIHLDMTserSWTHLPWGPMDLIV 237
Cdd:COG0500  25 PKGGRVLDLGCGTGR-NLLALAARFGGRVIGIDLSPEAIALARARAAKAGL-GNVEFLVADLA---ELDPLPAESFDLVV 99

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7705409  238 SNppYVFHqdmeqlapeirsYEDPAALdggeegmdiiTHILALAPRLLKDSGSIFLEVDPRHPELV 303
Cdd:COG0500 100 AF--GVLH------------HLPPEER----------EALLRELARALKPGGVLLLSASDAAAALS 141
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
163-257 1.86e-09

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 54.06  E-value: 1.86e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409  163 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRlqdriwIIHLDMtseRSWThlPWGPMDLIVSNppY 242
Cdd:COG4106   5 VLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLPNVR------FVVADL---RDLD--PPEPFDLVVSN--A 71

                        90
                ....*....|....*..
gi 7705409  243 VFH--QDMEQLAPEIRS 257
Cdd:COG4106  72 ALHwlPDHAALLARLAA 88
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 163-256 2.04e-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: 54.36  E-value: 2.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409  163 ILEVGCGSGAISLSLLSQlPQSRVIAVDKREAAISLThENAQRLRLQDRIWIIHLDMtseRSWTHLPWGPMDLIVSNPPY 242
Cdd:cd02440   2 VLDLGCGTGALALALASG-PGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDA---EELPPEADESFDVIISDPPL 76

                        90
                ....*....|....*
gi 7705409  243 V-FHQDMEQLAPEIR 256
Cdd:cd02440  77 HhLVEDLARFLEEAR 91
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 158-210 6.41e-08

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


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 53.63  E-value: 6.41e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 7705409  158 PGSpLILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLQD 210
Cdd:COG2242 247 PGD-VLWDIGAGSGSVSIEAARLAPGGRVYAIERDPERAALIRANARRFGVPN 298
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 163-309 3.89e-07

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


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 48.84  E-value: 3.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409  163 ILEVGCGSGAISLSLLSQlpQSRVIAVDKREAAISLTHENAQRLRLqdRIWIIHLDMtserswTHLPW--GPMDLIVSNp 240
Cdd:COG2226  26 VLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGL--NVEFVVGDA------EDLPFpdGSFDLVISS- 94

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7705409  241 pYVFH--QDMEQLAPEIRsyedpaaldggeegmdiithilalapRLLKDSGS-IFLEVDPRHPELVSSWLQS 309
Cdd:COG2226  95 -FVLHhlPDPERALAEIA--------------------------RVLKPGGRlVVVDFSPPDLAELEELLAE 139
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 158-217 5.57e-07

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 50.16  E-value: 5.57e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7705409  158 PGSpLILEVGCGSGAISLSLLSQL-PQSRVIAVDKREAAISLTHENAQRLRLQDRiWIIHL 217
Cdd:COG2519  91 PGA-RVLEAGTGSGALTLALARAVgPEGKVYSYERREDFAEIARKNLERFGLPDN-VELKL 149
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 163-293 3.14e-06

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


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 46.77  E-value: 3.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409    163 ILEVGCGSGAISLSLLSQlpQSRVIAVDKREAAISLTHENAQRLRLQDRIWIIHLDMTSErswthlpwGPMDLIVSNPPY 242
Cdd:TIGR00537  23 VLEIGAGTGLVAIRLKGK--GKCILTTDINPFAVKELRENAKLNNVGLDVVMTDLFKGVR--------GKFDVILFNPPY 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 7705409    243 VFHQDMEQlapeIRSYEDpAALDGGEEGMDIITHILALAPRLLKDSGSIFL 293
Cdd:TIGR00537  93 LPLEDDLR----RGDWLD-VAIDGGKDGRKVIDRFLDELPEILKEGGRVQL 138
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 163-238 7.28e-06

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 45.31  E-value: 7.28e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7705409  163 ILEVGCGSGAISLSLLSQLpQSRVIAVDKREAAISLTHENAQRLRLQDRIWIIHLDMtserswTHLPW-GPMDLIVS 238
Cdd:COG2230  55 VLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADY------RDLPAdGQFDAIVS 124
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 163-295 9.09e-06

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: 44.62  E-value: 9.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409  163 ILEVGCGSGAISLSLLSQlpQSRVIAVDKREAAIslthENAQRLRLQDRIWIIHLDMTSerswTHLPWGPMDLIVSNppY 242
Cdd:COG2227  28 VLDVGCGTGRLALALARR--GADVTGVDISPEAL----EIARERAAELNVDFVQGDLED----LPLEDGSFDLVICS--E 95

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 7705409  243 VFHqdmeqlapeirSYEDPAALdggeegmdiithiLALAPRLLKDSGSIFLEV 295
Cdd:COG2227  96 VLE-----------HLPDPAAL-------------LRELARLLKPGGLLLLST 124
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 164-256 1.20e-05

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 43.51  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409    164 LEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLQDRIW--IIHLDMTSerswthLPWGPMDLIVSNpp 241
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVRveLFQLDLGE------LDPGSFDVVVAS-- 72

                          90
                  ....*....|....*..
gi 7705409    242 YVFH--QDMEQLAPEIR 256
Cdd:pfam08242  73 NVLHhlADPRAVLRNIR 89
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 163-239 1.28e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 44.72  E-value: 1.28e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7705409    163 ILEVGCGSGAISLSLLSQL-PQSRVIAVDKREAAISLTHENAQRLRLqDRIWIIHLDMTSERswTHLPWGPMDLIVSN 239
Cdd:pfam13847   7 VLDLGCGTGHLSFELAEELgPNAEVVGIDISEEAIEKARENAQKLGF-DNVEFEQGDIEELP--ELLEDDKFDVVISN 81
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 163-215 2.01e-05

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 44.79  E-value: 2.01e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 7705409   163 ILEVGCGSGAISL--SLLSQlPQSRVIAVDKREAAISLTHENAQRLRLQDRIWII 215
Cdd:PRK00377  44 ILDIGCGTGSVTVeaSLLVG-ETGKVYAVDKDEKAINLTRRNAEKFGVLNNIVLI 97
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
163-209 2.63e-05

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


Pssm-ID: 181354  Cd Length: 187  Bit Score: 44.22  E-value: 2.63e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 7705409   163 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLQ 209
Cdd:PRK08287  35 LIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKENRQRFGCG 81
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
154-308 3.55e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 44.26  E-value: 3.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409  154 AVGSPGSpLILEVGCGSGAISLsLLSQLPQSRVIAVDKREAAISLTHENAQRLRLQDRIWIIHLDmtserSWTHLPWGPM 233
Cdd:COG4076  31 RVVKPGD-VVLDIGTGSGLLSM-LAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINAD-----ATDLDLPEKA 103

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7705409  234 DLIVSnppyvfhqdmEQLapeirsyeDPAALDggEEGMDIITHILAlapRLLKDSGSIFlevdprhPELVSSWLQ 308
Cdd:COG4076 104 DVIIS----------EML--------DTALLD--EGQVPILNHARK---RLLKPGGRII-------PERITNAAQ 148
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 164-256 4.46e-05

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 41.50  E-value: 4.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409    164 LEVGCGSGAISLSLLSQLPqsRVIAVDKREAAISLTHENAQRLRLQdriwIIHLDMtserswTHLPW--GPMDLIVSNpp 241
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMLELAREKAPREGLT----FVVGDA------EDLPFpdNSFDLVLSS-- 66

                          90
                  ....*....|....*..
gi 7705409    242 YVFH--QDMEQLAPEIR 256
Cdd:pfam08241  67 EVLHhvEDPERALREIA 83
rADc smart00650
Ribosomal RNA adenine dimethylases;
152-242 6.86e-05

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 42.88  E-value: 6.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409     152 SHAVGSPGSPlILEVGCGSGAISLSLLSQLpqSRVIAV--DKREAAISlthenAQRLRLQDRIWIIHLDMTSerswTHLP 229
Cdd:smart00650   7 RAANLRPGDT-VLEIGPGKGALTEELLERA--KRVTAIeiDPRLAPRL-----REKFAAADNLTVIHGDALK----FDLP 74

                           90
                   ....*....|...
gi 7705409     230 WGPMDLIVSNPPY 242
Cdd:smart00650  75 KLQPYKVVGNLPY 87
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
162-241 7.26e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 42.97  E-value: 7.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409  162 LILEVGCGSGAisLSLLSQLPQ-SRVIAVDKREAAISLTHENAqrLRLQDRIWIIHLDMTSERswthlPWGPMDLIVSNP 240
Cdd:COG2263  48 TVLDLGCGTGM--LAIGAALLGaKKVVGVDIDPEALEIARENA--ERLGVRVDFIRADVTRIP-----LGGSVDTVVMNP 118


                .
gi 7705409  241 P 241
Cdd:COG2263 119 P 119
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
163-239 1.65e-04

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 42.85  E-value: 1.65e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7705409  163 ILEVGCGSG--AIsLSLLsqLPQSRVIAVDKREAAISLTHENAQRLRLQDRIWIIHLDMTSErswthlpwGPMDLIVSN 239
Cdd:COG2264 152 VLDVGCGSGilAI-AAAK--LGAKRVLAVDIDPVAVEAARENAELNGVEDRIEVVLGDLLED--------GPYDLVVAN 219
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 182-242 2.67e-04

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


Pssm-ID: 439886 [Multi-domain]  Cd Length: 369  Bit Score: 42.40  E-value: 2.67e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7705409  182 PQSRVIAVDKREAAISLTHENAQRLRLQDRIWIIHLDMtserSWTHLPWGPmDLIVSNPPY 242
Cdd:COG0116 249 PPLPIFGSDIDPRAIEAARENAERAGVADLIEFEQADF----RDLEPPAEP-GLIITNPPY 304
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
163-249 4.09e-04

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


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 41.85  E-value: 4.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409   163 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLQDRiwIIHLDMTSERSwthlpwGPMDLIVSNPPy 242
Cdd:PRK09489 200 VLDVGCGAGVLSAVLARHSPKIRLTLSDVSAAALESSRATLAANGLEGE--VFASNVFSDIK------GRFDMIISNPP- 270


                 ....*..
gi 7705409   243 vFHQDME 249
Cdd:PRK09489 271 -FHDGIQ 276
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 154-291 4.13e-04

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 40.70  E-value: 4.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409  154 AVGSPGSpLILEVGCGSGAISL--SLLSqlpqSRVIAVDKREAAISLTHENAQRLRLQDrIWIIHLDMTSerswTHLPWG 231
Cdd:COG1041  22 AGAKEGD-TVLDPFCGTGTILIeaGLLG----RRVIGSDIDPKMVEGARENLEHYGYED-ADVIRGDARD----LPLADE 91

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409  232 PMDLIVSNPPYVfhqdmeqlapeirsyedPAALDGGEEGMDIITHILALAPRLLKDSGSI 291
Cdd:COG1041  92 SVDAIVTDPPYG-----------------RSSKISGEELLELYEKALEEAARVLKPGGRV 134
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 163-239 7.61e-04

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


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 40.35  E-value: 7.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409    163 ILEVGCGSGAISLSLLSQLPQSRVIAVDkreaaISLT-HENAQRLRLQDRIWiIHLDMtserswTHLPWGP--MDLIVSN 239
Cdd:TIGR02072  38 VLDIGCGTGYLTRALLKRFPQAEFIALD-----ISAGmLAQAKTKLSENVQF-ICGDA------EKLPLEDssFDLIVSN 105
PRK15001 PRK15001
23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;
163-204 1.30e-03

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


Pssm-ID: 184963 [Multi-domain]  Cd Length: 378  Bit Score: 40.40  E-value: 1.30e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 7705409   163 ILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQ 204
Cdd:PRK15001 232 IVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVE 273
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 158-242 2.53e-03

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: 38.49  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409    158 PGSPlILEVGCGSGAISL-----------SLLSQLPQSRVIAVDKREAAISLTHENAQRLRLQDRIWIIHLDMTSerswT 226
Cdd:pfam01170  28 PGDP-LLDPMCGSGTILIeaalmganiapGKFDARVRAPLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAAD----L 102

                          90
                  ....*....|....*.
gi 7705409    227 HLPWGPMDLIVSNPPY 242
Cdd:pfam01170 103 PLLEGSVDVIVTNPPY 118
Methyltransf_15 pfam09445
RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as ...
 162-242 3.39e-03

RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as Schizosaccharomyces pombe Tgs1 and Giardia lamblia Tgs2 catalyze methylation of the exocyclic N2 amine of 7-methylguanosine.


Pssm-ID: 370496  Cd Length: 165  Bit Score: 37.70  E-value: 3.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409    162 LILEVGCGSGAISLSLLSQLPqsRVIAVDKREAAISLTHENAQRLRLQDRIWIIHLDMTSERSWTHLPWGPMDLIVSNPP 241
Cdd:pfam09445   3 RILDVFCGGGGNTIQFANVFD--SVISIDINLEHLACAQHNAEVYGVSDRIWLIHGDWFELLAKLKFEKIKYDCVFASPP 80


                  .
gi 7705409    242 Y 242
Cdd:pfam09445  81 W 81
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 163-239 6.20e-03

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: 38.02  E-value: 6.20e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7705409    163 ILEVGCGSG--AISLSLLSqlpQSRVIAVDKREAAISLTHENAQRLRLQDRiwiIHLDMTSErswthLPWGPMDLIVSN 239
Cdd:pfam06325 165 VLDVGCGSGilAIAALKLG---AKKVVGVDIDPVAVRAAKENAELNGVEAR---LEVYLPGD-----LPKEKADVVVAN 232
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
163-242 8.74e-03

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 37.19  E-value: 8.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705409   163 ILEVGCGSGAISLSLLSQLPQSRVIAVDKReaaisLTHENAQRLRLQDRIWIIHLDMtserswTHLPWGPMDLIVSNPPY 242
Cdd:PRK14896  33 VLEIGPGKGALTDELAKRAKKVYAIELDPR-----LAEFLRDDEIAAGNVEIIEGDA------LKVDLPEFNKVVSNLPY 101
 
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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