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Conserved domains on  [gi|16129175|ref|NP_415730|]
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protein-(glutamine-N(5)) methyltransferase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 1-277 4.39e-141

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: 397.88  E-value: 4.39e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175     1 MEYQHWLREAISQLQASESPRRDAEILLEHVTGRGRTFILAFGETQLTDEQCQQLDALLTRRRDGEPIAHLTGVREFWSL 80
Cdd:TIGR00536   4 QEFLRWASSALSRAIARENPWLEALLLLEHDLGRERDLLLAFLTEELTPDEKERIFRLVLRRVKGVPVAYLLGSKEFYGL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175    81 PLFVSPATLIPRPDTECLVEQALARLPEQPC--RILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAI 158
Cdd:TIGR00536  84 EFFVNEHVLIPRPETEELVEKALASLISQPPilHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175   159 K-NIHILQSDWFSALAGQQFAMIVSNPPYIDEQDPHLQQGDVRFEPLTALVAADSGMADIVHIIEQSRNALVSGGFLLLE 237
Cdd:TIGR00536 164 EhRVEFIQSNLFEPLAGQKIDIIVSNPPYIDEEDLADLPNVVRFEPLLALVGGDDGLNILRQIIELAPDYLKPNGFLVCE 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 16129175   238 HG-WQQGEAVRQAFILAGYHDVETCRDYGDNERVTLGRYYQ 277
Cdd:TIGR00536 244 IGnWQQKSLKELLRIKFTWYDVENGRDLNGKERVVLGFYHS 284
 
Name Accession Description Interval E-value
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 1-277 4.39e-141

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: 397.88  E-value: 4.39e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175     1 MEYQHWLREAISQLQASESPRRDAEILLEHVTGRGRTFILAFGETQLTDEQCQQLDALLTRRRDGEPIAHLTGVREFWSL 80
Cdd:TIGR00536   4 QEFLRWASSALSRAIARENPWLEALLLLEHDLGRERDLLLAFLTEELTPDEKERIFRLVLRRVKGVPVAYLLGSKEFYGL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175    81 PLFVSPATLIPRPDTECLVEQALARLPEQPC--RILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAI 158
Cdd:TIGR00536  84 EFFVNEHVLIPRPETEELVEKALASLISQPPilHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175   159 K-NIHILQSDWFSALAGQQFAMIVSNPPYIDEQDPHLQQGDVRFEPLTALVAADSGMADIVHIIEQSRNALVSGGFLLLE 237
Cdd:TIGR00536 164 EhRVEFIQSNLFEPLAGQKIDIIVSNPPYIDEEDLADLPNVVRFEPLLALVGGDDGLNILRQIIELAPDYLKPNGFLVCE 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 16129175   238 HG-WQQGEAVRQAFILAGYHDVETCRDYGDNERVTLGRYYQ 277
Cdd:TIGR00536 244 IGnWQQKSLKELLRIKFTWYDVENGRDLNGKERVVLGFYHS 284
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 1-275 5.20e-139

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 392.22  E-value: 5.20e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175    1 MEYQHWLREAISQLQAsesPRRDAEILLEHVTGRGRTFILAFGETQLTDEQCQQLDALLTRRRDGEPIAHLTGVREFWSL 80
Cdd:PRK09328   2 MTIAEALREATARLAS---PRLDAELLLAHVLGLSRTDLLLNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFWGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175   81 PLFVSPATLIPRPDTECLVEQALARLP-EQPCRILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAIK 159
Cdd:PRK09328  79 DFKVSPGVLIPRPETEELVEWALEALLlKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGLGA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175  160 NIHILQSDWFSALAGQQFAMIVSNPPYIDEQDPHLQQGDVR-FEPLTALVAADSGMADIVHIIEQSRNALVSGGFLLLEH 238
Cdd:PRK09328 159 RVEFLQGDWFEPLPGGRFDLIVSNPPYIPEADIHLLQPEVRdHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGWLLLEI 238

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 16129175  239 GWQQGEAVRQAFILAGYHDVETCRDYGDNERVTLGRY 275
Cdd:PRK09328 239 GYDQGEAVRALLAAAGFADVETRKDLAGRDRVVLGRR 275
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 1-274 3.09e-131

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 372.95  E-value: 3.09e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175   1 MEYQHWLREAISQLQA--SESPRRDAEILLEHVTGRGRTFILAFGETQLTDEQCQQLDALLTRRRDGEPIAHLTGVREFW 78
Cdd:COG2890   1 MTIRELLRWAAARLAAagVDSARLEAELLLAHVLGLDRADLLLHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175  79 SLPLFVSPATLIPRPDTECLVEQALARLP-EQPCRILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLA 157
Cdd:COG2890  81 GLEFKVDPGVLIPRPETEELVELALALLPaGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175 158 IKN-IHILQSDWFSALAG-QQFAMIVSNPPYIDEQDPHLQQGDVR-FEPLTALVAADSGMADIVHIIEQSRNALVSGGFL 234
Cdd:COG2890 161 LEDrVRFLQGDLFEPLPGdGRFDLIVSNPPYIPEDEIALLPPEVRdHEPRLALDGGEDGLDFYRRIIAQAPRLLKPGGWL 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 16129175 235 LLEHGWQQGEAVRQAFILAGYHDVETCRDYGDNERVTLGR 274
Cdd:COG2890 241 LLEIGEDQGEAVRALLEAAGFADVETHKDLAGRDRVVVAR 280
PrmC_N pfam17827
PrmC N-terminal domain; This entry corresponds to the N-terminal alpha helical domain of the ...
 6-73 1.45e-20

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: 82.91  E-value: 1.45e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175     6 WLREAISQLQAS--ESPRRDAEILLEHVTGRGRTFILAFGETQLTDEQCQQLDALLTRRRDGEPIAHLTG 73
Cdd:pfam17827   2 ALRWASSRLKEAgiESPRLDAELLLAHVLGLDRTDLLLHPEEELSEEELERFEELLERRAAGEPLQYILG 71
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 112-237 1.81e-16

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: 73.23  E-value: 1.81e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175 112 RILDLGTGTGAIALALAsERPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHILQSDWFSAL--AGQQFAMIVSNPPYide 189
Cdd:cd02440   1 RVLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPpeADESFDVIISDPPL--- 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 16129175 190 qdphlqqgdvrfepltalvaaDSGMADIVHIIEQSRNALVSGGFLLLE 237
Cdd:cd02440  77 ---------------------HHLVEDLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 1-277 4.39e-141

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: 397.88  E-value: 4.39e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175     1 MEYQHWLREAISQLQASESPRRDAEILLEHVTGRGRTFILAFGETQLTDEQCQQLDALLTRRRDGEPIAHLTGVREFWSL 80
Cdd:TIGR00536   4 QEFLRWASSALSRAIARENPWLEALLLLEHDLGRERDLLLAFLTEELTPDEKERIFRLVLRRVKGVPVAYLLGSKEFYGL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175    81 PLFVSPATLIPRPDTECLVEQALARLPEQPC--RILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAI 158
Cdd:TIGR00536  84 EFFVNEHVLIPRPETEELVEKALASLISQPPilHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175   159 K-NIHILQSDWFSALAGQQFAMIVSNPPYIDEQDPHLQQGDVRFEPLTALVAADSGMADIVHIIEQSRNALVSGGFLLLE 237
Cdd:TIGR00536 164 EhRVEFIQSNLFEPLAGQKIDIIVSNPPYIDEEDLADLPNVVRFEPLLALVGGDDGLNILRQIIELAPDYLKPNGFLVCE 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 16129175   238 HG-WQQGEAVRQAFILAGYHDVETCRDYGDNERVTLGRYYQ 277
Cdd:TIGR00536 244 IGnWQQKSLKELLRIKFTWYDVENGRDLNGKERVVLGFYHS 284
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 1-275 5.20e-139

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 392.22  E-value: 5.20e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175    1 MEYQHWLREAISQLQAsesPRRDAEILLEHVTGRGRTFILAFGETQLTDEQCQQLDALLTRRRDGEPIAHLTGVREFWSL 80
Cdd:PRK09328   2 MTIAEALREATARLAS---PRLDAELLLAHVLGLSRTDLLLNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFWGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175   81 PLFVSPATLIPRPDTECLVEQALARLP-EQPCRILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAIK 159
Cdd:PRK09328  79 DFKVSPGVLIPRPETEELVEWALEALLlKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGLGA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175  160 NIHILQSDWFSALAGQQFAMIVSNPPYIDEQDPHLQQGDVR-FEPLTALVAADSGMADIVHIIEQSRNALVSGGFLLLEH 238
Cdd:PRK09328 159 RVEFLQGDWFEPLPGGRFDLIVSNPPYIPEADIHLLQPEVRdHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGWLLLEI 238

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 16129175  239 GWQQGEAVRQAFILAGYHDVETCRDYGDNERVTLGRY 275
Cdd:PRK09328 239 GYDQGEAVRALLAAAGFADVETRKDLAGRDRVVLGRR 275
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 1-274 3.09e-131

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 372.95  E-value: 3.09e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175   1 MEYQHWLREAISQLQA--SESPRRDAEILLEHVTGRGRTFILAFGETQLTDEQCQQLDALLTRRRDGEPIAHLTGVREFW 78
Cdd:COG2890   1 MTIRELLRWAAARLAAagVDSARLEAELLLAHVLGLDRADLLLHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175  79 SLPLFVSPATLIPRPDTECLVEQALARLP-EQPCRILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLA 157
Cdd:COG2890  81 GLEFKVDPGVLIPRPETEELVELALALLPaGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175 158 IKN-IHILQSDWFSALAG-QQFAMIVSNPPYIDEQDPHLQQGDVR-FEPLTALVAADSGMADIVHIIEQSRNALVSGGFL 234
Cdd:COG2890 161 LEDrVRFLQGDLFEPLPGdGRFDLIVSNPPYIPEDEIALLPPEVRdHEPRLALDGGEDGLDFYRRIIAQAPRLLKPGGWL 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 16129175 235 LLEHGWQQGEAVRQAFILAGYHDVETCRDYGDNERVTLGR 274
Cdd:COG2890 241 LLEIGEDQGEAVRALLEAAGFADVETHKDLAGRDRVVVAR 280
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 23-272 1.62e-130

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: 369.88  E-value: 1.62e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175    23 DAEILLEHVTGRGRTFILAFGETQLTDEQCQQLDALLTRRRDGEPIAHLTGVREFWSLPLFVSPATLIPRPDTECLVEQA 102
Cdd:TIGR03534   1 DAELLLAHVLGKDRAQLLLHPEDELTPEELAAFDALLARRAAGEPVAYILGEREFYGLDFKVSPGVLIPRPETEELVEAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175   103 LARLPEQPcRILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHILQSDWFSALAGQQFAMIVS 182
Cdd:TIGR03534  81 LERLKKGP-RVLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKNARRLGLENVEFLQGDWFEPLPSGKFDLIVS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175   183 NPPYIDEQDPHLQQGDVR-FEPLTALVAADSGMADIVHIIEQSRNALVSGGFLLLEHGWQQGEAVRQAFILAGYHDVETC 261
Cdd:TIGR03534 160 NPPYIPEADIHLLDPEVRdFEPRLALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFEAAGFADVETR 239

                         250
                  ....*....|.
gi 16129175   262 RDYGDNERVTL 272
Cdd:TIGR03534 240 KDLAGKDRVVL 250
PRK14966 PRK14966
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; ...
 1-277 1.93e-63

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


Pssm-ID: 184930 [Multi-domain]  Cd Length: 423  Bit Score: 204.93  E-value: 1.93e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175    1 MEYQHWLreAISQLqasesPRRDAEILLEHVTGRGRTFILAFGETQLTDEQCQQLDALLTRRRDGEPIAHLTGVREFWSL 80
Cdd:PRK14966 151 MTFDEWL--GLSKL-----PKNEARMLLQYASEYTRVQLLTRGGEEMPDEVRQRADRLAQRRLNGEPVAYILGVREFYGR 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175   81 PLFVSPATLIPRPDTECLVEQALARLPEQPcRILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAIKn 160
Cdd:PRK14966 224 RFAVNPNVLIPRPETEHLVEAVLARLPENG-RVWDLGTGSGAVAVTVALERPDAFVRASDISPPALETARKNAADLGAR- 301

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175  161 IHILQSDWFSA--LAGQQFAMIVSNPPYIDEQDPHLQQGDVRFEPLTALVAADSGMADIVHIIEQSRNALVSGGFLLLEH 238
Cdd:PRK14966 302 VEFAHGSWFDTdmPSEGKWDIIVSNPPYIENGDKHLLQGDLRFEPQIALTDFSDGLSCIRTLAQGAPDRLAEGGFLLLEH 381

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 16129175  239 GWQQGEAVRQAFILAGYHDVETCRDYGDNERVTLGRYYQ 277
Cdd:PRK14966 382 GFDQGAAVRGVLAENGFSGVETLPDLAGLDRVTLGKYMK 420
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
 1-276 1.34e-47

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


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 165.42  E-value: 1.34e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175    1 MEY--QHWLREAISQLQ--ASESPRRDAEILLEHVTGRGRTFILAFGETQLTDEQCQQLDALLTRRRDGEPIAHLTGVRE 76
Cdd:PRK01544   1 MQYsiKQILSDATDKLNkiGISSPQLEARILLQHVINKPIEYLLINLDEQLNEAEIEAFEKLLERRLKHEPIAYITGVKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175   77 FWSLPLFVSPATLIPRPDTECLVEQAL-------------------------ARLPEQPCRILDLGTGTGAIALALASER 131
Cdd:PRK01544  81 FYSREFIVNKHVLIPRSDTEVLVDVVFqchsresgnpekkqlnpcfrgndisSNCNDKFLNILELGTGSGCIAISLLCEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175  132 PDCEIIAVDRMPDAVSLAQRNA-QHLAIKNIHILQSDWFSALAGQQFAMIVSNPPYID-EQDPHLQQGDVRFEPLTALVA 209
Cdd:PRK01544 161 PNANVIATDISLDAIEVAKSNAiKYEVTDRIQIIHSNWFENIEKQKFDFIVSNPPYIShSEKSEMAIETINYEPSIALFA 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129175  210 ADSGMADIVHIIEQSRNALVSGGFLLLEHGWQQGEAVRQAFILAGYHDVETCRDYGDNERV------TLGRYY 276
Cdd:PRK01544 241 EEDGLQAYFIIAENAKQFLKPNGKIILEIGFKQEEAVTQIFLDHGYNIESVYKDLQGHSRVilispiNLNRSY 313
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 76-236 7.89e-25

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: 97.95  E-value: 7.89e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175  76 EFWSLP-LFvSPATLiprpD--TECLVEQALARLPEqpcRILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRN 152
Cdd:COG2813  21 TFVTLPgVF-SRDRL----DigTRLLLEHLPEPLGG---RVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARAN 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175 153 AQHLAIKNIHILQSDWFSALAGQQFAMIVSNPPYideqdpHlQQGDVRFEpltalvaadsgmadIVH-IIEQSRNALVSG 231
Cdd:COG2813  93 AAANGLENVEVLWSDGLSGVPDGSFDLILSNPPF------H-AGRAVDKE--------------VAHaLIADAARHLRPG 151


                ....*
gi 16129175 232 GFLLL 236
Cdd:COG2813 152 GELWL 156
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 102-186 1.44e-21

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: 90.20  E-value: 1.44e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175 102 ALARLPeQPCRILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAIKN-IHILQSD---WFSALAGQQF 177
Cdd:COG4123  31 AFAPVK-KGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLEDrITVIHGDlkeFAAELPPGSF 109


                ....*....
gi 16129175 178 AMIVSNPPY 186
Cdd:COG4123 110 DLVVSNPPY 118
PrmC_N pfam17827
PrmC N-terminal domain; This entry corresponds to the N-terminal alpha helical domain of the ...
 6-73 1.45e-20

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: 82.91  E-value: 1.45e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175     6 WLREAISQLQAS--ESPRRDAEILLEHVTGRGRTFILAFGETQLTDEQCQQLDALLTRRRDGEPIAHLTG 73
Cdd:pfam17827   2 ALRWASSRLKEAgiESPRLDAELLLAHVLGLDRTDLLLHPEEELSEEELERFEELLERRAAGEPLQYILG 71
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 112-236 3.58e-20

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: 84.95  E-value: 3.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175   112 RILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHILQSDWFSALAGQQFAMIVSNPPYideqd 191
Cdd:pfam05175  34 KVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGLENGEVVASDVYSGVEDGKFDLIISNPPF----- 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 16129175   192 pHlQQGDVRFepltalvaadsgmaDIVH-IIEQSRNALVSGGFLLL 236
Cdd:pfam05175 109 -H-AGLATTY--------------NVAQrFIADAKRHLRPGGELWI 138
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 112-237 1.81e-16

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: 73.23  E-value: 1.81e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175 112 RILDLGTGTGAIALALAsERPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHILQSDWFSAL--AGQQFAMIVSNPPYide 189
Cdd:cd02440   1 RVLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPpeADESFDVIISDPPL--- 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 16129175 190 qdphlqqgdvrfepltalvaaDSGMADIVHIIEQSRNALVSGGFLLLE 237
Cdd:cd02440  77 ---------------------HHLVEDLARFLEEARRLLKPGGVLVLT 103
PRK14967 PRK14967
putative methyltransferase; Provisional
 91-238 2.58e-15

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 73.16  E-value: 2.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175   91 PRPDTECLVEqALARLPEQP-CRILDLGTGTGAIALAlASERPDCEIIAVDRMPDAVSLAQRNAQhLAIKNIHILQSDWF 169
Cdd:PRK14967  18 PQEDTQLLAD-ALAAEGLGPgRRVLDLCTGSGALAVA-AAAAGAGSVTAVDISRRAVRSARLNAL-LAGVDVDVRRGDWA 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129175  170 SALAGQQFAMIVSNPPYIdeqdPHLQQGDVRFEPLTALVAADSGMADIVHIIEQSRNALVSGGFLLLEH 238
Cdd:PRK14967  95 RAVEFRPFDVVVSNPPYV----PAPPDAPPSRGPARAWDAGPDGRAVLDRLCDAAPALLAPGGSLLLVQ 159
PRK14968 PRK14968
putative methyltransferase; Provisional
 91-236 3.23e-15

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 71.85  E-value: 3.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175   91 PRPDTECLVEQALARLPEqpcRILDLGTGTGAIALALASErpDCEIIAVDRMPDAVSLAQRNAQHLAIKN--IHILQSDW 168
Cdd:PRK14968   8 PAEDSFLLAENAVDKKGD---RVLEVGTGSGIVAIVAAKN--GKKVVGVDINPYAVECAKCNAKLNNIRNngVEVIRSDL 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129175  169 FSALAGQQFAMIVSNPPYIDEQDPHLQQGDVRFepltALVAADSGMADIVHIIEQSRNALVSGGFLLL 236
Cdd:PRK14968  83 FEPFRGDKFDVILFNPPYLPTEEEEEWDDWLNY----ALSGGKDGREVIDRFLDEVGRYLKPGGRILL 146
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 111-183 5.46e-14

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 67.83  E-value: 5.46e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129175   111 CRILDLGTGTGAIALALASE-RPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHILQSDWFS---ALAGQQFAMIVSN 183
Cdd:pfam13847   5 MRVLDLGCGTGHLSFELAEElGPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEElpeLLEDDKFDVVISN 81
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 95-185 2.41e-12

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: 66.35  E-value: 2.41e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175  95 TECLVEQALARLPEQPC-RILDLGTGTGAIALALAseRPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHILQSDWFSALA 173
Cdd:COG2265 218 AEALYAAALEWLDLTGGeRVLDLYCGVGTFALPLA--RRAKKVIGVEIVPEAVEDARENARLNGLKNVEFVAGDLEEVLP 295

                        90
                ....*....|....*.
gi 16129175 174 ----GQQFAMIVSNPP 185
Cdd:COG2265 296 ellwGGRPDVVVLDPP 311
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
109-183 3.82e-12

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 61.38  E-value: 3.82e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129175 109 QPCRILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRNAQhlaikNIHILQSDWFSALAGQQFAMIVSN 183
Cdd:COG4106   1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLP-----NVRFVVADLRDLDPPEPFDLVVSN 70
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 99-183 6.93e-10

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: 55.79  E-value: 6.93e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175  99 VEQALARLPEQPCRILDLGTGTGAIALALASErpDCEIIAVDRMPDAVSLAQRNAQHLaikNIHILQSDWFS-ALAGQQF 177
Cdd:COG2227  14 LAALLARLLPAGGRVLDVGCGTGRLALALARR--GADVTGVDISPEALEIARERAAEL---NVDFVQGDLEDlPLEDGSF 88


                ....*.
gi 16129175 178 AMIVSN 183
Cdd:COG2227  89 DLVICS 94
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
102-165 7.08e-10

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


Pssm-ID: 181354  Cd Length: 187  Bit Score: 56.93  E-value: 7.08e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129175  102 ALARLPEQPCR-ILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHILQ 165
Cdd:PRK08287  23 ALSKLELHRAKhLIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKENRQRFGCGNIDIIP 87
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 100-255 8.44e-10

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: 55.77  E-value: 8.44e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175 100 EQALARLPEQPC-RILDLGTGTGAIALALAseRPDCEIIAVDRMPDAVSLAQRNAQHLAIkNIHILQSDWFS-ALAGQQF 177
Cdd:COG2226  12 EALLAALGLRPGaRVLDLGCGTGRLALALA--ERGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAEDlPFPDGSF 88

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129175 178 AMIVSNppyideqdphlqqgdvrfeplTALVAadsgMADIVHIIEQSRNALVSGG-FLLLEHGWQQGEAVRQAFILAGY 255
Cdd:COG2226  89 DLVISS---------------------FVLHH----LPDPERALAEIARVLKPGGrLVVVDFSPPDLAELEELLAEAGF 142
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 113-183 1.92e-09

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 53.72  E-value: 1.92e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129175   113 ILDLGTGTGAIALALAsERPDCEIIAVDRMPDAVSLAQRNAQHLAIkNIHILQSDWFS-ALAGQQFAMIVSN 183
Cdd:pfam13649   1 VLDLGCGTGRLTLALA-RRGGARVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDlPFPDGSFDLVVSS 70
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 101-183 2.97e-09

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 55.69  E-value: 2.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175 101 QALARLPEqPCRILDLGTGTGAIALALAsERPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHILQSDW--FSALAGQQFA 178
Cdd:COG0500  19 ALLERLPK-GGRVLDLGCGTGRNLLALA-ARFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLaeLDPLPAESFD 96


                ....*
gi 16129175 179 MIVSN 183
Cdd:COG0500  97 LVVAF 101
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 102-174 5.59e-09

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


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 56.33  E-value: 5.59e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129175 102 ALARL-PEQPCRILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHILQSDWFSALAG 174
Cdd:COG2242 239 TLAKLaLRPGDVLWDIGAGSGSVSIEAARLAPGGRVYAIERDPERAALIRANARRFGVPNVEVVEGEAPEALAD 312
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
112-234 4.53e-08

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


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 53.40  E-value: 4.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175  112 RILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRNaqhLAIKNI--HILQSDWFSALAGqQFAMIVSNPPYIDE 189
Cdd:PRK09489 199 KVLDVGCGAGVLSAVLARHSPKIRLTLSDVSAAALESSRAT---LAANGLegEVFASNVFSDIKG-RFDMIISNPPFHDG 274

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 16129175  190 QDphlqqgdvrfeplTALVAADSgmadivhIIEQSRNALVSGGFL 234
Cdd:PRK09489 275 IQ-------------TSLDAAQT-------LIRGAVRHLNSGGEL 299
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 98-182 9.04e-08

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 50.70  E-value: 9.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175  98 LVEQALARLPEQP-CRILDLGTGTGAIALALAsERPDCEIIAVDRMPDAVSLAQRNAQHLAIKN-IHILQSDWFSALAGQ 175
Cdd:COG2230  39 KLDLILRKLGLKPgMRVLDIGCGWGGLALYLA-RRYGVRVTGVTLSPEQLEYARERAAEAGLADrVEVRLADYRDLPADG 117


                ....*..
gi 16129175 176 QFAMIVS 182
Cdd:COG2230 118 QFDAIVS 124
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
112-185 9.05e-08

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 51.06  E-value: 9.05e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129175 112 RILDLGTGTG--AIALALASERpdcEIIAVDRMPDAVSLAQRNAQHLAiKNIHILQSDWFSALAGQQFAMIVSNPP 185
Cdd:COG2263  48 TVLDLGCGTGmlAIGAALLGAK---KVVGVDIDPEALEIARENAERLG-VRVDFIRADVTRIPLGGSVDTVVMNPP 119
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 111-275 9.23e-08

16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA G966 N2-methylase RsmD is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440505 [Multi-domain]  Cd Length: 183  Bit Score: 50.85  E-value: 9.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175 111 CRILDLGTGTGAIAL-AL---ASerpdcEIIAVDRMPDAVSLAQRNAQHL-AIKNIHILQSD---WFSALAGQQFAMIVS 182
Cdd:COG0742  43 ARVLDLFAGSGALGLeALsrgAA-----SVVFVEKDRKAAAVIRKNLEKLgLEDRARVIRGDalrFLKRLAGEPFDLVFL 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175 183 NPPYideqdphlQQGDVrfepltalvaadsgmADIVHIIEQSrNALVSGGFLLLEHGWQQGEAVrqafILAGYHDVETcR 262
Cdd:COG0742 118 DPPY--------AKGLL---------------EKALELLAEN-GLLAPGGLIVVEHSKREELPE----LPAGLELLKE-R 168

                       170
                ....*....|...
gi 16129175 263 DYGDNeRVTLGRY 275
Cdd:COG0742 169 KYGDT-RLSFYRR 180
PRK07402 PRK07402
precorrin-6Y C5,15-methyltransferase subunit CbiT;
105-165 3.50e-07

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


Pssm-ID: 180961  Cd Length: 196  Bit Score: 49.61  E-value: 3.50e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129175  105 RLPEQPCrILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHILQ 165
Cdd:PRK07402  37 RLEPDSV-LWDIGAGTGTIPVEAGLLCPKGRVIAIERDEEVVNLIRRNCDRFGVKNVEVIE 96
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
93-236 8.22e-07

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


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 49.56  E-value: 8.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175  93 PDTECLveqALARLPEQ-----PCRILDLGTGTGAIALALASERPDC-EIIAVDRMPDAVSLAQRNAqHLAIKNIHILQS 166
Cdd:COG0827  97 PDAIGL---LIGYLVEKftkkeGLRILDPAVGTGNLLTTVLNQLKKKvNAYGVEVDDLLIRLAAVLA-NLQGHPVELFHQ 172

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129175 167 DWFSALAGQQFAMIVSNPPYIDEQDphlQQGDVRFEpltalVAADSGMADIVH-IIEQSRNALVSGGFLLL 236
Cdd:COG0827 173 DALQPLLIDPVDVVISDLPVGYYPN---DERAKRFK-----LKADEGHSYAHHlFIEQSLNYLKPGGYLFF 235
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
97-183 1.06e-06

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 49.02  E-value: 1.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175  97 CLveQALARLPEQPCRILDLGTGTG--AIALAL--ASerpdcEIIAVDRMPDAVSLAQRNAQ--HLAiKNIHILQSDwfs 170
Cdd:COG2264 138 CL--EALEKLLKPGKTVLDVGCGSGilAIAAAKlgAK-----RVLAVDIDPVAVEAARENAElnGVE-DRIEVVLGD--- 206

                        90
                ....*....|...
gi 16129175 171 ALAGQQFAMIVSN 183
Cdd:COG2264 207 LLEDGPYDLVVAN 219
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 93-256 1.93e-06

Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal structure and biogenesis]; Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) is part of the Pathway/BioSystem: Archaeal ribosomal proteins


Pssm-ID: 444210 [Multi-domain]  Cd Length: 306  Bit Score: 48.03  E-value: 1.93e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175  93 PDTECLVEQALARLPE-----QPCRILDLGTGTGAIALALASERPDC-EIIAVDRMPDAVSLAQRNAQH---LAIKNIHI 163
Cdd:COG5459  59 PATYAAVRAALAELAEagpdfAPLTVLDVGAGPGTAAWAAADAWPSLlDATLLERSAAALALGRRLARAaanPALETAEW 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175 164 LQSDWFSALAGQQFAMIV-SNppYIDEQDPHLQQGDVRfepltALVAADSGMadiVHIIEQSRNAlvsggflllehGWQQ 242
Cdd:COG5459 139 RLADLAAALPAPPADLVVaSY--VLNELADAARAALVD-----RLWLAPDGA---LLIVEPGTPA-----------GSRR 197

                       170
                ....*....|....
gi 16129175 243 GEAVRQAFILAGYH 256
Cdd:COG5459 198 LLAARDRLIAAGAH 211
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 101-211 2.59e-06

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 46.72  E-value: 2.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175 101 QALARLpEQPCRILDLGTGTG--AIALALASeRPDCEIIAVDRMPDAVSLAQRNAQHLAI-KNIHILQSD---WFSALAG 174
Cdd:COG4122   9 YLLARL-LGAKRILEIGTGTGysTLWLARAL-PDDGRLTTIEIDPERAAIARENFARAGLaDRIRLILGDaleVLPRLAD 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 16129175 175 QQFAMIV------SNPPYIDEQDPHLQQGdvrfepltALVAAD 211
Cdd:COG4122  87 GPFDLVFidadksNYPDYLELALPLLRPG--------GLIVAD 121
Methyltransf_4 pfam02390
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ...
 113-193 3.64e-06

Putative methyltransferase; This is a family of putative methyltransferases. The aligned region contains the GXGXG S-AdoMet binding site suggesting a putative methyltransferase activity.


Pssm-ID: 367068  Cd Length: 173  Bit Score: 46.13  E-value: 3.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175   113 ILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHILQSD----WFSALAGQQFAMIVSNPPyid 188
Cdd:pfam02390   5 FLEIGCGMGGFLVAMAKANPDKNFIGIEIRVPGVAKALKKIDALGLQNLRILCGNaldvLPNYFPPGSLQKIFINFP--- 81


                  ....*
gi 16129175   189 eqDPH 193
Cdd:pfam02390  82 --DPW 84
TIGR00091 TIGR00091
tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent ...
 113-167 2.27e-05

tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent methyltransferase is found in a single copy in most Bacteria. It is also found, with a short amino-terminal extension in eukaryotes. Its function is unknown. In E. coli, this protein flanks the DNA repair protein MutY, also called micA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 161703  Cd Length: 194  Bit Score: 44.27  E-value: 2.27e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16129175   113 ILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHILQSD 167
Cdd:TIGR00091  20 HLEIGCGKGRFLIDMAKQNPDKNFLGIEIHTPIVLAANNKANKLGLKNLHVLCGD 74
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 124-186 2.99e-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: 2.99e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129175 124 ALALASERPDCEIIAVDRMPDAVSLAQRNAQ--HLAiKNIHILQSDWFSALAGQQFAMIVSNPPY 186
Cdd:COG0116 241 AEARIKRDPPLPIFGSDIDPRAIEAARENAEraGVA-DLIEFEQADFRDLEPPAEPGLIITNPPY 304
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 109-168 3.84e-05

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


Pssm-ID: 313513  Cd Length: 172  Bit Score: 43.09  E-value: 3.84e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129175   109 QPCRILDLGTGTGAIALALASERPDCEIIAVDRmPDAVSLAQRNAQHLAIKN-IHILQSDW 168
Cdd:pfam10294  46 SGLNVLELGSGTGLVGIAVALLLPGASVTITDL-EEALELLKKNIELNALSSkVVVKVLDW 105
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 46-182 4.23e-05

16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ribosomal structure and biogenesis]; 16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440126  Cd Length: 211  Bit Score: 43.60  E-value: 4.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175  46 QLTDEQCQQLDAL------------LTRRRDgepiahltgVREFWSLPLFvspatliprpdtECLveQALARLPEQPCRI 113
Cdd:COG0357  15 ELSEEQLEQLEAYlelllkwnkkinLTAIRD---------PEELWERHIL------------DSL--ALLPLLPKEGARV 71

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129175 114 LDLGTGTG--AIALALAseRPDCEIIAVDrmpdavSLA------QRNAQHLAIKNIHILQSDWFSALAGQQFAMIVS 182
Cdd:COG0357  72 LDVGSGAGfpGIPLAIA--RPDLQVTLVD------SLGkkiaflREVVRELGLKNVTVVHGRAEELAPREKFDVVTA 140
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
98-196 5.07e-05

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 43.06  E-value: 5.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175  98 LVEQALARLPEQP-CRILDLGTGTGAIALALAsERPDcEIIAVDRMPDAVSLAQRNAQHlaiknIHILQSDwFSALA--G 174
Cdd:COG4976  34 LAEELLARLPPGPfGRVLDLGCGTGLLGEALR-PRGY-RLTGVDLSEEMLAKAREKGVY-----DRLLVAD-LADLAepD 105

                        90       100
                ....*....|....*....|....
gi 16129175 175 QQFAMIVSN--PPYIDEQDPHLQQ 196
Cdd:COG4976 106 GRFDLIVAAdvLTYLGDLAAVFAG 129
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
97-154 9.54e-05

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 42.83  E-value: 9.54e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129175   97 CLveQALARLPEQPCRILDLGTGTG--AIALAL--ASerpdcEIIAVDRMPDAVSLAQRNAQ 154
Cdd:PRK00517 109 CL--EALEKLVLPGKTVLDVGCGSGilAIAAAKlgAK-----KVLAVDIDPQAVEAARENAE 163
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
109-192 1.50e-04

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 41.46  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175   109 QPCRILDLGTGTGAIALALASeRPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHILQSDW--FSALAGQ--QFAMIVSNP 184
Cdd:pfam03602  41 EGARVLDLFAGSGALGLEALS-RGAKRVTLVEKDKRAVQILKENLQLLGLPGAVLVMDALlaLLRLAGKgpVFDIVFLDP 119


                  ....*...
gi 16129175   185 PYIDEQDP 192
Cdd:pfam03602 120 PYAKGLIE 127
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
90-167 1.60e-04

protein-L-isoaspartate(D-aspartate) O-methyltransferase;


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 41.73  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175   90 IPRPDTECLVEQALARLPEQpcRILDLGTGTG---AIaLALASERpdceIIAVDRMPDAVSLAQRNAQHLAIKNIHILQS 166
Cdd:PRK00312  61 ISQPYMVARMTELLELKPGD--RVLEIGTGSGyqaAV-LAHLVRR----VFSVERIKTLQWEAKRRLKQLGLHNVSVRHG 133


                 .
gi 16129175  167 D 167
Cdd:PRK00312 134 D 134
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 103-183 4.56e-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: 40.73  E-value: 4.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175   103 LARLPE----QPCRILDLGTGTGAIALALASERPDCEIIAVDRMPdaVSLAQrnAQHLAIKNIHILQSDWFSA-LAGQQF 177
Cdd:TIGR02072  24 LALLKEkgifIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISA--GMLAQ--AKTKLSENVQFICGDAEKLpLEDSSF 99


                  ....*.
gi 16129175   178 AMIVSN 183
Cdd:TIGR02072 100 DLIVSN 105
PRK06202 PRK06202
hypothetical protein; Provisional
 100-155 5.90e-04

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 40.37  E-value: 5.90e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175  100 EQALARLPEQPCRILDLGTGTG--AIALALASERP--DCEIIAVDRMPDAVSLAQRNAQH 155
Cdd:PRK06202  51 LLRPALSADRPLTLLDIGCGGGdlAIDLARWARRDglRLEVTAIDPDPRAVAFARANPRR 110
trmB PRK00121
tRNA (guanine-N(7)-)-methyltransferase; Reviewed
 113-167 1.07e-03

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


Pssm-ID: 234649  Cd Length: 202  Bit Score: 39.37  E-value: 1.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16129175  113 ILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHILQSD 167
Cdd:PRK00121  44 HLEIGFGKGEFLVEMAKANPDINFIGIEVHEPGVGKALKKIEEEGLTNLRLLCGD 98
PRK08317 PRK08317
hypothetical protein; Provisional
 92-158 1.08e-03

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 39.53  E-value: 1.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175   92 RPDTECLVEQALARLPEQPC-RILDLGTGTGAIALALASE-RPDCEIIAVDRMPDAVSLAQ-RNAQHLAI 158
Cdd:PRK08317   1 LPDFRRYRARTFELLAVQPGdRVLDVGCGPGNDARELARRvGPEGRVVGIDRSEAMLALAKeRAAGLGPN 70
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 114-165 1.27e-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: 1.27e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 16129175   114 LDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHILQ 165
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVRVE 52
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 114-162 1.86e-03

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 36.87  E-value: 1.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 16129175   114 LDLGTGTGAIALALAseRPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIH 162
Cdd:pfam08241   1 LDVGCGTGLLTELLA--RLGARVTGVDISPEMLELAREKAPREGLTFVV 47
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 112-167 2.21e-03

tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442010 [Multi-domain]  Cd Length: 333  Bit Score: 39.07  E-value: 2.21e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16129175 112 RILDLGTGTGAIALALASERPdCEIIAVDRMPDAVSLAQRNAQ--HLAiKNIHILQSD 167
Cdd:COG2520 183 RVLDMFAGVGPFSIPIAKRSG-AKVVAIDINPDAVEYLKENIRlnKVE-DRVTPILGD 238
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 112-186 2.77e-03

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


Pssm-ID: 439801 [Multi-domain]  Cd Length: 270  Bit Score: 38.57  E-value: 2.77e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129175 112 RILDLGTGTGAIALALAsERPDcEIIAVDRMPDAVSLAQRNAQHLaiKNIHILQSD----WFSALAGQQFAMIVSNPPY 186
Cdd:COG0030  40 TVLEIGPGLGALTRALL-ERAA-RVTAVEIDRRLAAILRETFAAY--PNLTVIEGDalkvDLPALAAGEPLKVVGNLPY 114
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 97-154 3.30e-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: 38.40  E-value: 3.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129175    97 CLveQALARLPEQPCRILDLGTGTG--AIALAL--ASerpdcEIIAVDRMPDAVSLAQRNAQ 154
Cdd:pfam06325 151 CL--EALERLVKPGESVLDVGCGSGilAIAALKlgAK-----KVVGVDIDPVAVRAAKENAE 205
PRK14904 PRK14904
16S rRNA methyltransferase B; Provisional
 101-185 9.05e-03

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237858 [Multi-domain]  Cd Length: 445  Bit Score: 37.35  E-value: 9.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175  101 QALARL---PEQPCRILDLGTGTGAIALALASERPDC-EIIAVDRMPDAVSLAQRNAQHLAIKNIHILQSDWFSALAGQQ 176
Cdd:PRK14904 239 QALACLllnPQPGSTVLDLCAAPGGKSTFMAELMQNRgQITAVDRYPQKLEKIRSHASALGITIIETIEGDARSFSPEEQ 318


                 ....*....
gi 16129175  177 FAMIVSNPP 185
Cdd:PRK14904 319 PDAILLDAP 327
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
91-240 9.79e-03

Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 36.70  E-value: 9.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175  91 PRPDTECLVEQALarlPEQPCRILDLGTGTGAIALALA--------SERPDCEIIAVDRMPDAVSLAQRNaqhLAIKNI- 161
Cdd:COG0286  28 PREVVRLMVELLD---PKPGETVYDPACGSGGFLVEAAeylkehggDERKKLSLYGQEINPTTYRLAKMN---LLLHGIg 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129175 162 --HILQSDWFSALAGQ--QFAMIVSNPPYIDEQDPHLQQGDV--RFEPLTALVaADSGMADIVHIIEQ----SRNALV-S 230
Cdd:COG0286 102 dpNIELGDTLSNDGDEleKFDVVLANPPFGGKWKKEELKDDLlgRFGYGLPPK-SNADLLFLQHILSLlkpgGRAAVVlP 180

                       170       180
                ....*....|....*....|.
gi 16129175 231 GGFL-----------LLEHGW 240
Cdd:COG0286 181 DGVLfrgaekeirkkLLENDL 201
 
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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