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Conserved domains on  [gi|2421839396|dbj|BDV32404|]
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methyltransferase [Microbacterium terricola]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 106779)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RsmC super family cl34491
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 172-298 1.99e-23

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


The actual alignment was detected with superfamily member COG2813:

Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 97.57  E-value: 1.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 172 QLPTP-AGRALDLGSGCGIQALRVRRAADG--VVATDISARAVWFTRLNARLNGVDGIETRGGSLFEPVAGEQFDRIVSN 248
Cdd:COG2813    44 HLPEPlGGRVLDLGCGYGVIGLALAKRNPEarVTLVDVNARAVELARANAAANGLENVEVLWSDGLSGVPDGSFDLILSN 123

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2421839396 249 PPFvitpraadvpayeyRDGGMVGDDLVAAFVTGVGEHLAPGGVAQLLGN 298
Cdd:COG2813   124 PPF--------------HAGRAVDKEVAHALIADAARHLRPGGELWLVAN 159
PksD super family cl43841
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 66-526 1.59e-08

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


The actual alignment was detected with superfamily member COG3321:

Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 57.57  E-value: 1.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396   66 RALGDRHDPLAVLARLFVLGMPQSAAAVDSALPR----------------LGADGLVRLALAERDGSTVRPTALVRPQSF 129
Cdd:COG3321    825 RGEDELAQLLTALAQLWVAGVPVDWSALYPGRGRrrvplptypfqredaaAALLAAALAAALAAAAALGALLLAALAAAL 904

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396  130 TDSHGDGRWWIASDLDEAALQGPLREDHVLGVGGASLTLAGLQLPTPAGRALDLGSGCGIQALRVRRAADGVVATDISAR 209
Cdd:COG3321    905 AAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAA 984

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396  210 AVWFTRLNARLNGVDGIETRGGSLFEPVAGEQFDRIVSNPPFVITPRAADVPAYEYRDGGMVGDDLVAAFVTGVGEHLAP 289
Cdd:COG3321    985 AAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALA 1064

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396  290 GGVAQLLGNWETRAGRDGLDRVRDWVEASPVPLDAWVVEREALDPLSYAELWIRDGGTLPGASGFARLIDAWLDDFTARD 369
Cdd:COG3321   1065 LAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAA 1144

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396  370 VSEVGFGYLLLRRPLAGEPTLRRFERIPHALEGRATLGGHLADALAMHDLLVDVDDAELTASVLLVAPDVTEARHHMPGA 449
Cdd:COG3321   1145 AAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALL 1224

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2421839396  450 EAPTVIELRQGGGYGRSLSVDPALAALVGACDADLPLGSLIDAIAQLLEVDAVELRADLLPRVRELLFTGFLSIARG 526
Cdd:COG3321   1225 AAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAAL 1301
 
Name Accession Description Interval E-value
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 172-298 1.99e-23

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: 97.57  E-value: 1.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 172 QLPTP-AGRALDLGSGCGIQALRVRRAADG--VVATDISARAVWFTRLNARLNGVDGIETRGGSLFEPVAGEQFDRIVSN 248
Cdd:COG2813    44 HLPEPlGGRVLDLGCGYGVIGLALAKRNPEarVTLVDVNARAVELARANAAANGLENVEVLWSDGLSGVPDGSFDLILSN 123

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2421839396 249 PPFvitpraadvpayeyRDGGMVGDDLVAAFVTGVGEHLAPGGVAQLLGN 298
Cdd:COG2813   124 PPF--------------HAGRAVDKEVAHALIADAARHLRPGGELWLVAN 159
PRK14968 PRK14968
putative methyltransferase; Provisional
 168-296 7.34e-23

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 95.74  E-value: 7.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 168 LAGLQLPTPAGRALDLGSGCGIQALRVRRAADGVVATDISARAVWFTRLNARLNGVD--GIETRGGSLFEPVAGEQFDRI 245
Cdd:PRK14968   15 LAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRnnGVEVIRSDLFEPFRGDKFDVI 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2421839396 246 VSNPPFVITPRAADVPAY-EYR-DGGMVGDDLVAAFVTGVGEHLAPGGVAQLL 296
Cdd:PRK14968   95 LFNPPYLPTEEEEEWDDWlNYAlSGGKDGREVIDRFLDEVGRYLKPGGRILLL 147
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 173-298 1.59e-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: 88.80  E-value: 1.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 173 LPTP-AGRALDLGSGCGIQALRVRRAADG--VVATDISARAVWFTRLNARLNGVDGIETRGGSLFEPVAGEQFDRIVSNP 249
Cdd:pfam05175  27 LPKDlSGKVLDLGCGAGVLGAALAKESPDaeLTMVDINARALESARENLAANGLENGEVVASDVYSGVEDGKFDLIISNP 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2421839396 250 PFvitpraadvpayeyRDGGMVGDDLVAAFVTGVGEHLAPGGVAQLLGN 298
Cdd:pfam05175 107 PF--------------HAGLATTYNVAQRFIADAKRHLRPGGELWIVAN 141
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 169-292 2.86e-17

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: 81.36  E-value: 2.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 169 AGLQLPTPAGRALDLGSGCGIQALRVRRAADG--VVATDISARAVWFTRLNARLNGVDGIETRGGSLFEPVAGEQFDRIV 246
Cdd:TIGR03534  79 AALERLKKGPRVLDLGTGSGAIALALAKERPDarVTAVDISPEALAVARKNARRLGLENVEFLQGDWFEPLPSGKFDLIV 158

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2421839396 247 SNPPFV----ITPRAADVPAYEYR---DGGMVGDDLVAAFVTGVGEHLAPGGV 292
Cdd:TIGR03534 159 SNPPYIpeadIHLLDPEVRDFEPRlalFGGEDGLDFYRRIIAQAPRLLKPGGW 211
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 179-292 2.05e-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: 55.13  E-value: 2.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 179 RALDLGSGCGIQALRVRRAADG-VVATDISARAVWFTRLNARLNGVDGIETRGGSLFEPV--AGEQFDRIVSNPPFvitp 255
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGArVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPpeADESFDVIISDPPL---- 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2421839396 256 raadvpayeyrdggMVGDDLVAAFVTGVGEHLAPGGV 292
Cdd:cd02440    77 --------------HHLVEDLARFLEEARRLLKPGGV 99
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 66-526 1.59e-08

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 57.57  E-value: 1.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396   66 RALGDRHDPLAVLARLFVLGMPQSAAAVDSALPR----------------LGADGLVRLALAERDGSTVRPTALVRPQSF 129
Cdd:COG3321    825 RGEDELAQLLTALAQLWVAGVPVDWSALYPGRGRrrvplptypfqredaaAALLAAALAAALAAAAALGALLLAALAAAL 904

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396  130 TDSHGDGRWWIASDLDEAALQGPLREDHVLGVGGASLTLAGLQLPTPAGRALDLGSGCGIQALRVRRAADGVVATDISAR 209
Cdd:COG3321    905 AAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAA 984

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396  210 AVWFTRLNARLNGVDGIETRGGSLFEPVAGEQFDRIVSNPPFVITPRAADVPAYEYRDGGMVGDDLVAAFVTGVGEHLAP 289
Cdd:COG3321    985 AAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALA 1064

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396  290 GGVAQLLGNWETRAGRDGLDRVRDWVEASPVPLDAWVVEREALDPLSYAELWIRDGGTLPGASGFARLIDAWLDDFTARD 369
Cdd:COG3321   1065 LAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAA 1144

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396  370 VSEVGFGYLLLRRPLAGEPTLRRFERIPHALEGRATLGGHLADALAMHDLLVDVDDAELTASVLLVAPDVTEARHHMPGA 449
Cdd:COG3321   1145 AAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALL 1224

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2421839396  450 EAPTVIELRQGGGYGRSLSVDPALAALVGACDADLPLGSLIDAIAQLLEVDAVELRADLLPRVRELLFTGFLSIARG 526
Cdd:COG3321   1225 AAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAAL 1301
 
Name Accession Description Interval E-value
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 172-298 1.99e-23

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: 97.57  E-value: 1.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 172 QLPTP-AGRALDLGSGCGIQALRVRRAADG--VVATDISARAVWFTRLNARLNGVDGIETRGGSLFEPVAGEQFDRIVSN 248
Cdd:COG2813    44 HLPEPlGGRVLDLGCGYGVIGLALAKRNPEarVTLVDVNARAVELARANAAANGLENVEVLWSDGLSGVPDGSFDLILSN 123

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2421839396 249 PPFvitpraadvpayeyRDGGMVGDDLVAAFVTGVGEHLAPGGVAQLLGN 298
Cdd:COG2813   124 PPF--------------HAGRAVDKEVAHALIADAARHLRPGGELWLVAN 159
PRK14968 PRK14968
putative methyltransferase; Provisional
 168-296 7.34e-23

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 95.74  E-value: 7.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 168 LAGLQLPTPAGRALDLGSGCGIQALRVRRAADGVVATDISARAVWFTRLNARLNGVD--GIETRGGSLFEPVAGEQFDRI 245
Cdd:PRK14968   15 LAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRnnGVEVIRSDLFEPFRGDKFDVI 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2421839396 246 VSNPPFVITPRAADVPAY-EYR-DGGMVGDDLVAAFVTGVGEHLAPGGVAQLL 296
Cdd:PRK14968   95 LFNPPYLPTEEEEEWDDWlNYAlSGGKDGREVIDRFLDEVGRYLKPGGRILLL 147
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 173-298 1.59e-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: 88.80  E-value: 1.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 173 LPTP-AGRALDLGSGCGIQALRVRRAADG--VVATDISARAVWFTRLNARLNGVDGIETRGGSLFEPVAGEQFDRIVSNP 249
Cdd:pfam05175  27 LPKDlSGKVLDLGCGAGVLGAALAKESPDaeLTMVDINARALESARENLAANGLENGEVVASDVYSGVEDGKFDLIISNP 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2421839396 250 PFvitpraadvpayeyRDGGMVGDDLVAAFVTGVGEHLAPGGVAQLLGN 298
Cdd:pfam05175 107 PF--------------HAGLATTYNVAQRFIADAKRHLRPGGELWIVAN 141
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 169-292 2.86e-17

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: 81.36  E-value: 2.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 169 AGLQLPTPAGRALDLGSGCGIQALRVRRAADG--VVATDISARAVWFTRLNARLNGVDGIETRGGSLFEPVAGEQFDRIV 246
Cdd:TIGR03534  79 AALERLKKGPRVLDLGTGSGAIALALAKERPDarVTAVDISPEALAVARKNARRLGLENVEFLQGDWFEPLPSGKFDLIV 158

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2421839396 247 SNPPFV----ITPRAADVPAYEYR---DGGMVGDDLVAAFVTGVGEHLAPGGV 292
Cdd:TIGR03534 159 SNPPYIpeadIHLLDPEVRDFEPRlalFGGEDGLDFYRRIIAQAPRLLKPGGW 211
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 179-296 5.31e-16

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: 76.05  E-value: 5.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 179 RALDLGSGCGIQALRVRRAADGVVATDISARAVWFTRLNARLNGVdGIETRGGSLFEPVAGeQFDRIVSNPPFVITP--- 255
Cdd:TIGR00537  22 DVLEIGAGTGLVAIRLKGKGKCILTTDINPFAVKELRENAKLNNV-GLDVVMTDLFKGVRG-KFDVILFNPPYLPLEddl 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2421839396 256 RAADVPAYEYrDGGMVGDDLVAAFVTGVGEHLAPGGVAQLL 296
Cdd:TIGR00537 100 RRGDWLDVAI-DGGKDGRKVIDRFLDELPEILKEGGRVQLI 139
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 171-311 9.55e-16

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 77.51  E-value: 9.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 171 LQLPTPAGRALDLGSGCGIQALRVRRAADG--VVATDISARAVWFTRLNARLNGVDGIETRGGSLFEPVAGEQFDRIVSN 248
Cdd:PRK09328  103 ALLLKEPLRVLDLGTGSGAIALALAKERPDaeVTAVDISPEALAVARRNAKHGLGARVEFLQGDWFEPLPGGRFDLIVSN 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 249 PPFV----ITPRAADVPAYEYR---DGGMVGDDLVAAFVTGVGEHLAPGG-------------VAQLL---GNWETRAGR 305
Cdd:PRK09328  183 PPYIpeadIHLLQPEVRDHEPHlalFGGEDGLDFYRRIIEQAPRYLKPGGwllleigydqgeaVRALLaaaGFADVETRK 262


                  ....*...
gi 2421839396 306 D--GLDRV 311
Cdd:PRK09328  263 DlaGRDRV 270
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 174-292 5.05e-14

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 72.49  E-value: 5.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 174 PTPAGRALDL--GSGC-GIQALRVRRAADgVVATDISARAVWFTRLNARLNGVDG-IETRGGSLFEPVAG-EQFDRIVSN 248
Cdd:COG2890   110 AGAPPRVLDLgtGSGAiALALAKERPDAR-VTAVDISPDALAVARRNAERLGLEDrVRFLQGDLFEPLPGdGRFDLIVSN 188

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2421839396 249 PPFV----ITPRAADVPAYEYR---DGGMVGDDLVAAFVTGVGEHLAPGGV 292
Cdd:COG2890   189 PPYIpedeIALLPPEVRDHEPRlalDGGEDGLDFYRRIIAQAPRLLKPGGW 239
PRK14967 PRK14967
putative methyltransferase; Provisional
 176-295 4.04e-13

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 68.54  E-value: 4.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 176 PAGRALDLGSGCGIQALRVRRA-ADGVVATDISARAVWFTRLNARLNGVDgIETRGGSLFEPVAGEQFDRIVSNPPFVIT 254
Cdd:PRK14967   36 PGRRVLDLCTGSGALAVAAAAAgAGSVTAVDISRRAVRSARLNALLAGVD-VDVRRGDWARAVEFRPFDVVVSNPPYVPA 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2421839396 255 P---RAADVPAYEY---RDGGMVGDDLVAAfvtgVGEHLAPGGVAQL 295
Cdd:PRK14967  115 PpdaPPSRGPARAWdagPDGRAVLDRLCDA----APALLAPGGSLLL 157
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 168-317 4.38e-10

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: 60.83  E-value: 4.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 168 LAGLQLPTPAGRALDL--GSGCGIQALRVRRAADGVVATDISARAVWFTRLNARLNGV-DGIETRGGSLFEPVAGEQFDR 244
Cdd:TIGR00536 106 LASLISQPPILHILDLgtGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQLeHRVEFIQSNLFEPLAGQKIDI 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 245 IVSNPPFVITPRAADVPAyEYR-------DGGMVGDDLVAAFVTGVGEHLAPGGVAQL-LGNWETRAGRDGLDRVRDWVE 316
Cdd:TIGR00536 186 IVSNPPYIDEEDLADLPN-VVRfepllalVGGDDGLNILRQIIELAPDYLKPNGFLVCeIGNWQQKSLKELLRIKFTWYD 264


                  .
gi 2421839396 317 A 317
Cdd:TIGR00536 265 V 265
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 164-293 1.77e-09

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 57.97  E-value: 1.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 164 ASLTLAG--LQLPTPAG-RALDLGSGCGIQALRVRRA-ADGVVATDISARAVWFTRLNARLNGVDgIETRGGSLFEPVAG 239
Cdd:COG3897    55 SGQALARylLDHPEVAGkRVLELGCGLGLVGIAAAKAgAADVTATDYDPEALAALRLNAALNGVA-ITTRLGDWRDPPAA 133

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2421839396 240 EQFDRIVsnppfvitprAADVpAYEyrdggmvgDDLVAAFVTGVGEHLAPGGVA 293
Cdd:COG3897   134 GGFDLIL----------GGDV-LYE--------RDLAEPLLPFLDRLAAPGGEV 168
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 179-292 2.05e-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: 55.13  E-value: 2.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 179 RALDLGSGCGIQALRVRRAADG-VVATDISARAVWFTRLNARLNGVDGIETRGGSLFEPV--AGEQFDRIVSNPPFvitp 255
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGArVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPpeADESFDVIISDPPL---- 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2421839396 256 raadvpayeyrdggMVGDDLVAAFVTGVGEHLAPGGV 292
Cdd:cd02440    77 --------------HHLVEDLARFLEEARRLLKPGGV 99
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 66-526 1.59e-08

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 57.57  E-value: 1.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396   66 RALGDRHDPLAVLARLFVLGMPQSAAAVDSALPR----------------LGADGLVRLALAERDGSTVRPTALVRPQSF 129
Cdd:COG3321    825 RGEDELAQLLTALAQLWVAGVPVDWSALYPGRGRrrvplptypfqredaaAALLAAALAAALAAAAALGALLLAALAAAL 904

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396  130 TDSHGDGRWWIASDLDEAALQGPLREDHVLGVGGASLTLAGLQLPTPAGRALDLGSGCGIQALRVRRAADGVVATDISAR 209
Cdd:COG3321    905 AAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAA 984

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396  210 AVWFTRLNARLNGVDGIETRGGSLFEPVAGEQFDRIVSNPPFVITPRAADVPAYEYRDGGMVGDDLVAAFVTGVGEHLAP 289
Cdd:COG3321    985 AAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALA 1064

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396  290 GGVAQLLGNWETRAGRDGLDRVRDWVEASPVPLDAWVVEREALDPLSYAELWIRDGGTLPGASGFARLIDAWLDDFTARD 369
Cdd:COG3321   1065 LAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAA 1144

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396  370 VSEVGFGYLLLRRPLAGEPTLRRFERIPHALEGRATLGGHLADALAMHDLLVDVDDAELTASVLLVAPDVTEARHHMPGA 449
Cdd:COG3321   1145 AAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALL 1224

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2421839396  450 EAPTVIELRQGGGYGRSLSVDPALAALVGACDADLPLGSLIDAIAQLLEVDAVELRADLLPRVRELLFTGFLSIARG 526
Cdd:COG3321   1225 AAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAAL 1301
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 166-293 2.66e-08

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 53.01  E-value: 2.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 166 LTLAGLQLPtPAGRALDLGSGCGIQALRVRRAADG-VVATDISARAVWFTRLNARLNGV-DGIETRGGSLFEPVAGEQFD 243
Cdd:COG2230    42 LILRKLGLK-PGMRVLDIGCGWGGLALYLARRYGVrVTGVTLSPEQLEYARERAAEAGLaDRVEVRLADYRDLPADGQFD 120

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2421839396 244 RIVSnppfvitpraadVPAYEYrdggmVGDDLVAAFVTGVGEHLAPGGVA 293
Cdd:COG2230   121 AIVS------------IGMFEH-----VGPENYPAYFAKVARLLKPGGRL 153
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 176-291 2.77e-08

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 54.77  E-value: 2.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 176 PAGRALDLGSGCGIQALRV--RRAADGVVATDISARAVWFTRLNARLNGVDG-IETRGGSLFEPVA---GEQFDRIVSNP 249
Cdd:COG4123    37 KGGRVLDLGTGTGVIALMLaqRSPGARITGVEIQPEAAELARRNVALNGLEDrITVIHGDLKEFAAelpPGSFDLVVSNP 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2421839396 250 PFvITPRAADVPAYEYRDGGMVGDDL-VAAFVTGVGEHLAPGG 291
Cdd:COG4123   117 PY-FKAGSGRKSPDEARAIARHEDALtLEDLIRAAARLLKPGG 158
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 174-250 1.91e-07

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: 53.26  E-value: 1.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 174 PTPAGRALDLGSGCGIQALRVRRAADGVVATDISARAVWFTRLNARLNGVDGIETRGGSLFEPVA----GEQFDRIVSNP 249
Cdd:COG2265   231 LTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGLKNVEFVAGDLEEVLPellwGGRPDVVVLDP 310


                  .
gi 2421839396 250 P 250
Cdd:COG2265   311 P 311
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 181-291 6.82e-06

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 44.48  E-value: 6.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 181 LDLGSGCGIQALRVRRAADG-VVATDISARAVWFTRLNARLNGVDgIETRGGSLFE-PVAGEQFDRIVSNPPFVITPRaa 258
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGArVTGVDLSPEMLERARERAAEAGLN-VEFVQGDAEDlPFPDGSFDLVVSSGVLHHLPD-- 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2421839396 259 dvpayeyrdggmvgDDLVAAFvTGVGEHLAPGG 291
Cdd:pfam13649  79 --------------PDLEAAL-REIARVLKPGG 96
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
166-261 6.99e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 46.82  E-value: 6.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 166 LTLAGLQLPTPAGRALDLGSGCGIQALRVRRA-ADGVVATDISARAVWFTRLNARLNGVDgIETRGGSLFEPVAGEQFDR 244
Cdd:COG2263    35 LHLAYLRGDIEGKTVLDLGCGTGMLAIGAALLgAKKVVGVDIDPEALEIARENAERLGVR-VDFIRADVTRIPLGGSVDT 113

                          90
                  ....*....|....*..
gi 2421839396 245 IVSNPPFVITPRAADVP 261
Cdd:COG2263   114 VVMNPPFGAQRRHADRP 130
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 172-248 1.03e-05

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 45.01  E-value: 1.03e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2421839396 172 QLPTPAGRALDLGSGCGIQALRVRRAADGVVATDISARAVWFTRLNARLNGVDGIEtrgGSLFE-PVAGEQFDRIVSN 248
Cdd:COG2227    20 RLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNVDFVQ---GDLEDlPLEDGSFDLVICS 94
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
 181-252 2.15e-05

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


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 47.17  E-value: 2.15e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2421839396 181 LDLGSGCGIQALRVRRAADGVVATDISARAVWFTRLNA-RLNGVDGIETRGGSLFEPVAGEQFDRIVSNPPFV 252
Cdd:PRK01544  145 LGTGSGCIAISLLCELPNANVIATDISLDAIEVAKSNAiKYEVTDRIQIIHSNWFENIEKQKFDFIVSNPPYI 217
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
171-248 7.32e-05

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 44.78  E-value: 7.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 171 LQLPTPAGRALDLGSGCGIQA-LRVRRAADGVVATDISARAVWFTRLNARLNGV-DGIETRGGSLFEpvaGEQFDRIVSN 248
Cdd:COG2264   143 EKLLKPGKTVLDVGCGSGILAiAAAKLGAKRVLAVDIDPVAVEAARENAELNGVeDRIEVVLGDLLE---DGPYDLVVAN 219
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
162-251 2.99e-04

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


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 43.00  E-value: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 162 GGASLTLAGLQLPTpAGRALDLGSGCGIQALRVRRAADGV--VATDISARAVWFTRLNARLNGVDGiETRGGSLFEPVAG 239
Cdd:PRK09489  183 VGSQLLLSTLTPHT-KGKVLDVGCGAGVLSAVLARHSPKIrlTLSDVSAAALESSRATLAANGLEG-EVFASNVFSDIKG 260

                          90
                  ....*....|..
gi 2421839396 240 eQFDRIVSNPPF 251
Cdd:PRK09489  261 -RFDMIISNPPF 271
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
174-293 3.03e-04

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


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 42.48  E-value: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 174 PTPAGRALDLGSGCG---IQAL-RVRRAADGVVAT------DISARAVWFTRLNARLNGVDG--IEtRGGSLF-EPVAGE 240
Cdd:COG0286    41 PKPGETVYDPACGSGgflVEAAeYLKEHGGDERKKlslygqEINPTTYRLAKMNLLLHGIGDpnIE-LGDTLSnDGDELE 119

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2421839396 241 QFDRIVSNPPFVITpraadvpayeyRDGGMVGDDLVAAFVTGVG--------------EHLAPGGVA 293
Cdd:COG0286   120 KFDVVLANPPFGGK-----------WKKEELKDDLLGRFGYGLPpksnadllflqhilSLLKPGGRA 175
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
173-292 4.64e-04

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 41.14  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 173 LPTPAGRALDLGSGCGIQALRVRRAADGVVATDISARAVwfTRLNARLNGVDGIETRGGSLFEPvaGEQFDRIVsnppfv 252
Cdd:COG4976    43 PPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEML--AKAREKGVYDRLLVADLADLAEP--DGRFDLIV------ 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2421839396 253 itprAADVPAYeyrdggmvGDDLVAAFvTGVGEHLAPGGV 292
Cdd:COG4976   113 ----AADVLTY--------LGDLAAVF-AGVARALKPGGL 139
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 174-248 6.53e-04

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: 39.98  E-value: 6.53e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2421839396 174 PTPAGRALDLGSGCGIQALRVRRAADGVVATDISARAVWFTRLNARLNGVDgIETRGGSLFE-PVAGEQFDRIVSN 248
Cdd:COG2226    20 LRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLN-VEFVVGDAEDlPFPDGSFDLVISS 94
arsM PRK11873
arsenite methyltransferase;
145-248 6.75e-04

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 41.47  E-value: 6.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 145 DEAALQGpLREDHVLGVG-GASLTLAGLQlptPAGRALDLGSGCGIQALRVRRA--ADG-VVATDISARAVWFTRLNARL 220
Cdd:PRK11873   49 SEEELAA-VPEGANLGLGcGNPTALAELK---PGETVLDLGSGGGFDCFLAARRvgPTGkVIGVDMTPEMLAKARANARK 124

                          90       100
                  ....*....|....*....|....*....
gi 2421839396 221 NGVDGIETRGGSLFE-PVAGEQFDRIVSN 248
Cdd:PRK11873  125 AGYTNVEFRLGEIEAlPVADNSVDVIISN 153
TRM1 COG1867
tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N, ...
 176-227 1.26e-03

tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N,N-dimethylase Trm1 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441472  Cd Length: 383  Bit Score: 41.01  E-value: 1.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2421839396 176 PAGRALDLGSGCGIQALRVrrAADG---VVATDISARAVWFTRLNARLNGVDGIE 227
Cdd:COG1867    57 REISYLDALAASGIRGLRY--ALEVgikVTLNDIDPEAVELIRENLELNGLEDVE 109
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 181-248 2.50e-03

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 37.26  E-value: 2.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2421839396 181 LDLGSGCGIQALRVRRAADGVVATDISARAVWFTRLNARLNGVDGIETRGGSLfePVAGEQFDRIVSN 248
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTFVVGDAEDL--PFPDNSFDLVLSS 66
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
176-248 2.54e-03

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 37.50  E-value: 2.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2421839396 176 PAGRALDLGSGCGIQALRVRRAADG--VVATDISARAVwfTRLNARLNGVDGIEtrgGSLFEPVAGEQFDRIVSN 248
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFPGarVTGVDLSPEML--ARARARLPNVRFVV---ADLRDLDPPEPFDLVVSN 70
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 181-248 3.49e-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: 39.56  E-value: 3.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2421839396 181 LDLGSGCGIQAL-RVRRAADGVVATDISARAVWFTRLNARLNGVDGIETRGGSLFEPVagEQFDRIVSN 248
Cdd:pfam06325 166 LDVGCGSGILAIaALKLGAKKVVGVDIDPVAVRAAKENAELNGVEARLEVYLPGDLPK--EKADVVVAN 232
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
179-248 4.26e-03

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 38.98  E-value: 4.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2421839396 179 RALDLGSGCGIQALRVRR-AADGVVATDISARAVWFTRLNARLNGV-DGIETRGGSLfepvageQFDRIVSN 248
Cdd:PRK00517  122 TVLDVGCGSGILAIAAAKlGAKKVLAVDIDPQAVEAARENAELNGVeLNVYLPQGDL-------KADVIVAN 186
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 41-479 6.77e-03

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 39.45  E-value: 6.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396   41 AESVRAAWGVAADDAIARGLRSPADRALGDRHDPLAVLARLFVLGMPQSAAAVDSALPRLGADGLVRLALAERDGSTVRP 120
Cdd:COG1020    899 REAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAA 978

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396  121 TALVRPQsftdshgDGRWWIASDLDEAALQGPLREDHVLGVGGASLTLAglqlptpagrALDLGSGCGIQALRVRRAADG 200
Cdd:COG1020    979 AAAPPAE-------EEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLL----------LALARAARLLLLLLLLLLLFL 1041

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396  201 VVATDISARAVwftRLNARLNGVDGIETRGGSLFEPVAGEQFDRIVSNPPFVITPRAADVPAYEYRDGGMVGDDLVAAFV 280
Cdd:COG1020   1042 AAAAAAAAAAA---AAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALL 1118

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396  281 TGVGEHLAPGGVAQLLGNWETRAGRDGLDRVRDWVEASPVPLDAWVVEREALDPLSYAELWIRDGGTLPGASGFARLIDA 360
Cdd:COG1020   1119 LALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLL 1198

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396  361 WLDDFTARDVSEVGFGYLLLRRPLAGEPTLRRFERIPHALEGRATLGGHLADALAMHDLLVDVDDAELTASVLLVAPDVT 440
Cdd:COG1020   1199 LLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALAL 1278

                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 2421839396  441 EARHHMPGAEAPTVIELRQGGGYGRSLSVDPALAALVGA 479
Cdd:COG1020   1279 LLPALARARAARTARALALLLLLALLLLLALALALLLLL 1317
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
178-251 6.83e-03

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 37.60  E-value: 6.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421839396 178 GRALDL--GSGC-GIQALRvrRAADGVVATDISARAVWFTRLNARLNGVDGIETRGGS----LFEPVAGEQFDRIVSNPP 250
Cdd:pfam03602  43 ARVLDLfaGSGAlGLEALS--RGAKRVTLVEKDKRAVQILKENLQLLGLPGAVLVMDAllalLRLAGKGPVFDIVFLDPP 120


                  .
gi 2421839396 251 F 251
Cdd:pfam03602 121 Y 121
 
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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