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Conserved domains on  [gi|1672722804|ref|WP_138362882|]
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MULTISPECIES: 50S ribosomal protein L11 methyltransferase [Klebsiella]

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
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
3-286 2.22e-138

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.).


The actual alignment was detected with superfamily member TIGR00406:

Pssm-ID: 473071  Cd Length: 288  Bit Score: 391.89  E-value: 2.22e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804   3 WIQLKLNTTGANAEELSDALMDAGSVSITFQDTHDTPVFEP-LPGETRLWGDTDVIGLFDAETDMKEVVAILEQHRLLGR 81
Cdd:TIGR00406   1 WIEIRINTTKELAEATSDALEEAGAVGVTFEDDKDTIYFEPhLPGEKRLWGNLDVIALFDAETDMNNSVIPLLEAFCLDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804  82 GFVHKIEQLE-DKDWEREWMDNFHPMCFGKRLWICPSWREVP-DENAVNVMLDPGLAFGTGTHPTTAMCLQWLDGLDLKG 159
Cdd:TIGR00406  81 GRNHKIEFDEfSKDWERAWKDNFHPVQFGKRFWICPSWRDVPsDEDALIIMLDPGLAFGTGTHPTTSLCLEWLEDLDLKD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 160 KTIIDFGCGSGILAIAALKLGAAKAIGIDIDPQAIQASRDNAERNGVSGRLELYLPQ-DQPEAMKADVVVANILAGPLRE 238
Cdd:TIGR00406 161 KNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAVESARKNAELNQVSDRLQVKLIYlEQPIEGKADVIVANILAEVIKE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1672722804 239 LAPLISVLPVTGGLLGLSGILASQSESVCEAYTDLFVLDPVVEKDEWC 286
Cdd:TIGR00406 241 LYPQFSRLVKPGGWLILSGILETQAQSVCDAYEQGFTVVEIRQREEWC 288
 
Name Accession Description Interval E-value
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
3-286 2.22e-138

ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an S-adenosyl-L-methionine-dependent methyltransferase required for the modification of ribosomal protein L11. This protein is found in bacteria and (with a probable transit peptide) in Arabidopsis. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273061  Cd Length: 288  Bit Score: 391.89  E-value: 2.22e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804   3 WIQLKLNTTGANAEELSDALMDAGSVSITFQDTHDTPVFEP-LPGETRLWGDTDVIGLFDAETDMKEVVAILEQHRLLGR 81
Cdd:TIGR00406   1 WIEIRINTTKELAEATSDALEEAGAVGVTFEDDKDTIYFEPhLPGEKRLWGNLDVIALFDAETDMNNSVIPLLEAFCLDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804  82 GFVHKIEQLE-DKDWEREWMDNFHPMCFGKRLWICPSWREVP-DENAVNVMLDPGLAFGTGTHPTTAMCLQWLDGLDLKG 159
Cdd:TIGR00406  81 GRNHKIEFDEfSKDWERAWKDNFHPVQFGKRFWICPSWRDVPsDEDALIIMLDPGLAFGTGTHPTTSLCLEWLEDLDLKD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 160 KTIIDFGCGSGILAIAALKLGAAKAIGIDIDPQAIQASRDNAERNGVSGRLELYLPQ-DQPEAMKADVVVANILAGPLRE 238
Cdd:TIGR00406 161 KNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAVESARKNAELNQVSDRLQVKLIYlEQPIEGKADVIVANILAEVIKE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1672722804 239 LAPLISVLPVTGGLLGLSGILASQSESVCEAYTDLFVLDPVVEKDEWC 286
Cdd:TIGR00406 241 LYPQFSRLVKPGGWLILSGILETQAQSVCDAYEQGFTVVEIRQREEWC 288
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
2-292 4.25e-127

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: 363.51  E-value: 4.25e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804   2 PWIQLKLNTTGANAEELSDALMDAGSVSITFQDTH---DTPVFEPLPGETRLWGDTDVIGLFDAETDMKEVVAILEQHRL 78
Cdd:pfam06325   1 TWLELSIHTTREAAEPVSNILEEFGALGVAIEDADlleDRDIFEPGLGEERLWDEVRVKALFDEETDALELIAQLAELIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804  79 LGRGFVHKIEQLEDKDWEREWMDNFHPMCFGKRLWICPSWREVPD-ENAVNVMLDPGLAFGTGTHPTTAMCLQWLDGLDL 157
Cdd:pfam06325  81 GLDSPKVTVEEVAEEDWARAWKKYFHPVRIGERLTIVPSWEDYPEnPDALNIELDPGMAFGTGTHPTTKLCLEALERLVK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 158 KGKTIIDFGCGSGILAIAALKLGAAKAIGIDIDPQAIQASRDNAERNGVSGRLELYLPQDQPEaMKADVVVANILAGPLR 237
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEARLEVYLPGDLPK-EKADVVVANILADPLI 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1672722804 238 ELAPLISVLPVTGGLLGLSGILASQSESVCEAYTDLFVLDPVVEKDEWCRITGYK 292
Cdd:pfam06325 240 ELAPDIYALVKPGGYLILSGILKEQAQMVAEAYSQGFELITVEHREEWVCIVGKK 294
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
1-293 1.66e-109

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 318.66  E-value: 1.66e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804   1 MPWIQLKLNTTGANAEELSDALMDAGSVSITFQDthdtpvfePLPGEtrlWGDTDVIGLFDAETDMKEVVAILEQHRLLG 80
Cdd:COG2264     1 MKWIELTITTPEEAAEALSDALEELGAEGVEIED--------APPGL---WERVGVKAYFPEDEDLEELLAALAEALGEL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804  81 RGFVHKIEQLEDKDWEREWMDNFHPMCFGKRLWICPSWREV-PDENAVNVMLDPGLAFGTGTHPTTAMCLQWLDGLDLKG 159
Cdd:COG2264    70 GAPEITVEEVEEEDWVEEWKKYFKPIRVGDRLVIVPSWEEYePDPGEIVIEIDPGMAFGTGTHPTTRLCLEALEKLLKPG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 160 KTIIDFGCGSGILAIAALKLGAAKAIGIDIDPQAIQASRDNAERNGVSGRLELYLPQDQPEAmKADVVVANILAGPLREL 239
Cdd:COG2264   150 KTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVEDRIEVVLGDLLEDG-PYDLVVANILANPLIEL 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1672722804 240 APLIS-------------VLpvtggllglsgilASQSESVCEAYTDL-FVLDPVVEKDEWCRITGYKK 293
Cdd:COG2264   229 APDLAallkpggylilsgIL-------------EEQADEVLAAYEAAgFELVERRERGEWVALVLRKK 283
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
1-293 7.48e-106

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 308.23  E-value: 7.48e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804   1 MPWIQLKLNTTGANAEELSDALMDAGSVsitfqdthdtpvfeplpgetrlwgdtdviglfdaetdmkevvAILEQHRLLG 80
Cdd:PRK00517    1 MKWIELTLNTTPEAAEALSDILMELGAL------------------------------------------AALANLAGLG 38
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804  81 RGFV---HKIEQLEDKDWEREWMDNFHPMCFGKRLWICPSWREVPDENAVNVMLDPGLAFGTGTHPTTAMCLQWLDGLDL 157
Cdd:PRK00517   39 LDLGeptYTIEEVEDEDWEREWKKYFHPIRIGDRLWIVPSWEDPPDPDEINIELDPGMAFGTGTHPTTRLCLEALEKLVL 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 158 KGKTIIDFGCGSGILAIAALKLGAAKAIGIDIDPQAIQASRDNAERNGVsgRLELYLPQDQPeamKADVVVANILAGPLR 237
Cdd:PRK00517  119 PGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGV--ELNVYLPQGDL---KADVIVANILANPLL 193
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 238 ELAPLIS-------------VLpvtggllglsgilASQSESVCEAYTDL-FVLDPVVEKDEWCRITGYKK 293
Cdd:PRK00517  194 ELAPDLArllkpggrlilsgIL-------------EEQADEVLEAYEEAgFTLDEVLERGEWVALVGKKK 250
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
161-230 5.53e-04

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: 38.57  E-value: 5.53e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1672722804 161 TIIDFGCGSGILAIAALKLGAAKAIGIDIDPQAIQASRDNAERNG------VSGRLELyLPQDQPEamKADVVVAN 230
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLadnvevLKGDAEE-LPPEADE--SFDVIISD 73
 
Name Accession Description Interval E-value
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
3-286 2.22e-138

ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an S-adenosyl-L-methionine-dependent methyltransferase required for the modification of ribosomal protein L11. This protein is found in bacteria and (with a probable transit peptide) in Arabidopsis. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273061  Cd Length: 288  Bit Score: 391.89  E-value: 2.22e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804   3 WIQLKLNTTGANAEELSDALMDAGSVSITFQDTHDTPVFEP-LPGETRLWGDTDVIGLFDAETDMKEVVAILEQHRLLGR 81
Cdd:TIGR00406   1 WIEIRINTTKELAEATSDALEEAGAVGVTFEDDKDTIYFEPhLPGEKRLWGNLDVIALFDAETDMNNSVIPLLEAFCLDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804  82 GFVHKIEQLE-DKDWEREWMDNFHPMCFGKRLWICPSWREVP-DENAVNVMLDPGLAFGTGTHPTTAMCLQWLDGLDLKG 159
Cdd:TIGR00406  81 GRNHKIEFDEfSKDWERAWKDNFHPVQFGKRFWICPSWRDVPsDEDALIIMLDPGLAFGTGTHPTTSLCLEWLEDLDLKD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 160 KTIIDFGCGSGILAIAALKLGAAKAIGIDIDPQAIQASRDNAERNGVSGRLELYLPQ-DQPEAMKADVVVANILAGPLRE 238
Cdd:TIGR00406 161 KNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAVESARKNAELNQVSDRLQVKLIYlEQPIEGKADVIVANILAEVIKE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1672722804 239 LAPLISVLPVTGGLLGLSGILASQSESVCEAYTDLFVLDPVVEKDEWC 286
Cdd:TIGR00406 241 LYPQFSRLVKPGGWLILSGILETQAQSVCDAYEQGFTVVEIRQREEWC 288
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
2-292 4.25e-127

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: 363.51  E-value: 4.25e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804   2 PWIQLKLNTTGANAEELSDALMDAGSVSITFQDTH---DTPVFEPLPGETRLWGDTDVIGLFDAETDMKEVVAILEQHRL 78
Cdd:pfam06325   1 TWLELSIHTTREAAEPVSNILEEFGALGVAIEDADlleDRDIFEPGLGEERLWDEVRVKALFDEETDALELIAQLAELIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804  79 LGRGFVHKIEQLEDKDWEREWMDNFHPMCFGKRLWICPSWREVPD-ENAVNVMLDPGLAFGTGTHPTTAMCLQWLDGLDL 157
Cdd:pfam06325  81 GLDSPKVTVEEVAEEDWARAWKKYFHPVRIGERLTIVPSWEDYPEnPDALNIELDPGMAFGTGTHPTTKLCLEALERLVK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 158 KGKTIIDFGCGSGILAIAALKLGAAKAIGIDIDPQAIQASRDNAERNGVSGRLELYLPQDQPEaMKADVVVANILAGPLR 237
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEARLEVYLPGDLPK-EKADVVVANILADPLI 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1672722804 238 ELAPLISVLPVTGGLLGLSGILASQSESVCEAYTDLFVLDPVVEKDEWCRITGYK 292
Cdd:pfam06325 240 ELAPDIYALVKPGGYLILSGILKEQAQMVAEAYSQGFELITVEHREEWVCIVGKK 294
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
1-293 1.66e-109

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 318.66  E-value: 1.66e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804   1 MPWIQLKLNTTGANAEELSDALMDAGSVSITFQDthdtpvfePLPGEtrlWGDTDVIGLFDAETDMKEVVAILEQHRLLG 80
Cdd:COG2264     1 MKWIELTITTPEEAAEALSDALEELGAEGVEIED--------APPGL---WERVGVKAYFPEDEDLEELLAALAEALGEL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804  81 RGFVHKIEQLEDKDWEREWMDNFHPMCFGKRLWICPSWREV-PDENAVNVMLDPGLAFGTGTHPTTAMCLQWLDGLDLKG 159
Cdd:COG2264    70 GAPEITVEEVEEEDWVEEWKKYFKPIRVGDRLVIVPSWEEYePDPGEIVIEIDPGMAFGTGTHPTTRLCLEALEKLLKPG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 160 KTIIDFGCGSGILAIAALKLGAAKAIGIDIDPQAIQASRDNAERNGVSGRLELYLPQDQPEAmKADVVVANILAGPLREL 239
Cdd:COG2264   150 KTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVEDRIEVVLGDLLEDG-PYDLVVANILANPLIEL 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1672722804 240 APLIS-------------VLpvtggllglsgilASQSESVCEAYTDL-FVLDPVVEKDEWCRITGYKK 293
Cdd:COG2264   229 APDLAallkpggylilsgIL-------------EEQADEVLAAYEAAgFELVERRERGEWVALVLRKK 283
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
1-293 7.48e-106

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 308.23  E-value: 7.48e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804   1 MPWIQLKLNTTGANAEELSDALMDAGSVsitfqdthdtpvfeplpgetrlwgdtdviglfdaetdmkevvAILEQHRLLG 80
Cdd:PRK00517    1 MKWIELTLNTTPEAAEALSDILMELGAL------------------------------------------AALANLAGLG 38
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804  81 RGFV---HKIEQLEDKDWEREWMDNFHPMCFGKRLWICPSWREVPDENAVNVMLDPGLAFGTGTHPTTAMCLQWLDGLDL 157
Cdd:PRK00517   39 LDLGeptYTIEEVEDEDWEREWKKYFHPIRIGDRLWIVPSWEDPPDPDEINIELDPGMAFGTGTHPTTRLCLEALEKLVL 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 158 KGKTIIDFGCGSGILAIAALKLGAAKAIGIDIDPQAIQASRDNAERNGVsgRLELYLPQDQPeamKADVVVANILAGPLR 237
Cdd:PRK00517  119 PGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGV--ELNVYLPQGDL---KADVIVANILANPLL 193
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 238 ELAPLIS-------------VLpvtggllglsgilASQSESVCEAYTDL-FVLDPVVEKDEWCRITGYKK 293
Cdd:PRK00517  194 ELAPDLArllkpggrlilsgIL-------------EEQADEVLEAYEEAgFTLDEVLERGEWVALVGKKK 250
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
158-230 4.89e-10

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: 58.62  E-value: 4.89e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1672722804 158 KGKTIIDFGCGSGILAIAALKLGAAKAI-GIDIDPQAIQASRDNAERNGVSGRLELYL-----PQDQPEAMKADVVVAN 230
Cdd:COG4123    37 KGGRVLDLGTGTGVIALMLAQRSPGARItGVEIQPEAAELARRNVALNGLEDRITVIHgdlkeFAAELPPGSFDLVVSN 115
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
156-238 1.06e-09

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 56.84  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 156 DLKGKTIIDFGCGSGILAIAALKLGAAKAIGIDIDPQAIQASRDNAERNGVSgrlelylpqdqpeamkADVVVANILAGP 235
Cdd:COG2263    43 DIEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDIDPEALEIARENAERLGVR----------------VDFIRADVTRIP 106

                  ...
gi 1672722804 236 LRE 238
Cdd:COG2263   107 LGG 109
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
152-229 1.37e-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: 56.82  E-value: 1.37e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1672722804 152 LDGLDLKGKTIIDFGCGSGILAIAALKLGAAKAIGIDIDPQAIQASRDNAERNGVSGRLELYLPQDQPEAMKADVVVA 229
Cdd:COG3897    64 LDHPEVAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALAALRLNAALNGVAITTRLGDWRDPPAAGGFDLILG 141
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
149-230 9.36e-09

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 55.16  E-value: 9.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 149 LQWLDglDLKGKTIIDFGCGSGILAIAALKLGAAKAI-GIDIDPQAIQASRDNAERNGVSGRLELY---LPQDQPEAMKA 224
Cdd:COG2890   105 LALLP--AGAPPRVLDLGTGSGAIALALAKERPDARVtAVDISPDALAVARRNAERLGLEDRVRFLqgdLFEPLPGDGRF 182

                  ....*.
gi 1672722804 225 DVVVAN 230
Cdd:COG2890   183 DLIVSN 188
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
159-230 2.15e-07

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: 50.19  E-value: 2.15e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1672722804 159 GKTIIDFGCGSGILAIAALKLGAAKAI-GIDIDPQAIQASRDNAERNGVSGrLELYLPQ--DQPEAMKADVVVAN 230
Cdd:COG2813    50 GGRVLDLGCGYGVIGLALAKRNPEARVtLVDVNARAVELARANAAANGLEN-VEVLWSDglSGVPDGSFDLILSN 123
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
150-230 5.36e-07

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: 47.70  E-value: 5.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 150 QWLDGLDLKGKTIIDFGCGSGILAIaALKLGAAKAIGIDIDPQAIQASRDNAERNGVSgrlelYLPQD----QPEAMKAD 225
Cdd:COG2227    16 ALLARLLPAGGRVLDVGCGTGRLAL-ALARRGADVTGVDISPEALEIARERAAELNVD-----FVQGDledlPLEDGSFD 89

                  ....*
gi 1672722804 226 VVVAN 230
Cdd:COG2227    90 LVICS 94
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
149-230 5.47e-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: 50.17  E-value: 5.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 149 LQWLDglDLKGKTIIDFGCGSG----ILAiaalkLGAAKAIGIDIDPQAIQASRDNAERNGVS------GRLELYLPQdQ 218
Cdd:COG2265   226 LEWLD--LTGGERVLDLYCGVGtfalPLA-----RRAKKVIGVEIVPEAVEDARENARLNGLKnvefvaGDLEEVLPE-L 297
                          90
                  ....*....|..
gi 1672722804 219 PEAMKADVVVAN 230
Cdd:COG2265   298 LWGGRPDVVVLD 309
PRK14968 PRK14968
putative methyltransferase; Provisional
155-209 6.76e-07

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 48.74  E-value: 6.76e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1672722804 155 LDLKGKTIIDFGCGSGILAIaALKLGAAKAIGIDIDPQAIQASRDNAERNGVSGR 209
Cdd:PRK14968   20 VDKKGDRVLEVGTGSGIVAI-VAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNN 73
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
130-229 6.91e-07

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 48.00  E-value: 6.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 130 MLDPGLAFGTGTHPTTAMCLQ---------WLDGLDLK-GKTIIDFGCGSGILAIAALKLGAAKAIGIDIDPQAIQASRD 199
Cdd:COG2230    13 FLDPTMTYSCAYFEDPDDTLEeaqeakldlILRKLGLKpGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARE 92
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1672722804 200 NAERNGVSGRLELYLpQD---QPEAMKADVVVA 229
Cdd:COG2230    93 RAAEAGLADRVEVRL-ADyrdLPADGQFDAIVS 124
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
158-230 8.88e-07

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 48.37  E-value: 8.88e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1672722804 158 KGKTIIDFGCGSGILAIAALKLGAAKAIGIDIDPQAIQASRDNAERNGVsGRLELYLpQD-----QPEAMKADVVVAN 230
Cdd:COG0500    26 KGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGL-GNVEFLV-ADlaeldPLPAESFDLVVAF 101
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
131-230 1.69e-06

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: 47.20  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 131 LDPGlafgtgthptTAMCLQWLDglDLKGKTIIDFGCGSGILAIAALKLGAAKAI-GIDIDPQAIQASRDNAERNGVSGr 209
Cdd:pfam05175  16 LDIG----------SRLLLEHLP--KDLSGKVLDLGCGAGVLGAALAKESPDAELtMVDINARALESARENLAANGLEN- 82
                          90       100
                  ....*....|....*....|....
gi 1672722804 210 LELYlPQD---QPEAMKADVVVAN 230
Cdd:pfam05175  83 GEVV-ASDvysGVEDGKFDLIISN 105
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
158-238 2.05e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 47.72  E-value: 2.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 158 KGKTIIDFGCGSGILAIAALKLGAAKAIGIDIDPQAIQASRDNAERNGVSGRLELyLPQDQ-----PEamKADVVVANIL 232
Cdd:COG4076    35 PGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITV-INADAtdldlPE--KADVIISEML 111

                  ....*..
gi 1672722804 233 A-GPLRE 238
Cdd:COG4076   112 DtALLDE 118
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
162-230 8.25e-06

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 43.71  E-value: 8.25e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 162 IIDFGCGSGILAIAALKLGAAKAIGIDIDPQAIQASRDNAERNGVSGRLELYLPQDQP-EAMKADVVVAN 230
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPfPDGSFDLVVSS 70
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
158-230 1.06e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 44.72  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 158 KGKTIIDFGCGSGILAIA--ALKLGAAKAIGIDIDPQAIQASRDNAERNGVSgRLELY------LPQDQPEAmKADVVVA 229
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFElaEELGPNAEVVGIDISEEAIEKARENAQKLGFD-NVEFEqgdieeLPELLEDD-KFDVVIS 80

                  .
gi 1672722804 230 N 230
Cdd:pfam13847  81 N 81
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
149-229 2.32e-05

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 44.44  E-value: 2.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 149 LQWL-DGLDLKGKTIIDFGCGSGILAIAALKLGAAKAiGIDIDPQAIQASRDNAERNGVSGRLElYLPQD-QPEAMKADV 226
Cdd:PRK07580   53 LSWLpADGDLTGLRILDAGCGVGSLSIPLARRGAKVV-ASDISPQMVEEARERAPEAGLAGNIT-FEVGDlESLLGRFDT 130

                  ...
gi 1672722804 227 VVA 229
Cdd:PRK07580  131 VVC 133
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
143-230 6.75e-05

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


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 42.73  E-value: 6.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 143 PTTAMCLQWLDGLDlKGKTIIDFGCGSGILAI------------AALKLGAAKAIGIDIDPQAIQASRDNAERNGVSGRL 210
Cdd:pfam01170  14 ETLAAAMVNLAGWK-PGDPLLDPMCGSGTILIeaalmganiapgKFDARVRAPLYGSDIDRRMVQGARLNAENAGVGDLI 92
                          90       100
                  ....*....|....*....|....*.
gi 1672722804 211 ELY------LPQDQPEamkADVVVAN 230
Cdd:pfam01170  93 EFVqadaadLPLLEGS---VDVIVTN 115
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
160-230 4.27e-04

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: 41.18  E-value: 4.27e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1672722804 160 KTIIDFGCGSGILAIAALKLGAAKAI-GIDIDPQAIQASRDNAERNGVSGRLELYlpQ----DQPEAMKADVVVAN 230
Cdd:TIGR00536 116 LHILDLGTGSGCIALALAYEFPNAEViAVDISPDALAVAEENAEKNQLEHRVEFI--QsnlfEPLAGQKIDIIVSN 189
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
158-245 4.88e-04

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 40.55  E-value: 4.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 158 KGKTIIDFGCGSGILAIAALKL--GAAKAIGIDIDPQAIQASRDNAERNGVSGRLELyLPQDQPEAM-----KADVVvan 230
Cdd:PRK00377   40 KGDMILDIGCGTGSVTVEASLLvgETGKVYAVDKDEKAINLTRRNAEKFGVLNNIVL-IKGEAPEILftineKFDRI--- 115
                          90
                  ....*....|....*
gi 1672722804 231 ILAGPLRELAPLISV 245
Cdd:PRK00377  116 FIGGGSEKLKEIISA 130
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
161-230 5.53e-04

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: 38.57  E-value: 5.53e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1672722804 161 TIIDFGCGSGILAIAALKLGAAKAIGIDIDPQAIQASRDNAERNG------VSGRLELyLPQDQPEamKADVVVAN 230
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLadnvevLKGDAEE-LPPEADE--SFDVIISD 73
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
185-212 1.02e-03

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


Pssm-ID: 439886 [Multi-domain]  Cd Length: 369  Bit Score: 40.08  E-value: 1.02e-03
                          10        20
                  ....*....|....*....|....*...
gi 1672722804 185 IGIDIDPQAIQASRDNAERNGVSGRLEL 212
Cdd:COG0116   254 FGSDIDPRAIEAARENAERAGVADLIEF 281
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
158-230 1.05e-03

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 39.76  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 158 KGKTIIDFGCGSGILAIAALKLGAAKAI-GIDIDPQAIQASRDNAERnGVSGRLELY-------LPQDqpeamKADVVVA 229
Cdd:PRK09328  108 EPLRVLDLGTGSGAIALALAKERPDAEVtAVDISPEALAVARRNAKH-GLGARVEFLqgdwfepLPGG-----RFDLIVS 181

                  .
gi 1672722804 230 N 230
Cdd:PRK09328  182 N 182
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
118-174 1.28e-03

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 39.84  E-value: 1.28e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 118 WREVPDE-NAVN-VMLDpglaFGTGTHPTTAMCLQWLDG-LDLKGKTIIDFGCGSGILAI 174
Cdd:PLN02585  105 WRKIYGEtDEVNkVQLD----IRLGHAQTVEKVLLWLAEdGSLAGVTVCDAGCGTGSLAI 160
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
160-229 1.37e-03

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


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 38.32  E-value: 1.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1672722804 160 KTIIDFGCGSGILA-IAALKLGAAKAIGIDIDPQAIQASRDNAERNGVSGRLEL-------YLPQDQPEamKADVVVA 229
Cdd:pfam13679  27 ITIVDHGAGKGYLGfILYYLKYGVRVYGIDTRAELVEKANALAQKLGFNKRMSFlegtiagSTPVELPD--RVDVVTA 102
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
150-210 1.57e-03

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: 38.05  E-value: 1.57e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1672722804 150 QWLDGLDLK-GKTIIDFGCGSGILAIaALKLGAAKAIGIDIDPQAIQASRDNAERNGVSGRL 210
Cdd:COG2226    13 ALLAALGLRpGARVLDLGCGTGRLAL-ALAERGARVTGVDISPEMLELARERAAEAGLNVEF 73
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
163-230 3.15e-03

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 36.19  E-value: 3.15e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1672722804 163 IDFGCGSGILAIAALKLGAAKAI-GIDIDPQAIQASRDNAERNGVSGRLELYLPQDQPEAM---KADVVVAN 230
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYtGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELdpgSFDVVVAS 72
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
185-213 5.07e-03

bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2))-methyltransferase RlmL;


Pssm-ID: 236981 [Multi-domain]  Cd Length: 702  Bit Score: 38.24  E-value: 5.07e-03
                          10        20
                  ....*....|....*....|....*....
gi 1672722804 185 IGIDIDPQAIQASRDNAERNGVSGRLELY 213
Cdd:PRK11783  260 YGSDIDPRVIQAARKNARRAGVAELITFE 288
PRK14967 PRK14967
putative methyltransferase; Provisional
159-230 5.48e-03

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 37.34  E-value: 5.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1672722804 159 GKTIIDFGCGSGILAIAALKLGAAKAIGIDIDPQAIQASRDNAERNGVSGRLELYLPQDQPEAMKADVVVAN 230
Cdd:PRK14967   37 GRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNALLAGVDVDVRRGDWARAVEFRPFDVVVSN 108
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
158-230 6.22e-03

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 35.57  E-value: 6.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1672722804 158 KGKTIIDFGCGSGILAIA-ALKLGAAKAIGIDIDPQAIQASRDNAER-NGVSGRLELYLPQDQpeamkADVVVAN 230
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALlAERFPGARVTGVDLSPEMLARARARLPNvRFVVADLRDLDPPEP-----FDLVVSN 70
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
152-230 6.24e-03

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 36.64  E-value: 6.24e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1672722804 152 LDGLDLKGKTIIDFGCGSGILAIaALKLGAAKAIGIDIDPQAIQASRDNAERNGVSGRLELYLPQdqpeamKADVVVAN 230
Cdd:pfam13489  16 LLPKLPSPGRVLDFGCGTGIFLR-LLRAQGFSVTGVDPSPIAIERALLNVRFDQFDEQEAAVPAG------KFDVIVAR 87
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
150-230 9.47e-03

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


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 37.24  E-value: 9.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672722804 150 QWLDGLDLK-GKTIIDFGCGSGIL--AIAALKLGAAKAIGIDIDPQAIQASRDNAERNGVSgrLELYlPQD--QPEAMK- 223
Cdd:COG0827   106 YLVEKFTKKeGLRILDPAVGTGNLltTVLNQLKKKVNAYGVEVDDLLIRLAAVLANLQGHP--VELF-HQDalQPLLIDp 182

                  ....*..
gi 1672722804 224 ADVVVAN 230
Cdd:COG0827   183 VDVVISD 189
 
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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