NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2527434988|ref|WP_288450785|]
View 

peptide chain release factor N(5)-glutamine methyltransferase [uncultured Acinetobacter sp.]

Protein Classification

HemK/PrmC family methyltransferase( domain architecture ID 11483836)

HemK/PrmC family methyltransferase is a class I SAM-dependent methyltransferase that catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; such as peptide chain release factor N(5)-glutamine methyltransferase that methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:0003676|GO:0032259|GO:1904047
PubMed:  12741815|12504684|12826405
SCOP:  3000118

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 1-269 1.40e-122

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


:

Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 350.62  E-value: 1.40e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988   1 MNIAQALNLRGEPDSYERQEAIWLLEHIVHLNALELRMRSLQVLSSEQEQAYLEGLVRLAQGEPLAYITGSQPFWSLDLI 80
Cdd:PRK09328    2 MTIAEALREATARLASPRLDAELLLAHVLGLSRTDLLLNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFWGLDFK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  81 VTKDTLVPRPDTEILIETVLE-LTLPKHSNVVDLGTGTGAIALSLAKERPDWRVLATDIYQPTLDIAAKNAQKHQLDRVE 159
Cdd:PRK09328   82 VSPGVLIPRPETEELVEWALEaLLLKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGLGARVE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 160 FVCGAWYEAIPAQRFDLIVSNPPYIDADDVHMQH---LATEPRRALVADHQGLSDLEHIIKQAPQWLNIDGWLVLEHGYD 236
Cdd:PRK09328  162 FLQGDWFEPLPGGRFDLIVSNPPYIPEADIHLLQpevRDHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGWLLLEIGYD 241

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2527434988 237 QGNAVRQIFNAAGFAQMQTVKDYGGNDRISLGQ 269
Cdd:PRK09328  242 QGEAVRALLAAAGFADVETRKDLAGRDRVVLGR 274
 
Name Accession Description Interval E-value
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 1-269 1.40e-122

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 350.62  E-value: 1.40e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988   1 MNIAQALNLRGEPDSYERQEAIWLLEHIVHLNALELRMRSLQVLSSEQEQAYLEGLVRLAQGEPLAYITGSQPFWSLDLI 80
Cdd:PRK09328    2 MTIAEALREATARLASPRLDAELLLAHVLGLSRTDLLLNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFWGLDFK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  81 VTKDTLVPRPDTEILIETVLE-LTLPKHSNVVDLGTGTGAIALSLAKERPDWRVLATDIYQPTLDIAAKNAQKHQLDRVE 159
Cdd:PRK09328   82 VSPGVLIPRPETEELVEWALEaLLLKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGLGARVE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 160 FVCGAWYEAIPAQRFDLIVSNPPYIDADDVHMQH---LATEPRRALVADHQGLSDLEHIIKQAPQWLNIDGWLVLEHGYD 236
Cdd:PRK09328  162 FLQGDWFEPLPGGRFDLIVSNPPYIPEADIHLLQpevRDHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGWLLLEIGYD 241

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2527434988 237 QGNAVRQIFNAAGFAQMQTVKDYGGNDRISLGQ 269
Cdd:PRK09328  242 QGEAVRALLAAAGFADVETRKDLAGRDRVVLGR 274
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 20-267 6.29e-122

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: 347.92  E-value: 6.29e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  20 EAIWLLEHIVHLNALELRMRSLQVLSSEQEQAYLEGLVRLAQGEPLAYITGSQPFWSLDLIVTKDTLVPRPDTEILIETV 99
Cdd:TIGR03534   1 DAELLLAHVLGKDRAQLLLHPEDELTPEELAAFDALLARRAAGEPVAYILGEREFYGLDFKVSPGVLIPRPETEELVEAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 100 LELtLPKHSNVVDLGTGTGAIALSLAKERPDWRVLATDIYQPTLDIAAKNAQKHQLDRVEFVCGAWYEAIPAQRFDLIVS 179
Cdd:TIGR03534  81 LER-LKKGPRVLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKNARRLGLENVEFLQGDWFEPLPSGKFDLIVS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 180 NPPYIDADDVHMQH---LATEPRRALVADHQGLSDLEHIIKQAPQWLNIDGWLVLEHGYDQGNAVRQIFNAAGFAQMQTV 256
Cdd:TIGR03534 160 NPPYIPEADIHLLDpevRDFEPRLALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFEAAGFADVETR 239

                         250
                  ....*....|.
gi 2527434988 257 KDYGGNDRISL 267
Cdd:TIGR03534 240 KDLAGKDRVVL 250
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 1-271 4.86e-115

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 331.73  E-value: 4.86e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988   1 MNIAQALN-----LRGEPDSYERQEAIWLLEHIVHLNALELRMRSLQVLSSEQEQAYLEGLVRLAQGEPLAYITGSQPFW 75
Cdd:COG2890     1 MTIRELLRwaaarLAAAGVDSARLEAELLLAHVLGLDRADLLLHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  76 SLDLIVTKDTLVPRPDTEILIETVLE-LTLPKHSNVVDLGTGTGAIALSLAKERPDWRVLATDIYQPTLDIAAKNAQKHQ 154
Cdd:COG2890    81 GLEFKVDPGVLIPRPETEELVELALAlLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 155 L-DRVEFVCGAWYEAIPA-QRFDLIVSNPPYIDADDVH-MQH--LATEPRRALVADHQGLSDLEHIIKQAPQWLNIDGWL 229
Cdd:COG2890   161 LeDRVRFLQGDLFEPLPGdGRFDLIVSNPPYIPEDEIAlLPPevRDHEPRLALDGGEDGLDFYRRIIAQAPRLLKPGGWL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2527434988 230 VLEHGYDQGNAVRQIFNAAGFAQMQTVKDYGGNDRISLGQMK 271
Cdd:COG2890   241 LLEIGEDQGEAVRALLEAAGFADVETHKDLAGRDRVVVARRP 282
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 92-246 1.73e-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: 85.72  E-value: 1.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  92 TEILIETvleLTLPKHSNVVDLGTGTGAIALSLAKERPDWRVLATDIYQPTLDIAAKNAQKHQLDRVEFVCGAWYEAIPA 171
Cdd:pfam05175  20 SRLLLEH---LPKDLSGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGLENGEVVASDVYSGVED 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2527434988 172 QRFDLIVSNPPYidaddvHmQHLATEPRRAlvadhqglsdlEHIIKQAPQWLNIDG--WLVLEH--GYDQgnAVRQIFN 246
Cdd:pfam05175  97 GKFDLIISNPPF------H-AGLATTYNVA-----------QRFIADAKRHLRPGGelWIVANRflGYPP--LLEELFG 155
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 109-202 6.19e-15

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: 69.00  E-value: 6.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 109 NVVDLGTGTGAIALSLAkERPDWRVLATDIYQPTLDIAAKNAQKHQLDRVEFVCGAWYEAIPA--QRFDLIVSNPPYIDA 186
Cdd:cd02440     1 RVLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEadESFDVIISDPPLHHL 79

                          90
                  ....*....|....*.
gi 2527434988 187 DDVHMQHLAtEPRRAL 202
Cdd:cd02440    80 VEDLARFLE-EARRLL 94
 
Name Accession Description Interval E-value
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 1-269 1.40e-122

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 350.62  E-value: 1.40e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988   1 MNIAQALNLRGEPDSYERQEAIWLLEHIVHLNALELRMRSLQVLSSEQEQAYLEGLVRLAQGEPLAYITGSQPFWSLDLI 80
Cdd:PRK09328    2 MTIAEALREATARLASPRLDAELLLAHVLGLSRTDLLLNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFWGLDFK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  81 VTKDTLVPRPDTEILIETVLE-LTLPKHSNVVDLGTGTGAIALSLAKERPDWRVLATDIYQPTLDIAAKNAQKHQLDRVE 159
Cdd:PRK09328   82 VSPGVLIPRPETEELVEWALEaLLLKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGLGARVE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 160 FVCGAWYEAIPAQRFDLIVSNPPYIDADDVHMQH---LATEPRRALVADHQGLSDLEHIIKQAPQWLNIDGWLVLEHGYD 236
Cdd:PRK09328  162 FLQGDWFEPLPGGRFDLIVSNPPYIPEADIHLLQpevRDHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGWLLLEIGYD 241

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2527434988 237 QGNAVRQIFNAAGFAQMQTVKDYGGNDRISLGQ 269
Cdd:PRK09328  242 QGEAVRALLAAAGFADVETRKDLAGRDRVVLGR 274
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 20-267 6.29e-122

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: 347.92  E-value: 6.29e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  20 EAIWLLEHIVHLNALELRMRSLQVLSSEQEQAYLEGLVRLAQGEPLAYITGSQPFWSLDLIVTKDTLVPRPDTEILIETV 99
Cdd:TIGR03534   1 DAELLLAHVLGKDRAQLLLHPEDELTPEELAAFDALLARRAAGEPVAYILGEREFYGLDFKVSPGVLIPRPETEELVEAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 100 LELtLPKHSNVVDLGTGTGAIALSLAKERPDWRVLATDIYQPTLDIAAKNAQKHQLDRVEFVCGAWYEAIPAQRFDLIVS 179
Cdd:TIGR03534  81 LER-LKKGPRVLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKNARRLGLENVEFLQGDWFEPLPSGKFDLIVS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 180 NPPYIDADDVHMQH---LATEPRRALVADHQGLSDLEHIIKQAPQWLNIDGWLVLEHGYDQGNAVRQIFNAAGFAQMQTV 256
Cdd:TIGR03534 160 NPPYIPEADIHLLDpevRDFEPRLALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFEAAGFADVETR 239

                         250
                  ....*....|.
gi 2527434988 257 KDYGGNDRISL 267
Cdd:TIGR03534 240 KDLAGKDRVVL 250
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 1-271 4.86e-115

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 331.73  E-value: 4.86e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988   1 MNIAQALN-----LRGEPDSYERQEAIWLLEHIVHLNALELRMRSLQVLSSEQEQAYLEGLVRLAQGEPLAYITGSQPFW 75
Cdd:COG2890     1 MTIRELLRwaaarLAAAGVDSARLEAELLLAHVLGLDRADLLLHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  76 SLDLIVTKDTLVPRPDTEILIETVLE-LTLPKHSNVVDLGTGTGAIALSLAKERPDWRVLATDIYQPTLDIAAKNAQKHQ 154
Cdd:COG2890    81 GLEFKVDPGVLIPRPETEELVELALAlLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 155 L-DRVEFVCGAWYEAIPA-QRFDLIVSNPPYIDADDVH-MQH--LATEPRRALVADHQGLSDLEHIIKQAPQWLNIDGWL 229
Cdd:COG2890   161 LeDRVRFLQGDLFEPLPGdGRFDLIVSNPPYIPEDEIAlLPPevRDHEPRLALDGGEDGLDFYRRIIAQAPRLLKPGGWL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2527434988 230 VLEHGYDQGNAVRQIFNAAGFAQMQTVKDYGGNDRISLGQMK 271
Cdd:COG2890   241 LLEIGEDQGEAVRALLEAAGFADVETHKDLAGRDRVVVARRP 282
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 3-268 1.29e-73

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: 226.47  E-value: 1.29e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988   3 IAQALNLRGEPDSYERqEAIWLLEHIVHLNA-LELRMRSLQvLSSEQEQAYLEGLVRLAQGEPLAYITGSQPFWSLDLIV 81
Cdd:TIGR00536  10 ASSALSRAIARENPWL-EALLLLEHDLGRERdLLLAFLTEE-LTPDEKERIFRLVLRRVKGVPVAYLLGSKEFYGLEFFV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  82 TKDTLVPRPDTEILIETVLELTLPKHS--NVVDLGTGTGAIALSLAKERPDWRVLATDIYQPTLDIAAKNAQKHQL-DRV 158
Cdd:TIGR00536  88 NEHVLIPRPETEELVEKALASLISQPPilHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQLeHRV 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 159 EFVCGAWYEAIPAQRFDLIVSNPPYIDADDVHMQHLAT--EPRRALVADHQGLSDLEHIIKQAPQWLNIDGWLVLEHGYD 236
Cdd:TIGR00536 168 EFIQSNLFEPLAGQKIDIIVSNPPYIDEEDLADLPNVVrfEPLLALVGGDDGLNILRQIIELAPDYLKPNGFLVCEIGNW 247

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2527434988 237 Q-GNAVRQIFNAAGFAQMQTVKDYGGNDRISLG 268
Cdd:TIGR00536 248 QqKSLKELLRIKFTWYDVENGRDLNGKERVVLG 280
PRK14966 PRK14966
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; ...
 18-269 3.76e-51

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


Pssm-ID: 184930 [Multi-domain]  Cd Length: 423  Bit Score: 172.96  E-value: 3.76e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  18 RQEAIWLLEHIVHLNALELRMRSLQVLSSEQEQAYLEGLVRLAQGEPLAYITGSQPFWSLDLIVTKDTLVPRPDTEILIE 97
Cdd:PRK14966  164 KNEARMLLQYASEYTRVQLLTRGGEEMPDEVRQRADRLAQRRLNGEPVAYILGVREFYGRRFAVNPNVLIPRPETEHLVE 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  98 TVLElTLPKHSNVVDLGTGTGAIALSLAKERPDWRVLATDIYQPTLDIAAKNAQKHQLdRVEFVCGAWYEA-IPAQ-RFD 175
Cdd:PRK14966  244 AVLA-RLPENGRVWDLGTGSGAVAVTVALERPDAFVRASDISPPALETARKNAADLGA-RVEFAHGSWFDTdMPSEgKWD 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 176 LIVSNPPYIDADDVHMQH--LATEPRRALVADHQGLSDLEHIIKQAPQWLNIDGWLVLEHGYDQGNAVRQIFNAAGFAQM 253
Cdd:PRK14966  322 IIVSNPPYIENGDKHLLQgdLRFEPQIALTDFSDGLSCIRTLAQGAPDRLAEGGFLLLEHGFDQGAAVRGVLAENGFSGV 401

                         250
                  ....*....|....*.
gi 2527434988 254 QTVKDYGGNDRISLGQ 269
Cdd:PRK14966  402 ETLPDLAGLDRVTLGK 417
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
 20-265 1.68e-48

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


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 167.73  E-value: 1.68e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  20 EAIWLLEHIVHLNALELRMRSLQVLSSEQEQAYLEGLVRLAQGEPLAYITGSQPFWSLDLIVTKDTLVPRPDTEILIETV 99
Cdd:PRK01544   27 EARILLQHVINKPIEYLLINLDEQLNEAEIEAFEKLLERRLKHEPIAYITGVKEFYSREFIVNKHVLIPRSDTEVLVDVV 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 100 LELTL-------------------------PKHSNVVDLGTGTGAIALSLAKERPDWRVLATDIYQPTLDIAAKNAQKHQ 154
Cdd:PRK01544  107 FQCHSresgnpekkqlnpcfrgndissncnDKFLNILELGTGSGCIAISLLCELPNANVIATDISLDAIEVAKSNAIKYE 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 155 L-DRVEFVCGAWYEAIPAQRFDLIVSNPPYIDADD---VHMQHLATEPRRALVADHQGLSDLEHIIKQAPQWLNIDGWLV 230
Cdd:PRK01544  187 VtDRIQIIHSNWFENIEKQKFDFIVSNPPYISHSEkseMAIETINYEPSIALFAEEDGLQAYFIIAENAKQFLKPNGKII 266

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2527434988 231 LEHGYDQGNAVRQIFNAAGFAQMQTVKDYGGNDRI 265
Cdd:PRK01544  267 LEIGFKQEEAVTQIFLDHGYNIESVYKDLQGHSRV 301
L3_gln_methyl TIGR03533
protein-(glutamine-N5) methyltransferase, ribosomal protein L3-specific; Members of this ...
 20-234 9.58e-38

protein-(glutamine-N5) methyltransferase, ribosomal protein L3-specific; Members of this protein family methylate ribosomal protein L3 on a glutamine side chain. This family is related to HemK, a protein-glutamine methyltranferase for peptide chain release factors. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 274633 [Multi-domain]  Cd Length: 284  Bit Score: 134.18  E-value: 9.58e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  20 EAIWLLEHIVHL--NALElRMRSLQVLSSEQEQayLEGLV--RLAQGEPLAYITGSQPFWSLDLIVTKDTLVPRPDTEIL 95
Cdd:TIGR03533  32 EAVYLVLHALHLplDILE-PFLDARLTPSEKER--ILELIerRIEERIPVAYLTNEAWFAGLEFYVDERVLIPRSPIAEL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  96 IE----TVLELTLPKHsnVVDLGTGTGAIALSLAKERPDWRVLATDIYQPTLDIAAKNAQKHQL-DRVEFVCGAWYEAIP 170
Cdd:TIGR03533 109 IEdgfaPWLEPEPVKR--ILDLCTGSGCIAIACAYAFPEAEVDAVDISPDALAVAEINIERHGLeDRVTLIQSDLFAALP 186

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2527434988 171 AQRFDLIVSNPPYIDADDvhMQHLAT----EPRRALVADHQGLSDLEHIIKQAPQWLNIDGWLVLEHG 234
Cdd:TIGR03533 187 GRKYDLIVSNPPYVDAED--MADLPAeyhhEPELALASGEDGLDLVRRILAEAADHLNENGVLVVEVG 252
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 92-230 6.04e-26

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: 100.65  E-value: 6.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  92 TEILIETvleLTLPKHSNVVDLGTGTGAIALSLAKERPDWRVLATDIYQPTLDIAAKNAQKHQLDRVEFVCGAWYEAIPA 171
Cdd:COG2813    38 TRLLLEH---LPEPLGGRVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAANGLENVEVLWSDGLSGVPD 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2527434988 172 QRFDLIVSNPPYidaddvhmqhlateprralvadHQGLSD----LEHIIKQAPQWLNIDG--WLV 230
Cdd:COG2813   115 GSFDLILSNPPF----------------------HAGRAVdkevAHALIADAARHLRPGGelWLV 157
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 104-250 5.48e-22

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: 91.36  E-value: 5.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 104 LPKHSNVVDLGTGTGAIALSLAKERPDWRVLATDIyQPTL-DIAAKNAQKHQL-DRVEFVCG---AWYEAIPAQRFDLIV 178
Cdd:COG4123    35 VKKGGRVLDLGTGTGVIALMLAQRSPGARITGVEI-QPEAaELARRNVALNGLeDRITVIHGdlkEFAAELPPGSFDLVV 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2527434988 179 SNPPYIDADDVhmqHLATEPRRALvADHQGLSDLEHIIKQAPQWLNIDGWLVLEHGYDQGNAVRQIFNAAGF 250
Cdd:COG4123   114 SNPPYFKAGSG---RKSPDEARAI-ARHEDALTLEDLIRAAARLLKPGGRFALIHPAERLAEILAALRKYGL 181
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 92-246 1.73e-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: 85.72  E-value: 1.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  92 TEILIETvleLTLPKHSNVVDLGTGTGAIALSLAKERPDWRVLATDIYQPTLDIAAKNAQKHQLDRVEFVCGAWYEAIPA 171
Cdd:pfam05175  20 SRLLLEH---LPKDLSGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGLENGEVVASDVYSGVED 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2527434988 172 QRFDLIVSNPPYidaddvHmQHLATEPRRAlvadhqglsdlEHIIKQAPQWLNIDG--WLVLEH--GYDQgnAVRQIFN 246
Cdd:pfam05175  97 GKFDLIISNPPF------H-AGLATTYNVA-----------QRFIADAKRHLRPGGelWIVANRflGYPP--LLEELFG 155
PrmC_rel_meth TIGR03704
putative protein-(glutamine-N5) methyltransferase, unknown substrate-specific; This protein ...
 58-251 1.26e-18

putative protein-(glutamine-N5) methyltransferase, unknown substrate-specific; This protein family is closely related to two different families of protein-(glutamine-N5) methyltransferase. The first is PrmB, which modifies ribosomal protein L3 in some bacteria. The second is PrmC (HemK), which modifies peptide chain release factors 1 and 2 in most bacteria and also in eukaryotes. The glutamine side chain-binding motif NPPY shared by PrmB and PrmC is N[VAT]PY in this family. The protein substrate is unknown. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 274733 [Multi-domain]  Cd Length: 251  Bit Score: 82.52  E-value: 1.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  58 RLAQGEPLAYITGSQPFWSLDLIVTKDTLVPRPDTEILIETVLELT--LPKHSNVVDLGTGTGAIALSLAKERPDWRVLA 135
Cdd:TIGR03704  36 RRVAGLPLEHVLGWAEFCGLRIAVDPGVFVPRRRTEFLVDEAAALArpRSGTLVVVDLCCGSGAVGAALAAALDGIELHA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 136 TDIYQPTLDIAAKNAQKHQLDRVEfvcGAWYEAIPAQ---RFDLIVSNPPYIDADDVHM---QHLATEPRRALVADHQGL 209
Cdd:TIGR03704 116 ADIDPAAVRCARRNLADAGGTVHE---GDLYDALPTAlrgRVDILAANAPYVPTDAIALmppEARDHEPRVALDGGADGL 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2527434988 210 SDLEHIIKQAPQWLNIDGWLVLEHGYDQGNAVRQIFNAAGFA 251
Cdd:TIGR03704 193 DVLRRVAAGAPDWLAPGGHLLVETSERQAPLAVEAFARAGLI 234
PRK14967 PRK14967
putative methyltransferase; Provisional
 88-233 4.34e-18

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 80.48  E-value: 4.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  88 PRPDTEILIETVLELTLPKHSNVVDLGTGTGAIALSlAKERPDWRVLATDIYQPTLDIAAKNAQKHQLDrVEFVCGAWYE 167
Cdd:PRK14967   18 PQEDTQLLADALAAEGLGPGRRVLDLCTGSGALAVA-AAAAGAGSVTAVDISRRAVRSARLNALLAGVD-VDVRRGDWAR 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2527434988 168 AIPAQRFDLIVSNPPYIDADDvhMQHLATEPRRALVADHQGLSDLEHIIKQAPQWLNIDGWLVLEH 233
Cdd:PRK14967   96 AVEFRPFDVVVSNPPYVPAPP--DAPPSRGPARAWDAGPDGRAVLDRLCDAAPALLAPGGSLLLVQ 159
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 109-202 6.19e-15

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: 69.00  E-value: 6.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 109 NVVDLGTGTGAIALSLAkERPDWRVLATDIYQPTLDIAAKNAQKHQLDRVEFVCGAWYEAIPA--QRFDLIVSNPPYIDA 186
Cdd:cd02440     1 RVLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEadESFDVIISDPPLHHL 79

                          90
                  ....*....|....*.
gi 2527434988 187 DDVHMQHLAtEPRRAL 202
Cdd:cd02440    80 VEDLARFLE-EARRLL 94
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 92-182 2.31e-13

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: 69.05  E-value: 2.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  92 TEILIETVLE-LTLPKHSNVVDLGTGTGAIALSLAkeRPDWRVLATDIYQPTLDIAAKNAQKHQLDRVEFVCGAWYEAIP 170
Cdd:COG2265   218 AEALYAAALEwLDLTGGERVLDLYCGVGTFALPLA--RRAKKVIGVEIVPEAVEDARENARLNGLKNVEFVAGDLEEVLP 295

                          90
                  ....*....|....*.
gi 2527434988 171 AQ----RFDLIVSNPP 182
Cdd:COG2265   296 ELlwggRPDVVVLDPP 311
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
108-233 3.91e-13

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 63.69  E-value: 3.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 108 SNVVDLGTGTGAIALSLAKERPDWRVLATDIYQPTLDIAAKNaqkhqLDRVEFVCGAWYEAIPAQRFDLIVSNppyiDAd 187
Cdd:COG4106     3 RRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARAR-----LPNVRFVVADLRDLDPPEPFDLVVSN----AA- 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2527434988 188 dvhMQHLateprralvADHQGLsdLEHIIkqapQWLNIDGWLVLEH 233
Cdd:COG4106    73 ---LHWL---------PDHAAL--LARLA----AALAPGGVLAVQV 100
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 101-251 1.23e-12

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: 63.86  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 101 ELTLPKHSNVVDLGTGTGAIALSLAkeRPDWRVLATDIYQPTLDIAAKNAQKHQLdRVEFVCGAWYE-AIPAQRFDLIVS 179
Cdd:COG2226    17 ALGLRPGARVLDLGCGTGRLALALA--ERGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAEDlPFPDGSFDLVIS 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2527434988 180 NppyidaddvhmqhlateprraLVADHqgLSDLEHIIKQAPQWLNIDGWLVL-EHGYDQGNAVRQIFNAAGFA 251
Cdd:COG2226    94 S---------------------FVLHH--LPDPERALAEIARVLKPGGRLVVvDFSPPDLAELEELLAEAGFE 143
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 96-232 2.32e-12

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: 62.73  E-value: 2.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  96 IETVLELTLPKHSNVVDLGTGTGAIALSLAKErpDWRVLATDIYQPTLDIAAKNAQKHqldRVEFVCGAWYE-AIPAQRF 174
Cdd:COG2227    14 LAALLARLLPAGGRVLDVGCGTGRLALALARR--GADVTGVDISPEALEIARERAAEL---NVDFVQGDLEDlPLEDGSF 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2527434988 175 DLIVSNppyidadDVhMQHLAteprralvadhqglsDLEHIIKQAPQWLNIDGWLVLE 232
Cdd:COG2227    89 DLVICS-------EV-LEHLP---------------DPAALLRELARLLKPGGLLLLS 123
PrmC_N pfam17827
PrmC N-terminal domain; This entry corresponds to the N-terminal alpha helical domain of the ...
 4-70 1.07e-11

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: 59.03  E-value: 1.07e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2527434988   4 AQALNLRGEPDsyERQEAIWLLEHIVHLNALELRMRSLQVLSSEQEQAYLEGLVRLAQGEPLAYITG 70
Cdd:pfam17827   7 SSRLKEAGIES--PRLDAELLLAHVLGLDRTDLLLHPEEELSEEELERFEELLERRAAGEPLQYILG 71
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 110-204 2.50e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 58.73  E-value: 2.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 110 VVDLGTGTGAIALSLAKeRPDWRVLATDIYQPTLDIAAKNAQKHQLdRVEFVCGAwYEAIP--AQRFDLIVSNPPyidad 187
Cdd:pfam13649   1 VLDLGCGTGRLTLALAR-RGGARVTGVDLSPEMLERARERAAEAGL-NVEFVQGD-AEDLPfpDGSFDLVVSSGV----- 72

                          90
                  ....*....|....*..
gi 2527434988 188 dvhMQHLATEPRRALVA 204
Cdd:pfam13649  73 ---LHHLPDPDLEAALR 86
PRK14968 PRK14968
putative methyltransferase; Provisional
 84-184 3.95e-11

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 60.68  E-value: 3.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  84 DTLVPRPDTEILIETVLEltlPKHSNVVDLGTGTGAIALSLAKErpDWRVLATDIYQPTLDIAAKNAQKHQLDR--VEFV 161
Cdd:PRK14968    4 EVYEPAEDSFLLAENAVD---KKGDRVLEVGTGSGIVAIVAAKN--GKKVVGVDINPYAVECAKCNAKLNNIRNngVEVI 78

                          90       100
                  ....*....|....*....|...
gi 2527434988 162 CGAWYEAIPAQRFDLIVSNPPYI 184
Cdd:PRK14968   79 RSDLFEPFRGDKFDVILFNPPYL 101
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 103-204 4.80e-11

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 60.70  E-value: 4.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 103 TLPKHSNVVDLGTGTGAIALSLAkERPDWRVLATDIYQPTLDIAAKNAQKHQLDRVEFVCGAWYE--AIPAQRFDLIVSN 180
Cdd:COG0500    23 RLPKGGRVLDLGCGTGRNLLALA-ARFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAEldPLPAESFDLVVAF 101

                          90       100
                  ....*....|....*....|....
gi 2527434988 181 ppyidadDVHmQHLATEPRRALVA 204
Cdd:COG0500   102 -------GVL-HHLPPEEREALLR 117
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 106-249 2.50e-10

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 57.43  E-value: 2.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 106 KHSNVVDLGTGTGAIALSLAKE-RPDWRVLATDIYQPTLDIAAKNAQKHQLDRVEFVCGAWyEAIPA----QRFDLIVSN 180
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEElGPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDI-EELPElledDKFDVVISN 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2527434988 181 PPYIDADD-----VHMQHLATEPRRALVADHQGLSDLEHIIKqapQWLNIDGWLVLEHGydQGNAVRQIFNAAG 249
Cdd:pfam13847  82 CVLNHIPDpdkvlQEILRVLKPGGRLIISDPDSLAELPAHVK---EDSTYYAGCVGGAI--LKKKLYELLEEAG 150
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
103-229 3.51e-09

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


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 56.48  E-value: 3.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 103 TLPKH--SNVVDLGTGTGAIALSLAKERPDWRVLATDIYQPTLDIAAKNAQKHQLDRvEFVCGAWYEAIPAqRFDLIVSN 180
Cdd:PRK09489  191 TLTPHtkGKVLDVGCGAGVLSAVLARHSPKIRLTLSDVSAAALESSRATLAANGLEG-EVFASNVFSDIKG-RFDMIISN 268

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2527434988 181 PPYIDAddvhmqhLATEPRRAlvadhqglsdlEHIIKQAPQWLNIDGWL 229
Cdd:PRK09489  269 PPFHDG-------IQTSLDAA-----------QTLIRGAVRHLNSGGEL 299
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
110-182 8.51e-09

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 54.14  E-value: 8.51e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2527434988 110 VVDLGTGTG--AIALSL--AKerpdwRVLATDIYQPTLDIAAKNAQKHQlDRVEFVCgAWYEAIPAQ-RFDLIVSNPP 182
Cdd:COG2263    49 VLDLGCGTGmlAIGAALlgAK-----KVVGVDIDPEALEIARENAERLG-VRVDFIR-ADVTRIPLGgSVDTVVMNPP 119
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 102-179 9.90e-09

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: 9.90e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2527434988 102 LTLPKHSNVVDLGTGTGAIALSLAKERpDWRVLATDIYQPTLDIAAKNAQKHQL-DRVEFVCGAWYEAIPAQRFDLIVS 179
Cdd:COG2230    47 LGLKPGMRVLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAEAGLaDRVEVRLADYRDLPADGQFDAIVS 124
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
100-180 8.62e-08

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 52.10  E-value: 8.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 100 LELTLPKHSNVVDLGTGTG--AIALSL--AKerpdwRVLATDIYQPTLDIAAKNAQKHQL-DRVEFVCGawyEAIPAQRF 174
Cdd:COG2264   142 LEKLLKPGKTVLDVGCGSGilAIAAAKlgAK-----RVLAVDIDPVAVEAARENAELNGVeDRIEVVLG---DLLEDGPY 213


                  ....*.
gi 2527434988 175 DLIVSN 180
Cdd:COG2264   214 DLVVAN 219
PRK08317 PRK08317
hypothetical protein; Provisional
 89-202 3.56e-07

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 49.94  E-value: 3.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  89 RPDTEILIETVLELTLPKHSN-VVDLGTGTGAIALSLAKE-RPDWRVLATDIYQPTLDIaAKNAQKHQLDRVEFVCG-AW 165
Cdd:PRK08317    1 LPDFRRYRARTFELLAVQPGDrVLDVGCGPGNDARELARRvGPEGRVVGIDRSEAMLAL-AKERAAGLGPNVEFVRGdAD 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2527434988 166 YEAIPAQRFDLIVSnppyidaDDVhMQHLAtEPRRAL 202
Cdd:PRK08317   80 GLPFPDGSFDAVRS-------DRV-LQHLE-DPARAL 107
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 100-251 1.45e-06

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 47.04  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 100 LELTLPKHSNVVDLGTGTGAIALSLAKERPDwrVLATDIYQPTLDIAAKNAQKHQLDRVEfvcgawyEAIPAQRFDLIVS 179
Cdd:pfam13489  16 LLPKLPSPGRVLDFGCGTGIFLRLLRAQGFS--VTGVDPSPIAIERALLNVRFDQFDEQE-------AAVPAGKFDVIVA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 180 N------PPYIDAddvhMQHLAT---EPRRALVADHQGLSDLEHIIKQAPQWLNIDGWlvleHGYDQGNAVRQIFNAAGF 250
Cdd:pfam13489  87 RevlehvPDPPAL----LRQIAAllkPGGLLLLSTPLASDEADRLLLEWPYLRPRNGH----ISLFSARSLKRLLEEAGF 158


                  .
gi 2527434988 251 A 251
Cdd:pfam13489 159 E 159
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 88-188 1.79e-06

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


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 47.16  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  88 PRPDTEILIETVLELtlpKHSNVVDLGTGTGAIALSLAKERPdwRVLATDIYQPTLDIAAKNAQKHQLDrVEFVCGAWYE 167
Cdd:TIGR00537   4 PAEDSLLLEANLREL---KPDDVLEIGAGTGLVAIRLKGKGK--CILTTDINPFAVKELRENAKLNNVG-LDVVMTDLFK 77

                          90       100
                  ....*....|....*....|.
gi 2527434988 168 AIpAQRFDLIVSNPPYIDADD 188
Cdd:TIGR00537  78 GV-RGKFDVILFNPPYLPLED 97
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 109-187 3.12e-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: 46.33  E-value: 3.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 109 NVVDLGTGTGAIALSLAKE-RPDWRVLATDIYQPTLDIAAKNAQKHQL-DRVEFVCGAWYEAIPA---QRFDLIvsnppY 183
Cdd:COG4122    19 RILEIGTGTGYSTLWLARAlPDDGRLTTIEIDPERAAIARENFARAGLaDRIRLILGDALEVLPRladGPFDLV-----F 93


                  ....
gi 2527434988 184 IDAD 187
Cdd:COG4122    94 IDAD 97
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 108-233 3.25e-06

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: 46.23  E-value: 3.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 108 SNVVDLGTGTGAI---ALSL-AKerpdwRVLATDIYQPTLDIAAKNAQKHQL-DRVEFVCG---AWYEAIPAQRFDLIVS 179
Cdd:COG0742    43 ARVLDLFAGSGALgleALSRgAA-----SVVFVEKDRKAAAVIRKNLEKLGLeDRARVIRGdalRFLKRLAGEPFDLVFL 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2527434988 180 NPPYidaddvhmqhlateprralvadHQGLSD--LEHIIKQapQWLNIDGWLVLEH 233
Cdd:COG0742   118 DPPY----------------------AKGLLEkaLELLAEN--GLLAPGGLIVVEH 149
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
93-256 3.73e-06

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 46.14  E-value: 3.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  93 EILIETVLELTLPKHSNVVDLGTGTGAIALSLAKERpdWRVLATDIYQPTLDIAAKNAQKHQLDRVEFVCGAWyeaiPAQ 172
Cdd:COG4976    33 LLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRG--YRLTGVDLSEEMLAKAREKGVYDRLLVADLADLAE----PDG 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 173 RFDLIVSNppyidadDVhMQHLAteprralvadhqglsDLEHIIKQAPQWLNIDGWLVL-------EHGYDQG-NAVRQI 244
Cdd:COG4976   107 RFDLIVAA-------DV-LTYLG---------------DLAAVFAGVARALKPGGLFIFsvedadgSGRYAHSlDYVRDL 163

                         170
                  ....*....|..
gi 2527434988 245 FNAAGFAQMQTV 256
Cdd:COG4976   164 LAAAGFEVPGLL 175
PRK15001 PRK15001
23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;
110-197 8.17e-06

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


Pssm-ID: 184963 [Multi-domain]  Cd Length: 378  Bit Score: 46.56  E-value: 8.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 110 VVDLGTGTGAIALSLAKERPDWRVLATDIYQPTLDIAAKNAQKH---QLDRVEFVCGAWYEAIPAQRFDLIVSNPPYida 186
Cdd:PRK15001  232 IVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNmpeALDRCEFMINNALSGVEPFRFNAVLCNPPF--- 308

                          90
                  ....*....|.
gi 2527434988 187 ddvHMQHLATE 197
Cdd:PRK15001  309 ---HQQHALTD 316
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 111-202 8.95e-06

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 43.42  E-value: 8.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 111 VDLGTGTGAIALSLAKERPdwRVLATDIYQPTLDIAAKNAQKhqlDRVEFVCGAwYEAIP--AQRFDLIVSNppyidadd 188
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMLELAREKAPR---EGLTFVVGD-AEDLPfpDNSFDLVLSS-------- 66

                          90
                  ....*....|....
gi 2527434988 189 vHMQHLATEPRRAL 202
Cdd:pfam08241  67 -EVLHHVEDPERAL 79
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 108-178 1.49e-05

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


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 45.15  E-value: 1.49e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2527434988 108 SNVVDLGTGTGAIALSLAKE-RPDWRVLATDIYQPTLDIAAKNAQKHQL-DRVEFVCGAWYEAIPAQRFDLIV 178
Cdd:COG2519    93 ARVLEAGTGSGALTLALARAvGPEGKVYSYERREDFAEIARKNLERFGLpDNVELKLGDIREGIDEGDVDAVF 165
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
100-250 4.37e-05

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 43.60  E-value: 4.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 100 LELTLPKHSNVVDLGTGTG--AIALSL--AKErpdwrVLATDIYQPTLDIAAKNAQKHQLDRVEFVCGAwyeaipAQRFD 175
Cdd:PRK00517  113 LEKLVLPGKTVLDVGCGSGilAIAAAKlgAKK-----VLAVDIDPQAVEAARENAELNGVELNVYLPQG------DLKAD 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2527434988 176 LIVSNppyIdaddvhmqhLAtEPrralvadhqglsdLEHIIKQAPQWLNIDGWLVLEhG--YDQGNAVRQIFNAAGF 250
Cdd:PRK00517  182 VIVAN---I---------LA-NP-------------LLELAPDLARLLKPGGRLILS-GilEEQADEVLEAYEEAGF 231
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 101-170 4.88e-05

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: 44.00  E-value: 4.88e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 101 ELTLPKHSNVVDLGTGTGAIALSLAKERPDWRVLATDIYQPTLDIAAKNAQKHQLDRVEFVCGAWYEAIP 170
Cdd:COG2242   242 KLALRPGDVLWDIGAGSGSVSIEAARLAPGGRVYAIERDPERAALIRANARRFGVPNVEVVEGEAPEALA 311
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 111-180 5.05e-05

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 41.20  E-value: 5.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2527434988 111 VDLGTGTGAIALSLAKERPDWRVLATDIYQPTLDIAAKNAQKHQLDRVEFVCGAWYEAI--PAQRFDLIVSN 180
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGelDPGSFDVVVAS 72
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 95-180 8.14e-05

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: 43.04  E-value: 8.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  95 LIETVLELTLPKHSNVVDLGTGTGAIALSLAKERPDWRVLATDIYQPTLDIaaknAQKHQLDRVEFVCG-AWYEAIPAQR 173
Cdd:TIGR02072  23 LLALLKEKGIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQ----AKTKLSENVQFICGdAEKLPLEDSS 98


                  ....*..
gi 2527434988 174 FDLIVSN 180
Cdd:TIGR02072  99 FDLIVSN 105
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 109-178 1.23e-04

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: 41.55  E-value: 1.23e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2527434988 109 NVVDLGTGTGAIALSLAKERPDWRVLATDiYQPTLDIAAKNAQKHQL-DRVEFVCGAWYEAIP-----AQRFDLIV 178
Cdd:pfam10294  49 NVLELGSGTGLVGIAVALLLPGASVTITD-LEEALELLKKNIELNALsSKVVVKVLDWGENLPpdlfdGHPVDLIL 123
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 97-177 5.68e-04

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 40.14  E-value: 5.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988  97 ETVLELTLPKHSNVVDLGTGTGAIALSLAKE-RPDWRVLATDIYQPTLDIAAKNAQKHQL-DRVEFVCG-AwyEAIP--A 171
Cdd:PRK00216   42 KTIKWLGVRPGDKVLDLACGTGDLAIALAKAvGKTGEVVGLDFSEGMLAVGREKLRDLGLsGNVEFVQGdA--EALPfpD 119


                  ....*.
gi 2527434988 172 QRFDLI 177
Cdd:PRK00216  120 NSFDAV 125
arsM PRK11873
arsenite methyltransferase;
110-180 6.26e-04

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 40.32  E-value: 6.26e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2527434988 110 VVDLGTGTGAIALsLAKER--PDWRVLATDIYQPTLDIAAKNAQKHQLDRVEFVCGAwYEAIP--AQRFDLIVSN 180
Cdd:PRK11873   81 VLDLGSGGGFDCF-LAARRvgPTGKVIGVDMTPEMLAKARANARKAGYTNVEFRLGE-IEALPvaDNSVDVIISN 153
Methyltransf_4 pfam02390
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ...
 110-163 7.20e-04

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: 39.58  E-value: 7.20e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2527434988 110 VVDLGTGTGAIALSLAKERPDWRVLATDIYQPTLDIAAKNAQKHQLDRVEFVCG 163
Cdd:pfam02390   5 FLEIGCGMGGFLVAMAKANPDKNFIGIEIRVPGVAKALKKIDALGLQNLRILCG 58
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 121-183 8.21e-04

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


Pssm-ID: 439886 [Multi-domain]  Cd Length: 369  Bit Score: 40.08  E-value: 8.21e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2527434988 121 ALSLAKERPDWRVLATDIYQPTLDIAAKNAQKHQL-DRVEFVCGAWYEAIPAQRFDLIVSNPPY 183
Cdd:COG0116   241 AEARIKRDPPLPIFGSDIDPRAIEAARENAERAGVaDLIEFEQADFRDLEPPAEPGLIITNPPY 304
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
102-163 8.80e-04

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


Pssm-ID: 181354  Cd Length: 187  Bit Score: 39.21  E-value: 8.80e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2527434988 102 LTLPKHSNVVDLGTGTGAIALSLAKERPDWRVLATDIYQPTLDIAAKNAQKHQLDRVEFVCG 163
Cdd:PRK08287   27 LELHRAKHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKENRQRFGCGNIDIIPG 88
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 109-180 1.11e-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: 1.11e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2527434988 109 NVVDLGTGTG--AIALSL--AKErpdwrVLATDIYQPTLDIAAKNAQKHQLDRVEFVCGAWyeAIPAQRFDLIVSN 180
Cdd:pfam06325 164 SVLDVGCGSGilAIAALKlgAKK-----VVGVDIDPVAVRAAKENAELNGVEARLEVYLPG--DLPKEKADVVVAN 232
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
110-179 1.45e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 38.86  E-value: 1.45e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2527434988 110 VVDLGTGTGAIALSLAKERPDwRVLATDIYQPTLDIAAKNAQKHQL-DRVEFVCGAWYEAIPAQRFDLIVS 179
Cdd:COG4076    39 VLDIGTGSGLLSMLAARAGAK-KVYAVEVNPDIAAVARRIIAANGLsDRITVINADATDLDLPEKADVIIS 108
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 114-183 2.05e-03

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


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 38.01  E-value: 2.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2527434988 114 GTGTGAI-ALSLAkerpdWRVLATDIYQPTLDIAAKNAQKHQLDRVEFVCG-AWYEAIPAQRFDLIVSNPPY 183
Cdd:COG1041    36 GTGTILIeAGLLG-----RRVIGSDIDPKMVEGARENLEHYGYEDADVIRGdARDLPLADESVDAIVTDPPY 102
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 114-183 3.40e-03

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


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 37.72  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 114 GTGTGAI---------ALSLAKERPDWRVLATDIYQPTLDIAAKNAQKHQL-DRVEFVCG-AWYEAIPAQRFDLIVSNPP 182
Cdd:pfam01170  38 GSGTILIeaalmganiAPGKFDARVRAPLYGSDIDRRMVQGARLNAENAGVgDLIEFVQAdAADLPLLEGSVDVIVTNPP 117


                  .
gi 2527434988 183 Y 183
Cdd:pfam01170 118 Y 118
trmB PRK00121
tRNA (guanine-N(7)-)-methyltransferase; Reviewed
 110-163 4.11e-03

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


Pssm-ID: 234649  Cd Length: 202  Bit Score: 37.45  E-value: 4.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2527434988 110 VVDLGTGTGAIALSLAKERPDWRVLATDIYQPTLDIAAKNAQKHQLDRVEFVCG 163
Cdd:PRK00121   44 HLEIGFGKGEFLVEMAKANPDINFIGIEVHEPGVGKALKKIEEEGLTNLRLLCG 97
Methyltransf_15 pfam09445
RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as ...
 110-183 4.65e-03

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


Pssm-ID: 370496  Cd Length: 165  Bit Score: 36.93  E-value: 4.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434988 110 VVDLGTGTGAIALSLAKERPdwRVLATDIYQPTLDIAAKNAQKHQ-LDRVEFVCGAWYEAIPAQRF-----DLIVSNPPY 183
Cdd:pfam09445   4 ILDVFCGGGGNTIQFANVFD--SVISIDINLEHLACAQHNAEVYGvSDRIWLIHGDWFELLAKLKFekikyDCVFASPPW 81
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 132-182 9.55e-03

23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 37.08  E-value: 9.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2527434988 132 RVLATDIYQPTLDIAAKNAQKHQL-DRVEFVCG---AW--YEAIPAQRFDLIVSNPP 182
Cdd:COG1092   241 SVTSVDLSATALEWAKENAALNGLdDRHEFVQAdafDWlrELAREGERFDLIILDPP 297
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH