NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1907172882|ref|XP_036022115|]
View 

electron transfer flavoprotein beta subunit lysine methyltransferase isoform X1 [Mus musculus]

Protein Classification

methyltransferase( domain architecture ID 10008106)

S-adenosyl-L-methionine (SAM)-dependent methyltransferase similar to Saccharomyces cerevisiae protein N-methyltransferase NNT1, which is involved in rDNA silencing and in lifespan determination

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 56-255 4.55e-50

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: 163.52  E-value: 4.55e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172882  56 LTPEIQLRLLTPRCKFWwERADLWPY----SDPYWAIYWPGGQALSRYLLDNPAVvRGKSVLDLGSGCGATAIAAKMSGA 131
Cdd:COG3897    16 LVPEIRLHLAADAHPLW-DATEEALGesgaPPPFWAFLWPSGQALARYLLDHPEV-AGKRVLELGCGLGLVGIAAAKAGA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172882 132 SKILANDIDPIAGMAITLNCKLNGLnPFPVLTKNILNTQ-QGKFDLIVLGDMFYDEDLADSLHLWLQNyFWTHGTRVLIG 210
Cdd:COG3897    94 ADVTATDYDPEALAALRLNAALNGV-AITTRLGDWRDPPaAGGFDLILGGDVLYERDLAEPLLPFLDR-LAAPGGEVLIG 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907172882 211 DPGRPQFsgHSIRHQLYQLVEYTLPEPTQQENNGLTTSAVWDFHP 255
Cdd:COG3897   172 DPGRGYL--PAFRERLEALAGYEVVTRELEDTEKVKRGRVLRLRR 214
 
Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 56-255 4.55e-50

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: 163.52  E-value: 4.55e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172882  56 LTPEIQLRLLTPRCKFWwERADLWPY----SDPYWAIYWPGGQALSRYLLDNPAVvRGKSVLDLGSGCGATAIAAKMSGA 131
Cdd:COG3897    16 LVPEIRLHLAADAHPLW-DATEEALGesgaPPPFWAFLWPSGQALARYLLDHPEV-AGKRVLELGCGLGLVGIAAAKAGA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172882 132 SKILANDIDPIAGMAITLNCKLNGLnPFPVLTKNILNTQ-QGKFDLIVLGDMFYDEDLADSLHLWLQNyFWTHGTRVLIG 210
Cdd:COG3897    94 ADVTATDYDPEALAALRLNAALNGV-AITTRLGDWRDPPaAGGFDLILGGDVLYERDLAEPLLPFLDR-LAAPGGEVLIG 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907172882 211 DPGRPQFsgHSIRHQLYQLVEYTLPEPTQQENNGLTTSAVWDFHP 255
Cdd:COG3897   172 DPGRGYL--PAFRERLEALAGYEVVTRELEDTEKVKRGRVLRLRR 214
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 94-178 2.32e-12

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: 65.36  E-value: 2.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172882  94 QALSRYLLDnpavvrGKSVLDLGSGCGATAIAAKMSGASKILANDIDPIAGMAITLNCKLNGLNP-FPVltKNILNTQQG 172
Cdd:pfam06325 153 EALERLVKP------GESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEArLEV--YLPGDLPKE 224


                  ....*.
gi 1907172882 173 KFDLIV 178
Cdd:pfam06325 225 KADVVV 230
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
94-178 4.08e-12

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 64.02  E-value: 4.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172882  94 QALSRYLLdnpavvRGKSVLDLGSGCGATAIAAKMSGASKILANDIDPIAGMAITLNCKLNGlnpfpVLTKNILNTQQGK 173
Cdd:PRK00517  111 EALEKLVL------PGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNG-----VELNVYLPQGDLK 179


                  ....*
gi 1907172882 174 FDLIV 178
Cdd:PRK00517  180 ADVIV 184
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 112-199 7.76e-05

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: 40.88  E-value: 7.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172882 112 VLDLGSGCGATAIAAKMSGASKILANDIDPIAGMAITLNCKLNGLNPFPVLTKNILNTQQ---GKFDLIVLGDMFydEDL 188
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeadESFDVIISDPPL--HHL 79

                          90
                  ....*....|.
gi 1907172882 189 ADSLHLWLQNY 199
Cdd:cd02440    80 VEDLARFLEEA 90
 
Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 56-255 4.55e-50

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: 163.52  E-value: 4.55e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172882  56 LTPEIQLRLLTPRCKFWwERADLWPY----SDPYWAIYWPGGQALSRYLLDNPAVvRGKSVLDLGSGCGATAIAAKMSGA 131
Cdd:COG3897    16 LVPEIRLHLAADAHPLW-DATEEALGesgaPPPFWAFLWPSGQALARYLLDHPEV-AGKRVLELGCGLGLVGIAAAKAGA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172882 132 SKILANDIDPIAGMAITLNCKLNGLnPFPVLTKNILNTQ-QGKFDLIVLGDMFYDEDLADSLHLWLQNyFWTHGTRVLIG 210
Cdd:COG3897    94 ADVTATDYDPEALAALRLNAALNGV-AITTRLGDWRDPPaAGGFDLILGGDVLYERDLAEPLLPFLDR-LAAPGGEVLIG 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907172882 211 DPGRPQFsgHSIRHQLYQLVEYTLPEPTQQENNGLTTSAVWDFHP 255
Cdd:COG3897   172 DPGRGYL--PAFRERLEALAGYEVVTRELEDTEKVKRGRVLRLRR 214
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
94-178 3.39e-13

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 67.51  E-value: 3.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172882  94 QALSRYLLdnpavvRGKSVLDLGSGCGATAIAAKMSGASKILANDIDPIAGMAITLNCKLNGL-NPFPVLTKNILntQQG 172
Cdd:COG2264   140 EALEKLLK------PGKTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVeDRIEVVLGDLL--EDG 211


                  ....*.
gi 1907172882 173 KFDLIV 178
Cdd:COG2264   212 PYDLVV 217
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 94-178 2.32e-12

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: 65.36  E-value: 2.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172882  94 QALSRYLLDnpavvrGKSVLDLGSGCGATAIAAKMSGASKILANDIDPIAGMAITLNCKLNGLNP-FPVltKNILNTQQG 172
Cdd:pfam06325 153 EALERLVKP------GESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEArLEV--YLPGDLPKE 224


                  ....*.
gi 1907172882 173 KFDLIV 178
Cdd:pfam06325 225 KADVVV 230
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
94-178 4.08e-12

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 64.02  E-value: 4.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172882  94 QALSRYLLdnpavvRGKSVLDLGSGCGATAIAAKMSGASKILANDIDPIAGMAITLNCKLNGlnpfpVLTKNILNTQQGK 173
Cdd:PRK00517  111 EALEKLVL------PGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNG-----VELNVYLPQGDLK 179


                  ....*
gi 1907172882 174 FDLIV 178
Cdd:PRK00517  180 ADVIV 184
PRK14968 PRK14968
putative methyltransferase; Provisional
 100-178 1.60e-08

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 52.98  E-value: 1.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172882 100 LLDNPAVVRGKSVLDLGSGCGATAIAAKMSGAsKILANDIDPIAGMAITLNCKLNGLNPFPV------LTKNILNtqqGK 173
Cdd:PRK14968   15 LAENAVDKKGDRVLEVGTGSGIVAIVAAKNGK-KVVGVDINPYAVECAKCNAKLNNIRNNGVevirsdLFEPFRG---DK 90


                  ....*
gi 1907172882 174 FDLIV 178
Cdd:PRK14968   91 FDVIL 95
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
107-141 1.22e-07

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 50.67  E-value: 1.22e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1907172882 107 VRGKSVLDLGSGCGATAIAAKMSGASKILANDIDP 141
Cdd:COG2263    44 IEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDIDP 78
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 90-192 1.28e-07

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: 50.02  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172882  90 WPGGQALSRYLL------DNPAVVRGKSVLDLGSGCGATAIA-AKMSGASKILANDIDPIAGMaITLNCKLNGLNP---F 159
Cdd:pfam10294  22 WDAAVVLSKYLEmkifkeLGANNLSGLNVLELGSGTGLVGIAvALLLPGASVTITDLEEALEL-LKKNIELNALSSkvvV 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907172882 160 PVLT--KNI--LNTQQGKFDLIVLGDMFYDED----LADSL 192
Cdd:pfam10294 101 KVLDwgENLppDLFDGHPVDLILAADCVYNEDsfplLEKTL 141
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 97-178 1.61e-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: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172882  97 SRYLLDN-PAVVRGKsVLDLGSGCGATAIA-AKMSGASKILANDIDPiagMAITL---NCKLNGLNPFPVLTKNIL-NTQ 170
Cdd:COG2813    38 TRLLLEHlPEPLGGR-VLDLGCGYGVIGLAlAKRNPEARVTLVDVNA---RAVELaraNAAANGLENVEVLWSDGLsGVP 113


                  ....*...
gi 1907172882 171 QGKFDLIV 178
Cdd:COG2813   114 DGSFDLIL 121
PRK04338 PRK04338
N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional
 111-177 4.98e-07

N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional


Pssm-ID: 235286  Cd Length: 382  Bit Score: 49.91  E-value: 4.98e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172882 111 SVLDLGSGCGATAI-AAKMSGASKILANDIDPIAGMAITLNCKLNGLNPFPVLTK--NILNTQQGKFDLI 177
Cdd:PRK04338   60 SVLDALSASGIRGIrYALETGVEKVTLNDINPDAVELIKKNLELNGLENEKVFNKdaNALLHEERKFDVV 129
PRK14967 PRK14967
putative methyltransferase; Provisional
 106-156 8.81e-07

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 48.51  E-value: 8.81e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907172882 106 VVRGKSVLDLGSGCGATAIAAKMSGASKILANDIDPIAGMAITLNCKLNGL 156
Cdd:PRK14967   34 LGPGRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNALLAGV 84
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 108-178 5.91e-06

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: 45.91  E-value: 5.91e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907172882 108 RGKSVLDLGSGCGATAIA-AKMSGASKILANDIDPI-AGMAiTLNCKLNGLNP-FPVLTKNILN----TQQGKFDLIV 178
Cdd:COG4123    37 KGGRVLDLGTGTGVIALMlAQRSPGARITGVEIQPEaAELA-RRNVALNGLEDrITVIHGDLKEfaaeLPPGSFDLVV 113
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 97-178 7.20e-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: 44.89  E-value: 7.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172882  97 SRYLLDNPAVVRGKSVLDLGSGCGA-TAIAAKMSGASKILANDIDPIAGMAITLNCKLNGLNPFPVLTKNIL-NTQQGKF 174
Cdd:pfam05175  20 SRLLLEHLPKDLSGKVLDLGCGAGVlGAALAKESPDAELTMVDINARALESARENLAANGLENGEVVASDVYsGVEDGKF 99


                  ....
gi 1907172882 175 DLIV 178
Cdd:pfam05175 100 DLII 103
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 101-178 1.67e-05

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 45.15  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172882 101 LDNPAVVRGKSVLDLGSGCGATAIA-AKMSGASKILANDIDPIAgMAITL-NCKLNGLNPFPVLTKNILNT-QQGKFDLI 177
Cdd:PRK09328  101 LEALLLKEPLRVLDLGTGSGAIALAlAKERPDAEVTAVDISPEA-LAVARrNAKHGLGARVEFLQGDWFEPlPGGRFDLI 179


                  .
gi 1907172882 178 V 178
Cdd:PRK09328  180 V 180
TRM1 COG1867
tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N, ...
 108-177 1.73e-05

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


Pssm-ID: 441472  Cd Length: 383  Bit Score: 45.25  E-value: 1.73e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907172882 108 RGKSVLDLGSGCGATAI-AAKMSGAsKILANDIDPIAGMAITLNCKLNGLNPFPVLTKN---ILNTQQGKFDLI 177
Cdd:COG1867    57 REISYLDALAASGIRGLrYALEVGI-KVTLNDIDPEAVELIRENLELNGLEDVEVYNRDanaLLHELGRRFDVV 129
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 108-178 2.47e-05

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 44.37  E-value: 2.47e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907172882 108 RGKSVLDLGSGCGATAIA-AKMSGASKILANDIDPIAgMAIT-LNCKLNGL-NPFPVLTKNILN--TQQGKFDLIV 178
Cdd:COG2890   112 APPRVLDLGTGSGAIALAlAKERPDARVTAVDISPDA-LAVArRNAERLGLeDRVRFLQGDLFEplPGDGRFDLIV 186
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 82-212 5.72e-05

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


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 41.54  E-value: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172882  82 SDPYWAIYWPggQALSRYLldNPAVVRGKSVLDLGSGCGATAIAAKMSGAsKILAndIDPIAGMAITLNCKLNGLNPfPV 161
Cdd:COG2227     2 SDPDARDFWD--RRLAALL--ARLLPAGGRVLDVGCGTGRLALALARRGA-DVTG--VDISPEALEIARERAAELNV-DF 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907172882 162 LTKNI--LNTQQGKFDLIVLGDMFY----DEDLADSLHLWLQnyfwtHGTRVLIGDP 212
Cdd:COG2227    74 VQGDLedLPLEDGSFDLVICSEVLEhlpdPAALLRELARLLK-----PGGLLLLSTP 125
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 112-199 7.76e-05

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: 40.88  E-value: 7.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172882 112 VLDLGSGCGATAIAAKMSGASKILANDIDPIAGMAITLNCKLNGLNPFPVLTKNILNTQQ---GKFDLIVLGDMFydEDL 188
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeadESFDVIISDPPL--HHL 79

                          90
                  ....*....|.
gi 1907172882 189 ADSLHLWLQNY 199
Cdd:cd02440    80 VEDLARFLEEA 90
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 107-179 1.86e-04

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: 42.09  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172882 107 VRGKSVLDLGSGCGATAIAAKMSGASKILAndIDpIAGMAITL---NCKLNGLNP---------FPVLTKniLNTQQGKF 174
Cdd:COG1092   215 AKGKRVLNLFSYTGGFSVHAAAGGAKSVTS--VD-LSATALEWakeNAALNGLDDrhefvqadaFDWLRE--LAREGERF 289


                  ....*
gi 1907172882 175 DLIVL 179
Cdd:COG1092   290 DLIIL 294
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
105-141 2.50e-04

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 41.43  E-value: 2.50e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907172882 105 AVVRGKSVLDLGSGCGATAIAAKMSGASKILANDIDP 141
Cdd:COG2521   129 GVRRGDRVLDTCTGLGYTAIEALKRGAREVITVEKDP 165
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 85-195 3.10e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 40.67  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172882  85 YWAIYWPGGQA--LSRYLLDNPAVVRGKSVLDLGSGCGATAIAAKMSGASKILANDIDPIagmAITL---NCKLNGLNPF 159
Cdd:COG0500     1 PWDSYYSDELLpgLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPE---AIALaraRAAKAGLGNV 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907172882 160 PVLTKNILNTQ---QGKFDLIVLGDMFYDEDLADSLHLW 195
Cdd:COG0500    78 EFLVADLAELDplpAESFDLVVAFGVLHHLPPEEREALL 116
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 107-141 5.67e-04

Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)- dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria) and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.


Pssm-ID: 176184 [Multi-domain]  Cd Length: 341  Bit Score: 40.68  E-value: 5.67e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907172882 107 VRGKSVLDLGSG-CGATAIA-AKMSGASKILANDIDP 141
Cdd:cd05281   162 VSGKSVLITGCGpIGLMAIAvAKAAGASLVIASDPNP 198
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 79-212 6.75e-04

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 39.14  E-value: 6.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172882  79 WPYSDPYWAIYWPGG--------QALSRYLLDNPAVVRGKSVLDLGSGCGATAI-AAKMSGAsKILANDIDPIAGMAITL 149
Cdd:COG2230    14 LDPTMTYSCAYFEDPddtleeaqEAKLDLILRKLGLKPGMRVLDIGCGWGGLALyLARRYGV-RVTGVTLSPEQLEYARE 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907172882 150 NCKLNGL-NPFPVLTKNILNTQ-QGKFDLIVLGDMF------YDEDLADSLHLWLqnyfwTHGTRVLIGDP 212
Cdd:COG2230    93 RAAEAGLaDRVEVRLADYRDLPaDGQFDAIVSIGMFehvgpeNYPAYFAKVARLL-----KPGGRLLLHTP 158
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 109-186 1.75e-03

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


Pssm-ID: 442010 [Multi-domain]  Cd Length: 333  Bit Score: 39.07  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172882 109 GKSVLDLGSGCGATAI-AAKMSGAsKILANDIDPIAGMAITLNCKLNGL--NPFPVLT--KNILNTQQGKFDLIVLG--- 180
Cdd:COG2520   181 GERVLDMFAGVGPFSIpIAKRSGA-KVVAIDINPDAVEYLKENIRLNKVedRVTPILGdaREVAPELEGKADRIIMNlph 259


                  ....*...
gi 1907172882 181 --DMFYDE 186
Cdd:COG2520   260 saDEFLDA 267
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 112-193 6.01e-03

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 35.23  E-value: 6.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172882 112 VLDLGSGCGATAIAAKMSGASKILANDIDPIAGMAITLNCKLNGLN-----------PFPvltknilntqQGKFDLIVLG 180
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNvefvqgdaedlPFP----------DGSFDLVVSS 70

                          90
                  ....*....|....*.
gi 1907172882 181 DMFY---DEDLADSLH 193
Cdd:pfam13649  71 GVLHhlpDPDLEAALR 86
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
105-157 6.14e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 36.94  E-value: 6.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907172882 105 AVVRGKSVLDLGSGCGATAIAAKMSGASKILANDIDP-IAGMAITlNCKLNGLN 157
Cdd:COG4076    32 VVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPdIAAVARR-IIAANGLS 84
 
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