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Conserved domains on  [gi|1907172885|ref|XP_036022116|]
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electron transfer flavoprotein beta subunit lysine methyltransferase isoform X2 [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

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List of domain hits

Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
56-156 1.47e-32

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: 115.75  E-value: 1.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172885  56 LTPEIQLRLLTPRCKFWwERADLWPY----SDPYWAIYWPGGQALSRYLLDNPAVvRGKSVLDLGSGCGATAIAAKMSGA 131
Cdd:COG3897    16 LVPEIRLHLAADAHPLW-DATEEALGesgaPPPFWAFLWPSGQALARYLLDHPEV-AGKRVLELGCGLGLVGIAAAKAGA 93
                          90       100
                  ....*....|....*....|....*
gi 1907172885 132 SKILANDIDPIAGMAITLNCKLNGL 156
Cdd:COG3897    94 ADVTATDYDPEALAALRLNAALNGV 118
 
Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
56-156 1.47e-32

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: 115.75  E-value: 1.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172885  56 LTPEIQLRLLTPRCKFWwERADLWPY----SDPYWAIYWPGGQALSRYLLDNPAVvRGKSVLDLGSGCGATAIAAKMSGA 131
Cdd:COG3897    16 LVPEIRLHLAADAHPLW-DATEEALGesgaPPPFWAFLWPSGQALARYLLDHPEV-AGKRVLELGCGLGLVGIAAAKAGA 93
                          90       100
                  ....*....|....*....|....*
gi 1907172885 132 SKILANDIDPIAGMAITLNCKLNGL 156
Cdd:COG3897    94 ADVTATDYDPEALAALRLNAALNGV 118
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
94-167 8.19e-11

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 59.01  E-value: 8.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172885  94 QALSRYLLdnpavvRGKSVLDLGSGCGATAIAAKMSGASKILANDIDPIAGMAITLNCKLNGLN----------PFPVLT 163
Cdd:PRK00517  111 EALEKLVL------PGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGVElnvylpqgdlKADVIV 184

                  ....
gi 1907172885 164 KNIL 167
Cdd:PRK00517  185 ANIL 188
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
94-167 1.78e-10

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: 58.43  E-value: 1.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172885  94 QALSRYLLDnpavvrGKSVLDLGSGCGATAIAAKMSGASKILANDIDPIAGMAITLNCKLNGLN--------------PF 159
Cdd:pfam06325 153 EALERLVKP------GESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEarlevylpgdlpkeKA 226

                  ....*...
gi 1907172885 160 PVLTKNIL 167
Cdd:pfam06325 227 DVVVANIL 234
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
107-141 2.51e-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: 2.51e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907172885 107 VRGKSVLDLGSG-CGATAIA-AKMSGASKILANDIDP 141
Cdd:cd05281   162 VSGKSVLITGCGpIGLMAIAvAKAAGASLVIASDPNP 198
 
Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
56-156 1.47e-32

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: 115.75  E-value: 1.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172885  56 LTPEIQLRLLTPRCKFWwERADLWPY----SDPYWAIYWPGGQALSRYLLDNPAVvRGKSVLDLGSGCGATAIAAKMSGA 131
Cdd:COG3897    16 LVPEIRLHLAADAHPLW-DATEEALGesgaPPPFWAFLWPSGQALARYLLDHPEV-AGKRVLELGCGLGLVGIAAAKAGA 93
                          90       100
                  ....*....|....*....|....*
gi 1907172885 132 SKILANDIDPIAGMAITLNCKLNGL 156
Cdd:COG3897    94 ADVTATDYDPEALAALRLNAALNGV 118
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
94-167 6.00e-11

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 59.42  E-value: 6.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172885  94 QALSRYLLdnpavvRGKSVLDLGSGCGATAIAAKMSGASKILANDIDPIAGMAITLNCKLNGLN--------------PF 159
Cdd:COG2264   140 EALEKLLK------PGKTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVEdrievvlgdlledgPY 213

                  ....*...
gi 1907172885 160 PVLTKNIL 167
Cdd:COG2264   214 DLVVANIL 221
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
94-167 8.19e-11

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 59.01  E-value: 8.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172885  94 QALSRYLLdnpavvRGKSVLDLGSGCGATAIAAKMSGASKILANDIDPIAGMAITLNCKLNGLN----------PFPVLT 163
Cdd:PRK00517  111 EALEKLVL------PGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGVElnvylpqgdlKADVIV 184

                  ....
gi 1907172885 164 KNIL 167
Cdd:PRK00517  185 ANIL 188
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
94-167 1.78e-10

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: 58.43  E-value: 1.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172885  94 QALSRYLLDnpavvrGKSVLDLGSGCGATAIAAKMSGASKILANDIDPIAGMAITLNCKLNGLN--------------PF 159
Cdd:pfam06325 153 EALERLVKP------GESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEarlevylpgdlpkeKA 226

                  ....*...
gi 1907172885 160 PVLTKNIL 167
Cdd:pfam06325 227 DVVVANIL 234
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
107-141 4.82e-08

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 50.67  E-value: 4.82e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1907172885 107 VRGKSVLDLGSGCGATAIAAKMSGASKILANDIDP 141
Cdd:COG2263    44 IEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDIDP 78
PRK14968 PRK14968
putative methyltransferase; Provisional
100-161 2.04e-07

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 48.74  E-value: 2.04e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907172885 100 LLDNPAVVRGKSVLDLGSGCGATAIAAKMSGAsKILANDIDPIAGMAITLNCKLNGLNPFPV 161
Cdd:PRK14968   15 LAENAVDKKGDRVLEVGTGSGIVAIVAAKNGK-KVVGVDINPYAVECAKCNAKLNNIRNNGV 75
PRK14967 PRK14967
putative methyltransferase; Provisional
106-156 7.91e-07

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 47.35  E-value: 7.91e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907172885 106 VVRGKSVLDLGSGCGATAIAAKMSGASKILANDIDPIAGMAITLNCKLNGL 156
Cdd:PRK14967   34 LGPGRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNALLAGV 84
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
90-158 1.77e-05

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


Pssm-ID: 313513  Cd Length: 172  Bit Score: 43.09  E-value: 1.77e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907172885  90 WPGGQALSRYLL------DNPAVVRGKSVLDLGSGCGATAIA-AKMSGASKILANDIDPIAGMaITLNCKLNGLNP 158
Cdd:pfam10294  22 WDAAVVLSKYLEmkifkeLGANNLSGLNVLELGSGTGLVGIAvALLLPGASVTITDLEEALEL-LKKNIELNALSS 96
PRK04338 PRK04338
N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional
111-165 2.93e-05

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


Pssm-ID: 235286  Cd Length: 382  Bit Score: 43.37  E-value: 2.93e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907172885 111 SVLDLGSGCGATAI-AAKMSGASKILANDIDPIAGMAITLNCKLNGLNPFPVLTKN 165
Cdd:PRK04338   60 SVLDALSASGIRGIrYALETGVEKVTLNDINPDAVELIKKNLELNGLENEKVFNKD 115
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
97-157 3.54e-05

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: 42.48  E-value: 3.54e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907172885  97 SRYLLDN-PAVVRGKsVLDLGSGCGATAIA-AKMSGASKILANDIDPiagMAITL---NCKLNGLN 157
Cdd:COG2813    38 TRLLLEHlPEPLGGR-VLDLGCGYGVIGLAlAKRNPEARVTLVDVNA---RAVELaraNAAANGLE 99
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
108-156 7.83e-05

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: 41.67  E-value: 7.83e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907172885 108 RGKSVLDLGSGCGATAIA-AKMSGASKILANDIDPI-AGMAiTLNCKLNGL 156
Cdd:COG4123    37 KGGRVLDLGTGTGVIALMlAQRSPGARITGVEIQPEaAELA-RRNVALNGL 86
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
105-141 1.12e-04

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 41.43  E-value: 1.12e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907172885 105 AVVRGKSVLDLGSGCGATAIAAKMSGASKILANDIDP 141
Cdd:COG2521   129 GVRRGDRVLDTCTGLGYTAIEALKRGAREVITVEKDP 165
TRM1 COG1867
tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N, ...
108-158 1.74e-04

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


Pssm-ID: 441472  Cd Length: 383  Bit Score: 41.01  E-value: 1.74e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907172885 108 RGKSVLDLGSGCGATAI-AAKMSGAsKILANDIDPIAGMAITLNCKLNGLNP 158
Cdd:COG1867    57 REISYLDALAASGIRGLrYALEVGI-KVTLNDIDPEAVELIRENLELNGLED 107
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
107-141 2.51e-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: 2.51e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907172885 107 VRGKSVLDLGSG-CGATAIA-AKMSGASKILANDIDP 141
Cdd:cd05281   162 VSGKSVLITGCGpIGLMAIAvAKAAGASLVIASDPNP 198
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
112-143 1.96e-03

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: 36.25  E-value: 1.96e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1907172885 112 VLDLGSGCGATAIAAKMSGASKILANDIDPIA 143
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVA 33
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
105-157 3.18e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 36.94  E-value: 3.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907172885 105 AVVRGKSVLDLGSGCGATAIAAKMSGASKILANDIDP-IAGMAITlNCKLNGLN 157
Cdd:COG4076    32 VVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPdIAAVARR-IIAANGLS 84
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
79-141 4.37e-03

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 36.06  E-value: 4.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907172885  79 WPYSDPYWAIYWPGG--------QALSRYLLDNPAVVRGKSVLDLGSGCGATAI-AAKMSGAsKILANDIDP 141
Cdd:COG2230    14 LDPTMTYSCAYFEDPddtleeaqEAKLDLILRKLGLKPGMRVLDIGCGWGGLALyLARRYGV-RVTGVTLSP 84
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
97-172 4.74e-03

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: 36.03  E-value: 4.74e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907172885  97 SRYLLDNPAVVRGKSVLDLGSGCGA-TAIAAKMSGASKILANDIDPIAGMAITLNCKLNGLNPFPVLTKNILNTQQE 172
Cdd:pfam05175  20 SRLLLEHLPKDLSGKVLDLGCGAGVlGAALAKESPDAELTMVDINARALESARENLAANGLENGEVVASDVYSGVED 96
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
101-143 5.32e-03

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 36.29  E-value: 5.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1907172885 101 LDNPAVVRGKSVLDLGSGCGATAIA-AKMSGASKILANDIDPIA 143
Cdd:PRK09328  101 LEALLLKEPLRVLDLGTGSGAIALAlAKERPDAEVTAVDISPEA 144
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
108-143 5.63e-03

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 36.28  E-value: 5.63e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907172885 108 RGKSVLDLGSGCGATAIA-AKMSGASKILANDIDPIA 143
Cdd:COG2890   112 APPRVLDLGTGSGAIALAlAKERPDARVTAVDISPDA 148
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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