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Conserved domains on  [gi|1958769899|ref|XP_038963652|]
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electron transfer flavoprotein beta subunit lysine methyltransferase isoform X2 [Rattus norvegicus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10008106)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; similar to Homo sapiens electron transfer flavoprotein beta subunit lysine methyltransferase

CATH:  3.40.50.150
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168|GO:0032259|GO:0008757
PubMed:  12826405|12504684
SCOP:  3000118

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 7.43e-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: 114.98  E-value: 7.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769899  56 LTPEIQLRLLTPRCKFWwERADLWPY----SDPYWAIYWPGGQALSRYLLDNPDvVRGKSVLDLGSGCGATAIAAKMSGA 131
Cdd:COG3897    16 LVPEIRLHLAADAHPLW-DATEEALGesgaPPPFWAFLWPSGQALARYLLDHPE-VAGKRVLELGCGLGLVGIAAAKAGA 93

                          90       100
                  ....*....|....*....|....*
gi 1958769899 132 SNILANDVDPIAGMAITLNCKLNGL 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 7.43e-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: 114.98  E-value: 7.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769899  56 LTPEIQLRLLTPRCKFWwERADLWPY----SDPYWAIYWPGGQALSRYLLDNPDvVRGKSVLDLGSGCGATAIAAKMSGA 131
Cdd:COG3897    16 LVPEIRLHLAADAHPLW-DATEEALGesgaPPPFWAFLWPSGQALARYLLDHPE-VAGKRVLELGCGLGLVGIAAAKAGA 93

                          90       100
                  ....*....|....*....|....*
gi 1958769899 132 SNILANDVDPIAGMAITLNCKLNGL 156
Cdd:COG3897    94 ADVTATDYDPEALAALRLNAALNGV 118
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 94-167 3.87e-09

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: 55.35  E-value: 3.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769899  94 QALSRYLLDnpdvvrGKSVLDLGSGCGATAIAAKMSGASNILANDVDPIAGMAITLNCKLNGLN--------------PF 159
Cdd:pfam06325 153 EALERLVKP------GESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEarlevylpgdlpkeKA 226


                  ....*...
gi 1958769899 160 PILTKNIL 167
Cdd:pfam06325 227 DVVVANIL 234
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
94-167 4.72e-09

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 54.77  E-value: 4.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769899  94 QALSRYLLdnpdvvRGKSVLDLGSGCGATAIAAKMSGASNILANDVDPIAGMAITLNCKLNGLN----------PFPILT 163
Cdd:PRK00517  111 EALEKLVL------PGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGVElnvylpqgdlKADVIV 184


                  ....
gi 1958769899 164 KNIL 167
Cdd:PRK00517  185 ANIL 188
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 107-141 8.17e-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: 39.52  E-value: 8.17e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1958769899 107 VRGKSVLDLGSG-CGATAIA-AKMSGASNILANDVDP 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 7.43e-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: 114.98  E-value: 7.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769899  56 LTPEIQLRLLTPRCKFWwERADLWPY----SDPYWAIYWPGGQALSRYLLDNPDvVRGKSVLDLGSGCGATAIAAKMSGA 131
Cdd:COG3897    16 LVPEIRLHLAADAHPLW-DATEEALGesgaPPPFWAFLWPSGQALARYLLDHPE-VAGKRVLELGCGLGLVGIAAAKAGA 93

                          90       100
                  ....*....|....*....|....*
gi 1958769899 132 SNILANDVDPIAGMAITLNCKLNGL 156
Cdd:COG3897    94 ADVTATDYDPEALAALRLNAALNGV 118
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
94-167 1.34e-09

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 56.33  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769899  94 QALSRYLLdnpdvvRGKSVLDLGSGCGATAIAAKMSGASNILANDVDPIAGMAITLNCKLNGLN--------------PF 159
Cdd:COG2264   140 EALEKLLK------PGKTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVEdrievvlgdlledgPY 213


                  ....*...
gi 1958769899 160 PILTKNIL 167
Cdd:COG2264   214 DLVVANIL 221
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 94-167 3.87e-09

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: 55.35  E-value: 3.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769899  94 QALSRYLLDnpdvvrGKSVLDLGSGCGATAIAAKMSGASNILANDVDPIAGMAITLNCKLNGLN--------------PF 159
Cdd:pfam06325 153 EALERLVKP------GESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEarlevylpgdlpkeKA 226


                  ....*...
gi 1958769899 160 PILTKNIL 167
Cdd:pfam06325 227 DVVVANIL 234
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
94-167 4.72e-09

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 54.77  E-value: 4.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769899  94 QALSRYLLdnpdvvRGKSVLDLGSGCGATAIAAKMSGASNILANDVDPIAGMAITLNCKLNGLN----------PFPILT 163
Cdd:PRK00517  111 EALEKLVL------PGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGVElnvylpqgdlKADVIV 184


                  ....
gi 1958769899 164 KNIL 167
Cdd:PRK00517  185 ANIL 188
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
107-141 7.17e-07

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 47.98  E-value: 7.17e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1958769899 107 VRGKSVLDLGSGCGATAIAAKMSGASNILANDVDP 141
Cdd:COG2263    44 IEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDIDP 78
PRK14967 PRK14967
putative methyltransferase; Provisional
 105-156 9.77e-07

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 47.74  E-value: 9.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958769899 105 DVVRGKSVLDLGSGCGATAIAAKMSGASNILANDVDPIAGMAITLNCKLNGL 156
Cdd:PRK14967   33 GLGPGRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNALLAGV 84
PRK14968 PRK14968
putative methyltransferase; Provisional
 100-161 2.79e-06

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 46.05  E-value: 2.79e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958769899 100 LLDNPDVVRGKSVLDLGSGCGATAIAAKMSGAsNILANDVDPIAGMAITLNCKLNGLNPFPI 161
Cdd:PRK14968   15 LAENAVDKKGDRVLEVGTGSGIVAIVAAKNGK-KVVGVDINPYAVECAKCNAKLNNIRNNGV 75
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 97-157 3.11e-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: 42.87  E-value: 3.11e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958769899  97 SRYLLDNPDVVRGKSVLDLGSGCGATAIA-AKMSGASNILANDVDPiagMAITL---NCKLNGLN 157
Cdd:COG2813    38 TRLLLEHLPEPLGGRVLDLGCGYGVIGLAlAKRNPEARVTLVDVNA---RAVELaraNAAANGLE 99
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 90-150 4.12e-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: 42.32  E-value: 4.12e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958769899  90 WPGGQALSRYLL------DNPDVVRGKSVLDLGSGCGAT--AIAAKMSGASNILAN--DVDPIAGMAITLN 150
Cdd:pfam10294  22 WDAAVVLSKYLEmkifkeLGANNLSGLNVLELGSGTGLVgiAVALLLPGASVTITDleEALELLKKNIELN 92
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 107-141 8.17e-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: 39.52  E-value: 8.17e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1958769899 107 VRGKSVLDLGSG-CGATAIA-AKMSGASNILANDVDP 141
Cdd:cd05281   162 VSGKSVLITGCGpIGLMAIAvAKAAGASLVIASDPNP 198
PRK04338 PRK04338
N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional
 111-165 1.49e-03

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


Pssm-ID: 235286  Cd Length: 382  Bit Score: 38.74  E-value: 1.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958769899 111 SVLDLGSGCGATAI-AAKMSGASNILANDVDPIAGMAITLNCKLNGLNPFPILTKN 165
Cdd:PRK04338   60 SVLDALSASGIRGIrYALETGVEKVTLNDINPDAVELIKKNLELNGLENEKVFNKD 115
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 105-156 1.90e-03

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: 38.20  E-value: 1.90e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958769899 105 DVVRGKSVLDLGSGCGATAIA-AKMSGASNILANDVDPI-AGMAiTLNCKLNGL 156
Cdd:COG4123    34 PVKKGGRVLDLGTGTGVIALMlAQRSPGARITGVEIQPEaAELA-RRNVALNGL 86
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
106-141 2.12e-03

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 38.35  E-value: 2.12e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1958769899 106 VVRGKSVLDLGSGCGATAIAAKMSGASNILANDVDP 141
Cdd:COG2521   130 VRRGDRVLDTCTGLGYTAIEALKRGAREVITVEKDP 165
TRM1 COG1867
tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N, ...
 108-158 2.58e-03

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


Pssm-ID: 441472  Cd Length: 383  Bit Score: 37.93  E-value: 2.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958769899 108 RGKSVLDLGSGCGATAI-AAKMSGAsNILANDVDPIAGMAITLNCKLNGLNP 158
Cdd:COG1867    57 REISYLDALAASGIRGLrYALEVGI-KVTLNDIDPEAVELIRENLELNGLED 107
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 112-143 6.76e-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: 35.10  E-value: 6.76e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1958769899 112 VLDLGSGCGATAIAAKMSGASNILANDVDPIA 143
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVA 33
 
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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