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Conserved domains on  [gi|38454282|ref|NP_942067|]
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electron transfer flavoprotein beta subunit lysine methyltransferase [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, ...
 56-255 2.48e-51

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: 166.60  E-value: 2.48e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38454282  56 LTPEIQLRLLTPRCKFWwERADLWPY----SDPYWAIYWPGGQALSRYLLDNPDvVRGKSVLDLGSGCGATAIAAKMSGA 131
Cdd:COG3897  16 LVPEIRLHLAADAHPLW-DATEEALGesgaPPPFWAFLWPSGQALARYLLDHPE-VAGKRVLELGCGLGLVGIAAAKAGA 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38454282 132 SNILANDVDPIAGMAITLNCKLNGLnPFPILTKNILNTR-QGKFDLIVLGDMFYDEDLADSLHLWLQNCfWAYGTRVLIG 210
Cdd:COG3897  94 ADVTATDYDPEALAALRLNAALNGV-AITTRLGDWRDPPaAGGFDLILGGDVLYERDLAEPLLPFLDRL-AAPGGEVLIG 171

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 38454282 211 DPGRPQFSGHSiqHQLYQLAEYTLPEPTQQDNNGLTTSAVWDFHP 255
Cdd:COG3897 172 DPGRGYLPAFR--ERLEALAGYEVVTRELEDTEKVKRGRVLRLRR 214
 
Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 56-255 2.48e-51

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: 166.60  E-value: 2.48e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38454282  56 LTPEIQLRLLTPRCKFWwERADLWPY----SDPYWAIYWPGGQALSRYLLDNPDvVRGKSVLDLGSGCGATAIAAKMSGA 131
Cdd:COG3897  16 LVPEIRLHLAADAHPLW-DATEEALGesgaPPPFWAFLWPSGQALARYLLDHPE-VAGKRVLELGCGLGLVGIAAAKAGA 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38454282 132 SNILANDVDPIAGMAITLNCKLNGLnPFPILTKNILNTR-QGKFDLIVLGDMFYDEDLADSLHLWLQNCfWAYGTRVLIG 210
Cdd:COG3897  94 ADVTATDYDPEALAALRLNAALNGV-AITTRLGDWRDPPaAGGFDLILGGDVLYERDLAEPLLPFLDRL-AAPGGEVLIG 171

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 38454282 211 DPGRPQFSGHSiqHQLYQLAEYTLPEPTQQDNNGLTTSAVWDFHP 255
Cdd:COG3897 172 DPGRGYLPAFR--ERLEALAGYEVVTRELEDTEKVKRGRVLRLRR 214
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 94-178 6.65e-11

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: 61.13  E-value: 6.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38454282    94 QALSRYLLDnpdvvrGKSVLDLGSGCGATAIAAKMSGASNILANDVDPIAGMAITLNCKLNGLNP--FPILTKNILntrQ 171
Cdd:pfam06325 153 EALERLVKP------GESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEArlEVYLPGDLP---K 223


                  ....*..
gi 38454282   172 GKFDLIV 178
Cdd:pfam06325 224 EKADVVV 230
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
94-178 3.19e-10

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 58.62  E-value: 3.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38454282   94 QALSRYLLdnpdvvRGKSVLDLGSGCGATAIAAKMSGASNILANDVDPIAGMAITLNCKLNGLNPFPILTKNilntrQGK 173
Cdd:PRK00517 111 EALEKLVL------PGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGVELNVYLPQG-----DLK 179


                 ....*
gi 38454282  174 FDLIV 178
Cdd:PRK00517 180 ADVIV 184
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 112-199 1.94e-04

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 39.72  E-value: 1.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38454282 112 VLDLGSGCGATAIAAKMSGASNILANDVDPIAGMAITLNCKLNGLNPFPILTKNILN---TRQGKFDLIVLGDMFydEDL 188
Cdd:cd02440   2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEElppEADESFDVIISDPPL--HHL 79

                        90
                ....*....|.
gi 38454282 189 ADSLHLWLQNC 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 2.48e-51

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: 166.60  E-value: 2.48e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38454282  56 LTPEIQLRLLTPRCKFWwERADLWPY----SDPYWAIYWPGGQALSRYLLDNPDvVRGKSVLDLGSGCGATAIAAKMSGA 131
Cdd:COG3897  16 LVPEIRLHLAADAHPLW-DATEEALGesgaPPPFWAFLWPSGQALARYLLDHPE-VAGKRVLELGCGLGLVGIAAAKAGA 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38454282 132 SNILANDVDPIAGMAITLNCKLNGLnPFPILTKNILNTR-QGKFDLIVLGDMFYDEDLADSLHLWLQNCfWAYGTRVLIG 210
Cdd:COG3897  94 ADVTATDYDPEALAALRLNAALNGV-AITTRLGDWRDPPaAGGFDLILGGDVLYERDLAEPLLPFLDRL-AAPGGEVLIG 171

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 38454282 211 DPGRPQFSGHSiqHQLYQLAEYTLPEPTQQDNNGLTTSAVWDFHP 255
Cdd:COG3897 172 DPGRGYLPAFR--ERLEALAGYEVVTRELEDTEKVKRGRVLRLRR 214
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
94-178 4.02e-11

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 61.73  E-value: 4.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38454282  94 QALSRYLLdnpdvvRGKSVLDLGSGCGATAIAAKMSGASNILANDVDPIAGMAITLNCKLNGL-NPFPILTKNILntRQG 172
Cdd:COG2264 140 EALEKLLK------PGKTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVeDRIEVVLGDLL--EDG 211


                ....*.
gi 38454282 173 KFDLIV 178
Cdd:COG2264 212 PYDLVV 217
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 94-178 6.65e-11

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: 61.13  E-value: 6.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38454282    94 QALSRYLLDnpdvvrGKSVLDLGSGCGATAIAAKMSGASNILANDVDPIAGMAITLNCKLNGLNP--FPILTKNILntrQ 171
Cdd:pfam06325 153 EALERLVKP------GESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEArlEVYLPGDLP---K 223


                  ....*..
gi 38454282   172 GKFDLIV 178
Cdd:pfam06325 224 EKADVVV 230
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
94-178 3.19e-10

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 58.62  E-value: 3.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38454282   94 QALSRYLLdnpdvvRGKSVLDLGSGCGATAIAAKMSGASNILANDVDPIAGMAITLNCKLNGLNPFPILTKNilntrQGK 173
Cdd:PRK00517 111 EALEKLVL------PGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGVELNVYLPQG-----DLK 179


                 ....*
gi 38454282  174 FDLIV 178
Cdd:PRK00517 180 ADVIV 184
PRK14968 PRK14968
putative methyltransferase; Provisional
 100-178 2.65e-08

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 52.21  E-value: 2.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38454282  100 LLDNPDVVRGKSVLDLGSGCGATAIAAKMSGAsNILANDVDPIAGMAITLNCKLNGLNPFPI------LTKNIlntRQGK 173
Cdd:PRK14968  15 LAENAVDKKGDRVLEVGTGSGIVAIVAAKNGK-KVVGVDINPYAVECAKCNAKLNNIRNNGVevirsdLFEPF---RGDK 90


                 ....*
gi 38454282  174 FDLIV 178
Cdd:PRK14968  91 FDVIL 95
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 97-178 2.07e-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: 49.80  E-value: 2.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38454282  97 SRYLLDNPDVVRGKSVLDLGSGCGATAIA-AKMSGASNILANDVDPiagMAITL---NCKLNGLNPFPILTKNIL-NTRQ 171
Cdd:COG2813  38 TRLLLEHLPEPLGGRVLDLGCGYGVIGLAlAKRNPEARVTLVDVNA---RAVELaraNAAANGLENVEVLWSDGLsGVPD 114


                ....*..
gi 38454282 172 GKFDLIV 178
Cdd:COG2813 115 GSFDLIL 121
PRK14967 PRK14967
putative methyltransferase; Provisional
 105-156 9.14e-07

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 48.51  E-value: 9.14e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 38454282  105 DVVRGKSVLDLGSGCGATAIAAKMSGASNILANDVDPIAGMAITLNCKLNGL 156
Cdd:PRK14967  33 GLGPGRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNALLAGV 84
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
107-141 1.08e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 47.98  E-value: 1.08e-06
                        10        20        30
                ....*....|....*....|....*....|....*
gi 38454282 107 VRGKSVLDLGSGCGATAIAAKMSGASNILANDVDP 141
Cdd:COG2263  44 IEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDIDP 78
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 90-192 3.95e-06

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: 45.79  E-value: 3.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38454282    90 WPGGQALSRYLL------DNPDVVRGKSVLDLGSGCGATAIA-AKMSGASNILANDVDPIAGMaITLNCKLNGLNP---F 159
Cdd:pfam10294  22 WDAAVVLSKYLEmkifkeLGANNLSGLNVLELGSGTGLVGIAvALLLPGASVTITDLEEALEL-LKKNIELNALSSkvvV 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 38454282   160 PILT--KNI---LNTRQgKFDLIVLGDMFYDED----LADSL 192
Cdd:pfam10294 101 KVLDwgENLppdLFDGH-PVDLILAADCVYNEDsfplLEKTL 141
PRK04338 PRK04338
N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional
 111-177 8.78e-06

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


Pssm-ID: 235286  Cd Length: 382  Bit Score: 46.06  E-value: 8.78e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38454282  111 SVLDLGSGCGATAI-AAKMSGASNILANDVDPIAGMAITLNCKLNGLNPFPILTK--NILNTRQGKFDLI 177
Cdd:PRK04338  60 SVLDALSASGIRGIrYALETGVEKVTLNDINPDAVELIKKNLELNGLENEKVFNKdaNALLHEERKFDVV 129
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 97-178 1.70e-05

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: 44.12  E-value: 1.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38454282    97 SRYLLDNPDVVRGKSVLDLGSGCGA-TAIAAKMSGASNILANDVDPIAGMAITLNCKLNGLNPFPILTKNILNTRQ-GKF 174
Cdd:pfam05175  20 SRLLLEHLPKDLSGKVLDLGCGAGVlGAALAKESPDAELTMVDINARALESARENLAANGLENGEVVASDVYSGVEdGKF 99


                  ....
gi 38454282   175 DLIV 178
Cdd:pfam05175 100 DLII 103
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 101-178 6.14e-05

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 43.23  E-value: 6.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38454282  101 LDNPDVVRGKSVLDLGSGCGATAIA-AKMSGASNILANDVDPIAgMAITL-NCKLNGLNPFPILTKNILNT-RQGKFDLI 177
Cdd:PRK09328 101 LEALLLKEPLRVLDLGTGSGAIALAlAKERPDAEVTAVDISPEA-LAVARrNAKHGLGARVEFLQGDWFEPlPGGRFDLI 179


                 .
gi 38454282  178 V 178
Cdd:PRK09328 180 V 180
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 105-178 1.12e-04

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: 42.44  E-value: 1.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38454282 105 DVVRGKSVLDLGSGCGATAIA-AKMSGASNILANDVDPI-AGMAiTLNCKLNGLNP-FPILTKNILNTRQ----GKFDLI 177
Cdd:COG4123  34 PVKKGGRVLDLGTGTGVIALMlAQRSPGARITGVEIQPEaAELA-RRNVALNGLEDrITVIHGDLKEFAAelppGSFDLV 112


                .
gi 38454282 178 V 178
Cdd:COG4123 113 V 113
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 82-200 1.15e-04

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: 40.77  E-value: 1.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38454282  82 SDPYWAIYWPggQALSRYLLDNpdVVRGKSVLDLGSGCGATAIAAKMSGAsNILAndVDPIAGMAITLNCKLNGLNPfPI 161
Cdd:COG2227   2 SDPDARDFWD--RRLAALLARL--LPAGGRVLDVGCGTGRLALALARRGA-DVTG--VDISPEALEIARERAAELNV-DF 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 38454282 162 LTKNI--LNTRQGKFDLIVLGDMFydEDLADsLHLWLQNCF 200
Cdd:COG2227  74 VQGDLedLPLEDGSFDLVICSEVL--EHLPD-PAALLRELA 111
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 112-199 1.94e-04

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 39.72  E-value: 1.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38454282 112 VLDLGSGCGATAIAAKMSGASNILANDVDPIAGMAITLNCKLNGLNPFPILTKNILN---TRQGKFDLIVLGDMFydEDL 188
Cdd:cd02440   2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEElppEADESFDVIISDPPL--HHL 79

                        90
                ....*....|.
gi 38454282 189 ADSLHLWLQNC 199
Cdd:cd02440  80 VEDLARFLEEA 90
TRM1 COG1867
tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N, ...
 108-177 2.60e-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: 41.78  E-value: 2.60e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38454282 108 RGKSVLDLGSGCGATAI-AAKMSGAsNILANDVDPIAGMAITLNCKLNGLNPFPILTKN---ILNTRQGKFDLI 177
Cdd:COG1867  57 REISYLDALAASGIRGLrYALEVGI-KVTLNDIDPEAVELIRENLELNGLEDVEVYNRDanaLLHELGRRFDVV 129
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 108-178 3.77e-04

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 40.90  E-value: 3.77e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38454282 108 RGKSVLDLGSGCGATAIA-AKMSGASNILANDVDPIAgMAIT-LNCKLNGL-NPFPILTKNILN--TRQGKFDLIV 178
Cdd:COG2890 112 APPRVLDLGTGSGAIALAlAKERPDARVTAVDISPDA-LAVArRNAERLGLeDRVRFLQGDLFEplPGDGRFDLIV 186
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 107-179 5.04e-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: 40.94  E-value: 5.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38454282 107 VRGKSVLDLGSGCGATAIAAKMSGASNILAndVDpIAGMAITL---NCKLNGLNP---------FPILTKniLNTRQGKF 174
Cdd:COG1092 215 AKGKRVLNLFSYTGGFSVHAAAGGAKSVTS--VD-LSATALEWakeNAALNGLDDrhefvqadaFDWLRE--LAREGERF 289


                ....*
gi 38454282 175 DLIVL 179
Cdd:COG1092 290 DLIIL 294
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 107-141 1.20e-03

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: 1.20e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 38454282 107 VRGKSVLDLGSG-CGATAIA-AKMSGASNILANDVDP 141
Cdd:cd05281 162 VSGKSVLITGCGpIGLMAIAvAKAAGASLVIASDPNP 198
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 85-200 2.19e-03

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 37.97  E-value: 2.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38454282  85 YWAIYWPGGQA--LSRYLLDNPDVVRGKSVLDLGSGCGATAIAAKMSGASNILANDVDPIagmAITL---NCKLNGLNPF 159
Cdd:COG0500   1 PWDSYYSDELLpgLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPE---AIALaraRAAKAGLGNV 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 38454282 160 PILTKNILNT---RQGKFDLIVLGDMFYDEDLADSLHLwLQNCF 200
Cdd:COG0500  78 EFLVADLAELdplPAESFDLVVAFGVLHHLPPEEREAL-LRELA 120
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
106-141 3.03e-03

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 38.35  E-value: 3.03e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 38454282 106 VVRGKSVLDLGSGCGATAIAAKMSGASNILANDVDP 141
Cdd:COG2521 130 VRRGDRVLDTCTGLGYTAIEALKRGAREVITVEKDP 165
 
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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