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Conserved domains on  [gi|2462531132|ref|XP_054227632|]
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electron transfer flavoprotein beta subunit lysine methyltransferase isoform X1 [Homo sapiens]

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, ...
 47-262 3.23e-47

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: 156.20  E-value: 3.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132  47 IKAFLEENTEVTSSgsLTPEIQLRLLTPRCKFW---WERADLWPHSDPYWAIYWPGGQALSRYLLDNPDVvRGKSVLDLG 123
Cdd:COG3897     2 SEDFIRANTRLETV--LVPEIRLHLAADAHPLWdatEEALGESGAPPPFWAFLWPSGQALARYLLDHPEV-AGKRVLELG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132 124 SGCGATAIAAKMSGASRILANDIDPIAGMAITLNCELNRLnPFPILIQNILNLEQD-KWDLVVLGDMFYDEDLADSLHQW 202
Cdd:COG3897    79 CGLGLVGIAAAKAGAADVTATDYDPEALAALRLNAALNGV-AITTRLGDWRDPPAAgGFDLILGGDVLYERDLAEPLLPF 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132 203 LKKCfWTYRTRVLIGDPGRPQFSGHSiqHHLHKVVEYSLLESTRQENSGLTTSTVWGFQP 262
Cdd:COG3897   158 LDRL-AAPGGEVLIGDPGRGYLPAFR--ERLEALAGYEVVTRELEDTEKVKRGRVLRLRR 214
 
Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 47-262 3.23e-47

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: 156.20  E-value: 3.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132  47 IKAFLEENTEVTSSgsLTPEIQLRLLTPRCKFW---WERADLWPHSDPYWAIYWPGGQALSRYLLDNPDVvRGKSVLDLG 123
Cdd:COG3897     2 SEDFIRANTRLETV--LVPEIRLHLAADAHPLWdatEEALGESGAPPPFWAFLWPSGQALARYLLDHPEV-AGKRVLELG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132 124 SGCGATAIAAKMSGASRILANDIDPIAGMAITLNCELNRLnPFPILIQNILNLEQD-KWDLVVLGDMFYDEDLADSLHQW 202
Cdd:COG3897    79 CGLGLVGIAAAKAGAADVTATDYDPEALAALRLNAALNGV-AITTRLGDWRDPPAAgGFDLILGGDVLYERDLAEPLLPF 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132 203 LKKCfWTYRTRVLIGDPGRPQFSGHSiqHHLHKVVEYSLLESTRQENSGLTTSTVWGFQP 262
Cdd:COG3897   158 LDRL-AAPGGEVLIGDPGRGYLPAFR--ERLEALAGYEVVTRELEDTEKVKRGRVLRLRR 214
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
101-174 1.04e-10

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 60.17  E-value: 1.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132 101 QALSRYLLdnpdvvRGKSVLDLGSGCGATAIAAKMSGASRILANDIDPIAGMAITLNCELNRLN----------PFPILI 170
Cdd:PRK00517  111 EALEKLVL------PGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGVElnvylpqgdlKADVIV 184


                  ....
gi 2462531132 171 QNIL 174
Cdd:PRK00517  185 ANIL 188
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 101-174 6.94e-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: 58.05  E-value: 6.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132 101 QALSRYLLDnpdvvrGKSVLDLGSGCGATAIAAKMSGASRILANDIDPIAGMAITLNCELNRLN--------------PF 166
Cdd:pfam06325 153 EALERLVKP------GESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEarlevylpgdlpkeKA 226


                  ....*...
gi 2462531132 167 PILIQNIL 174
Cdd:pfam06325 227 DVVVANIL 234
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 119-206 1.04e-06

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: 46.27  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132 119 VLDLGSGCGATAIAAKMSGASRILANDIDPIAGMAITLNCELNRLNPFPILIQNILNLEQD---KWDLVVLGDMFydEDL 195
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEadeSFDVIISDPPL--HHL 79

                          90
                  ....*....|.
gi 2462531132 196 ADSLHQWLKKC 206
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, ...
 47-262 3.23e-47

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: 156.20  E-value: 3.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132  47 IKAFLEENTEVTSSgsLTPEIQLRLLTPRCKFW---WERADLWPHSDPYWAIYWPGGQALSRYLLDNPDVvRGKSVLDLG 123
Cdd:COG3897     2 SEDFIRANTRLETV--LVPEIRLHLAADAHPLWdatEEALGESGAPPPFWAFLWPSGQALARYLLDHPEV-AGKRVLELG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132 124 SGCGATAIAAKMSGASRILANDIDPIAGMAITLNCELNRLnPFPILIQNILNLEQD-KWDLVVLGDMFYDEDLADSLHQW 202
Cdd:COG3897    79 CGLGLVGIAAAKAGAADVTATDYDPEALAALRLNAALNGV-AITTRLGDWRDPPAAgGFDLILGGDVLYERDLAEPLLPF 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132 203 LKKCfWTYRTRVLIGDPGRPQFSGHSiqHHLHKVVEYSLLESTRQENSGLTTSTVWGFQP 262
Cdd:COG3897   158 LDRL-AAPGGEVLIGDPGRGYLPAFR--ERLEALAGYEVVTRELEDTEKVKRGRVLRLRR 214
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
101-185 2.51e-11

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 62.50  E-value: 2.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132 101 QALSRYLLdnpdvvRGKSVLDLGSGCGATAIAAKMSGASRILANDIDPIAGMAITLNCELNRLNPFPILIQNILnLEQDK 180
Cdd:COG2264   140 EALEKLLK------PGKTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVEDRIEVVLGDL-LEDGP 212


                  ....*
gi 2462531132 181 WDLVV 185
Cdd:COG2264   213 YDLVV 217
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
101-174 1.04e-10

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 60.17  E-value: 1.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132 101 QALSRYLLdnpdvvRGKSVLDLGSGCGATAIAAKMSGASRILANDIDPIAGMAITLNCELNRLN----------PFPILI 170
Cdd:PRK00517  111 EALEKLVL------PGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGVElnvylpqgdlKADVIV 184


                  ....
gi 2462531132 171 QNIL 174
Cdd:PRK00517  185 ANIL 188
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 101-174 6.94e-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: 58.05  E-value: 6.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132 101 QALSRYLLDnpdvvrGKSVLDLGSGCGATAIAAKMSGASRILANDIDPIAGMAITLNCELNRLN--------------PF 166
Cdd:pfam06325 153 EALERLVKP------GESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEarlevylpgdlpkeKA 226


                  ....*...
gi 2462531132 167 PILIQNIL 174
Cdd:pfam06325 227 DVVVANIL 234
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 97-206 1.05e-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: 50.41  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132  97 WPGGQALSRYLL------DNPDVVRGKSVLDLGSGCGAT--AIAAKMSGASRILAnDIDPIAGMaITLNCELNRLNP--- 165
Cdd:pfam10294  22 WDAAVVLSKYLEmkifkeLGANNLSGLNVLELGSGTGLVgiAVALLLPGASVTIT-DLEEALEL-LKKNIELNALSSkvv 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462531132 166 FPILI--QNILNLEQDK--WDLVVLGDMFYDEDLADSLHQWLKKC 206
Cdd:pfam10294 100 VKVLDwgENLPPDLFDGhpVDLILAADCVYNEDSFPLLEKTLKDL 144
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
114-148 1.24e-07

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 50.67  E-value: 1.24e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2462531132 114 VRGKSVLDLGSGCGATAIAAKMSGASRILANDIDP 148
Cdd:COG2263    44 IEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDIDP 78
PRK14967 PRK14967
putative methyltransferase; Provisional
 112-163 4.66e-07

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 49.28  E-value: 4.66e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462531132 112 DVVRGKSVLDLGSGCGATAIAAKMSGASRILANDIDPIAGMAITLNCELNRL 163
Cdd:PRK14967   33 GLGPGRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNALLAGV 84
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 119-206 1.04e-06

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: 46.27  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132 119 VLDLGSGCGATAIAAKMSGASRILANDIDPIAGMAITLNCELNRLNPFPILIQNILNLEQD---KWDLVVLGDMFydEDL 195
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEadeSFDVIISDPPL--HHL 79

                          90
                  ....*....|.
gi 2462531132 196 ADSLHQWLKKC 206
Cdd:cd02440    80 VEDLARFLEEA 90
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 104-185 2.10e-06

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: 47.11  E-value: 2.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132 104 SRYLLDNPDVVRGKSVLDLGSGCGATAIA-AKMSGASRILANDIDPiagMAITL---NCELNRLNPFPILIQNIL-NLEQ 178
Cdd:COG2813    38 TRLLLEHLPEPLGGRVLDLGCGYGVIGLAlAKRNPEARVTLVDVNA---RAVELaraNAAANGLENVEVLWSDGLsGVPD 114


                  ....*..
gi 2462531132 179 DKWDLVV 185
Cdd:COG2813   115 GSFDLIL 121
PRK14968 PRK14968
putative methyltransferase; Provisional
 107-185 4.97e-06

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 46.05  E-value: 4.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132 107 LLDNPDVVRGKSVLDLGSGCGATAIAAKMSGAsRILANDIDPIAGMAITLNCELNRLNPFPI------LIQNILNleqDK 180
Cdd:PRK14968   15 LAENAVDKKGDRVLEVGTGSGIVAIVAAKNGK-KVVGVDINPYAVECAKCNAKLNNIRNNGVevirsdLFEPFRG---DK 90


                  ....*
gi 2462531132 181 WDLVV 185
Cdd:PRK14968   91 FDVIL 95
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 89-204 2.44e-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: 42.70  E-value: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132  89 SDPYWAIYWPggQALSRYLLDNpdVVRGKSVLDLGSGCGATAIAAKMSGAsRILANDIDPIAGMAITLNCELNRLNPFPI 168
Cdd:COG2227     2 SDPDARDFWD--RRLAALLARL--LPAGGRVLDVGCGTGRLALALARRGA-DVTGVDISPEALEIARERAAELNVDFVQG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462531132 169 LIQNiLNLEQDKWDLVVLGDMFY----DEDLADSLHQWLK 204
Cdd:COG2227    77 DLED-LPLEDGSFDLVICSEVLEhlpdPAALLRELARLLK 115
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 86-204 2.72e-05

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 43.38  E-value: 2.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132  86 WPHSDPYWAIYWPGG--------QALSRYLLDNPDVVRGKSVLDLGSGCGATAI-AAKMSGAsRILANDIDP-------- 148
Cdd:COG2230    14 LDPTMTYSCAYFEDPddtleeaqEAKLDLILRKLGLKPGMRVLDIGCGWGGLALyLARRYGV-RVTGVTLSPeqleyare 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462531132 149 -IAGMAITLNCElnrlnpfpILIQNILNLEQD-KWDLVVLGDMF------YDEDLADSLHQWLK 204
Cdd:COG2230    93 rAAEAGLADRVE--------VRLADYRDLPADgQFDAIVSIGMFehvgpeNYPAYFAKVARLLK 148
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 112-185 3.66e-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: 43.98  E-value: 3.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132 112 DVVRGKSVLDLGSGCGATAIA-AKMSGASRILANDIDPI-AGMAiTLNCELN----RLNPFPILIQNILN-LEQDKWDLV 184
Cdd:COG4123    34 PVKKGGRVLDLGTGTGVIALMlAQRSPGARITGVEIQPEaAELA-RRNVALNgledRITVIHGDLKEFAAeLPPGSFDLV 112


                  .
gi 2462531132 185 V 185
Cdd:COG4123   113 V 113
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 104-185 3.76e-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: 42.96  E-value: 3.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132 104 SRYLLDNPDVVRGKSVLDLGSGCGA-TAIAAKMSGASRILANDIDPIAGMAITLNCELNRLNPFPILIQNIL-NLEQDKW 181
Cdd:pfam05175  20 SRLLLEHLPKDLSGKVLDLGCGAGVlGAALAKESPDAELTMVDINARALESARENLAANGLENGEVVASDVYsGVEDGKF 99


                  ....
gi 2462531132 182 DLVV 185
Cdd:pfam05175 100 DLII 103
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
113-165 7.52e-05

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 42.97  E-value: 7.52e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462531132 113 VVRGKSVLDLGSGCGATAIAAKMSGASRILANDIDPIAgmaitlnCELNRLNP 165
Cdd:COG2521   130 VRRGDRVLDTCTGLGYTAIEALKRGAREVITVEKDPNV-------LELAELNP 175
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 114-148 4.62e-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: 41.07  E-value: 4.62e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2462531132 114 VRGKSVLDLGSG-CGATAIA-AKMSGASRILANDIDP 148
Cdd:cd05281   162 VSGKSVLITGCGpIGLMAIAvAKAAGASLVIASDPNP 198
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 92-205 4.63e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 40.28  E-value: 4.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132  92 YWAIYWPGGQA--LSRYLLDNPDVVRGKSVLDLGSGCGATAIAAKMSGASRILANDIDPIagmAITLNCELNR---LNPF 166
Cdd:COG0500     1 PWDSYYSDELLpgLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPE---AIALARARAAkagLGNV 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462531132 167 PILIQNILN---LEQDKWDLVVLGDMFYDEDLA------DSLHQWLKK 205
Cdd:COG0500    78 EFLVADLAEldpLPAESFDLVVAFGVLHHLPPEereallRELARALKP 125
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 108-185 8.78e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 39.76  E-value: 8.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132 108 LDNPDVVRGKSVLDLGSGCGATAIA-AKMSGASRILANDIDPIAgMAITL-NCELNRLNPFPILIQNIL-NLEQDKWDLV 184
Cdd:PRK09328  101 LEALLLKEPLRVLDLGTGSGAIALAlAKERPDAEVTAVDISPEA-LAVARrNAKHGLGARVEFLQGDWFePLPGGRFDLI 179


                  .
gi 2462531132 185 V 185
Cdd:PRK09328  180 V 180
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 115-185 1.99e-03

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 38.59  E-value: 1.99e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462531132 115 RGKSVLDLGSGCGATAIA-AKMSGASRILANDIDPIAgMAIT-LNCELNRLNPFPILIQ-NILN--LEQDKWDLVV 185
Cdd:COG2890   112 APPRVLDLGTGSGAIALAlAKERPDARVTAVDISPDA-LAVArRNAERLGLEDRVRFLQgDLFEplPGDGRFDLIV 186
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 119-205 2.27e-03

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 36.39  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132 119 VLDLGSGCGATAIAAKMSGASRILANDIDPIAGMAITLNCELNRLNpFPILIQNILNL--EQDKWDLVVLGDMFY---DE 193
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLN-VEFVQGDAEDLpfPDGSFDLVVSSGVLHhlpDP 79

                          90
                  ....*....|....*
gi 2462531132 194 DLADSL---HQWLKK 205
Cdd:pfam13649  80 DLEAALreiARVLKP 94
PRK04338 PRK04338
N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional
 118-184 3.49e-03

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


Pssm-ID: 235286  Cd Length: 382  Bit Score: 38.36  E-value: 3.49e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132 118 SVLDLGSGCGATAI-AAKMSGASRILANDIDPIAGMAITLNCELNRLNPFPILIQ--NILNLEQDKWDLV 184
Cdd:PRK04338   60 SVLDALSASGIRGIrYALETGVEKVTLNDINPDAVELIKKNLELNGLENEKVFNKdaNALLHEERKFDVV 129
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
115-201 4.13e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 37.29  E-value: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132 115 RGKSVLDLGSGCGATAIA-AKMsgASRILAndIDPIAGMaitLNCELNRLNPFPILIQNILNLEQ--DKWDLVVLGDMF- 190
Cdd:COG4976    46 PFGRVLDLGCGTGLLGEAlRPR--GYRLTG--VDLSEEM---LAKAREKGVYDRLLVADLADLAEpdGRFDLIVAADVLt 118

                          90
                  ....*....|.
gi 2462531132 191 YDEDLADSLHQ 201
Cdd:COG4976   119 YLGDLAAVFAG 129
TRM1 COG1867
tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N, ...
 115-165 8.74e-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: 37.16  E-value: 8.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462531132 115 RGKSVLDLGSGCGATAI-AAKMSGAsRILANDIDPIAGMAITLNCELNRLNP 165
Cdd:COG1867    57 REISYLDALAASGIRGLrYALEVGI-KVTLNDIDPEAVELIRENLELNGLED 107
Met_10 pfam02475
Met-10+ like-protein; The methionine-10 mutant allele of N. crassa codes for a protein of ...
 116-207 9.25e-03

Met-10+ like-protein; The methionine-10 mutant allele of N. crassa codes for a protein of unknown function, Swiss:O27901. However, homologous proteins have been found in yeast suggesting this protein may be involved in methionine biosynthesis, transport and/or utilization.


Pssm-ID: 396850 [Multi-domain]  Cd Length: 198  Bit Score: 36.18  E-value: 9.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132 116 GKSVLDLGSGCGATAI-AAKMSGASRILANDIDPIAGMAITLNCELNRLNPF--PILIQNILNLEQDKWDLVVLGdmfyd 192
Cdd:pfam02475 100 GEVVVDMFAGIGPFSIpIAKHSKARRVYAIELNPESYKYLKENIKLNKVEDVvkPILGDVREVILEDVADRVVMN----- 174

                          90
                  ....*....|....*
gi 2462531132 193 edLADSLHQWLKKCF 207
Cdd:pfam02475 175 --LPGSAHEFLDKAF 187
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
115-204 9.56e-03

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 34.80  E-value: 9.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531132 115 RGKSVLDLGSGCGA-TAIAAKMSGASRILANDIDPiagMAITLNCElnRLNPFPILIQNILNLE-QDKWDLVVLGDMFY- 191
Cdd:COG4106     1 PPRRVLDLGCGTGRlTALLAERFPGARVTGVDLSP---EMLARARA--RLPNVRFVVADLRDLDpPEPFDLVVSNAALHw 75

                          90
                  ....*....|....*.
gi 2462531132 192 ---DEDLADSLHQWLK 204
Cdd:COG4106    76 lpdHAALLARLAAALA 91
 
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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