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Conserved domains on  [gi|1169282677|emb|SFZ97297|]
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tRNA (adenine37-N(6))-methyltransferase TrmN6 [hydrothermal vent metagenome]

Protein Classification

tRNA1(Val) (adenine(37)-N6)-methyltransferase( domain architecture ID 11467886)

tRNA(1)(Val) (adenine(37)-N(6))-methyltransferase is a class I SAM-dependent methyltransferase that specifically methylates the adenine in position 37 of tRNA(1)(Val)

CATH:  2.20.25.110
EC:  2.1.1.223
Gene Ontology:  GO:0016430|GO:1904047|GO:0008170|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
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 2-181 6.26e-56

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: 176.87  E-value: 6.26e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   2 DVGCGVGIISLLLSRDFPVfTSI--IDKQESMLNYAKHNFYLNNLE--VKTY---LNSFQEHNTEDRYDFIVSNPPFYDA 74
Cdd:COG4123    43 DLGTGTGVIALMLAQRSPG-ARItgVEIQPEAAELARRNVALNGLEdrITVIhgdLKEFAAELPPGSFDLVVSNPPYFKA 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677  75 -SVTQSENRHLNIARYSQHLPIEDFIKRVKTFLKPKGWFIFCYDAKQIDILLQHLKINGINPEKIQFVHSKIDRDSKLVM 153
Cdd:COG4123   122 gSGRKSPDEARAIARHEDALTLEDLIRAAARLLKPGGRFALIHPAERLAEILAALRKYGLGPKRLRPVHPRPGKPAKRVL 201

                         170       180
                  ....*....|....*....|....*...
gi 1169282677 154 IAARNNSKSMTQILPPFIVFNDENVYTE 181
Cdd:COG4123   202 LEARKGGRAGLRILPPLVIHDEDGEYTP 229
 
Name Accession Description Interval E-value
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 2-181 6.26e-56

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: 176.87  E-value: 6.26e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   2 DVGCGVGIISLLLSRDFPVfTSI--IDKQESMLNYAKHNFYLNNLE--VKTY---LNSFQEHNTEDRYDFIVSNPPFYDA 74
Cdd:COG4123    43 DLGTGTGVIALMLAQRSPG-ARItgVEIQPEAAELARRNVALNGLEdrITVIhgdLKEFAAELPPGSFDLVVSNPPYFKA 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677  75 -SVTQSENRHLNIARYSQHLPIEDFIKRVKTFLKPKGWFIFCYDAKQIDILLQHLKINGINPEKIQFVHSKIDRDSKLVM 153
Cdd:COG4123   122 gSGRKSPDEARAIARHEDALTLEDLIRAAARLLKPGGRFALIHPAERLAEILAALRKYGLGPKRLRPVHPRPGKPAKRVL 201

                         170       180
                  ....*....|....*....|....*...
gi 1169282677 154 IAARNNSKSMTQILPPFIVFNDENVYTE 181
Cdd:COG4123   202 LEARKGGRAGLRILPPLVIHDEDGEYTP 229
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 2-148 1.46e-09

protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein family are HemK (PrmC), a protein once thought to be involved in heme biosynthesis but now recognized to be a protein-glutamine methyltransferase that modifies the peptide chain release factors. All members of the seed alignment are encoded next to the release factor 1 gene (prfA) and confirmed by phylogenetic analysis. SIMBAL analysis (manuscript in prep.) shows the motif [LIV]PRx[DE]TE (in Escherichia coli, IPRPDTE) confers specificity for the release factors rather than for ribosomal protein L3. [Protein fate, Protein modification and repair]


Pssm-ID: 274634 [Multi-domain]  Cd Length: 250  Bit Score: 55.55  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   2 DVGCGVGIISLLLSRDFP---VFTSiiDKQESMLNYAKHNFYLNNLE-VKTYLNSFQEHNTEDRYDFIVSNPPFYDASVT 77
Cdd:TIGR03534  92 DLGTGSGAIALALAKERPdarVTAV--DISPEALAVARKNARRLGLEnVEFLQGDWFEPLPSGKFDLIVSNPPYIPEADI 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677  78 qsENRHLNIARYSQHL----------PIEDFIKRVKTFLKPKGWFIFCYDAKQIDILLQHLKINGinpekiqFVHSKIDR 147
Cdd:TIGR03534 170 --HLLDPEVRDFEPRLalfggedgldFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFEAAG-------FADVETRK 240


                  .
gi 1169282677 148 D 148
Cdd:TIGR03534 241 D 241
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 2-110 8.94e-09

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 51.03  E-value: 8.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   2 DVGCGVGIISLLLSRDFPVFTSIIDKQESMLNYAKHNFYLNNLEVKTYLNSFQEHNTED-RYDFIVSNPPFydasvtqse 80
Cdd:pfam13649   3 DLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDgSFDLVVSSGVL--------- 73

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1169282677  81 nrhlniarysQHLPIED---FIKRVKTFLKPKG 110
Cdd:pfam13649  74 ----------HHLPDPDleaALREIARVLKPGG 96
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 2-147 1.72e-08

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 52.86  E-value: 1.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   2 DVGCGVGIISLLLSRDFP---VFTSiiDKQESMLNYAKHNF-YLNNLEVKTYLNSFQEHNTEDRYDFIVSNPPfY----D 73
Cdd:PRK09328  114 DLGTGSGAIALALAKERPdaeVTAV--DISPEALAVARRNAkHGLGARVEFLQGDWFEPLPGGRFDLIVSNPP-YipeaD 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677  74 ASVTQSENRhlniarysQHLPIE---------DFIKRV----KTFLKPKGWFIFCYDAKQIDILLQHLKINGInpEKIQF 140
Cdd:PRK09328  191 IHLLQPEVR--------DHEPHLalfggedglDFYRRIieqaPRYLKPGGWLLLEIGYDQGEAVRALLAAAGF--ADVET 260


                  ....*....
gi 1169282677 141 VH--SKIDR 147
Cdd:PRK09328  261 RKdlAGRDR 269
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 2-116 4.64e-08

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: 49.35  E-value: 4.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   2 DVGCGVGIISLLLSRDFPVFTSIIDKQESMLNYAKHNFYLNNLEVKTYL--NSFQEHNTED-RYDFIVSNPPFydasvtq 78
Cdd:cd02440     4 DLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLkgDAEELPPEADeSFDVIISDPPL------- 76

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1169282677  79 senrhlniarYSQHLPIEDFIKRVKTFLKPKGWFIFCY 116
Cdd:cd02440    77 ----------HHLVEDLARFLEEARRLLKPGGVLVLTL 104
 
Name Accession Description Interval E-value
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 2-181 6.26e-56

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: 176.87  E-value: 6.26e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   2 DVGCGVGIISLLLSRDFPVfTSI--IDKQESMLNYAKHNFYLNNLE--VKTY---LNSFQEHNTEDRYDFIVSNPPFYDA 74
Cdd:COG4123    43 DLGTGTGVIALMLAQRSPG-ARItgVEIQPEAAELARRNVALNGLEdrITVIhgdLKEFAAELPPGSFDLVVSNPPYFKA 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677  75 -SVTQSENRHLNIARYSQHLPIEDFIKRVKTFLKPKGWFIFCYDAKQIDILLQHLKINGINPEKIQFVHSKIDRDSKLVM 153
Cdd:COG4123   122 gSGRKSPDEARAIARHEDALTLEDLIRAAARLLKPGGRFALIHPAERLAEILAALRKYGLGPKRLRPVHPRPGKPAKRVL 201

                         170       180
                  ....*....|....*....|....*...
gi 1169282677 154 IAARNNSKSMTQILPPFIVFNDENVYTE 181
Cdd:COG4123   202 LEARKGGRAGLRILPPLVIHDEDGEYTP 229
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 2-110 9.52e-11

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: 58.28  E-value: 9.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   2 DVGCGVGIISLLLSRDFPVfTSI--IDKQESMLNYAKHNFYLNNLE-VKTYLNSFQEHNTEDRYDFIVSNPPFYDASVTQ 78
Cdd:COG2813    55 DLGCGYGVIGLALAKRNPE-ARVtlVDVNARAVELARANAAANGLEnVEVLWSDGLSGVPDGSFDLILSNPPFHAGRAVD 133

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1169282677  79 SEnrhlniarysqhlPIEDFIKRVKTFLKPKG 110
Cdd:COG2813   134 KE-------------VAHALIADAARHLRPGG 152
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 2-148 1.46e-09

protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein family are HemK (PrmC), a protein once thought to be involved in heme biosynthesis but now recognized to be a protein-glutamine methyltransferase that modifies the peptide chain release factors. All members of the seed alignment are encoded next to the release factor 1 gene (prfA) and confirmed by phylogenetic analysis. SIMBAL analysis (manuscript in prep.) shows the motif [LIV]PRx[DE]TE (in Escherichia coli, IPRPDTE) confers specificity for the release factors rather than for ribosomal protein L3. [Protein fate, Protein modification and repair]


Pssm-ID: 274634 [Multi-domain]  Cd Length: 250  Bit Score: 55.55  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   2 DVGCGVGIISLLLSRDFP---VFTSiiDKQESMLNYAKHNFYLNNLE-VKTYLNSFQEHNTEDRYDFIVSNPPFYDASVT 77
Cdd:TIGR03534  92 DLGTGSGAIALALAKERPdarVTAV--DISPEALAVARKNARRLGLEnVEFLQGDWFEPLPSGKFDLIVSNPPYIPEADI 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677  78 qsENRHLNIARYSQHL----------PIEDFIKRVKTFLKPKGWFIFCYDAKQIDILLQHLKINGinpekiqFVHSKIDR 147
Cdd:TIGR03534 170 --HLLDPEVRDFEPRLalfggedgldFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFEAAG-------FADVETRK 240


                  .
gi 1169282677 148 D 148
Cdd:TIGR03534 241 D 241
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 2-110 8.94e-09

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 51.03  E-value: 8.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   2 DVGCGVGIISLLLSRDFPVFTSIIDKQESMLNYAKHNFYLNNLEVKTYLNSFQEHNTED-RYDFIVSNPPFydasvtqse 80
Cdd:pfam13649   3 DLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDgSFDLVVSSGVL--------- 73

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1169282677  81 nrhlniarysQHLPIED---FIKRVKTFLKPKG 110
Cdd:pfam13649  74 ----------HHLPDPDleaALREIARVLKPGG 96
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 2-110 9.21e-09

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: 52.59  E-value: 9.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   2 DVGCGVGIISLLLSRDFP-VFTSIIDKQESMLNYAKHNFYLNNLE-VKTYLNSFQEHNTEDRYDFIVSNPPFYDASVTqs 79
Cdd:pfam05175  37 DLGCGAGVLGAALAKESPdAELTMVDINARALESARENLAANGLEnGEVVASDVYSGVEDGKFDLIISNPPFHAGLAT-- 114

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1169282677  80 enrHLNIArysqhlpiEDFIKRVKTFLKPKG 110
Cdd:pfam05175 115 ---TYNVA--------QRFIADAKRHLRPGG 134
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 2-114 1.07e-08

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 53.51  E-value: 1.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   2 DVGCGVGIISLLLSRDFPVFTSI-IDKQESMLNYAKHNFYLNNLE--VKTYLNSFQEHNTEDRYDFIVSNPPFYDAsvtQ 78
Cdd:TIGR00536 120 DLGTGSGCIALALAYEFPNAEVIaVDISPDALAVAEENAEKNQLEhrVEFIQSNLFEPLAGQKIDIIVSNPPYIDE---E 196

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1169282677  79 SENRHLNIARYSQHLP----------IEDFIKRVKTFLKPKGWFIF 114
Cdd:TIGR00536 197 DLADLPNVVRFEPLLAlvggddglniLRQIIELAPDYLKPNGFLVC 242
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 2-147 1.72e-08

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 52.86  E-value: 1.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   2 DVGCGVGIISLLLSRDFP---VFTSiiDKQESMLNYAKHNF-YLNNLEVKTYLNSFQEHNTEDRYDFIVSNPPfY----D 73
Cdd:PRK09328  114 DLGTGSGAIALALAKERPdaeVTAV--DISPEALAVARRNAkHGLGARVEFLQGDWFEPLPGGRFDLIVSNPP-YipeaD 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677  74 ASVTQSENRhlniarysQHLPIE---------DFIKRV----KTFLKPKGWFIFCYDAKQIDILLQHLKINGInpEKIQF 140
Cdd:PRK09328  191 IHLLQPEVR--------DHEPHLalfggedglDFYRRIieqaPRYLKPGGWLLLEIGYDQGEAVRALLAAAGF--ADVET 260


                  ....*....
gi 1169282677 141 VH--SKIDR 147
Cdd:PRK09328  261 RKdlAGRDR 269
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 2-116 4.64e-08

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: 49.35  E-value: 4.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   2 DVGCGVGIISLLLSRDFPVFTSIIDKQESMLNYAKHNFYLNNLEVKTYL--NSFQEHNTED-RYDFIVSNPPFydasvtq 78
Cdd:cd02440     4 DLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLkgDAEELPPEADeSFDVIISDPPL------- 76

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1169282677  79 senrhlniarYSQHLPIEDFIKRVKTFLKPKGWFIFCY 116
Cdd:cd02440    77 ----------HHLVEDLARFLEEARRLLKPGGVLVLTL 104
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 2-114 1.14e-07

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 50.53  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   2 DVGCGVGIISLLLSRDFP---VFTsiIDKQESMLNYAKHNFYLNNLE--VKTYL-NSFQEHNTEDRYDFIVSNPPfYdas 75
Cdd:COG2890   118 DLGTGSGAIALALAKERPdarVTA--VDISPDALAVARRNAERLGLEdrVRFLQgDLFEPLPGDGRFDLIVSNPP-Y--- 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169282677  76 VTQSEnRHLNIARYSQHLPIE---------DFIKRV----KTFLKPKGWFIF 114
Cdd:COG2890   192 IPEDE-IALLPPEVRDHEPRLaldggedglDFYRRIiaqaPRLLKPGGWLLL 242
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
2-114 1.91e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 47.51  E-value: 1.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   2 DVGCGVGIISLLLSRDFPVFTSI-IDKQESMLNYAKHNfyLNNLEVktYLNSFQEHNTEDRYDFIVSNppfydASVtqse 80
Cdd:COG4106     7 DLGCGTGRLTALLAERFPGARVTgVDLSPEMLARARAR--LPNVRF--VVADLRDLDPPEPFDLVVSN-----AAL---- 73

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1169282677  81 nrhlniarysQHLP-IEDFIKRVKTFLKPKGWFIF 114
Cdd:COG4106    74 ----------HWLPdHAALLARLAAALAPGGVLAV 98
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 2-114 1.21e-06

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: 45.78  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   2 DVGCGVGIISLLLSR-DFPVFtsIIDKQESMLNYAKHNfyLNNLEVKTYLNSFQEHNTED-RYDFIVSNppfydASVtqs 79
Cdd:COG2227    30 DVGCGTGRLALALARrGADVT--GVDISPEALEIARER--AAELNVDFVQGDLEDLPLEDgSFDLVICS-----EVL--- 97

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1169282677  80 enrhlniarysQHLP-IEDFIKRVKTFLKPKGWFIF 114
Cdd:COG2227    98 -----------EHLPdPAALLRELARLLKPGGLLLL 122
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
1-73 4.47e-06

16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 46.08  E-value: 4.47e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169282677   1 MDVGCGVGIISLLLSRDFP-VFTSIIDKQESMLNYAKHNFYLNNLEVKTYL-NSFQehNTEDRYDFIVSNPPFYD 73
Cdd:PRK09489  201 LDVGCGAGVLSAVLARHSPkIRLTLSDVSAAALESSRATLAANGLEGEVFAsNVFS--DIKGRFDMIISNPPFHD 273
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 1-114 3.64e-05

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: 43.41  E-value: 3.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   1 MDVGCGVGIIS---LLLSRDfPVFTSIIDKQEsmLNYAKHNFYLNNLEvktylNSFQEHNTED----RYDFIVSNPpfyd 73
Cdd:pfam06325 166 LDVGCGSGILAiaaLKLGAK-KVVGVDIDPVA--VRAAKENAELNGVE-----ARLEVYLPGDlpkeKADVVVANI---- 233

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1169282677  74 asvtqsenrhlnIARysqhlPIEDFIKRVKTFLKPKGWFIF 114
Cdd:pfam06325 234 ------------LAD-----PLIELAPDIYALVKPGGYLIL 257
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 2-114 5.71e-05

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 40.34  E-value: 5.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   2 DVGCGVGIISLLLSRDFPVFTSiIDKQESMLNYAKhnfylnnlevktylnsfqEHNTEDRYDFIVSNP---PFYDASVTq 78
Cdd:pfam08241   2 DVGCGTGLLTELLARLGARVTG-VDISPEMLELAR------------------EKAPREGLTFVVGDAedlPFPDNSFD- 61

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1169282677  79 senrhLNIARYS-QHLP-IEDFIKRVKTFLKPKGWFIF 114
Cdd:pfam08241  62 -----LVLSSEVlHHVEdPERALREIARVLKPGGILII 94
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
1-133 1.15e-04

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 41.68  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   1 MDVGCGVGIISLLLSR---------DfpvftsiIDKQeSMLNyAKHNFYLNNLEVKTYLNSFQEhntedRYDFIVSNppf 71
Cdd:PRK00517  124 LDVGCGSGILAIAAAKlgakkvlavD-------IDPQ-AVEA-ARENAELNGVELNVYLPQGDL-----KADVIVAN--- 186

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169282677  72 ydasvtqsenrhlnI-ARysqhlPIEDFIKRVKTFLKPKGWFIFC-YDAKQIDILLQHLKINGI 133
Cdd:PRK00517  187 --------------IlAN-----PLLELAPDLARLLKPGGRLILSgILEEQADEVLEAYEEAGF 231
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 2-115 1.18e-04

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 40.75  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   2 DVGCGVGIISLLLSRDFPVFTSiIDKQESMLNYAKHNFYLNNLEVktylnSFQEHNTEDrydfivsnPPFYDASVtqsen 81
Cdd:COG2226    28 DLGCGTGRLALALAERGARVTG-VDISPEMLELARERAAEAGLNV-----EFVVGDAED--------LPFPDGSF----- 88

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1169282677  82 rHLNIARYS-QHLP-IEDFIKRVKTFLKPKGWFIFC 115
Cdd:COG2226    89 -DLVISSFVlHHLPdPERALAEIARVLKPGGRLVVV 123
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
25-114 5.11e-04

Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 39.79  E-value: 5.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677  25 IDKQESMLNYAKHNFYLNNLEVKT--YLNSF-QEHNTEDRYDFIVSNPPFYdASVTQSENRHLNIARYSQHLPIED---- 97
Cdd:COG0286    81 QEINPTTYRLAKMNLLLHGIGDPNieLGDTLsNDGDELEKFDVVLANPPFG-GKWKKEELKDDLLGRFGYGLPPKSnadl 159

                          90
                  ....*....|....*...
gi 1169282677  98 -FIKRVKTFLKPKGWFIF 114
Cdd:COG0286   160 lFLQHILSLLKPGGRAAV 177
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 1-116 1.41e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 37.78  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   1 MDVGCGVGIISLLL-SRDFPVFTSI-IDKQESMLNYAKHNF---YLNNLEV-KTYLNSFQEHNTEDRYDFIVSNPPFYDA 74
Cdd:pfam13847   8 LDLGCGTGHLSFELaEELGPNAEVVgIDISEEAIEKARENAqklGFDNVEFeQGDIEELPELLEDDKFDVVISNCVLNHI 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1169282677  75 SVTQSenrhlniarysqhlpiedFIKRVKTFLKPKGWFIFCY 116
Cdd:pfam13847  88 PDPDK------------------VLQEILRVLKPGGRLIISD 111
L3_gln_methyl TIGR03533
protein-(glutamine-N5) methyltransferase, ribosomal protein L3-specific; Members of this ...
 1-83 1.56e-03

protein-(glutamine-N5) methyltransferase, ribosomal protein L3-specific; Members of this protein family methylate ribosomal protein L3 on a glutamine side chain. This family is related to HemK, a protein-glutamine methyltranferase for peptide chain release factors. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 274633 [Multi-domain]  Cd Length: 284  Bit Score: 38.26  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   1 MDVGCGVGIISLLLSRDFP-VFTSIIDKQESMLNYAKHNFYLNNLEVKTYL---NSFQEHnTEDRYDFIVSNPPFYDASV 76
Cdd:TIGR03533 126 LDLCTGSGCIAIACAYAFPeAEVDAVDISPDALAVAEINIERHGLEDRVTLiqsDLFAAL-PGRKYDLIVSNPPYVDAED 204

                          90
                  ....*....|
gi 1169282677  77 TQS---ENRH 83
Cdd:TIGR03533 205 MADlpaEYHH 214
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 1-114 3.15e-03

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 36.83  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   1 MDVGCGVGIISLLLSRDFPV-FTSIiDKQESMLNYAKHNFYLNNLE--VKTYLNSFQEHNTEDRYDFIVSNPPFYdasvt 77
Cdd:COG2230    56 LDIGCGWGGLALYLARRYGVrVTGV-TLSPEQLEYARERAAEAGLAdrVEVRLADYRDLPADGQFDAIVSIGMFE----- 129

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1169282677  78 qsenrHLNIARYsqhlpiEDFIKRVKTFLKPKGWFIF 114
Cdd:COG2230   130 -----HVGPENY------PAYFAKVARLLKPGGRLLL 155
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 2-126 3.62e-03

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 36.82  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   2 DVGCGVGIISLLL-SRDFPVFTSIiDKQESMLNYAKHNF---YLNNLEVKtyLNSFQE--HNTEDRYDFIVSNppfydas 75
Cdd:COG0500    32 DLGCGTGRNLLALaARFGGRVIGI-DLSPEAIALARARAakaGLGNVEFL--VADLAEldPLPAESFDLVVAF------- 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1169282677  76 vtqsenrhlNIARYSQHLPIEDFIKRVKTFLKPKGWFIFCYDAKQIDILLQ 126
Cdd:COG0500   102 ---------GVLHHLPPEEREALLRELARALKPGGVLLLSASDAAAALSLA 143
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
2-118 6.68e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 36.13  E-value: 6.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169282677   2 DVGCGVGIISLLLSrdfPVFTSI--IDKQESMLNYAK-----HNFYLNNLevktylNSFQEHntEDRYDFIVSNppfydA 74
Cdd:COG4976    52 DLGCGTGLLGEALR---PRGYRLtgVDLSEEMLAKARekgvyDRLLVADL------ADLAEP--DGRFDLIVAA-----D 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1169282677  75 SVTQSENrhlniarysqhlpIEDFIKRVKTFLKPKGWFIFCYDA 118
Cdd:COG4976   116 VLTYLGD-------------LAAVFAGVARALKPGGLFIFSVED 146
 
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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