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Conserved domains on  [gi|489919085|ref|WP_003822447|]
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MULTISPECIES: trans-aconitate 2-methyltransferase [Bifidobacterium]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11467871)

SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0032259|GO:0008757|GO:0008168|GO:1904047
PubMed:  12826405|12504684
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
10-63 3.44e-24

Trans-aconitate methyltransferase [Energy production and conversion];


:

Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 86.42  E-value: 3.44e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489919085  10 RMLDIGCGPGNSTAVLRERYPHAEILGVDSSPDMIEAARKAYPDIDFQLCDVST 63
Cdd:COG4106    4 RVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLPNVRFVVADLRD 57
 
Name Accession Description Interval E-value
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
10-63 3.44e-24

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 86.42  E-value: 3.44e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489919085  10 RMLDIGCGPGNSTAVLRERYPHAEILGVDSSPDMIEAARKAYPDIDFQLCDVST 63
Cdd:COG4106    4 RVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLPNVRFVVADLRD 57
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 8-63 6.32e-23

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 86.92  E-value: 6.32e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489919085   8 VKRMLDIGCGPGNSTAVLRERYPHAEILGVDSSPDMIEAARKAYPDIDFQLCDVST 63
Cdd:PRK01683  32 PRYVVDLGCGPGNSTELLVERWPAARITGIDSSPAMLAEARSRLPDCQFVEADIAS 87
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 12-61 1.83e-13

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 59.11  E-value: 1.83e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489919085  12 LDIGCGPGNSTAVLRERYpHAEILGVDSSPDMIEAARK----AYPDIDFQLCDV 61
Cdd:pfam13649  2 LDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERAREraaeAGLNVEFVQGDA 54
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 9-64 1.10e-10

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 54.21  E-value: 1.10e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489919085    9 KRMLDIGCGPGNSTAVLRERYPHAEILGVDSSPDMIEAARKAYP-DIDFQLCDVSTH 64
Cdd:TIGR02072  36 ASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLSeNVQFICGDAEKL 92
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 10-63 2.89e-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: 45.88  E-value: 2.89e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489919085  10 RMLDIGCGPGNSTAVLReRYPHAEILGVDSSPDMIEAARKA-----YPDIDFQLCDVST 63
Cdd:cd02440    1 RVLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAaaallADNVEVLKGDAEE 58
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
9-48 1.76e-06

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 42.79  E-value: 1.76e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 489919085     9 KRMLDIGCGPGNSTAVLRERYPHAEILGVDSSPDMIEAAR 48
Cdd:smart00828   1 KRVLDFGCGYGSDLIDLAERHPHLQLHGYTISPEQAEVGR 40
 
Name Accession Description Interval E-value
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
10-63 3.44e-24

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 86.42  E-value: 3.44e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489919085  10 RMLDIGCGPGNSTAVLRERYPHAEILGVDSSPDMIEAARKAYPDIDFQLCDVST 63
Cdd:COG4106    4 RVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLPNVRFVVADLRD 57
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 8-63 6.32e-23

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 86.92  E-value: 6.32e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489919085   8 VKRMLDIGCGPGNSTAVLRERYPHAEILGVDSSPDMIEAARKAYPDIDFQLCDVST 63
Cdd:PRK01683  32 PRYVVDLGCGPGNSTELLVERWPAARITGIDSSPAMLAEARSRLPDCQFVEADIAS 87
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 9-63 1.73e-14

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 64.71  E-value: 1.73e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489919085   9 KRMLDIGCGPGNSTAVLRERYPHAEILGVDSSPDMIEAARKayPDIDFQLCDVST 63
Cdd:PRK14103  31 RRVVDLGCGPGNLTRYLARRWPGAVIEALDSSPEMVAAARE--RGVDARTGDVRD 83
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 12-61 1.83e-13

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 59.11  E-value: 1.83e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489919085  12 LDIGCGPGNSTAVLRERYpHAEILGVDSSPDMIEAARK----AYPDIDFQLCDV 61
Cdd:pfam13649  2 LDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERAREraaeAGLNVEFVQGDA 54
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
5-61 1.65e-12

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 58.47  E-value: 1.65e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489919085   5 GGGVKRMLDIGCGPGNSTAVLRERYPHaeILGVDSSPDMIEAARKAYPDIDFQLCDV 61
Cdd:COG4976   44 PGPFGRVLDLGCGTGLLGEALRPRGYR--LTGVDLSEEMLAKAREKGVYDRLLVADL 98
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 10-61 1.05e-11

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 56.46  E-value: 1.05e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489919085  10 RMLDIGCGPGNSTAVLRERYpHAEILGVDSSPDMIEAARKAYP-----DIDFQLCDV 61
Cdd:COG0500   29 RVLDLGCGTGRNLLALAARF-GGRVIGIDLSPEAIALARARAAkaglgNVEFLVADL 84
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 9-61 5.45e-11

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: 53.84  E-value: 5.45e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489919085   9 KRMLDIGCGPGNSTAVLRERypHAEILGVDSSPDMIEAARKAYPD----IDFQLCDV 61
Cdd:COG2226   24 ARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEaglnVEFVVGDA 78
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 9-64 1.10e-10

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 54.21  E-value: 1.10e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489919085    9 KRMLDIGCGPGNSTAVLRERYPHAEILGVDSSPDMIEAARKAYP-DIDFQLCDVSTH 64
Cdd:TIGR02072  36 ASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLSeNVQFICGDAEKL 92
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 12-60 1.20e-10

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 51.98  E-value: 1.20e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 489919085  12 LDIGCGPGNSTAVLRERYPHAEILGVDSSPDMIEAARKAYPDIDFQLCD 60
Cdd:pfam08242  1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAV 49
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 9-61 1.67e-10

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: 51.94  E-value: 1.67e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489919085   9 KRMLDIGCGPGNSTAVLRERypHAEILGVDSSPDMIEAARKAYPD--IDFQLCDV 61
Cdd:COG2227   26 GRVLDVGCGTGRLALALARR--GADVTGVDISPEALEIARERAAElnVDFVQGDL 78
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 12-61 1.44e-09

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 48.82  E-value: 1.44e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489919085  12 LDIGCGPGNSTAVLRERYPHaeILGVDSSPDMIEAARKAYPD--IDFQLCDV 61
Cdd:pfam08241  1 LDVGCGTGLLTELLARLGAR--VTGVDISPEMLELAREKAPRegLTFVVGDA 50
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 9-61 5.44e-09

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 48.57  E-value: 5.44e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489919085    9 KRMLDIGCGPGNSTAVLRER-YPHAEILGVDSSPDMIEAAR-----KAYPDIDFQLCDV 61
Cdd:pfam13847   5 MRVLDLGCGTGHLSFELAEElGPNAEVVGIDISEEAIEKARenaqkLGFDNVEFEQGDI 63
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 10-63 2.89e-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: 45.88  E-value: 2.89e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489919085  10 RMLDIGCGPGNSTAVLReRYPHAEILGVDSSPDMIEAARKA-----YPDIDFQLCDVST 63
Cdd:cd02440    1 RVLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAaaallADNVEVLKGDAEE 58
PRK08317 PRK08317
hypothetical protein; Provisional
 10-50 2.90e-07

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 44.93  E-value: 2.90e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 489919085  10 RMLDIGCGPGNSTAVLRERY-PHAEILGVDSSPDMIEAARKA 50
Cdd:PRK08317  22 RVLDVGCGPGNDARELARRVgPEGRVVGIDRSEAMLALAKER 63
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 9-65 4.67e-07

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 44.52  E-value: 4.67e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489919085   9 KRMLDIGCGPGNSTAVLRERYP---HAEILGVDSSPDMIEAARKAYPDIDFqlCDVSTHR 65
Cdd:PRK11088  87 TALLDIGCGEGYYTHALADALPeitTMQLFGLDISKVAIKYAAKRYPQVTF--CVASSHR 144
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
9-48 1.76e-06

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 42.79  E-value: 1.76e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 489919085     9 KRMLDIGCGPGNSTAVLRERYPHAEILGVDSSPDMIEAAR 48
Cdd:smart00828   1 KRVLDFGCGYGSDLIDLAERHPHLQLHGYTISPEQAEVGR 40
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 1-49 2.00e-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: 42.10  E-value: 2.00e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 489919085   1 MPEDGGGvkRMLDIGCGPGNSTAVLRERYPHAEILGVDSSPDMIEAARK 49
Cdd:COG2813   45 LPEPLGG--RVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARA 91
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 10-60 4.16e-06

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 41.07  E-value: 4.16e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489919085  10 RMLDIGCGPGNSTAVLRERYpHAEILGVDSSPDMIEAARKAYPD------IDFQLCD 60
Cdd:COG2230   54 RVLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAEagladrVEVRLAD 109
PRK06922 PRK06922
class I SAM-dependent methyltransferase;
10-49 4.68e-06

class I SAM-dependent methyltransferase;


Pssm-ID: 180751 [Multi-domain]  Cd Length: 677  Bit Score: 41.78  E-value: 4.68e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 489919085  10 RMLDIGCGPGNSTAVLRERYPHAEILGVDSSPDMIEAARK 49
Cdd:PRK06922 421 TIVDVGAGGGVMLDMIEEETEDKRIYGIDISENVIDTLKK 460
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 9-56 1.68e-05

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 39.72  E-value: 1.68e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 489919085    9 KRMLDIGCGPGNSTAVLRERYPHAEilGVDSSPDMIEAARKAYPDIDF 56
Cdd:pfam13489  24 GRVLDFGCGTGIFLRLLRAQGFSVT--GVDPSPIAIERALLNVRFDQF 69
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 12-49 2.57e-05

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 39.36  E-value: 2.57e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 489919085  12 LDIGCGPGNSTAVLRERypHAEILGVDSSPDMIEAARK 49
Cdd:PRK10258  47 LDAGCGPGWMSRYWRER--GSQVTALDLSPPMLAQARQ 82
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 1-49 3.55e-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: 38.73  E-value: 3.55e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 489919085    1 MPEDGGGvkRMLDIGCGPGNSTAVLRERYPHAEILGVDSSPDMIEAARK 49
Cdd:pfam05175  27 LPKDLSG--KVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARE 73
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 9-60 4.50e-05

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 38.66  E-value: 4.50e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489919085   9 KRMLDIGCGPGNSTAVLRERypHAEILGVDSSPDMIEAARKAYPD------IDFQLCD 60
Cdd:PRK07580  65 LRILDAGCGVGSLSIPLARR--GAKVVASDISPQMVEEARERAPEaglagnITFEVGD 120
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 10-61 8.25e-05

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 37.83  E-value: 8.25e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489919085  10 RMLDIGCGPGNSTAVLRERYPH-AEILGVDSSPDMIEAARK------AYPDIDFQLCDV 61
Cdd:PRK00216  54 KVLDLACGTGDLAIALAKAVGKtGEVVGLDFSEGMLAVGREklrdlgLSGNVEFVQGDA 112
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 9-49 8.97e-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: 37.82  E-value: 8.97e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 489919085   9 KRMLDIGCGPGNSTAVLRERYPHAEILGVDSSPDMIEAARK 49
Cdd:COG4123   39 GRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARR 79
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 9-61 2.54e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 36.68  E-value: 2.54e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489919085   9 KRMLDIGCGPGN-STAVLRERyPHAEILGVDSSPDMIE-----AARKAYPDIDFQLCDV 61
Cdd:PRK09328 110 LRVLDLGTGSGAiALALAKER-PDAEVTAVDISPEALAvarrnAKHGLGARVEFLQGDW 167
PRK05785 PRK05785
hypothetical protein; Provisional
 6-47 3.61e-04

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 36.20  E-value: 3.61e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 489919085   6 GGVKRMLDIGCGPGNSTAVLRERYpHAEILGVDSSPDMIEAA 47
Cdd:PRK05785  50 GRPKKVLDVAAGKGELSYHFKKVF-KYYVVALDYAENMLKMN 90
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 4-49 3.65e-04

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 36.28  E-value: 3.65e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 489919085   4 DGGGVKRMLDIGCGPGN-STAVLRERyPHAEILGVDSSPDMIEAARK 49
Cdd:COG2890  109 PAGAPPRVLDLGTGSGAiALALAKER-PDARVTAVDISPDALAVARR 154
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 9-48 8.71e-04

Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal structure and biogenesis]; Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) is part of the Pathway/BioSystem: Archaeal ribosomal proteins


Pssm-ID: 444210 [Multi-domain]  Cd Length: 306  Bit Score: 35.32  E-value: 8.71e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 489919085   9 KRMLDIGCGPGNSTAVLRERYPH-AEILGVDSSPDMIEAAR 48
Cdd:COG5459   82 LTVLDVGAGPGTAAWAAADAWPSlLDATLLERSAAALALGR 122
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
 4-49 1.33e-03

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


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 34.08  E-value: 1.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 489919085    4 DGGGVKRMLDIGCGPGNSTAVLRERYPHAEILGVDSSPDMIEAARK 49
Cdd:pfam13679  22 DENGPITIVDHGAGKGYLGFILYYLKYGVRVYGIDTRAELVEKANA 67
CheR pfam01739
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ...
 6-53 1.38e-03

CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase - the C-terminal domain (this one) binds SAM.


Pssm-ID: 426403  Cd Length: 190  Bit Score: 34.56  E-value: 1.38e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489919085    6 GGVKRMLDIGCGPGN---STAV-LRERYPHAE-----ILGVDSSPDMIEAARKA-YPD 53
Cdd:pfam01739  29 GKRVRIWSAGCSSGEepySLAMlLKETFPNAArwdfkILATDIDLSVLEKARAGvYPE 86
PRK15451 PRK15451
carboxy-S-adenosyl-L-methionine synthase CmoA;
10-49 3.26e-03

carboxy-S-adenosyl-L-methionine synthase CmoA;


Pssm-ID: 185348  Cd Length: 247  Bit Score: 33.46  E-value: 3.26e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 489919085  10 RMLDIGCGPGNSTAVLRE--RYPHAEILGVDSSPDMIEAARK 49
Cdd:PRK15451  59 QVYDLGCSLGAATLSVRRniHHDNCKIIAIDNSPAMIERCRR 100
PLN02244 PLN02244
tocopherol O-methyltransferase
 3-48 3.58e-03

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 33.56  E-value: 3.58e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 489919085   3 EDGGGVKRMLDIGCGPGNSTAVLRERYpHAEILGVDSSPdmIEAAR 48
Cdd:PLN02244 114 DDEKRPKRIVDVGCGIGGSSRYLARKY-GANVKGITLSP--VQAAR 156
PRK15001 PRK15001
23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;
1-48 3.91e-03

23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;


Pssm-ID: 184963 [Multi-domain]  Cd Length: 378  Bit Score: 33.46  E-value: 3.91e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 489919085   1 MPEDGGGvkRMLDIGCGPGNSTAVLRERYPHAEILGVDSSPDMIEAAR 48
Cdd:PRK15001 224 LPENLEG--EIVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSR 269
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 6-49 3.98e-03

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: 33.48  E-value: 3.98e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 489919085    6 GGVKRMLDIGCGPGNSTAVLRERYPHAEILGVDSSPDMIEAARK 49
Cdd:TIGR00536 113 PPILHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEE 156
 
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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