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Conserved domains on  [gi|2197376918|ref|WP_239247413|]
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MULTISPECIES: tRNA (guanosine(46)-N(7))-methyltransferase TrmB [unclassified Alteromonas]

Protein Classification

tRNA (guanine(46)-N(7))-methyltransferase TrmB( domain architecture ID 11415463)

tRNA (guanine(46)-N(7))-methyltransferase TrmB catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA

CATH:  3.40.50.150
EC:  2.1.1.33
Gene Symbol:  trmB
Gene Ontology:  GO:0008176|GO:0008168|GO:1904047|GO:0008176
PubMed:  12826405|12504684
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TrmB COG0220
tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 ...
 53-218 1.11e-33

tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 N7-methylase TrmB is part of the Pathway/BioSystem: tRNA modification


:

Pssm-ID: 439990  Cd Length: 204  Bit Score: 119.86  E-value: 1.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197376918  53 GFSGEIILDSCCGVGESTANIAGANPNARVIGIDKSALRVDKHEHYSAQQ--DNYRVIRADVNDFWRLVKQSSwnVTQHF 130
Cdd:COG0220    30 GNDAPLVLEIGFGKGEFLVELAAANPDINFIGIEVHEPGVAKALKKAEEEglTNVRLLRGDAVELLELFPDGS--LDRIY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197376918 131 LLYPNPYPKKTQVQKRWHgSAAMVDLMA--ITPN--IEVRSNWLIYLMEFAQA-AKHYGMvsDLSEVTGDDH-------M 198
Cdd:COG0220   108 LNFPDPWPKKRHHKRRLV-QPEFLALLArvLKPGgeLHLATDWEDYAEEMLEVlSAHPGF--ENLAETGDYAprpedrpL 184

                         170       180
                  ....*....|....*....|
gi 2197376918 199 TPFERKYRGSGQSCWQLNCR 218
Cdd:COG0220   185 TKYERKGLRLGRPIYYLIFR 204
 
Name Accession Description Interval E-value
TrmB COG0220
tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 ...
 53-218 1.11e-33

tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 N7-methylase TrmB is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439990  Cd Length: 204  Bit Score: 119.86  E-value: 1.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197376918  53 GFSGEIILDSCCGVGESTANIAGANPNARVIGIDKSALRVDKHEHYSAQQ--DNYRVIRADVNDFWRLVKQSSwnVTQHF 130
Cdd:COG0220    30 GNDAPLVLEIGFGKGEFLVELAAANPDINFIGIEVHEPGVAKALKKAEEEglTNVRLLRGDAVELLELFPDGS--LDRIY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197376918 131 LLYPNPYPKKTQVQKRWHgSAAMVDLMA--ITPN--IEVRSNWLIYLMEFAQA-AKHYGMvsDLSEVTGDDH-------M 198
Cdd:COG0220   108 LNFPDPWPKKRHHKRRLV-QPEFLALLArvLKPGgeLHLATDWEDYAEEMLEVlSAHPGF--ENLAETGDYAprpedrpL 184

                         170       180
                  ....*....|....*....|
gi 2197376918 199 TPFERKYRGSGQSCWQLNCR 218
Cdd:COG0220   185 TKYERKGLRLGRPIYYLIFR 204
Methyltransf_4 pfam02390
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ...
 58-215 1.34e-07

Putative methyltransferase; This is a family of putative methyltransferases. The aligned region contains the GXGXG S-AdoMet binding site suggesting a putative methyltransferase activity.


Pssm-ID: 367068  Cd Length: 173  Bit Score: 49.60  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197376918  58 IILDSCCGVGESTANIAGANPNARVIGIDKSALRVDKHEHYSAQQD--NYRVIRADVNDFWR--LVKQSSWNVtqhFLLY 133
Cdd:pfam02390   4 VFLEIGCGMGGFLVAMAKANPDKNFIGIEIRVPGVAKALKKIDALGlqNLRILCGNALDVLPnyFPPGSLQKI---FINF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197376918 134 PNPYPKKTQVQKRW---HGSAAMVDLMAITPNIEVRSNWLIYlmeFAQAAKHYGMVSDLSEVTGDDH-----------MT 199
Cdd:pfam02390  81 PDPWPKKRHHKRRLlqpEFLKEYARVLKPGGVLHLATDVEEY---AEEMLKHLAEHPLFERLDLENDlapgplsplrpAT 157

                         170
                  ....*....|....*.
gi 2197376918 200 PFERKYRGSGQSCWQL 215
Cdd:pfam02390 158 EYEQKVQRLGGPIYRL 173
trmB PRK00121
tRNA (guanine-N(7)-)-methyltransferase; Reviewed
 57-140 1.37e-07

tRNA (guanine-N(7)-)-methyltransferase; Reviewed


Pssm-ID: 234649  Cd Length: 202  Bit Score: 50.16  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197376918  57 EIILDSCCGVGESTANIAGANPNARVIGIDK------SALR-VDKHEHysaqqDNYRVIRADVNDFWR--LVKQSswnVT 127
Cdd:PRK00121   42 PIHLEIGFGKGEFLVEMAKANPDINFIGIEVhepgvgKALKkIEEEGL-----TNLRLLCGDAVEVLLdmFPDGS---LD 113

                          90
                  ....*....|...
gi 2197376918 128 QHFLLYPNPYPKK 140
Cdd:PRK00121  114 RIYLNFPDPWPKK 126
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 59-115 2.63e-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: 39.34  E-value: 2.63e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2197376918  59 ILDSCCGVGESTANIAgANPNARVIGIDKS--ALRVDKHEHYSAQQDNYRVIRADVNDF 115
Cdd:cd02440     2 VLDLGCGTGALALALA-SGPGARVTGVDISpvALELARKAAAALLADNVEVLKGDAEEL 59
 
Name Accession Description Interval E-value
TrmB COG0220
tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 ...
 53-218 1.11e-33

tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 N7-methylase TrmB is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439990  Cd Length: 204  Bit Score: 119.86  E-value: 1.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197376918  53 GFSGEIILDSCCGVGESTANIAGANPNARVIGIDKSALRVDKHEHYSAQQ--DNYRVIRADVNDFWRLVKQSSwnVTQHF 130
Cdd:COG0220    30 GNDAPLVLEIGFGKGEFLVELAAANPDINFIGIEVHEPGVAKALKKAEEEglTNVRLLRGDAVELLELFPDGS--LDRIY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197376918 131 LLYPNPYPKKTQVQKRWHgSAAMVDLMA--ITPN--IEVRSNWLIYLMEFAQA-AKHYGMvsDLSEVTGDDH-------M 198
Cdd:COG0220   108 LNFPDPWPKKRHHKRRLV-QPEFLALLArvLKPGgeLHLATDWEDYAEEMLEVlSAHPGF--ENLAETGDYAprpedrpL 184

                         170       180
                  ....*....|....*....|
gi 2197376918 199 TPFERKYRGSGQSCWQLNCR 218
Cdd:COG0220   185 TKYERKGLRLGRPIYYLIFR 204
Methyltransf_4 pfam02390
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ...
 58-215 1.34e-07

Putative methyltransferase; This is a family of putative methyltransferases. The aligned region contains the GXGXG S-AdoMet binding site suggesting a putative methyltransferase activity.


Pssm-ID: 367068  Cd Length: 173  Bit Score: 49.60  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197376918  58 IILDSCCGVGESTANIAGANPNARVIGIDKSALRVDKHEHYSAQQD--NYRVIRADVNDFWR--LVKQSSWNVtqhFLLY 133
Cdd:pfam02390   4 VFLEIGCGMGGFLVAMAKANPDKNFIGIEIRVPGVAKALKKIDALGlqNLRILCGNALDVLPnyFPPGSLQKI---FINF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197376918 134 PNPYPKKTQVQKRW---HGSAAMVDLMAITPNIEVRSNWLIYlmeFAQAAKHYGMVSDLSEVTGDDH-----------MT 199
Cdd:pfam02390  81 PDPWPKKRHHKRRLlqpEFLKEYARVLKPGGVLHLATDVEEY---AEEMLKHLAEHPLFERLDLENDlapgplsplrpAT 157

                         170
                  ....*....|....*.
gi 2197376918 200 PFERKYRGSGQSCWQL 215
Cdd:pfam02390 158 EYEQKVQRLGGPIYRL 173
trmB PRK00121
tRNA (guanine-N(7)-)-methyltransferase; Reviewed
 57-140 1.37e-07

tRNA (guanine-N(7)-)-methyltransferase; Reviewed


Pssm-ID: 234649  Cd Length: 202  Bit Score: 50.16  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197376918  57 EIILDSCCGVGESTANIAGANPNARVIGIDK------SALR-VDKHEHysaqqDNYRVIRADVNDFWR--LVKQSswnVT 127
Cdd:PRK00121   42 PIHLEIGFGKGEFLVEMAKANPDINFIGIEVhepgvgKALKkIEEEGL-----TNLRLLCGDAVEVLLdmFPDGS---LD 113

                          90
                  ....*....|...
gi 2197376918 128 QHFLLYPNPYPKK 140
Cdd:PRK00121  114 RIYLNFPDPWPKK 126
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
59-115 2.60e-06

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 44.43  E-value: 2.60e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2197376918  59 ILDSCCGVGESTANIAGANPNARVIGIDKSALRVDKHEhysAQQDNYRVIRADVNDF 115
Cdd:COG4106     5 VLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARAR---ARLPNVRFVVADLRDL 58
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 59-115 6.90e-05

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 40.62  E-value: 6.90e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2197376918  59 ILDSCCGVGESTANIAgANPNARVIGIDKSALRVDK-HEHYSAQQDNYRVIRADVNDF 115
Cdd:pfam13649   1 VLDLGCGTGRLTLALA-RRGGARVTGVDLSPEMLERaRERAAEAGLNVEFVQGDAEDL 57
PRK08317 PRK08317
hypothetical protein; Provisional
 49-89 2.50e-04

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 40.69  E-value: 2.50e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2197376918  49 AWLDGFSGEIILDSCCGVGESTANIAGA-NPNARVIGIDKSA 89
Cdd:PRK08317   13 ELLAVQPGDRVLDVGCGPGNDARELARRvGPEGRVVGIDRSE 54
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 59-115 2.63e-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: 39.34  E-value: 2.63e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2197376918  59 ILDSCCGVGESTANIAgANPNARVIGIDKS--ALRVDKHEHYSAQQDNYRVIRADVNDF 115
Cdd:cd02440     2 VLDLGCGTGALALALA-SGPGARVTGVDISpvALELARKAAAALLADNVEVLKGDAEEL 59
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 49-114 4.07e-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: 39.21  E-value: 4.07e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2197376918  49 AWLDGFSGEIILDSCCGVGESTANIAGAnpNARVIGIDKSALRVDK-HEHYSAQQDNYRVIRADVND 114
Cdd:COG2226    16 AALGLRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELaRERAAEAGLNVEFVVGDAED 80
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 55-126 5.48e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 38.94  E-value: 5.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2197376918  55 SGEIILDSCCGVGESTANIAG-ANPNARVIGIDKS--ALRVDKHEHYSAQQDNYRVIRADVNDFWRLVKQSSWNV 126
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEeLGPNAEVVGIDISeeAIEKARENAQKLGFDNVEFEQGDIEELPELLEDDKFDV 77
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 49-114 1.10e-03

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 38.98  E-value: 1.10e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2197376918  49 AWLDGFSGEIILDSCCGVGESTANIAG-ANPNARVIGIDKSA--LRV--DKHEHYSaQQDNYRVIRADVND 114
Cdd:PRK00216   45 KWLGVRPGDKVLDLACGTGDLAIALAKaVGKTGEVVGLDFSEgmLAVgrEKLRDLG-LSGNVEFVQGDAEA 114
Methyltr_RsmB-F pfam01189
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ...
 50-94 1.79e-03

16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ribosomal methyltransferase RsmB/F enzyme. There is a catalytic cysteine residue at 180 in UniProtKB:Q5SII2, with another highly conserved cysteine at residue 230. It methylates the C(5) position of cytosine 2870 (m5C2870) in 25S rRNA.


Pssm-ID: 426109 [Multi-domain]  Cd Length: 199  Bit Score: 38.17  E-value: 1.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2197376918  50 WLDGFSGEIILDSCCGVGESTANIAGANPN-ARVIGIDKSALRVDK 94
Cdd:pfam01189   3 LLAPQEGETILDMCAAPGGKTTHIAELMKNqGTVVAVDINKHRLKR 48
PRK10901 PRK10901
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
46-111 7.53e-03

16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;


Pssm-ID: 236790 [Multi-domain]  Cd Length: 427  Bit Score: 36.71  E-value: 7.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2197376918  46 DVSA-----WLDGFSGEIILDSCCGVGESTANIAGANPNARVIGIDKSALRVDK-HEHYSAQQDNYRVIRAD 111
Cdd:PRK10901  230 DAAAqlaatLLAPQNGERVLDACAAPGGKTAHILELAPQAQVVALDIDAQRLERvRENLQRLGLKATVIVGD 301
 
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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