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Conserved domains on  [gi|499884254|ref|WP_011564988|]
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tRNA (guanosine(46)-N7)-methyltransferase TrmB [Rubrobacter xylanophilus]

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 ...
 45-219 7.93e-56

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: 176.48  E-value: 7.93e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254  45 ELFGDQRPLELDVGCGTGEYICHLARSDPEANFVGVDLHLKSLHKAIRRAEEANLQNIKFICADFRQMYPLLRPSALRAV 124
Cdd:COG0220   27 ELFGNDAPLVLEIGFGKGEFLVELAAANPDINFIGIEVHEPGVAKALKKAEEEGLTNVRLLRGDAVELLELFPDGSLDRI 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254 125 YLHFPDPGIKPRYRKRRLFNERFLEEMHRAVVPGGRMSLVTDDEDYFRQMLELIERDGRWRRAHEEP-YLTGFDPPVKSR 203
Cdd:COG0220  107 YLNFPDPWPKKRHHKRRLVQPEFLALLARVLKPGGELHLATDWEDYAEEMLEVLSAHPGFENLAETGdYAPRPEDRPLTK 186

                        170
                 ....*....|....*.
gi 499884254 204 FQKMWERRGRTIYRFE 219
Cdd:COG0220  187 YERKGLRLGRPIYYLI 202
 
Name Accession Description Interval E-value
TrmB COG0220
tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 ...
 45-219 7.93e-56

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: 176.48  E-value: 7.93e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254  45 ELFGDQRPLELDVGCGTGEYICHLARSDPEANFVGVDLHLKSLHKAIRRAEEANLQNIKFICADFRQMYPLLRPSALRAV 124
Cdd:COG0220   27 ELFGNDAPLVLEIGFGKGEFLVELAAANPDINFIGIEVHEPGVAKALKKAEEEGLTNVRLLRGDAVELLELFPDGSLDRI 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254 125 YLHFPDPGIKPRYRKRRLFNERFLEEMHRAVVPGGRMSLVTDDEDYFRQMLELIERDGRWRRAHEEP-YLTGFDPPVKSR 203
Cdd:COG0220  107 YLNFPDPWPKKRHHKRRLVQPEFLALLARVLKPGGELHLATDWEDYAEEMLEVLSAHPGFENLAETGdYAPRPEDRPLTK 186

                        170
                 ....*....|....*.
gi 499884254 204 FQKMWERRGRTIYRFE 219
Cdd:COG0220  187 YERKGLRLGRPIYYLI 202
trmB PRK00121
tRNA (guanine-N(7)-)-methyltransferase; Reviewed
 25-211 7.58e-45

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


Pssm-ID: 234649  Cd Length: 202  Bit Score: 148.39  E-value: 7.58e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254  25 RFTGRQLYHEAERLPGLSSP-----ELFGDQRPLELDVGCGTGEYICHLARSDPEANFVGVDLHLKSLHKAIRRAEEANL 99
Cdd:PRK00121  10 RLTKGQQRAIEELWPRLSPApldwaELFGNDAPIHLEIGFGKGEFLVEMAKANPDINFIGIEVHEPGVGKALKKIEEEGL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254 100 QNIKFICAD----FRQMYPllrPSALRAVYLHFPDPGIKPRYRKRRLFNERFLEEMHRAVVPGGRMSLVTDDEDYFRQML 175
Cdd:PRK00121  90 TNLRLLCGDavevLLDMFP---DGSLDRIYLNFPDPWPKKRHHKRRLVQPEFLALYARKLKPGGEIHFATDWEGYAEYML 166

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 499884254 176 ELIERDGRWRRAHEEPYLTGFDPPVKSRFQKMWERR 211
Cdd:PRK00121 167 EVLSAEGGFLVSEAGDYVPRPEGRPMTEYERKGLRK 202
Methyltransf_4 pfam02390
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ...
 50-217 5.33e-41

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: 137.81  E-value: 5.33e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254   50 QRPLELDVGCGTGEYICHLARSDPEANFVGVDLHLKSLHKAIRRAEEANLQNIKFICAD-FRQMYPLLRPSALRAVYLHF 128
Cdd:pfam02390   1 DAPVFLEIGCGMGGFLVAMAKANPDKNFIGIEIRVPGVAKALKKIDALGLQNLRILCGNaLDVLPNYFPPGSLQKIFINF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254  129 PDPGIKPRYRKRRLFNERFLEEMHRAVVPGGRMSLVTDDEDYFRQMLELIERDGRWRRAHEEPYLTgfDPPVK-----SR 203
Cdd:pfam02390  81 PDPWPKKRHHKRRLLQPEFLKEYARVLKPGGVLHLATDVEEYAEEMLKHLAEHPLFERLDLENDLA--PGPLSplrpaTE 158

                         170
                  ....*....|....
gi 499884254  204 FQKMWERRGRTIYR 217
Cdd:pfam02390 159 YEQKVQRLGGPIYR 172
TIGR00091 TIGR00091
tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent ...
 44-222 3.79e-35

tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent methyltransferase is found in a single copy in most Bacteria. It is also found, with a short amino-terminal extension in eukaryotes. Its function is unknown. In E. coli, this protein flanks the DNA repair protein MutY, also called micA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 161703  Cd Length: 194  Bit Score: 123.24  E-value: 3.79e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254   44 PELFGDQRPLELDVGCGTGEYICHLARSDPEANFVGVDLHLKSLHKAIRRAEEANLQNIKFICADFRQMYPLLRP-SALR 122
Cdd:TIGR00091  10 ATVFGNKAPLHLEIGCGKGRFLIDMAKQNPDKNFLGIEIHTPIVLAANNKANKLGLKNLHVLCGDANELLDKFFPdGSLS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254  123 AVYLHFPDPGIKPRYRKRRLFNERFLEEMHRAVVPGGRMSLVTDDEDYFRQMLELIERDGRWRRAHEEPYLTG---FDPP 199
Cdd:TIGR00091  90 KVFLNFPDPWPKKRHNKRRITQPHFLKEYANVLKKGGVIHFKTDNEPLFEDMLKVLSENDLFENTSKSTDLNNsplSRPR 169

                         170       180
                  ....*....|....*....|...
gi 499884254  200 VKSRFQKMWERRGRTIYRFELVR 222
Cdd:TIGR00091 170 NMTEYEQRFERLGHPVFDLCFER 192
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 55-161 1.59e-12

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: 61.68  E-value: 1.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254  55 LDVGCGTGEYICHLARsDPEANFVGVDLHLKSLHKAIRRAEEANLQNIKFICADFRQmYPLLRPSALRAVYLHFPDPGIK 134
Cdd:cd02440    3 LDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEE-LPPEADESFDVIISDPPLHHLV 80

                         90       100
                 ....*....|....*....|....*..
gi 499884254 135 PRYRkrrlfneRFLEEMHRAVVPGGRM 161
Cdd:cd02440   81 EDLA-------RFLEEARRLLKPGGVL 100
 
Name Accession Description Interval E-value
TrmB COG0220
tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 ...
 45-219 7.93e-56

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: 176.48  E-value: 7.93e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254  45 ELFGDQRPLELDVGCGTGEYICHLARSDPEANFVGVDLHLKSLHKAIRRAEEANLQNIKFICADFRQMYPLLRPSALRAV 124
Cdd:COG0220   27 ELFGNDAPLVLEIGFGKGEFLVELAAANPDINFIGIEVHEPGVAKALKKAEEEGLTNVRLLRGDAVELLELFPDGSLDRI 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254 125 YLHFPDPGIKPRYRKRRLFNERFLEEMHRAVVPGGRMSLVTDDEDYFRQMLELIERDGRWRRAHEEP-YLTGFDPPVKSR 203
Cdd:COG0220  107 YLNFPDPWPKKRHHKRRLVQPEFLALLARVLKPGGELHLATDWEDYAEEMLEVLSAHPGFENLAETGdYAPRPEDRPLTK 186

                        170
                 ....*....|....*.
gi 499884254 204 FQKMWERRGRTIYRFE 219
Cdd:COG0220  187 YERKGLRLGRPIYYLI 202
trmB PRK00121
tRNA (guanine-N(7)-)-methyltransferase; Reviewed
 25-211 7.58e-45

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


Pssm-ID: 234649  Cd Length: 202  Bit Score: 148.39  E-value: 7.58e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254  25 RFTGRQLYHEAERLPGLSSP-----ELFGDQRPLELDVGCGTGEYICHLARSDPEANFVGVDLHLKSLHKAIRRAEEANL 99
Cdd:PRK00121  10 RLTKGQQRAIEELWPRLSPApldwaELFGNDAPIHLEIGFGKGEFLVEMAKANPDINFIGIEVHEPGVGKALKKIEEEGL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254 100 QNIKFICAD----FRQMYPllrPSALRAVYLHFPDPGIKPRYRKRRLFNERFLEEMHRAVVPGGRMSLVTDDEDYFRQML 175
Cdd:PRK00121  90 TNLRLLCGDavevLLDMFP---DGSLDRIYLNFPDPWPKKRHHKRRLVQPEFLALYARKLKPGGEIHFATDWEGYAEYML 166

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 499884254 176 ELIERDGRWRRAHEEPYLTGFDPPVKSRFQKMWERR 211
Cdd:PRK00121 167 EVLSAEGGFLVSEAGDYVPRPEGRPMTEYERKGLRK 202
Methyltransf_4 pfam02390
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ...
 50-217 5.33e-41

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: 137.81  E-value: 5.33e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254   50 QRPLELDVGCGTGEYICHLARSDPEANFVGVDLHLKSLHKAIRRAEEANLQNIKFICAD-FRQMYPLLRPSALRAVYLHF 128
Cdd:pfam02390   1 DAPVFLEIGCGMGGFLVAMAKANPDKNFIGIEIRVPGVAKALKKIDALGLQNLRILCGNaLDVLPNYFPPGSLQKIFINF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254  129 PDPGIKPRYRKRRLFNERFLEEMHRAVVPGGRMSLVTDDEDYFRQMLELIERDGRWRRAHEEPYLTgfDPPVK-----SR 203
Cdd:pfam02390  81 PDPWPKKRHHKRRLLQPEFLKEYARVLKPGGVLHLATDVEEYAEEMLKHLAEHPLFERLDLENDLA--PGPLSplrpaTE 158

                         170
                  ....*....|....
gi 499884254  204 FQKMWERRGRTIYR 217
Cdd:pfam02390 159 YEQKVQRLGGPIYR 172
TIGR00091 TIGR00091
tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent ...
 44-222 3.79e-35

tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent methyltransferase is found in a single copy in most Bacteria. It is also found, with a short amino-terminal extension in eukaryotes. Its function is unknown. In E. coli, this protein flanks the DNA repair protein MutY, also called micA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 161703  Cd Length: 194  Bit Score: 123.24  E-value: 3.79e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254   44 PELFGDQRPLELDVGCGTGEYICHLARSDPEANFVGVDLHLKSLHKAIRRAEEANLQNIKFICADFRQMYPLLRP-SALR 122
Cdd:TIGR00091  10 ATVFGNKAPLHLEIGCGKGRFLIDMAKQNPDKNFLGIEIHTPIVLAANNKANKLGLKNLHVLCGDANELLDKFFPdGSLS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254  123 AVYLHFPDPGIKPRYRKRRLFNERFLEEMHRAVVPGGRMSLVTDDEDYFRQMLELIERDGRWRRAHEEPYLTG---FDPP 199
Cdd:TIGR00091  90 KVFLNFPDPWPKKRHNKRRITQPHFLKEYANVLKKGGVIHFKTDNEPLFEDMLKVLSENDLFENTSKSTDLNNsplSRPR 169

                         170       180
                  ....*....|....*....|...
gi 499884254  200 VKSRFQKMWERRGRTIYRFELVR 222
Cdd:TIGR00091 170 NMTEYEQRFERLGHPVFDLCFER 192
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
 41-206 7.64e-21

bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) methyltransferase; Reviewed


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 89.92  E-value: 7.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254  41 LSSPELFGDQRPLELDVGCGTGEYICHLARSDPEANFVGVDLHLKSLHKAIRRAEEANLQNIKFICADFRQMYPLLRPSA 120
Cdd:PRK01544 338 FSKEKLVNEKRKVFLEIGFGMGEHFINQAKMNPDALFIGVEVYLNGVANVLKLAGEQNITNFLLFPNNLDLILNDLPNNS 417

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254 121 LRAVYLHFPDPGIKPRYRKRRLFNERFLEEMHRAVVPGGRMSLVTDDEDYFRQMLELIERDGRWRRAHEEPYLTGFDPPV 200
Cdd:PRK01544 418 LDGIYILFPDPWIKNKQKKKRIFNKERLKILQDKLKDNGNLVFASDIENYFYEAIELIQQNGNFEIINKNDYLKPHDNYV 497


                 ....*.
gi 499884254 201 KSRFQK 206
Cdd:PRK01544 498 ITKYHQ 503
PRK14121 PRK14121
tRNA (guanine-N(7)-)-methyltransferase; Provisional
 44-216 1.46e-20

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


Pssm-ID: 237615  Cd Length: 390  Bit Score: 88.48  E-value: 1.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254  44 PELFGDQRPLELDVGCGTGEYICHLARSDPEANFVGVDLHLKSLHKAIRRAEEANLQNIKFICADFRQMYPLLRPSALRA 123
Cdd:PRK14121 116 DFISKNQEKILIEIGFGSGRHLLYQAKNNPNKLFIGIEIHTPSIEQVLKQIELLNLKNLLIINYDARLLLELLPSNSVEK 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254 124 VYLHFPDP-GIKPryrKRRLFNERFLEEMHRAVVPGGRMSLVTDDEDYFRQMLELIErdgrwrrAHEEPYLT---GFDPP 199
Cdd:PRK14121 196 IFVHFPVPwDKKP---HRRVISEDFLNEALRVLKPGGTLELRTDSELYFEFSLELFL-------KLPKAKIEikkNAQLE 265

                        170
                 ....*....|....*..
gi 499884254 200 VKSRFQKMWERRGRTIY 216
Cdd:PRK14121 266 VSSKYEDRWKKQNKDIY 282
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 55-159 2.09e-17

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 74.14  E-value: 2.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254   55 LDVGCGTGEYICHLARSdPEANFVGVDLHLKSLHKAIRRAEEANLqNIKFICADFRQMyPLLRPSA----LRAVYLHFPD 130
Cdd:pfam13649   2 LDLGCGTGRLTLALARR-GGARVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDL-PFPDGSFdlvvSSGVLHHLPD 78

                          90       100
                  ....*....|....*....|....*....
gi 499884254  131 PGIkpryrkrrlfnERFLEEMHRAVVPGG 159
Cdd:pfam13649  79 PDL-----------EAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 55-182 2.13e-17

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: 75.42  E-value: 2.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254  55 LDVGCGTGEYICHLARSDpeANFVGVDLHLKSLHKAIRRAEEANLqNIKFICADFRQMyPLLRPSA----LRAVYLHFPD 130
Cdd:COG2226   27 LDLGCGTGRLALALAERG--ARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAEDL-PFPDGSFdlviSSFVLHHLPD 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499884254 131 PgikpryrkrrlfnERFLEEMHRAVVPGGRMSLVTDDEDYFRQMLELIERDG 182
Cdd:COG2226  103 P-------------ERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEAG 141
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 55-204 2.09e-14

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 69.17  E-value: 2.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254  55 LDVGCGTGEYICHLARSdPEANFVGVDLHLKSLHKAIRRAEEANLQNIKFICADFRQMYPLLRPSA----LRAVyLHFpd 130
Cdd:COG0500   31 LDLGCGTGRNLLALAAR-FGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAELDPLPAESFdlvvAFGV-LHH-- 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499884254 131 pgIKPRYRkrrlfnERFLEEMHRAVVPGGR--MSLVTDDEDYFRQMLELIERDGRWRRAHEEPYLTGFDPPVKSRF 204
Cdd:COG0500  107 --LPPEER------EALLRELARALKPGGVllLSASDAAAALSLARLLLLATASLLELLLLLRLLALELYLRALLA 174
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
55-161 1.34e-13

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 64.46  E-value: 1.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254  55 LDVGCGTGEYICHLARSDPEANFVGVDLHlkslHKAIRRAeEANLQNIKFICADFRQmYPLLRPSAL---RAVYLHFPDP 131
Cdd:COG4106    6 LDLGCGTGRLTALLAERFPGARVTGVDLS----PEMLARA-RARLPNVRFVVADLRD-LDPPEPFDLvvsNAALHWLPDH 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 499884254 132 gikpryrkrrlfnERFLEEMHRAVVPGGRM 161
Cdd:COG4106   80 -------------AALLARLAAALAPGGVL 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 55-165 4.88e-13

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: 63.50  E-value: 4.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254  55 LDVGCGTGEYICHLARSDpeANFVGVDLHLKSLHKAIRRAEEanlQNIKFICADFRQMyPLLRPSA----LRAVYLHFPD 130
Cdd:COG2227   29 LDVGCGTGRLALALARRG--ADVTGVDISPEALEIARERAAE---LNVDFVQGDLEDL-PLEDGSFdlviCSEVLEHLPD 102

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 499884254 131 PgikpryrkrrlfnERFLEEMHRAVVPGGRMSLVT 165
Cdd:COG2227  103 P-------------AALLRELARLLKPGGLLLLST 124
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 55-161 1.59e-12

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: 61.68  E-value: 1.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254  55 LDVGCGTGEYICHLARsDPEANFVGVDLHLKSLHKAIRRAEEANLQNIKFICADFRQmYPLLRPSALRAVYLHFPDPGIK 134
Cdd:cd02440    3 LDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEE-LPPEADESFDVIISDPPLHHLV 80

                         90       100
                 ....*....|....*....|....*..
gi 499884254 135 PRYRkrrlfneRFLEEMHRAVVPGGRM 161
Cdd:cd02440   81 EDLA-------RFLEEARRLLKPGGVL 100
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 55-163 3.58e-12

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 60.37  E-value: 3.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254   55 LDVGCGTGEYICHLARSDPeaNFVGVDLHLKSLHKAIRRAEEANLqniKFICADFRQMyPLLRPSA----LRAVYLHFPD 130
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMLELAREKAPREGL---TFVVGDAEDL-PFPDNSFdlvlSSEVLHHVED 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 499884254  131 PgikpryrkrrlfnERFLEEMHRAVVPGGRMSL 163
Cdd:pfam08241  75 P-------------ERALREIARVLKPGGILII 94
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 55-166 2.81e-10

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 56.86  E-value: 2.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254  55 LDVGCGTGEYICHLARsDPEANFVGVDLHLKSLHKAIRRAEEANLQN-IKFICADFRQmypLLRPSALRAV-----YLHF 128
Cdd:COG2230   56 LDIGCGWGGLALYLAR-RYGVRVTGVTLSPEQLEYARERAAEAGLADrVEVRLADYRD---LPADGQFDAIvsigmFEHV 131

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 499884254 129 PDPGIkpryrkrrlfnERFLEEMHRAVVPGGRMSLVTD 166
Cdd:COG2230  132 GPENY-----------PAYFAKVARLLKPGGRLLLHTP 158
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 55-181 3.74e-10

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 56.27  E-value: 3.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254   55 LDVGCGTGeYICHLARS--DPEANFVGVDLHLKSLHKAIRRAEEANLQNIKFICADFRQMYPLLRPSA-----LRAVYLH 127
Cdd:pfam13847   8 LDLGCGTG-HLSFELAEelGPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEELPELLEDDKfdvviSNCVLNH 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 499884254  128 FPDPgikpryrkrrlfnERFLEEMHRAVVPGGRmsLVTDDEDYFRQMLELIERD 181
Cdd:pfam13847  87 IPDP-------------DKVLQEILRVLKPGGR--LIISDPDSLAELPAHVKED 125
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 55-160 5.65e-09

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 51.98  E-value: 5.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254   55 LDVGCGTGEYICHLARSDPEANFVGVDLHLKSLHKAIRRAEEANLQNIKFIcaDFRQMYPLLRPSA------LRAVYLHF 128
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVRV--ELFQLDLGELDPGsfdvvvASNVLHHL 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 499884254  129 PDPgikpryrkrrlfnERFLEEMHRAVVPGGR 160
Cdd:pfam08242  79 ADP-------------RAVLRNIRRLLKPGGV 97
PRK08317 PRK08317
hypothetical protein; Provisional
 55-176 1.35e-07

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 50.32  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254  55 LDVGCGTGEYICHLA-RSDPEANFVGVDLHLKSLHKAIRRAeEANLQNIKFICADFRQM-YPLLRPSALRA--VYLHFPD 130
Cdd:PRK08317  24 LDVGCGPGNDARELArRVGPEGRVVGIDRSEAMLALAKERA-AGLGPNVEFVRGDADGLpFPDGSFDAVRSdrVLQHLED 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 499884254 131 PgikpryrkrrlfnERFLEEMHRAVVPGGRM--------SLV--TDDEDYFRQMLE 176
Cdd:PRK08317 103 P-------------ARALAEIARVLRPGGRVvvldtdwdTLVwhSGDRALMRKILN 145
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 55-112 1.67e-06

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: 47.28  E-value: 1.67e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 499884254   55 LDVGCGTGEYICHLARSDPEANFVGVDLHLKSLhkaiRRAEEANLQNIKFICADFRQM 112
Cdd:TIGR02072  39 LDIGCGTGYLTRALLKRFPQAEFIALDISAGML----AQAKTKLSENVQFICGDAEKL 92
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 55-160 6.44e-06

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 45.33  E-value: 6.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254   55 LDVGCGTGEYICHLARSDPE-ANFVGVDLHLKSLHKAIRRAEEANlqNIKFICADFRQMyPLLRPSaLRAVYLHFpdpGI 133
Cdd:TIGR01934  44 LDVACGTGDLAIELAKSAPDrGKVTGVDFSSEMLEVAKKKSELPL--NIEFIQADAEAL-PFEDNS-FDAVTIAF---GL 116

                          90       100
                  ....*....|....*....|....*....
gi 499884254  134 K--PRYRKRrlfnerfLEEMHRAVVPGGR 160
Cdd:TIGR01934 117 RnvTDIQKA-------LREMYRVLKPGGR 138
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
55-199 4.21e-05

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 42.68  E-value: 4.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254  55 LDVGCGTGEYICHLArsdPEANFV-GVDLhlkSlHKAIRRAEEANLQnIKFICADFRQMYPLLRPSAL---RAVYLHFPD 130
Cdd:COG4976   51 LDLGCGTGLLGEALR---PRGYRLtGVDL---S-EEMLAKAREKGVY-DRLLVADLADLAEPDGRFDLivaADVLTYLGD 122

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499884254 131 PgikpryrkrrlfnERFLEEMHRAVVPGGRMSLVTDDEdyfrqmlelierDGRWRRAHEEPYL------TGFDPP 199
Cdd:COG4976  123 L-------------AAVFAGVARALKPGGLFIFSVEDA------------DGSGRYAHSLDYVrdllaaAGFEVP 172
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 55-160 5.67e-05

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 42.83  E-value: 5.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254  55 LDVGCGTGEYICHLAR-SDPEANFVGVDLHLKSLHKAIRRAEEANLQ-NIKFICADfrqmypllrpsALRavyLHFPDP- 131
Cdd:PRK00216  56 LDLACGTGDLAIALAKaVGKTGEVVGLDFSEGMLAVGREKLRDLGLSgNVEFVQGD-----------AEA---LPFPDNs 121

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 499884254 132 --------GIK--PRYrkrrlfnERFLEEMHRAVVPGGR 160
Cdd:PRK00216 122 fdavtiafGLRnvPDI-------DKALREMYRVLKPGGR 153
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 55-108 1.12e-04

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: 41.71  E-value: 1.12e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499884254  55 LDVGCGTGeYI-CHLARSDPEANFVGVDLHLKSLHKAIRRAEEANLQNIKFICAD 108
Cdd:COG2813   54 LDLGCGYG-VIgLALAKRNPEARVTLVDVNARAVELARANAAANGLENVEVLWSD 107
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
55-182 4.03e-04

Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 40.04  E-value: 4.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254   55 LDVGCGTGEYICHLAR-SDPEANFVGVDlHLKSL-HKAIRRAEEANLQNIKFICADFRQMYPLLRPsaLRAVYLHFPDPG 132
Cdd:pfam01135  78 LEIGSGSGYLTACFARmVGEVGRVVSIE-HIPELvEIARRNLEKLGLENVIVVVGDGRQGWPEFAP--YDAIHVGAAAPE 154

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 499884254  133 IkPryrkRRLFNErfLEEMHRAVVPGGrmslvtddEDYfRQMLELIERDG 182
Cdd:pfam01135 155 I-P----EALIDQ--LKEGGRLVIPVG--------PNG-NQVLQQFDKRN 188
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
48-161 2.56e-03

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 37.80  E-value: 2.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254   48 GDQRPLE-LDVGCGTGEYICHLARS-DPEANFVGVDLHLKSLHKAIRRAEEANLQNIKFICADfrqmypllrpsalrAVY 125
Cdd:pfam01209  39 GVKRGNKfLDVAGGTGDWTFGLSDSaGSSGKVVGLDINENMLKEGEKKAKEEGKYNIEFLQGN--------------AEE 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 499884254  126 LHFPDP---------GIK--PRYRKrrlfnerFLEEMHRAVVPGGRM 161
Cdd:pfam01209 105 LPFEDDsfdivtisfGLRnfPDYLK-------VLKEAFRVLKPGGRV 144
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 55-164 4.80e-03

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: 37.05  E-value: 4.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499884254  55 LDVGCGTGEyICHL--ARSdPEANFVGVDLHLKSLHKAIRRAEEANLQN-IKFICADFRQMYPLLRPSALRAV-----Yl 126
Cdd:COG4123   42 LDLGTGTGV-IALMlaQRS-PGARITGVEIQPEAAELARRNVALNGLEDrITVIHGDLKEFAAELPPGSFDLVvsnppY- 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 499884254 127 HFPDPGIKPRYRKRRL--FN-----ERFLEEMHRAVVPGGRMSLV 164
Cdd:COG4123  119 FKAGSGRKSPDEARAIarHEdaltlEDLIRAAARLLKPGGRFALI 163
 
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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