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Conserved domains on  [gi|1958752250|ref|XP_038958877|]
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tRNA:m(4)X modification enzyme TRM13 homolog isoform X3 [Rattus norvegicus]

Protein Classification

class I SAM-dependent methyltransferase; bifunctional glycosyltransferase/class I SAM-dependent methyltransferase( domain architecture ID 10525157)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor| bifunctional glycosyltransferase/class I SAM-dependent methyltransferase catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds and/or the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TRM13 pfam05206
Methyltransferase TRM13; This is a family of eukaryotic proteins which are responsible for 2 ...
 24-328 2.27e-111

Methyltransferase TRM13; This is a family of eukaryotic proteins which are responsible for 2'-O-methylation of tRNA at position 4. TRM13 shows no sequence similarity to other known methyltransferases.


:

Pssm-ID: 398743  Cd Length: 256  Bit Score: 324.63  E-value: 2.27e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752250  24 KQQASILGNIEKLKLLGPRRCFVEFGAGKGKLSHWVDIAL--KDAENVHFILVEKVTTRFKVDGKHRKKNS--VFERLQI 99
Cdd:pfam05206   1 IQQSSLIGNLEELGLLNPDSAYVEFGAGRGELSRYVNQCIqeDKLGNSGYVLIDRASNRMKFDRKIRKDESepIIKRLRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752250 100 DIQHLCLNRLPVLREGRlPVVGIGKHLCGVATDLALRCLVETYAASfkekdeeplakrvkndktekesntlakegsekdv 179
Cdd:pfam05206  81 DIKDLNLDAVLSLEDGS-PVVAVSKHLCGAATDLTLRCLLNSLNNS---------------------------------- 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752250 180 petRTPVAGIVIALCCHHRCDWRHYVGKEYFKALGLGAVEFYYFQRMSSWATCGMRtsleasdvtaerkdaQKDEEEEHD 259
Cdd:pfam05206 126 ---TDKFRGLLIAMCCHHVCNWRTYVNREFLLELGITYDEFQILTKMVSWAVCGKR---------------DENSKEEKE 187

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752250 260 DVGDRLTDGSTDSLPGTLTVEEKKKIGHLCKLLIDQGRLQYLQQKGFSPALQYYTDPLVSLENVLLTAV 328
Cdd:pfam05206 188 KEEDDVVEGSVENHISGLSSEEREEIGLKCKRLIDEGRLLWLKEKGFEAELVKYVEPDVSLENVCLLAR 256
 
Name Accession Description Interval E-value
TRM13 pfam05206
Methyltransferase TRM13; This is a family of eukaryotic proteins which are responsible for 2 ...
 24-328 2.27e-111

Methyltransferase TRM13; This is a family of eukaryotic proteins which are responsible for 2'-O-methylation of tRNA at position 4. TRM13 shows no sequence similarity to other known methyltransferases.


Pssm-ID: 398743  Cd Length: 256  Bit Score: 324.63  E-value: 2.27e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752250  24 KQQASILGNIEKLKLLGPRRCFVEFGAGKGKLSHWVDIAL--KDAENVHFILVEKVTTRFKVDGKHRKKNS--VFERLQI 99
Cdd:pfam05206   1 IQQSSLIGNLEELGLLNPDSAYVEFGAGRGELSRYVNQCIqeDKLGNSGYVLIDRASNRMKFDRKIRKDESepIIKRLRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752250 100 DIQHLCLNRLPVLREGRlPVVGIGKHLCGVATDLALRCLVETYAASfkekdeeplakrvkndktekesntlakegsekdv 179
Cdd:pfam05206  81 DIKDLNLDAVLSLEDGS-PVVAVSKHLCGAATDLTLRCLLNSLNNS---------------------------------- 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752250 180 petRTPVAGIVIALCCHHRCDWRHYVGKEYFKALGLGAVEFYYFQRMSSWATCGMRtsleasdvtaerkdaQKDEEEEHD 259
Cdd:pfam05206 126 ---TDKFRGLLIAMCCHHVCNWRTYVNREFLLELGITYDEFQILTKMVSWAVCGKR---------------DENSKEEKE 187

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752250 260 DVGDRLTDGSTDSLPGTLTVEEKKKIGHLCKLLIDQGRLQYLQQKGFSPALQYYTDPLVSLENVLLTAV 328
Cdd:pfam05206 188 KEEDDVVEGSVENHISGLSSEEREEIGLKCKRLIDEGRLLWLKEKGFEAELVKYVEPDVSLENVCLLAR 256
 
Name Accession Description Interval E-value
TRM13 pfam05206
Methyltransferase TRM13; This is a family of eukaryotic proteins which are responsible for 2 ...
 24-328 2.27e-111

Methyltransferase TRM13; This is a family of eukaryotic proteins which are responsible for 2'-O-methylation of tRNA at position 4. TRM13 shows no sequence similarity to other known methyltransferases.


Pssm-ID: 398743  Cd Length: 256  Bit Score: 324.63  E-value: 2.27e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752250  24 KQQASILGNIEKLKLLGPRRCFVEFGAGKGKLSHWVDIAL--KDAENVHFILVEKVTTRFKVDGKHRKKNS--VFERLQI 99
Cdd:pfam05206   1 IQQSSLIGNLEELGLLNPDSAYVEFGAGRGELSRYVNQCIqeDKLGNSGYVLIDRASNRMKFDRKIRKDESepIIKRLRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752250 100 DIQHLCLNRLPVLREGRlPVVGIGKHLCGVATDLALRCLVETYAASfkekdeeplakrvkndktekesntlakegsekdv 179
Cdd:pfam05206  81 DIKDLNLDAVLSLEDGS-PVVAVSKHLCGAATDLTLRCLLNSLNNS---------------------------------- 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752250 180 petRTPVAGIVIALCCHHRCDWRHYVGKEYFKALGLGAVEFYYFQRMSSWATCGMRtsleasdvtaerkdaQKDEEEEHD 259
Cdd:pfam05206 126 ---TDKFRGLLIAMCCHHVCNWRTYVNREFLLELGITYDEFQILTKMVSWAVCGKR---------------DENSKEEKE 187

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752250 260 DVGDRLTDGSTDSLPGTLTVEEKKKIGHLCKLLIDQGRLQYLQQKGFSPALQYYTDPLVSLENVLLTAV 328
Cdd:pfam05206 188 KEEDDVVEGSVENHISGLSSEEREEIGLKCKRLIDEGRLLWLKEKGFEAELVKYVEPDVSLENVCLLAR 256
 
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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