NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568922675|ref|XP_006501487|]
View 

tRNA:m(4)X modification enzyme TRM13 homolog isoform X2 [Mus musculus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 7.43e-115

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: 333.11  E-value: 7.43e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922675   24 KQQASILGNIEKLKLLGPRRCFVEFGAGKGKLSHWVDIAL--KDAENVHFILVERVTTRFKVDGKHRKKDS--VFERLQI 99
Cdd:pfam05206   1 IQQSSLIGNLEELGLLNPDSAYVEFGAGRGELSRYVNQCIqeDKLGNSGYVLIDRASNRMKFDRKIRKDESepIIKRLRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922675  100 DIQHLCLNRVPVLREGRlPVVGIGKHLCGVATDVALRCLVETYAASfeekdeeplakrikndktekesntlakegsekdv 179
Cdd:pfam05206  81 DIKDLNLDAVLSLEDGS-PVVAVSKHLCGAATDLTLRCLLNSLNNS---------------------------------- 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922675  180 petWTPVAGIVIALCCHHRCDWRHYVGKEYFKALGLGAVEFYYFQRMSSWATCGMRtslegsdvtperkdaQRDENEEHD 259
Cdd:pfam05206 126 ---TDKFRGLLIAMCCHHVCNWRTYVNREFLLELGITYDEFQILTKMVSWAVCGKR---------------DENSKEEKE 187

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568922675  260 DGGDRLTDGNTDSLPGILTVEEKKKIGHLCKLLIDQGRLQYLQQKGFSPALQYYTDPLVSLENVLLTAV 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 7.43e-115

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: 333.11  E-value: 7.43e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922675   24 KQQASILGNIEKLKLLGPRRCFVEFGAGKGKLSHWVDIAL--KDAENVHFILVERVTTRFKVDGKHRKKDS--VFERLQI 99
Cdd:pfam05206   1 IQQSSLIGNLEELGLLNPDSAYVEFGAGRGELSRYVNQCIqeDKLGNSGYVLIDRASNRMKFDRKIRKDESepIIKRLRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922675  100 DIQHLCLNRVPVLREGRlPVVGIGKHLCGVATDVALRCLVETYAASfeekdeeplakrikndktekesntlakegsekdv 179
Cdd:pfam05206  81 DIKDLNLDAVLSLEDGS-PVVAVSKHLCGAATDLTLRCLLNSLNNS---------------------------------- 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922675  180 petWTPVAGIVIALCCHHRCDWRHYVGKEYFKALGLGAVEFYYFQRMSSWATCGMRtslegsdvtperkdaQRDENEEHD 259
Cdd:pfam05206 126 ---TDKFRGLLIAMCCHHVCNWRTYVNREFLLELGITYDEFQILTKMVSWAVCGKR---------------DENSKEEKE 187

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568922675  260 DGGDRLTDGNTDSLPGILTVEEKKKIGHLCKLLIDQGRLQYLQQKGFSPALQYYTDPLVSLENVLLTAV 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 7.43e-115

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: 333.11  E-value: 7.43e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922675   24 KQQASILGNIEKLKLLGPRRCFVEFGAGKGKLSHWVDIAL--KDAENVHFILVERVTTRFKVDGKHRKKDS--VFERLQI 99
Cdd:pfam05206   1 IQQSSLIGNLEELGLLNPDSAYVEFGAGRGELSRYVNQCIqeDKLGNSGYVLIDRASNRMKFDRKIRKDESepIIKRLRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922675  100 DIQHLCLNRVPVLREGRlPVVGIGKHLCGVATDVALRCLVETYAASfeekdeeplakrikndktekesntlakegsekdv 179
Cdd:pfam05206  81 DIKDLNLDAVLSLEDGS-PVVAVSKHLCGAATDLTLRCLLNSLNNS---------------------------------- 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922675  180 petWTPVAGIVIALCCHHRCDWRHYVGKEYFKALGLGAVEFYYFQRMSSWATCGMRtslegsdvtperkdaQRDENEEHD 259
Cdd:pfam05206 126 ---TDKFRGLLIAMCCHHVCNWRTYVNREFLLELGITYDEFQILTKMVSWAVCGKR---------------DENSKEEKE 187

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568922675  260 DGGDRLTDGNTDSLPGILTVEEKKKIGHLCKLLIDQGRLQYLQQKGFSPALQYYTDPLVSLENVLLTAV 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH