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Conserved domains on  [gi|564350754|ref|XP_006238104|]
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tRNA methyltransferase 10 homolog B isoform X1 [Rattus norvegicus]

Protein Classification

RNA methyltransferase( domain architecture ID 13031075)

SpoU family RNA methyltransferase catalyzes the methylation of rRNA or tRNA at specific sites in a S-adenosyl-L-methionine (SAM)-dependent manner

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Trm10euk_B cd18100
eukaryotic tRNA m1G9 methyltransferase Trm10 homolog B; Eukaryotic tRNA m1G9 methyltransferase ...
 125-307 5.37e-116

eukaryotic tRNA m1G9 methyltransferase Trm10 homolog B; Eukaryotic tRNA m1G9 methyltransferase Trm10 homolog B (TM10B) catalyzes the N(1) methylation of guanine at Position 9 (m(1)G9) of tRNA, which might play a role in the stabilization of tRNA and in translation termination efficiency. Trm10 is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.


:

Pssm-ID: 349973  Cd Length: 182  Bit Score: 332.30  E-value: 5.37e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350754 125 PRLCVDLSMTQHMSKKELSRLAGQIRRLYGSNKKASRPFWIYLTGFSTDSPLYEECLRMNDGFSAYVLDVTEEDCFSLFP 204
Cdd:cd18100    1 LRVCIDLSLEHKMSEKEISKLAQQLRRLYGSNRKAEKPLHIYLTSFDKEGLLYKECVRKNDGFENYLIDMTEESHSELFP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350754 205 LETLVYLTPDSEHPLEDIDLSTVYIIGGLVDESIQKKVTFQKAQEYSVKTARLPIQEHMIRCQnEKNFHSEILAINQVFD 284
Cdd:cd18100   81 KEEIVYLSPDSENVLESIDPNKVYVIGGLVDESIQKKLTLQKAKEHGIQTARLPIDEYMVKAD-GKGNYSTVLAINQVFD 159

                        170       180
                 ....*....|....*....|...
gi 564350754 285 ILSAYLETRDWPEALKKGVSPGK 307
Cdd:cd18100  160 ILLKYYETGDWREALSAGVPQRK 182
 
Name Accession Description Interval E-value
Trm10euk_B cd18100
eukaryotic tRNA m1G9 methyltransferase Trm10 homolog B; Eukaryotic tRNA m1G9 methyltransferase ...
 125-307 5.37e-116

eukaryotic tRNA m1G9 methyltransferase Trm10 homolog B; Eukaryotic tRNA m1G9 methyltransferase Trm10 homolog B (TM10B) catalyzes the N(1) methylation of guanine at Position 9 (m(1)G9) of tRNA, which might play a role in the stabilization of tRNA and in translation termination efficiency. Trm10 is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.


Pssm-ID: 349973  Cd Length: 182  Bit Score: 332.30  E-value: 5.37e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350754 125 PRLCVDLSMTQHMSKKELSRLAGQIRRLYGSNKKASRPFWIYLTGFSTDSPLYEECLRMNDGFSAYVLDVTEEDCFSLFP 204
Cdd:cd18100    1 LRVCIDLSLEHKMSEKEISKLAQQLRRLYGSNRKAEKPLHIYLTSFDKEGLLYKECVRKNDGFENYLIDMTEESHSELFP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350754 205 LETLVYLTPDSEHPLEDIDLSTVYIIGGLVDESIQKKVTFQKAQEYSVKTARLPIQEHMIRCQnEKNFHSEILAINQVFD 284
Cdd:cd18100   81 KEEIVYLSPDSENVLESIDPNKVYVIGGLVDESIQKKLTLQKAKEHGIQTARLPIDEYMVKAD-GKGNYSTVLAINQVFD 159

                        170       180
                 ....*....|....*....|...
gi 564350754 285 ILSAYLETRDWPEALKKGVSPGK 307
Cdd:cd18100  160 ILLKYYETGDWREALSAGVPQRK 182
tRNA_m1G_MT pfam01746
tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC: ...
 135-307 8.26e-54

tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC:2.1.1.31. In E.coli K12 this enzyme catalyzes the conversion of a guanosine residue to N1-methylguanine in position 37, next to the anticodon, in tRNA.


Pssm-ID: 396350  Cd Length: 182  Bit Score: 174.07  E-value: 8.26e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350754  135 QHMSKKELSRLAGQIRRLYGSNKKASRPFWIYLTGFSTDSPLYEECLRMND----GFSAYVLDVT-----EEDCFSLFPL 205
Cdd:pfam01746   1 GLAQEKGLVSLVVQNLRDYTANRRNTVDDEPYGGGFGMVLKPEPEFEALESvnyeKWKVILLTPTgkpffQEGAVDLSQK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350754  206 ETLVYLTPDSEHPLEDIDLSTVYIIGGLVDESIQKKV----TFQKAQEYSVKTARLPIQEHMIRCQNeknfHSEILAINQ 281
Cdd:pfam01746  81 EHLVYLCGDYEGVDERVDDDKEYSIGDFVDKGGEKGAlvliDLVKRLLPGVLTASLPIDSFLLEKPH----YTRPLTLNQ 156

                         170       180
                  ....*....|....*....|....*.
gi 564350754  282 VFDILSAYLETRDWPEALKKGVSPGK 307
Cdd:pfam01746 157 VPEILLSGNHIRNWKEALLRTIPRRK 182
 
Name Accession Description Interval E-value
Trm10euk_B cd18100
eukaryotic tRNA m1G9 methyltransferase Trm10 homolog B; Eukaryotic tRNA m1G9 methyltransferase ...
 125-307 5.37e-116

eukaryotic tRNA m1G9 methyltransferase Trm10 homolog B; Eukaryotic tRNA m1G9 methyltransferase Trm10 homolog B (TM10B) catalyzes the N(1) methylation of guanine at Position 9 (m(1)G9) of tRNA, which might play a role in the stabilization of tRNA and in translation termination efficiency. Trm10 is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.


Pssm-ID: 349973  Cd Length: 182  Bit Score: 332.30  E-value: 5.37e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350754 125 PRLCVDLSMTQHMSKKELSRLAGQIRRLYGSNKKASRPFWIYLTGFSTDSPLYEECLRMNDGFSAYVLDVTEEDCFSLFP 204
Cdd:cd18100    1 LRVCIDLSLEHKMSEKEISKLAQQLRRLYGSNRKAEKPLHIYLTSFDKEGLLYKECVRKNDGFENYLIDMTEESHSELFP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350754 205 LETLVYLTPDSEHPLEDIDLSTVYIIGGLVDESIQKKVTFQKAQEYSVKTARLPIQEHMIRCQnEKNFHSEILAINQVFD 284
Cdd:cd18100   81 KEEIVYLSPDSENVLESIDPNKVYVIGGLVDESIQKKLTLQKAKEHGIQTARLPIDEYMVKAD-GKGNYSTVLAINQVFD 159

                        170       180
                 ....*....|....*....|...
gi 564350754 285 ILSAYLETRDWPEALKKGVSPGK 307
Cdd:cd18100  160 ILLKYYETGDWREALSAGVPQRK 182
SPOUT_Trm10-like cd18089
tRNA methyltransferase Trm10-like; Family of tRNA methyltransferase Trm10-like proteins ...
 125-301 1.42e-58

tRNA methyltransferase Trm10-like; Family of tRNA methyltransferase Trm10-like proteins catalyzes the N(1) methylation of guanine at position 9 (m(1)G9) of tRNA (eukaryotes) or N(1) methylation of guanine or adenine at position 9 (m1G9/m1A9) of tRNA (archaea), which might play a role in the stabilization of tRNA and in translation termination efficiency. Trm10 is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.


Pssm-ID: 349962  Cd Length: 171  Bit Score: 185.82  E-value: 1.42e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350754 125 PRLCVDLSMTQHMSKKELSRLAGQIRRLYGSNKKASRPFWIYLTGFSTDSPLYEECLRMNDGFSAYVLDVTEEDCFsLFP 204
Cdd:cd18089    1 PRIVIDLSFDDLMTEKEIRSLAKQLSRCYGANRRSEKPLRLHLTSFSGDLKQRLLKKSGAENWKIITHEESLLEEE-AFP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350754 205 LETLVYLTPDSEHPLEDIDLSTVYIIGGLVDESIQKKVTFQKAQEYSVKTARLPIQEHMIRCqneknfHSEILAINQVFD 284
Cdd:cd18089   80 KEKLVYLTADAEEVLEELDPDKVYIIGGIVDRNRHKGLTLNKAEELGIRTARLPIREYIKLK------GRKVLTVNHVFE 153

                        170
                 ....*....|....*..
gi 564350754 285 ILSAYLETRDWPEALKK 301
Cdd:cd18089  154 ILLRYLEGGDWKEALEE 170
tRNA_m1G_MT pfam01746
tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC: ...
 135-307 8.26e-54

tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC:2.1.1.31. In E.coli K12 this enzyme catalyzes the conversion of a guanosine residue to N1-methylguanine in position 37, next to the anticodon, in tRNA.


Pssm-ID: 396350  Cd Length: 182  Bit Score: 174.07  E-value: 8.26e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350754  135 QHMSKKELSRLAGQIRRLYGSNKKASRPFWIYLTGFSTDSPLYEECLRMND----GFSAYVLDVT-----EEDCFSLFPL 205
Cdd:pfam01746   1 GLAQEKGLVSLVVQNLRDYTANRRNTVDDEPYGGGFGMVLKPEPEFEALESvnyeKWKVILLTPTgkpffQEGAVDLSQK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350754  206 ETLVYLTPDSEHPLEDIDLSTVYIIGGLVDESIQKKV----TFQKAQEYSVKTARLPIQEHMIRCQNeknfHSEILAINQ 281
Cdd:pfam01746  81 EHLVYLCGDYEGVDERVDDDKEYSIGDFVDKGGEKGAlvliDLVKRLLPGVLTASLPIDSFLLEKPH----YTRPLTLNQ 156

                         170       180
                  ....*....|....*....|....*.
gi 564350754  282 VFDILSAYLETRDWPEALKKGVSPGK 307
Cdd:pfam01746 157 VPEILLSGNHIRNWKEALLRTIPRRK 182
Trm10_MRRP1 cd18102
Mitochondrial ribonuclease P protein 1; Mitochondrial ribonuclease P protein 1 (or tRNA ...
 125-304 8.71e-45

Mitochondrial ribonuclease P protein 1; Mitochondrial ribonuclease P protein 1 (or tRNA methyltransferase 10 homolog C) functions in mitochondrial tRNA maturation and is part of mitochondrial ribonuclease P, an enzyme composed of MRPP1/RG9MTD1, MRPP2/HSD17B10 and MRPP3/KIAA0391, which cleaves tRNA molecules in their 5'-ends. MRRP1 is related to Trm10, a tRNA m1G9 methyltransferase and is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.


Pssm-ID: 349975  Cd Length: 179  Bit Score: 150.77  E-value: 8.71e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350754 125 PRLCVDLSMTQHMSKKELSRLAGQIRRLYGSNKKASRPFWIYLTGFSTDSPLYE------ECLRMNDGFsayvLDVTEED 198
Cdd:cd18102    1 QPLVIDMSYEDLMSPREIKNTARQLLEAYSANRRSTEPFHLHFCNLDPDGESIKrllrliPKLSLDKFP----ITVTEKS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350754 199 CFSLFPLETLVYLTPDSEHPLEDIDLSTVYIIGGLVDESIQKKVTFQKAQEYSVKTARLPIQEHMIRCQNEKNfhseiLA 278
Cdd:cd18102   77 YLDLFPKEKLVYLSPDAPEVLKEFDPDKVYIIGGLVDKSTKKPLSLAKAKKEGIRMARLPLDRYLKWGGGSKS-----LT 151

                        170       180
                 ....*....|....*....|....*.
gi 564350754 279 INQVFDILSAYLETRDWPEALKKGVS 304
Cdd:cd18102  152 LNQVVSILLDLKDTGDWKEALKHVPP 177
Trm10euk_A cd18101
eukaryotic tRNA m1G9 methyltransferase Trm10 homolog A; Eukaryotic tRNA m1G9 methyltransferase ...
 126-301 5.45e-44

eukaryotic tRNA m1G9 methyltransferase Trm10 homolog A; Eukaryotic tRNA m1G9 methyltransferase Trm10 homolog A (TM10A) catalyzes the N(1) methylation of guanine at Position 9 (m(1)G9) of tRNA, which might play a role in the stabilization of tRNA and in translation termination efficiency. Trm10 is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.


Pssm-ID: 349974  Cd Length: 174  Bit Score: 148.52  E-value: 5.45e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350754 126 RLCVDLSMTQHMSKKELSRLAGQIRRLYGSNKKASRPFWIYLTGFSTDSplyEECLRMNDGFSAYVLDVTEEDCFSLFPL 205
Cdd:cd18101    2 RVAIDCSFDDLMTEKDIKKLVKQIQRCYAENRRADNPVQLYLTSLGGKT---KENMEKDKGYENWDVNFKEEHYLEVFKK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350754 206 ETLVYLTPDSEHPLEDIDLSTVYIIGGLVDESIQKKVTFQKAQEYSVKTARLPIQEHMircqneKNFHSEILAINQVFDI 285
Cdd:cd18101   79 EDIVYLTSDSPNVLEDLDEDKVYIIGGLVDHNHHKGLCYKRAVELGIQHARLPIDEYV------KMKTRKVLTINHVFEI 152

                        170
                 ....*....|....*.
gi 564350754 286 LSAYLETRDWPEALKK 301
Cdd:cd18101  153 LLRYTEGKDWKEAFFK 168
Trm10arch cd18099
archaeal tRNA(m1G9/m1A9)-methyltransferase Trm10; Archaeal tRNA(m1G9/m1A9)-methyltransferase ...
 125-241 2.31e-03

archaeal tRNA(m1G9/m1A9)-methyltransferase Trm10; Archaeal tRNA(m1G9/m1A9)-methyltransferase Trm10 catalyzes the N(1) methylation of guanine or adenine at position 9 (m1G9/m1A9) of tRNA, which might play a role in the stabilization of tRNA and in translation termination efficiency. Trm10 is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.


Pssm-ID: 349972  Cd Length: 170  Bit Score: 38.15  E-value: 2.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350754 125 PRLCVDLSMTQHMSKKELSRLAGQIRRLYGSNKKAsrpFWIY-LTGFSTDSPLYEECLRMNDGFSAYVLDVTEEDcfslf 203
Cdd:cd18099    1 PYFIIDLSLWDLHTEKEKKKLVLQVLLSIGVIRKY---LWDGnLVLTWANSMFLEMLNKVESLSLYTVGLKEKGE----- 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 564350754 204 plETLVYLTPDSEHPL-EDIDLST-VYIIGGLVDESIQKK 241
Cdd:cd18099   73 --DNAVLLDPYAEEVAtEDIIRDTkAFIIGGIVDKGGNKK 110
 
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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