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Conserved domains on  [gi|568927360|ref|XP_006538308|]
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tRNA methyltransferase 10 homolog B isoform X2 [Mus musculus]

Protein Classification

RNA methyltransferase; RsmE family 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; RsmE family RNA methyltransferase similar to 16S rRNA (uracil(1498)-N(3))-methyltransferase RsmE that specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA

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 ...
 63-245 5.14e-115

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: 327.30  E-value: 5.14e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927360  63 PRLCVDLSMTQHMSKKELSRLAGQIRRLYGSNKKASRPFWICLTGFSTASPLYEECLRMNDGFSAYLLDVTEEDCFSLFP 142
Cdd:cd18100    1 LRVCIDLSLEHKMSEKEISKLAQQLRRLYGSNRKAEKPLHIYLTSFDKEGLLYKECVRKNDGFENYLIDMTEESHSELFP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927360 143 LETLVYLTPDSEHSLEDIDQSTVYVIGGLVDESIQKKVTFQKAREYSVKTARLPIQEYMiKRQNEKNYHSEILAINQVFD 222
Cdd:cd18100   81 KEEIVYLSPDSENVLESIDPNKVYVIGGLVDESIQKKLTLQKAKEHGIQTARLPIDEYM-VKADGKGNYSTVLAINQVFD 159

                        170       180
                 ....*....|....*....|...
gi 568927360 223 ILSTYFETRNWPEALKKGVSPGK 245
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 ...
 63-245 5.14e-115

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: 327.30  E-value: 5.14e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927360  63 PRLCVDLSMTQHMSKKELSRLAGQIRRLYGSNKKASRPFWICLTGFSTASPLYEECLRMNDGFSAYLLDVTEEDCFSLFP 142
Cdd:cd18100    1 LRVCIDLSLEHKMSEKEISKLAQQLRRLYGSNRKAEKPLHIYLTSFDKEGLLYKECVRKNDGFENYLIDMTEESHSELFP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927360 143 LETLVYLTPDSEHSLEDIDQSTVYVIGGLVDESIQKKVTFQKAREYSVKTARLPIQEYMiKRQNEKNYHSEILAINQVFD 222
Cdd:cd18100   81 KEEIVYLSPDSENVLESIDPNKVYVIGGLVDESIQKKLTLQKAKEHGIQTARLPIDEYM-VKADGKGNYSTVLAINQVFD 159

                        170       180
                 ....*....|....*....|...
gi 568927360 223 ILSTYFETRNWPEALKKGVSPGK 245
Cdd:cd18100  160 ILLKYYETGDWREALSAGVPQRK 182
tRNA_m1G_MT pfam01746
tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC: ...
 73-245 4.33e-58

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: 182.93  E-value: 4.33e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927360   73 QHMSKKELSRLAGQIRRLYGSNKKASRPFWICLTGFSTASPLYEECLRMND----GFSAYLLDVT-----EEDCFSLFPL 143
Cdd:pfam01746   1 GLAQEKGLVSLVVQNLRDYTANRRNTVDDEPYGGGFGMVLKPEPEFEALESvnyeKWKVILLTPTgkpffQEGAVDLSQK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927360  144 ETLVYLTPDSEHSLEDIDQSTVYVIGGLVDESIQKKV----TFQKAREYSVKTARLPIQEYMIKRQNeknyHSEILAINQ 219
Cdd:pfam01746  81 EHLVYLCGDYEGVDERVDDDKEYSIGDFVDKGGEKGAlvliDLVKRLLPGVLTASLPIDSFLLEKPH----YTRPLTLNQ 156

                         170       180
                  ....*....|....*....|....*.
gi 568927360  220 VFDILSTYFETRNWPEALKKGVSPGK 245
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 ...
 63-245 5.14e-115

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: 327.30  E-value: 5.14e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927360  63 PRLCVDLSMTQHMSKKELSRLAGQIRRLYGSNKKASRPFWICLTGFSTASPLYEECLRMNDGFSAYLLDVTEEDCFSLFP 142
Cdd:cd18100    1 LRVCIDLSLEHKMSEKEISKLAQQLRRLYGSNRKAEKPLHIYLTSFDKEGLLYKECVRKNDGFENYLIDMTEESHSELFP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927360 143 LETLVYLTPDSEHSLEDIDQSTVYVIGGLVDESIQKKVTFQKAREYSVKTARLPIQEYMiKRQNEKNYHSEILAINQVFD 222
Cdd:cd18100   81 KEEIVYLSPDSENVLESIDPNKVYVIGGLVDESIQKKLTLQKAKEHGIQTARLPIDEYM-VKADGKGNYSTVLAINQVFD 159

                        170       180
                 ....*....|....*....|...
gi 568927360 223 ILSTYFETRNWPEALKKGVSPGK 245
Cdd:cd18100  160 ILLKYYETGDWREALSAGVPQRK 182
tRNA_m1G_MT pfam01746
tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC: ...
 73-245 4.33e-58

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: 182.93  E-value: 4.33e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927360   73 QHMSKKELSRLAGQIRRLYGSNKKASRPFWICLTGFSTASPLYEECLRMND----GFSAYLLDVT-----EEDCFSLFPL 143
Cdd:pfam01746   1 GLAQEKGLVSLVVQNLRDYTANRRNTVDDEPYGGGFGMVLKPEPEFEALESvnyeKWKVILLTPTgkpffQEGAVDLSQK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927360  144 ETLVYLTPDSEHSLEDIDQSTVYVIGGLVDESIQKKV----TFQKAREYSVKTARLPIQEYMIKRQNeknyHSEILAINQ 219
Cdd:pfam01746  81 EHLVYLCGDYEGVDERVDDDKEYSIGDFVDKGGEKGAlvliDLVKRLLPGVLTASLPIDSFLLEKPH----YTRPLTLNQ 156

                         170       180
                  ....*....|....*....|....*.
gi 568927360  220 VFDILSTYFETRNWPEALKKGVSPGK 245
Cdd:pfam01746 157 VPEILLSGNHIRNWKEALLRTIPRRK 182
SPOUT_Trm10-like cd18089
tRNA methyltransferase Trm10-like; Family of tRNA methyltransferase Trm10-like proteins ...
 63-239 7.44e-56

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: 176.57  E-value: 7.44e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927360  63 PRLCVDLSMTQHMSKKELSRLAGQIRRLYGSNKKASRPFWICLTGFSTASPLYEECLRMNDGFSAYLLDVTEEDCFsLFP 142
Cdd:cd18089    1 PRIVIDLSFDDLMTEKEIRSLAKQLSRCYGANRRSEKPLRLHLTSFSGDLKQRLLKKSGAENWKIITHEESLLEEE-AFP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927360 143 LETLVYLTPDSEHSLEDIDQSTVYVIGGLVDESIQKKVTFQKAREYSVKTARLPIQEYMikrqneKNYHSEILAINQVFD 222
Cdd:cd18089   80 KEKLVYLTADAEEVLEELDPDKVYIIGGIVDRNRHKGLTLNKAEELGIRTARLPIREYI------KLKGRKVLTVNHVFE 153

                        170
                 ....*....|....*..
gi 568927360 223 ILSTYFETRNWPEALKK 239
Cdd:cd18089  154 ILLRYLEGGDWKEALEE 170
Trm10_MRRP1 cd18102
Mitochondrial ribonuclease P protein 1; Mitochondrial ribonuclease P protein 1 (or tRNA ...
 63-242 1.21e-42

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: 143.06  E-value: 1.21e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927360  63 PRLCVDLSMTQHMSKKELSRLAGQIRRLYGSNKKASRPFWICLTGFSTASPLYE------ECLRMNDGFsaylLDVTEED 136
Cdd:cd18102    1 QPLVIDMSYEDLMSPREIKNTARQLLEAYSANRRSTEPFHLHFCNLDPDGESIKrllrliPKLSLDKFP----ITVTEKS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927360 137 CFSLFPLETLVYLTPDSEHSLEDIDQSTVYVIGGLVDESIQKKVTFQKAREYSVKTARLPIQEYMIKRQNEKNyhseiLA 216
Cdd:cd18102   77 YLDLFPKEKLVYLSPDAPEVLKEFDPDKVYIIGGLVDKSTKKPLSLAKAKKEGIRMARLPLDRYLKWGGGSKS-----LT 151

                        170       180
                 ....*....|....*....|....*.
gi 568927360 217 INQVFDILSTYFETRNWPEALKKGVS 242
Cdd:cd18102  152 LNQVVSILLDLKDTGDWKEALKHVPP 177
Trm10euk_A cd18101
eukaryotic tRNA m1G9 methyltransferase Trm10 homolog A; Eukaryotic tRNA m1G9 methyltransferase ...
 64-239 2.42e-42

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: 142.36  E-value: 2.42e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927360  64 RLCVDLSMTQHMSKKELSRLAGQIRRLYGSNKKASRPFWICLTGFSTASplyEECLRMNDGFSAYLLDVTEEDCFSLFPL 143
Cdd:cd18101    2 RVAIDCSFDDLMTEKDIKKLVKQIQRCYAENRRADNPVQLYLTSLGGKT---KENMEKDKGYENWDVNFKEEHYLEVFKK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927360 144 ETLVYLTPDSEHSLEDIDQSTVYVIGGLVDESIQKKVTFQKAREYSVKTARLPIQEYMikrqneKNYHSEILAINQVFDI 223
Cdd:cd18101   79 EDIVYLTSDSPNVLEDLDEDKVYIIGGLVDHNHHKGLCYKRAVELGIQHARLPIDEYV------KMKTRKVLTINHVFEI 152

                        170
                 ....*....|....*.
gi 568927360 224 LSTYFETRNWPEALKK 239
Cdd:cd18101  153 LLRYTEGKDWKEAFFK 168
 
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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