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Conserved domains on  [gi|558611354|ref|NP_001273879|]
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tRNA methyltransferase 10 homolog B isoform b [Homo sapiens]

Protein Classification

RNA methyltransferase( domain architecture ID 1000317)

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
SPOUT_MTase super family cl38912
SPOUT superfamily of SAM-dependent RNA methyltransferases; The SPOUT (SpoU-TrmD) ...
 125-247 5.42e-61

SPOUT superfamily of SAM-dependent RNA methyltransferases; The SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, also known as class IV methyltransferase family, is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot. Members of the SPOUT superfamily that have been characterized functionally are involved in post-transcriptional RNA modification by catalyzing methylation of the 2-OH group of ribose, the N-1 atom of guanosine 37 in tRNA, or the N-3 atom of uridine 1498 in 16S rRNA.


The actual alignment was detected with superfamily member cd18100:

Pssm-ID: 476814  Cd Length: 182  Bit Score: 190.17  E-value: 5.42e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611354 125 PRLCIDLSMTHYMSKK---------------------------------------------------LDITEEDCFSLFP 153
Cdd:cd18100    1 LRVCIDLSLEHKMSEKeisklaqqlrrlygsnrkaekplhiyltsfdkegllykecvrkndgfenylIDMTEESHSELFP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611354 154 LETLVYLTPDSEHALEDVDLNKVYILGGLVDESIQKKVTFQKAREYSVKTARLPIQEYMVRNQnGKNYHSEILAINQ--- 230
Cdd:cd18100   81 KEEIVYLSPDSENVLESIDPNKVYVIGGLVDESIQKKLTLQKAKEHGIQTARLPIDEYMVKAD-GKGNYSTVLAINQvfd 159

                        170       180
                 ....*....|....*....|...
gi 558611354 231 ------ETHNWPEALKKGVSSGK 247
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 ...
 125-247 5.42e-61

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: 190.17  E-value: 5.42e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611354 125 PRLCIDLSMTHYMSKK---------------------------------------------------LDITEEDCFSLFP 153
Cdd:cd18100    1 LRVCIDLSLEHKMSEKeisklaqqlrrlygsnrkaekplhiyltsfdkegllykecvrkndgfenylIDMTEESHSELFP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611354 154 LETLVYLTPDSEHALEDVDLNKVYILGGLVDESIQKKVTFQKAREYSVKTARLPIQEYMVRNQnGKNYHSEILAINQ--- 230
Cdd:cd18100   81 KEEIVYLSPDSENVLESIDPNKVYVIGGLVDESIQKKLTLQKAKEHGIQTARLPIDEYMVKAD-GKGNYSTVLAINQvfd 159

                        170       180
                 ....*....|....*....|...
gi 558611354 231 ------ETHNWPEALKKGVSSGK 247
Cdd:cd18100  160 illkyyETGDWREALSAGVPQRK 182
tRNA_m1G_MT pfam01746
tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC: ...
 144-247 5.33e-25

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: 97.42  E-value: 5.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611354  144 TEEDCFSLFPLETLVYLTPDSEHALEDVDLNKVYILGGLVDESIQKKV----TFQKAREYSVKTARLPIQEYMvrnqNGK 219
Cdd:pfam01746  70 FQEGAVDLSQKEHLVYLCGDYEGVDERVDDDKEYSIGDFVDKGGEKGAlvliDLVKRLLPGVLTASLPIDSFL----LEK 145

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 558611354  220 NYHSEILAINQ---------ETHNWPEALKKGVSSGK 247
Cdd:pfam01746 146 PHYTRPLTLNQvpeillsgnHIRNWKEALLRTIPRRK 182
 
Name Accession Description Interval E-value
Trm10euk_B cd18100
eukaryotic tRNA m1G9 methyltransferase Trm10 homolog B; Eukaryotic tRNA m1G9 methyltransferase ...
 125-247 5.42e-61

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: 190.17  E-value: 5.42e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611354 125 PRLCIDLSMTHYMSKK---------------------------------------------------LDITEEDCFSLFP 153
Cdd:cd18100    1 LRVCIDLSLEHKMSEKeisklaqqlrrlygsnrkaekplhiyltsfdkegllykecvrkndgfenylIDMTEESHSELFP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611354 154 LETLVYLTPDSEHALEDVDLNKVYILGGLVDESIQKKVTFQKAREYSVKTARLPIQEYMVRNQnGKNYHSEILAINQ--- 230
Cdd:cd18100   81 KEEIVYLSPDSENVLESIDPNKVYVIGGLVDESIQKKLTLQKAKEHGIQTARLPIDEYMVKAD-GKGNYSTVLAINQvfd 159

                        170       180
                 ....*....|....*....|...
gi 558611354 231 ------ETHNWPEALKKGVSSGK 247
Cdd:cd18100  160 illkyyETGDWREALSAGVPQRK 182
Trm10_MRRP1 cd18102
Mitochondrial ribonuclease P protein 1; Mitochondrial ribonuclease P protein 1 (or tRNA ...
 126-244 2.77e-29

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: 108.78  E-value: 2.77e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611354 126 RLCIDLSMTHYMskkLDITEEDCFSLFPLETLVYLTPDSEHALEDVDLNKVYILGGLVDESIQKKVTFQKAREYSVKTAR 205
Cdd:cd18102   58 RLIPKLSLDKFP---ITVTEKSYLDLFPKEKLVYLSPDAPEVLKEFDPDKVYIIGGLVDKSTKKPLSLAKAKKEGIRMAR 134

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 558611354 206 LPIQEYMVRNQNGKNyhseiLAINQ---------ETHNWPEALKKGVS 244
Cdd:cd18102  135 LPLDRYLKWGGGSKS-----LTLNQvvsilldlkDTGDWKEALKHVPP 177
SPOUT_Trm10-like cd18089
tRNA methyltransferase Trm10-like; Family of tRNA methyltransferase Trm10-like proteins ...
 140-241 4.06e-29

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: 108.01  E-value: 4.06e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611354 140 KLDITEEDCFS--LFPLETLVYLTPDSEHALEDVDLNKVYILGGLVDESIQKKVTFQKAREYSVKTARLPIQEYMVRNqn 217
Cdd:cd18089   64 KIITHEESLLEeeAFPKEKLVYLTADAEEVLEELDPDKVYIIGGIVDRNRHKGLTLNKAEELGIRTARLPIREYIKLK-- 141

                         90       100       110
                 ....*....|....*....|....*....|...
gi 558611354 218 gknyHSEILAINQ---------ETHNWPEALKK 241
Cdd:cd18089  142 ----GRKVLTVNHvfeillrylEGGDWKEALEE 170
Trm10euk_A cd18101
eukaryotic tRNA m1G9 methyltransferase Trm10 homolog A; Eukaryotic tRNA m1G9 methyltransferase ...
 122-241 4.87e-25

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: 97.29  E-value: 4.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611354 122 HSGPRLCIDLSMTHYMSKKLDITEEDCFSLFPLETLVYLTPDSEHALEDVDLNKVYILGGLVDESIQKKVTFQKAREYSV 201
Cdd:cd18101   46 LGGKTKENMEKDKGYENWDVNFKEEHYLEVFKKEDIVYLTSDSPNVLEDLDEDKVYIIGGLVDHNHHKGLCYKRAVELGI 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 558611354 202 KTARLPIQEYMVRNQngknyhSEILAINQ---------ETHNWPEALKK 241
Cdd:cd18101  126 QHARLPIDEYVKMKT------RKVLTINHvfeillrytEGKDWKEAFFK 168
tRNA_m1G_MT pfam01746
tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC: ...
 144-247 5.33e-25

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: 97.42  E-value: 5.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611354  144 TEEDCFSLFPLETLVYLTPDSEHALEDVDLNKVYILGGLVDESIQKKV----TFQKAREYSVKTARLPIQEYMvrnqNGK 219
Cdd:pfam01746  70 FQEGAVDLSQKEHLVYLCGDYEGVDERVDDDKEYSIGDFVDKGGEKGAlvliDLVKRLLPGVLTASLPIDSFL----LEK 145

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 558611354  220 NYHSEILAINQ---------ETHNWPEALKKGVSSGK 247
Cdd:pfam01746 146 PHYTRPLTLNQvpeillsgnHIRNWKEALLRTIPRRK 182
 
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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