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Conserved domains on  [gi|558611326|ref|NP_001273882|]
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tRNA methyltransferase 10 homolog B isoform e [Homo sapiens]

Protein Classification

Trm10euk_B domain-containing protein( domain architecture ID 13031075)

Trm10euk_B domain-containing protein

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 ...
33-187 4.61e-97

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: 279.15  E-value: 4.61e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611326  33 RLAGQIRRLYGSNKKADRPFWICLTGFTTDSPLYEECVRMNDGFSSYLLDITEEDCFSLFPLETLVYLTPDSEHALEDVD 112
Cdd:cd18100   20 KLAQQLRRLYGSNRKAEKPLHIYLTSFDKEGLLYKECVRKNDGFENYLIDMTEESHSELFPKEEIVYLSPDSENVLESID 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611326 113 LNKVYILGGLVDESIQKKVTFQKAREYSVKTARLPIQEYMVRNQnGKNYHSEILAINQ---------ETHNWPEALKKGV 183
Cdd:cd18100  100 PNKVYVIGGLVDESIQKKLTLQKAKEHGIQTARLPIDEYMVKAD-GKGNYSTVLAINQvfdillkyyETGDWREALSAGV 178

                 ....
gi 558611326 184 SSGK 187
Cdd:cd18100  179 PQRK 182
 
Name Accession Description Interval E-value
Trm10euk_B cd18100
eukaryotic tRNA m1G9 methyltransferase Trm10 homolog B; Eukaryotic tRNA m1G9 methyltransferase ...
33-187 4.61e-97

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: 279.15  E-value: 4.61e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611326  33 RLAGQIRRLYGSNKKADRPFWICLTGFTTDSPLYEECVRMNDGFSSYLLDITEEDCFSLFPLETLVYLTPDSEHALEDVD 112
Cdd:cd18100   20 KLAQQLRRLYGSNRKAEKPLHIYLTSFDKEGLLYKECVRKNDGFENYLIDMTEESHSELFPKEEIVYLSPDSENVLESID 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611326 113 LNKVYILGGLVDESIQKKVTFQKAREYSVKTARLPIQEYMVRNQnGKNYHSEILAINQ---------ETHNWPEALKKGV 183
Cdd:cd18100  100 PNKVYVIGGLVDESIQKKLTLQKAKEHGIQTARLPIDEYMVKAD-GKGNYSTVLAINQvfdillkyyETGDWREALSAGV 178

                 ....
gi 558611326 184 SSGK 187
Cdd:cd18100  179 PQRK 182
tRNA_m1G_MT pfam01746
tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC: ...
33-187 2.19e-40

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: 135.55  E-value: 2.19e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611326   33 RLAGQIRRLYGSNKKADRPFWICLTGFTTDSPLYEECVRMND----GFSSYLLD-----ITEEDCFSLFPLETLVYLTPD 103
Cdd:pfam01746  10 SLVVQNLRDYTANRRNTVDDEPYGGGFGMVLKPEPEFEALESvnyeKWKVILLTptgkpFFQEGAVDLSQKEHLVYLCGD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611326  104 SEHALEDVDLNKVYILGGLVDESIQKKV----TFQKAREYSVKTARLPIQEYMvrnqNGKNYHSEILAINQ--------- 170
Cdd:pfam01746  90 YEGVDERVDDDKEYSIGDFVDKGGEKGAlvliDLVKRLLPGVLTASLPIDSFL----LEKPHYTRPLTLNQvpeillsgn 165
                         170
                  ....*....|....*..
gi 558611326  171 ETHNWPEALKKGVSSGK 187
Cdd:pfam01746 166 HIRNWKEALLRTIPRRK 182
 
Name Accession Description Interval E-value
Trm10euk_B cd18100
eukaryotic tRNA m1G9 methyltransferase Trm10 homolog B; Eukaryotic tRNA m1G9 methyltransferase ...
33-187 4.61e-97

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: 279.15  E-value: 4.61e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611326  33 RLAGQIRRLYGSNKKADRPFWICLTGFTTDSPLYEECVRMNDGFSSYLLDITEEDCFSLFPLETLVYLTPDSEHALEDVD 112
Cdd:cd18100   20 KLAQQLRRLYGSNRKAEKPLHIYLTSFDKEGLLYKECVRKNDGFENYLIDMTEESHSELFPKEEIVYLSPDSENVLESID 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611326 113 LNKVYILGGLVDESIQKKVTFQKAREYSVKTARLPIQEYMVRNQnGKNYHSEILAINQ---------ETHNWPEALKKGV 183
Cdd:cd18100  100 PNKVYVIGGLVDESIQKKLTLQKAKEHGIQTARLPIDEYMVKAD-GKGNYSTVLAINQvfdillkyyETGDWREALSAGV 178

                 ....
gi 558611326 184 SSGK 187
Cdd:cd18100  179 PQRK 182
SPOUT_Trm10-like cd18089
tRNA methyltransferase Trm10-like; Family of tRNA methyltransferase Trm10-like proteins ...
34-181 2.19e-40

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: 134.97  E-value: 2.19e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611326  34 LAGQIRRLYGSNKKADRPFWICLTGFTTDSPLYEECVRMNDGFSSYLLDITEEDCFsLFPLETLVYLTPDSEHALEDVDL 113
Cdd:cd18089   21 LAKQLSRCYGANRRSEKPLRLHLTSFSGDLKQRLLKKSGAENWKIITHEESLLEEE-AFPKEKLVYLTADAEEVLEELDP 99
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 558611326 114 NKVYILGGLVDESIQKKVTFQKAREYSVKTARLPIQEYMVRNqngknyHSEILAINQ---------ETHNWPEALKK 181
Cdd:cd18089  100 DKVYIIGGIVDRNRHKGLTLNKAEELGIRTARLPIREYIKLK------GRKVLTVNHvfeillrylEGGDWKEALEE 170
tRNA_m1G_MT pfam01746
tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC: ...
33-187 2.19e-40

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: 135.55  E-value: 2.19e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611326   33 RLAGQIRRLYGSNKKADRPFWICLTGFTTDSPLYEECVRMND----GFSSYLLD-----ITEEDCFSLFPLETLVYLTPD 103
Cdd:pfam01746  10 SLVVQNLRDYTANRRNTVDDEPYGGGFGMVLKPEPEFEALESvnyeKWKVILLTptgkpFFQEGAVDLSQKEHLVYLCGD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611326  104 SEHALEDVDLNKVYILGGLVDESIQKKV----TFQKAREYSVKTARLPIQEYMvrnqNGKNYHSEILAINQ--------- 170
Cdd:pfam01746  90 YEGVDERVDDDKEYSIGDFVDKGGEKGAlvliDLVKRLLPGVLTASLPIDSFL----LEKPHYTRPLTLNQvpeillsgn 165
                         170
                  ....*....|....*..
gi 558611326  171 ETHNWPEALKKGVSSGK 187
Cdd:pfam01746 166 HIRNWKEALLRTIPRRK 182
Trm10_MRRP1 cd18102
Mitochondrial ribonuclease P protein 1; Mitochondrial ribonuclease P protein 1 (or tRNA ...
33-184 1.88e-35

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: 122.65  E-value: 1.88e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611326  33 RLAGQIRRLYGSNKKADRPFWICLTGFTTDSPLYEECVRMNDG--FSSYLLDITEEDCFSLFPLETLVYLTPDSEHALED 110
Cdd:cd18102   20 NTARQLLEAYSANRRSTEPFHLHFCNLDPDGESIKRLLRLIPKlsLDKFPITVTEKSYLDLFPKEKLVYLSPDAPEVLKE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611326 111 VDLNKVYILGGLVDESIQKKVTFQKAREYSVKTARLPIQEYMVRNQNGKNyhseiLAINQ---------ETHNWPEALKK 181
Cdd:cd18102  100 FDPDKVYIIGGLVDKSTKKPLSLAKAKKEGIRMARLPLDRYLKWGGGSKS-----LTLNQvvsilldlkDTGDWKEALKH 174

                 ...
gi 558611326 182 GVS 184
Cdd:cd18102  175 VPP 177
Trm10euk_A cd18101
eukaryotic tRNA m1G9 methyltransferase Trm10 homolog A; Eukaryotic tRNA m1G9 methyltransferase ...
37-181 6.33e-31

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: 110.77  E-value: 6.33e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611326  37 QIRRLYGSNKKADRPFWICLTGFTTDSPLYEECvrmNDGFSSYLLDITEEDCFSLFPLETLVYLTPDSEHALEDVDLNKV 116
Cdd:cd18101   24 QIQRCYAENRRADNPVQLYLTSLGGKTKENMEK---DKGYENWDVNFKEEHYLEVFKKEDIVYLTSDSPNVLEDLDEDKV 100
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 558611326 117 YILGGLVDESIQKKVTFQKAREYSVKTARLPIQEYMVRNQngknyhSEILAINQ---------ETHNWPEALKK 181
Cdd:cd18101  101 YIIGGLVDHNHHKGLCYKRAVELGIQHARLPIDEYVKMKT------RKVLTINHvfeillrytEGKDWKEAFFK 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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