6KMR,2J6A,6H1D,6KMS,6PED,5CM2


Conserved Protein Domain Family
Trm112-like

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cd21089: Trm112-like 
eukaryotic tRNA methyltransferase 112, a partner protein of both rRNA/tRNA and protein methyltransferases, and similar proteins
This family contains eukaryotic tRNA methyltransferase 112 (Trm112)-like proteins such as human multifunctional methyltransferase subunit Trm112 protein, which acts as an activator of both rRNA/tRNA and protein methyltransferases. Trm112 acts as an obligate activating platform for at least four methyltransferases (MTase) involved in the modification of 18S rRNA (Bud23), tRNA (Trm9 and Trm11) and translation termination factor eRF1 (Mtq2) in eukaryotes. Hence, Trm112 is at a nexus between ribosome synthesis and function. Trm112 is a partner protein of N6amt1 (N6 -adenine-specific DNA methyltransferase 1), which is suggested to be the N6-adenine DNA methyltransferase (MTase) in human cells. Trm112 binds to a hydrophobic surface of N6amt1, stabilizing its structure but not directly contributing to substrate binding and catalysis. In Yarrowia lipolytica, it forms a complex with Trm9 methyltransferase, which is involved in the 5-methoxycarbonylmethyluridine (mcm(5)U) modification of the tRNA anticodon wobble position and hence promotes translational fidelity. In Saccharomyces cerevisiae, Trm112 (also called Ynr046w or tRNA methyltransferase 112) is a zinc binding protein that is plurifunctional and a component of the eRF1 methyltransferase, putatively containing a zinc finger signature motif.
Statistics
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PSSM-Id: 411041
Aligned: 51 rows
Threshold Bit Score: 135.752
Created: 23-Dec-2019
Updated: 25-Oct-2021
Structure
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Program:
Drawing:
Aligned Rows:
 
heterodimerZn binding site
Conserved site includes 19 residues -Click on image for an interactive view with Cn3D
Feature 1:heterodimer interface [polypeptide binding site]
Evidence:
  • Comment:N6 -adenine-specific DNA methyltransferase (N6amt1) forms a stable complex with a partner protein Trm112 and the complex functions as a glutamine-specific MTase for eRF1 in mammals
  • Structure:6KMR: Human multifunctional methyltransferase subunit TRM112-like interacts with methyltransferase N6amt1; contacts at 4.0A
    View structure with Cn3D
  • Structure:5CM2: Yarrowia lipolytica tRNA methyltransferase activator subunit interacts with tRNA methyltransferase; contacts at 4.0A
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1        #  # #### #                  #                                          #  #  # 
6KMR_A         3 KLLTHNLLSSHVRGVg----------sRGFPLRLQAt-------------------------eVRICp-VEFNPNFVARM 46  Homo sapiens
2J6A_A         2 KFLTTNFLKCSVKACdt--------snDNFPLQYDGsk-----------------------cqLVQDesIEFNPEFLLNI 50  Saccharomyces c...
5CM2_M         2 KFLTSNFVQCASKQCvs--------sgNAFPLTFSAl-------------------------eMVQQe-AEFDPEFLVSM 47  Yarrowia lipoly...
NP_014444      2 KFLTTNFLKCSVKACdt--------snDNFPLQYDGsk-----------------------cqLVQDesIEFNPEFLLNI 50  Saccharomyces c...
XP_002365720   2 RLLTHNLIACNRRQCt-----------GGFPLKIVVdeks--------------------edaTTVEp-SEFQPELVKQL 49  Toxoplasma gond...
XP_001348245   2 RLLTHNFLKCNETQCt-----------GGYPLTIKLdmds--------------------qenIKIId-QDINVEFVKNV 49  Plasmodium falc...
XP_002786668   2 RLLTHNLMMCNRKQCs-----------GGYPLRICPkqqpqgdvgmkdsedetspepeqerptFKVEe-SDFNPDFIRHM 69  Perkinsus marin...
XP_002896722   2 RLLTHNMLVCHVKACadtagreagarpLNFPLRMDG---------------------------VVVLe-TQYSKSFMLHI 53  Phytophthora in...
XP_008892475   2 RLLTHNMLVCHVKACadtagreagtrpLNFPLRIAPem-----------------------dgVVVLe-TQYSKSFMLHI 57  Phytophthora pa...
XP_008896919   2 RLITHNLLVCNKKGVe-----------NGYPLAIEAe-------------------------eVEVVa-CDFQAAFVRKM 44  Phytophthora pa...
Feature 1          # #                                                                      # ###
6KMR_A        47 IPKvEWSAFLEAADNlrl---iqVPKGPVegy-------eeNEEFLRTMHHLLLEVEviEGTLQCPeSGRMFPISRGIPN 116 Homo sapiens
2J6A_A        51 VDRvDWPAVLTVAAElgn---naLPPTKPsfpssiqeltddDMAILNDLHTLLLQTSiaEGEMKCRnCGHIYYIKNGIPN 127 Saccharomyces c...
5CM2_M        48 LERiDWAALVKVANDlgn---esLPDVKPeidep---faegNQGLLQELHSLLIETCivEGTMKCEnCGHTYFIKNSIPN 121 Yarrowia lipoly...
NP_014444     51 VDRvDWPAVLTVAAElgn---naLPPTKPsfpssiqeltddDMAILNDLHTLLLQTSiaEGEMKCRnCGHIYYIKNGIPN 127 Saccharomyces c...
XP_002365720  50 LGKlDWEALVKTADQfg----lqLPPTFTesd-------ksDEHFLRAVHEAVVEFHvlEGKLVCPvCAREYPVSNGIPN 118 Toxoplasma gond...
XP_001348245  50 LSKvDYDVLYNTAKQfgi---nlLASYNSdh--------leDEEFLNSVHHALFKVHimEGSLVCPkCNISFPIKDGIPN 118 Plasmodium falc...
XP_002786668  70 LDKlEWDALLSTLTQcqgl-tqsLPPSYTesd-------kdDENFLKAVHDVIIDYHilEADLKCPkCDRVYPITKGIPN 141 Perkinsus marin...
XP_002896722  54 MKSiDYPALCHTTKElnhpevpiLPEQIPtdl-------aeQDELLKLIHRVIFDTNivEGELICNnCGRSYAITNAVPN 126 Phytophthora in...
XP_008892475  58 MKSiDYPALCHTTKElnhpevpiLPEQIPadl-------seQDELLKLIHRVIFDTNivEGELICNnCGRSYPVTNAVPN 130 Phytophthora pa...
XP_008896919  45 LTKlDWNAFLTGAKAlkl--adgLPETLPsaee-----gatDEETLRKIHHALLEVHvkQGKLMCPeSGRAFPIIDGIPN 117 Phytophthora pa...
Feature 1        ## 
6KMR_A       117 MLL 119 Homo sapiens
2J6A_A       128 LLL 130 Saccharomyces cerevisiae
5CM2_M       122 FLL 124 Yarrowia lipolytica CLIB122
NP_014444    128 LLL 130 Saccharomyces cerevisiae S288C
XP_002365720 119 MLL 121 Toxoplasma gondii ME49
XP_001348245 119 MLT 121 Plasmodium falciparum 3D7
XP_002786668 142 MLL 144 Perkinsus marinus ATCC 50983
XP_002896722 127 MLL 129 Phytophthora infestans T30-4
XP_008892475 131 MLL 133 Phytophthora parasitica INRA-310
XP_008896919 118 MLL 120 Phytophthora parasitica INRA-310

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