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Conserved domains on  [gi|544346331|ref|NP_001269711|]
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mitochondrial tRNA-specific 2-thiouridylase 1 isoform d [Homo sapiens]

Protein Classification

tRNA-specific 2-thiouridylase( domain architecture ID 10113449)

MnmA/TRMU family tRNA-specific 2-thiouridylase catalyzes the 2-thiolation of uridine at the wobble position of tRNAs

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
5-269 1.34e-106

MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


:

Pssm-ID: 467502 [Multi-domain]  Cd Length: 349  Bit Score: 314.06  E-value: 1.34e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331   5 GADAIATGHYARTSLEDeevfeqkhvkkpeglfrnrfevRNAVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGGLTKE 84
Cdd:cd01998  114 GADYIATGHYARIEEDN----------------------RGRYRLLRAVDPNKDQSYFLSRLSQEQLSRTLFPLGHLTKS 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331  85 FVKKIAAENRLhHVLQKKESMGMCFIGKRNFEHFLLQYLQPR-PGHFISIeDNKVLGTHKGWFLYTLGQRANIG-GLREP 162
Cdd:cd01998  172 EVREIAREAGL-PVAEKKDSQGICFIGKRDFRDFLKEYLPEKlPGPIVDI-DGKVLGEHKGLWFYTIGQRKGLGiAAGEP 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331 163 WYVVEKDSVKGDVFVAPrtDHPALYRDLLRTSRVHWIAEEPPaalvrDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTA 242
Cdd:cd01998  250 LYVVKKDPEKNIVVVGP--GHPALFSDTLRASDLNWISPEPP-----LEPLECEAKIRYRQPPVPCTVTPLDDGRLKVEF 322
                        250       260
                 ....*....|....*....|....*..
gi 544346331 243 VQAVRALATGQFAVFYKGDECLGSGKI 269
Cdd:cd01998  323 DEPQRAVTPGQAAVFYDGDEVLGGGII 349
 
Name Accession Description Interval E-value
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
5-269 1.34e-106

MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467502 [Multi-domain]  Cd Length: 349  Bit Score: 314.06  E-value: 1.34e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331   5 GADAIATGHYARTSLEDeevfeqkhvkkpeglfrnrfevRNAVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGGLTKE 84
Cdd:cd01998  114 GADYIATGHYARIEEDN----------------------RGRYRLLRAVDPNKDQSYFLSRLSQEQLSRTLFPLGHLTKS 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331  85 FVKKIAAENRLhHVLQKKESMGMCFIGKRNFEHFLLQYLQPR-PGHFISIeDNKVLGTHKGWFLYTLGQRANIG-GLREP 162
Cdd:cd01998  172 EVREIAREAGL-PVAEKKDSQGICFIGKRDFRDFLKEYLPEKlPGPIVDI-DGKVLGEHKGLWFYTIGQRKGLGiAAGEP 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331 163 WYVVEKDSVKGDVFVAPrtDHPALYRDLLRTSRVHWIAEEPPaalvrDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTA 242
Cdd:cd01998  250 LYVVKKDPEKNIVVVGP--GHPALFSDTLRASDLNWISPEPP-----LEPLECEAKIRYRQPPVPCTVTPLDDGRLKVEF 322
                        250       260
                 ....*....|....*....|....*..
gi 544346331 243 VQAVRALATGQFAVFYKGDECLGSGKI 269
Cdd:cd01998  323 DEPQRAVTPGQAAVFYDGDEVLGGGII 349
MnmA COG0482
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ...
5-271 2.17e-91

tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ribosomal structure and biogenesis]; tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440250 [Multi-domain]  Cd Length: 353  Bit Score: 275.39  E-value: 2.17e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331   5 GADAIATGHYARtsledeevfeqkhVKKPEGLFRnrfevrnavkLLQAADSFKDQTFFLSQVSQDALRRTIFPLGGLTKE 84
Cdd:COG0482  116 GADYIATGHYAR-------------VEEKDGRYE----------LLRGVDPNKDQSYFLYRLTQEQLSKTLFPLGELTKP 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331  85 FVKKIAAENRLHhVLQKKESMGMCFIGKRNFEHFLLQYLQPRPGHFISIeDNKVLGTHKGWFLYTLGQRANIG-GLREPW 163
Cdd:COG0482  173 EVREIAEELGLP-VADKKDSQGICFIGDGDYRDFLERYLPEKPGDIVDL-DGKVLGEHDGLHYYTIGQRKGLGiGGGEPL 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331 164 YVVEKDSVKGDVFVAPRTDhpaLYRDLLRTSRVHWIAEEPPAalvrdKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAV 243
Cdd:COG0482  251 YVVGKDPETNTVIVGQGEA---LYSRELTAEDVNWISGEPPE-----EPLRCTAKIRYRQPPVPATLTPLEDGRVRVEFD 322
                        250       260
                 ....*....|....*....|....*...
gi 544346331 244 QAVRALATGQFAVFYKGDECLGSGKILR 271
Cdd:COG0482  323 EPQRAVTPGQSAVFYDGDRVLGGGIIER 350
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
5-269 1.51e-88

tRNA-specific 2-thiouridylase MnmA; Reviewed


Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 268.09  E-value: 1.51e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331   5 GADAIATGHYARtsledeevfeqkhvkkpeglfrnrfeVRNAVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGGLTKE 84
Cdd:PRK00143 116 GADYIATGHYAR--------------------------IRDGRELLRGVDPNKDQSYFLYQLTQEQLAKLLFPLGELTKP 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331  85 FVKKIAAENRLhHVLQKKESMGMCFIGKRNFEHFLLQYLQPRPGHFISIeDNKVLGTHKGWFLYTLGQRA--NIGGLREP 162
Cdd:PRK00143 170 EVREIAEEAGL-PVAKKKDSQGICFIGERDYRDFLKRYLPAQPGEIVDL-DGKVLGEHKGLMYYTIGQRKglGIGGDGEP 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331 163 WYVVEKDSVKGDVFVAPRtdhPALYRDLLRTSRVHWIAEEPPAalvrdKMMECHFRFRHQMALVPCVLTLnQDGTVWVTA 242
Cdd:PRK00143 248 WYVVGKDPETNTVVVGQG---EALYSRELIASDLNWVGGEPPE-----EPFECTAKIRYRQKPVPATVEL-EDDRVEVEF 318
                        250       260
                 ....*....|....*....|....*..
gi 544346331 243 VQAVRALATGQFAVFYKGDECLGSGKI 269
Cdd:PRK00143 319 DEPQRAVTPGQAAVFYDGDRVLGGGII 345
trmU TIGR00420
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ...
5-269 5.97e-73

tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase (trmU, asuE, or mnmA) is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine (mnm5s2U34) present in the wobble position of some tRNAs. This enzyme appears not to occur in the Archaea. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273069 [Multi-domain]  Cd Length: 352  Bit Score: 228.42  E-value: 5.97e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331    5 GADAIATGHYARTSledeevfeqkhvkkpeglfrnrfEVRNAVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGGLTKE 84
Cdd:TIGR00420 117 GNDKIATGHYARIA-----------------------EIEGKSLLLRALDKNKDQSYFLYHLSHEQLAKLLFPLGELLKP 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331   85 FVKKIAAENRLHhVLQKKESMGMCFIGKRNFEHFLLQYLQPRPGHFISIEDNKVLGTHKGWFLYTLGQRA--NIGGLREP 162
Cdd:TIGR00420 174 EVRQIAKNAGLP-TAEKKDSQGICFIGERKFRDFLKKYLPVKPGVIITVDGQSVIGEHDGLWFYTIGQRKglGIGGAAEP 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331  163 WYVVEKDSVKGDVFVAprTDHPALYRDLLRTSRVHWIAEEPpaalvRDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTA 242
Cdd:TIGR00420 253 WFVVEKDLETNELVVS--HGKPDLASRGLLAQQFHWLDDEP-----NPFEMRCTVKIRYRQVPVQCKLKLLDDNLIEVIF 325
                         250       260
                  ....*....|....*....|....*..
gi 544346331  243 VQAVRALATGQFAVFYKGDECLGSGKI 269
Cdd:TIGR00420 326 DEPQAGVTPGQSAVLYKGDICLGGGII 352
tRNA_Me_trans pfam03054
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ...
5-112 1.44e-36

tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs.


Pssm-ID: 460787 [Multi-domain]  Cd Length: 202  Bit Score: 129.68  E-value: 1.44e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331    5 GADAIATGHYARTSLEDEevfeqkhvkkpeglfrnrfevrNAVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGGLTKE 84
Cdd:pfam03054 118 GADYVATGHYARVSLNKD----------------------GGSELLRALDKNKDQSYFLSTLSQEQLEKLLFPLGELTKE 175
                          90       100
                  ....*....|....*....|....*...
gi 544346331   85 FVKKIAAENRLhHVLQKKESMGMCFIGK 112
Cdd:pfam03054 176 EVRKIAKEAGL-ATAKKKDSQGICFIGK 202
 
Name Accession Description Interval E-value
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
5-269 1.34e-106

MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467502 [Multi-domain]  Cd Length: 349  Bit Score: 314.06  E-value: 1.34e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331   5 GADAIATGHYARTSLEDeevfeqkhvkkpeglfrnrfevRNAVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGGLTKE 84
Cdd:cd01998  114 GADYIATGHYARIEEDN----------------------RGRYRLLRAVDPNKDQSYFLSRLSQEQLSRTLFPLGHLTKS 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331  85 FVKKIAAENRLhHVLQKKESMGMCFIGKRNFEHFLLQYLQPR-PGHFISIeDNKVLGTHKGWFLYTLGQRANIG-GLREP 162
Cdd:cd01998  172 EVREIAREAGL-PVAEKKDSQGICFIGKRDFRDFLKEYLPEKlPGPIVDI-DGKVLGEHKGLWFYTIGQRKGLGiAAGEP 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331 163 WYVVEKDSVKGDVFVAPrtDHPALYRDLLRTSRVHWIAEEPPaalvrDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTA 242
Cdd:cd01998  250 LYVVKKDPEKNIVVVGP--GHPALFSDTLRASDLNWISPEPP-----LEPLECEAKIRYRQPPVPCTVTPLDDGRLKVEF 322
                        250       260
                 ....*....|....*....|....*..
gi 544346331 243 VQAVRALATGQFAVFYKGDECLGSGKI 269
Cdd:cd01998  323 DEPQRAVTPGQAAVFYDGDEVLGGGII 349
MnmA COG0482
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ...
5-271 2.17e-91

tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ribosomal structure and biogenesis]; tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440250 [Multi-domain]  Cd Length: 353  Bit Score: 275.39  E-value: 2.17e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331   5 GADAIATGHYARtsledeevfeqkhVKKPEGLFRnrfevrnavkLLQAADSFKDQTFFLSQVSQDALRRTIFPLGGLTKE 84
Cdd:COG0482  116 GADYIATGHYAR-------------VEEKDGRYE----------LLRGVDPNKDQSYFLYRLTQEQLSKTLFPLGELTKP 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331  85 FVKKIAAENRLHhVLQKKESMGMCFIGKRNFEHFLLQYLQPRPGHFISIeDNKVLGTHKGWFLYTLGQRANIG-GLREPW 163
Cdd:COG0482  173 EVREIAEELGLP-VADKKDSQGICFIGDGDYRDFLERYLPEKPGDIVDL-DGKVLGEHDGLHYYTIGQRKGLGiGGGEPL 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331 164 YVVEKDSVKGDVFVAPRTDhpaLYRDLLRTSRVHWIAEEPPAalvrdKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAV 243
Cdd:COG0482  251 YVVGKDPETNTVIVGQGEA---LYSRELTAEDVNWISGEPPE-----EPLRCTAKIRYRQPPVPATLTPLEDGRVRVEFD 322
                        250       260
                 ....*....|....*....|....*...
gi 544346331 244 QAVRALATGQFAVFYKGDECLGSGKILR 271
Cdd:COG0482  323 EPQRAVTPGQSAVFYDGDRVLGGGIIER 350
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
5-269 1.51e-88

tRNA-specific 2-thiouridylase MnmA; Reviewed


Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 268.09  E-value: 1.51e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331   5 GADAIATGHYARtsledeevfeqkhvkkpeglfrnrfeVRNAVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGGLTKE 84
Cdd:PRK00143 116 GADYIATGHYAR--------------------------IRDGRELLRGVDPNKDQSYFLYQLTQEQLAKLLFPLGELTKP 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331  85 FVKKIAAENRLhHVLQKKESMGMCFIGKRNFEHFLLQYLQPRPGHFISIeDNKVLGTHKGWFLYTLGQRA--NIGGLREP 162
Cdd:PRK00143 170 EVREIAEEAGL-PVAKKKDSQGICFIGERDYRDFLKRYLPAQPGEIVDL-DGKVLGEHKGLMYYTIGQRKglGIGGDGEP 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331 163 WYVVEKDSVKGDVFVAPRtdhPALYRDLLRTSRVHWIAEEPPAalvrdKMMECHFRFRHQMALVPCVLTLnQDGTVWVTA 242
Cdd:PRK00143 248 WYVVGKDPETNTVVVGQG---EALYSRELIASDLNWVGGEPPE-----EPFECTAKIRYRQKPVPATVEL-EDDRVEVEF 318
                        250       260
                 ....*....|....*....|....*..
gi 544346331 243 VQAVRALATGQFAVFYKGDECLGSGKI 269
Cdd:PRK00143 319 DEPQRAVTPGQAAVFYDGDRVLGGGII 345
trmU TIGR00420
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ...
5-269 5.97e-73

tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase (trmU, asuE, or mnmA) is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine (mnm5s2U34) present in the wobble position of some tRNAs. This enzyme appears not to occur in the Archaea. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273069 [Multi-domain]  Cd Length: 352  Bit Score: 228.42  E-value: 5.97e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331    5 GADAIATGHYARTSledeevfeqkhvkkpeglfrnrfEVRNAVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGGLTKE 84
Cdd:TIGR00420 117 GNDKIATGHYARIA-----------------------EIEGKSLLLRALDKNKDQSYFLYHLSHEQLAKLLFPLGELLKP 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331   85 FVKKIAAENRLHhVLQKKESMGMCFIGKRNFEHFLLQYLQPRPGHFISIEDNKVLGTHKGWFLYTLGQRA--NIGGLREP 162
Cdd:TIGR00420 174 EVRQIAKNAGLP-TAEKKDSQGICFIGERKFRDFLKKYLPVKPGVIITVDGQSVIGEHDGLWFYTIGQRKglGIGGAAEP 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331  163 WYVVEKDSVKGDVFVAprTDHPALYRDLLRTSRVHWIAEEPpaalvRDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTA 242
Cdd:TIGR00420 253 WFVVEKDLETNELVVS--HGKPDLASRGLLAQQFHWLDDEP-----NPFEMRCTVKIRYRQVPVQCKLKLLDDNLIEVIF 325
                         250       260
                  ....*....|....*....|....*..
gi 544346331  243 VQAVRALATGQFAVFYKGDECLGSGKI 269
Cdd:TIGR00420 326 DEPQAGVTPGQSAVLYKGDICLGGGII 352
tRNA_Me_trans pfam03054
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ...
5-112 1.44e-36

tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs.


Pssm-ID: 460787 [Multi-domain]  Cd Length: 202  Bit Score: 129.68  E-value: 1.44e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331    5 GADAIATGHYARTSLEDEevfeqkhvkkpeglfrnrfevrNAVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGGLTKE 84
Cdd:pfam03054 118 GADYVATGHYARVSLNKD----------------------GGSELLRALDKNKDQSYFLSTLSQEQLEKLLFPLGELTKE 175
                          90       100
                  ....*....|....*....|....*...
gi 544346331   85 FVKKIAAENRLhHVLQKKESMGMCFIGK 112
Cdd:pfam03054 176 EVRKIAKEAGL-ATAKKKDSQGICFIGK 202
tRNA_Me_trans_C pfam20258
Aminomethyltransferase beta-barrel domain; This domain is found at the C-terminus of tRNA ...
188-269 5.11e-32

Aminomethyltransferase beta-barrel domain; This domain is found at the C-terminus of tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs.


Pssm-ID: 466409 [Multi-domain]  Cd Length: 77  Bit Score: 113.91  E-value: 5.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331  188 RDLLRTSRVHWIAEEPPaalvrDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAVQAVRALATGQFAVFYKGDECLGSG 267
Cdd:pfam20258   1 SDGLRAKDPNWLGDKPP-----TEPLECTVKVRHRQPPVPCVVELIDDETVEVHFDEPVRAVTPGQAAVFYDGDRCLGGG 75

                  ..
gi 544346331  268 KI 269
Cdd:pfam20258  76 II 77
mnmA PRK14665
tRNA-specific 2-thiouridylase MnmA; Provisional
9-270 2.34e-27

tRNA-specific 2-thiouridylase MnmA; Provisional


Pssm-ID: 173128 [Multi-domain]  Cd Length: 360  Bit Score: 109.25  E-value: 2.34e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331   9 IATGHYARtsledeevfeqkhvkkpeglfrnRFEVRNAVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGGLTKEFVKK 88
Cdd:PRK14665 117 LATGHYVR-----------------------KQWIDGNYYITPAEDVDKDQSFFLWGLRQEILQRMLLPMGGMTKSEARA 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331  89 IAAENRLHHVLQKKESMGMCF--IGKRNFEHFLL----------QYLQPRPGHFISiEDNKVLGTHKGWFLYTLGQRANI 156
Cdd:PRK14665 174 YAAERGFEKVAKKRDSLGVCFcpMDYRSFLKKCLcdesgdknrnIYRKVERGRFLD-ESGNFIAWHEGYPFYTIGQRRGL 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331 157 G-GLREPWYVVEKDSVKGDVFVAprtDHPALYRDLLRTSrvHWIAEEPPAALVRDKMMeCHFRFRHQMAlvPCVLTLNQD 235
Cdd:PRK14665 253 GiQLNRAVFVKEIHPETNEVVLA---SLKALEKTEMWLK--DWNIVNESRLLGCDDII-VKIRYRKQEN--HCTVTITPD 324
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 544346331 236 GTVWVTAVQAVRALATGQFAVFYKGDECLGSGKIL 270
Cdd:PRK14665 325 NLLHVQLHEPLTAIAEGQAAAFYKDGLLLGGGIIT 359
PRK14664 PRK14664
tRNA-specific 2-thiouridylase MnmA; Provisional
1-269 2.97e-27

tRNA-specific 2-thiouridylase MnmA; Provisional


Pssm-ID: 173127 [Multi-domain]  Cd Length: 362  Bit Score: 108.89  E-value: 2.97e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331   1 MMCSGADA-----IATGHYARtsLEdeevfeqkhvkkpeglfrnrfEVRNAVKLLQAADSFKDQTFFLSQVSQDALRRTI 75
Cdd:PRK14664  99 MLIEWADKlgcawIATGHYSR--LE---------------------ERNGHIYIVAGDDDKKDQSYFLWRLGQDILRRCI 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331  76 FPLGGLTKEFVKKIAAENRLHHVLQKKESMGMCFIgKRNFEHFLLQY-----LQPRPGHFISIEDNKvLGTHKGWFLYTL 150
Cdd:PRK14664 156 FPLGNYTKQTVREYLREKGYEAKSKEGESMEVCFI-KGDYRDFLREQcpeldTEVGPGWFVNSEGVK-LGQHKGFPYYTI 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346331 151 GQRANIG-GLREPWYVVEKDSVKGDVFVAprtDHPALYRDLLRTSRVHwIAEEppaalvrDKMMECH---FRFRHQMALV 226
Cdd:PRK14664 234 GQRKGLEiALGKPAYVLKINPQKNTVMLG---DAEQLKAEYMLAEQDN-IVDE-------QELFACPdlaVRIRYRSRPI 302
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 544346331 227 PCVLTLNQDGTVWVTAVQAVRALATGQFAVFYKGDECLGSGKI 269
Cdd:PRK14664 303 PCRVKRLEDGRLLVRFLAEASAIAPGQSAVFYEGRRVLGGAFI 345
tRNA_Me_trans_M pfam20259
tRNA methyl transferase PRC-barrel domain; This family represents a central PRC-barrel domain ...
116-179 3.75e-26

tRNA methyl transferase PRC-barrel domain; This family represents a central PRC-barrel domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs.


Pssm-ID: 466410 [Multi-domain]  Cd Length: 66  Bit Score: 98.06  E-value: 3.75e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544346331  116 EHFLLQYLQPRPGHFISIEDNKVLGTHKGWFLYTLGQR--ANIGGLREPWYVVEKDSVKGDVFVAP 179
Cdd:pfam20259   1 KDFLKEYLPVKPGDIIDIDTGEVLGEHEGIWFYTIGQRkgLGIGGYGEPWYVVEKDPKKNTVYVGR 66
 
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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