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Conserved domains on  [gi|568993391|ref|XP_006521487|]
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mitochondrial tRNA-specific 2-thiouridylase 1 isoform X2 [Mus musculus]

Protein Classification

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

Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble

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 6.78e-104

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: 307.13  E-value: 6.78e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391   5 GADAVATGHYARTSLEDeevfeqkhtkkpdglfrnrfevRNPVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGELTKD 84
Cdd:cd01998  114 GADYIATGHYARIEEDN----------------------RGRYRLLRAVDPNKDQSYFLSRLSQEQLSRTLFPLGHLTKS 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391  85 FVKKIAAENSLhHVLQKRESMGICFIGKRNLEHFLLQYLQPR-PGKFVSIeDNTVLGTHKGWFLYTLGQRAKIS-GLREP 162
Cdd:cd01998  172 EVREIAREAGL-PVAEKKDSQGICFIGKRDFRDFLKEYLPEKlPGPIVDI-DGKVLGEHKGLWFYTIGQRKGLGiAAGEP 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391 163 WYVVEKDGTKGDVLVAPrvDHPALYRDLLRTNRVHWIAEEPPaalvrDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTA 242
Cdd:cd01998  250 LYVVKKDPEKNIVVVGP--GHPALFSDTLRASDLNWISPEPP-----LEPLECEAKIRYRQPPVPCTVTPLDDGRLKVEF 322
                        250       260
                 ....*....|....*....|....*..
gi 568993391 243 VKAVRGLALGQFAVFYKGEECLGSGKI 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 6.78e-104

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: 307.13  E-value: 6.78e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391   5 GADAVATGHYARTSLEDeevfeqkhtkkpdglfrnrfevRNPVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGELTKD 84
Cdd:cd01998  114 GADYIATGHYARIEEDN----------------------RGRYRLLRAVDPNKDQSYFLSRLSQEQLSRTLFPLGHLTKS 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391  85 FVKKIAAENSLhHVLQKRESMGICFIGKRNLEHFLLQYLQPR-PGKFVSIeDNTVLGTHKGWFLYTLGQRAKIS-GLREP 162
Cdd:cd01998  172 EVREIAREAGL-PVAEKKDSQGICFIGKRDFRDFLKEYLPEKlPGPIVDI-DGKVLGEHKGLWFYTIGQRKGLGiAAGEP 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391 163 WYVVEKDGTKGDVLVAPrvDHPALYRDLLRTNRVHWIAEEPPaalvrDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTA 242
Cdd:cd01998  250 LYVVKKDPEKNIVVVGP--GHPALFSDTLRASDLNWISPEPP-----LEPLECEAKIRYRQPPVPCTVTPLDDGRLKVEF 322
                        250       260
                 ....*....|....*....|....*..
gi 568993391 243 VKAVRGLALGQFAVFYKGEECLGSGKI 269
Cdd:cd01998  323 DEPQRAVTPGQAAVFYDGDEVLGGGII 349
MnmA COG0482
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ...
5-271 3.97e-89

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: 269.62  E-value: 3.97e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391   5 GADAVATGHYARTSLEDeevfeqkhtkkpdglfrNRFEvrnpvkLLQAADSFKDQTFFLSQVSQDALRRTIFPLGELTKD 84
Cdd:COG0482  116 GADYIATGHYARVEEKD-----------------GRYE------LLRGVDPNKDQSYFLYRLTQEQLSKTLFPLGELTKP 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391  85 FVKKIAAENSLhHVLQKRESMGICFIGKRNLEHFLLQYLQPRPGKFVSIeDNTVLGTHKGWFLYTLGQRakiSGLR---- 160
Cdd:COG0482  173 EVREIAEELGL-PVADKKDSQGICFIGDGDYRDFLERYLPEKPGDIVDL-DGKVLGEHDGLHYYTIGQR---KGLGiggg 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391 161 EPWYVVEKDGTKGDVLVAPRvdhPALYRDLLRTNRVHWIAEEPPAalvrdKMMECHFRFRHQMALVPCVLTLNQDGTVWV 240
Cdd:COG0482  248 EPLYVVGKDPETNTVIVGQG---EALYSRELTAEDVNWISGEPPE-----EPLRCTAKIRYRQPPVPATLTPLEDGRVRV 319
                        250       260       270
                 ....*....|....*....|....*....|.
gi 568993391 241 TAVKAVRGLALGQFAVFYKGEECLGSGKILR 271
Cdd:COG0482  320 EFDEPQRAVTPGQSAVFYDGDRVLGGGIIER 350
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
5-269 2.16e-86

tRNA-specific 2-thiouridylase MnmA; Reviewed


Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 262.31  E-value: 2.16e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391   5 GADAVATGHYARtsledeevfeqkhtkkpdglfrnrfeVRNPVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGELTKD 84
Cdd:PRK00143 116 GADYIATGHYAR--------------------------IRDGRELLRGVDPNKDQSYFLYQLTQEQLAKLLFPLGELTKP 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391  85 FVKKIAAENSLhHVLQKRESMGICFIGKRNLEHFLLQYLQPRPGKFVSIeDNTVLGTHKGWFLYTLGQRaK---ISGLRE 161
Cdd:PRK00143 170 EVREIAEEAGL-PVAKKKDSQGICFIGERDYRDFLKRYLPAQPGEIVDL-DGKVLGEHKGLMYYTIGQR-KglgIGGDGE 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391 162 PWYVVEKDGTKGDVLVAPRvdhPALYRDLLRTNRVHWIAEEPPAalvrdKMMECHFRFRHQMALVPCVLTLnQDGTVWVT 241
Cdd:PRK00143 247 PWYVVGKDPETNTVVVGQG---EALYSRELIASDLNWVGGEPPE-----EPFECTAKIRYRQKPVPATVEL-EDDRVEVE 317
                        250       260
                 ....*....|....*....|....*...
gi 568993391 242 AVKAVRGLALGQFAVFYKGEECLGSGKI 269
Cdd:PRK00143 318 FDEPQRAVTPGQAAVFYDGDRVLGGGII 345
trmU TIGR00420
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ...
5-269 1.73e-69

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: 219.56  E-value: 1.73e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391    5 GADAVATGHYARTSlEDEEVFeqkhtkkpdglfrnrfevrnpvKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGELTKD 84
Cdd:TIGR00420 117 GNDKIATGHYARIA-EIEGKS----------------------LLLRALDKNKDQSYFLYHLSHEQLAKLLFPLGELLKP 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391   85 FVKKIAAENSLhHVLQKRESMGICFIGKRNLEHFLLQYLQPRPGKFVSIEDNTVLGTHKGWFLYTLGQRA--KISGLREP 162
Cdd:TIGR00420 174 EVRQIAKNAGL-PTAEKKDSQGICFIGERKFRDFLKKYLPVKPGVIITVDGQSVIGEHDGLWFYTIGQRKglGIGGAAEP 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391  163 WYVVEKDGTKGDVLVAPrvDHPALYRDLLRTNRVHWIAEEPpaalvRDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTA 242
Cdd:TIGR00420 253 WFVVEKDLETNELVVSH--GKPDLASRGLLAQQFHWLDDEP-----NPFEMRCTVKIRYRQVPVQCKLKLLDDNLIEVIF 325
                         250       260
                  ....*....|....*....|....*..
gi 568993391  243 VKAVRGLALGQFAVFYKGEECLGSGKI 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 4.67e-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: 128.52  E-value: 4.67e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391    5 GADAVATGHYARTSLEDEEVFEqkhtkkpdglfrnrfevrnpvkLLQAADSFKDQTFFLSQVSQDALRRTIFPLGELTKD 84
Cdd:pfam03054 118 GADYVATGHYARVSLNKDGGSE----------------------LLRALDKNKDQSYFLSTLSQEQLEKLLFPLGELTKE 175
                          90       100
                  ....*....|....*....|....*...
gi 568993391   85 FVKKIAAENSLhHVLQKRESMGICFIGK 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 6.78e-104

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: 307.13  E-value: 6.78e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391   5 GADAVATGHYARTSLEDeevfeqkhtkkpdglfrnrfevRNPVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGELTKD 84
Cdd:cd01998  114 GADYIATGHYARIEEDN----------------------RGRYRLLRAVDPNKDQSYFLSRLSQEQLSRTLFPLGHLTKS 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391  85 FVKKIAAENSLhHVLQKRESMGICFIGKRNLEHFLLQYLQPR-PGKFVSIeDNTVLGTHKGWFLYTLGQRAKIS-GLREP 162
Cdd:cd01998  172 EVREIAREAGL-PVAEKKDSQGICFIGKRDFRDFLKEYLPEKlPGPIVDI-DGKVLGEHKGLWFYTIGQRKGLGiAAGEP 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391 163 WYVVEKDGTKGDVLVAPrvDHPALYRDLLRTNRVHWIAEEPPaalvrDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTA 242
Cdd:cd01998  250 LYVVKKDPEKNIVVVGP--GHPALFSDTLRASDLNWISPEPP-----LEPLECEAKIRYRQPPVPCTVTPLDDGRLKVEF 322
                        250       260
                 ....*....|....*....|....*..
gi 568993391 243 VKAVRGLALGQFAVFYKGEECLGSGKI 269
Cdd:cd01998  323 DEPQRAVTPGQAAVFYDGDEVLGGGII 349
MnmA COG0482
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ...
5-271 3.97e-89

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: 269.62  E-value: 3.97e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391   5 GADAVATGHYARTSLEDeevfeqkhtkkpdglfrNRFEvrnpvkLLQAADSFKDQTFFLSQVSQDALRRTIFPLGELTKD 84
Cdd:COG0482  116 GADYIATGHYARVEEKD-----------------GRYE------LLRGVDPNKDQSYFLYRLTQEQLSKTLFPLGELTKP 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391  85 FVKKIAAENSLhHVLQKRESMGICFIGKRNLEHFLLQYLQPRPGKFVSIeDNTVLGTHKGWFLYTLGQRakiSGLR---- 160
Cdd:COG0482  173 EVREIAEELGL-PVADKKDSQGICFIGDGDYRDFLERYLPEKPGDIVDL-DGKVLGEHDGLHYYTIGQR---KGLGiggg 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391 161 EPWYVVEKDGTKGDVLVAPRvdhPALYRDLLRTNRVHWIAEEPPAalvrdKMMECHFRFRHQMALVPCVLTLNQDGTVWV 240
Cdd:COG0482  248 EPLYVVGKDPETNTVIVGQG---EALYSRELTAEDVNWISGEPPE-----EPLRCTAKIRYRQPPVPATLTPLEDGRVRV 319
                        250       260       270
                 ....*....|....*....|....*....|.
gi 568993391 241 TAVKAVRGLALGQFAVFYKGEECLGSGKILR 271
Cdd:COG0482  320 EFDEPQRAVTPGQSAVFYDGDRVLGGGIIER 350
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
5-269 2.16e-86

tRNA-specific 2-thiouridylase MnmA; Reviewed


Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 262.31  E-value: 2.16e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391   5 GADAVATGHYARtsledeevfeqkhtkkpdglfrnrfeVRNPVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGELTKD 84
Cdd:PRK00143 116 GADYIATGHYAR--------------------------IRDGRELLRGVDPNKDQSYFLYQLTQEQLAKLLFPLGELTKP 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391  85 FVKKIAAENSLhHVLQKRESMGICFIGKRNLEHFLLQYLQPRPGKFVSIeDNTVLGTHKGWFLYTLGQRaK---ISGLRE 161
Cdd:PRK00143 170 EVREIAEEAGL-PVAKKKDSQGICFIGERDYRDFLKRYLPAQPGEIVDL-DGKVLGEHKGLMYYTIGQR-KglgIGGDGE 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391 162 PWYVVEKDGTKGDVLVAPRvdhPALYRDLLRTNRVHWIAEEPPAalvrdKMMECHFRFRHQMALVPCVLTLnQDGTVWVT 241
Cdd:PRK00143 247 PWYVVGKDPETNTVVVGQG---EALYSRELIASDLNWVGGEPPE-----EPFECTAKIRYRQKPVPATVEL-EDDRVEVE 317
                        250       260
                 ....*....|....*....|....*...
gi 568993391 242 AVKAVRGLALGQFAVFYKGEECLGSGKI 269
Cdd:PRK00143 318 FDEPQRAVTPGQAAVFYDGDRVLGGGII 345
trmU TIGR00420
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ...
5-269 1.73e-69

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: 219.56  E-value: 1.73e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391    5 GADAVATGHYARTSlEDEEVFeqkhtkkpdglfrnrfevrnpvKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGELTKD 84
Cdd:TIGR00420 117 GNDKIATGHYARIA-EIEGKS----------------------LLLRALDKNKDQSYFLYHLSHEQLAKLLFPLGELLKP 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391   85 FVKKIAAENSLhHVLQKRESMGICFIGKRNLEHFLLQYLQPRPGKFVSIEDNTVLGTHKGWFLYTLGQRA--KISGLREP 162
Cdd:TIGR00420 174 EVRQIAKNAGL-PTAEKKDSQGICFIGERKFRDFLKKYLPVKPGVIITVDGQSVIGEHDGLWFYTIGQRKglGIGGAAEP 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391  163 WYVVEKDGTKGDVLVAPrvDHPALYRDLLRTNRVHWIAEEPpaalvRDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTA 242
Cdd:TIGR00420 253 WFVVEKDLETNELVVSH--GKPDLASRGLLAQQFHWLDDEP-----NPFEMRCTVKIRYRQVPVQCKLKLLDDNLIEVIF 325
                         250       260
                  ....*....|....*....|....*..
gi 568993391  243 VKAVRGLALGQFAVFYKGEECLGSGKI 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 4.67e-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: 128.52  E-value: 4.67e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391    5 GADAVATGHYARTSLEDEEVFEqkhtkkpdglfrnrfevrnpvkLLQAADSFKDQTFFLSQVSQDALRRTIFPLGELTKD 84
Cdd:pfam03054 118 GADYVATGHYARVSLNKDGGSE----------------------LLRALDKNKDQSYFLSTLSQEQLEKLLFPLGELTKE 175
                          90       100
                  ....*....|....*....|....*...
gi 568993391   85 FVKKIAAENSLhHVLQKRESMGICFIGK 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 8.23e-30

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: 108.13  E-value: 8.23e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391  188 RDLLRTNRVHWIAEEPPaalvrDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAVKAVRGLALGQFAVFYKGEECLGSG 267
Cdd:pfam20258   1 SDGLRAKDPNWLGDKPP-----TEPLECTVKVRHRQPPVPCVVELIDDETVEVHFDEPVRAVTPGQAAVFYDGDRCLGGG 75

                  ..
gi 568993391  268 KI 269
Cdd:pfam20258  76 II 77
PRK14664 PRK14664
tRNA-specific 2-thiouridylase MnmA; Provisional
1-269 4.64e-26

tRNA-specific 2-thiouridylase MnmA; Provisional


Pssm-ID: 173127 [Multi-domain]  Cd Length: 362  Bit Score: 105.81  E-value: 4.64e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391   1 MMCSGADA-----VATGHYARtsLEdeevfeqkhtkkpdglfrnrfEVRNPVKLLQAADSFKDQTFFLSQVSQDALRRTI 75
Cdd:PRK14664  99 MLIEWADKlgcawIATGHYSR--LE---------------------ERNGHIYIVAGDDDKKDQSYFLWRLGQDILRRCI 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391  76 FPLGELTKDFVKKIAAENSLHHVLQKRESMGICFIgKRNLEHFLLQY-----LQPRPGKFVSIEdNTVLGTHKGWFLYTL 150
Cdd:PRK14664 156 FPLGNYTKQTVREYLREKGYEAKSKEGESMEVCFI-KGDYRDFLREQcpeldTEVGPGWFVNSE-GVKLGQHKGFPYYTI 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391 151 GQRAKIS-GLREPWYVVEKDGTKGDVLVAprvDHPALYRDLLRTNRVHwIAEEppaalvrDKMMECH---FRFRHQMALV 226
Cdd:PRK14664 234 GQRKGLEiALGKPAYVLKINPQKNTVMLG---DAEQLKAEYMLAEQDN-IVDE-------QELFACPdlaVRIRYRSRPI 302
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 568993391 227 PCVLTLNQDGTVWVTAVKAVRGLALGQFAVFYKGEECLGSGKI 269
Cdd:PRK14664 303 PCRVKRLEDGRLLVRFLAEASAIAPGQSAVFYEGRRVLGGAFI 345
mnmA PRK14665
tRNA-specific 2-thiouridylase MnmA; Provisional
9-270 3.79e-24

tRNA-specific 2-thiouridylase MnmA; Provisional


Pssm-ID: 173128 [Multi-domain]  Cd Length: 360  Bit Score: 100.39  E-value: 3.79e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391   9 VATGHYARTsledeevfeqkhtKKPDGLFRnrfevrnpvkLLQAADSFKDQTFFLSQVSQDALRRTIFPLGELTKDFVKK 88
Cdd:PRK14665 117 LATGHYVRK-------------QWIDGNYY----------ITPAEDVDKDQSFFLWGLRQEILQRMLLPMGGMTKSEARA 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391  89 IAAENSLHHVLQKRESMGICF--IGKRNLEHFLL----------QYLQPRPGKFVSiEDNTVLGTHKGWFLYTLGQRAKI 156
Cdd:PRK14665 174 YAAERGFEKVAKKRDSLGVCFcpMDYRSFLKKCLcdesgdknrnIYRKVERGRFLD-ESGNFIAWHEGYPFYTIGQRRGL 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993391 157 S-GLREPWYVVEKDGTKGDVLVAprvDHPALYRDLLRTNrvHWIAEEPPAALVRDKMMeCHFRFRHQMAlvPCVLTLNQD 235
Cdd:PRK14665 253 GiQLNRAVFVKEIHPETNEVVLA---SLKALEKTEMWLK--DWNIVNESRLLGCDDII-VKIRYRKQEN--HCTVTITPD 324
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 568993391 236 GTVWVTAVKAVRGLALGQFAVFYKGEECLGSGKIL 270
Cdd:PRK14665 325 NLLHVQLHEPLTAIAEGQAAAFYKDGLLLGGGIIT 359
tRNA_Me_trans_M pfam20259
tRNA methyl transferase PRC-barrel domain; This family represents a central PRC-barrel domain ...
116-179 4.98e-23

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: 89.97  E-value: 4.98e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568993391  116 EHFLLQYLQPRPGKFVSIEDNTVLGTHKGWFLYTLGQR--AKISGLREPWYVVEKDGTKGDVLVAP 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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