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Conserved domains on  [gi|544346333|ref|NP_001269712|]
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mitochondrial tRNA-specific 2-thiouridylase 1 isoform e [Homo sapiens]

Protein Classification

adenine nucleotide alpha hydrolase family protein( domain architecture ID 188)

AANH (adenine nucleotide alpha hydrolase) family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AANH_superfamily super family cl00292
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase ...
37-243 9.37e-88

Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase (AANH) superfamily includes N-type ATP PPases, ATP sulfurylases, universal stress response proteins (USPs), and electron transfer flavoproteins (ETFs). The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.


The actual alignment was detected with superfamily member cd01998:

Pssm-ID: 469708 [Multi-domain]  Cd Length: 349  Bit Score: 265.14  E-value: 9.37e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346333  37 LEMVSQDALRRTIFPLGGLTKEFVKKIAAENRLHhVLQKKESMGMCFIGKRNFEHFLLQYLQPR-PGHFISIeDNKVLGT 115
Cdd:cd01998  150 LSRLSQEQLSRTLFPLGHLTKSEVREIAREAGLP-VAEKKDSQGICFIGKRDFRDFLKEYLPEKlPGPIVDI-DGKVLGE 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346333 116 HKGWFLYTLGQRANIG-GLREPWYVVEKDSVKGDVFVAPrtDHPALYRDLLRTSRVHWIAEEPPaalvrDKMMECHFRFR 194
Cdd:cd01998  228 HKGLWFYTIGQRKGLGiAAGEPLYVVKKDPEKNIVVVGP--GHPALFSDTLRASDLNWISPEPP-----LEPLECEAKIR 300
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 544346333 195 HQMALVPCVLTLNQDGTVWVTAVQAVRALATGQFAVFYKGDECLGSGKI 243
Cdd:cd01998  301 YRQPPVPCTVTPLDDGRLKVEFDEPQRAVTPGQAAVFYDGDEVLGGGII 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 ...
37-243 9.37e-88

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: 265.14  E-value: 9.37e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346333  37 LEMVSQDALRRTIFPLGGLTKEFVKKIAAENRLHhVLQKKESMGMCFIGKRNFEHFLLQYLQPR-PGHFISIeDNKVLGT 115
Cdd:cd01998  150 LSRLSQEQLSRTLFPLGHLTKSEVREIAREAGLP-VAEKKDSQGICFIGKRDFRDFLKEYLPEKlPGPIVDI-DGKVLGE 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346333 116 HKGWFLYTLGQRANIG-GLREPWYVVEKDSVKGDVFVAPrtDHPALYRDLLRTSRVHWIAEEPPaalvrDKMMECHFRFR 194
Cdd:cd01998  228 HKGLWFYTIGQRKGLGiAAGEPLYVVKKDPEKNIVVVGP--GHPALFSDTLRASDLNWISPEPP-----LEPLECEAKIR 300
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 544346333 195 HQMALVPCVLTLNQDGTVWVTAVQAVRALATGQFAVFYKGDECLGSGKI 243
Cdd:cd01998  301 YRQPPVPCTVTPLDDGRLKVEFDEPQRAVTPGQAAVFYDGDEVLGGGII 349
MnmA COG0482
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ...
39-245 8.24e-74

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: 229.56  E-value: 8.24e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346333  39 MVSQDALRRTIFPLGGLTKEFVKKIAAENRLHhVLQKKESMGMCFIGKRNFEHFLLQYLQPRPGHFISIeDNKVLGTHKG 118
Cdd:COG0482  153 RLTQEQLSKTLFPLGELTKPEVREIAEELGLP-VADKKDSQGICFIGDGDYRDFLERYLPEKPGDIVDL-DGKVLGEHDG 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346333 119 WFLYTLGQRANIG-GLREPWYVVEKDSVKGDVFVAPRTDhpaLYRDLLRTSRVHWIAEEPPAalvrdKMMECHFRFRHQM 197
Cdd:COG0482  231 LHYYTIGQRKGLGiGGGEPLYVVGKDPETNTVIVGQGEA---LYSRELTAEDVNWISGEPPE-----EPLRCTAKIRYRQ 302
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 544346333 198 ALVPCVLTLNQDGTVWVTAVQAVRALATGQFAVFYKGDECLGSGKILR 245
Cdd:COG0482  303 PPVPATLTPLEDGRVRVEFDEPQRAVTPGQSAVFYDGDRVLGGGIIER 350
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
37-243 1.10e-71

tRNA-specific 2-thiouridylase MnmA; Reviewed


Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 223.79  E-value: 1.10e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346333  37 LEMVSQDALRRTIFPLGGLTKEFVKKIAAENRLHhVLQKKESMGMCFIGKRNFEHFLLQYLQPRPGHFISIeDNKVLGTH 116
Cdd:PRK00143 148 LYQLTQEQLAKLLFPLGELTKPEVREIAEEAGLP-VAKKKDSQGICFIGERDYRDFLKRYLPAQPGEIVDL-DGKVLGEH 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346333 117 KGWFLYTLGQRA--NIGGLREPWYVVEKDSVKGDVFVAPRtdhPALYRDLLRTSRVHWIAEEPPAalvrdKMMECHFRFR 194
Cdd:PRK00143 226 KGLMYYTIGQRKglGIGGDGEPWYVVGKDPETNTVVVGQG---EALYSRELIASDLNWVGGEPPE-----EPFECTAKIR 297
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 544346333 195 HQMALVPCVLTLnQDGTVWVTAVQAVRALATGQFAVFYKGDECLGSGKI 243
Cdd:PRK00143 298 YRQKPVPATVEL-EDDRVEVEFDEPQRAVTPGQAAVFYDGDRVLGGGII 345
trmU TIGR00420
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ...
37-243 6.02e-59

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: 191.45  E-value: 6.02e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346333   37 LEMVSQDALRRTIFPLGGLTKEFVKKIAAENRLHhVLQKKESMGMCFIGKRNFEHFLLQYLQPRPGHFISIEDNKVLGTH 116
Cdd:TIGR00420 152 LYHLSHEQLAKLLFPLGELLKPEVRQIAKNAGLP-TAEKKDSQGICFIGERKFRDFLKKYLPVKPGVIITVDGQSVIGEH 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346333  117 KGWFLYTLGQRA--NIGGLREPWYVVEKDSVKGDVFVAprTDHPALYRDLLRTSRVHWIAEEPpaalvRDKMMECHFRFR 194
Cdd:TIGR00420 231 DGLWFYTIGQRKglGIGGAAEPWFVVEKDLETNELVVS--HGKPDLASRGLLAQQFHWLDDEP-----NPFEMRCTVKIR 303
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 544346333  195 HQMALVPCVLTLNQDGTVWVTAVQAVRALATGQFAVFYKGDECLGSGKI 243
Cdd:TIGR00420 304 YRQVPVQCKLKLLDDNLIEVIFDEPQAGVTPGQSAVLYKGDICLGGGII 352
tRNA_Me_trans_C pfam20258
Aminomethyltransferase beta-barrel domain; This domain is found at the C-terminus of tRNA ...
162-243 1.91e-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: 114.29  E-value: 1.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346333  162 RDLLRTSRVHWIAEEPPaalvrDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAVQAVRALATGQFAVFYKGDECLGSG 241
Cdd:pfam20258   1 SDGLRAKDPNWLGDKPP-----TEPLECTVKVRHRQPPVPCVVELIDDETVEVHFDEPVRAVTPGQAAVFYDGDRCLGGG 75

                  ..
gi 544346333  242 KI 243
Cdd:pfam20258  76 II 77
 
Name Accession Description Interval E-value
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
37-243 9.37e-88

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: 265.14  E-value: 9.37e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346333  37 LEMVSQDALRRTIFPLGGLTKEFVKKIAAENRLHhVLQKKESMGMCFIGKRNFEHFLLQYLQPR-PGHFISIeDNKVLGT 115
Cdd:cd01998  150 LSRLSQEQLSRTLFPLGHLTKSEVREIAREAGLP-VAEKKDSQGICFIGKRDFRDFLKEYLPEKlPGPIVDI-DGKVLGE 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346333 116 HKGWFLYTLGQRANIG-GLREPWYVVEKDSVKGDVFVAPrtDHPALYRDLLRTSRVHWIAEEPPaalvrDKMMECHFRFR 194
Cdd:cd01998  228 HKGLWFYTIGQRKGLGiAAGEPLYVVKKDPEKNIVVVGP--GHPALFSDTLRASDLNWISPEPP-----LEPLECEAKIR 300
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 544346333 195 HQMALVPCVLTLNQDGTVWVTAVQAVRALATGQFAVFYKGDECLGSGKI 243
Cdd:cd01998  301 YRQPPVPCTVTPLDDGRLKVEFDEPQRAVTPGQAAVFYDGDEVLGGGII 349
MnmA COG0482
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ...
39-245 8.24e-74

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: 229.56  E-value: 8.24e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346333  39 MVSQDALRRTIFPLGGLTKEFVKKIAAENRLHhVLQKKESMGMCFIGKRNFEHFLLQYLQPRPGHFISIeDNKVLGTHKG 118
Cdd:COG0482  153 RLTQEQLSKTLFPLGELTKPEVREIAEELGLP-VADKKDSQGICFIGDGDYRDFLERYLPEKPGDIVDL-DGKVLGEHDG 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346333 119 WFLYTLGQRANIG-GLREPWYVVEKDSVKGDVFVAPRTDhpaLYRDLLRTSRVHWIAEEPPAalvrdKMMECHFRFRHQM 197
Cdd:COG0482  231 LHYYTIGQRKGLGiGGGEPLYVVGKDPETNTVIVGQGEA---LYSRELTAEDVNWISGEPPE-----EPLRCTAKIRYRQ 302
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 544346333 198 ALVPCVLTLNQDGTVWVTAVQAVRALATGQFAVFYKGDECLGSGKILR 245
Cdd:COG0482  303 PPVPATLTPLEDGRVRVEFDEPQRAVTPGQSAVFYDGDRVLGGGIIER 350
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
37-243 1.10e-71

tRNA-specific 2-thiouridylase MnmA; Reviewed


Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 223.79  E-value: 1.10e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346333  37 LEMVSQDALRRTIFPLGGLTKEFVKKIAAENRLHhVLQKKESMGMCFIGKRNFEHFLLQYLQPRPGHFISIeDNKVLGTH 116
Cdd:PRK00143 148 LYQLTQEQLAKLLFPLGELTKPEVREIAEEAGLP-VAKKKDSQGICFIGERDYRDFLKRYLPAQPGEIVDL-DGKVLGEH 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346333 117 KGWFLYTLGQRA--NIGGLREPWYVVEKDSVKGDVFVAPRtdhPALYRDLLRTSRVHWIAEEPPAalvrdKMMECHFRFR 194
Cdd:PRK00143 226 KGLMYYTIGQRKglGIGGDGEPWYVVGKDPETNTVVVGQG---EALYSRELIASDLNWVGGEPPE-----EPFECTAKIR 297
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 544346333 195 HQMALVPCVLTLnQDGTVWVTAVQAVRALATGQFAVFYKGDECLGSGKI 243
Cdd:PRK00143 298 YRQKPVPATVEL-EDDRVEVEFDEPQRAVTPGQAAVFYDGDRVLGGGII 345
trmU TIGR00420
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ...
37-243 6.02e-59

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: 191.45  E-value: 6.02e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346333   37 LEMVSQDALRRTIFPLGGLTKEFVKKIAAENRLHhVLQKKESMGMCFIGKRNFEHFLLQYLQPRPGHFISIEDNKVLGTH 116
Cdd:TIGR00420 152 LYHLSHEQLAKLLFPLGELLKPEVRQIAKNAGLP-TAEKKDSQGICFIGERKFRDFLKKYLPVKPGVIITVDGQSVIGEH 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346333  117 KGWFLYTLGQRA--NIGGLREPWYVVEKDSVKGDVFVAprTDHPALYRDLLRTSRVHWIAEEPpaalvRDKMMECHFRFR 194
Cdd:TIGR00420 231 DGLWFYTIGQRKglGIGGAAEPWFVVEKDLETNELVVS--HGKPDLASRGLLAQQFHWLDDEP-----NPFEMRCTVKIR 303
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 544346333  195 HQMALVPCVLTLNQDGTVWVTAVQAVRALATGQFAVFYKGDECLGSGKI 243
Cdd:TIGR00420 304 YRQVPVQCKLKLLDDNLIEVIFDEPQAGVTPGQSAVLYKGDICLGGGII 352
tRNA_Me_trans_C pfam20258
Aminomethyltransferase beta-barrel domain; This domain is found at the C-terminus of tRNA ...
162-243 1.91e-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: 114.29  E-value: 1.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346333  162 RDLLRTSRVHWIAEEPPaalvrDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAVQAVRALATGQFAVFYKGDECLGSG 241
Cdd:pfam20258   1 SDGLRAKDPNWLGDKPP-----TEPLECTVKVRHRQPPVPCVVELIDDETVEVHFDEPVRAVTPGQAAVFYDGDRCLGGG 75

                  ..
gi 544346333  242 KI 243
Cdd:pfam20258  76 II 77
tRNA_Me_trans_M pfam20259
tRNA methyl transferase PRC-barrel domain; This family represents a central PRC-barrel domain ...
90-153 1.57e-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: 98.45  E-value: 1.57e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544346333   90 EHFLLQYLQPRPGHFISIEDNKVLGTHKGWFLYTLGQR--ANIGGLREPWYVVEKDSVKGDVFVAP 153
Cdd:pfam20259   1 KDFLKEYLPVKPGDIIDIDTGEVLGEHEGIWFYTIGQRkgLGIGGYGEPWYVVEKDPKKNTVYVGR 66
PRK14664 PRK14664
tRNA-specific 2-thiouridylase MnmA; Provisional
42-243 1.39e-20

tRNA-specific 2-thiouridylase MnmA; Provisional


Pssm-ID: 173127 [Multi-domain]  Cd Length: 362  Bit Score: 90.01  E-value: 1.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346333  42 QDALRRTIFPLGGLTKEFVKKIAAENRLHHVLQKKESMGMCFIgKRNFEHFLLQY-----LQPRPGHFISIEDNKvLGTH 116
Cdd:PRK14664 148 QDILRRCIFPLGNYTKQTVREYLREKGYEAKSKEGESMEVCFI-KGDYRDFLREQcpeldTEVGPGWFVNSEGVK-LGQH 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346333 117 KGWFLYTLGQRANIG-GLREPWYVVEKDSVKGDVFVAprtDHPALYRDLLRTSRVHwIAEEppaalvrDKMMECH---FR 192
Cdd:PRK14664 226 KGFPYYTIGQRKGLEiALGKPAYVLKINPQKNTVMLG---DAEQLKAEYMLAEQDN-IVDE-------QELFACPdlaVR 294
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 544346333 193 FRHQMALVPCVLTLNQDGTVWVTAVQAVRALATGQFAVFYKGDECLGSGKI 243
Cdd:PRK14664 295 IRYRSRPIPCRVKRLEDGRLLVRFLAEASAIAPGQSAVFYEGRRVLGGAFI 345
mnmA PRK14665
tRNA-specific 2-thiouridylase MnmA; Provisional
42-244 2.49e-20

tRNA-specific 2-thiouridylase MnmA; Provisional


Pssm-ID: 173128 [Multi-domain]  Cd Length: 360  Bit Score: 89.22  E-value: 2.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346333  42 QDALRRTIFPLGGLTKEFVKKIAAENRLHHVLQKKESMGMCF--IGKRNFEHFLL----------QYLQPRPGHFISiED 109
Cdd:PRK14665 153 QEILQRMLLPMGGMTKSEARAYAAERGFEKVAKKRDSLGVCFcpMDYRSFLKKCLcdesgdknrnIYRKVERGRFLD-ES 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346333 110 NKVLGTHKGWFLYTLGQRANIG-GLREPWYVVEKDSVKGDVFVAprtDHPALYRDLLRTSrvHWIAEEPPAALVRDKMMe 188
Cdd:PRK14665 232 GNFIAWHEGYPFYTIGQRRGLGiQLNRAVFVKEIHPETNEVVLA---SLKALEKTEMWLK--DWNIVNESRLLGCDDII- 305
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 544346333 189 CHFRFRHQMAlvPCVLTLNQDGTVWVTAVQAVRALATGQFAVFYKGDECLGSGKIL 244
Cdd:PRK14665 306 VKIRYRKQEN--HCTVTITPDNLLHVQLHEPLTAIAEGQAAAFYKDGLLLGGGIIT 359
tRNA_Me_trans pfam03054
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ...
40-86 5.42e-17

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: 77.29  E-value: 5.42e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 544346333   40 VSQDALRRTIFPLGGLTKEFVKKIAAENRLhHVLQKKESMGMCFIGK 86
Cdd:pfam03054 157 LSQEQLEKLLFPLGELTKEEVRKIAKEAGL-ATAKKKDSQGICFIGK 202
 
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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