|
Name |
Accession |
Description |
Interval |
E-value |
| mnmA |
PRK00143 |
tRNA-specific 2-thiouridylase MnmA; Reviewed |
1-358 |
4.32e-178 |
|
tRNA-specific 2-thiouridylase MnmA; Reviewed
Pssm-ID: 234664 [Multi-domain] Cd Length: 346 Bit Score: 498.06 E-value: 4.32e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 1 MRVLAAMSGGVDSAVAAARAVEAGHDVVGVHLALSRMPGTLRTGarGCCTIEDSMDAQRAATLLGIPYYVWDFSERFKSD 80
Cdd:PRK00143 1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVFMKLWDDDDETGKG--GCCAEEDIADARRVADKLGIPHYVVDFEKEFWDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 81 VVEDFISEYQAGRTPNPCMRCNEKIKFAALMEKALALGFDAVCTGHYANVVPDAhgnlELHRASAWAKDQSYVLGVLTSE 160
Cdd:PRK00143 79 VIDYFLDEYKAGRTPNPCVLCNKEIKFKAFLEYARELGADYIATGHYARIRDGR----ELLRGVDPNKDQSYFLYQLTQE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 161 QLAHAMFPLGDTPsKDLIRAEAAQRGLSVAQKPDSHDICFIPDGDTRGWLADKVGISEGDIVDTEGNKLGTHEGTPGFTI 240
Cdd:PRK00143 155 QLAKLLFPLGELT-KPEVREIAEEAGLPVAKKKDSQGICFIGERDYRDFLKRYLPAQPGEIVDLDGKVLGEHKGLMYYTI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 241 GQRKGLHIGTpapDGQPRFVLEIRPKTNTVVVGPREALDITEIAGTSYTWCGqaQENPETAFDVDVQIRAHADPVPAIAQ 320
Cdd:PRK00143 234 GQRKGLGIGG---DGEPWYVVGKDPETNTVVVGQGEALYSRELIASDLNWVG--GEPPEEPFECTAKIRYRQKPVPATVE 308
|
330 340 350
....*....|....*....|....*....|....*...
gi 1431816623 321 LVGDELVVRPTTPLNSVAAGQTAVIYVGTRVLGQFTIS 358
Cdd:PRK00143 309 LEDDRVEVEFDEPQRAVTPGQAAVFYDGDRVLGGGIIE 346
|
|
| MnmA |
COG0482 |
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ... |
1-362 |
1.21e-175 |
|
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: 492.26 E-value: 1.21e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 1 MRVLAAMSGGVDSAVAAARAVEAGHDVVGVHLALSRMPGTlrTGARGCCTIEDSMDAQRAATLLGIPYYVWDFSERFKSD 80
Cdd:COG0482 1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVTMKLWDDDDA--SGSGGCCSLEDIEDARRVADKLGIPHYVVDFEEEFKDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 81 VVEDFISEYQAGRTPNPCMRCNEKIKFAALMEKALALGFDAVCTGHYANVVpDAHGNLELHRASAWAKDQSYVLGVLTSE 160
Cdd:COG0482 79 VIDYFLDEYLAGRTPNPCVLCNREIKFGALLEKALELGADYIATGHYARVE-EKDGRYELLRGVDPNKDQSYFLYRLTQE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 161 QLAHAMFPLGDTPsKDLIRAEAAQRGLSVAQKPDSHDICFIPDGDTRGWLADKVGISEGDIVDTEGNKLGTHEGTPGFTI 240
Cdd:COG0482 158 QLSKTLFPLGELT-KPEVREIAEELGLPVADKKDSQGICFIGDGDYRDFLERYLPEKPGDIVDLDGKVLGEHDGLHYYTI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 241 GQRKGLHIGTpapdGQPRFVLEIRPKTNTVVVGPREALDITEIAGTSYTWCGqaQENPETAFDVDVQIRAHADPVPA-IA 319
Cdd:COG0482 237 GQRKGLGIGG----GEPLYVVGKDPETNTVIVGQGEALYSRELTAEDVNWIS--GEPPEEPLRCTAKIRYRQPPVPAtLT 310
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1431816623 320 QLVGDELVVRPTTPLNSVAAGQTAVIYVGTRVLGQFTISRTVS 362
Cdd:COG0482 311 PLEDGRVRVEFDEPQRAVTPGQSAVFYDGDRVLGGGIIERTER 353
|
|
| MnmA_TRMU-like |
cd01998 |
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ... |
2-353 |
5.29e-138 |
|
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: 396.88 E-value: 5.29e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 2 RVLAAMSGGVDSAVAAARAVEAGHDVVGVHLALSRmpgTLRTGARGCCTIEDSMDAQRAATLLGIPYYVWDFSERFKSDV 81
Cdd:cd01998 1 KVAVAMSGGVDSSVAAALLKEQGYDVIGVFMKNWD---DEDNEKGGCCSEEDIEDARRVADQLGIPLYVVDFSEEYWERV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 82 VEDFISEYQAGRTPNPCMRCNEKIKFAALMEKALALGFDAVCTGHYANVVPDAHGNLELHRASAWAKDQSYVLGVLTSEQ 161
Cdd:cd01998 78 FDPFLEEYKAGRTPNPDVLCNREIKFGALLDAAKKLGADYIATGHYARIEEDNRGRYRLLRAVDPNKDQSYFLSRLSQEQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 162 LAHAMFPLGDTPSKDlIRAEAAQRGLSVAQKPDSHDICFIPDGDTRGWLADKVG-ISEGDIVDTEGNKLGTHEGTPGFTI 240
Cdd:cd01998 158 LSRTLFPLGHLTKSE-VREIAREAGLPVAEKKDSQGICFIGKRDFRDFLKEYLPeKLPGPIVDIDGKVLGEHKGLWFYTI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 241 GQRKGLHIGTpapdGQPRFVLEIRPKTNTVVVGP-REALDITEIAGTSYTWCGqaQENPETAFDVDVQIRAHADPVPAIA 319
Cdd:cd01998 237 GQRKGLGIAA----GEPLYVVKKDPEKNIVVVGPgHPALFSDTLRASDLNWIS--PEPPLEPLECEAKIRYRQPPVPCTV 310
|
330 340 350
....*....|....*....|....*....|....*
gi 1431816623 320 QLVGDE-LVVRPTTPLNSVAAGQTAVIYVGTRVLG 353
Cdd:cd01998 311 TPLDDGrLKVEFDEPQRAVTPGQAAVFYDGDEVLG 345
|
|
| tRNA_Me_trans |
pfam03054 |
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ... |
1-203 |
1.24e-95 |
|
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: 283.37 E-value: 1.24e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 1 MRVLAAMSGGVDSAVAAARAVEAGHDVVGVHLALSRMPGTLRTGARgCCTIEDSMDAQRAATLLGIPYYVWDFSERFKSD 80
Cdd:pfam03054 1 MKVVVAMSGGVDSSVAAYLLKEQGHNVIGVFMKNWDEEQSLDEEGK-CCSEEDLADAQRVCEQLGIPLYVVNFEKEYWED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 81 VVEDFISEYQAGRTPNPCMRCNEKIKFAALMEKALA-LGFDAVCTGHYANVVPDAHGNLELHRASAWAKDQSYVLGVLTS 159
Cdd:pfam03054 80 VFEPFLDEYKNGRTPNPDVLCNKEIKFGALLDYALEnLGADYVATGHYARVSLNKDGGSELLRALDKNKDQSYFLSTLSQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1431816623 160 EQLAHAMFPLGDTPsKDLIRAEAAQRGLSVAQKPDSHDICFIPD 203
Cdd:pfam03054 160 EQLEKLLFPLGELT-KEEVRKIAKEAGLATAKKKDSQGICFIGK 202
|
|
| trmU |
TIGR00420 |
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ... |
1-353 |
3.25e-83 |
|
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: 257.31 E-value: 3.25e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 1 MRVLAAMSGGVDSAVAAARAVEAGHDVVGVHLALSRMpgTLRTGARGCCTIEDSMDAQRAATLLGIPYYVWDFSERFKSD 80
Cdd:TIGR00420 1 KKVIVGLSGGVDSSVSAYLLKQQGYEVVGVFMKNWEE--DDKNDGHGCTSAEDLRDAQAICEKLGIPLEKVNFQKEYWNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 81 VVEDFISEYQAGRTPNPCMRCNEKIKFAALMEKAL-ALGFDAVCTGHYANVVPDaHGNLELHRASAWAKDQSYVLGVLTS 159
Cdd:TIGR00420 79 VFEPFIQEYKEGRTPNPDILCNKFIKFGAFLEYAAeLLGNDKIATGHYARIAEI-EGKSLLLRALDKNKDQSYFLYHLSH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 160 EQLAHAMFPLGDTpSKDLIRAEAAQRGLSVAQKPDSHDICFIPDGDTRGWLADKVGISEGDIVDTEGNK-LGTHEGTPGF 238
Cdd:TIGR00420 158 EQLAKLLFPLGEL-LKPEVRQIAKNAGLPTAEKKDSQGICFIGERKFRDFLKKYLPVKPGVIITVDGQSvIGEHDGLWFY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 239 TIGQRKGLHIGTPApdgQPRFVLEIRPKTNTVVVG-PREALDITEIAGTSYTWCGQAQENPETAFdvDVQIRAHADPVPA 317
Cdd:TIGR00420 237 TIGQRKGLGIGGAA---EPWFVVEKDLETNELVVShGKPDLASRGLLAQQFHWLDDEPNPFEMRC--TVKIRYRQVPVQC 311
|
330 340 350
....*....|....*....|....*....|....*..
gi 1431816623 318 IAQLVGDELV-VRPTTPLNSVAAGQTAVIYVGTRVLG 353
Cdd:TIGR00420 312 KLKLLDDNLIeVIFDEPQAGVTPGQSAVLYKGDICLG 348
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| mnmA |
PRK00143 |
tRNA-specific 2-thiouridylase MnmA; Reviewed |
1-358 |
4.32e-178 |
|
tRNA-specific 2-thiouridylase MnmA; Reviewed
Pssm-ID: 234664 [Multi-domain] Cd Length: 346 Bit Score: 498.06 E-value: 4.32e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 1 MRVLAAMSGGVDSAVAAARAVEAGHDVVGVHLALSRMPGTLRTGarGCCTIEDSMDAQRAATLLGIPYYVWDFSERFKSD 80
Cdd:PRK00143 1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVFMKLWDDDDETGKG--GCCAEEDIADARRVADKLGIPHYVVDFEKEFWDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 81 VVEDFISEYQAGRTPNPCMRCNEKIKFAALMEKALALGFDAVCTGHYANVVPDAhgnlELHRASAWAKDQSYVLGVLTSE 160
Cdd:PRK00143 79 VIDYFLDEYKAGRTPNPCVLCNKEIKFKAFLEYARELGADYIATGHYARIRDGR----ELLRGVDPNKDQSYFLYQLTQE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 161 QLAHAMFPLGDTPsKDLIRAEAAQRGLSVAQKPDSHDICFIPDGDTRGWLADKVGISEGDIVDTEGNKLGTHEGTPGFTI 240
Cdd:PRK00143 155 QLAKLLFPLGELT-KPEVREIAEEAGLPVAKKKDSQGICFIGERDYRDFLKRYLPAQPGEIVDLDGKVLGEHKGLMYYTI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 241 GQRKGLHIGTpapDGQPRFVLEIRPKTNTVVVGPREALDITEIAGTSYTWCGqaQENPETAFDVDVQIRAHADPVPAIAQ 320
Cdd:PRK00143 234 GQRKGLGIGG---DGEPWYVVGKDPETNTVVVGQGEALYSRELIASDLNWVG--GEPPEEPFECTAKIRYRQKPVPATVE 308
|
330 340 350
....*....|....*....|....*....|....*...
gi 1431816623 321 LVGDELVVRPTTPLNSVAAGQTAVIYVGTRVLGQFTIS 358
Cdd:PRK00143 309 LEDDRVEVEFDEPQRAVTPGQAAVFYDGDRVLGGGIIE 346
|
|
| MnmA |
COG0482 |
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ... |
1-362 |
1.21e-175 |
|
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: 492.26 E-value: 1.21e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 1 MRVLAAMSGGVDSAVAAARAVEAGHDVVGVHLALSRMPGTlrTGARGCCTIEDSMDAQRAATLLGIPYYVWDFSERFKSD 80
Cdd:COG0482 1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVTMKLWDDDDA--SGSGGCCSLEDIEDARRVADKLGIPHYVVDFEEEFKDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 81 VVEDFISEYQAGRTPNPCMRCNEKIKFAALMEKALALGFDAVCTGHYANVVpDAHGNLELHRASAWAKDQSYVLGVLTSE 160
Cdd:COG0482 79 VIDYFLDEYLAGRTPNPCVLCNREIKFGALLEKALELGADYIATGHYARVE-EKDGRYELLRGVDPNKDQSYFLYRLTQE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 161 QLAHAMFPLGDTPsKDLIRAEAAQRGLSVAQKPDSHDICFIPDGDTRGWLADKVGISEGDIVDTEGNKLGTHEGTPGFTI 240
Cdd:COG0482 158 QLSKTLFPLGELT-KPEVREIAEELGLPVADKKDSQGICFIGDGDYRDFLERYLPEKPGDIVDLDGKVLGEHDGLHYYTI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 241 GQRKGLHIGTpapdGQPRFVLEIRPKTNTVVVGPREALDITEIAGTSYTWCGqaQENPETAFDVDVQIRAHADPVPA-IA 319
Cdd:COG0482 237 GQRKGLGIGG----GEPLYVVGKDPETNTVIVGQGEALYSRELTAEDVNWIS--GEPPEEPLRCTAKIRYRQPPVPAtLT 310
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1431816623 320 QLVGDELVVRPTTPLNSVAAGQTAVIYVGTRVLGQFTISRTVS 362
Cdd:COG0482 311 PLEDGRVRVEFDEPQRAVTPGQSAVFYDGDRVLGGGIIERTER 353
|
|
| MnmA_TRMU-like |
cd01998 |
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ... |
2-353 |
5.29e-138 |
|
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: 396.88 E-value: 5.29e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 2 RVLAAMSGGVDSAVAAARAVEAGHDVVGVHLALSRmpgTLRTGARGCCTIEDSMDAQRAATLLGIPYYVWDFSERFKSDV 81
Cdd:cd01998 1 KVAVAMSGGVDSSVAAALLKEQGYDVIGVFMKNWD---DEDNEKGGCCSEEDIEDARRVADQLGIPLYVVDFSEEYWERV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 82 VEDFISEYQAGRTPNPCMRCNEKIKFAALMEKALALGFDAVCTGHYANVVPDAHGNLELHRASAWAKDQSYVLGVLTSEQ 161
Cdd:cd01998 78 FDPFLEEYKAGRTPNPDVLCNREIKFGALLDAAKKLGADYIATGHYARIEEDNRGRYRLLRAVDPNKDQSYFLSRLSQEQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 162 LAHAMFPLGDTPSKDlIRAEAAQRGLSVAQKPDSHDICFIPDGDTRGWLADKVG-ISEGDIVDTEGNKLGTHEGTPGFTI 240
Cdd:cd01998 158 LSRTLFPLGHLTKSE-VREIAREAGLPVAEKKDSQGICFIGKRDFRDFLKEYLPeKLPGPIVDIDGKVLGEHKGLWFYTI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 241 GQRKGLHIGTpapdGQPRFVLEIRPKTNTVVVGP-REALDITEIAGTSYTWCGqaQENPETAFDVDVQIRAHADPVPAIA 319
Cdd:cd01998 237 GQRKGLGIAA----GEPLYVVKKDPEKNIVVVGPgHPALFSDTLRASDLNWIS--PEPPLEPLECEAKIRYRQPPVPCTV 310
|
330 340 350
....*....|....*....|....*....|....*
gi 1431816623 320 QLVGDE-LVVRPTTPLNSVAAGQTAVIYVGTRVLG 353
Cdd:cd01998 311 TPLDDGrLKVEFDEPQRAVTPGQAAVFYDGDEVLG 345
|
|
| tRNA_Me_trans |
pfam03054 |
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ... |
1-203 |
1.24e-95 |
|
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: 283.37 E-value: 1.24e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 1 MRVLAAMSGGVDSAVAAARAVEAGHDVVGVHLALSRMPGTLRTGARgCCTIEDSMDAQRAATLLGIPYYVWDFSERFKSD 80
Cdd:pfam03054 1 MKVVVAMSGGVDSSVAAYLLKEQGHNVIGVFMKNWDEEQSLDEEGK-CCSEEDLADAQRVCEQLGIPLYVVNFEKEYWED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 81 VVEDFISEYQAGRTPNPCMRCNEKIKFAALMEKALA-LGFDAVCTGHYANVVPDAHGNLELHRASAWAKDQSYVLGVLTS 159
Cdd:pfam03054 80 VFEPFLDEYKNGRTPNPDVLCNKEIKFGALLDYALEnLGADYVATGHYARVSLNKDGGSELLRALDKNKDQSYFLSTLSQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1431816623 160 EQLAHAMFPLGDTPsKDLIRAEAAQRGLSVAQKPDSHDICFIPD 203
Cdd:pfam03054 160 EQLEKLLFPLGELT-KEEVRKIAKEAGLATAKKKDSQGICFIGK 202
|
|
| trmU |
TIGR00420 |
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ... |
1-353 |
3.25e-83 |
|
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: 257.31 E-value: 3.25e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 1 MRVLAAMSGGVDSAVAAARAVEAGHDVVGVHLALSRMpgTLRTGARGCCTIEDSMDAQRAATLLGIPYYVWDFSERFKSD 80
Cdd:TIGR00420 1 KKVIVGLSGGVDSSVSAYLLKQQGYEVVGVFMKNWEE--DDKNDGHGCTSAEDLRDAQAICEKLGIPLEKVNFQKEYWNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 81 VVEDFISEYQAGRTPNPCMRCNEKIKFAALMEKAL-ALGFDAVCTGHYANVVPDaHGNLELHRASAWAKDQSYVLGVLTS 159
Cdd:TIGR00420 79 VFEPFIQEYKEGRTPNPDILCNKFIKFGAFLEYAAeLLGNDKIATGHYARIAEI-EGKSLLLRALDKNKDQSYFLYHLSH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 160 EQLAHAMFPLGDTpSKDLIRAEAAQRGLSVAQKPDSHDICFIPDGDTRGWLADKVGISEGDIVDTEGNK-LGTHEGTPGF 238
Cdd:TIGR00420 158 EQLAKLLFPLGEL-LKPEVRQIAKNAGLPTAEKKDSQGICFIGERKFRDFLKKYLPVKPGVIITVDGQSvIGEHDGLWFY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 239 TIGQRKGLHIGTPApdgQPRFVLEIRPKTNTVVVG-PREALDITEIAGTSYTWCGQAQENPETAFdvDVQIRAHADPVPA 317
Cdd:TIGR00420 237 TIGQRKGLGIGGAA---EPWFVVEKDLETNELVVShGKPDLASRGLLAQQFHWLDDEPNPFEMRC--TVKIRYRQVPVQC 311
|
330 340 350
....*....|....*....|....*....|....*..
gi 1431816623 318 IAQLVGDELV-VRPTTPLNSVAAGQTAVIYVGTRVLG 353
Cdd:TIGR00420 312 KLKLLDDNLIeVIFDEPQAGVTPGQSAVLYKGDICLG 348
|
|
| PRK14664 |
PRK14664 |
tRNA-specific 2-thiouridylase MnmA; Provisional |
2-353 |
8.71e-64 |
|
tRNA-specific 2-thiouridylase MnmA; Provisional
Pssm-ID: 173127 [Multi-domain] Cd Length: 362 Bit Score: 207.50 E-value: 8.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 2 RVLAAMSGGVDSAVAAARAVEAGHDVVGVhlalsrmpgTLRTGArgcctiEDSMDAQRAATLLGIPYYVWDFSERFKSDV 81
Cdd:PRK14664 7 RVLVGMSGGIDSTATCLMLQEQGYEIVGV---------TMRVWG------DEPQDARELAARMGIEHYVADERVPFKDTI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 82 VEDFISEYQAGRTPNPCMRCNEKIKFAALMEKALALGFDAVCTGHYANvVPDAHGNLELHRASAWAKDQSYVLGVLTSEQ 161
Cdd:PRK14664 72 VKNFIDEYRQGRTPNPCVMCNPLFKFRMLIEWADKLGCAWIATGHYSR-LEERNGHIYIVAGDDDKKDQSYFLWRLGQDI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 162 LAHAMFPLGDTpSKDLIRAEAAQRGLSV-AQKPDSHDICFIpDGDTRGWLADK-----VGISEGDIVDTEGNKLGTHEGT 235
Cdd:PRK14664 151 LRRCIFPLGNY-TKQTVREYLREKGYEAkSKEGESMEVCFI-KGDYRDFLREQcpeldTEVGPGWFVNSEGVKLGQHKGF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 236 PGFTIGQRKGLHIGTpapdGQPRFVLEIRPKTNTVVVGPREALDiteiagTSYTWCGQAQENPETAF----DVDVQIRAH 311
Cdd:PRK14664 229 PYYTIGQRKGLEIAL----GKPAYVLKINPQKNTVMLGDAEQLK------AEYMLAEQDNIVDEQELfacpDLAVRIRYR 298
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1431816623 312 ADPVPAIAQLVGD-ELVVRPTTPLNSVAAGQTAVIYVGTRVLG 353
Cdd:PRK14664 299 SRPIPCRVKRLEDgRLLVRFLAEASAIAPGQSAVFYEGRRVLG 341
|
|
| mnmA |
PRK14665 |
tRNA-specific 2-thiouridylase MnmA; Provisional |
2-353 |
7.29e-47 |
|
tRNA-specific 2-thiouridylase MnmA; Provisional
Pssm-ID: 173128 [Multi-domain] Cd Length: 360 Bit Score: 163.18 E-value: 7.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 2 RVLAAMSGGVDSAVAAARAVEAGHDVVGVHLALSRMPGTlrtgargcctIEDSMDAQRAATLLGIPYYVWDFSERFKSDV 81
Cdd:PRK14665 7 RVLLGMSGGTDSSVAAMLLLEAGYEVTGVTFRFYEFNGS----------TEYLEDARALAERLGIGHITYDARKVFRKQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 82 VEDFISEYQAGRTPNPCMRCNEKIKFAALMEKALALGFDAVCTGHYANVVpDAHGNLELHRASAWAKDQSYVLGVLTSEQ 161
Cdd:PRK14665 77 IDYFIDEYMSGHTPVPCTLCNNYLKWPLLAKIADEMGIFYLATGHYVRKQ-WIDGNYYITPAEDVDKDQSFFLWGLRQEI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 162 LAHAMFPLGDTpSKDLIRAEAAQRG-LSVAQKPDSHDICFIPdGDTRG----WLADKVG---------ISEGDIVDTEGN 227
Cdd:PRK14665 156 LQRMLLPMGGM-TKSEARAYAAERGfEKVAKKRDSLGVCFCP-MDYRSflkkCLCDESGdknrniyrkVERGRFLDESGN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 228 KLGTHEGTPGFTIGQRKGLHIGTpapdGQPRFVLEIRPKTNTVVVGPREALDITEIAGTSYTWCgqaqeNPETAF---DV 304
Cdd:PRK14665 234 FIAWHEGYPFYTIGQRRGLGIQL----NRAVFVKEIHPETNEVVLASLKALEKTEMWLKDWNIV-----NESRLLgcdDI 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1431816623 305 DVQIRAHADPVPAIAQLVGDELV-VRPTTPLNSVAAGQTAVIYVGTRVLG 353
Cdd:PRK14665 305 IVKIRYRKQENHCTVTITPDNLLhVQLHEPLTAIAEGQAAAFYKDGLLLG 354
|
|
| tRNA_Me_trans_M |
pfam20259 |
tRNA methyl transferase PRC-barrel domain; This family represents a central PRC-barrel domain ... |
207-274 |
2.30e-18 |
|
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: 78.42 E-value: 2.30e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1431816623 207 RGWLADKVGISEGDIVDTE-GNKLGTHEGTPGFTIGQRKGLHIGTpapDGQPRFVLEIRPKTNTVVVGP 274
Cdd:pfam20259 1 KDFLKEYLPVKPGDIIDIDtGEVLGEHEGIWFYTIGQRKGLGIGG---YGEPWYVVEKDPKKNTVYVGR 66
|
|
| tRNA_Me_trans_C |
pfam20258 |
Aminomethyltransferase beta-barrel domain; This domain is found at the C-terminus of tRNA ... |
281-357 |
2.78e-09 |
|
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: 53.05 E-value: 2.78e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1431816623 281 TEIAGTSYTWCGQaqENPETAFDVDVQIRAHADPVPAIAQLVGDELV-VRPTTPLNSVAAGQTAVIYVGTRVLGQFTI 357
Cdd:pfam20258 2 DGLRAKDPNWLGD--KPPTEPLECTVKVRHRQPPVPCVVELIDDETVeVHFDEPVRAVTPGQAAVFYDGDRCLGGGII 77
|
|
| TilS |
COG0037 |
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ... |
2-126 |
1.04e-05 |
|
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439807 [Multi-domain] Cd Length: 235 Bit Score: 46.36 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 2 RVLAAMSGGVDS----AVAAARAVEAGHDVVGVHLAlsrmPGtLRTGARgcctiEDSMDAQRAATLLGIPYYVwdfsERF 77
Cdd:COG0037 17 RILVAVSGGKDSlallHLLAKLRRRLGFELVAVHVD----HG-LREESD-----EDAEFVAELCEELGIPLHV----VRV 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1431816623 78 KsdvvEDFISEYQAGrtpNPCMRCNEkIKFAALMEKALALGFDAVCTGH 126
Cdd:COG0037 83 D----VPAIAKKEGK---SPEAAARR-ARYGALYELARELGADKIATGH 123
|
|
| COG1606 |
COG1606 |
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only]; |
2-193 |
6.39e-04 |
|
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
Pssm-ID: 441214 [Multi-domain] Cd Length: 265 Bit Score: 40.86 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 2 RVLAAMSGGVDSavaaARAVEAGHDVVG--VHLALSRMPgTLRTGARGcctiedsmDAQRAATLLGIPYYVWDFSErFKs 79
Cdd:COG1606 17 SVLVAFSGGVDS----TLLAKVAHDVLGdrVLAVTADSP-SLPERELE--------EAKELAKEIGIRHEVIETDE-LE- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 80 dvVEDFISeyqagrtpNPCMRCN--EKIKFAALMEKALALGFDAVCTGhyANvVPDAHGnlelHRASAWAKDQsyvLGVL 157
Cdd:COG1606 82 --DPEFVA--------NPPDRCYhcKKELFSKLKELAKELGYAVVADG--TN-ADDLGD----YRPGLRAAKE---LGVR 141
|
170 180 190
....*....|....*....|....*....|....*.
gi 1431816623 158 TSeqLAHAMFplgdtpSKDLIRAEAAQRGLSVAQKP 193
Cdd:COG1606 142 SP--LAEAGL------TKAEIRELARELGLPTWDKP 169
|
|
| TtuA-like |
cd01993 |
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ... |
2-129 |
3.69e-03 |
|
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) 2-sulfurtransferase, also called tRNA thiouridine synthetase TtuA, catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T). TtuA belongs to the adenine nucleotide alpha hydrolase superfamily (AANH) that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This domain has a strongly conserved motif SGGKD at the N-terminus.
Pssm-ID: 467497 [Multi-domain] Cd Length: 190 Bit Score: 38.08 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431816623 2 RVLAAMSGGVDSAVAAARAVEAGHDVVGVHLALsrmpgtlrtGARGccTIEDSMD-AQRAATLLGIPYYVWDFSERFKSD 80
Cdd:cd01993 10 KILVAVSGGKDSLALLAVLKKLGYNVEALYINL---------GIGE--YSEKSEEvVKKLAEKLNLPLHVVDLKEEYGLG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1431816623 81 VVEdfISEyqAGRTPnPCMRCNEKIKFaaLMEK-ALALGFDAVCTGHYAN 129
Cdd:cd01993 79 IPE--LAK--KSRRP-PCSVCGLVKRY--IMNKfAVENGFDVVATGHNLD 121
|
|
| |
