|
Name |
Accession |
Description |
Interval |
E-value |
| mnmA |
PRK00143 |
tRNA-specific 2-thiouridylase MnmA; Reviewed |
1-354 |
0e+00 |
|
tRNA-specific 2-thiouridylase MnmA; Reviewed
Pssm-ID: 234664 [Multi-domain] Cd Length: 346 Bit Score: 510.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 1 MKVLAAMSGGVDSSVAAARMVDAGHEVVGVHMALSTAPGTlrTGSRGCCSKEDAADARRVADVLGIPFYVWDFAEKFKED 80
Cdd:PRK00143 1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVFMKLWDDDDE--TGKGGCCAEEDIADARRVADKLGIPHYVVDFEKEFWDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 81 VINDFVSSYARGETPNPCVRCNQQIKFAALSARAVALGFDTVATGHYARLS-GGRLRRAVDRDKDQSYVLAVLTAQQLRH 159
Cdd:PRK00143 79 VIDYFLDEYKAGRTPNPCVLCNKEIKFKAFLEYARELGADYIATGHYARIRdGRELLRGVDPNKDQSYFLYQLTQEQLAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 160 AAFPIGDTPKRQIRAEAARRGLAVANKPDSHDICFIPSGNTKAFLGERIGVRRGVVVDADGVVLASHDGVHGFTIGQRRG 239
Cdd:PRK00143 159 LLFPLGELTKPEVREIAEEAGLPVAKKKDSQGICFIGERDYRDFLKRYLPAQPGEIVDLDGKVLGEHKGLMYYTIGQRKG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 240 LGIAGpgpNGRPRYVTAIDADTATVHVGDVTDLDVQTLTGRAPVFTAGAAPSGPVDCVVQVRAHGETVSAVAELIGDALF 319
Cdd:PRK00143 239 LGIGG---DGEPWYVVGKDPETNTVVVGQGEALYSRELIASDLNWVGGEPPEEPFECTAKIRYRQKPVPATVELEDDRVE 315
|
330 340 350
....*....|....*....|....*....|....*
gi 15610161 320 VQLHAPLRGVARGQTLVLYRpdpaGDEVLGSATIA 354
Cdd:PRK00143 316 VEFDEPQRAVTPGQAAVFYD----GDRVLGGGIIE 346
|
|
| MnmA |
COG0482 |
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ... |
1-356 |
4.20e-173 |
|
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: 485.71 E-value: 4.20e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 1 MKVLAAMSGGVDSSVAAARMVDAGHEVVGVHMALSTAPGTlrTGSRGCCSKEDAADARRVADVLGIPFYVWDFAEKFKED 80
Cdd:COG0482 1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVTMKLWDDDDA--SGSGGCCSLEDIEDARRVADKLGIPHYVVDFEEEFKDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 81 VINDFVSSYARGETPNPCVRCNQQIKFAALSARAVALGFDTVATGHYARLS----GGRLRRAVDRDKDQSYVLAVLTAQQ 156
Cdd:COG0482 79 VIDYFLDEYLAGRTPNPCVLCNREIKFGALLEKALELGADYIATGHYARVEekdgRYELLRGVDPNKDQSYFLYRLTQEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 157 LRHAAFPIGDTPKRQIRAEAARRGLAVANKPDSHDICFIPSGNTKAFLGERIGVRRGVVVDADGVVLASHDGVHGFTIGQ 236
Cdd:COG0482 159 LSKTLFPLGELTKPEVREIAEELGLPVADKKDSQGICFIGDGDYRDFLERYLPEKPGDIVDLDGKVLGEHDGLHYYTIGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 237 RRGLGIAGpgpnGRPRYVTAIDADTATVHVGDVTDLDVQTLTGRAPVFTAGAAPSGPVDCVVQVRAHGETVSAVAELIGD 316
Cdd:COG0482 239 RKGLGIGG----GEPLYVVGKDPETNTVIVGQGEALYSRELTAEDVNWISGEPPEEPLRCTAKIRYRQPPVPATLTPLED 314
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 15610161 317 A-LFVQLHAPLRGVARGQTLVLYRpdpaGDEVLGSATIAGA 356
Cdd:COG0482 315 GrVRVEFDEPQRAVTPGQSAVFYD----GDRVLGGGIIERT 351
|
|
| MnmA_TRMU-like |
cd01998 |
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ... |
2-353 |
2.24e-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: 397.26 E-value: 2.24e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 2 KVLAAMSGGVDSSVAAARMVDAGHEVVGVHMALStapGTLRTGSRGCCSKEDAADARRVADVLGIPFYVWDFAEKFKEDV 81
Cdd:cd01998 1 KVAVAMSGGVDSSVAAALLKEQGYDVIGVFMKNW---DDEDNEKGGCCSEEDIEDARRVADQLGIPLYVVDFSEEYWERV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 82 INDFVSSYARGETPNPCVRCNQQIKFAALSARAVALGFDTVATGHYARLS-----GGRLRRAVDRDKDQSYVLAVLTAQQ 156
Cdd:cd01998 78 FDPFLEEYKAGRTPNPDVLCNREIKFGALLDAAKKLGADYIATGHYARIEednrgRYRLLRAVDPNKDQSYFLSRLSQEQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 157 LRHAAFPIGDTPKRQIRAEAARRGLAVANKPDSHDICFIPSGNTKAFLGERIGVRRG-VVVDADGVVLASHDGVHGFTIG 235
Cdd:cd01998 158 LSRTLFPLGHLTKSEVREIAREAGLPVAEKKDSQGICFIGKRDFRDFLKEYLPEKLPgPIVDIDGKVLGEHKGLWFYTIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 236 QRRGLGIAgpgpNGRPRYVTAIDADTATVHVGDV-TDLDVQTLTGRAPVFTAGAAPSGPVDCVVQVRAHGETVSAVAELI 314
Cdd:cd01998 238 QRKGLGIA----AGEPLYVVKKDPEKNIVVVGPGhPALFSDTLRASDLNWISPEPPLEPLECEAKIRYRQPPVPCTVTPL 313
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15610161 315 GDA-LFVQLHAPLRGVARGQTLVLYRpdpaGDEVLGSATI 353
Cdd:cd01998 314 DDGrLKVEFDEPQRAVTPGQAAVFYD----GDEVLGGGII 349
|
|
| tRNA_Me_trans |
pfam03054 |
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ... |
1-196 |
7.97e-110 |
|
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: 319.20 E-value: 7.97e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 1 MKVLAAMSGGVDSSVAAARMVDAGHEVVGVHMALSTAPGTLRTGSRgCCSKEDAADARRVADVLGIPFYVWDFAEKFKED 80
Cdd:pfam03054 1 MKVVVAMSGGVDSSVAAYLLKEQGHNVIGVFMKNWDEEQSLDEEGK-CCSEEDLADAQRVCEQLGIPLYVVNFEKEYWED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 81 VINDFVSSYARGETPNPCVRCNQQIKFAALSARAVA-LGFDTVATGHYARLS-----GGRLRRAVDRDKDQSYVLAVLTA 154
Cdd:pfam03054 80 VFEPFLDEYKNGRTPNPDVLCNKEIKFGALLDYALEnLGADYVATGHYARVSlnkdgGSELLRALDKNKDQSYFLSTLSQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15610161 155 QQLRHAAFPIGDTPKRQIRAEAARRGLAVANKPDSHDICFIP 196
Cdd:pfam03054 160 EQLEKLLFPLGELTKEEVRKIAKEAGLATAKKKDSQGICFIG 201
|
|
| trmU |
TIGR00420 |
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ... |
1-353 |
1.47e-85 |
|
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: 263.09 E-value: 1.47e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 1 MKVLAAMSGGVDSSVAAARMVDAGHEVVGVHMALSTApgTLRTGSRGCCSKEDAADARRVADVLGIPFYVWDFAEKFKED 80
Cdd:TIGR00420 1 KKVIVGLSGGVDSSVSAYLLKQQGYEVVGVFMKNWEE--DDKNDGHGCTSAEDLRDAQAICEKLGIPLEKVNFQKEYWNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 81 VINDFVSSYARGETPNPCVRCNQQIKFAALSARAV-ALGFDTVATGHYARLSG----GRLRRAVDRDKDQSYVLAVLTAQ 155
Cdd:TIGR00420 79 VFEPFIQEYKEGRTPNPDILCNKFIKFGAFLEYAAeLLGNDKIATGHYARIAEiegkSLLLRALDKNKDQSYFLYHLSHE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 156 QLRHAAFPIGDTPKRQIRAEAARRGLAVANKPDSHDICFIPSGNTKAFLGERIGVRRGV-VVDADGVVLASHDGVHGFTI 234
Cdd:TIGR00420 159 QLAKLLFPLGELLKPEVRQIAKNAGLPTAEKKDSQGICFIGERKFRDFLKKYLPVKPGViITVDGQSVIGEHDGLWFYTI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 235 GQRRGLGIagPGPNGrPRYVTAIDADTATVHVGDvTDLDVQTLTGRAPVFT-AGAAP-SGPVDCVVQVRAHGETVSAVAE 312
Cdd:TIGR00420 239 GQRKGLGI--GGAAE-PWFVVEKDLETNELVVSH-GKPDLASRGLLAQQFHwLDDEPnPFEMRCTVKIRYRQVPVQCKLK 314
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 15610161 313 LIGDALF-VQLHAPLRGVARGQTLVLYRpdpaGDEVLGSATI 353
Cdd:TIGR00420 315 LLDDNLIeVIFDEPQAGVTPGQSAVLYK----GDICLGGGII 352
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| mnmA |
PRK00143 |
tRNA-specific 2-thiouridylase MnmA; Reviewed |
1-354 |
0e+00 |
|
tRNA-specific 2-thiouridylase MnmA; Reviewed
Pssm-ID: 234664 [Multi-domain] Cd Length: 346 Bit Score: 510.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 1 MKVLAAMSGGVDSSVAAARMVDAGHEVVGVHMALSTAPGTlrTGSRGCCSKEDAADARRVADVLGIPFYVWDFAEKFKED 80
Cdd:PRK00143 1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVFMKLWDDDDE--TGKGGCCAEEDIADARRVADKLGIPHYVVDFEKEFWDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 81 VINDFVSSYARGETPNPCVRCNQQIKFAALSARAVALGFDTVATGHYARLS-GGRLRRAVDRDKDQSYVLAVLTAQQLRH 159
Cdd:PRK00143 79 VIDYFLDEYKAGRTPNPCVLCNKEIKFKAFLEYARELGADYIATGHYARIRdGRELLRGVDPNKDQSYFLYQLTQEQLAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 160 AAFPIGDTPKRQIRAEAARRGLAVANKPDSHDICFIPSGNTKAFLGERIGVRRGVVVDADGVVLASHDGVHGFTIGQRRG 239
Cdd:PRK00143 159 LLFPLGELTKPEVREIAEEAGLPVAKKKDSQGICFIGERDYRDFLKRYLPAQPGEIVDLDGKVLGEHKGLMYYTIGQRKG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 240 LGIAGpgpNGRPRYVTAIDADTATVHVGDVTDLDVQTLTGRAPVFTAGAAPSGPVDCVVQVRAHGETVSAVAELIGDALF 319
Cdd:PRK00143 239 LGIGG---DGEPWYVVGKDPETNTVVVGQGEALYSRELIASDLNWVGGEPPEEPFECTAKIRYRQKPVPATVELEDDRVE 315
|
330 340 350
....*....|....*....|....*....|....*
gi 15610161 320 VQLHAPLRGVARGQTLVLYRpdpaGDEVLGSATIA 354
Cdd:PRK00143 316 VEFDEPQRAVTPGQAAVFYD----GDRVLGGGIIE 346
|
|
| MnmA |
COG0482 |
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ... |
1-356 |
4.20e-173 |
|
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: 485.71 E-value: 4.20e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 1 MKVLAAMSGGVDSSVAAARMVDAGHEVVGVHMALSTAPGTlrTGSRGCCSKEDAADARRVADVLGIPFYVWDFAEKFKED 80
Cdd:COG0482 1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVTMKLWDDDDA--SGSGGCCSLEDIEDARRVADKLGIPHYVVDFEEEFKDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 81 VINDFVSSYARGETPNPCVRCNQQIKFAALSARAVALGFDTVATGHYARLS----GGRLRRAVDRDKDQSYVLAVLTAQQ 156
Cdd:COG0482 79 VIDYFLDEYLAGRTPNPCVLCNREIKFGALLEKALELGADYIATGHYARVEekdgRYELLRGVDPNKDQSYFLYRLTQEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 157 LRHAAFPIGDTPKRQIRAEAARRGLAVANKPDSHDICFIPSGNTKAFLGERIGVRRGVVVDADGVVLASHDGVHGFTIGQ 236
Cdd:COG0482 159 LSKTLFPLGELTKPEVREIAEELGLPVADKKDSQGICFIGDGDYRDFLERYLPEKPGDIVDLDGKVLGEHDGLHYYTIGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 237 RRGLGIAGpgpnGRPRYVTAIDADTATVHVGDVTDLDVQTLTGRAPVFTAGAAPSGPVDCVVQVRAHGETVSAVAELIGD 316
Cdd:COG0482 239 RKGLGIGG----GEPLYVVGKDPETNTVIVGQGEALYSRELTAEDVNWISGEPPEEPLRCTAKIRYRQPPVPATLTPLED 314
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 15610161 317 A-LFVQLHAPLRGVARGQTLVLYRpdpaGDEVLGSATIAGA 356
Cdd:COG0482 315 GrVRVEFDEPQRAVTPGQSAVFYD----GDRVLGGGIIERT 351
|
|
| MnmA_TRMU-like |
cd01998 |
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ... |
2-353 |
2.24e-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: 397.26 E-value: 2.24e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 2 KVLAAMSGGVDSSVAAARMVDAGHEVVGVHMALStapGTLRTGSRGCCSKEDAADARRVADVLGIPFYVWDFAEKFKEDV 81
Cdd:cd01998 1 KVAVAMSGGVDSSVAAALLKEQGYDVIGVFMKNW---DDEDNEKGGCCSEEDIEDARRVADQLGIPLYVVDFSEEYWERV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 82 INDFVSSYARGETPNPCVRCNQQIKFAALSARAVALGFDTVATGHYARLS-----GGRLRRAVDRDKDQSYVLAVLTAQQ 156
Cdd:cd01998 78 FDPFLEEYKAGRTPNPDVLCNREIKFGALLDAAKKLGADYIATGHYARIEednrgRYRLLRAVDPNKDQSYFLSRLSQEQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 157 LRHAAFPIGDTPKRQIRAEAARRGLAVANKPDSHDICFIPSGNTKAFLGERIGVRRG-VVVDADGVVLASHDGVHGFTIG 235
Cdd:cd01998 158 LSRTLFPLGHLTKSEVREIAREAGLPVAEKKDSQGICFIGKRDFRDFLKEYLPEKLPgPIVDIDGKVLGEHKGLWFYTIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 236 QRRGLGIAgpgpNGRPRYVTAIDADTATVHVGDV-TDLDVQTLTGRAPVFTAGAAPSGPVDCVVQVRAHGETVSAVAELI 314
Cdd:cd01998 238 QRKGLGIA----AGEPLYVVKKDPEKNIVVVGPGhPALFSDTLRASDLNWISPEPPLEPLECEAKIRYRQPPVPCTVTPL 313
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15610161 315 GDA-LFVQLHAPLRGVARGQTLVLYRpdpaGDEVLGSATI 353
Cdd:cd01998 314 DDGrLKVEFDEPQRAVTPGQAAVFYD----GDEVLGGGII 349
|
|
| tRNA_Me_trans |
pfam03054 |
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ... |
1-196 |
7.97e-110 |
|
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: 319.20 E-value: 7.97e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 1 MKVLAAMSGGVDSSVAAARMVDAGHEVVGVHMALSTAPGTLRTGSRgCCSKEDAADARRVADVLGIPFYVWDFAEKFKED 80
Cdd:pfam03054 1 MKVVVAMSGGVDSSVAAYLLKEQGHNVIGVFMKNWDEEQSLDEEGK-CCSEEDLADAQRVCEQLGIPLYVVNFEKEYWED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 81 VINDFVSSYARGETPNPCVRCNQQIKFAALSARAVA-LGFDTVATGHYARLS-----GGRLRRAVDRDKDQSYVLAVLTA 154
Cdd:pfam03054 80 VFEPFLDEYKNGRTPNPDVLCNKEIKFGALLDYALEnLGADYVATGHYARVSlnkdgGSELLRALDKNKDQSYFLSTLSQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15610161 155 QQLRHAAFPIGDTPKRQIRAEAARRGLAVANKPDSHDICFIP 196
Cdd:pfam03054 160 EQLEKLLFPLGELTKEEVRKIAKEAGLATAKKKDSQGICFIG 201
|
|
| trmU |
TIGR00420 |
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ... |
1-353 |
1.47e-85 |
|
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: 263.09 E-value: 1.47e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 1 MKVLAAMSGGVDSSVAAARMVDAGHEVVGVHMALSTApgTLRTGSRGCCSKEDAADARRVADVLGIPFYVWDFAEKFKED 80
Cdd:TIGR00420 1 KKVIVGLSGGVDSSVSAYLLKQQGYEVVGVFMKNWEE--DDKNDGHGCTSAEDLRDAQAICEKLGIPLEKVNFQKEYWNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 81 VINDFVSSYARGETPNPCVRCNQQIKFAALSARAV-ALGFDTVATGHYARLSG----GRLRRAVDRDKDQSYVLAVLTAQ 155
Cdd:TIGR00420 79 VFEPFIQEYKEGRTPNPDILCNKFIKFGAFLEYAAeLLGNDKIATGHYARIAEiegkSLLLRALDKNKDQSYFLYHLSHE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 156 QLRHAAFPIGDTPKRQIRAEAARRGLAVANKPDSHDICFIPSGNTKAFLGERIGVRRGV-VVDADGVVLASHDGVHGFTI 234
Cdd:TIGR00420 159 QLAKLLFPLGELLKPEVRQIAKNAGLPTAEKKDSQGICFIGERKFRDFLKKYLPVKPGViITVDGQSVIGEHDGLWFYTI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 235 GQRRGLGIagPGPNGrPRYVTAIDADTATVHVGDvTDLDVQTLTGRAPVFT-AGAAP-SGPVDCVVQVRAHGETVSAVAE 312
Cdd:TIGR00420 239 GQRKGLGI--GGAAE-PWFVVEKDLETNELVVSH-GKPDLASRGLLAQQFHwLDDEPnPFEMRCTVKIRYRQVPVQCKLK 314
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 15610161 313 LIGDALF-VQLHAPLRGVARGQTLVLYRpdpaGDEVLGSATI 353
Cdd:TIGR00420 315 LLDDNLIeVIFDEPQAGVTPGQSAVLYK----GDICLGGGII 352
|
|
| mnmA |
PRK14665 |
tRNA-specific 2-thiouridylase MnmA; Provisional |
2-341 |
5.60e-52 |
|
tRNA-specific 2-thiouridylase MnmA; Provisional
Pssm-ID: 173128 [Multi-domain] Cd Length: 360 Bit Score: 176.66 E-value: 5.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 2 KVLAAMSGGVDSSVAAARMVDAGHEVVGVHMALSTAPGtlrtgsrgccSKEDAADARRVADVLGIPFYVWDFAEKFKEDV 81
Cdd:PRK14665 7 RVLLGMSGGTDSSVAAMLLLEAGYEVTGVTFRFYEFNG----------STEYLEDARALAERLGIGHITYDARKVFRKQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 82 INDFVSSYARGETPNPCVRCNQQIKFAALSARAVALGFDTVATGHYAR---LSGG-RLRRAVDRDKDQSYVLAVLTAQQL 157
Cdd:PRK14665 77 IDYFIDEYMSGHTPVPCTLCNNYLKWPLLAKIADEMGIFYLATGHYVRkqwIDGNyYITPAEDVDKDQSFFLWGLRQEIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 158 RHAAFPIGDTPKRQIRAEAARRG-LAVANKPDSHDICFIPSgNTKAFLGERI-------------GVRRGVVVDADGVVL 223
Cdd:PRK14665 157 QRMLLPMGGMTKSEARAYAAERGfEKVAKKRDSLGVCFCPM-DYRSFLKKCLcdesgdknrniyrKVERGRFLDESGNFI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 224 ASHDGVHGFTIGQRRGLGIAgpgpNGRPRYVTAIDADTATVHVGDVTDLDVQTLTGRAPVFTAGAAPSGPVDCVVQVRAH 303
Cdd:PRK14665 236 AWHEGYPFYTIGQRRGLGIQ----LNRAVFVKEIHPETNEVVLASLKALEKTEMWLKDWNIVNESRLLGCDDIIVKIRYR 311
|
330 340 350
....*....|....*....|....*....|....*....
gi 15610161 304 GETVSAVAELIGDA-LFVQLHAPLRGVARGQTLVLYRPD 341
Cdd:PRK14665 312 KQENHCTVTITPDNlLHVQLHEPLTAIAEGQAAAFYKDG 350
|
|
| PRK14664 |
PRK14664 |
tRNA-specific 2-thiouridylase MnmA; Provisional |
2-359 |
5.83e-51 |
|
tRNA-specific 2-thiouridylase MnmA; Provisional
Pssm-ID: 173127 [Multi-domain] Cd Length: 362 Bit Score: 173.99 E-value: 5.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 2 KVLAAMSGGVDSSVAAARMVDAGHEVVGVhmalstapgTLRTGSrgccskEDAADARRVADVLGIPFYVWDFAEKFKEDV 81
Cdd:PRK14664 7 RVLVGMSGGIDSTATCLMLQEQGYEIVGV---------TMRVWG------DEPQDARELAARMGIEHYVADERVPFKDTI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 82 INDFVSSYARGETPNPCVRCNQQIKFAALSARAVALGFDTVATGHYARLS--GGRLRRAV--DRDKDQSYVLAVLTAQQL 157
Cdd:PRK14664 72 VKNFIDEYRQGRTPNPCVMCNPLFKFRMLIEWADKLGCAWIATGHYSRLEerNGHIYIVAgdDDKKDQSYFLWRLGQDIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 158 RHAAFPIGDTPKRQIRAEAARRGL-AVANKPDSHDICFIpSGNTKAFLGER-----IGVRRGVVVDADGVVLASHDGVHG 231
Cdd:PRK14664 152 RRCIFPLGNYTKQTVREYLREKGYeAKSKEGESMEVCFI-KGDYRDFLREQcpeldTEVGPGWFVNSEGVKLGQHKGFPY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 232 FTIGQRRGLGIAgpgpNGRPRYVTAIDADTATVHVGDVTDLDVQTLTGRAPVFTAGAAPSGPVDCVVQVRAHGETVSAVA 311
Cdd:PRK14664 231 YTIGQRKGLEIA----LGKPAYVLKINPQKNTVMLGDAEQLKAEYMLAEQDNIVDEQELFACPDLAVRIRYRSRPIPCRV 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 15610161 312 ELIGDA-LFVQLHAPLRGVARGQTLVLYRpdpaGDEVLGSATIAGASGL 359
Cdd:PRK14664 307 KRLEDGrLLVRFLAEASAIAPGQSAVFYE----GRRVLGGAFIASQRGI 351
|
|
| tRNA_Me_trans_C |
pfam20258 |
Aminomethyltransferase beta-barrel domain; This domain is found at the C-terminus of tRNA ... |
274-353 |
1.77e-20 |
|
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: 84.25 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 274 VQTLTGRAPVFTAGAAPSGPVDCVVQVRAHGETVSAVAELIGD-ALFVQLHAPLRGVARGQTLVLYrpdpAGDEVLGSAT 352
Cdd:pfam20258 1 SDGLRAKDPNWLGDKPPTEPLECTVKVRHRQPPVPCVVELIDDeTVEVHFDEPVRAVTPGQAAVFY----DGDRCLGGGI 76
|
.
gi 15610161 353 I 353
Cdd:pfam20258 77 I 77
|
|
| tRNA_Me_trans_M |
pfam20259 |
tRNA methyl transferase PRC-barrel domain; This family represents a central PRC-barrel domain ... |
201-268 |
3.92e-16 |
|
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: 72.25 E-value: 3.92e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15610161 201 KAFLGERIGVRRGV-VVDADGVVLASHDGVHGFTIGQRRGLGIAGpgpNGRPRYVTAIDADTATVHVGD 268
Cdd:pfam20259 1 KDFLKEYLPVKPGDiIDIDTGEVLGEHEGIWFYTIGQRKGLGIGG---YGEPWYVVEKDPKKNTVYVGR 66
|
|
| TilS |
COG0037 |
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ... |
2-126 |
2.20e-10 |
|
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: 60.23 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 2 KVLAAMSGGVDSSV---AAARMVD-AGHEVVGVHMALStapgtLRTGSRgccskEDAADARRVADVLGIPFYVwdfaEKF 77
Cdd:COG0037 17 RILVAVSGGKDSLAllhLLAKLRRrLGFELVAVHVDHG-----LREESD-----EDAEFVAELCEELGIPLHV----VRV 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 15610161 78 KedvindfVSSYARGETPNPCVRCnQQIKFAALSARAVALGFDTVATGH 126
Cdd:COG0037 83 D-------VPAIAKKEGKSPEAAA-RRARYGALYELARELGADKIATGH 123
|
|
| TtuA-like |
cd01993 |
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ... |
2-126 |
8.15e-09 |
|
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: 54.64 E-value: 8.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 2 KVLAAMSGGVDSSVAAARMVDAGHEVVGVHMALSTAPgtlrtgsrgcCSKEDAADARRVADVLGIPFYVWDFAEKFKEDv 81
Cdd:cd01993 10 KILVAVSGGKDSLALLAVLKKLGYNVEALYINLGIGE----------YSEKSEEVVKKLAEKLNLPLHVVDLKEEYGLG- 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 15610161 82 indfVSSYARGETPNPCVRCNqQIKFAALSARAVALGFDTVATGH 126
Cdd:cd01993 79 ----IPELAKKSRRPPCSVCG-LVKRYIMNKFAVENGFDVVATGH 118
|
|
| NAD_synthase |
pfam02540 |
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ... |
2-192 |
2.99e-08 |
|
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is induced by stress factors such as heat shock and glucose limitation.
Pssm-ID: 396888 [Multi-domain] Cd Length: 241 Bit Score: 53.92 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 2 KVLAAMSGGVDSSVAAARMVDA-GHE-VVGVHMALSTAPgtlrtgsrgccsKEDAADARRVADVLGIPFYVWDfaekfke 79
Cdd:pfam02540 20 GVVLGLSGGIDSSLVAYLAVKAlGKEnVLALIMPSSQSS------------EEDVQDALALAENLGIEYKTID------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 80 dvINDFVSSYARGETPNPC--VRCNQQ--IKFAALSARAVALGFDTVATGHYARLSGGRLRRAVDrdkdqsyvLAVLTAq 155
Cdd:pfam02540 81 --IKPIVRAFSQLFQDASEdfAKGNLKarIRMAILYYIANKFNYLVLGTGNKSELAVGYFTKYGD--------GACDIA- 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 15610161 156 qlrhaafPIGDTPKRQIRAEAARRGL--AVANKPDSHDI 192
Cdd:pfam02540 150 -------PIGDLYKTQVYELARYLNVpeRIIKKPPSADL 181
|
|
| COG1606 |
COG1606 |
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only]; |
2-187 |
4.76e-07 |
|
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
Pssm-ID: 441214 [Multi-domain] Cd Length: 265 Bit Score: 50.49 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 2 KVLAAMSGGVDSSVAAARMVDA-GHEVVGVHMALSTAPgtlrtgsrgccsKEDAADARRVADVLGIPFYVWDFAEKFKED 80
Cdd:COG1606 17 SVLVAFSGGVDSTLLAKVAHDVlGDRVLAVTADSPSLP------------ERELEEAKELAKEIGIRHEVIETDELEDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 81 VI-NDfvssyargetPNPCVRCNQQIkFAALSARAVALGFDTVATG-HYARLSGGRL-RRAVDRdkdqsyvLAVLTAqqL 157
Cdd:COG1606 85 FVaNP----------PDRCYHCKKEL-FSKLKELAKELGYAVVADGtNADDLGDYRPgLRAAKE-------LGVRSP--L 144
|
170 180 190
....*....|....*....|....*....|
gi 15610161 158 RHAAFpigdTpKRQIRAEAARRGLAVANKP 187
Cdd:COG1606 145 AEAGL----T-KAEIRELARELGLPTWDKP 169
|
|
| PRK13980 |
PRK13980 |
NAD synthetase; Provisional |
8-89 |
5.51e-06 |
|
NAD synthetase; Provisional
Pssm-ID: 184435 [Multi-domain] Cd Length: 265 Bit Score: 47.13 E-value: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 8 SGGVDSSVAAARMVDA-GHE-VVGVHMALSTAPgtlrtgsrgccsKEDAADARRVADVLGIPFYVWDfaekfkedvINDF 85
Cdd:PRK13980 38 SGGIDSAVVAYLAVKAlGKEnVLALLMPSSVSP------------PEDLEDAELVAEDLGIEYKVIE---------ITPI 96
|
....
gi 15610161 86 VSSY 89
Cdd:PRK13980 97 VDAF 100
|
|
| NadE |
COG0171 |
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
2-72 |
1.58e-05 |
|
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ synthetase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 439941 [Multi-domain] Cd Length: 542 Bit Score: 46.76 E-value: 1.58e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15610161 2 KVLAAMSGGVDSSVAAARMVDA-GHE-VVGVHMAlstAPGTlrtgsrgccSKEDAADARRVADVLGIPFYVWD 72
Cdd:COG0171 288 GVVLGLSGGIDSALVAALAVDAlGPEnVLGVTMP---SRYT---------SDESLEDAEELAENLGIEYEEID 348
|
|
| NAD_synthase |
cd00553 |
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ... |
8-72 |
5.09e-05 |
|
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de novo nicotinamide adenine dinucleotide (NAD(+)) biosynthesis, an amide transfer from either ammonia or glutamine to nicotinic acid adenine dinucleotide (NaAD). The conversion of NaAD to NAD(+) occurs via a NAD-adenylate intermediate and requires ATP and Mg(2+). The intermediate is subsequently cleaved into NAD(+) and AMP. In many prokaryotes, such as Escherichia coli, NAD synthase consists of a single domain and is strictly ammonia dependent. In contrast, eukaryotes and other prokaryotes have an additional N-terminal amidohydrolase domain that prefer glutamine. Interestingly, NAD(+) synthases in these prokaryotes, can also utilize ammonia as an amide source.
Pssm-ID: 467484 [Multi-domain] Cd Length: 248 Bit Score: 44.08 E-value: 5.09e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15610161 8 SGGVDSSVAAA---RMVDAGHeVVGVHMalstaPGtlrTGSrgccSKEDAADARRVADVLGIPFYVWD 72
Cdd:cd00553 31 SGGIDSAVVAAlavRALGAEN-VLALIM-----PS---RYS----SKETRDDAKALAENLGIEYRTID 85
|
|
| LarE-like |
cd01990 |
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ... |
2-187 |
1.16e-04 |
|
Lactate racemization operon protein LarE and similar proteins; This subfamily includes Lactiplantibacillus plantarum LarE, a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family. LarE is part of the lar operon, encoding five Lar proteins (LarA-E) that collaboratively synthesize and incorporate a niacin-derived Ni-containing cofactor into LarA, an Ni-dependent lactate racemase. It catalyzes successive thiolation reactions by donating the sulfur atom of their exclusive cysteine residues to the substrate. The LarE-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. Proteins from this subfamily probably binds ATP. This domain is about 200 amino acids long with a strongly conserved motif SGGxDS at the N-terminus.
Pssm-ID: 467494 [Multi-domain] Cd Length: 222 Bit Score: 43.02 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 2 KVLAAMSGGVDSSVAAARMVDA-GHEVVGVhmalstapgtlrTGSRGCCSKEDAADARRVADVLGIPFYVWDFAEKFKED 80
Cdd:cd01990 1 KVVVAFSGGVDSSLLAKLAKEVlGDNVVAV------------TADSPLVPREELEEAKRIAEEIGIRHEIIKTDELDDEE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 81 VINDfvssyargeTPNPCVRCNQQIkFAALSARAVALGFDTVATG-HYARLSGGR--LRRAVDRDKDQSYVLAVLTaqql 157
Cdd:cd01990 69 YVAN---------DPDRCYHCKKAL-YSTLKEIAKERGYDVVLDGtNADDLKDYRpgLLAAAELGIRSPLPELGLT---- 134
|
170 180 190
....*....|....*....|....*....|
gi 15610161 158 rhaafpigdtpKRQIRAEAARRGLAVANKP 187
Cdd:cd01990 135 -----------KSEIRELARELGLPNWDKP 153
|
|
| ThiI |
pfam02568 |
Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for ... |
2-125 |
3.92e-04 |
|
Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for thiamine biosynthesis.
Pssm-ID: 280691 [Multi-domain] Cd Length: 197 Bit Score: 41.26 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 2 KVLAAMSGGVDSSVAAARMVDAGHEVVGVHMalSTAPGTlrtgsrgccSKEDAADARRVADVLG-------IPFYVWDFa 74
Cdd:pfam02568 5 KVLALISGGIDSPVAAYMMMRRGCRVVALHF--INNPGT---------SAEAIGKVQKLAELLArygtsheVRLVVFDF- 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 15610161 75 ekfkEDVINDFVSSYARGETPNPCVRCnqQIKFAALSARavALGFDTVATG 125
Cdd:pfam02568 73 ----TDVQKEILEKAPEGYRCVLLKRC--MYRIAEKVAE--EEGADALVTG 115
|
|
| TilS_N |
cd01992 |
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ... |
2-126 |
4.11e-04 |
|
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine synthase (EC 6.3.4.19), also called tRNA(Ile)-2-lysyl-cytidine synthase or tRNA(Ile)-lysidine synthetase, catalyzes the ligation of lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. This subfamily belongs to the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This domain has a strongly conserved motif SGGXD at the N-terminus.
Pssm-ID: 467496 [Multi-domain] Cd Length: 185 Bit Score: 40.66 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 2 KVLAAMSGGVDSSVAAARMVDA----GHEVVGV---HMalstapgtLRTGsrgccSKEDAADARRVADVLGIPFYVWDFA 74
Cdd:cd01992 1 KILVAVSGGPDSMALLHLLKELrpklGLKLVAVhvdHG--------LREE-----SAEEAQFVAKLCKKLGIPLHILTVT 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 15610161 75 EKFKEDvindfvSSY---ARgetpnpcvrcnqQIKFAALSARAVALGFDTVATGH 126
Cdd:cd01992 68 EAPKSG------GNLeaaAR------------EARYAFLERAAKEHGIDVLLTAH 104
|
|
| GMP_synthase_C |
cd01997 |
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ... |
2-31 |
6.86e-04 |
|
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP synthetase (glutamine-hydrolyzing, EC 6.3.5.2) contains two subdomains: the ATP pyrophosphatase domain at the N-terminal and the dimerization domain at the C-terminal end. The ATP-PPase domain is a twisted, five-stranded parallel beta-sheet sandwiched between helical layers. It has a signature nucleotide-binding motif, or PP-loop, at the end of the first-beta strand. GMP synthetase is a homodimer, but in some archaea, it is a heterodimer made up of ATP pyrophosphatase (ATP-PPase) and a GATase subunit. In eukaryotes and bacteria, the two catalytic units are encoded by a single gene producing a two-domain-type GMP with a GATase domain in the N-terminus and an ATP-PPase domain in the C-terminus.
Pssm-ID: 467501 [Multi-domain] Cd Length: 311 Bit Score: 40.99 E-value: 6.86e-04
10 20 30
....*....|....*....|....*....|..
gi 15610161 2 KVLAAMSGGVDSSVAAARMVDA-GHE-VVGVH 31
Cdd:cd01997 9 KVLCLVSGGVDSTVCAALLHKAlGDErVIAVH 40
|
|
| PRK08349 |
PRK08349 |
hypothetical protein; Validated |
1-32 |
1.10e-03 |
|
hypothetical protein; Validated
Pssm-ID: 169396 Cd Length: 198 Bit Score: 39.72 E-value: 1.10e-03
10 20 30
....*....|....*....|....*....|..
gi 15610161 1 MKVLAAMSGGVDSSVAAARMVDAGHEVVGVHM 32
Cdd:PRK08349 1 MKAVALLSSGIDSPVAIYLMLRRGVEVYPVHF 32
|
|
| QueC-like |
cd01995 |
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ... |
1-125 |
1.24e-03 |
|
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC 6.3.4.20) is also called 7-cyano-7-carbaguanine synthase, preQ(0) synthase, or queuosine biosynthesis protein QueC. It catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)), as part of the biosynthesis pathway of queuosine (Q). Q is one of the most complex modifications occurring at the wobble position of tRNAs with GUN anticodons, and is implicated in a number of biological activities, including accuracy of decoding, virulence, and cellular differentiation. This subfamily 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: 467499 [Multi-domain] Cd Length: 208 Bit Score: 39.52 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610161 1 MKVLAAMSGGVDSSVAAARMVDAGHEVVGVHmalstapgtLRTGSRGccSKEDAADARRVADVLGIPFYVWD---FAEKF 77
Cdd:cd01995 1 MKAVVLLSGGLDSTTLLYWALKEGYEVHALT---------FDYGQRH--AKEELEAAKLIAKLLGIEHKVIDlsfLGELG 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15610161 78 KEDVINDFV----SSYARGETPNPCVRCNQQIKFAALSARAVALGFDTVATG 125
Cdd:cd01995 70 GSSLTDEGEevpdGEYDEESIPSTWVPNRNLIFLSIAAAYAESLGASAIVIG 121
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|
| guaA |
PRK00074 |
GMP synthase; Reviewed |
2-18 |
1.30e-03 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 40.42 E-value: 1.30e-03
|
| PPase_ThiI |
cd01712 |
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole ... |
2-35 |
1.93e-03 |
|
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole synthesis in the thiamine biosynthesis pathway. ThiI is also responsible for the 4-thiouridine (S4U) modification at position 8 in some prokaryotic tRNAs. ThiI contains a PP-loop pyrophosphatase domain which binds ATP and activates tRNA by adenylation. The PP-loop pyrophosphatase catalytic domain of ThiI proteins is always accompanied by a THUMP domain towards the N terminus. THUMP domains are predicted to bind RNA and are widespread in bacteria, archaea, and eukaryotes. The acronym was derived from the names of RNA-modifying enzymes in which this domain is found, namely, thiouridine synthases (ThiI), methylases, and archaeal pseudouridine synthases. ThiI proteins from gamma-proteobacteria and from archaea of the genus Thermoplasma also contain a C-terminal extension of approximately 100 amino acid residues which accepts sulfur in the form of a persulfide on a cysteine residue. This persulfide is responsible for a nucleophilic attack of the adenylated tRNA substrate, completing the sulfur insertion forming a disulfide-bridge between the rhodanese-like domain and a second cysteine residue located in the PP-loop domain. The reaction releases AMP and modified tRNA, and leaves the enzyme in an oxidized state. The disulfide is then reductively cleaved to complete the enzymatic cycle. The pyrophosphatase domain of ThiI belongs to the adenine nucleotide hydrolase (AANH) superfamily and it binds to adenosine nucleotide.
Pssm-ID: 467485 [Multi-domain] Cd Length: 185 Bit Score: 38.69 E-value: 1.93e-03
10 20 30
....*....|....*....|....*....|....
gi 15610161 2 KVLAAMSGGVDSSVAAARMVDAGHEVVGVHMALS 35
Cdd:cd01712 6 KVLVLLSGGIDSPVAAWMMMKRGVEVDFLHFHSG 39
|
|
| PRK13981 |
PRK13981 |
NAD synthetase; Provisional |
2-70 |
5.59e-03 |
|
NAD synthetase; Provisional
Pssm-ID: 237577 [Multi-domain] Cd Length: 540 Bit Score: 38.60 E-value: 5.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15610161 2 KVLAAMSGGVDSSVAAARMVDA-GHE-VVGVHMalstaPgtlrtgSRgCCSKEDAADARRVADVLGIPFYV 70
Cdd:PRK13981 282 GVVLGLSGGIDSALVAAIAVDAlGAErVRAVMM-----P------SR-YTSEESLDDAAALAKNLGVRYDI 340
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