|
Name |
Accession |
Description |
Interval |
E-value |
| MnmA_TRMU-like |
cd01998 |
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ... |
83-439 |
2.32e-164 |
|
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: 468.52 E-value: 2.32e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 83 RVAVLLSGGVDSSVALRLLHAAGHSCTAFYLKIWFQEgfENFWNQCPWEDDLKYAKHVCEQVDVPLEVVHLTDEYWERVV 162
Cdd:cd01998 1 KVAVAMSGGVDSSVAAALLKEQGYDVIGVFMKNWDDE--DNEKGGCCSEEDIEDARRVADQLGIPLYVVDFSEEYWERVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 163 SYIIEEYRCGRTPNPDVLCNTRIKFGAFMDAISDMEYDYVGSGHYAKVVHPPADQndasSVLELSQDMVKDQTYFLSHLS 242
Cdd:cd01998 79 DPFLEEYKAGRTPNPDVLCNREIKFGALLDAAKKLGADYIATGHYARIEEDNRGR----YRLLRAVDPNKDQSYFLSRLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 243 QTQLKRLLFPLGCVKKDEVRKLATQFDLPNKDRKDSQGICFLGKIKFSDFVCRHIGE-MEGIILEAEsGDFLGNHRGFWF 321
Cdd:cd01998 155 QEQLSRTLFPLGHLTKSEVREIAREAGLPVAEKKDSQGICFIGKRDFRDFLKEYLPEkLPGPIVDID-GKVLGEHKGLWF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 322 YTIGQRQGLRLP-GGPWYVVEKDTKNNVVFVSRNYYSIDKRRriFRVGSLRWNSGKPSGKVRELRCKVRHGPGFYSCSFE 400
Cdd:cd01998 234 YTIGQRKGLGIAaGEPLYVVKKDPEKNIVVVGPGHPALFSDT--LRASDLNWISPEPPLEPLECEAKIRYRQPPVPCTVT 311
|
330 340 350
....*....|....*....|....*....|....*....
gi 145336613 401 MEGDGdVAVVHLDEDDQGLAAGQFAAFYEGTTCIGSGVI 439
Cdd:cd01998 312 PLDDG-RLKVEFDEPQRAVTPGQAAVFYDGDEVLGGGII 349
|
|
| MnmA |
COG0482 |
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ... |
83-443 |
5.09e-144 |
|
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: 417.15 E-value: 5.09e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 83 RVAVLLSGGVDSSVALRLLHAAGHSCTAFYLKIWFQEGFENFwNQCPWEDDLKYAKHVCEQVDVPLEVVHLTDEYWERVV 162
Cdd:COG0482 2 RVVVGMSGGVDSSVAAALLKEQGYEVIGVTMKLWDDDDASGS-GGCCSLEDIEDARRVADKLGIPHYVVDFEEEFKDRVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 163 SYIIEEYRCGRTPNPDVLCNTRIKFGAFMDAISDMEYDYVGSGHYAKVVHppadqNDASSVLELSQDMVKDQTYFLSHLS 242
Cdd:COG0482 81 DYFLDEYLAGRTPNPCVLCNREIKFGALLEKALELGADYIATGHYARVEE-----KDGRYELLRGVDPNKDQSYFLYRLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 243 QTQLKRLLFPLGCVKKDEVRKLATQFDLPNKDRKDSQGICFLGKIKFSDFVCRHIGEMEGIILEaESGDFLGNHRGFWFY 322
Cdd:COG0482 156 QEQLSKTLFPLGELTKPEVREIAEELGLPVADKKDSQGICFIGDGDYRDFLERYLPEKPGDIVD-LDGKVLGEHDGLHYY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 323 TIGQRQGLRLPGG-PWYVVEKDTKNNVVFVSRNYysiDKRRRIFRVGSLRWNSGKPSGKVRELRCKVRHGPGFYSCSFEM 401
Cdd:COG0482 235 TIGQRKGLGIGGGePLYVVGKDPETNTVIVGQGE---ALYSRELTAEDVNWISGEPPEEPLRCTAKIRYRQPPVPATLTP 311
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 145336613 402 EGDGDVaVVHLDEDDQGLAAGQFAAFYEGTTCIGSGVILESW 443
Cdd:COG0482 312 LEDGRV-RVEFDEPQRAVTPGQSAVFYDGDRVLGGGIIERTE 352
|
|
| mnmA |
PRK00143 |
tRNA-specific 2-thiouridylase MnmA; Reviewed |
83-439 |
3.97e-139 |
|
tRNA-specific 2-thiouridylase MnmA; Reviewed
Pssm-ID: 234664 [Multi-domain] Cd Length: 346 Bit Score: 404.07 E-value: 3.97e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 83 RVAVLLSGGVDSSVALRLLHAAGHSCTAFYLKIWfQEGFENFWNQCPWEDDLKYAKHVCEQVDVPLEVVHLTDEYWERVV 162
Cdd:PRK00143 2 RVVVGMSGGVDSSVAAALLKEQGYEVIGVFMKLW-DDDDETGKGGCCAEEDIADARRVADKLGIPHYVVDFEKEFWDRVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 163 SYIIEEYRCGRTPNPDVLCNTRIKFGAFMDAISDMEYDYVGSGHYAKVVHPPadqndassvlELSQ--DMVKDQTYFLSH 240
Cdd:PRK00143 81 DYFLDEYKAGRTPNPCVLCNKEIKFKAFLEYARELGADYIATGHYARIRDGR----------ELLRgvDPNKDQSYFLYQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 241 LSQTQLKRLLFPLGCVKKDEVRKLATQFDLPNKDRKDSQGICFLGKIKFSDFVCRHIGEMEGIILEAEsGDFLGNHRGFW 320
Cdd:PRK00143 151 LTQEQLAKLLFPLGELTKPEVREIAEEAGLPVAKKKDSQGICFIGERDYRDFLKRYLPAQPGEIVDLD-GKVLGEHKGLM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 321 FYTIGQRQGLRLPGG--PWYVVEKDTKNNVVFVSRNYYSidkRRRIFRVGSLRWNSGKPSGKVRELRCKVRHGPGFYSCS 398
Cdd:PRK00143 230 YYTIGQRKGLGIGGDgePWYVVGKDPETNTVVVGQGEAL---YSRELIASDLNWVGGEPPEEPFECTAKIRYRQKPVPAT 306
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 145336613 399 FEMEGDGdvAVVHLDEDDQGLAAGQFAAFYEGTTCIGSGVI 439
Cdd:PRK00143 307 VELEDDR--VEVEFDEPQRAVTPGQAAVFYDGDRVLGGGII 345
|
|
| trmU |
TIGR00420 |
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ... |
83-439 |
2.42e-125 |
|
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: 369.41 E-value: 2.42e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 83 RVAVLLSGGVDSSVALRLLHAAGHSCTAFYLKIWFQEGFENFWNqCPWEDDLKYAKHVCEQVDVPLEVVHLTDEYWERVV 162
Cdd:TIGR00420 2 KVIVGLSGGVDSSVSAYLLKQQGYEVVGVFMKNWEEDDKNDGHG-CTSAEDLRDAQAICEKLGIPLEKVNFQKEYWNKVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 163 SYIIEEYRCGRTPNPDVLCNTRIKFGAFMD-AISDMEYDYVGSGHYAKVvhppaDQNDASSVLELSQDMVKDQTYFLSHL 241
Cdd:TIGR00420 81 EPFIQEYKEGRTPNPDILCNKFIKFGAFLEyAAELLGNDKIATGHYARI-----AEIEGKSLLLRALDKNKDQSYFLYHL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 242 SQTQLKRLLFPLGCVKKDEVRKLATQFDLPNKDRKDSQGICFLGKIKFSDFVCRHIGEMEGIILEAESGDFLGNHRGFWF 321
Cdd:TIGR00420 156 SHEQLAKLLFPLGELLKPEVRQIAKNAGLPTAEKKDSQGICFIGERKFRDFLKKYLPVKPGVIITVDGQSVIGEHDGLWF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 322 YTIGQRQGLRLPG--GPWYVVEKDTKNNVVFVSRNYYSIDKRRriFRVGSLRWNSGKPsgKVRELRC--KVRHGPGFYSC 397
Cdd:TIGR00420 236 YTIGQRKGLGIGGaaEPWFVVEKDLETNELVVSHGKPDLASRG--LLAQQFHWLDDEP--NPFEMRCtvKIRYRQVPVQC 311
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 145336613 398 SFEMEGDgDVAVVHLDEDDQGLAAGQFAAFYEGTTCIGSGVI 439
Cdd:TIGR00420 312 KLKLLDD-NLIEVIFDEPQAGVTPGQSAVLYKGDICLGGGII 352
|
|
| tRNA_Me_trans |
pfam03054 |
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ... |
82-286 |
2.83e-113 |
|
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: 333.07 E-value: 2.83e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 82 LRVAVLLSGGVDSSVALRLLHAAGHSCTAFYLKIWFQEGFENFWNQCPWEDDLKYAKHVCEQVDVPLEVVHLTDEYWERV 161
Cdd:pfam03054 1 MKVVVAMSGGVDSSVAAYLLKEQGHNVIGVFMKNWDEEQSLDEEGKCCSEEDLADAQRVCEQLGIPLYVVNFEKEYWEDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 162 VSYIIEEYRCGRTPNPDVLCNTRIKFGAFMD-AISDMEYDYVGSGHYAKVVHPpadqNDASSVLELSQDMVKDQTYFLSH 240
Cdd:pfam03054 81 FEPFLDEYKNGRTPNPDVLCNKEIKFGALLDyALENLGADYVATGHYARVSLN----KDGGSELLRALDKNKDQSYFLST 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 145336613 241 LSQTQLKRLLFPLGCVKKDEVRKLATQFDLPNKDRKDSQGICFLGK 286
Cdd:pfam03054 157 LSQEQLEKLLFPLGELTKEEVRKIAKEAGLATAKKKDSQGICFIGK 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 ... |
83-439 |
2.32e-164 |
|
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: 468.52 E-value: 2.32e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 83 RVAVLLSGGVDSSVALRLLHAAGHSCTAFYLKIWFQEgfENFWNQCPWEDDLKYAKHVCEQVDVPLEVVHLTDEYWERVV 162
Cdd:cd01998 1 KVAVAMSGGVDSSVAAALLKEQGYDVIGVFMKNWDDE--DNEKGGCCSEEDIEDARRVADQLGIPLYVVDFSEEYWERVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 163 SYIIEEYRCGRTPNPDVLCNTRIKFGAFMDAISDMEYDYVGSGHYAKVVHPPADQndasSVLELSQDMVKDQTYFLSHLS 242
Cdd:cd01998 79 DPFLEEYKAGRTPNPDVLCNREIKFGALLDAAKKLGADYIATGHYARIEEDNRGR----YRLLRAVDPNKDQSYFLSRLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 243 QTQLKRLLFPLGCVKKDEVRKLATQFDLPNKDRKDSQGICFLGKIKFSDFVCRHIGE-MEGIILEAEsGDFLGNHRGFWF 321
Cdd:cd01998 155 QEQLSRTLFPLGHLTKSEVREIAREAGLPVAEKKDSQGICFIGKRDFRDFLKEYLPEkLPGPIVDID-GKVLGEHKGLWF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 322 YTIGQRQGLRLP-GGPWYVVEKDTKNNVVFVSRNYYSIDKRRriFRVGSLRWNSGKPSGKVRELRCKVRHGPGFYSCSFE 400
Cdd:cd01998 234 YTIGQRKGLGIAaGEPLYVVKKDPEKNIVVVGPGHPALFSDT--LRASDLNWISPEPPLEPLECEAKIRYRQPPVPCTVT 311
|
330 340 350
....*....|....*....|....*....|....*....
gi 145336613 401 MEGDGdVAVVHLDEDDQGLAAGQFAAFYEGTTCIGSGVI 439
Cdd:cd01998 312 PLDDG-RLKVEFDEPQRAVTPGQAAVFYDGDEVLGGGII 349
|
|
| MnmA |
COG0482 |
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ... |
83-443 |
5.09e-144 |
|
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: 417.15 E-value: 5.09e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 83 RVAVLLSGGVDSSVALRLLHAAGHSCTAFYLKIWFQEGFENFwNQCPWEDDLKYAKHVCEQVDVPLEVVHLTDEYWERVV 162
Cdd:COG0482 2 RVVVGMSGGVDSSVAAALLKEQGYEVIGVTMKLWDDDDASGS-GGCCSLEDIEDARRVADKLGIPHYVVDFEEEFKDRVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 163 SYIIEEYRCGRTPNPDVLCNTRIKFGAFMDAISDMEYDYVGSGHYAKVVHppadqNDASSVLELSQDMVKDQTYFLSHLS 242
Cdd:COG0482 81 DYFLDEYLAGRTPNPCVLCNREIKFGALLEKALELGADYIATGHYARVEE-----KDGRYELLRGVDPNKDQSYFLYRLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 243 QTQLKRLLFPLGCVKKDEVRKLATQFDLPNKDRKDSQGICFLGKIKFSDFVCRHIGEMEGIILEaESGDFLGNHRGFWFY 322
Cdd:COG0482 156 QEQLSKTLFPLGELTKPEVREIAEELGLPVADKKDSQGICFIGDGDYRDFLERYLPEKPGDIVD-LDGKVLGEHDGLHYY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 323 TIGQRQGLRLPGG-PWYVVEKDTKNNVVFVSRNYysiDKRRRIFRVGSLRWNSGKPSGKVRELRCKVRHGPGFYSCSFEM 401
Cdd:COG0482 235 TIGQRKGLGIGGGePLYVVGKDPETNTVIVGQGE---ALYSRELTAEDVNWISGEPPEEPLRCTAKIRYRQPPVPATLTP 311
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 145336613 402 EGDGDVaVVHLDEDDQGLAAGQFAAFYEGTTCIGSGVILESW 443
Cdd:COG0482 312 LEDGRV-RVEFDEPQRAVTPGQSAVFYDGDRVLGGGIIERTE 352
|
|
| mnmA |
PRK00143 |
tRNA-specific 2-thiouridylase MnmA; Reviewed |
83-439 |
3.97e-139 |
|
tRNA-specific 2-thiouridylase MnmA; Reviewed
Pssm-ID: 234664 [Multi-domain] Cd Length: 346 Bit Score: 404.07 E-value: 3.97e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 83 RVAVLLSGGVDSSVALRLLHAAGHSCTAFYLKIWfQEGFENFWNQCPWEDDLKYAKHVCEQVDVPLEVVHLTDEYWERVV 162
Cdd:PRK00143 2 RVVVGMSGGVDSSVAAALLKEQGYEVIGVFMKLW-DDDDETGKGGCCAEEDIADARRVADKLGIPHYVVDFEKEFWDRVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 163 SYIIEEYRCGRTPNPDVLCNTRIKFGAFMDAISDMEYDYVGSGHYAKVVHPPadqndassvlELSQ--DMVKDQTYFLSH 240
Cdd:PRK00143 81 DYFLDEYKAGRTPNPCVLCNKEIKFKAFLEYARELGADYIATGHYARIRDGR----------ELLRgvDPNKDQSYFLYQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 241 LSQTQLKRLLFPLGCVKKDEVRKLATQFDLPNKDRKDSQGICFLGKIKFSDFVCRHIGEMEGIILEAEsGDFLGNHRGFW 320
Cdd:PRK00143 151 LTQEQLAKLLFPLGELTKPEVREIAEEAGLPVAKKKDSQGICFIGERDYRDFLKRYLPAQPGEIVDLD-GKVLGEHKGLM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 321 FYTIGQRQGLRLPGG--PWYVVEKDTKNNVVFVSRNYYSidkRRRIFRVGSLRWNSGKPSGKVRELRCKVRHGPGFYSCS 398
Cdd:PRK00143 230 YYTIGQRKGLGIGGDgePWYVVGKDPETNTVVVGQGEAL---YSRELIASDLNWVGGEPPEEPFECTAKIRYRQKPVPAT 306
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 145336613 399 FEMEGDGdvAVVHLDEDDQGLAAGQFAAFYEGTTCIGSGVI 439
Cdd:PRK00143 307 VELEDDR--VEVEFDEPQRAVTPGQAAVFYDGDRVLGGGII 345
|
|
| trmU |
TIGR00420 |
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ... |
83-439 |
2.42e-125 |
|
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: 369.41 E-value: 2.42e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 83 RVAVLLSGGVDSSVALRLLHAAGHSCTAFYLKIWFQEGFENFWNqCPWEDDLKYAKHVCEQVDVPLEVVHLTDEYWERVV 162
Cdd:TIGR00420 2 KVIVGLSGGVDSSVSAYLLKQQGYEVVGVFMKNWEEDDKNDGHG-CTSAEDLRDAQAICEKLGIPLEKVNFQKEYWNKVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 163 SYIIEEYRCGRTPNPDVLCNTRIKFGAFMD-AISDMEYDYVGSGHYAKVvhppaDQNDASSVLELSQDMVKDQTYFLSHL 241
Cdd:TIGR00420 81 EPFIQEYKEGRTPNPDILCNKFIKFGAFLEyAAELLGNDKIATGHYARI-----AEIEGKSLLLRALDKNKDQSYFLYHL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 242 SQTQLKRLLFPLGCVKKDEVRKLATQFDLPNKDRKDSQGICFLGKIKFSDFVCRHIGEMEGIILEAESGDFLGNHRGFWF 321
Cdd:TIGR00420 156 SHEQLAKLLFPLGELLKPEVRQIAKNAGLPTAEKKDSQGICFIGERKFRDFLKKYLPVKPGVIITVDGQSVIGEHDGLWF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 322 YTIGQRQGLRLPG--GPWYVVEKDTKNNVVFVSRNYYSIDKRRriFRVGSLRWNSGKPsgKVRELRC--KVRHGPGFYSC 397
Cdd:TIGR00420 236 YTIGQRKGLGIGGaaEPWFVVEKDLETNELVVSHGKPDLASRG--LLAQQFHWLDDEP--NPFEMRCtvKIRYRQVPVQC 311
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 145336613 398 SFEMEGDgDVAVVHLDEDDQGLAAGQFAAFYEGTTCIGSGVI 439
Cdd:TIGR00420 312 KLKLLDD-NLIEVIFDEPQAGVTPGQSAVLYKGDICLGGGII 352
|
|
| tRNA_Me_trans |
pfam03054 |
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ... |
82-286 |
2.83e-113 |
|
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: 333.07 E-value: 2.83e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 82 LRVAVLLSGGVDSSVALRLLHAAGHSCTAFYLKIWFQEGFENFWNQCPWEDDLKYAKHVCEQVDVPLEVVHLTDEYWERV 161
Cdd:pfam03054 1 MKVVVAMSGGVDSSVAAYLLKEQGHNVIGVFMKNWDEEQSLDEEGKCCSEEDLADAQRVCEQLGIPLYVVNFEKEYWEDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 162 VSYIIEEYRCGRTPNPDVLCNTRIKFGAFMD-AISDMEYDYVGSGHYAKVVHPpadqNDASSVLELSQDMVKDQTYFLSH 240
Cdd:pfam03054 81 FEPFLDEYKNGRTPNPDVLCNKEIKFGALLDyALENLGADYVATGHYARVSLN----KDGGSELLRALDKNKDQSYFLST 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 145336613 241 LSQTQLKRLLFPLGCVKKDEVRKLATQFDLPNKDRKDSQGICFLGK 286
Cdd:pfam03054 157 LSQEQLEKLLFPLGELTKEEVRKIAKEAGLATAKKKDSQGICFIGK 202
|
|
| PRK14664 |
PRK14664 |
tRNA-specific 2-thiouridylase MnmA; Provisional |
77-439 |
4.80e-41 |
|
tRNA-specific 2-thiouridylase MnmA; Provisional
Pssm-ID: 173127 [Multi-domain] Cd Length: 362 Bit Score: 150.87 E-value: 4.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 77 MPEKPLRVAVLLSGGVDSSVALRLLHAAGHSCTAFYLKIWfqegfenfwnqcpwEDDLKYAKHVCEQVDVPLEVVHLTDE 156
Cdd:PRK14664 1 MKESKKRVLVGMSGGIDSTATCLMLQEQGYEIVGVTMRVW--------------GDEPQDARELAARMGIEHYVADERVP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 157 YWERVVSYIIEEYRCGRTPNPDVLCNTRIKFGAFMDAISDMEYDYVGSGHYAKVvhppaDQNDASSVLELSQDMVKDQTY 236
Cdd:PRK14664 67 FKDTIVKNFIDEYRQGRTPNPCVMCNPLFKFRMLIEWADKLGCAWIATGHYSRL-----EERNGHIYIVAGDDDKKDQSY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 237 FLSHLSQTQLKRLLFPLGCVKKDEVRKLATQFDLPNKDRK-DSQGICFLgKIKFSDFVCRHIGEME-----GIILEAEsG 310
Cdd:PRK14664 142 FLWRLGQDILRRCIFPLGNYTKQTVREYLREKGYEAKSKEgESMEVCFI-KGDYRDFLREQCPELDtevgpGWFVNSE-G 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 311 DFLGNHRGFWFYTIGQRQGLRLP-GGPWYVVEKDTKNNVVFVS-----RNYYSIDKRRRIFRVGSLRwnsgkpsgKVREL 384
Cdd:PRK14664 220 VKLGQHKGFPYYTIGQRKGLEIAlGKPAYVLKINPQKNTVMLGdaeqlKAEYMLAEQDNIVDEQELF--------ACPDL 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 145336613 385 RCKVRHGPGFYSCSFEMEGDGDVAVVHLDEdDQGLAAGQFAAFYEGTTCIGSGVI 439
Cdd:PRK14664 292 AVRIRYRSRPIPCRVKRLEDGRLLVRFLAE-ASAIAPGQSAVFYEGRRVLGGAFI 345
|
|
| mnmA |
PRK14665 |
tRNA-specific 2-thiouridylase MnmA; Provisional |
77-441 |
2.78e-40 |
|
tRNA-specific 2-thiouridylase MnmA; Provisional
Pssm-ID: 173128 [Multi-domain] Cd Length: 360 Bit Score: 148.54 E-value: 2.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 77 MPEKPLRVAVLLSGGVDSSVALRLLHAAGHSCTAFYLKIWFQEGFENFwnqcpweddLKYAKHVCEQVDVPlevvHLT-- 154
Cdd:PRK14665 1 MMEKNKRVLLGMSGGTDSSVAAMLLLEAGYEVTGVTFRFYEFNGSTEY---------LEDARALAERLGIG----HITyd 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 155 --DEYWERVVSYIIEEYRCGRTPNPDVLCNTRIKFgAFMDAISD-MEYDYVGSGHYAKVVhppadQNDASSVLELSQDMV 231
Cdd:PRK14665 68 arKVFRKQIIDYFIDEYMSGHTPVPCTLCNNYLKW-PLLAKIADeMGIFYLATGHYVRKQ-----WIDGNYYITPAEDVD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 232 KDQTYFLSHLSQTQLKRLLFPLGCVKKDEVRKLATQ--FDLPNKdRKDSQGICFLgKIKFSDFV-------CRHIGEMEG 302
Cdd:PRK14665 142 KDQSFFLWGLRQEILQRMLLPMGGMTKSEARAYAAErgFEKVAK-KRDSLGVCFC-PMDYRSFLkkclcdeSGDKNRNIY 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 303 IILEA-----ESGDFLGNHRGFWFYTIGQRQGLRLPGGPWYVVEK--DTKNNVVFVSRNyySIDKRRRIFRvgslRWNSG 375
Cdd:PRK14665 220 RKVERgrfldESGNFIAWHEGYPFYTIGQRRGLGIQLNRAVFVKEihPETNEVVLASLK--ALEKTEMWLK----DWNIV 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145336613 376 KPSgkvRELRC-----KVRHGPGFYSCSFEMEGDGDVAvVHLDEDDQGLAAGQFAAFYEGTTCIGSGVILE 441
Cdd:PRK14665 294 NES---RLLGCddiivKIRYRKQENHCTVTITPDNLLH-VQLHEPLTAIAEGQAAAFYKDGLLLGGGIITM 360
|
|
| tRNA_Me_trans_M |
pfam20259 |
tRNA methyl transferase PRC-barrel domain; This family represents a central PRC-barrel domain ... |
290-353 |
9.17e-29 |
|
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: 108.08 E-value: 9.17e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145336613 290 SDFVCRHIGEMEGIILEAESGDFLGNHRGFWFYTIGQRQGLRLPG--GPWYVVEKDTKNNVVFVSR 353
Cdd:pfam20259 1 KDFLKEYLPVKPGDIIDIDTGEVLGEHEGIWFYTIGQRKGLGIGGygEPWYVVEKDPKKNTVYVGR 66
|
|
| tRNA_Me_trans_C |
pfam20258 |
Aminomethyltransferase beta-barrel domain; This domain is found at the C-terminus of tRNA ... |
362-439 |
6.10e-27 |
|
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: 103.51 E-value: 6.10e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145336613 362 RRIFRVGSLRWNSGKPSGKVRELRCKVRHGPGFYSCSFEMEGDGDVaVVHLDEDDQGLAAGQFAAFYEGTTCIGSGVI 439
Cdd:pfam20258 1 SDGLRAKDPNWLGDKPPTEPLECTVKVRHRQPPVPCVVELIDDETV-EVHFDEPVRAVTPGQAAVFYDGDRCLGGGII 77
|
|
| TtuA-like |
cd01993 |
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ... |
77-157 |
3.18e-06 |
|
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: 47.71 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 77 MPEKPLRVAVLLSGGVDSSVALRLLHAAGHSCTAFYLKIwfqeGFENFWnqcpwEDDLKYAKHVCEQVDVPLEVVHLTDE 156
Cdd:cd01993 4 MFEKDDKILVAVSGGKDSLALLAVLKKLGYNVEALYINL----GIGEYS-----EKSEEVVKKLAEKLNLPLHVVDLKEE 74
|
.
gi 145336613 157 Y 157
Cdd:cd01993 75 Y 75
|
|
| Asn_synthase_B_C |
cd01991 |
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
83-156 |
7.00e-06 |
|
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or synthetase) B is always associated with an N-terminal amidotransferase domain. Family members that contain this domain catalyze the conversion of aspartate to asparagine. Asparagine synthase B catalyzes the synthesis of asparagine from aspartate, Mg(2+)ATP, and glutamine. The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase.
Pssm-ID: 467495 [Multi-domain] Cd Length: 224 Bit Score: 47.27 E-value: 7.00e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145336613 83 RVAVLLSGGVDSSVALRLLHAAG-----HSCTAfylkiwfqeGFENfwnqcPWEDDLKYAKHVCEQVDVPLEVVHLTDE 156
Cdd:cd01991 4 PVGVLLSGGLDSSLIAALAARLLpetpiDLFTV---------GFEG-----SPTPDRAAARRVAEELGTEHHEVEVTIE 68
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
84-168 |
3.76e-05 |
|
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis
Pssm-ID: 440136 [Multi-domain] Cd Length: 558 Bit Score: 46.37 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 84 VAVLLSGGVDSS--VAL--RLLHAAGHSCTAfylkiwfqeGFENfwnqcPWEDDLKYAKHVCEQVDVPLEVVHLTD---- 155
Cdd:COG0367 259 VGAFLSGGLDSSaiAALaaRLSKGPLKTFSI---------GFED-----SAYDESPYARAVAEHLGTEHHEVTVTPedll 324
|
90
....*....|...
gi 145336613 156 EYWERVVsYIIEE 168
Cdd:COG0367 325 DALPDLV-WHLDE 336
|
|
| TilS |
COG0037 |
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ... |
76-271 |
5.26e-04 |
|
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: 41.74 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 76 SMPEKPLRVAVLLSGGVDSSVALRLLHA----AGHSCTAFYLkiwfQEGFENFwnqcpWEDDLKYAKHVCEQVDVPLEVV 151
Cdd:COG0037 10 RLLEPGDRILVAVSGGKDSLALLHLLAKlrrrLGFELVAVHV----DHGLREE-----SDEDAEFVAELCEELGIPLHVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 152 HLTDEYWERVVSYIIEEYrCGrtpnpdvlcntRIKFGAFMDAISDMEYDYVGSGHyakvvHppADqndassvlelsqDMV 231
Cdd:COG0037 81 RVDVPAIAKKEGKSPEAA-AR-----------RARYGALYELARELGADKIATGH-----H--LD------------DQA 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 145336613 232 kdQTYFLSHLSQTQLKRL--------LF-----PLGCVKKDEVRKLATQFDLP 271
Cdd:COG0037 130 --ETFLLNLLRGSGLAGLagmppsrgGGvrlirPLLYVSRKEIEAYAKENGLP 180
|
|
| Asn_synthase |
pfam00733 |
Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
83-168 |
7.84e-04 |
|
Asparagine synthase; This family is always found associated with pfam00310. Members of this family catalyze the conversion of aspartate to asparagine.
Pssm-ID: 395594 [Multi-domain] Cd Length: 279 Bit Score: 41.45 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 83 RVAVLLSGGVDSSV----ALRLLHAAGHSCTAfylkiwfqeGFENFWNqcpweDDLKYAKHVCEQVDVPLEVVHLTDE-- 156
Cdd:pfam00733 19 PVGAFLSGGLDSSSiaalAARQSPSPLHTFSI---------GFEGRGY-----DEAPYAREVAEHLGTDHHELVVTPEdl 84
|
90
....*....|....
gi 145336613 157 --YWERVVsYIIEE 168
Cdd:pfam00733 85 ldALPDVI-WHLDE 97
|
|
| GMP_synthase_C |
cd01997 |
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ... |
83-104 |
8.26e-03 |
|
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: 38.29 E-value: 8.26e-03
|
| PRK13795 |
PRK13795 |
hypothetical protein; Provisional |
82-161 |
8.40e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237510 [Multi-domain] Cd Length: 636 Bit Score: 38.82 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336613 82 LRVAVLLSGGVDSSVALRLLHAAGHSCTAFYLK--IWFQEGFENfwnqcpweddlkyAKHVCEQVDVPLEVVHLTDEYWE 159
Cdd:PRK13795 244 LPVSVSFSGGKDSLVVLDLAREALKDFKAFFNNtgLEFPETVEN-------------VKEVAEEYGIELIEADAGDAFWR 310
|
..
gi 145336613 160 RV 161
Cdd:PRK13795 311 AV 312
|
|
| QueC |
pfam06508 |
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ... |
83-154 |
8.40e-03 |
|
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis of 7-carboxy-7-deazaguanine. They catalyze the conversion of 7-deaza-7-carboxyguanine to preQ0.
Pssm-ID: 428982 [Multi-domain] Cd Length: 210 Bit Score: 37.60 E-value: 8.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145336613 83 RVAVLLSGGVDSSVALRLLHAAGHSCTAfylkIWFQEGfenfwnQcPWEDDLKYAKHVCEQVDVPLEVVHLT 154
Cdd:pfam06508 1 KAVVLLSGGLDSTTCLAWAKKEGYEVYA----LSFDYG------Q-RHRKELECAKKIAKALGVEHKILDLD 61
|
|
| |
