|
Name |
Accession |
Description |
Interval |
E-value |
| MnmA |
COG0482 |
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ... |
4-365 |
0e+00 |
|
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: 630.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 4 QRVVVGMSGGVDSSVTAWLLKEQGYDVVGLFMKNWEDDD--DGEYCSTRQDWIDVVSVADLIGIDVEAVNFAAEYKDRVF 81
Cdd:COG0482 1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVTMKLWDDDDasGSGGCCSLEDIEDARRVADKLGIPHYVVDFEEEFKDRVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 82 AEFLREYSAGRTPNPDVLCNAEIKFKAFLDHAMSLGAETIATGHYARVREREGRFELLKAFDHTKDQSYFLHRLNQAQLS 161
Cdd:COG0482 81 DYFLDEYLAGRTPNPCVLCNREIKFGALLEKALELGADYIATGHYARVEEKDGRYELLRGVDPNKDQSYFLYRLTQEQLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 162 KTLFPLGEMPKTRVREIAEQIGLPNAKKKDSTGICFIGERPFRDFLNRYLPTRPGPMKTPDGKRVGEHIGLAFYTFGQRK 241
Cdd:COG0482 161 KTLFPLGELTKPEVREIAEELGLPVADKKDSQGICFIGDGDYRDFLERYLPEKPGDIVDLDGKVLGEHDGLHYYTIGQRK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 242 GIGLGGskdgsGEPWFVAGKDIASNTLYVAQGHehpWLLSRELVAGNVSWVAGEPPADGFACGAKTRYRQADAPCsfaRA 321
Cdd:COG0482 241 GLGIGG-----GEPLYVVGKDPETNTVIVGQGE---ALYSRELTAEDVNWISGEPPEEPLRCTAKIRYRQPPVPA---TL 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 661253701 322 KAGEAGEARFSlgFDTPQWAVTPGQSAVLYDGEICLGGGIIESV 365
Cdd:COG0482 310 TPLEDGRVRVE--FDEPQRAVTPGQSAVFYDGDRVLGGGIIERT 351
|
|
| mnmA |
PRK00143 |
tRNA-specific 2-thiouridylase MnmA; Reviewed |
4-363 |
0e+00 |
|
tRNA-specific 2-thiouridylase MnmA; Reviewed
Pssm-ID: 234664 [Multi-domain] Cd Length: 346 Bit Score: 617.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 4 QRVVVGMSGGVDSSVTAWLLKEQGYDVVGLFMKNWEDDDDG--EYCSTRQDWIDVVSVADLIGIDVEAVNFAAEYKDRVF 81
Cdd:PRK00143 1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVFMKLWDDDDETgkGGCCAEEDIADARRVADKLGIPHYVVDFEKEFWDRVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 82 AEFLREYSAGRTPNPDVLCNAEIKFKAFLDHAMSLGAETIATGHYARVREREgrfELLKAFDHTKDQSYFLHRLNQAQLS 161
Cdd:PRK00143 81 DYFLDEYKAGRTPNPCVLCNKEIKFKAFLEYARELGADYIATGHYARIRDGR---ELLRGVDPNKDQSYFLYQLTQEQLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 162 KTLFPLGEMPKTRVREIAEQIGLPNAKKKDSTGICFIGERPFRDFLNRYLPTRPGPMKTPDGKRVGEHIGLAFYTFGQRK 241
Cdd:PRK00143 158 KLLFPLGELTKPEVREIAEEAGLPVAKKKDSQGICFIGERDYRDFLKRYLPAQPGEIVDLDGKVLGEHKGLMYYTIGQRK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 242 GIGLGgskdGSGEPWFVAGKDIASNTLYVAQGhehPWLLSRELVAGNVSWVAGEPPADGFACGAKTRYRQADAPCSFara 321
Cdd:PRK00143 238 GLGIG----GDGEPWYVVGKDPETNTVVVGQG---EALYSRELIASDLNWVGGEPPEEPFECTAKIRYRQKPVPATV--- 307
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 661253701 322 kagEAGEARFSLGFDTPQWAVTPGQSAVLYDGEICLGGGIIE 363
Cdd:PRK00143 308 ---ELEDDRVEVEFDEPQRAVTPGQAAVFYDGDRVLGGGIIE 346
|
|
| MnmA_TRMU-like |
cd01998 |
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ... |
5-362 |
0e+00 |
|
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: 553.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 5 RVVVGMSGGVDSSVTAWLLKEQGYDVVGLFMKNWEDDDDG-EYCSTRQDWIDVVSVADLIGIDVEAVNFAAEYKDRVFAE 83
Cdd:cd01998 1 KVAVAMSGGVDSSVAAALLKEQGYDVIGVFMKNWDDEDNEkGGCCSEEDIEDARRVADQLGIPLYVVDFSEEYWERVFDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 84 FLREYSAGRTPNPDVLCNAEIKFKAFLDHAMSLGAETIATGHYARVRERE-GRFELLKAFDHTKDQSYFLHRLNQAQLSK 162
Cdd:cd01998 81 FLEEYKAGRTPNPDVLCNREIKFGALLDAAKKLGADYIATGHYARIEEDNrGRYRLLRAVDPNKDQSYFLSRLSQEQLSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 163 TLFPLGEMPKTRVREIAEQIGLPNAKKKDSTGICFIGERPFRDFLNRYLPTR-PGPMKTPDGKRVGEHIGLAFYTFGQRK 241
Cdd:cd01998 161 TLFPLGHLTKSEVREIAREAGLPVAEKKDSQGICFIGKRDFRDFLKEYLPEKlPGPIVDIDGKVLGEHKGLWFYTIGQRK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 242 GIGLggskdGSGEPWFVAGKDIASNTLYVAQGheHPWLLSRELVAGNVSWVAGEPPADGFACGAKTRYRQADAPCSFARa 321
Cdd:cd01998 241 GLGI-----AAGEPLYVVKKDPEKNIVVVGPG--HPALFSDTLRASDLNWISPEPPLEPLECEAKIRYRQPPVPCTVTP- 312
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 661253701 322 kageAGEARFSLGFDTPQWAVTPGQSAVLYDGEICLGGGII 362
Cdd:cd01998 313 ----LDDGRLKVEFDEPQRAVTPGQAAVFYDGDEVLGGGII 349
|
|
| trmU |
TIGR00420 |
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ... |
4-362 |
4.14e-165 |
|
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: 466.48 E-value: 4.14e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 4 QRVVVGMSGGVDSSVTAWLLKEQGYDVVGLFMKNWEDDDDGEY--CSTRQDWIDVVSVADLIGIDVEAVNFAAEYKDRVF 81
Cdd:TIGR00420 1 KKVIVGLSGGVDSSVSAYLLKQQGYEVVGVFMKNWEEDDKNDGhgCTSAEDLRDAQAICEKLGIPLEKVNFQKEYWNKVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 82 AEFLREYSAGRTPNPDVLCNAEIKFKAFLDHAMS-LGAETIATGHYARVREREGRFELLKAFDHTKDQSYFLHRLNQAQL 160
Cdd:TIGR00420 81 EPFIQEYKEGRTPNPDILCNKFIKFGAFLEYAAElLGNDKIATGHYARIAEIEGKSLLLRALDKNKDQSYFLYHLSHEQL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 161 SKTLFPLGEMPKTRVREIAEQIGLPNAKKKDSTGICFIGERPFRDFLNRYLPTRPGPMKTPDGKRV-GEHIGLAFYTFGQ 239
Cdd:TIGR00420 161 AKLLFPLGELLKPEVRQIAKNAGLPTAEKKDSQGICFIGERKFRDFLKKYLPVKPGVIITVDGQSViGEHDGLWFYTIGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 240 RKGIGLGGSKdgsgEPWFVAGKDIASNTLYVaqGHEHPWLLSRELVAGNVSWVAGEPPADGFACGAKTRYRQADAPCSFA 319
Cdd:TIGR00420 241 RKGLGIGGAA----EPWFVVEKDLETNELVV--SHGKPDLASRGLLAQQFHWLDDEPNPFEMRCTVKIRYRQVPVQCKLK 314
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 661253701 320 RAKageagEARFSLGFDTPQWAVTPGQSAVLYDGEICLGGGII 362
Cdd:TIGR00420 315 LLD-----DNLIEVIFDEPQAGVTPGQSAVLYKGDICLGGGII 352
|
|
| tRNA_Me_trans |
pfam03054 |
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ... |
4-200 |
4.25e-111 |
|
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: 323.44 E-value: 4.25e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 4 QRVVVGMSGGVDSSVTAWLLKEQGYDVVGLFMKNWEDD---DDGEYCSTRQDWIDVVSVADLIGIDVEAVNFAAEYKDRV 80
Cdd:pfam03054 1 MKVVVAMSGGVDSSVAAYLLKEQGHNVIGVFMKNWDEEqslDEEGKCCSEEDLADAQRVCEQLGIPLYVVNFEKEYWEDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 81 FAEFLREYSAGRTPNPDVLCNAEIKFKAFLDHA-MSLGAETIATGHYARVRERE-GRFELLKAFDHTKDQSYFLHRLNQA 158
Cdd:pfam03054 81 FEPFLDEYKNGRTPNPDVLCNKEIKFGALLDYAlENLGADYVATGHYARVSLNKdGGSELLRALDKNKDQSYFLSTLSQE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 661253701 159 QLSKTLFPLGEMPKTRVREIAEQIGLPNAKKKDSTGICFIGE 200
Cdd:pfam03054 161 QLEKLLFPLGELTKEEVRKIAKEAGLATAKKKDSQGICFIGK 202
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MnmA |
COG0482 |
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ... |
4-365 |
0e+00 |
|
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: 630.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 4 QRVVVGMSGGVDSSVTAWLLKEQGYDVVGLFMKNWEDDD--DGEYCSTRQDWIDVVSVADLIGIDVEAVNFAAEYKDRVF 81
Cdd:COG0482 1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVTMKLWDDDDasGSGGCCSLEDIEDARRVADKLGIPHYVVDFEEEFKDRVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 82 AEFLREYSAGRTPNPDVLCNAEIKFKAFLDHAMSLGAETIATGHYARVREREGRFELLKAFDHTKDQSYFLHRLNQAQLS 161
Cdd:COG0482 81 DYFLDEYLAGRTPNPCVLCNREIKFGALLEKALELGADYIATGHYARVEEKDGRYELLRGVDPNKDQSYFLYRLTQEQLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 162 KTLFPLGEMPKTRVREIAEQIGLPNAKKKDSTGICFIGERPFRDFLNRYLPTRPGPMKTPDGKRVGEHIGLAFYTFGQRK 241
Cdd:COG0482 161 KTLFPLGELTKPEVREIAEELGLPVADKKDSQGICFIGDGDYRDFLERYLPEKPGDIVDLDGKVLGEHDGLHYYTIGQRK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 242 GIGLGGskdgsGEPWFVAGKDIASNTLYVAQGHehpWLLSRELVAGNVSWVAGEPPADGFACGAKTRYRQADAPCsfaRA 321
Cdd:COG0482 241 GLGIGG-----GEPLYVVGKDPETNTVIVGQGE---ALYSRELTAEDVNWISGEPPEEPLRCTAKIRYRQPPVPA---TL 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 661253701 322 KAGEAGEARFSlgFDTPQWAVTPGQSAVLYDGEICLGGGIIESV 365
Cdd:COG0482 310 TPLEDGRVRVE--FDEPQRAVTPGQSAVFYDGDRVLGGGIIERT 351
|
|
| mnmA |
PRK00143 |
tRNA-specific 2-thiouridylase MnmA; Reviewed |
4-363 |
0e+00 |
|
tRNA-specific 2-thiouridylase MnmA; Reviewed
Pssm-ID: 234664 [Multi-domain] Cd Length: 346 Bit Score: 617.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 4 QRVVVGMSGGVDSSVTAWLLKEQGYDVVGLFMKNWEDDDDG--EYCSTRQDWIDVVSVADLIGIDVEAVNFAAEYKDRVF 81
Cdd:PRK00143 1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVFMKLWDDDDETgkGGCCAEEDIADARRVADKLGIPHYVVDFEKEFWDRVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 82 AEFLREYSAGRTPNPDVLCNAEIKFKAFLDHAMSLGAETIATGHYARVREREgrfELLKAFDHTKDQSYFLHRLNQAQLS 161
Cdd:PRK00143 81 DYFLDEYKAGRTPNPCVLCNKEIKFKAFLEYARELGADYIATGHYARIRDGR---ELLRGVDPNKDQSYFLYQLTQEQLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 162 KTLFPLGEMPKTRVREIAEQIGLPNAKKKDSTGICFIGERPFRDFLNRYLPTRPGPMKTPDGKRVGEHIGLAFYTFGQRK 241
Cdd:PRK00143 158 KLLFPLGELTKPEVREIAEEAGLPVAKKKDSQGICFIGERDYRDFLKRYLPAQPGEIVDLDGKVLGEHKGLMYYTIGQRK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 242 GIGLGgskdGSGEPWFVAGKDIASNTLYVAQGhehPWLLSRELVAGNVSWVAGEPPADGFACGAKTRYRQADAPCSFara 321
Cdd:PRK00143 238 GLGIG----GDGEPWYVVGKDPETNTVVVGQG---EALYSRELIASDLNWVGGEPPEEPFECTAKIRYRQKPVPATV--- 307
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 661253701 322 kagEAGEARFSLGFDTPQWAVTPGQSAVLYDGEICLGGGIIE 363
Cdd:PRK00143 308 ---ELEDDRVEVEFDEPQRAVTPGQAAVFYDGDRVLGGGIIE 346
|
|
| MnmA_TRMU-like |
cd01998 |
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ... |
5-362 |
0e+00 |
|
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: 553.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 5 RVVVGMSGGVDSSVTAWLLKEQGYDVVGLFMKNWEDDDDG-EYCSTRQDWIDVVSVADLIGIDVEAVNFAAEYKDRVFAE 83
Cdd:cd01998 1 KVAVAMSGGVDSSVAAALLKEQGYDVIGVFMKNWDDEDNEkGGCCSEEDIEDARRVADQLGIPLYVVDFSEEYWERVFDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 84 FLREYSAGRTPNPDVLCNAEIKFKAFLDHAMSLGAETIATGHYARVRERE-GRFELLKAFDHTKDQSYFLHRLNQAQLSK 162
Cdd:cd01998 81 FLEEYKAGRTPNPDVLCNREIKFGALLDAAKKLGADYIATGHYARIEEDNrGRYRLLRAVDPNKDQSYFLSRLSQEQLSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 163 TLFPLGEMPKTRVREIAEQIGLPNAKKKDSTGICFIGERPFRDFLNRYLPTR-PGPMKTPDGKRVGEHIGLAFYTFGQRK 241
Cdd:cd01998 161 TLFPLGHLTKSEVREIAREAGLPVAEKKDSQGICFIGKRDFRDFLKEYLPEKlPGPIVDIDGKVLGEHKGLWFYTIGQRK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 242 GIGLggskdGSGEPWFVAGKDIASNTLYVAQGheHPWLLSRELVAGNVSWVAGEPPADGFACGAKTRYRQADAPCSFARa 321
Cdd:cd01998 241 GLGI-----AAGEPLYVVKKDPEKNIVVVGPG--HPALFSDTLRASDLNWISPEPPLEPLECEAKIRYRQPPVPCTVTP- 312
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 661253701 322 kageAGEARFSLGFDTPQWAVTPGQSAVLYDGEICLGGGII 362
Cdd:cd01998 313 ----LDDGRLKVEFDEPQRAVTPGQAAVFYDGDEVLGGGII 349
|
|
| trmU |
TIGR00420 |
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ... |
4-362 |
4.14e-165 |
|
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: 466.48 E-value: 4.14e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 4 QRVVVGMSGGVDSSVTAWLLKEQGYDVVGLFMKNWEDDDDGEY--CSTRQDWIDVVSVADLIGIDVEAVNFAAEYKDRVF 81
Cdd:TIGR00420 1 KKVIVGLSGGVDSSVSAYLLKQQGYEVVGVFMKNWEEDDKNDGhgCTSAEDLRDAQAICEKLGIPLEKVNFQKEYWNKVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 82 AEFLREYSAGRTPNPDVLCNAEIKFKAFLDHAMS-LGAETIATGHYARVREREGRFELLKAFDHTKDQSYFLHRLNQAQL 160
Cdd:TIGR00420 81 EPFIQEYKEGRTPNPDILCNKFIKFGAFLEYAAElLGNDKIATGHYARIAEIEGKSLLLRALDKNKDQSYFLYHLSHEQL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 161 SKTLFPLGEMPKTRVREIAEQIGLPNAKKKDSTGICFIGERPFRDFLNRYLPTRPGPMKTPDGKRV-GEHIGLAFYTFGQ 239
Cdd:TIGR00420 161 AKLLFPLGELLKPEVRQIAKNAGLPTAEKKDSQGICFIGERKFRDFLKKYLPVKPGVIITVDGQSViGEHDGLWFYTIGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 240 RKGIGLGGSKdgsgEPWFVAGKDIASNTLYVaqGHEHPWLLSRELVAGNVSWVAGEPPADGFACGAKTRYRQADAPCSFA 319
Cdd:TIGR00420 241 RKGLGIGGAA----EPWFVVEKDLETNELVV--SHGKPDLASRGLLAQQFHWLDDEPNPFEMRCTVKIRYRQVPVQCKLK 314
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 661253701 320 RAKageagEARFSLGFDTPQWAVTPGQSAVLYDGEICLGGGII 362
Cdd:TIGR00420 315 LLD-----DNLIEVIFDEPQAGVTPGQSAVLYKGDICLGGGII 352
|
|
| tRNA_Me_trans |
pfam03054 |
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ... |
4-200 |
4.25e-111 |
|
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: 323.44 E-value: 4.25e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 4 QRVVVGMSGGVDSSVTAWLLKEQGYDVVGLFMKNWEDD---DDGEYCSTRQDWIDVVSVADLIGIDVEAVNFAAEYKDRV 80
Cdd:pfam03054 1 MKVVVAMSGGVDSSVAAYLLKEQGHNVIGVFMKNWDEEqslDEEGKCCSEEDLADAQRVCEQLGIPLYVVNFEKEYWEDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 81 FAEFLREYSAGRTPNPDVLCNAEIKFKAFLDHA-MSLGAETIATGHYARVRERE-GRFELLKAFDHTKDQSYFLHRLNQA 158
Cdd:pfam03054 81 FEPFLDEYKNGRTPNPDVLCNKEIKFGALLDYAlENLGADYVATGHYARVSLNKdGGSELLRALDKNKDQSYFLSTLSQE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 661253701 159 QLSKTLFPLGEMPKTRVREIAEQIGLPNAKKKDSTGICFIGE 200
Cdd:pfam03054 161 QLEKLLFPLGELTKEEVRKIAKEAGLATAKKKDSQGICFIGK 202
|
|
| PRK14664 |
PRK14664 |
tRNA-specific 2-thiouridylase MnmA; Provisional |
2-364 |
4.66e-74 |
|
tRNA-specific 2-thiouridylase MnmA; Provisional
Pssm-ID: 173127 [Multi-domain] Cd Length: 362 Bit Score: 234.46 E-value: 4.66e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 2 KKQRVVVGMSGGVDSSVTAWLLKEQGYDVVGLFMKNWEDDDDgeycstrqdwiDVVSVADLIGIDVEAVNFAAEYKDRVF 81
Cdd:PRK14664 4 SKKRVLVGMSGGIDSTATCLMLQEQGYEIVGVTMRVWGDEPQ-----------DARELAARMGIEHYVADERVPFKDTIV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 82 AEFLREYSAGRTPNPDVLCNAEIKFKAFLDHAMSLGAETIATGHYARVREREGRFELLKAFDHTKDQSYFLHRLNQAQLS 161
Cdd:PRK14664 73 KNFIDEYRQGRTPNPCVMCNPLFKFRMLIEWADKLGCAWIATGHYSRLEERNGHIYIVAGDDDKKDQSYFLWRLGQDILR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 162 KTLFPLGEMPKTRVREIAEQIGL-PNAKKKDSTGICFIgERPFRDFLNRYLP-----TRPGPMKTPDGKRVGEHIGLAFY 235
Cdd:PRK14664 153 RCIFPLGNYTKQTVREYLREKGYeAKSKEGESMEVCFI-KGDYRDFLREQCPeldteVGPGWFVNSEGVKLGQHKGFPYY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 236 TFGQRKGIGLggskdGSGEPWFVAGKDIASNTLYVAQGHEhpwLLSRELVAGNVSWVAGEppaDGFAC---GAKTRYRQA 312
Cdd:PRK14664 232 TIGQRKGLEI-----ALGKPAYVLKINPQKNTVMLGDAEQ---LKAEYMLAEQDNIVDEQ---ELFACpdlAVRIRYRSR 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 661253701 313 DAPCSFARAKageagEARFSLGFDTPQWAVTPGQSAVLYDGEICLGGGIIES 364
Cdd:PRK14664 301 PIPCRVKRLE-----DGRLLVRFLAEASAIAPGQSAVFYEGRRVLGGAFIAS 347
|
|
| mnmA |
PRK14665 |
tRNA-specific 2-thiouridylase MnmA; Provisional |
2-362 |
4.43e-52 |
|
tRNA-specific 2-thiouridylase MnmA; Provisional
Pssm-ID: 173128 [Multi-domain] Cd Length: 360 Bit Score: 177.43 E-value: 4.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 2 KKQRVVVGMSGGVDSSVTAWLLKEQGYDVVGLFMKNWEDDDDGEYCStrqdwiDVVSVADLIGIDVEAVNFAAEYKDRVF 81
Cdd:PRK14665 4 KNKRVLLGMSGGTDSSVAAMLLLEAGYEVTGVTFRFYEFNGSTEYLE------DARALAERLGIGHITYDARKVFRKQII 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 82 AEFLREYSAGRTPNPDVLCNAEIKFKAFLDHAMSLGAETIATGHYARVREREGRFELLKAFDHTKDQSYFLHRLNQAQLS 161
Cdd:PRK14665 78 DYFIDEYMSGHTPVPCTLCNNYLKWPLLAKIADEMGIFYLATGHYVRKQWIDGNYYITPAEDVDKDQSFFLWGLRQEILQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 162 KTLFPLGEMPKTRVREIAEQIG-LPNAKKKDSTGICFIgERPFRDFLNRYLPT-------------RPGPMKTPDGKRVG 227
Cdd:PRK14665 158 RMLLPMGGMTKSEARAYAAERGfEKVAKKRDSLGVCFC-PMDYRSFLKKCLCDesgdknrniyrkvERGRFLDESGNFIA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 228 EHIGLAFYTFGQRKGIGLGGSKdgsgePWFVAGKDIASNTLYVA--QGHEHPWLLSRELVAGNVSWVAGEppADGFacgA 305
Cdd:PRK14665 237 WHEGYPFYTIGQRRGLGIQLNR-----AVFVKEIHPETNEVVLAslKALEKTEMWLKDWNIVNESRLLGC--DDII---V 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 661253701 306 KTRYRQADAPCSFARAKageagEARFSLGFDTPQWAVTPGQSAVLYDGEICLGGGII 362
Cdd:PRK14665 307 KIRYRKQENHCTVTITP-----DNLLHVQLHEPLTAIAEGQAAAFYKDGLLLGGGII 358
|
|
| tRNA_Me_trans_C |
pfam20258 |
Aminomethyltransferase beta-barrel domain; This domain is found at the C-terminus of tRNA ... |
281-362 |
6.70e-23 |
|
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: 91.18 E-value: 6.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 281 SRELVAGNVSWVAGEPPADGFACGAKTRYRQADAPCSFARAKAGEagearFSLGFDTPQWAVTPGQSAVLYDGEICLGGG 360
Cdd:pfam20258 1 SDGLRAKDPNWLGDKPPTEPLECTVKVRHRQPPVPCVVELIDDET-----VEVHFDEPVRAVTPGQAAVFYDGDRCLGGG 75
|
..
gi 661253701 361 II 362
Cdd:pfam20258 76 II 77
|
|
| tRNA_Me_trans_M |
pfam20259 |
tRNA methyl transferase PRC-barrel domain; This family represents a central PRC-barrel domain ... |
204-272 |
1.28e-22 |
|
tRNA methyl transferase PRC-barrel domain; This family represents a central PRC-barrel domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs.
Pssm-ID: 466410 [Multi-domain] Cd Length: 66 Bit Score: 89.97 E-value: 1.28e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 204 RDFLNRYLPTRPGPMKTPD-GKRVGEHIGLAFYTFGQRKGIGLGgskdGSGEPWFVAGKDIASNTLYVAQ 272
Cdd:pfam20259 1 KDFLKEYLPVKPGDIIDIDtGEVLGEHEGIWFYTIGQRKGLGIG----GYGEPWYVVEKDPKKNTVYVGR 66
|
|
| TilS |
COG0037 |
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ... |
2-125 |
1.83e-07 |
|
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: 51.76 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 2 KKQRVVVGMSGGVDSSVTAWLLKE----QGYDVVGLFM---KNWEDDDDGEYCstrQDWidvvsvADLIGIDVEAVNFAA 74
Cdd:COG0037 14 PGDRILVAVSGGKDSLALLHLLAKlrrrLGFELVAVHVdhgLREESDEDAEFV---AEL------CEELGIPLHVVRVDV 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 661253701 75 EYkdrvfaeflreYSAGRTPNPDVLCnAEIKFKAFLDHAMSLGAETIATGH 125
Cdd:COG0037 85 PA-----------IAKKEGKSPEAAA-RRARYGALYELARELGADKIATGH 123
|
|
| nadE |
TIGR00552 |
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ... |
4-185 |
2.10e-06 |
|
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the biosynthesis of the essensial cofactor NAD. The member of this family from Bacillus subtilis is a strictly NH(3)-dependent NAD(+) synthetase of 272 amino acids. Proteins consisting only of the domain modeled here may be named as NH3-dependent NAD+ synthetase. Amidotransferase activity may reside in a separate protein, or not be present. Some other members of the family, such as from Mycobacterium tuberculosis, are considerably longer, contain an apparent amidotransferase domain, and show glutamine-dependent as well as NH(3)-dependent activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]
Pssm-ID: 273132 [Multi-domain] Cd Length: 250 Bit Score: 48.54 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 4 QRVVVGMSGGVDSSVTAWLLKEQ-GYDVVGLFM--KNWEDDDDGEycstrqdwiDVVSVADLIGIdveavnfaaEYKDRV 80
Cdd:TIGR00552 23 KGVVLGLSGGIDSAVVAALCVEAlGEQNHALLLphSVQTPEQDVQ---------DALALAEPLGI---------NYKNID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 81 FAEFLREYSAGR---TPNPDVLC----NAEIKFKAFLDHAMSLGAETIATGHYArvreregrfELLKAFdHTKdqsyflh 153
Cdd:TIGR00552 85 IAPIAASFQAQTetgDELSDFLAkgnlKARLRMAALYAIANKHNLLVLGTGNKS---------ELMLGY-FTK------- 147
|
170 180 190
....*....|....*....|....*....|..
gi 661253701 154 rlnQAQLSKTLFPLGEMPKTRVREIAEQIGLP 185
Cdd:TIGR00552 148 ---YGDGGCDIAPIGDLFKTQVYELAKRLNVP 176
|
|
| PRK13980 |
PRK13980 |
NAD synthetase; Provisional |
3-194 |
3.28e-06 |
|
NAD synthetase; Provisional
Pssm-ID: 184435 [Multi-domain] Cd Length: 265 Bit Score: 48.28 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 3 KQRVVVGMSGGVDSSVTAWLLKEQ-GYD-VVGLFMKnweddddgEYCSTRQDWIDVVSVADLIGIDVEAVNFaaeykDRV 80
Cdd:PRK13980 30 AKGVVLGLSGGIDSAVVAYLAVKAlGKEnVLALLMP--------SSVSPPEDLEDAELVAEDLGIEYKVIEI-----TPI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 81 FAEFLREYsagrtPNPDVLCNAEIKFKA---FL-DHAMSLGAETIATGHyarvreregRFELLKAfdhtkdqsYFlhrln 156
Cdd:PRK13980 97 VDAFFSAI-----PDADRLRVGNIMARTrmvLLyDYANRENRLVLGTGN---------KSELLLG--------YF----- 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 661253701 157 qaqlskTLF--------PLGEMPKTRVREIAEQIGLPN--AKKKDSTG 194
Cdd:PRK13980 150 ------TKYgdgavdlnPIGDLYKTQVRELARHLGVPEdiIEKPPSAD 191
|
|
| NAD_synthase |
pfam02540 |
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ... |
4-185 |
9.30e-06 |
|
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: 46.61 E-value: 9.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 4 QRVVVGMSGGVDSSVTAWLL-----KEQgydVVGLFMKnweddddgEYCSTRQDWIDVVSVADLIGIDVEAVNFAAEYkd 78
Cdd:pfam02540 19 KGVVLGLSGGIDSSLVAYLAvkalgKEN---VLALIMP--------SSQSSEEDVQDALALAENLGIEYKTIDIKPIV-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 79 RVFAEFLREysagrTPNPDVLCN--AEIKFKAFLDHAMSLGAETIATGHYArvreregrfELLKAFdHTKdqsyflhrln 156
Cdd:pfam02540 86 RAFSQLFQD-----ASEDFAKGNlkARIRMAILYYIANKFNYLVLGTGNKS---------ELAVGY-FTK---------- 140
|
170 180
....*....|....*....|....*....
gi 661253701 157 QAQLSKTLFPLGEMPKTRVREIAEQIGLP 185
Cdd:pfam02540 141 YGDGACDIAPIGDLYKTQVYELARYLNVP 169
|
|
| nadE |
PRK00876 |
NAD(+) synthase; |
1-45 |
1.11e-05 |
|
NAD(+) synthase;
Pssm-ID: 179150 [Multi-domain] Cd Length: 326 Bit Score: 46.87 E-value: 1.11e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 661253701 1 MKKQRVVVGMSGGVDSSVTAWL-LKEQGYD-VVGLFMKnwEDDDDGE 45
Cdd:PRK00876 31 LRRRGVVLGLSGGIDSSVTAALcVRALGKErVYGLLMP--ERDSSPE 75
|
|
| TtuA-like |
cd01993 |
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ... |
2-34 |
3.06e-05 |
|
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: 44.24 E-value: 3.06e-05
10 20 30
....*....|....*....|....*....|...
gi 661253701 2 KKQRVVVGMSGGVDSSVTAWLLKEQGYDVVGLF 34
Cdd:cd01993 7 KDDKILVAVSGGKDSLALLAVLKKLGYNVEALY 39
|
|
| LarE-like |
cd01990 |
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ... |
5-193 |
3.44e-05 |
|
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: 44.56 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 5 RVVVGMSGGVDSSVTAWLLKEQGYD----VVGL--FMKNWEDDDdgeycsTRQdwidvvsVADLIGIDVEAVNFaAEYKD 78
Cdd:cd01990 1 KVVVAFSGGVDSSLLAKLAKEVLGDnvvaVTADspLVPREELEE------AKR-------IAEEIGIRHEIIKT-DELDD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 79 RVFAEflreysagRTPNPDVLCNAEIkFKAFLDHAMSLGAETIATGHYA--RVREREGrfelLKAFdhtkdqsyflhrln 156
Cdd:cd01990 67 EEYVA--------NDPDRCYHCKKAL-YSTLKEIAKERGYDVVLDGTNAddLKDYRPG----LLAA-------------- 119
|
170 180 190
....*....|....*....|....*....|....*...
gi 661253701 157 qAQLS-KTLFPLGEMPKTRVREIAEQIGLPNAKKKDST 193
Cdd:cd01990 120 -AELGiRSPLPELGLTKSEIRELARELGLPNWDKPASA 156
|
|
| QueC-like |
cd01995 |
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ... |
5-34 |
4.66e-05 |
|
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: 44.14 E-value: 4.66e-05
10 20 30
....*....|....*....|....*....|
gi 661253701 5 RVVVGMSGGVDSSVTAWLLKEQGYDVVGLF 34
Cdd:cd01995 2 KAVVLLSGGLDSTTLLYWALKEGYEVHALT 31
|
|
| AANH-like |
cd01986 |
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ... |
6-57 |
8.50e-05 |
|
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide alpha hydrolase (AANH)-like proteins includes N-type ATP PPases and ATP sulfurylases. The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.
Pssm-ID: 467490 [Multi-domain] Cd Length: 74 Bit Score: 40.51 E-value: 8.50e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 661253701 6 VVVGMSGGVDSSVTAWLLKEQGYD--VVGLFMKNWEDDDDgEYCSTRQDWIDVV 57
Cdd:cd01986 1 VVVGYSGGKDSSVALHLASRLGRKaeVAVVHIDHGIGFKE-EAESVASIARRSI 53
|
|
| QueC |
COG0603 |
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ... |
2-33 |
6.49e-04 |
|
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; 7-cyano-7-deazaguanine synthase (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440368 [Multi-domain] Cd Length: 223 Bit Score: 40.92 E-value: 6.49e-04
10 20 30
....*....|....*....|....*....|..
gi 661253701 2 KKQRVVVGMSGGVDSSVTAWLLKEQGYDVVGL 33
Cdd:COG0603 1 MMKKAVVLLSGGLDSTTCLAWALARGYEVYAL 32
|
|
| NAD_synthase |
cd00553 |
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ... |
4-187 |
1.40e-03 |
|
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: 39.85 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 4 QRVVVGMSGGVDSSVTAWLLKE--QGYDVVGLFM---KNWEDDDDgeycstrqdwiDVVSVADLIGIDVEAVNFAAEYkD 78
Cdd:cd00553 24 KGFVLGLSGGIDSAVVAALAVRalGAENVLALIMpsrYSSKETRD-----------DAKALAENLGIEYRTIDIDPIV-D 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 79 RVFAEFlrEYSAGRTPNPDVLCN--AEIKFKAFLDHAMSLGAETIATGHYArvreregrfELL-----KAFDHTKDqsyf 151
Cdd:cd00553 92 AFLKAL--EHAGGSEAEDLALGNiqARLRMVLLYALANLLGGLVLGTGNKS---------ELLlgyftKYGDGAAD---- 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 661253701 152 lhrLNqaqlsktlfPLGEMPKTRVREIAEQIGLPNA 187
Cdd:cd00553 157 ---IN---------PIGDLYKTQVRELARYLGVPEE 180
|
|
| CTU1-like |
cd01713 |
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ... |
2-125 |
2.26e-03 |
|
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human cytoplasmic tRNA 2-thiolation protein 1, also called cytosolic thiouridylase subunit 1 (CTU1), ATP-binding domain-containing protein 3 (ATPBD3), cancer-associated gene protein, or cytoplasmic tRNA adenylyltransferase 1. CTU1 plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). It directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. The CTU1-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.
Pssm-ID: 467486 Cd Length: 208 Bit Score: 39.11 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661253701 2 KKQRVVVGMSGGVDSSVTAWLLKEqgydvvglFMKNWEDD--------DDG--EYcstRQDWIDVV-SVADLIGIDVEAV 70
Cdd:cd01713 17 PGDRVAVGLSGGKDSTVLLYVLKE--------LNKRHDYGveliavtiDEGikGY---RDDSLEAArKLAEEYGIPLEIV 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 661253701 71 NFAAEYK---DRVFAeflreySAGRTPNPDVLCnAEIKFKAFLDHAMSLGAETIATGH 125
Cdd:cd01713 86 SFEDEFGftlDELIV------GKGGKKNACTYC-GVFRRRALNRGARELGADKLATGH 136
|
|
| guaA |
PRK00074 |
GMP synthase; Reviewed |
2-25 |
2.70e-03 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 39.65 E-value: 2.70e-03
|
| COG1365 |
COG1365 |
Predicted ATPase, PP-loop superfamily [General function prediction only]; |
2-33 |
3.75e-03 |
|
Predicted ATPase, PP-loop superfamily [General function prediction only];
Pssm-ID: 440976 Cd Length: 256 Bit Score: 38.88 E-value: 3.75e-03
10 20 30
....*....|....*....|....*....|..
gi 661253701 2 KKQRVVVGMSGGVDSSVTAWLLKEQGYDVVGL 33
Cdd:COG1365 59 KNPKVVVAFSGGVDSSASLIIAKWIGFDVEAV 90
|
|
| PPase_ThiI |
cd01712 |
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole ... |
4-37 |
5.99e-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: 37.53 E-value: 5.99e-03
10 20 30
....*....|....*....|....*....|....
gi 661253701 4 QRVVVGMSGGVDSSVTAWLLKEQGYDVVGLFMKN 37
Cdd:cd01712 5 GKVLVLLSGGIDSPVAAWMMMKRGVEVDFLHFHS 38
|
|
| NadE |
COG0171 |
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
4-71 |
9.47e-03 |
|
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: 37.90 E-value: 9.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 661253701 4 QRVVVGMSGGVDSSVTAWLL-----KEqgyDVVGLFMKnweddddGEYcSTRQDWIDVVSVADLIGIDVEAVN 71
Cdd:COG0171 287 KGVVLGLSGGIDSALVAALAvdalgPE---NVLGVTMP-------SRY-TSDESLEDAEELAENLGIEYEEID 348
|
|
| |
