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Conserved domains on  [gi|21312518|ref|NP_082339|]
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mitochondrial tRNA-specific 2-thiouridylase 1 [Mus musculus]

Protein Classification

tRNA-specific 2-thiouridylase( domain architecture ID 10113449)

MnmA/TRMU family tRNA-specific 2-thiouridylase catalyzes the 2-thiolation of uridine at the wobble position of tRNAs

CATH:  2.30.30.280|3.40.50.620
EC:  2.8.1.-
Gene Ontology:  GO:0005524|GO:0000049|GO:0006400|GO:0016783
PubMed:  16387657|16871210|12012333
SCOP:  4007171

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
 6-383 5.69e-178

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: 499.72  E-value: 5.69e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518   6 HVVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWDSLD-EQGVCAADKDCEDAYKVCQILDIPFHQVSYVKEYWNDVFSD 84
Cdd:cd01998   1 KVAVAMSGGVDSSVAAALLKEQGYDVIGVFMKNWDDEDnEKGGCCSEEDIEDARRVADQLGIPLYVVDFSEEYWERVFDP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518  85 FLNEYEKGRTPNPDINCNKHIKFSCFYHYAvDNLGADAVATGHYARTSLEDeevfeqkhtkkpdglfrnrfevRNPVKLL 164
Cdd:cd01998  81 FLEEYKAGRTPNPDVLCNREIKFGALLDAA-KKLGADYIATGHYARIEEDN----------------------RGRYRLL 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518 165 QAADSFKDQTFFLSQVSQDALRRTIFPLGELTKDFVKKIAAENSLhHVLQKRESMGICFIGKRNLEHFLLQYLQPR-PGK 243
Cdd:cd01998 138 RAVDPNKDQSYFLSRLSQEQLSRTLFPLGHLTKSEVREIAREAGL-PVAEKKDSQGICFIGKRDFRDFLKEYLPEKlPGP 216

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518 244 FVSIeDNTVLGTHKGWFLYTLGQRAKIS-GLREPWYVVEKDGTKGDVLVAPrvDHPALYRDLLRTNRVHWIAEEPPaalv 322
Cdd:cd01998 217 IVDI-DGKVLGEHKGLWFYTIGQRKGLGiAAGEPLYVVKKDPEKNIVVVGP--GHPALFSDTLRASDLNWISPEPP---- 289

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21312518 323 rDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAVKAVRGLALGQFAVFYKGEECLGSGKI 383
Cdd:cd01998 290 -LEPLECEAKIRYRQPPVPCTVTPLDDGRLKVEFDEPQRAVTPGQAAVFYDGDEVLGGGII 349
 
Name Accession Description Interval E-value
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
 6-383 5.69e-178

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: 499.72  E-value: 5.69e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518   6 HVVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWDSLD-EQGVCAADKDCEDAYKVCQILDIPFHQVSYVKEYWNDVFSD 84
Cdd:cd01998   1 KVAVAMSGGVDSSVAAALLKEQGYDVIGVFMKNWDDEDnEKGGCCSEEDIEDARRVADQLGIPLYVVDFSEEYWERVFDP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518  85 FLNEYEKGRTPNPDINCNKHIKFSCFYHYAvDNLGADAVATGHYARTSLEDeevfeqkhtkkpdglfrnrfevRNPVKLL 164
Cdd:cd01998  81 FLEEYKAGRTPNPDVLCNREIKFGALLDAA-KKLGADYIATGHYARIEEDN----------------------RGRYRLL 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518 165 QAADSFKDQTFFLSQVSQDALRRTIFPLGELTKDFVKKIAAENSLhHVLQKRESMGICFIGKRNLEHFLLQYLQPR-PGK 243
Cdd:cd01998 138 RAVDPNKDQSYFLSRLSQEQLSRTLFPLGHLTKSEVREIAREAGL-PVAEKKDSQGICFIGKRDFRDFLKEYLPEKlPGP 216

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518 244 FVSIeDNTVLGTHKGWFLYTLGQRAKIS-GLREPWYVVEKDGTKGDVLVAPrvDHPALYRDLLRTNRVHWIAEEPPaalv 322
Cdd:cd01998 217 IVDI-DGKVLGEHKGLWFYTIGQRKGLGiAAGEPLYVVKKDPEKNIVVVGP--GHPALFSDTLRASDLNWISPEPP---- 289

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21312518 323 rDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAVKAVRGLALGQFAVFYKGEECLGSGKI 383
Cdd:cd01998 290 -LEPLECEAKIRYRQPPVPCTVTPLDDGRLKVEFDEPQRAVTPGQAAVFYDGDEVLGGGII 349
MnmA COG0482
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ...
 7-385 4.82e-155

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: 441.80  E-value: 4.82e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518   7 VVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWD--SLDEQGVCAADKDCEDAYKVCQILDIPFHQVSYVKEYWNDVFSD 84
Cdd:COG0482   3 VVVGMSGGVDSSVAAALLKEQGYEVIGVTMKLWDddDASGSGGCCSLEDIEDARRVADKLGIPHYVVDFEEEFKDRVIDY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518  85 FLNEYEKGRTPNPDINCNKHIKFSCFYHYAvDNLGADAVATGHYARTSLEDeevfeqkhtkkpdglfrNRFEvrnpvkLL 164
Cdd:COG0482  83 FLDEYLAGRTPNPCVLCNREIKFGALLEKA-LELGADYIATGHYARVEEKD-----------------GRYE------LL 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518 165 QAADSFKDQTFFLSQVSQDALRRTIFPLGELTKDFVKKIAAENSLhHVLQKRESMGICFIGKRNLEHFLLQYLQPRPGKF 244
Cdd:COG0482 139 RGVDPNKDQSYFLYRLTQEQLSKTLFPLGELTKPEVREIAEELGL-PVADKKDSQGICFIGDGDYRDFLERYLPEKPGDI 217

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518 245 VSIeDNTVLGTHKGWFLYTLGQRakiSGLR----EPWYVVEKDGTKGDVLVAPRvdhPALYRDLLRTNRVHWIAEEPPAa 320
Cdd:COG0482 218 VDL-DGKVLGEHDGLHYYTIGQR---KGLGigggEPLYVVGKDPETNTVIVGQG---EALYSRELTAEDVNWISGEPPE- 289

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21312518 321 lvrdKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAVKAVRGLALGQFAVFYKGEECLGSGKILR 385
Cdd:COG0482 290 ----EPLRCTAKIRYRQPPVPATLTPLEDGRVRVEFDEPQRAVTPGQSAVFYDGDRVLGGGIIER 350
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
 7-383 1.02e-151

tRNA-specific 2-thiouridylase MnmA; Reviewed


Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 432.96  E-value: 1.02e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518    7 VVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWDSLDE--QGVCAADKDCEDAYKVCQILDIPFHQVSYVKEYWNDVFSD 84
Cdd:PRK00143   3 VVVGMSGGVDSSVAAALLKEQGYEVIGVFMKLWDDDDEtgKGGCCAEEDIADARRVADKLGIPHYVVDFEKEFWDRVIDY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518   85 FLNEYEKGRTPNPDINCNKHIKFSCFYHYAVDnLGADAVATGHYARtsledeevfeqkhtkkpdglfrnrfeVRNPVKLL 164
Cdd:PRK00143  83 FLDEYKAGRTPNPCVLCNKEIKFKAFLEYARE-LGADYIATGHYAR--------------------------IRDGRELL 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518  165 QAADSFKDQTFFLSQVSQDALRRTIFPLGELTKDFVKKIAAENSLhHVLQKRESMGICFIGKRNLEHFLLQYLQPRPGKF 244
Cdd:PRK00143 136 RGVDPNKDQSYFLYQLTQEQLAKLLFPLGELTKPEVREIAEEAGL-PVAKKKDSQGICFIGERDYRDFLKRYLPAQPGEI 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518  245 VSIeDNTVLGTHKGWFLYTLGQRaK---ISGLREPWYVVEKDGTKGDVLVAPRvdhPALYRDLLRTNRVHWIAEEPPAal 321
Cdd:PRK00143 215 VDL-DGKVLGEHKGLMYYTIGQR-KglgIGGDGEPWYVVGKDPETNTVVVGQG---EALYSRELIASDLNWVGGEPPE-- 287

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21312518  322 vrdKMMECHFRFRHQMALVPCVLTLnQDGTVWVTAVKAVRGLALGQFAVFYKGEECLGSGKI 383
Cdd:PRK00143 288 ---EPFECTAKIRYRQKPVPATVEL-EDDRVEVEFDEPQRAVTPGQAAVFYDGDRVLGGGII 345
trmU TIGR00420
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ...
 7-383 9.34e-124

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: 362.47  E-value: 9.34e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518     7 VVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWDSLD--EQGVCAADKDCEDAYKVCQILDIPFHQVSYVKEYWNDVFSD 84
Cdd:TIGR00420   3 VIVGLSGGVDSSVSAYLLKQQGYEVVGVFMKNWEEDDknDGHGCTSAEDLRDAQAICEKLGIPLEKVNFQKEYWNKVFEP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518    85 FLNEYEKGRTPNPDINCNKHIKFSCFYHYAVDNLGADAVATGHYARTSlEDEEVFeqkhtkkpdglfrnrfevrnpvKLL 164
Cdd:TIGR00420  83 FIQEYKEGRTPNPDILCNKFIKFGAFLEYAAELLGNDKIATGHYARIA-EIEGKS----------------------LLL 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518   165 QAADSFKDQTFFLSQVSQDALRRTIFPLGELTKDFVKKIAAENSLhHVLQKRESMGICFIGKRNLEHFLLQYLQPRPGKF 244
Cdd:TIGR00420 140 RALDKNKDQSYFLYHLSHEQLAKLLFPLGELLKPEVRQIAKNAGL-PTAEKKDSQGICFIGERKFRDFLKKYLPVKPGVI 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518   245 VSIEDNTVLGTHKGWFLYTLGQRA--KISGLREPWYVVEKDGTKGDVLVAPrvDHPALYRDLLRTNRVHWIAEEPpaalv 322
Cdd:TIGR00420 219 ITVDGQSVIGEHDGLWFYTIGQRKglGIGGAAEPWFVVEKDLETNELVVSH--GKPDLASRGLLAQQFHWLDDEP----- 291

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21312518   323 RDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAVKAVRGLALGQFAVFYKGEECLGSGKI 383
Cdd:TIGR00420 292 NPFEMRCTVKIRYRQVPVQCKLKLLDDNLIEVIFDEPQAGVTPGQSAVLYKGDICLGGGII 352
tRNA_Me_trans pfam03054
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ...
 5-226 8.40e-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: 323.82  E-value: 8.40e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518     5 RHVVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWD---SLDEQGVCAADKDCEDAYKVCQILDIPFHQVSYVKEYWNDV 81
Cdd:pfam03054   1 MKVVVAMSGGVDSSVAAYLLKEQGHNVIGVFMKNWDeeqSLDEEGKCCSEEDLADAQRVCEQLGIPLYVVNFEKEYWEDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518    82 FSDFLNEYEKGRTPNPDINCNKHIKFSCFYHYAVDNLGADAVATGHYARTSLEDEEVFEqkhtkkpdglfrnrfevrnpv 161
Cdd:pfam03054  81 FEPFLDEYKNGRTPNPDVLCNKEIKFGALLDYALENLGADYVATGHYARVSLNKDGGSE--------------------- 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21312518   162 kLLQAADSFKDQTFFLSQVSQDALRRTIFPLGELTKDFVKKIAAENSLhHVLQKRESMGICFIGK 226
Cdd:pfam03054 140 -LLRALDKNKDQSYFLSTLSQEQLEKLLFPLGELTKEEVRKIAKEAGL-ATAKKKDSQGICFIGK 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 ...
 6-383 5.69e-178

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: 499.72  E-value: 5.69e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518   6 HVVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWDSLD-EQGVCAADKDCEDAYKVCQILDIPFHQVSYVKEYWNDVFSD 84
Cdd:cd01998   1 KVAVAMSGGVDSSVAAALLKEQGYDVIGVFMKNWDDEDnEKGGCCSEEDIEDARRVADQLGIPLYVVDFSEEYWERVFDP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518  85 FLNEYEKGRTPNPDINCNKHIKFSCFYHYAvDNLGADAVATGHYARTSLEDeevfeqkhtkkpdglfrnrfevRNPVKLL 164
Cdd:cd01998  81 FLEEYKAGRTPNPDVLCNREIKFGALLDAA-KKLGADYIATGHYARIEEDN----------------------RGRYRLL 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518 165 QAADSFKDQTFFLSQVSQDALRRTIFPLGELTKDFVKKIAAENSLhHVLQKRESMGICFIGKRNLEHFLLQYLQPR-PGK 243
Cdd:cd01998 138 RAVDPNKDQSYFLSRLSQEQLSRTLFPLGHLTKSEVREIAREAGL-PVAEKKDSQGICFIGKRDFRDFLKEYLPEKlPGP 216

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518 244 FVSIeDNTVLGTHKGWFLYTLGQRAKIS-GLREPWYVVEKDGTKGDVLVAPrvDHPALYRDLLRTNRVHWIAEEPPaalv 322
Cdd:cd01998 217 IVDI-DGKVLGEHKGLWFYTIGQRKGLGiAAGEPLYVVKKDPEKNIVVVGP--GHPALFSDTLRASDLNWISPEPP---- 289

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21312518 323 rDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAVKAVRGLALGQFAVFYKGEECLGSGKI 383
Cdd:cd01998 290 -LEPLECEAKIRYRQPPVPCTVTPLDDGRLKVEFDEPQRAVTPGQAAVFYDGDEVLGGGII 349
MnmA COG0482
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ...
 7-385 4.82e-155

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: 441.80  E-value: 4.82e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518   7 VVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWD--SLDEQGVCAADKDCEDAYKVCQILDIPFHQVSYVKEYWNDVFSD 84
Cdd:COG0482   3 VVVGMSGGVDSSVAAALLKEQGYEVIGVTMKLWDddDASGSGGCCSLEDIEDARRVADKLGIPHYVVDFEEEFKDRVIDY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518  85 FLNEYEKGRTPNPDINCNKHIKFSCFYHYAvDNLGADAVATGHYARTSLEDeevfeqkhtkkpdglfrNRFEvrnpvkLL 164
Cdd:COG0482  83 FLDEYLAGRTPNPCVLCNREIKFGALLEKA-LELGADYIATGHYARVEEKD-----------------GRYE------LL 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518 165 QAADSFKDQTFFLSQVSQDALRRTIFPLGELTKDFVKKIAAENSLhHVLQKRESMGICFIGKRNLEHFLLQYLQPRPGKF 244
Cdd:COG0482 139 RGVDPNKDQSYFLYRLTQEQLSKTLFPLGELTKPEVREIAEELGL-PVADKKDSQGICFIGDGDYRDFLERYLPEKPGDI 217

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518 245 VSIeDNTVLGTHKGWFLYTLGQRakiSGLR----EPWYVVEKDGTKGDVLVAPRvdhPALYRDLLRTNRVHWIAEEPPAa 320
Cdd:COG0482 218 VDL-DGKVLGEHDGLHYYTIGQR---KGLGigggEPLYVVGKDPETNTVIVGQG---EALYSRELTAEDVNWISGEPPE- 289

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21312518 321 lvrdKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAVKAVRGLALGQFAVFYKGEECLGSGKILR 385
Cdd:COG0482 290 ----EPLRCTAKIRYRQPPVPATLTPLEDGRVRVEFDEPQRAVTPGQSAVFYDGDRVLGGGIIER 350
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
 7-383 1.02e-151

tRNA-specific 2-thiouridylase MnmA; Reviewed


Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 432.96  E-value: 1.02e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518    7 VVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWDSLDE--QGVCAADKDCEDAYKVCQILDIPFHQVSYVKEYWNDVFSD 84
Cdd:PRK00143   3 VVVGMSGGVDSSVAAALLKEQGYEVIGVFMKLWDDDDEtgKGGCCAEEDIADARRVADKLGIPHYVVDFEKEFWDRVIDY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518   85 FLNEYEKGRTPNPDINCNKHIKFSCFYHYAVDnLGADAVATGHYARtsledeevfeqkhtkkpdglfrnrfeVRNPVKLL 164
Cdd:PRK00143  83 FLDEYKAGRTPNPCVLCNKEIKFKAFLEYARE-LGADYIATGHYAR--------------------------IRDGRELL 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518  165 QAADSFKDQTFFLSQVSQDALRRTIFPLGELTKDFVKKIAAENSLhHVLQKRESMGICFIGKRNLEHFLLQYLQPRPGKF 244
Cdd:PRK00143 136 RGVDPNKDQSYFLYQLTQEQLAKLLFPLGELTKPEVREIAEEAGL-PVAKKKDSQGICFIGERDYRDFLKRYLPAQPGEI 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518  245 VSIeDNTVLGTHKGWFLYTLGQRaK---ISGLREPWYVVEKDGTKGDVLVAPRvdhPALYRDLLRTNRVHWIAEEPPAal 321
Cdd:PRK00143 215 VDL-DGKVLGEHKGLMYYTIGQR-KglgIGGDGEPWYVVGKDPETNTVVVGQG---EALYSRELIASDLNWVGGEPPE-- 287

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21312518  322 vrdKMMECHFRFRHQMALVPCVLTLnQDGTVWVTAVKAVRGLALGQFAVFYKGEECLGSGKI 383
Cdd:PRK00143 288 ---EPFECTAKIRYRQKPVPATVEL-EDDRVEVEFDEPQRAVTPGQAAVFYDGDRVLGGGII 345
trmU TIGR00420
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ...
 7-383 9.34e-124

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: 362.47  E-value: 9.34e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518     7 VVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWDSLD--EQGVCAADKDCEDAYKVCQILDIPFHQVSYVKEYWNDVFSD 84
Cdd:TIGR00420   3 VIVGLSGGVDSSVSAYLLKQQGYEVVGVFMKNWEEDDknDGHGCTSAEDLRDAQAICEKLGIPLEKVNFQKEYWNKVFEP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518    85 FLNEYEKGRTPNPDINCNKHIKFSCFYHYAVDNLGADAVATGHYARTSlEDEEVFeqkhtkkpdglfrnrfevrnpvKLL 164
Cdd:TIGR00420  83 FIQEYKEGRTPNPDILCNKFIKFGAFLEYAAELLGNDKIATGHYARIA-EIEGKS----------------------LLL 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518   165 QAADSFKDQTFFLSQVSQDALRRTIFPLGELTKDFVKKIAAENSLhHVLQKRESMGICFIGKRNLEHFLLQYLQPRPGKF 244
Cdd:TIGR00420 140 RALDKNKDQSYFLYHLSHEQLAKLLFPLGELLKPEVRQIAKNAGL-PTAEKKDSQGICFIGERKFRDFLKKYLPVKPGVI 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518   245 VSIEDNTVLGTHKGWFLYTLGQRA--KISGLREPWYVVEKDGTKGDVLVAPrvDHPALYRDLLRTNRVHWIAEEPpaalv 322
Cdd:TIGR00420 219 ITVDGQSVIGEHDGLWFYTIGQRKglGIGGAAEPWFVVEKDLETNELVVSH--GKPDLASRGLLAQQFHWLDDEP----- 291

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21312518   323 RDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAVKAVRGLALGQFAVFYKGEECLGSGKI 383
Cdd:TIGR00420 292 NPFEMRCTVKIRYRQVPVQCKLKLLDDNLIEVIFDEPQAGVTPGQSAVLYKGDICLGGGII 352
tRNA_Me_trans pfam03054
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ...
 5-226 8.40e-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: 323.82  E-value: 8.40e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518     5 RHVVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWD---SLDEQGVCAADKDCEDAYKVCQILDIPFHQVSYVKEYWNDV 81
Cdd:pfam03054   1 MKVVVAMSGGVDSSVAAYLLKEQGHNVIGVFMKNWDeeqSLDEEGKCCSEEDLADAQRVCEQLGIPLYVVNFEKEYWEDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518    82 FSDFLNEYEKGRTPNPDINCNKHIKFSCFYHYAVDNLGADAVATGHYARTSLEDEEVFEqkhtkkpdglfrnrfevrnpv 161
Cdd:pfam03054  81 FEPFLDEYKNGRTPNPDVLCNKEIKFGALLDYALENLGADYVATGHYARVSLNKDGGSE--------------------- 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21312518   162 kLLQAADSFKDQTFFLSQVSQDALRRTIFPLGELTKDFVKKIAAENSLhHVLQKRESMGICFIGK 226
Cdd:pfam03054 140 -LLRALDKNKDQSYFLSTLSQEQLEKLLFPLGELTKEEVRKIAKEAGL-ATAKKKDSQGICFIGK 202
PRK14664 PRK14664
tRNA-specific 2-thiouridylase MnmA; Provisional
 5-383 2.10e-50

tRNA-specific 2-thiouridylase MnmA; Provisional


Pssm-ID: 173127 [Multi-domain]  Cd Length: 362  Bit Score: 173.99  E-value: 2.10e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518    5 RHVVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWDslDEQgvcaadkdcEDAYKVCQILDIPFHQVSYVKEYWNDVFSD 84
Cdd:PRK14664   6 KRVLVGMSGGIDSTATCLMLQEQGYEIVGVTMRVWG--DEP---------QDARELAARMGIEHYVADERVPFKDTIVKN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518   85 FLNEYEKGRTPNPDINCNKHIKFSCFYHYAvDNLGADAVATGHYARtsLEdeevfeqkhtkkpdglfrnrfEVRNPVKLL 164
Cdd:PRK14664  75 FIDEYRQGRTPNPCVMCNPLFKFRMLIEWA-DKLGCAWIATGHYSR--LE---------------------ERNGHIYIV 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518  165 QAADSFKDQTFFLSQVSQDALRRTIFPLGELTKDFVKKIAAENSLHHVLQKRESMGICFIgKRNLEHFLLQY-----LQP 239
Cdd:PRK14664 131 AGDDDKKDQSYFLWRLGQDILRRCIFPLGNYTKQTVREYLREKGYEAKSKEGESMEVCFI-KGDYRDFLREQcpeldTEV 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518  240 RPGKFVSIEdNTVLGTHKGWFLYTLGQRAKIS-GLREPWYVVEKDGTKGDVLVAprvDHPALYRDLLRTNRVHwIAEEpp 318
Cdd:PRK14664 210 GPGWFVNSE-GVKLGQHKGFPYYTIGQRKGLEiALGKPAYVLKINPQKNTVMLG---DAEQLKAEYMLAEQDN-IVDE-- 282

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21312518  319 aalvrDKMMECH---FRFRHQMALVPCVLTLNQDGTVWVTAVKAVRGLALGQFAVFYKGEECLGSGKI 383
Cdd:PRK14664 283 -----QELFACPdlaVRIRYRSRPIPCRVKRLEDGRLLVRFLAEASAIAPGQSAVFYEGRRVLGGAFI 345
mnmA PRK14665
tRNA-specific 2-thiouridylase MnmA; Provisional
 1-384 1.58e-43

tRNA-specific 2-thiouridylase MnmA; Provisional


Pssm-ID: 173128 [Multi-domain]  Cd Length: 360  Bit Score: 155.48  E-value: 1.58e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518    1 MSALRHVVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWDSLDEQgvcaadKDCEDAYKVCQILDIPFHQVSYVKEYWND 80
Cdd:PRK14665   2 MEKNKRVLLGMSGGTDSSVAAMLLLEAGYEVTGVTFRFYEFNGST------EYLEDARALAERLGIGHITYDARKVFRKQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518   81 VFSDFLNEYEKGRTPNPDINCNKHIKFSCFYHYAvDNLGADAVATGHYARTsledeevfeqkhtKKPDGLFRnrfevrnp 160
Cdd:PRK14665  76 IIDYFIDEYMSGHTPVPCTLCNNYLKWPLLAKIA-DEMGIFYLATGHYVRK-------------QWIDGNYY-------- 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518  161 vkLLQAADSFKDQTFFLSQVSQDALRRTIFPLGELTKDFVKKIAAENSLHHVLQKRESMGICF--IGKRNLEHFLL---- 234
Cdd:PRK14665 134 --ITPAEDVDKDQSFFLWGLRQEILQRMLLPMGGMTKSEARAYAAERGFEKVAKKRDSLGVCFcpMDYRSFLKKCLcdes 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518  235 ------QYLQPRPGKFVSiEDNTVLGTHKGWFLYTLGQRAKIS-GLREPWYVVEKDGTKGDVLVAprvDHPALYRDLLRT 307
Cdd:PRK14665 212 gdknrnIYRKVERGRFLD-ESGNFIAWHEGYPFYTIGQRRGLGiQLNRAVFVKEIHPETNEVVLA---SLKALEKTEMWL 287

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21312518  308 NrvHWIAEEPPAALVRDKMMeCHFRFRHQMAlvPCVLTLNQDGTVWVTAVKAVRGLALGQFAVFYKGEECLGSGKIL 384
Cdd:PRK14665 288 K--DWNIVNESRLLGCDDII-VKIRYRKQEN--HCTVTITPDNLLHVQLHEPLTAIAEGQAAAFYKDGLLLGGGIIT 359
tRNA_Me_trans_C pfam20258
Aminomethyltransferase beta-barrel domain; This domain is found at the C-terminus of tRNA ...
 302-383 6.80e-29

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: 107.75  E-value: 6.80e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518   302 RDLLRTNRVHWIAEEPPaalvrDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAVKAVRGLALGQFAVFYKGEECLGSG 381
Cdd:pfam20258   1 SDGLRAKDPNWLGDKPP-----TEPLECTVKVRHRQPPVPCVVELIDDETVEVHFDEPVRAVTPGQAAVFYDGDRCLGGG 75


                  ..
gi 21312518   382 KI 383
Cdd:pfam20258  76 II 77
tRNA_Me_trans_M pfam20259
tRNA methyl transferase PRC-barrel domain; This family represents a central PRC-barrel domain ...
 230-293 2.74e-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: 89.59  E-value: 2.74e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21312518   230 EHFLLQYLQPRPGKFVSIEDNTVLGTHKGWFLYTLGQR--AKISGLREPWYVVEKDGTKGDVLVAP 293
Cdd:pfam20259   1 KDFLKEYLPVKPGDIIDIDTGEVLGEHEGIWFYTIGQRkgLGIGGYGEPWYVVEKDPKKNTVYVGR 66
guaA PRK00074
GMP synthase; Reviewed
 5-35 1.00e-07

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 53.90  E-value: 1.00e-07
                         10        20        30
                 ....*....|....*....|....*....|..
gi 21312518    5 RHVVCALSGGVDSAVAALLLRRR-GYQVTGVF 35
Cdd:PRK00074 216 KKVILGLSGGVDSSVAAVLLHKAiGDQLTCVF 247
NAD_synthase pfam02540
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ...
 7-133 1.19e-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: 49.30  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518     7 VVCALSGGVDSAVAALLLRR--RGYQVTGVFMKnwdsldeqGVCAADKDCEDAYKVCQILDIPFHQVSYvkeywNDVFSD 84
Cdd:pfam02540  21 VVLGLSGGIDSSLVAYLAVKalGKENVLALIMP--------SSQSSEEDVQDALALAENLGIEYKTIDI-----KPIVRA 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 21312518    85 FLNEYEKGRTPNPDINCNKHIKFSCFYHYAvDNLGADAVATGHYARTSL 133
Cdd:pfam02540  88 FSQLFQDASEDFAKGNLKARIRMAILYYIA-NKFNYLVLGTGNKSELAV 135
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 5-127 3.42e-06

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: 47.91  E-value: 3.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518   5 RHVVCALSGGVDSAVAALLL----RRRGYQVTGVFMknwdslDEQGVCAADKDCEDAYKVCQILDIPFHQVSyvkeyWND 80
Cdd:COG0037  16 DRILVAVSGGKDSLALLHLLaklrRRLGFELVAVHV------DHGLREESDEDAEFVAELCEELGIPLHVVR-----VDV 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 21312518  81 VFSDFlneyEKGRTPnpdinCNK--HIKFSCFYHYAVDnLGADAVATGH 127
Cdd:COG0037  85 PAIAK----KEGKSP-----EAAarRARYGALYELARE-LGADKIATGH 123
NAD_synthase cd00553
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ...
 2-72 1.16e-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: 46.39  E-value: 1.16e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21312518   2 SALRHVVCALSGGVDSAVAALLLRR--RGYQVTGVFMKNWDSLDEqgvcaadkDCEDAYKVCQILDIPFHQVS 72
Cdd:cd00553  21 SGAKGFVLGLSGGIDSAVVAALAVRalGAENVLALIMPSRYSSKE--------TRDDAKALAENLGIEYRTID 85
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 7-55 2.58e-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: 42.05  E-value: 2.58e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 21312518   7 VVCALSGGVDSAVAALLLRR--RGYQVTGVFMKNWDSLDE--QGVCAADKDCE 55
Cdd:cd01986   1 VVVGYSGGKDSSVALHLASRlgRKAEVAVVHIDHGIGFKEeaESVASIARRSI 53
GMP_synthase_C cd01997
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ...
 5-35 3.21e-05

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: 45.61  E-value: 3.21e-05
                        10        20        30
                ....*....|....*....|....*....|...
gi 21312518   5 RHVVCALSGGVDSAVAALLLRR--RGYQVTGVF 35
Cdd:cd01997   8 KKVLCLVSGGVDSTVCAALLHKalGDERVIAVH 40
ThiI pfam02568
Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for ...
 7-38 7.16e-05

Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for thiamine biosynthesis.


Pssm-ID: 280691 [Multi-domain]  Cd Length: 197  Bit Score: 43.57  E-value: 7.16e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 21312518     7 VVCALSGGVDSAVAALLLRRRGYQVTGVFMKN 38
Cdd:pfam02568   6 VLALISGGIDSPVAAYMMMRRGCRVVALHFIN 37
PPase_ThiI cd01712
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole ...
 7-47 7.26e-05

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: 43.31  E-value: 7.26e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 21312518   7 VVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWDSLDEQGV 47
Cdd:cd01712   7 VLVLLSGGIDSPVAAWMMMKRGVEVDFLHFHSGPYTSEKAV 47
QueC-like cd01995
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ...
 7-126 9.16e-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: 43.37  E-value: 9.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518   7 VVCALSGGVDSAVAALLLRRRGYQVTGVFMknwdsldEQGVCAADKDCEDAYKVCQILDIPFH--QVSYVKEYWNDVFSD 84
Cdd:cd01995   3 AVVLLSGGLDSTTLLYWALKEGYEVHALTF-------DYGQRHAKEELEAAKLIAKLLGIEHKviDLSFLGELGGSSLTD 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 21312518  85 FLNEYEKGRTPNPDI------NCNKH---IKFScfyhYAVdNLGADAVATG 126
Cdd:cd01995  76 EGEEVPDGEYDEESIpstwvpNRNLIflsIAAA----YAE-SLGASAIVIG 121
TIGR00342 TIGR00342
tRNA sulfurtransferase ThiI; Members of this protein family are "ThiI", a sulfurtransferase ...
 7-38 1.03e-04

tRNA sulfurtransferase ThiI; Members of this protein family are "ThiI", a sulfurtransferase involved in 4-thiouridine modification of tRNA. This protein often is bifunctional, with genetically separable activities, where the C-terminal rhodanese-like domain (residues 385 to 482 in E. coli ThiI), a domain not included in this model, is sufficient to synthesize the thiazole moiety of thiamine (see TIGR04271). Note that ThiI, because of its role in tRNA modification, may occur in species (such as Mycoplasma genitalium) that lack de novo thiamine biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine, Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273025 [Multi-domain]  Cd Length: 371  Bit Score: 44.32  E-value: 1.03e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 21312518     7 VVCALSGGVDSAVAALLLRRRGYQVTGVFMKN 38
Cdd:TIGR00342 175 VLALLSGGIDSPVAAFMMMKRGCRVVAVHFFN 206
PLN02347 PLN02347
GMP synthetase
 6-26 1.29e-04

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 44.29  E-value: 1.29e-04
                         10        20
                 ....*....|....*....|.
gi 21312518    6 HVVCALSGGVDSAVAALLLRR 26
Cdd:PLN02347 231 HVICALSGGVDSTVAATLVHK 251
NadE COG0171
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ...
 5-72 2.42e-04

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: 43.30  E-value: 2.42e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21312518   5 RHVVCALSGGVDSAVAALLLRR-----RgyqVTGVFMKNWDSldeqgvcaADKDCEDAYKVCQILDIPFHQVS 72
Cdd:COG0171 287 KGVVLGLSGGIDSALVAALAVDalgpeN---VLGVTMPSRYT--------SDESLEDAEELAENLGIEYEEID 348
nadE TIGR00552
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ...
 7-114 9.31e-04

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: 40.83  E-value: 9.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518     7 VVCALSGGVDSA-VAALLLRRRGYQVTGVFMKNWDSLDEQgvcaadkDCEDAYKVCQILDIPFHQVSYvkeywNDVFSDF 85
Cdd:TIGR00552  25 VVLGLSGGIDSAvVAALCVEALGEQNHALLLPHSVQTPEQ-------DVQDALALAEPLGINYKNIDI-----APIAASF 92

                          90       100       110
                  ....*....|....*....|....*....|...
gi 21312518    86 LNEYEKGrTPNPDI----NCNKHIKFSCFYHYA 114
Cdd:TIGR00552  93 QAQTETG-DELSDFlakgNLKARLRMAALYAIA 124
PRK13980 PRK13980
NAD synthetase; Provisional
 7-96 3.17e-03

NAD synthetase; Provisional


Pssm-ID: 184435 [Multi-domain]  Cd Length: 265  Bit Score: 39.04  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518    7 VVCALSGGVDSAVAALLLRRR-GYQ-VTGVFMKNWDSLDEqgvcaadkDCEDAYKVCQILDIPfHQVSYVKEYwNDVFSD 84
Cdd:PRK13980  33 VVLGLSGGIDSAVVAYLAVKAlGKEnVLALLMPSSVSPPE--------DLEDAELVAEDLGIE-YKVIEITPI-VDAFFS 102

                         90
                 ....*....|..
gi 21312518   85 FLNEYEKGRTPN 96
Cdd:PRK13980 103 AIPDADRLRVGN 114
QueC COG0603
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ...
 5-31 5.06e-03

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: 38.22  E-value: 5.06e-03
                        10        20
                ....*....|....*....|....*..
gi 21312518   5 RHVVCALSGGVDSAVAALLLRRRGYQV 31
Cdd:COG0603   3 KKAVVLLSGGLDSTTCLAWALARGYEV 29
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 6-127 5.53e-03

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: 37.57  E-value: 5.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518   6 HVVCALSGGVDSAVAALLLRRRGYQvtgvfmKNWDsldeqgVCAA----------DKDCEDAYKVCQILDIPFHQVSyvk 75
Cdd:cd01992   1 KILVAVSGGPDSMALLHLLKELRPK------LGLK------LVAVhvdhglreesAEEAQFVAKLCKKLGIPLHILT--- 65

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 21312518  76 eyWNDVFSDFLNEYEKGRTpnpdincnkhIKFSCFYHYAVDNlGADAVATGH 127
Cdd:cd01992  66 --VTEAPKSGGNLEAAARE----------ARYAFLERAAKEH-GIDVLLTAH 104
PRK08349 PRK08349
hypothetical protein; Validated
 7-47 5.80e-03

hypothetical protein; Validated


Pssm-ID: 169396  Cd Length: 198  Bit Score: 37.79  E-value: 5.80e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 21312518    7 VVCALSGGVDSAVAALLLRRRGYQVTGVFMKNwDSLDEQGV 47
Cdd:PRK08349   3 AVALLSSGIDSPVAIYLMLRRGVEVYPVHFRQ-DEKKEEKV 42
ThiI COG0301
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ...
 6-35 5.90e-03

Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis]; Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440070 [Multi-domain]  Cd Length: 382  Bit Score: 38.53  E-value: 5.90e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 21312518   6 HVVCALSGGVDSAVAALLLRRRGYQVTGVF 35
Cdd:COG0301 176 KVLLLLSGGIDSPVAAYLMMKRGVEVEAVH 205
COG1365 COG1365
Predicted ATPase, PP-loop superfamily [General function prediction only];
7-126 8.38e-03

Predicted ATPase, PP-loop superfamily [General function prediction only];


Pssm-ID: 440976  Cd Length: 256  Bit Score: 37.72  E-value: 8.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312518   7 VVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWDSLDEQGVcaadkdcEDAYKVCQILDIpfhQVSYVKEYWNDVFSDFL 86
Cdd:COG1365  63 VVVAFSGGVDSSASLIIAKWIGFDVEAVTVKSTIILPQMFK-------KNIKELCKKLNV---KHEFIEIDLGEIIEDAL 132

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 21312518  87 neyeKGRTPnPDINCNKHIKfSCFYHYAVDNlGADAVATG 126
Cdd:COG1365 133 ----KGKFH-PCGRCHSLIE-EAVEDYAKKN-GIKIVIFG 165
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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