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Conserved domains on  [gi|1277938138|gb|PIV37161|]
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MAG: tRNA 2-thiouridine(34) synthase MnmA [Sulfurimonas sp. CG02_land_8_20_14_3_00_36_67]

Protein Classification

tRNA 2-thiouridine(34) synthase MnmA( domain architecture ID 10791795)

tRNA 2-thiouridine(34) synthase MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln) to form 5-taurinomethyl-2-thiouridine (tm5s2U)

CATH:  2.30.30.280|3.40.50.620
EC:  2.8.1.13
Gene Symbol:  mnmA
Gene Ontology:  GO:0005524|GO:0016783|GO:0000049|GO:0006400
PubMed:  3298234|16387657|16871210|12012333
SCOP:  4007171

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
 4-340 1.45e-157

tRNA-specific 2-thiouridylase MnmA; Reviewed


:

Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 444.90  E-value: 1.45e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   4 KKVLVGMSGGVDSTVSTLLLQEEGYEVEGLYMKLHSKPG-------YHEIHQARAQKAADYVGIKLHVLDLQKVFNEKVF 76
Cdd:PRK00143    1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVFMKLWDDDDetgkggcCAEEDIADARRVADKLGIPHYVVDFEKEFWDRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138  77 QPFITSYEKGNTPNPCALCNRNLKFGEMMKYAETIGADYLATGHYIKT-DGKNFYMAEDDTKDQSYFLFYVDKAILPKLL 155
Cdd:PRK00143   81 DYFLDEYKAGRTPNPCVLCNKEIKFKAFLEYARELGADYIATGHYARIrDGRELLRGVDPNKDQSYFLYQLTQEQLAKLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138 156 FPLGSRKKSDIKKFASSIkGLeSFASQAESSEICFVET-TYTDLLKDYVDVDnAGEVLDKDGNVVGEHKGYMHYTVGKRK 234
Cdd:PRK00143  161 FPLGELTKPEVREIAEEA-GL-PVAKKKDSQGICFIGErDYRDFLKRYLPAQ-PGEIVDLDGKVLGEHKGLMYYTIGQRK 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138 235 GFTVNGAHEPHYVLSTNPETNQIVVGTKEDLACGSVILNNLNMFND---LKEFDTTVKLRYRTRSIECHVKIENDKAFVT 311
Cdd:PRK00143  238 GLGIGGDGEPWYVVGKDPETNTVVVGQGEALYSRELIASDLNWVGGeppEEPFECTAKIRYRQKPVPATVELEDDRVEVE 317

                         330       340
                  ....*....|....*....|....*....
gi 1277938138 312 LKEDVFGVAVGQAAVFYDEDKLIGGGWIA 340
Cdd:PRK00143  318 FDEPQRAVTPGQAAVFYDGDRVLGGGIIE 346
 
Name Accession Description Interval E-value
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
 4-340 1.45e-157

tRNA-specific 2-thiouridylase MnmA; Reviewed


Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 444.90  E-value: 1.45e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   4 KKVLVGMSGGVDSTVSTLLLQEEGYEVEGLYMKLHSKPG-------YHEIHQARAQKAADYVGIKLHVLDLQKVFNEKVF 76
Cdd:PRK00143    1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVFMKLWDDDDetgkggcCAEEDIADARRVADKLGIPHYVVDFEKEFWDRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138  77 QPFITSYEKGNTPNPCALCNRNLKFGEMMKYAETIGADYLATGHYIKT-DGKNFYMAEDDTKDQSYFLFYVDKAILPKLL 155
Cdd:PRK00143   81 DYFLDEYKAGRTPNPCVLCNKEIKFKAFLEYARELGADYIATGHYARIrDGRELLRGVDPNKDQSYFLYQLTQEQLAKLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138 156 FPLGSRKKSDIKKFASSIkGLeSFASQAESSEICFVET-TYTDLLKDYVDVDnAGEVLDKDGNVVGEHKGYMHYTVGKRK 234
Cdd:PRK00143  161 FPLGELTKPEVREIAEEA-GL-PVAKKKDSQGICFIGErDYRDFLKRYLPAQ-PGEIVDLDGKVLGEHKGLMYYTIGQRK 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138 235 GFTVNGAHEPHYVLSTNPETNQIVVGTKEDLACGSVILNNLNMFND---LKEFDTTVKLRYRTRSIECHVKIENDKAFVT 311
Cdd:PRK00143  238 GLGIGGDGEPWYVVGKDPETNTVVVGQGEALYSRELIASDLNWVGGeppEEPFECTAKIRYRQKPVPATVELEDDRVEVE 317

                         330       340
                  ....*....|....*....|....*....
gi 1277938138 312 LKEDVFGVAVGQAAVFYDEDKLIGGGWIA 340
Cdd:PRK00143  318 FDEPQRAVTPGQAAVFYDGDRVLGGGIIE 346
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
 5-339 7.82e-145

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: 412.67  E-value: 7.82e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   5 KVLVGMSGGVDSTVSTLLLQEEGYEVEGLYMKLHSK--------PGYHEIHqaRAQKAADYVGIKLHVLDLQKVFNEKVF 76
Cdd:cd01998     1 KVAVAMSGGVDSSVAAALLKEQGYDVIGVFMKNWDDednekggcCSEEDIE--DARRVADQLGIPLYVVDFSEEYWERVF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138  77 QPFITSYEKGNTPNPCALCNRNLKFGEMMKYAETIGADYLATGHYIKTDGKNF-----YMAEDDTKDQSYFLFYVDKAIL 151
Cdd:cd01998    79 DPFLEEYKAGRTPNPDVLCNREIKFGALLDAAKKLGADYIATGHYARIEEDNRgryrlLRAVDPNKDQSYFLSRLSQEQL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138 152 PKLLFPLGSRKKSDIKKFASSIkGLEsFASQAESSEICFV-ETTYTDLLKDYVDVDNAGEVLDKDGNVVGEHKGYMHYTV 230
Cdd:cd01998   159 SRTLFPLGHLTKSEVREIAREA-GLP-VAEKKDSQGICFIgKRDFRDFLKEYLPEKLPGPIVDIDGKVLGEHKGLWFYTI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138 231 GKRKGFTVnGAHEPHYVLSTNPETNQIVVGT-KEDLACGSVILNNLNMFND---LKEFDTTVKLRYRTRSIECHVKI-EN 305
Cdd:cd01998   237 GQRKGLGI-AAGEPLYVVKKDPEKNIVVVGPgHPALFSDTLRASDLNWISPeppLEPLECEAKIRYRQPPVPCTVTPlDD 315

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1277938138 306 DKAFVTLKEDVFGVAVGQAAVFYDEDKLIGGGWI 339
Cdd:cd01998   316 GRLKVEFDEPQRAVTPGQAAVFYDGDEVLGGGII 349
MnmA COG0482
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ...
 4-342 6.71e-141

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: 402.90  E-value: 6.71e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   4 KKVLVGMSGGVDSTVSTLLLQEEGYEVEGLYMKLHSKPGYHE---------IHQARAqkAADYVGIKLHVLDLQKVFNEK 74
Cdd:COG0482     1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVTMKLWDDDDASGsggccsledIEDARR--VADKLGIPHYVVDFEEEFKDR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138  75 VFQPFITSYEKGNTPNPCALCNRNLKFGEMMKYAETIGADYLATGHYIKTDGKN----FYMAEDDTKDQSYFLFYVDKAI 150
Cdd:COG0482    79 VIDYFLDEYLAGRTPNPCVLCNREIKFGALLEKALELGADYIATGHYARVEEKDgryeLLRGVDPNKDQSYFLYRLTQEQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138 151 LPKLLFPLGSRKKSDIKKFASSIkGLeSFASQAESSEICFV-ETTYTDLLKDYVDvDNAGEVLDKDGNVVGEHKGYMHYT 229
Cdd:COG0482   159 LSKTLFPLGELTKPEVREIAEEL-GL-PVADKKDSQGICFIgDGDYRDFLERYLP-EKPGDIVDLDGKVLGEHDGLHYYT 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138 230 VGKRKGFTVnGAHEPHYVLSTNPETNQIVVGTKEDLACGSVILNNLNMFNDL---KEFDTTVKLRYRTRSIECHV-KIEN 305
Cdd:COG0482   236 IGQRKGLGI-GGGEPLYVVGKDPETNTVIVGQGEALYSRELTAEDVNWISGEppeEPLRCTAKIRYRQPPVPATLtPLED 314

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1277938138 306 DKAFVTLKEDVFGVAVGQAAVFYDEDKLIGGGWIAEA 342
Cdd:COG0482   315 GRVRVEFDEPQRAVTPGQSAVFYDGDRVLGGGIIERT 351
trmU TIGR00420
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ...
 4-339 2.87e-110

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: 325.11  E-value: 2.87e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   4 KKVLVGMSGGVDSTVSTLLLQEEGYEVEGLYMKLHSKPGYHEIHQ-------ARAQKAADYVGIKLHVLDLQKVFNEKVF 76
Cdd:TIGR00420   1 KKVIVGLSGGVDSSVSAYLLKQQGYEVVGVFMKNWEEDDKNDGHGctsaedlRDAQAICEKLGIPLEKVNFQKEYWNKVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138  77 QPFITSYEKGNTPNPCALCNRNLKFGEMMKYA-ETIGADYLATGHY--IKTDGKNFYMAE--DDTKDQSYFLFYVDKAIL 151
Cdd:TIGR00420  81 EPFIQEYKEGRTPNPDILCNKFIKFGAFLEYAaELLGNDKIATGHYarIAEIEGKSLLLRalDKNKDQSYFLYHLSHEQL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138 152 PKLLFPLGSRKKSDIKKFASSIkGLESfASQAESSEICFV-ETTYTDLLKDYVDVdNAGEVLDKDG-NVVGEHKGYMHYT 229
Cdd:TIGR00420 161 AKLLFPLGELLKPEVRQIAKNA-GLPT-AEKKDSQGICFIgERKFRDFLKKYLPV-KPGVIITVDGqSVIGEHDGLWFYT 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138 230 VGKRKGFTVNGAHEPHYVLSTNPETNQIVVG-TKEDLACGSVILNNLNMFNDLK---EFDTTVKLRYRTRSIECHVK-IE 304
Cdd:TIGR00420 238 IGQRKGLGIGGAAEPWFVVEKDLETNELVVShGKPDLASRGLLAQQFHWLDDEPnpfEMRCTVKIRYRQVPVQCKLKlLD 317

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1277938138 305 NDKAFVTLKEDVFGVAVGQAAVFYDEDKLIGGGWI 339
Cdd:TIGR00420 318 DNLIEVIFDEPQAGVTPGQSAVLYKGDICLGGGII 352
tRNA_Me_trans pfam03054
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ...
 4-192 1.19e-71

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: 221.36  E-value: 1.19e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   4 KKVLVGMSGGVDSTVSTLLLQEEGYEVEGLYMKLHSKPGYHEIHQ--------ARAQKAADYVGIKLHVLDLQKVFNEKV 75
Cdd:pfam03054   1 MKVVVAMSGGVDSSVAAYLLKEQGHNVIGVFMKNWDEEQSLDEEGkccseedlADAQRVCEQLGIPLYVVNFEKEYWEDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138  76 FQPFITSYEKGNTPNPCALCNRNLKFGEMMKYA-ETIGADYLATGHYIKT---DGKNFYM--AEDDTKDQSYFLFYVDKA 149
Cdd:pfam03054  81 FEPFLDEYKNGRTPNPDVLCNKEIKFGALLDYAlENLGADYVATGHYARVslnKDGGSELlrALDKNKDQSYFLSTLSQE 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1277938138 150 ILPKLLFPLGSRKKSDIKKFASSIkGLESfASQAESSEICFVE 192
Cdd:pfam03054 161 QLEKLLFPLGELTKEEVRKIAKEA-GLAT-AKKKDSQGICFIG 201
 
Name Accession Description Interval E-value
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
 4-340 1.45e-157

tRNA-specific 2-thiouridylase MnmA; Reviewed


Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 444.90  E-value: 1.45e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   4 KKVLVGMSGGVDSTVSTLLLQEEGYEVEGLYMKLHSKPG-------YHEIHQARAQKAADYVGIKLHVLDLQKVFNEKVF 76
Cdd:PRK00143    1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVFMKLWDDDDetgkggcCAEEDIADARRVADKLGIPHYVVDFEKEFWDRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138  77 QPFITSYEKGNTPNPCALCNRNLKFGEMMKYAETIGADYLATGHYIKT-DGKNFYMAEDDTKDQSYFLFYVDKAILPKLL 155
Cdd:PRK00143   81 DYFLDEYKAGRTPNPCVLCNKEIKFKAFLEYARELGADYIATGHYARIrDGRELLRGVDPNKDQSYFLYQLTQEQLAKLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138 156 FPLGSRKKSDIKKFASSIkGLeSFASQAESSEICFVET-TYTDLLKDYVDVDnAGEVLDKDGNVVGEHKGYMHYTVGKRK 234
Cdd:PRK00143  161 FPLGELTKPEVREIAEEA-GL-PVAKKKDSQGICFIGErDYRDFLKRYLPAQ-PGEIVDLDGKVLGEHKGLMYYTIGQRK 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138 235 GFTVNGAHEPHYVLSTNPETNQIVVGTKEDLACGSVILNNLNMFND---LKEFDTTVKLRYRTRSIECHVKIENDKAFVT 311
Cdd:PRK00143  238 GLGIGGDGEPWYVVGKDPETNTVVVGQGEALYSRELIASDLNWVGGeppEEPFECTAKIRYRQKPVPATVELEDDRVEVE 317

                         330       340
                  ....*....|....*....|....*....
gi 1277938138 312 LKEDVFGVAVGQAAVFYDEDKLIGGGWIA 340
Cdd:PRK00143  318 FDEPQRAVTPGQAAVFYDGDRVLGGGIIE 346
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
 5-339 7.82e-145

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: 412.67  E-value: 7.82e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   5 KVLVGMSGGVDSTVSTLLLQEEGYEVEGLYMKLHSK--------PGYHEIHqaRAQKAADYVGIKLHVLDLQKVFNEKVF 76
Cdd:cd01998     1 KVAVAMSGGVDSSVAAALLKEQGYDVIGVFMKNWDDednekggcCSEEDIE--DARRVADQLGIPLYVVDFSEEYWERVF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138  77 QPFITSYEKGNTPNPCALCNRNLKFGEMMKYAETIGADYLATGHYIKTDGKNF-----YMAEDDTKDQSYFLFYVDKAIL 151
Cdd:cd01998    79 DPFLEEYKAGRTPNPDVLCNREIKFGALLDAAKKLGADYIATGHYARIEEDNRgryrlLRAVDPNKDQSYFLSRLSQEQL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138 152 PKLLFPLGSRKKSDIKKFASSIkGLEsFASQAESSEICFV-ETTYTDLLKDYVDVDNAGEVLDKDGNVVGEHKGYMHYTV 230
Cdd:cd01998   159 SRTLFPLGHLTKSEVREIAREA-GLP-VAEKKDSQGICFIgKRDFRDFLKEYLPEKLPGPIVDIDGKVLGEHKGLWFYTI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138 231 GKRKGFTVnGAHEPHYVLSTNPETNQIVVGT-KEDLACGSVILNNLNMFND---LKEFDTTVKLRYRTRSIECHVKI-EN 305
Cdd:cd01998   237 GQRKGLGI-AAGEPLYVVKKDPEKNIVVVGPgHPALFSDTLRASDLNWISPeppLEPLECEAKIRYRQPPVPCTVTPlDD 315

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1277938138 306 DKAFVTLKEDVFGVAVGQAAVFYDEDKLIGGGWI 339
Cdd:cd01998   316 GRLKVEFDEPQRAVTPGQAAVFYDGDEVLGGGII 349
MnmA COG0482
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ...
 4-342 6.71e-141

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: 402.90  E-value: 6.71e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   4 KKVLVGMSGGVDSTVSTLLLQEEGYEVEGLYMKLHSKPGYHE---------IHQARAqkAADYVGIKLHVLDLQKVFNEK 74
Cdd:COG0482     1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVTMKLWDDDDASGsggccsledIEDARR--VADKLGIPHYVVDFEEEFKDR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138  75 VFQPFITSYEKGNTPNPCALCNRNLKFGEMMKYAETIGADYLATGHYIKTDGKN----FYMAEDDTKDQSYFLFYVDKAI 150
Cdd:COG0482    79 VIDYFLDEYLAGRTPNPCVLCNREIKFGALLEKALELGADYIATGHYARVEEKDgryeLLRGVDPNKDQSYFLYRLTQEQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138 151 LPKLLFPLGSRKKSDIKKFASSIkGLeSFASQAESSEICFV-ETTYTDLLKDYVDvDNAGEVLDKDGNVVGEHKGYMHYT 229
Cdd:COG0482   159 LSKTLFPLGELTKPEVREIAEEL-GL-PVADKKDSQGICFIgDGDYRDFLERYLP-EKPGDIVDLDGKVLGEHDGLHYYT 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138 230 VGKRKGFTVnGAHEPHYVLSTNPETNQIVVGTKEDLACGSVILNNLNMFNDL---KEFDTTVKLRYRTRSIECHV-KIEN 305
Cdd:COG0482   236 IGQRKGLGI-GGGEPLYVVGKDPETNTVIVGQGEALYSRELTAEDVNWISGEppeEPLRCTAKIRYRQPPVPATLtPLED 314

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1277938138 306 DKAFVTLKEDVFGVAVGQAAVFYDEDKLIGGGWIAEA 342
Cdd:COG0482   315 GRVRVEFDEPQRAVTPGQSAVFYDGDRVLGGGIIERT 351
trmU TIGR00420
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ...
 4-339 2.87e-110

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: 325.11  E-value: 2.87e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   4 KKVLVGMSGGVDSTVSTLLLQEEGYEVEGLYMKLHSKPGYHEIHQ-------ARAQKAADYVGIKLHVLDLQKVFNEKVF 76
Cdd:TIGR00420   1 KKVIVGLSGGVDSSVSAYLLKQQGYEVVGVFMKNWEEDDKNDGHGctsaedlRDAQAICEKLGIPLEKVNFQKEYWNKVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138  77 QPFITSYEKGNTPNPCALCNRNLKFGEMMKYA-ETIGADYLATGHY--IKTDGKNFYMAE--DDTKDQSYFLFYVDKAIL 151
Cdd:TIGR00420  81 EPFIQEYKEGRTPNPDILCNKFIKFGAFLEYAaELLGNDKIATGHYarIAEIEGKSLLLRalDKNKDQSYFLYHLSHEQL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138 152 PKLLFPLGSRKKSDIKKFASSIkGLESfASQAESSEICFV-ETTYTDLLKDYVDVdNAGEVLDKDG-NVVGEHKGYMHYT 229
Cdd:TIGR00420 161 AKLLFPLGELLKPEVRQIAKNA-GLPT-AEKKDSQGICFIgERKFRDFLKKYLPV-KPGVIITVDGqSVIGEHDGLWFYT 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138 230 VGKRKGFTVNGAHEPHYVLSTNPETNQIVVG-TKEDLACGSVILNNLNMFNDLK---EFDTTVKLRYRTRSIECHVK-IE 304
Cdd:TIGR00420 238 IGQRKGLGIGGAAEPWFVVEKDLETNELVVShGKPDLASRGLLAQQFHWLDDEPnpfEMRCTVKIRYRQVPVQCKLKlLD 317

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1277938138 305 NDKAFVTLKEDVFGVAVGQAAVFYDEDKLIGGGWI 339
Cdd:TIGR00420 318 DNLIEVIFDEPQAGVTPGQSAVLYKGDICLGGGII 352
PRK14664 PRK14664
tRNA-specific 2-thiouridylase MnmA; Provisional
 2-343 8.36e-85

tRNA-specific 2-thiouridylase MnmA; Provisional


Pssm-ID: 173127 [Multi-domain]  Cd Length: 362  Bit Score: 260.66  E-value: 8.36e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   2 KKKKVLVGMSGGVDSTVSTLLLQEEGYEVEGLYMKLHSKpgyhEIHQARAqkAADYVGIKLHVLDLQKVFNEKVFQPFIT 81
Cdd:PRK14664    4 SKKRVLVGMSGGIDSTATCLMLQEQGYEIVGVTMRVWGD----EPQDARE--LAARMGIEHYVADERVPFKDTIVKNFID 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138  82 SYEKGNTPNPCALCNRNLKFGEMMKYAETIGADYLATGHYIKTDGKNFYM----AEDDTKDQSYFLFYVDKAILPKLLFP 157
Cdd:PRK14664   78 EYRQGRTPNPCVMCNPLFKFRMLIEWADKLGCAWIATGHYSRLEERNGHIyivaGDDDKKDQSYFLWRLGQDILRRCIFP 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138 158 LGSRKKSDIKKFASSiKGLESFASQAESSEICFVETTYTDLLKDYV-DVD---NAGEVLDKDGNVVGEHKGYMHYTVGKR 233
Cdd:PRK14664  158 LGNYTKQTVREYLRE-KGYEAKSKEGESMEVCFIKGDYRDFLREQCpELDtevGPGWFVNSEGVKLGQHKGFPYYTIGQR 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138 234 KGFTVNGAHePHYVLSTNPETNQIVVGTKEDLACGSVILNNLNMFNDLKEF---DTTVKLRYRTRSIECHVK-IENDKAF 309
Cdd:PRK14664  237 KGLEIALGK-PAYVLKINPQKNTVMLGDAEQLKAEYMLAEQDNIVDEQELFacpDLAVRIRYRSRPIPCRVKrLEDGRLL 315

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1277938138 310 VTLKEDVFGVAVGQAAVFYDEDKLIGGGWIAEAK 343
Cdd:PRK14664  316 VRFLAEASAIAPGQSAVFYEGRRVLGGAFIASQR 349
tRNA_Me_trans pfam03054
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ...
 4-192 1.19e-71

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: 221.36  E-value: 1.19e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   4 KKVLVGMSGGVDSTVSTLLLQEEGYEVEGLYMKLHSKPGYHEIHQ--------ARAQKAADYVGIKLHVLDLQKVFNEKV 75
Cdd:pfam03054   1 MKVVVAMSGGVDSSVAAYLLKEQGHNVIGVFMKNWDEEQSLDEEGkccseedlADAQRVCEQLGIPLYVVNFEKEYWEDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138  76 FQPFITSYEKGNTPNPCALCNRNLKFGEMMKYA-ETIGADYLATGHYIKT---DGKNFYM--AEDDTKDQSYFLFYVDKA 149
Cdd:pfam03054  81 FEPFLDEYKNGRTPNPDVLCNKEIKFGALLDYAlENLGADYVATGHYARVslnKDGGSELlrALDKNKDQSYFLSTLSQE 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1277938138 150 ILPKLLFPLGSRKKSDIKKFASSIkGLESfASQAESSEICFVE 192
Cdd:pfam03054 161 QLEKLLFPLGELTKEEVRKIAKEA-GLAT-AKKKDSQGICFIG 201
mnmA PRK14665
tRNA-specific 2-thiouridylase MnmA; Provisional
 2-341 8.54e-71

tRNA-specific 2-thiouridylase MnmA; Provisional


Pssm-ID: 173128 [Multi-domain]  Cd Length: 360  Bit Score: 224.43  E-value: 8.54e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   2 KKKKVLVGMSGGVDSTVSTLLLQEEGYEVEGLYMKLHSKPGYHE-IHQARAqkAADYVGIKLHVLDLQKVFNEKVFQPFI 80
Cdd:PRK14665    4 KNKRVLLGMSGGTDSSVAAMLLLEAGYEVTGVTFRFYEFNGSTEyLEDARA--LAERLGIGHITYDARKVFRKQIIDYFI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138  81 TSYEKGNTPNPCALCNRNLKFGEMMKYAETIGADYLATGHYI---KTDGkNFYM--AEDDTKDQSYFLFYVDKAILPKLL 155
Cdd:PRK14665   82 DEYMSGHTPVPCTLCNNYLKWPLLAKIADEMGIFYLATGHYVrkqWIDG-NYYItpAEDVDKDQSFFLWGLRQEILQRML 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138 156 FPLGSRKKSDIKKFASSiKGLESFASQAESSEICFVETTYTDLLKDYVdVDNA-------------GEVLDKDGNVVGEH 222
Cdd:PRK14665  161 LPMGGMTKSEARAYAAE-RGFEKVAKKRDSLGVCFCPMDYRSFLKKCL-CDESgdknrniyrkverGRFLDESGNFIAWH 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138 223 KGYMHYTVGKRKGFTVNgAHEPHYVLSTNPETNQIVVGTKEDLACGSVILNNLNMFND---LKEFDTTVKLRYRTRSIEC 299
Cdd:PRK14665  239 EGYPFYTIGQRRGLGIQ-LNRAVFVKEIHPETNEVVLASLKALEKTEMWLKDWNIVNEsrlLGCDDIIVKIRYRKQENHC 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1277938138 300 HVKIENDKAF-VTLKEDVFGVAVGQAAVFYDEDKLIGGGWIAE 341
Cdd:PRK14665  318 TVTITPDNLLhVQLHEPLTAIAEGQAAAFYKDGLLLGGGIITM 360
tRNA_Me_trans_M pfam20259
tRNA methyl transferase PRC-barrel domain; This family represents a central PRC-barrel domain ...
 197-260 8.56e-16

tRNA methyl transferase PRC-barrel domain; This family represents a central PRC-barrel domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs.


Pssm-ID: 466410 [Multi-domain]  Cd Length: 66  Bit Score: 71.10  E-value: 8.56e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277938138 197 DLLKDYVDVdNAGEVLDKD-GNVVGEHKGYMHYTVGKRKGFTVNGAHEPHYVLSTNPETNQIVVG 260
Cdd:pfam20259   2 DFLKEYLPV-KPGDIIDIDtGEVLGEHEGIWFYTIGQRKGLGIGGYGEPWYVVEKDPKKNTVYVG 65
tRNA_Me_trans_C pfam20258
Aminomethyltransferase beta-barrel domain; This domain is found at the C-terminus of tRNA ...
 272-339 2.13e-15

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: 70.38  E-value: 2.13e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277938138 272 LNNLNMFNDLKEFDTTVKLRYRTRSIECHVK-IENDKAFVTLKEDVFGVAVGQAAVFYDEDKLIGGGWI 339
Cdd:pfam20258   9 PNWLGDKPPTEPLECTVKVRHRQPPVPCVVElIDDETVEVHFDEPVRAVTPGQAAVFYDGDRCLGGGII 77
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 2-120 7.01e-14

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: 70.25  E-value: 7.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   2 KKKKVLVGMSGGVDSTVSTLLL----QEEGYEVEGLYMKlHSKPGYHEIHQARAQKAADYVGIKLHVLDLQkvfnekvfq 77
Cdd:COG0037    14 PGDRILVAVSGGKDSLALLHLLaklrRRLGFELVAVHVD-HGLREESDEDAEFVAELCEELGIPLHVVRVD--------- 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1277938138  78 pfITSYEKGNTPNPCALCnRNLKFGEMMKYAETIGADYLATGH 120
Cdd:COG0037    84 --VPAIAKKEGKSPEAAA-RRARYGALYELARELGADKIATGH 123
TtuA-like cd01993
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ...
 2-120 5.66e-11

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: 60.80  E-value: 5.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   2 KKKKVLVGMSGGVDSTVSTLLLQEEGYEVEGLYMKLhSKPGYHEIHQARAQKAADYVGIKLHVLDLQKVFNEKVFQPFIT 81
Cdd:cd01993     7 KDDKILVAVSGGKDSLALLAVLKKLGYNVEALYINL-GIGEYSEKSEEVVKKLAEKLNLPLHVVDLKEEYGLGIPELAKK 85

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1277938138  82 SYEKgntpnPCALCNRnLKFGEMMKYAETIGADYLATGH 120
Cdd:cd01993    86 SRRP-----PCSVCGL-VKRYIMNKFAVENGFDVVATGH 118
QueC-like cd01995
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ...
 4-119 4.59e-10

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: 58.78  E-value: 4.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   4 KKVLVGMSGGVDSTVSTLLLQEEGYEVEGLYMKLHSKpgyHEIHQARAQK-AADYVGIKLHVLDLQKV--------FNEK 74
Cdd:cd01995     1 MKAVVLLSGGLDSTTLLYWALKEGYEVHALTFDYGQR---HAKEELEAAKlIAKLLGIEHKVIDLSFLgelggsslTDEG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1277938138  75 VFQPFITSYEKG--NTPNPcalcNRNLKF-----GemmkYAETIGADYLATG 119
Cdd:cd01995    78 EEVPDGEYDEESipSTWVP----NRNLIFlsiaaA----YAESLGASAIVIG 121
TtcA-like cd24138
tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) ...
 5-120 2.14e-09

tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) 2-sulfurtransferase, also called two-thiocytidine biosynthesis protein A or tRNA 2-thiocytidine biosynthesis protein TtcA, catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). TtcA 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: 467514 [Multi-domain]  Cd Length: 187  Bit Score: 56.13  E-value: 2.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   5 KVLVGMSGGVDSTVSTLLLQE------EGYEVEGLymklHSKPGYHEIHQARA--QKAADYVGIKLHVLDLQKVFNEKvf 76
Cdd:cd24138    10 RILVGLSGGKDSLTLLHLLEElkrrapIKFELVAV----TVDPGYPGYRPPREelAEILEELGEILEDEESEIIIIEK-- 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1277938138  77 qpfitsYEKGNtpNPCALCNRnLKFGEMMKYAETIGADYLATGH 120
Cdd:cd24138    84 ------EREEK--SPCSLCSR-LRRGILYSLAKELGCNKLALGH 118
QueC pfam06508
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ...
 5-119 1.85e-08

Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis of 7-carboxy-7-deazaguanine. They catalyze the conversion of 7-deaza-7-carboxyguanine to preQ0.


Pssm-ID: 428982 [Multi-domain]  Cd Length: 210  Bit Score: 53.78  E-value: 1.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   5 KVLVGMSGGVDSTVSTLLLQEEGYEVEGLYMKLHSKpgyHEIHQARAQKAADYVGIKLHVLDLQ--KVF--------NEK 74
Cdd:pfam06508   1 KAVVLLSGGLDSTTCLAWAKKEGYEVYALSFDYGQR---HRKELECAKKIAKALGVEHKILDLDflKQIggsaltddSIE 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1277938138  75 VFQPFITSYEKGNTPNPcalcNRNLKFGEM-MKYAETIGADYLATG 119
Cdd:pfam06508  78 VPKAELESEEIPNTYVP----GRNLIFLSIaASLAEALGAEAIFIG 119
QueC COG0603
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ...
 2-119 1.89e-07

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: 50.93  E-value: 1.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   2 KKKKVLVGMSGGVDSTVSTLLLQEEGYEVEGLYMKLHSKpgyHEIHQARAQKAADYVGIK-LHVLDLQKV---------- 70
Cdd:COG0603     1 MMKKAVVLLSGGLDSTTCLAWALARGYEVYALSFDYGQR---HRKELEAARRIAKALGVGeHKVIDLDFLgeiggsaltd 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1277938138  71 FNEKVfqPFiTSYEKGNTPN---PcalcNRNLKFGEMM-KYAETIGADYLATG 119
Cdd:COG0603    78 DSIEV--PE-GHYAEEGIPStyvP----GRNLIFLSIAaAYAEALGAEDIFIG 123
TIGR00364 TIGR00364
queuosine biosynthesis protein QueC; Members of this protein family are QueC, involved in ...
 7-119 2.07e-07

queuosine biosynthesis protein QueC; Members of this protein family are QueC, involved in synthesizing pre-Q0 from GTP en route to tRNA modification with queuosine. This protein family is represented by a single member in nearly every completed large (> 1000 genes) prokaryotic genome. In Rhizobium meliloti, the gene was designated exsB, possibly because of polar effects on exsA expression in a shared polycistronic mRNA. In Arthrobacter viscosus, the homologous gene was designated ALU1 and was associated with an aluminum tolerance phenotype. [Unknown function, General]


Pssm-ID: 129461 [Multi-domain]  Cd Length: 201  Bit Score: 50.85  E-value: 2.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   7 LVGMSGGVDSTVSTLLLQEEGYEVEGL---YMKLHSKpgyhEIHQARaqKAADYVGIKLHVLDLQKV--------FNEKV 75
Cdd:TIGR00364   2 IVVLSGGQDSTTCLLWAKDEGYEVHAVtfdYGQRHSR----ELESAR--KIAEALGIEHHLLDLSLLnqlggsalTREQE 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1277938138  76 fQPFITSYEKGNTPN---PcalcNRNLKF-GEMMKYAETIGADYLATG 119
Cdd:TIGR00364  76 -IPEQKSNEEDTLPNtfvP----GRNLVFlSIAASYAEAIGAEAIITG 118
LarE-like cd01990
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ...
 5-138 4.33e-07

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: 49.95  E-value: 4.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   5 KVLVGMSGGVDST-VSTLLLQEEGYEVEGLYMKLHSKPGyHEIHQARAQkaADYVGIKLHVLDLQKVFNEkvfqpfitSY 83
Cdd:cd01990     1 KVVVAFSGGVDSSlLAKLAKEVLGDNVVAVTADSPLVPR-EELEEAKRI--AEEIGIRHEIIKTDELDDE--------EY 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1277938138  84 EKgNTPNPCALCNRNLkFGEMMKYAETIGADYLAtghyiktDGKNFymaeDDTKD 138
Cdd:cd01990    70 VA-NDPDRCYHCKKAL-YSTLKEIAKERGYDVVL-------DGTNA----DDLKD 111
CTU1-like cd01713
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ...
 2-120 4.34e-07

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: 49.89  E-value: 4.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   2 KKKKVLVGMSGGVDSTVSTLLLQE----EGYEV--------EGLymklhskPGYHEIHQARAQKAADYVGIKLHVLDLQK 69
Cdd:cd01713    17 PGDRVAVGLSGGKDSTVLLYVLKElnkrHDYGVeliavtidEGI-------KGYRDDSLEAARKLAEEYGIPLEIVSFED 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1277938138  70 VFNekvfqpfITSYE----KGNTPNPCALC---NRNLkfgeMMKYAETIGADYLATGH 120
Cdd:cd01713    90 EFG-------FTLDElivgKGGKKNACTYCgvfRRRA----LNRGARELGADKLATGH 136
COG1365 COG1365
Predicted ATPase, PP-loop superfamily [General function prediction only];
2-119 6.49e-07

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


Pssm-ID: 440976  Cd Length: 256  Bit Score: 50.05  E-value: 6.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   2 KKKKVLVGMSGGVDSTVSTLLLQEEGYEVEGLYMKlhSKPGYHEIHQARAQKAADYVGIKLHVLDLQkvfnekvFQPFIT 81
Cdd:COG1365    59 KNPKVVVAFSGGVDSSASLIIAKWIGFDVEAVTVK--STIILPQMFKKNIKELCKKLNVKHEFIEID-------LGEIIE 129

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1277938138  82 SYEKGNTPnPCALCNRnLKFGEMMKYAETIGADYLATG 119
Cdd:COG1365   130 DALKGKFH-PCGRCHS-LIEEAVEDYAKKNGIKIVIFG 165
PPase_ThiI cd01712
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole ...
 5-119 7.09e-07

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: 48.70  E-value: 7.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   5 KVLVGMSGGVDSTVSTLLLQEEGYEVEGLYMKLhskPGYHeiHQARAQKAADYV--------GIKLHVldlqKVFNEKVF 76
Cdd:cd01712     6 KVLVLLSGGIDSPVAAWMMMKRGVEVDFLHFHS---GPYT--SEKAVEKVKDLArvlseyqgGVKLYL----VPFTDKIQ 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1277938138  77 QPFItsyEKGNTPNPCALCNRnlkfgeMM-----KYAETIGADYLATG 119
Cdd:cd01712    77 KEIL---EKVPESYRIVLMRR------MMyriaeKIAERLGADALVTG 115
PRK04527 PRK04527
argininosuccinate synthase; Provisional
 3-119 9.01e-06

argininosuccinate synthase; Provisional


Pssm-ID: 235305  Cd Length: 400  Bit Score: 47.14  E-value: 9.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   3 KKKVLVGMSGGVDSTVSTLLLQEEGYEVEGLYMKLhSKPGYHEIHQarAQKAADYVGIKLHV-LDLQKVFNEKVFQPFIT 81
Cdd:PRK04527    2 SKDIVLAFSGGLDTSFCIPYLQERGYAVHTVFADT-GGVDAEERDF--IEKRAAELGAASHVtVDGGPAIWEGFVKPLVW 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1277938138  82 SYEKGNTPNPCALCNRNLKFGEMMKYAETIGADYLATG 119
Cdd:PRK04527   79 AGEGYQGQYPLLVSDRYLIVDAALKRAEELGTRIIAHG 116
NadE COG0171
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ...
 4-71 2.32e-05

NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ synthetase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439941 [Multi-domain]  Cd Length: 542  Bit Score: 45.99  E-value: 2.32e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277938138   4 KKVLVGMSGGVDSTVSTLLLQEE-GYE-VEGLYMklhskPGY--HEIHQARAQKAADYVGIKLHVLDLQKVF 71
Cdd:COG0171   287 KGVVLGLSGGIDSALVAALAVDAlGPEnVLGVTM-----PSRytSDESLEDAEELAENLGIEYEEIDITPAV 353
ThiI pfam02568
Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for ...
 5-119 4.43e-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: 43.96  E-value: 4.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   5 KVLVGMSGGVDSTVSTLLLQEEGYEVEGLYMKLHSKPGYHEIHQAR--AQKAADY---VGIKLHVLDLQKVFNEKVfqpf 79
Cdd:pfam02568   5 KVLALISGGIDSPVAAYMMMRRGCRVVALHFINNPGTSAEAIGKVQklAELLARYgtsHEVRLVVFDFTDVQKEIL---- 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1277938138  80 itsyEKGNTPNPCALCNRNlkfgeMMK----YAETIGADYLATG 119
Cdd:pfam02568  81 ----EKAPEGYRCVLLKRC-----MYRiaekVAEEEGADALVTG 115
ThiI COG0301
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ...
 5-119 5.00e-05

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: 44.69  E-value: 5.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   5 KVLVGMSGGVDSTVSTLLLQEEGYEVEGLYMklHSKPGYHEIHQARAQKAADYV------GIKLHVLDLQKVFNEkvfqp 78
Cdd:COG0301   176 KVLLLLSGGIDSPVAAYLMMKRGVEVEAVHF--HSGPYTSERAEEKVKDLARKLsrygghRVKLYVVPFTEVQEE----- 248

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1277938138  79 fItsYEKGNTPNPCALCNRnlkfgEMMKYAETI----GADYLATG 119
Cdd:COG0301   249 -I--LEKVPERYRTVLLRR-----MMMRIAERIaekeGALALVTG 285
PRK10696 PRK10696
tRNA 2-thiocytidine biosynthesis protein TtcA; Provisional
 5-170 7.23e-05

tRNA 2-thiocytidine biosynthesis protein TtcA; Provisional


Pssm-ID: 236737 [Multi-domain]  Cd Length: 258  Bit Score: 43.69  E-value: 7.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   5 KVLVGMSGGVDSTvsTLL-----LQEEG-YEVEGLYMKLHSK-PGYHEiHQARaqkaaDYV---GIKLHVL--DLQKVFN 72
Cdd:PRK10696   31 RVMVCLSGGKDSY--TLLdillnLQKRApINFELVAVNLDQKqPGFPE-HVLP-----EYLeslGVPYHIEeqDTYSIVK 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138  73 EKVfqPFITSYekgntpnpCALCNRnLKFGEMMKYAETIGADYLATGHYiktdgknfymaEDDTKdQSYFL--FYVD--K 148
Cdd:PRK10696  103 EKI--PEGKTT--------CSLCSR-LRRGILYRTARELGATKIALGHH-----------RDDIL-ETLFLnmFYGGklK 159

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1277938138 149 AILPKLLF---------PLGSRKKSDIKKFA 170
Cdd:PRK10696  160 AMPPKLLSddgkhivirPLAYVAEKDIIKFA 190
ASS cd01999
argininosuccinate_synthase (ASS); Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle ...
 4-119 7.26e-05

argininosuccinate_synthase (ASS); Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle enzyme that catalyzes the penultimate step in arginine biosynthesis: the ATP-dependent ligation of citrulline to aspartate to form argininosuccinate, AMP and pyrophosphate. In humans, a defect in the ASS gene causes citrullinemia, a genetic disease characterized by severe vomiting spells and mental retardation. ASS is a homotetrameric enzyme of about 400 amino-acid residues. An arginine residue seems to be important for the enzyme's catalytic mechanism. The sequences of ASS from various prokaryotes, archaeabacteria and eukaryotes show significant similarity.


Pssm-ID: 467503  Cd Length: 386  Bit Score: 44.06  E-value: 7.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   4 KKVLVGMSGGVDSTVSTLLLQEE-GYEVEGLYMKLhskpGYHEIHQARAQKAADYVGIKLHVLDLQKVFNEKVFQPFITS 82
Cdd:cd01999     1 KKVVLAYSGGLDTSVILKWLKEEyGYEVIAFTADL----GQGDEEEEIEEKALKLGAVKVYVVDLREEFAEDYIFPAIKA 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1277938138  83 ---YEkGNTPNPCALcNRNLkFGEM-MKYAETIGADYLATG 119
Cdd:cd01999    77 naiYE-GRYPLGTAL-ARPL-IAKKlVEVAREEGATAVAHG 114
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 5-120 1.66e-04

N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine synthase (EC 6.3.4.19), also called tRNA(Ile)-2-lysyl-cytidine synthase or tRNA(Ile)-lysidine synthetase, catalyzes the ligation of lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. This subfamily belongs to the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This domain has a strongly conserved motif SGGXD at the N-terminus.


Pssm-ID: 467496 [Multi-domain]  Cd Length: 185  Bit Score: 41.81  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   5 KVLVGMSGGVDSTVSTLLLQEEGYEVEGLYMKLHskpgyheI-HQAR------AQKAADYV---GIKLHVLDLQKVFNEK 74
Cdd:cd01992     1 KILVAVSGGPDSMALLHLLKELRPKLGLKLVAVH-------VdHGLReesaeeAQFVAKLCkklGIPLHILTVTEAPKSG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1277938138  75 vfqpfiTSYEKGntpnpcAlcnRNLKFGEMMKYAETIGADYLATGH 120
Cdd:cd01992    74 ------GNLEAA------A---REARYAFLERAAKEHGIDVLLTAH 104
GMP_synthase_C cd01997
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ...
 2-23 3.66e-04

C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP synthetase (glutamine-hydrolyzing, EC 6.3.5.2) contains two subdomains: the ATP pyrophosphatase domain at the N-terminal and the dimerization domain at the C-terminal end. The ATP-PPase domain is a twisted, five-stranded parallel beta-sheet sandwiched between helical layers. It has a signature nucleotide-binding motif, or PP-loop, at the end of the first-beta strand. GMP synthetase is a homodimer, but in some archaea, it is a heterodimer made up of ATP pyrophosphatase (ATP-PPase) and a GATase subunit. In eukaryotes and bacteria, the two catalytic units are encoded by a single gene producing a two-domain-type GMP with a GATase domain in the N-terminus and an ATP-PPase domain in the C-terminus.


Pssm-ID: 467501 [Multi-domain]  Cd Length: 311  Bit Score: 41.76  E-value: 3.66e-04
                          10        20
                  ....*....|....*....|..
gi 1277938138   2 KKKKVLVGMSGGVDSTVSTLLL 23
Cdd:cd01997     6 GDKKVLCLVSGGVDSTVCAALL 27
NAD_synthase cd00553
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ...
 4-216 1.14e-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: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   4 KKVLVGMSGGVDSTVSTLLLQE--EGYEVEGLYMklhskPGY--HEIHQARAQKAADYVGIKLHVLDLQKVFNEkvfqpF 79
Cdd:cd00553    24 KGFVLGLSGGIDSAVVAALAVRalGAENVLALIM-----PSRysSKETRDDAKALAENLGIEYRTIDIDPIVDA-----F 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138  80 ITSYEKGNTPNPCALCNRNLKFGEMMK----YAETIGADYLATGHYiktdgknfymAEDDTkdqSYFLFYVDKA--ILpk 153
Cdd:cd00553    94 LKALEHAGGSEAEDLALGNIQARLRMVllyaLANLLGGLVLGTGNK----------SELLL---GYFTKYGDGAadIN-- 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1277938138 154 llfPLGSRKKSDIKKFASSIKGLESFASQAESSEICFVETTYTDLLKDYVDVDNAGEVLDKDG 216
Cdd:cd00553   159 ---PIGDLYKTQVRELARYLGVPEEIIEKPPSAELWPGQTDEDELGMPYEELDLILYGLVDGK 218
guaA PRK00074
GMP synthase; Reviewed
 2-25 1.21e-03

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 40.42  E-value: 1.21e-03
                          10        20
                  ....*....|....*....|....
gi 1277938138   2 KKKKVLVGMSGGVDSTVSTLLLQE 25
Cdd:PRK00074  214 GDKKVILGLSGGVDSSVAAVLLHK 237
NAD_synthase pfam02540
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ...
 4-170 4.97e-03

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: 38.13  E-value: 4.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   4 KKVLVGMSGGVDSTVSTLLLQE--EGYEVEGLYMKlHSKPGYHEIHQARAqkAADYVGIKLHVLDLqkvfnekvfQPFIT 81
Cdd:pfam02540  19 KGVVLGLSGGIDSSLVAYLAVKalGKENVLALIMP-SSQSSEEDVQDALA--LAENLGIEYKTIDI---------KPIVR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138  82 SYEKGNTPNPCALCNRNLKFGEMMK--YAETIGADYLATGhyikTDGKNFYMAeddtkdqSYFLFYVDKAIlpkLLFPLG 159
Cdd:pfam02540  87 AFSQLFQDASEDFAKGNLKARIRMAilYYIANKFNYLVLG----TGNKSELAV-------GYFTKYGDGAC---DIAPIG 152

                         170
                  ....*....|.
gi 1277938138 160 SRKKSDIKKFA 170
Cdd:pfam02540 153 DLYKTQVYELA 163
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 6-36 5.41e-03

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: 35.12  E-value: 5.41e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1277938138   6 VLVGMSGGVDSTVSTLLLQEEG--YEVEGLYMK 36
Cdd:cd01986     1 VVVGYSGGKDSSVALHLASRLGrkAEVAVVHID 33
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 5-120 6.33e-03

tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble position of a tRNA must discriminate between G and A of mRNA are AUA (Ile) vs. AUG (Met) and UGA (stop) vs. UGG (Trp). In all bacteria, the wobble position of the tRNA(Ile) recognizing AUA is lysidine, a lysine derivative of cytidine. This family describes a protein domain found, apparently, in all bacteria in a single copy. Eukaryotic sequences appear to be organellar. The domain archictecture of this protein family is variable; some, including characterized proteins of E. coli and B. subtilis known to be tRNA(Ile)-lysidine synthetase, include a conserved 50-residue domain that many other members lack. This protein belongs to the ATP-binding PP-loop family ( pfam01171). It appears in the literature and protein databases as TilS, YacA, and putative cell cycle protein MesJ (a misnomer). [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274129 [Multi-domain]  Cd Length: 189  Bit Score: 37.23  E-value: 6.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938138   5 KVLVGMSGGVDSTVstLLLqeegyevegLYMKLHSKPGYHEI-----HQAR--AQKAADYV-------GIKLHVLDLQkv 70
Cdd:TIGR02432   1 RILVAVSGGVDSMA--LLH---------LLLKLQPKIKIKLIaahvdHGLRpeSDEEAEFVqqfcrklNIPLEIKKVD-- 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1277938138  71 fnekvfqpfITSYEKGNTPNPCALCnRNLKFGEMMKYAETIGADYLATGH 120
Cdd:TIGR02432  68 ---------VKALAKGKKKNLEEAA-REARYDFFEEIAKKHGADYILTAH 107
nadE PRK00876
NAD(+) synthase;
1-35 8.31e-03

NAD(+) synthase;


Pssm-ID: 179150 [Multi-domain]  Cd Length: 326  Bit Score: 37.63  E-value: 8.31e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1277938138   1 MKKKKVLVGMSGGVDSTVS-TLLLQEEGYE-VEGLYM 35
Cdd:PRK00876   31 LRRRGVVLGLSGGIDSSVTaALCVRALGKErVYGLLM 67
 
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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