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Conserved domains on  [gi|254811448|sp|B8G5F1|]
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RecName: Full=tRNA-specific 2-thiouridylase MnmA

Protein Classification

MnmA/TRMU family protein( domain architecture ID 11422314)

MnmA/TRMU family protein similar to tRNA-specific 2-thiouridylase MnmA that catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln)

CATH:  2.30.30.280
EC:  2.8.1.-
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 COG0482
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ...
 4-357 0e+00

tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ribosomal structure and biogenesis]; tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain is part of the Pathway/BioSystem: tRNA modification


:

Pssm-ID: 440250 [Multi-domain]  Cd Length: 353  Bit Score: 546.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448   4 VLVAMSGGVDSSLAAALLQEAGHQVTGVTMHLWDDDEQGlRESLCCAAEAATSARRVCALLGIPFYVFNYQREFRRHVIE 83
Cdd:COG0482    3 VVVGMSGGVDSSVAAALLKEQGYEVIGVTMKLWDDDDAS-GSGGCCSLEDIEDARRVADKLGIPHYVVDFEEEFKDRVID 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448  84 YFIRAYTHGLTPNPCVECNRMIKFRALLDRARALGFDAVATGHYARIVRDDcGRYQLWRAVDTEKDQSYMLHMLGQADLA 163
Cdd:COG0482   82 YFLDEYLAGRTPNPCVLCNREIKFGALLEKALELGADYIATGHYARVEEKD-GRYELLRGVDPNKDQSYFLYRLTQEQLS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448 164 RLLFPIGEYTKQQVREMAAARCLPSANREESQDICFVPDGDYRNLLRIEAPESliPGPIVDLEGREIGRHRGLPLYTVGQ 243
Cdd:COG0482  161 KTLFPLGELTKPEVREIAEELGLPVADKKDSQGICFIGDGDYRDFLERYLPEK--PGDIVDLDGKVLGEHDGLHYYTIGQ 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448 244 RRGLGLGGGEPRYVVAIDPARNALIVGPVEALNRERFIVTDARWVDDAPPAETFHCQVQVRAHAEPLPARVSAQPDGRWL 323
Cdd:COG0482  239 RKGLGIGGGEPLYVVGKDPETNTVIVGQGEALYSRELTAEDVNWISGEPPEEPLRCTAKIRYRQPPVPATLTPLEDGRVR 318

                        330       340       350
                 ....*....|....*....|....*....|....
gi 254811448 324 VELERPQRAVSPGQAAVFYDGVRVLGGGWIARPE 357
Cdd:COG0482  319 VEFDEPQRAVTPGQSAVFYDGDRVLGGGIIERTE 352
 
Name Accession Description Interval E-value
MnmA COG0482
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ...
 4-357 0e+00

tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ribosomal structure and biogenesis]; tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440250 [Multi-domain]  Cd Length: 353  Bit Score: 546.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448   4 VLVAMSGGVDSSLAAALLQEAGHQVTGVTMHLWDDDEQGlRESLCCAAEAATSARRVCALLGIPFYVFNYQREFRRHVIE 83
Cdd:COG0482    3 VVVGMSGGVDSSVAAALLKEQGYEVIGVTMKLWDDDDAS-GSGGCCSLEDIEDARRVADKLGIPHYVVDFEEEFKDRVID 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448  84 YFIRAYTHGLTPNPCVECNRMIKFRALLDRARALGFDAVATGHYARIVRDDcGRYQLWRAVDTEKDQSYMLHMLGQADLA 163
Cdd:COG0482   82 YFLDEYLAGRTPNPCVLCNREIKFGALLEKALELGADYIATGHYARVEEKD-GRYELLRGVDPNKDQSYFLYRLTQEQLS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448 164 RLLFPIGEYTKQQVREMAAARCLPSANREESQDICFVPDGDYRNLLRIEAPESliPGPIVDLEGREIGRHRGLPLYTVGQ 243
Cdd:COG0482  161 KTLFPLGELTKPEVREIAEELGLPVADKKDSQGICFIGDGDYRDFLERYLPEK--PGDIVDLDGKVLGEHDGLHYYTIGQ 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448 244 RRGLGLGGGEPRYVVAIDPARNALIVGPVEALNRERFIVTDARWVDDAPPAETFHCQVQVRAHAEPLPARVSAQPDGRWL 323
Cdd:COG0482  239 RKGLGIGGGEPLYVVGKDPETNTVIVGQGEALYSRELTAEDVNWISGEPPEEPLRCTAKIRYRQPPVPATLTPLEDGRVR 318

                        330       340       350
                 ....*....|....*....|....*....|....
gi 254811448 324 VELERPQRAVSPGQAAVFYDGVRVLGGGWIARPE 357
Cdd:COG0482  319 VEFDEPQRAVTPGQSAVFYDGDRVLGGGIIERTE 352
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
 4-354 0e+00

tRNA-specific 2-thiouridylase MnmA; Reviewed


Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 526.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448   4 VLVAMSGGVDSSLAAALLQEAGHQVTGVTMHLWDDDEqGLRESLCCAAEAATSARRVCALLGIPFYVFNYQREFRRHVIE 83
Cdd:PRK00143   3 VVVGMSGGVDSSVAAALLKEQGYEVIGVFMKLWDDDD-ETGKGGCCAEEDIADARRVADKLGIPHYVVDFEKEFWDRVID 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448  84 YFIRAYTHGLTPNPCVECNRMIKFRALLDRARALGFDAVATGHYARIVRDdcgrYQLWRAVDTEKDQSYMLHMLGQADLA 163
Cdd:PRK00143  82 YFLDEYKAGRTPNPCVLCNKEIKFKAFLEYARELGADYIATGHYARIRDG----RELLRGVDPNKDQSYFLYQLTQEQLA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448 164 RLLFPIGEYTKQQVREMAAARCLPSANREESQDICFVPDGDYRNLLRIEAPESliPGPIVDLEGREIGRHRGLPLYTVgq 243
Cdd:PRK00143 158 KLLFPLGELTKPEVREIAEEAGLPVAKKKDSQGICFIGERDYRDFLKRYLPAQ--PGEIVDLDGKVLGEHKGLMYYTIgq 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448 244 rr-glglGGGEPRYVVAIDPARNALIVGPVEALNRERFIVTDARWVDDAPPAETFHCQVQVRAHAEPLPARVSAQpDGRW 322
Cdd:PRK00143 236 rkglgigGDGEPWYVVGKDPETNTVVVGQGEALYSRELIASDLNWVGGEPPEEPFECTAKIRYRQKPVPATVELE-DDRV 314

                        330       340       350
                 ....*....|....*....|....*....|..
gi 254811448 323 LVELERPQRAVSPGQAAVFYDGVRVLGGGWIA 354
Cdd:PRK00143 315 EVEFDEPQRAVTPGQAAVFYDGDRVLGGGIIE 346
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
 3-353 1.23e-179

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: 501.65  E-value: 1.23e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448   3 NVLVAMSGGVDSSLAAALLQEAGHQVTGVTMHLWDDDEQGLREslCCAAEAATSARRVCALLGIPFYVFNYQREFRRHVI 82
Cdd:cd01998    1 KVAVAMSGGVDSSVAAALLKEQGYDVIGVFMKNWDDEDNEKGG--CCSEEDIEDARRVADQLGIPLYVVDFSEEYWERVF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448  83 EYFIRAYTHGLTPNPCVECNRMIKFRALLDRARALGFDAVATGHYARIVRDDCGRYQLWRAVDTEKDQSYMLHMLGQADL 162
Cdd:cd01998   79 DPFLEEYKAGRTPNPDVLCNREIKFGALLDAAKKLGADYIATGHYARIEEDNRGRYRLLRAVDPNKDQSYFLSRLSQEQL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448 163 ARLLFPIGEYTKQQVREMAAARCLPSANREESQDICFVPDGDYRNLLRIEAPEsLIPGPIVDLEGREIGRHRGLPLYTVG 242
Cdd:cd01998  159 SRTLFPLGHLTKSEVREIAREAGLPVAEKKDSQGICFIGKRDFRDFLKEYLPE-KLPGPIVDIDGKVLGEHKGLWFYTIG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448 243 QRRGLGLGGGEPRYVVAIDPARNALIVGPV-EALNRERFIVTDARWVDDAPPAETFHCQVQVRAHAEPLPARVSAQPDGR 321
Cdd:cd01998  238 QRKGLGIAAGEPLYVVKKDPEKNIVVVGPGhPALFSDTLRASDLNWISPEPPLEPLECEAKIRYRQPPVPCTVTPLDDGR 317

                        330       340       350
                 ....*....|....*....|....*....|..
gi 254811448 322 WLVELERPQRAVSPGQAAVFYDGVRVLGGGWI 353
Cdd:cd01998  318 LKVEFDEPQRAVTPGQAAVFYDGDEVLGGGII 349
trmU TIGR00420
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ...
 3-353 4.57e-109

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: 322.80  E-value: 4.57e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448    3 NVLVAMSGGVDSSLAAALLQEAGHQVTGVTMHLWDDDeQGLRESLCCAAEAATSARRVCALLGIPFYVFNYQREFRRHVI 82
Cdd:TIGR00420   2 KVIVGLSGGVDSSVSAYLLKQQGYEVVGVFMKNWEED-DKNDGHGCTSAEDLRDAQAICEKLGIPLEKVNFQKEYWNKVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448   83 EYFIRAYTHGLTPNPCVECNRMIKFRALLDRA-RALGFDAVATGHYARIvRDDCGRYQLWRAVDTEKDQSYMLHMLGQAD 161
Cdd:TIGR00420  81 EPFIQEYKEGRTPNPDILCNKFIKFGAFLEYAaELLGNDKIATGHYARI-AEIEGKSLLLRALDKNKDQSYFLYHLSHEQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448  162 LARLLFPIGEYTKQQVREMAAARCLPSANREESQDICFVPDGDYRNLLRIEAPESliPGPIVDLEG-REIGRHRGLPLYT 240
Cdd:TIGR00420 160 LAKLLFPLGELLKPEVRQIAKNAGLPTAEKKDSQGICFIGERKFRDFLKKYLPVK--PGVIITVDGqSVIGEHDGLWFYT 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448  241 V-GQRRGLGLGGGEPRYVVAIDPARNALIVG-PVEALNRERFIVTDARWVDDAPPAETFHCQVQVRAHAEPLPARVSAQP 318
Cdd:TIGR00420 238 IgQRKGLGIGGAAEPWFVVEKDLETNELVVShGKPDLASRGLLAQQFHWLDDEPNPFEMRCTVKIRYRQVPVQCKLKLLD 317

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 254811448  319 DGRWLVELERPQRAVSPGQAAVFYDGVRVLGGGWI 353
Cdd:TIGR00420 318 DNLIEVIFDEPQAGVTPGQSAVLYKGDICLGGGII 352
tRNA_Me_trans pfam03054
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ...
 3-202 8.92e-102

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: 298.40  E-value: 8.92e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448    3 NVLVAMSGGVDSSLAAALLQEAGHQVTGVTMHLWDDDEQGLRESLCCAAEAATSARRVCALLGIPFYVFNYQREFRRHVI 82
Cdd:pfam03054   2 KVVVAMSGGVDSSVAAYLLKEQGHNVIGVFMKNWDEEQSLDEEGKCCSEEDLADAQRVCEQLGIPLYVVNFEKEYWEDVF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448   83 EYFIRAYTHGLTPNPCVECNRMIKFRALLDRARA-LGFDAVATGHYARIVRDDCGRYQLWRAVDTEKDQSYMLHMLGQAD 161
Cdd:pfam03054  82 EPFLDEYKNGRTPNPDVLCNKEIKFGALLDYALEnLGADYVATGHYARVSLNKDGGSELLRALDKNKDQSYFLSTLSQEQ 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 254811448  162 LARLLFPIGEYTKQQVREMAAARCLPSANREESQDICFVPD 202
Cdd:pfam03054 162 LEKLLFPLGELTKEEVRKIAKEAGLATAKKKDSQGICFIGK 202
 
Name Accession Description Interval E-value
MnmA COG0482
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ...
 4-357 0e+00

tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ribosomal structure and biogenesis]; tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440250 [Multi-domain]  Cd Length: 353  Bit Score: 546.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448   4 VLVAMSGGVDSSLAAALLQEAGHQVTGVTMHLWDDDEQGlRESLCCAAEAATSARRVCALLGIPFYVFNYQREFRRHVIE 83
Cdd:COG0482    3 VVVGMSGGVDSSVAAALLKEQGYEVIGVTMKLWDDDDAS-GSGGCCSLEDIEDARRVADKLGIPHYVVDFEEEFKDRVID 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448  84 YFIRAYTHGLTPNPCVECNRMIKFRALLDRARALGFDAVATGHYARIVRDDcGRYQLWRAVDTEKDQSYMLHMLGQADLA 163
Cdd:COG0482   82 YFLDEYLAGRTPNPCVLCNREIKFGALLEKALELGADYIATGHYARVEEKD-GRYELLRGVDPNKDQSYFLYRLTQEQLS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448 164 RLLFPIGEYTKQQVREMAAARCLPSANREESQDICFVPDGDYRNLLRIEAPESliPGPIVDLEGREIGRHRGLPLYTVGQ 243
Cdd:COG0482  161 KTLFPLGELTKPEVREIAEELGLPVADKKDSQGICFIGDGDYRDFLERYLPEK--PGDIVDLDGKVLGEHDGLHYYTIGQ 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448 244 RRGLGLGGGEPRYVVAIDPARNALIVGPVEALNRERFIVTDARWVDDAPPAETFHCQVQVRAHAEPLPARVSAQPDGRWL 323
Cdd:COG0482  239 RKGLGIGGGEPLYVVGKDPETNTVIVGQGEALYSRELTAEDVNWISGEPPEEPLRCTAKIRYRQPPVPATLTPLEDGRVR 318

                        330       340       350
                 ....*....|....*....|....*....|....
gi 254811448 324 VELERPQRAVSPGQAAVFYDGVRVLGGGWIARPE 357
Cdd:COG0482  319 VEFDEPQRAVTPGQSAVFYDGDRVLGGGIIERTE 352
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
 4-354 0e+00

tRNA-specific 2-thiouridylase MnmA; Reviewed


Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 526.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448   4 VLVAMSGGVDSSLAAALLQEAGHQVTGVTMHLWDDDEqGLRESLCCAAEAATSARRVCALLGIPFYVFNYQREFRRHVIE 83
Cdd:PRK00143   3 VVVGMSGGVDSSVAAALLKEQGYEVIGVFMKLWDDDD-ETGKGGCCAEEDIADARRVADKLGIPHYVVDFEKEFWDRVID 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448  84 YFIRAYTHGLTPNPCVECNRMIKFRALLDRARALGFDAVATGHYARIVRDdcgrYQLWRAVDTEKDQSYMLHMLGQADLA 163
Cdd:PRK00143  82 YFLDEYKAGRTPNPCVLCNKEIKFKAFLEYARELGADYIATGHYARIRDG----RELLRGVDPNKDQSYFLYQLTQEQLA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448 164 RLLFPIGEYTKQQVREMAAARCLPSANREESQDICFVPDGDYRNLLRIEAPESliPGPIVDLEGREIGRHRGLPLYTVgq 243
Cdd:PRK00143 158 KLLFPLGELTKPEVREIAEEAGLPVAKKKDSQGICFIGERDYRDFLKRYLPAQ--PGEIVDLDGKVLGEHKGLMYYTIgq 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448 244 rr-glglGGGEPRYVVAIDPARNALIVGPVEALNRERFIVTDARWVDDAPPAETFHCQVQVRAHAEPLPARVSAQpDGRW 322
Cdd:PRK00143 236 rkglgigGDGEPWYVVGKDPETNTVVVGQGEALYSRELIASDLNWVGGEPPEEPFECTAKIRYRQKPVPATVELE-DDRV 314

                        330       340       350
                 ....*....|....*....|....*....|..
gi 254811448 323 LVELERPQRAVSPGQAAVFYDGVRVLGGGWIA 354
Cdd:PRK00143 315 EVEFDEPQRAVTPGQAAVFYDGDRVLGGGIIE 346
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
 3-353 1.23e-179

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: 501.65  E-value: 1.23e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448   3 NVLVAMSGGVDSSLAAALLQEAGHQVTGVTMHLWDDDEQGLREslCCAAEAATSARRVCALLGIPFYVFNYQREFRRHVI 82
Cdd:cd01998    1 KVAVAMSGGVDSSVAAALLKEQGYDVIGVFMKNWDDEDNEKGG--CCSEEDIEDARRVADQLGIPLYVVDFSEEYWERVF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448  83 EYFIRAYTHGLTPNPCVECNRMIKFRALLDRARALGFDAVATGHYARIVRDDCGRYQLWRAVDTEKDQSYMLHMLGQADL 162
Cdd:cd01998   79 DPFLEEYKAGRTPNPDVLCNREIKFGALLDAAKKLGADYIATGHYARIEEDNRGRYRLLRAVDPNKDQSYFLSRLSQEQL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448 163 ARLLFPIGEYTKQQVREMAAARCLPSANREESQDICFVPDGDYRNLLRIEAPEsLIPGPIVDLEGREIGRHRGLPLYTVG 242
Cdd:cd01998  159 SRTLFPLGHLTKSEVREIAREAGLPVAEKKDSQGICFIGKRDFRDFLKEYLPE-KLPGPIVDIDGKVLGEHKGLWFYTIG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448 243 QRRGLGLGGGEPRYVVAIDPARNALIVGPV-EALNRERFIVTDARWVDDAPPAETFHCQVQVRAHAEPLPARVSAQPDGR 321
Cdd:cd01998  238 QRKGLGIAAGEPLYVVKKDPEKNIVVVGPGhPALFSDTLRASDLNWISPEPPLEPLECEAKIRYRQPPVPCTVTPLDDGR 317

                        330       340       350
                 ....*....|....*....|....*....|..
gi 254811448 322 WLVELERPQRAVSPGQAAVFYDGVRVLGGGWI 353
Cdd:cd01998  318 LKVEFDEPQRAVTPGQAAVFYDGDEVLGGGII 349
trmU TIGR00420
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ...
 3-353 4.57e-109

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: 322.80  E-value: 4.57e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448    3 NVLVAMSGGVDSSLAAALLQEAGHQVTGVTMHLWDDDeQGLRESLCCAAEAATSARRVCALLGIPFYVFNYQREFRRHVI 82
Cdd:TIGR00420   2 KVIVGLSGGVDSSVSAYLLKQQGYEVVGVFMKNWEED-DKNDGHGCTSAEDLRDAQAICEKLGIPLEKVNFQKEYWNKVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448   83 EYFIRAYTHGLTPNPCVECNRMIKFRALLDRA-RALGFDAVATGHYARIvRDDCGRYQLWRAVDTEKDQSYMLHMLGQAD 161
Cdd:TIGR00420  81 EPFIQEYKEGRTPNPDILCNKFIKFGAFLEYAaELLGNDKIATGHYARI-AEIEGKSLLLRALDKNKDQSYFLYHLSHEQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448  162 LARLLFPIGEYTKQQVREMAAARCLPSANREESQDICFVPDGDYRNLLRIEAPESliPGPIVDLEG-REIGRHRGLPLYT 240
Cdd:TIGR00420 160 LAKLLFPLGELLKPEVRQIAKNAGLPTAEKKDSQGICFIGERKFRDFLKKYLPVK--PGVIITVDGqSVIGEHDGLWFYT 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448  241 V-GQRRGLGLGGGEPRYVVAIDPARNALIVG-PVEALNRERFIVTDARWVDDAPPAETFHCQVQVRAHAEPLPARVSAQP 318
Cdd:TIGR00420 238 IgQRKGLGIGGAAEPWFVVEKDLETNELVVShGKPDLASRGLLAQQFHWLDDEPNPFEMRCTVKIRYRQVPVQCKLKLLD 317

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 254811448  319 DGRWLVELERPQRAVSPGQAAVFYDGVRVLGGGWI 353
Cdd:TIGR00420 318 DNLIEVIFDEPQAGVTPGQSAVLYKGDICLGGGII 352
tRNA_Me_trans pfam03054
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ...
 3-202 8.92e-102

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: 298.40  E-value: 8.92e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448    3 NVLVAMSGGVDSSLAAALLQEAGHQVTGVTMHLWDDDEQGLRESLCCAAEAATSARRVCALLGIPFYVFNYQREFRRHVI 82
Cdd:pfam03054   2 KVVVAMSGGVDSSVAAYLLKEQGHNVIGVFMKNWDEEQSLDEEGKCCSEEDLADAQRVCEQLGIPLYVVNFEKEYWEDVF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448   83 EYFIRAYTHGLTPNPCVECNRMIKFRALLDRARA-LGFDAVATGHYARIVRDDCGRYQLWRAVDTEKDQSYMLHMLGQAD 161
Cdd:pfam03054  82 EPFLDEYKNGRTPNPDVLCNKEIKFGALLDYALEnLGADYVATGHYARVSLNKDGGSELLRALDKNKDQSYFLSTLSQEQ 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 254811448  162 LARLLFPIGEYTKQQVREMAAARCLPSANREESQDICFVPD 202
Cdd:pfam03054 162 LEKLLFPLGELTKEEVRKIAKEAGLATAKKKDSQGICFIGK 202
PRK14664 PRK14664
tRNA-specific 2-thiouridylase MnmA; Provisional
 4-354 1.48e-92

tRNA-specific 2-thiouridylase MnmA; Provisional


Pssm-ID: 173127 [Multi-domain]  Cd Length: 362  Bit Score: 281.07  E-value: 1.48e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448   4 VLVAMSGGVDSSLAAALLQEAGHQVTGVTMHLWDDDEQglreslccaaeaatSARRVCALLGIPFYVFNYQREFRRHVIE 83
Cdd:PRK14664   8 VLVGMSGGIDSTATCLMLQEQGYEIVGVTMRVWGDEPQ--------------DARELAARMGIEHYVADERVPFKDTIVK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448  84 YFIRAYTHGLTPNPCVECNRMIKFRALLDRARALGFDAVATGHYARIvRDDCGRYQLWRAVDTEKDQSYMLHMLGQADLA 163
Cdd:PRK14664  74 NFIDEYRQGRTPNPCVMCNPLFKFRMLIEWADKLGCAWIATGHYSRL-EERNGHIYIVAGDDDKKDQSYFLWRLGQDILR 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448 164 RLLFPIGEYTKQQVREMAAARCLPSANRE-ESQDICFVpDGDYRNLLRIEAPE---SLIPGPIVDLEGREIGRHRGLPLY 239
Cdd:PRK14664 153 RCIFPLGNYTKQTVREYLREKGYEAKSKEgESMEVCFI-KGDYRDFLREQCPEldtEVGPGWFVNSEGVKLGQHKGFPYY 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448 240 TVGQRRGLGLGGGEPRYVVAIDPARNALIVGPVEALNRERFIVTDARWVDDappAETFHCQ---VQVRAHAEPLPARVSA 316
Cdd:PRK14664 232 TIGQRKGLEIALGKPAYVLKINPQKNTVMLGDAEQLKAEYMLAEQDNIVDE---QELFACPdlaVRIRYRSRPIPCRVKR 308

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 254811448 317 QPDGRWLVELERPQRAVSPGQAAVFYDGVRVLGGGWIA 354
Cdd:PRK14664 309 LEDGRLLVRFLAEASAIAPGQSAVFYEGRRVLGGAFIA 346
mnmA PRK14665
tRNA-specific 2-thiouridylase MnmA; Provisional
 4-353 1.79e-69

tRNA-specific 2-thiouridylase MnmA; Provisional


Pssm-ID: 173128 [Multi-domain]  Cd Length: 360  Bit Score: 221.73  E-value: 1.79e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448   4 VLVAMSGGVDSSLAAALLQEAGHQVTGVTMHLWDDDEqglreslccAAEAATSARRVCALLGIPFYVFNYQREFRRHVIE 83
Cdd:PRK14665   8 VLLGMSGGTDSSVAAMLLLEAGYEVTGVTFRFYEFNG---------STEYLEDARALAERLGIGHITYDARKVFRKQIID 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448  84 YFIRAYTHGLTPNPCVECNRMIKFRALLDRARALGFDAVATGHYARIVRDDcGRYQLWRAVDTEKDQSYMLHMLGQADLA 163
Cdd:PRK14665  79 YFIDEYMSGHTPVPCTLCNNYLKWPLLAKIADEMGIFYLATGHYVRKQWID-GNYYITPAEDVDKDQSFFLWGLRQEILQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448 164 RLLFPIGEYTKQQVREMAAAR-CLPSANREESQDICFVPdGDYRNLLRIEAPE-----------SLIPGPIVDLEGREIG 231
Cdd:PRK14665 158 RMLLPMGGMTKSEARAYAAERgFEKVAKKRDSLGVCFCP-MDYRSFLKKCLCDesgdknrniyrKVERGRFLDESGNFIA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448 232 RHRGLPLYTVGQRRGLGLGGGEPRYVVAIDPARNALIVGPVEALNRERFIVTDARWVDdapPAETFHCQ---VQVRAHAE 308
Cdd:PRK14665 237 WHEGYPFYTIGQRRGLGIQLNRAVFVKEIHPETNEVVLASLKALEKTEMWLKDWNIVN---ESRLLGCDdiiVKIRYRKQ 313

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 254811448 309 PLPARVSAQPDGRWLVELERPQRAVSPGQAAVFY-DGVrVLGGGWI 353
Cdd:PRK14665 314 ENHCTVTITPDNLLHVQLHEPLTAIAEGQAAAFYkDGL-LLGGGII 358
tRNA_Me_trans_C pfam20258
Aminomethyltransferase beta-barrel domain; This domain is found at the C-terminus of tRNA ...
 280-353 2.02e-25

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: 97.73  E-value: 2.02e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254811448  280 FIVTDARWVDDAPPAETFHCQVQVRAHAEPLPARVSAQPDGRWLVELERPQRAVSPGQAAVFYDGVRVLGGGWI 353
Cdd:pfam20258   4 LRAKDPNWLGDKPPTEPLECTVKVRHRQPPVPCVVELIDDETVEVHFDEPVRAVTPGQAAVFYDGDRCLGGGII 77
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 4-126 1.78e-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: 71.79  E-value: 1.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448   4 VLVAMSGGVDSS----LAAALLQEAGHQVTGVTMHlwdddeQGLRESlccAAEAATSARRVCALLGIPFYVFNYQrefrr 79
Cdd:COG0037   18 ILVAVSGGKDSLallhLLAKLRRRLGFELVAVHVD------HGLREE---SDEDAEFVAELCEELGIPLHVVRVD----- 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 254811448  80 hvieyfIRAYTHGLTPNPCVECnRMIKFRALLDRARALGFDAVATGH 126
Cdd:COG0037   84 ------VPAIAKKEGKSPEAAA-RRARYGALYELARELGADKIATGH 123
COG1606 COG1606
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
1-125 2.66e-09

ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];


Pssm-ID: 441214 [Multi-domain]  Cd Length: 265  Bit Score: 57.43  E-value: 2.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448   1 MANVLVAMSGGVDSSLAAALLQEA-GHQVTGVTMHLwdddeqglrESLccAAEAATSARRVCALLGIpfyvfnyqrefrR 79
Cdd:COG1606   15 LGSVLVAFSGGVDSTLLAKVAHDVlGDRVLAVTADS---------PSL--PERELEEAKELAKEIGI------------R 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 254811448  80 HVIEYF----IRAYTHGlTPNPCVECNRMIkFRALLDRARALGFDAVATG 125
Cdd:COG1606   72 HEVIETdeleDPEFVAN-PPDRCYHCKKEL-FSKLKELAKELGYAVVADG 119
LarE-like cd01990
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ...
 4-194 3.25e-09

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: 56.50  E-value: 3.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448   4 VLVAMSGGVDSSLAAALLQEA-GHQVTGVTmhlwdddeqGLRESLccAAEAATSARRVCALLGIPFYVFNYQREFRRHVI 82
Cdd:cd01990    2 VVVAFSGGVDSSLLAKLAKEVlGDNVVAVT---------ADSPLV--PREELEEAKRIAEEIGIRHEIIKTDELDDEEYV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448  83 EYfiraythglTPNPCVECNRMIkFRALLDRARALGFDAVATGHYArivrDDCGRYQ-LWRAvdtekdqsymLHMLGqad 161
Cdd:cd01990   71 AN---------DPDRCYHCKKAL-YSTLKEIAKERGYDVVLDGTNA----DDLKDYRpGLLA----------AAELG--- 123

                        170       180       190
                 ....*....|....*....|....*....|...
gi 254811448 162 lARLLFPIGEYTKQQVREMAAARCLPSANREES 194
Cdd:cd01990  124 -IRSPLPELGLTKSEIRELARELGLPNWDKPAS 155
TtuA-like cd01993
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ...
 4-126 5.49e-09

tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) 2-sulfurtransferase, also called tRNA thiouridine synthetase TtuA, catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T). TtuA belongs to the adenine nucleotide alpha hydrolase superfamily (AANH) that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467497 [Multi-domain]  Cd Length: 190  Bit Score: 55.41  E-value: 5.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448   4 VLVAMSGGVDSSLAAALLQEAGHQVTGVTMHLwdddeqGLRESLCCAAEAatsARRVCALLGIPFYVFNYQREfrrhviE 83
Cdd:cd01993   11 ILVAVSGGKDSLALLAVLKKLGYNVEALYINL------GIGEYSEKSEEV---VKKLAEKLNLPLHVVDLKEE------Y 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 254811448  84 YF-IRAYTHGLTPNPCVECNrMIKfRALLDR-ARALGFDAVATGH 126
Cdd:cd01993   76 GLgIPELAKKSRRPPCSVCG-LVK-RYIMNKfAVENGFDVVATGH 118
tRNA_Me_trans_M pfam20259
tRNA methyl transferase PRC-barrel domain; This family represents a central PRC-barrel domain ...
 219-271 1.40e-08

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: 50.68  E-value: 1.40e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 254811448  219 PGPIVDLE-GREIGRHRGLPLYTVGQRRGLG-LGGGEPRYVVAIDPARNALIVGP 271
Cdd:pfam20259  12 PGDIIDIDtGEVLGEHEGIWFYTIGQRKGLGiGGYGEPWYVVEKDPKKNTVYVGR 66
NAD_synthase pfam02540
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ...
 4-187 1.29e-07

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: 52.00  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448    4 VLVAMSGGVDSSLAAALLQEA--GHQVTGVTMHLWDDDEQGLREslccaaeaatsARRVCALLGIPFYVFNyqrefrrhv 81
Cdd:pfam02540  21 VVLGLSGGIDSSLVAYLAVKAlgKENVLALIMPSSQSSEEDVQD-----------ALALAENLGIEYKTID--------- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448   82 IEYFIRAYTHGLTPNPC--VECN-----RMIkfrALLDRARALGFDAVATGHYARIVRDDCGRYqlwravdtekdqsyml 154
Cdd:pfam02540  81 IKPIVRAFSQLFQDASEdfAKGNlkariRMA---ILYYIANKFNYLVLGTGNKSELAVGYFTKY---------------- 141

                         170       180       190
                  ....*....|....*....|....*....|...
gi 254811448  155 hmlgqADLARLLFPIGEYTKQQVREMAAARCLP 187
Cdd:pfam02540 142 -----GDGACDIAPIGDLYKTQVYELARYLNVP 169
CTU1-like cd01713
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ...
 4-187 5.54e-06

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: 46.81  E-value: 5.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448   4 VLVAMSGGVDSSLAAALLQE-AGHQVTGVTMHLWDDDE--QGLREslccaaEAATSARRVCALLGIPFYVFNYQREFRRH 80
Cdd:cd01713   21 VAVGLSGGKDSTVLLYVLKElNKRHDYGVELIAVTIDEgiKGYRD------DSLEAARKLAEEYGIPLEIVSFEDEFGFT 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448  81 VIEYFIRAythGLTPNPCVECN--RmikfRALLDR-ARALGFDAVATGHYArivrDDcgryqlwravdteKDQSYMLHML 157
Cdd:cd01713   95 LDELIVGK---GGKKNACTYCGvfR----RRALNRgARELGADKLATGHNL----DD-------------EAETILMNLL 150

                        170       180       190
                 ....*....|....*....|....*....|
gi 254811448 158 gQADLARLLfPIGEYTKqQVREMAAARCLP 187
Cdd:cd01713  151 -RGDVARLL-RTGPEPR-SEGEGLVPRIKP 177
guaA PRK00074
GMP synthase; Reviewed
 4-31 6.71e-06

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 47.73  E-value: 6.71e-06
                         10        20
                 ....*....|....*....|....*....
gi 254811448   4 VLVAMSGGVDSSLAAALLQEA-GHQVTGV 31
Cdd:PRK00074 218 VILGLSGGVDSSVAAVLLHKAiGDQLTCV 246
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 4-126 6.94e-06

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: 46.05  E-value: 6.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448   4 VLVAMSGGVDSS----LAAALLQEAGHQVTGVTMHlwdddeQGLRESlccAAEAATSARRVCALLGIPFYVFNYQREFRR 79
Cdd:cd01992    2 ILVAVSGGPDSMallhLLKELRPKLGLKLVAVHVD------HGLREE---SAEEAQFVAKLCKKLGIPLHILTVTEAPKS 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 254811448  80 HV-IEyfiRAYthgltpnpcvecnRMIKFRALLDRARALGFDAVATGH 126
Cdd:cd01992   73 GGnLE---AAA-------------REARYAFLERAAKEHGIDVLLTAH 104
TtcA-like cd24138
tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) ...
 4-134 1.36e-05

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: 45.34  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448   4 VLVAMSGGVDSSLAAALLQE-AGH-----QVTGVTMHLWDDDEQGLRESLCcaaeaatsarRVCALLGIPFYVFNYqref 77
Cdd:cd24138   11 ILVGLSGGKDSLTLLHLLEElKRRapikfELVAVTVDPGYPGYRPPREELA----------EILEELGEILEDEES---- 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 254811448  78 rRHVIEYFIRAYThgltpNPCVECNRMiKFRALLDRARALGFDAVATGHYarivRDD 134
Cdd:cd24138   77 -EIIIIEKEREEK-----SPCSLCSRL-RRGILYSLAKELGCNKLALGHH----LDD 122
COG1365 COG1365
Predicted ATPase, PP-loop superfamily [General function prediction only];
4-140 1.66e-05

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


Pssm-ID: 440976  Cd Length: 256  Bit Score: 45.81  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448   4 VLVAMSGGVDSSLAAALLQEAGHQVTGVTMHLWDDDEQGLRESLccaaeaatsaRRVCALLGI--PFYVFNYQrefrrHV 81
Cdd:COG1365   63 VVVAFSGGVDSSASLIIAKWIGFDVEAVTVKSTIILPQMFKKNI----------KELCKKLNVkhEFIEIDLG-----EI 127

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254811448  82 IEYFIRAYTHgltpnPCVECNRMIKfRALLDRARALGFDAVA------TGHYARIVRDDCGRYQL 140
Cdd:COG1365  128 IEDALKGKFH-----PCGRCHSLIE-EAVEDYAKKNGIKIVIfgdllsVGYLSIYKKDGIVRLNL 186
NAD_synthase cd00553
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ...
 4-182 7.20e-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: 43.70  E-value: 7.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448   4 VLVAMSGGVDSSLAAALLQEA--GHQVTGVTMHlwdddeqgLRESlccAAEAATSARRVCALLGIPFYVFNyQREFRRHV 81
Cdd:cd00553   26 FVLGLSGGIDSAVVAALAVRAlgAENVLALIMP--------SRYS---SKETRDDAKALAENLGIEYRTID-IDPIVDAF 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448  82 IEYFIRAYTHGLTPNpcVECN-----RMIkfrALLDRARALGFDAVATGHyarivRDDCGRYQLWRAVDtekdqsymlhm 156
Cdd:cd00553   94 LKALEHAGGSEAEDL--ALGNiqarlRMV---LLYALANLLGGLVLGTGN-----KSELLLGYFTKYGD----------- 152

                        170       180
                 ....*....|....*....|....*.
gi 254811448 157 lGQADLArllfPIGEYTKQQVREMAA 182
Cdd:cd00553  153 -GAADIN----PIGDLYKTQVRELAR 173
GMP_synthase_C cd01997
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ...
 4-31 1.73e-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: 42.91  E-value: 1.73e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 254811448   4 VLVAMSGGVDSSLAAALLQEA-GH-QVTGV 31
Cdd:cd01997   10 VLCLVSGGVDSTVCAALLHKAlGDeRVIAV 39
NadE COG0171
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ...
 4-72 2.32e-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: 42.91  E-value: 2.32e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254811448   4 VLVAMSGGVDSSLAAALLQEAG--HQVTGVTMhlwdddeqGLRESlccAAEAATSARRVCALLGIPFYVFN 72
Cdd:COG0171  289 VVLGLSGGIDSALVAALAVDALgpENVLGVTM--------PSRYT---SDESLEDAEELAENLGIEYEEID 348
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 4-134 4.82e-04

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: 40.69  E-value: 4.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448    4 VLVAMSGGVDS-SLAAALLQEA---GHQVTGVTMHlwdddeQGLRESlccAAEAATSARRVCALLGIPFYVFNYQrefrr 79
Cdd:TIGR02432   2 ILVAVSGGVDSmALLHLLLKLQpkiKIKLIAAHVD------HGLRPE---SDEEAEFVQQFCRKLNIPLEIKKVD----- 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 254811448   80 hvieyfIRAYTHGLTPNPCVECnRMIKFRALLDRARALGFDAVATGHYArivrDD 134
Cdd:TIGR02432  68 ------VKALAKGKKKNLEEAA-REARYDFFEEIAKKHGADYILTAHHA----DD 111
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 4-41 7.81e-04

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: 37.82  E-value: 7.81e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 254811448   4 VLVAMSGGVDSSLAAALLQEAGH--QVTGVTMHLWDDDEQ 41
Cdd:cd01986    1 VVVGYSGGKDSSVALHLASRLGRkaEVAVVHIDHGIGFKE 40
PPase_ThiI cd01712
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole ...
 4-125 1.03e-03

pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole synthesis in the thiamine biosynthesis pathway. ThiI is also responsible for the 4-thiouridine (S4U) modification at position 8 in some prokaryotic tRNAs. ThiI contains a PP-loop pyrophosphatase domain which binds ATP and activates tRNA by adenylation. The PP-loop pyrophosphatase catalytic domain of ThiI proteins is always accompanied by a THUMP domain towards the N terminus. THUMP domains are predicted to bind RNA and are widespread in bacteria, archaea, and eukaryotes. The acronym was derived from the names of RNA-modifying enzymes in which this domain is found, namely, thiouridine synthases (ThiI), methylases, and archaeal pseudouridine synthases. ThiI proteins from gamma-proteobacteria and from archaea of the genus Thermoplasma also contain a C-terminal extension of approximately 100 amino acid residues which accepts sulfur in the form of a persulfide on a cysteine residue. This persulfide is responsible for a nucleophilic attack of the adenylated tRNA substrate, completing the sulfur insertion forming a disulfide-bridge between the rhodanese-like domain and a second cysteine residue located in the PP-loop domain. The reaction releases AMP and modified tRNA, and leaves the enzyme in an oxidized state. The disulfide is then reductively cleaved to complete the enzymatic cycle. The pyrophosphatase domain of ThiI belongs to the adenine nucleotide hydrolase (AANH) superfamily and it binds to adenosine nucleotide.


Pssm-ID: 467485 [Multi-domain]  Cd Length: 185  Bit Score: 39.46  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448   4 VLVAMSGGVDSSLAAALLQEAGHQVTGVTMHLWDDDEQGLREslccaaeaatsarRVCALL--------GIPFYVFNYQR 75
Cdd:cd01712    7 VLVLLSGGIDSPVAAWMMMKRGVEVDFLHFHSGPYTSEKAVE-------------KVKDLArvlseyqgGVKLYLVPFTD 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 254811448  76 EFRRHVIEYFIRAYThgltpnpCVECNRMIkFRALLDRARALGFDAVATG 125
Cdd:cd01712   74 KIQKEILEKVPESYR-------IVLMRRMM-YRIAEKIAERLGADALVTG 115
ThiI pfam02568
Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for ...
 4-125 1.75e-03

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


Pssm-ID: 280691 [Multi-domain]  Cd Length: 197  Bit Score: 38.95  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448    4 VLVAMSGGVDSSLAAALLQEAGHQVTGVTMHlwdddeqglrESLCCAAEAATSARRVCALLG-------IPFYVFNY--- 73
Cdd:pfam02568   6 VLALISGGIDSPVAAYMMMRRGCRVVALHFI----------NNPGTSAEAIGKVQKLAELLArygtsheVRLVVFDFtdv 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 254811448   74 QREFRRHVIEyfiraythgltPNPCVECNRMIkFRALLDRARALGFDAVATG 125
Cdd:pfam02568  76 QKEILEKAPE-----------GYRCVLLKRCM-YRIAEKVAEEEGADALVTG 115
PRK13980 PRK13980
NAD synthetase; Provisional
 3-182 2.35e-03

NAD synthetase; Provisional


Pssm-ID: 184435 [Multi-domain]  Cd Length: 265  Bit Score: 39.04  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448   3 NVLVAMSGGVDSSLAAALLQEA-GHQ-VTGVTMHlwddDEQGLRESLccaaeaaTSARRVCALLGIPFYVFNYQRefrrh 80
Cdd:PRK13980  32 GVVLGLSGGIDSAVVAYLAVKAlGKEnVLALLMP----SSVSPPEDL-------EDAELVAEDLGIEYKVIEITP----- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448  81 VIEYFIRAYThgltpnpcvECNRMIK--FRAlldRARALGFDAVATgHYARIVRDDCGRYQLwravdtekdqsymlhMLG 158
Cdd:PRK13980  96 IVDAFFSAIP---------DADRLRVgnIMA---RTRMVLLYDYAN-RENRLVLGTGNKSEL---------------LLG 147

                        170       180
                 ....*....|....*....|....*...
gi 254811448 159 Q----ADLARLLFPIGEYTKQQVREMAA 182
Cdd:PRK13980 148 YftkyGDGAVDLNPIGDLYKTQVRELAR 175
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
 6-83 5.60e-03

PP-loop family; This family of proteins belongs to the PP-loop superfamily.


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 37.22  E-value: 5.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254811448    6 VAMSGGVDSS----LAAALLQEAGHQVTGVTMHlwdddeQGLRESlccAAEAATSARRVCALLGIPFYVFNYQ------- 74
Cdd:pfam01171   1 VAVSGGPDSMallyLLAKLKIKLGIELTAAHVN------HGLREE---SDREAEHVQALCRQLGIPLEILRVDvakksge 71

                          90
                  ....*....|....*
gi 254811448   75 ------REFRRHVIE 83
Cdd:pfam01171  72 nleaaaREARYDFFE 86
QueC COG0603
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ...
 1-66 9.85e-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: 37.06  E-value: 9.85e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254811448   1 MANVLVAMSGGVDSSLAAALLQEAGHQVTGVTMHLwdddeqGLRESlccaAEAAtSARRVCALLGI 66
Cdd:COG0603    2 MKKAVVLLSGGLDSTTCLAWALARGYEVYALSFDY------GQRHR----KELE-AARRIAKALGV 56
 
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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