NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|505453482|ref|WP_015640584|]
View 

MULTISPECIES: tRNA 2-thiouridine(34) synthase MnmA [Lactiplantibacillus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
 14-369 0e+00

tRNA-specific 2-thiouridylase MnmA; Reviewed


:

Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 622.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  14 TRVVVGMSGGVDSSVVALLLKQQGYDVVGVFMKNWDDTDE--NGVCTATEDYKDVAKVADKIGIPYYSINFEKEYWDRVF 91
Cdd:PRK00143   1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVFMKLWDDDDEtgKGGCCAEEDIADARRVADKLGIPHYVVDFEKEFWDRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  92 TYFLDEYKKGRTPNPDVICNKEIKFKAFLDYAMDLGADYIATGHYARLQHDEdgtmHLLRGVDSNKDQTYFLSQLDSKTL 171
Cdd:PRK00143  81 DYFLDEYKAGRTPNPCVLCNKEIKFKAFLEYARELGADYIATGHYARIRDGR----ELLRGVDPNKDQSYFLYQLTQEQL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482 172 QKVMFPLGEMVKPDVRKLALNAGLATAKKKDSVGICFIGEKNFKEFLGHYLPATPGKMMTFDGQVKGEHAGLMYYTIGQR 251
Cdd:PRK00143 157 AKLLFPLGELTKPEVREIAEEAGLPVAKKKDSQGICFIGERDYRDFLKRYLPAQPGEIVDLDGKVLGEHKGLMYYTIGQR 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482 252 RGLGIGGDGednEPWFVVGKDLKKNILYVGKGyhnPHLYATHLKASDLHFVTDEDLGNDFHVTAKFRYRQKDSGVTVHFN 331
Cdd:PRK00143 237 KGLGIGGDG---EPWYVVGKDPETNTVVVGQG---EALYSRELIASDLNWVGGEPPEEPFECTAKIRYRQKPVPATVELE 310

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 505453482 332 DDhtEVTVTFDDPVRAITPGQAVVFYNGEECLGSGMID 369
Cdd:PRK00143 311 DD--RVEVEFDEPQRAVTPGQAAVFYDGDRVLGGGIIE 346
 
Name Accession Description Interval E-value
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
 14-369 0e+00

tRNA-specific 2-thiouridylase MnmA; Reviewed


Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 622.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  14 TRVVVGMSGGVDSSVVALLLKQQGYDVVGVFMKNWDDTDE--NGVCTATEDYKDVAKVADKIGIPYYSINFEKEYWDRVF 91
Cdd:PRK00143   1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVFMKLWDDDDEtgKGGCCAEEDIADARRVADKLGIPHYVVDFEKEFWDRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  92 TYFLDEYKKGRTPNPDVICNKEIKFKAFLDYAMDLGADYIATGHYARLQHDEdgtmHLLRGVDSNKDQTYFLSQLDSKTL 171
Cdd:PRK00143  81 DYFLDEYKAGRTPNPCVLCNKEIKFKAFLEYARELGADYIATGHYARIRDGR----ELLRGVDPNKDQSYFLYQLTQEQL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482 172 QKVMFPLGEMVKPDVRKLALNAGLATAKKKDSVGICFIGEKNFKEFLGHYLPATPGKMMTFDGQVKGEHAGLMYYTIGQR 251
Cdd:PRK00143 157 AKLLFPLGELTKPEVREIAEEAGLPVAKKKDSQGICFIGERDYRDFLKRYLPAQPGEIVDLDGKVLGEHKGLMYYTIGQR 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482 252 RGLGIGGDGednEPWFVVGKDLKKNILYVGKGyhnPHLYATHLKASDLHFVTDEDLGNDFHVTAKFRYRQKDSGVTVHFN 331
Cdd:PRK00143 237 KGLGIGGDG---EPWYVVGKDPETNTVVVGQG---EALYSRELIASDLNWVGGEPPEEPFECTAKIRYRQKPVPATVELE 310

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 505453482 332 DDhtEVTVTFDDPVRAITPGQAVVFYNGEECLGSGMID 369
Cdd:PRK00143 311 DD--RVEVEFDEPQRAVTPGQAAVFYDGDRVLGGGIIE 346
MnmA COG0482
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ...
 14-373 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: 622.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  14 TRVVVGMSGGVDSSVVALLLKQQGYDVVGVFMKNWDDTD--ENGVCTATEDYKDVAKVADKIGIPYYSINFEKEYWDRVF 91
Cdd:COG0482    1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVTMKLWDDDDasGSGGCCSLEDIEDARRVADKLGIPHYVVDFEEEFKDRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  92 TYFLDEYKKGRTPNPDVICNKEIKFKAFLDYAMDLGADYIATGHYARLQHdEDGTMHLLRGVDSNKDQTYFLSQLDSKTL 171
Cdd:COG0482   81 DYFLDEYLAGRTPNPCVLCNREIKFGALLEKALELGADYIATGHYARVEE-KDGRYELLRGVDPNKDQSYFLYRLTQEQL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482 172 QKVMFPLGEMVKPDVRKLALNAGLATAKKKDSVGICFIGEKNFKEFLGHYLPATPGKMMTFDGQVKGEHAGLMYYTIGQR 251
Cdd:COG0482  160 SKTLFPLGELTKPEVREIAEELGLPVADKKDSQGICFIGDGDYRDFLERYLPEKPGDIVDLDGKVLGEHDGLHYYTIGQR 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482 252 RGLGIGGDgednEPWFVVGKDLKKNILYVGKGYhnpHLYATHLKASDLHFVTDEDLGNDFHVTAKFRYRQKDSGVTVHFN 331
Cdd:COG0482  240 KGLGIGGG----EPLYVVGKDPETNTVIVGQGE---ALYSRELTAEDVNWISGEPPEEPLRCTAKIRYRQPPVPATLTPL 312

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 505453482 332 DDHTeVTVTFDDPVRAITPGQAVVFYNGEECLGSGMIDAAYN 373
Cdd:COG0482  313 EDGR-VRVEFDEPQRAVTPGQSAVFYDGDRVLGGGIIERTER 353
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
 15-368 0e+00

MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467502 [Multi-domain]  Cd Length: 349  Bit Score: 569.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  15 RVVVGMSGGVDSSVVALLLKQQGYDVVGVFMKNWDDTD-ENGVCTATEDYKDVAKVADKIGIPYYSINFEKEYWDRVFTY 93
Cdd:cd01998    1 KVAVAMSGGVDSSVAAALLKEQGYDVIGVFMKNWDDEDnEKGGCCSEEDIEDARRVADQLGIPLYVVDFSEEYWERVFDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  94 FLDEYKKGRTPNPDVICNKEIKFKAFLDYAMDLGADYIATGHYARLQHDEDGTMHLLRGVDSNKDQTYFLSQLDSKTLQK 173
Cdd:cd01998   81 FLEEYKAGRTPNPDVLCNREIKFGALLDAAKKLGADYIATGHYARIEEDNRGRYRLLRAVDPNKDQSYFLSRLSQEQLSR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482 174 VMFPLGEMVKPDVRKLALNAGLATAKKKDSVGICFIGEKNFKEFLGHYLP-ATPGKMMTFDGQVKGEHAGLMYYTIGQRR 252
Cdd:cd01998  161 TLFPLGHLTKSEVREIAREAGLPVAEKKDSQGICFIGKRDFRDFLKEYLPeKLPGPIVDIDGKVLGEHKGLWFYTIGQRK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482 253 GLGIGgdgeDNEPWFVVGKDLKKNILYVGKGyhNPHLYATHLKASDLHFVTDEDLGNDFHVTAKFRYRQKDSGVTVHFND 332
Cdd:cd01998  241 GLGIA----AGEPLYVVKKDPEKNIVVVGPG--HPALFSDTLRASDLNWISPEPPLEPLECEAKIRYRQPPVPCTVTPLD 314

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 505453482 333 DhTEVTVTFDDPVRAITPGQAVVFYNGEECLGSGMI 368
Cdd:cd01998  315 D-GRLKVEFDEPQRAVTPGQAAVFYDGDEVLGGGII 349
trmU TIGR00420
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ...
 15-368 8.57e-166

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: 467.63  E-value: 8.57e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482   15 RVVVGMSGGVDSSVVALLLKQQGYDVVGVFMKNWDDTDEN--GVCTATEDYKDVAKVADKIGIPYYSINFEKEYWDRVFT 92
Cdd:TIGR00420   2 KVIVGLSGGVDSSVSAYLLKQQGYEVVGVFMKNWEEDDKNdgHGCTSAEDLRDAQAICEKLGIPLEKVNFQKEYWNKVFE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482   93 YFLDEYKKGRTPNPDVICNKEIKFKAFLDYAM-DLGADYIATGHYARLQHDEdGTMHLLRGVDSNKDQTYFLSQLDSKTL 171
Cdd:TIGR00420  82 PFIQEYKEGRTPNPDILCNKFIKFGAFLEYAAeLLGNDKIATGHYARIAEIE-GKSLLLRALDKNKDQSYFLYHLSHEQL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  172 QKVMFPLGEMVKPDVRKLALNAGLATAKKKDSVGICFIGEKNFKEFLGHYLPATPGKMMTFDGQ-VKGEHAGLMYYTIGQ 250
Cdd:TIGR00420 161 AKLLFPLGELLKPEVRQIAKNAGLPTAEKKDSQGICFIGERKFRDFLKKYLPVKPGVIITVDGQsVIGEHDGLWFYTIGQ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  251 RRGLGIGGdgeDNEPWFVVGKDLKKNILYVGKGYhnPHLYATHLKASDLHFVTDEDLGNDFHVTAKFRYRQKDSGVTVHF 330
Cdd:TIGR00420 241 RKGLGIGG---AAEPWFVVEKDLETNELVVSHGK--PDLASRGLLAQQFHWLDDEPNPFEMRCTVKIRYRQVPVQCKLKL 315

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 505453482  331 NDDHTeVTVTFDDPVRAITPGQAVVFYNGEECLGSGMI 368
Cdd:TIGR00420 316 LDDNL-IEVIFDEPQAGVTPGQSAVLYKGDICLGGGII 352
tRNA_Me_trans pfam03054
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ...
 15-211 5.84e-122

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: 350.78  E-value: 5.84e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482   15 RVVVGMSGGVDSSVVALLLKQQGYDVVGVFMKNWDDT---DENGVCTATEDYKDVAKVADKIGIPYYSINFEKEYWDRVF 91
Cdd:pfam03054   2 KVVVAMSGGVDSSVAAYLLKEQGHNVIGVFMKNWDEEqslDEEGKCCSEEDLADAQRVCEQLGIPLYVVNFEKEYWEDVF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482   92 TYFLDEYKKGRTPNPDVICNKEIKFKAFLDYA-MDLGADYIATGHYARLQHDEDGTMHLLRGVDSNKDQTYFLSQLDSKT 170
Cdd:pfam03054  82 EPFLDEYKNGRTPNPDVLCNKEIKFGALLDYAlENLGADYVATGHYARVSLNKDGGSELLRALDKNKDQSYFLSTLSQEQ 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 505453482  171 LQKVMFPLGEMVKPDVRKLALNAGLATAKKKDSVGICFIGE 211
Cdd:pfam03054 162 LEKLLFPLGELTKEEVRKIAKEAGLATAKKKDSQGICFIGK 202
 
Name Accession Description Interval E-value
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
 14-369 0e+00

tRNA-specific 2-thiouridylase MnmA; Reviewed


Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 622.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  14 TRVVVGMSGGVDSSVVALLLKQQGYDVVGVFMKNWDDTDE--NGVCTATEDYKDVAKVADKIGIPYYSINFEKEYWDRVF 91
Cdd:PRK00143   1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVFMKLWDDDDEtgKGGCCAEEDIADARRVADKLGIPHYVVDFEKEFWDRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  92 TYFLDEYKKGRTPNPDVICNKEIKFKAFLDYAMDLGADYIATGHYARLQHDEdgtmHLLRGVDSNKDQTYFLSQLDSKTL 171
Cdd:PRK00143  81 DYFLDEYKAGRTPNPCVLCNKEIKFKAFLEYARELGADYIATGHYARIRDGR----ELLRGVDPNKDQSYFLYQLTQEQL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482 172 QKVMFPLGEMVKPDVRKLALNAGLATAKKKDSVGICFIGEKNFKEFLGHYLPATPGKMMTFDGQVKGEHAGLMYYTIGQR 251
Cdd:PRK00143 157 AKLLFPLGELTKPEVREIAEEAGLPVAKKKDSQGICFIGERDYRDFLKRYLPAQPGEIVDLDGKVLGEHKGLMYYTIGQR 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482 252 RGLGIGGDGednEPWFVVGKDLKKNILYVGKGyhnPHLYATHLKASDLHFVTDEDLGNDFHVTAKFRYRQKDSGVTVHFN 331
Cdd:PRK00143 237 KGLGIGGDG---EPWYVVGKDPETNTVVVGQG---EALYSRELIASDLNWVGGEPPEEPFECTAKIRYRQKPVPATVELE 310

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 505453482 332 DDhtEVTVTFDDPVRAITPGQAVVFYNGEECLGSGMID 369
Cdd:PRK00143 311 DD--RVEVEFDEPQRAVTPGQAAVFYDGDRVLGGGIIE 346
MnmA COG0482
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ...
 14-373 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: 622.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  14 TRVVVGMSGGVDSSVVALLLKQQGYDVVGVFMKNWDDTD--ENGVCTATEDYKDVAKVADKIGIPYYSINFEKEYWDRVF 91
Cdd:COG0482    1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVTMKLWDDDDasGSGGCCSLEDIEDARRVADKLGIPHYVVDFEEEFKDRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  92 TYFLDEYKKGRTPNPDVICNKEIKFKAFLDYAMDLGADYIATGHYARLQHdEDGTMHLLRGVDSNKDQTYFLSQLDSKTL 171
Cdd:COG0482   81 DYFLDEYLAGRTPNPCVLCNREIKFGALLEKALELGADYIATGHYARVEE-KDGRYELLRGVDPNKDQSYFLYRLTQEQL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482 172 QKVMFPLGEMVKPDVRKLALNAGLATAKKKDSVGICFIGEKNFKEFLGHYLPATPGKMMTFDGQVKGEHAGLMYYTIGQR 251
Cdd:COG0482  160 SKTLFPLGELTKPEVREIAEELGLPVADKKDSQGICFIGDGDYRDFLERYLPEKPGDIVDLDGKVLGEHDGLHYYTIGQR 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482 252 RGLGIGGDgednEPWFVVGKDLKKNILYVGKGYhnpHLYATHLKASDLHFVTDEDLGNDFHVTAKFRYRQKDSGVTVHFN 331
Cdd:COG0482  240 KGLGIGGG----EPLYVVGKDPETNTVIVGQGE---ALYSRELTAEDVNWISGEPPEEPLRCTAKIRYRQPPVPATLTPL 312

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 505453482 332 DDHTeVTVTFDDPVRAITPGQAVVFYNGEECLGSGMIDAAYN 373
Cdd:COG0482  313 EDGR-VRVEFDEPQRAVTPGQSAVFYDGDRVLGGGIIERTER 353
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
 15-368 0e+00

MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467502 [Multi-domain]  Cd Length: 349  Bit Score: 569.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  15 RVVVGMSGGVDSSVVALLLKQQGYDVVGVFMKNWDDTD-ENGVCTATEDYKDVAKVADKIGIPYYSINFEKEYWDRVFTY 93
Cdd:cd01998    1 KVAVAMSGGVDSSVAAALLKEQGYDVIGVFMKNWDDEDnEKGGCCSEEDIEDARRVADQLGIPLYVVDFSEEYWERVFDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  94 FLDEYKKGRTPNPDVICNKEIKFKAFLDYAMDLGADYIATGHYARLQHDEDGTMHLLRGVDSNKDQTYFLSQLDSKTLQK 173
Cdd:cd01998   81 FLEEYKAGRTPNPDVLCNREIKFGALLDAAKKLGADYIATGHYARIEEDNRGRYRLLRAVDPNKDQSYFLSRLSQEQLSR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482 174 VMFPLGEMVKPDVRKLALNAGLATAKKKDSVGICFIGEKNFKEFLGHYLP-ATPGKMMTFDGQVKGEHAGLMYYTIGQRR 252
Cdd:cd01998  161 TLFPLGHLTKSEVREIAREAGLPVAEKKDSQGICFIGKRDFRDFLKEYLPeKLPGPIVDIDGKVLGEHKGLWFYTIGQRK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482 253 GLGIGgdgeDNEPWFVVGKDLKKNILYVGKGyhNPHLYATHLKASDLHFVTDEDLGNDFHVTAKFRYRQKDSGVTVHFND 332
Cdd:cd01998  241 GLGIA----AGEPLYVVKKDPEKNIVVVGPG--HPALFSDTLRASDLNWISPEPPLEPLECEAKIRYRQPPVPCTVTPLD 314

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 505453482 333 DhTEVTVTFDDPVRAITPGQAVVFYNGEECLGSGMI 368
Cdd:cd01998  315 D-GRLKVEFDEPQRAVTPGQAAVFYDGDEVLGGGII 349
trmU TIGR00420
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ...
 15-368 8.57e-166

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: 467.63  E-value: 8.57e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482   15 RVVVGMSGGVDSSVVALLLKQQGYDVVGVFMKNWDDTDEN--GVCTATEDYKDVAKVADKIGIPYYSINFEKEYWDRVFT 92
Cdd:TIGR00420   2 KVIVGLSGGVDSSVSAYLLKQQGYEVVGVFMKNWEEDDKNdgHGCTSAEDLRDAQAICEKLGIPLEKVNFQKEYWNKVFE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482   93 YFLDEYKKGRTPNPDVICNKEIKFKAFLDYAM-DLGADYIATGHYARLQHDEdGTMHLLRGVDSNKDQTYFLSQLDSKTL 171
Cdd:TIGR00420  82 PFIQEYKEGRTPNPDILCNKFIKFGAFLEYAAeLLGNDKIATGHYARIAEIE-GKSLLLRALDKNKDQSYFLYHLSHEQL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  172 QKVMFPLGEMVKPDVRKLALNAGLATAKKKDSVGICFIGEKNFKEFLGHYLPATPGKMMTFDGQ-VKGEHAGLMYYTIGQ 250
Cdd:TIGR00420 161 AKLLFPLGELLKPEVRQIAKNAGLPTAEKKDSQGICFIGERKFRDFLKKYLPVKPGVIITVDGQsVIGEHDGLWFYTIGQ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  251 RRGLGIGGdgeDNEPWFVVGKDLKKNILYVGKGYhnPHLYATHLKASDLHFVTDEDLGNDFHVTAKFRYRQKDSGVTVHF 330
Cdd:TIGR00420 241 RKGLGIGG---AAEPWFVVEKDLETNELVVSHGK--PDLASRGLLAQQFHWLDDEPNPFEMRCTVKIRYRQVPVQCKLKL 315

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 505453482  331 NDDHTeVTVTFDDPVRAITPGQAVVFYNGEECLGSGMI 368
Cdd:TIGR00420 316 LDDNL-IEVIFDEPQAGVTPGQSAVLYKGDICLGGGII 352
tRNA_Me_trans pfam03054
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ...
 15-211 5.84e-122

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: 350.78  E-value: 5.84e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482   15 RVVVGMSGGVDSSVVALLLKQQGYDVVGVFMKNWDDT---DENGVCTATEDYKDVAKVADKIGIPYYSINFEKEYWDRVF 91
Cdd:pfam03054   2 KVVVAMSGGVDSSVAAYLLKEQGHNVIGVFMKNWDEEqslDEEGKCCSEEDLADAQRVCEQLGIPLYVVNFEKEYWEDVF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482   92 TYFLDEYKKGRTPNPDVICNKEIKFKAFLDYA-MDLGADYIATGHYARLQHDEDGTMHLLRGVDSNKDQTYFLSQLDSKT 170
Cdd:pfam03054  82 EPFLDEYKNGRTPNPDVLCNKEIKFGALLDYAlENLGADYVATGHYARVSLNKDGGSELLRALDKNKDQSYFLSTLSQEQ 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 505453482  171 LQKVMFPLGEMVKPDVRKLALNAGLATAKKKDSVGICFIGE 211
Cdd:pfam03054 162 LEKLLFPLGELTKEEVRKIAKEAGLATAKKKDSQGICFIGK 202
PRK14664 PRK14664
tRNA-specific 2-thiouridylase MnmA; Provisional
 10-368 1.10e-77

tRNA-specific 2-thiouridylase MnmA; Provisional


Pssm-ID: 173127 [Multi-domain]  Cd Length: 362  Bit Score: 243.71  E-value: 1.10e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  10 DHSNTRVVVGMSGGVDSSVVALLLKQQGYDVVGVFMKNWDDTDEngvctatedykDVAKVADKIGIPYYSINFEKEYWDR 89
Cdd:PRK14664   2 KESKKRVLVGMSGGIDSTATCLMLQEQGYEIVGVTMRVWGDEPQ-----------DARELAARMGIEHYVADERVPFKDT 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  90 VFTYFLDEYKKGRTPNPDVICNKEIKFKAFLDYAMDLGADYIATGHYARLQhDEDGTMHLLRGVDSNKDQTYFLSQLDSK 169
Cdd:PRK14664  71 IVKNFIDEYRQGRTPNPCVMCNPLFKFRMLIEWADKLGCAWIATGHYSRLE-ERNGHIYIVAGDDDKKDQSYFLWRLGQD 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482 170 TLQKVMFPLGEMVKPDVRKLALNAGL-ATAKKKDSVGICFIgEKNFKEFLGHYLP-----ATPGKMMTFDGQVKGEHAGL 243
Cdd:PRK14664 150 ILRRCIFPLGNYTKQTVREYLREKGYeAKSKEGESMEVCFI-KGDYRDFLREQCPeldteVGPGWFVNSEGVKLGQHKGF 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482 244 MYYTIGQRRGLGIGgdgeDNEPWFVVGKDLKKNILYVGKGyhnPHLYATHLKASDLHFVTDEDLGNDFHVTAKFRYRQKD 323
Cdd:PRK14664 229 PYYTIGQRKGLEIA----LGKPAYVLKINPQKNTVMLGDA---EQLKAEYMLAEQDNIVDEQELFACPDLAVRIRYRSRP 301

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 505453482 324 SGVTVHFNDDhTEVTVTFDDPVRAITPGQAVVFYNGEECLGSGMI 368
Cdd:PRK14664 302 IPCRVKRLED-GRLLVRFLAEASAIAPGQSAVFYEGRRVLGGAFI 345
mnmA PRK14665
tRNA-specific 2-thiouridylase MnmA; Provisional
 12-368 3.68e-68

tRNA-specific 2-thiouridylase MnmA; Provisional


Pssm-ID: 173128 [Multi-domain]  Cd Length: 360  Bit Score: 219.03  E-value: 3.68e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  12 SNTRVVVGMSGGVDSSVVALLLKQQGYDVVGVFMKNWDDTDEngvctaTEDYKDVAKVADKIGIPYYSINFEKEYWDRVF 91
Cdd:PRK14665   4 KNKRVLLGMSGGTDSSVAAMLLLEAGYEVTGVTFRFYEFNGS------TEYLEDARALAERLGIGHITYDARKVFRKQII 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  92 TYFLDEYKKGRTPNPDVICNKEIKFKAFLDYAMDLGADYIATGHYARLQHdEDGTMHLLRGVDSNKDQTYFLSQLDSKTL 171
Cdd:PRK14665  78 DYFIDEYMSGHTPVPCTLCNNYLKWPLLAKIADEMGIFYLATGHYVRKQW-IDGNYYITPAEDVDKDQSFFLWGLRQEIL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482 172 QKVMFPLGEMVKPDVRKLALNAG-LATAKKKDSVGICFIgEKNFKEFLGHYLPAT-------------PGKMMTFDGQVK 237
Cdd:PRK14665 157 QRMLLPMGGMTKSEARAYAAERGfEKVAKKRDSLGVCFC-PMDYRSFLKKCLCDEsgdknrniyrkveRGRFLDESGNFI 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482 238 GEHAGLMYYTIGQRRGLGIGGD---------GEDNEpwfVVGKDLKKnilyvgkgyhnphLYATHLKASDLHFVTDEDLG 308
Cdd:PRK14665 236 AWHEGYPFYTIGQRRGLGIQLNravfvkeihPETNE---VVLASLKA-------------LEKTEMWLKDWNIVNESRLL 299

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482 309 NDFHVTAKFRYRQKDSGVTVHFNDDHTeVTVTFDDPVRAITPGQAVVFYNGEECLGSGMI 368
Cdd:PRK14665 300 GCDDIIVKIRYRKQENHCTVTITPDNL-LHVQLHEPLTAIAEGQAAAFYKDGLLLGGGII 358
tRNA_Me_trans_M pfam20259
tRNA methyl transferase PRC-barrel domain; This family represents a central PRC-barrel domain ...
 215-282 3.78e-23

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: 91.51  E-value: 3.78e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505453482  215 KEFLGHYLPATPGKMMTFD-GQVKGEHAGLMYYTIGQRRGLGIGGDGednEPWFVVGKDLKKNILYVGK 282
Cdd:pfam20259   1 KDFLKEYLPVKPGDIIDIDtGEVLGEHEGIWFYTIGQRKGLGIGGYG---EPWYVVEKDPKKNTVYVGR 66
tRNA_Me_trans_C pfam20258
Aminomethyltransferase beta-barrel domain; This domain is found at the C-terminus of tRNA ...
 292-368 2.49e-22

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: 89.64  E-value: 2.49e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505453482  292 THLKASDLHFVTDEDLGNDFHVTAKFRYRQKDSGVTVHFNDDHTeVTVTFDDPVRAITPGQAVVFYNGEECLGSGMI 368
Cdd:pfam20258   2 DGLRAKDPNWLGDKPPTEPLECTVKVRHRQPPVPCVVELIDDET-VEVHFDEPVRAVTPGQAAVFYDGDRCLGGGII 77
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 13-152 1.74e-12

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: 66.39  E-value: 1.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  13 NTRVVVGMSGGVDSSVVALLLKQ----QGYDVVGVFMknwddtDENGVCTATEDYKDVAKVADKIGIPYYSINFEKEYWD 88
Cdd:COG0037   15 GDRILVAVSGGKDSLALLHLLAKlrrrLGFELVAVHV------DHGLREESDEDAEFVAELCEELGIPLHVVRVDVPAIA 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  89 RvftyfldeyKKGRTPnpdviCNK--EIKFKAFLDYAMDLGADYIATGHyarlqH--DEDGT--MHLLRG 152
Cdd:COG0037   89 K---------KEGKSP-----EAAarRARYGALYELARELGADKIATGH-----HldDQAETflLNLLRG 139
CTU1-like cd01713
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ...
 15-152 1.89e-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: 51.05  E-value: 1.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  15 RVVVGMSGGVDSSVVALLLKQqgydvvgvFMKNWDD--------TDEngvctATEDYKD-----VAKVADKIGIPYYSIN 81
Cdd:cd01713   20 RVAVGLSGGKDSTVLLYVLKE--------LNKRHDYgveliavtIDE-----GIKGYRDdsleaARKLAEEYGIPLEIVS 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505453482  82 FEKEywdrvFTYFLDE--YKKGRTPNPDVICNKeIKFKAFLDYAMDLGADYIATGHYArlqHDEDGT--MHLLRG 152
Cdd:cd01713   87 FEDE-----FGFTLDEliVGKGGKKNACTYCGV-FRRRALNRGARELGADKLATGHNL---DDEAETilMNLLRG 152
COG1365 COG1365
Predicted ATPase, PP-loop superfamily [General function prediction only];
13-134 2.09e-07

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


Pssm-ID: 440976  Cd Length: 256  Bit Score: 51.59  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  13 NTRVVVGMSGGVDSSVVALLLKQQGYDVVGVFMKNW----DDTDENgvctatedykdVAKVADKIGIPYysinfekEYWD 88
Cdd:COG1365   60 NPKVVVAFSGGVDSSASLIIAKWIGFDVEAVTVKSTiilpQMFKKN-----------IKELCKKLNVKH-------EFIE 121

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 505453482  89 RVFTYFLDEYKKGRTPnPDVICNKEIKfKAFLDYAMDLGADYIATG 134
Cdd:COG1365  122 IDLGEIIEDALKGKFH-PCGRCHSLIE-EAVEDYAKKNGIKIVIFG 165
NadE COG0171
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ...
 15-81 1.47e-06

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: 50.23  E-value: 1.47e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505453482  15 RVVVGMSGGVDSSVVALLLKQ-QGYD-VVGVFM--KNwddtdengvcTATEDYKDVAKVADKIGIPYYSIN 81
Cdd:COG0171  288 GVVLGLSGGIDSALVAALAVDaLGPEnVLGVTMpsRY----------TSDESLEDAEELAENLGIEYEEID 348
TtcA-like cd24138
tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) ...
 13-199 1.55e-06

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: 48.04  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  13 NTRVVVGMSGGVDSSVVALLLK------QQGYDVVGVFMknwdDTDENGvctatedYKDVAKVADKIGIPYYSInFEKEY 86
Cdd:cd24138    8 GDRILVGLSGGKDSLTLLHLLEelkrraPIKFELVAVTV----DPGYPG-------YRPPREELAEILEELGEI-LEDEE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  87 WDRVFTYfldEYKKGRtpNPDVICNKeIKFKAFLDYAMDLGADYIATGHyarlqHDED----GTMHLLRGVDSNKDQTYF 162
Cdd:cd24138   76 SEIIIIE---KEREEK--SPCSLCSR-LRRGILYSLAKELGCNKLALGH-----HLDDavetLLMNLLYGGRLKTMPPKV 144

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 505453482 163 LSQLDSKTLQKVMFPLGEMvkpDVRKLALNAGLATAK 199
Cdd:cd24138  145 TMDRGGLTVIRPLIYVREK---DIRAFAEENGLPKIE 178
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 15-152 1.72e-06

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: 48.01  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482   15 RVVVGMSGGVDSsvVALLLkqqgydvvgvFMKNWDDTDENGVCTATEDY----------KDVAKVADKIGIPYYSINFEK 84
Cdd:TIGR02432   1 RILVAVSGGVDS--MALLH----------LLLKLQPKIKIKLIAAHVDHglrpesdeeaEFVQQFCRKLNIPLEIKKVDV 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505453482   85 EYWDRVFTYFLDEykKGRtpnpdvicnkEIKFKAFLDYAMDLGADYIATGHyarlqHDEDGT----MHLLRG 152
Cdd:TIGR02432  69 KALAKGKKKNLEE--AAR----------EARYDFFEEIAKKHGADYILTAH-----HADDQAetilMRLLRG 123
TtuA-like cd01993
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ...
 15-143 1.91e-06

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


Pssm-ID: 467497 [Multi-domain]  Cd Length: 190  Bit Score: 47.71  E-value: 1.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  15 RVVVGMSGGVDSSVVALLLKQQGYDVVGVFMknwddtdENGVCTATEDYKDVAK-VADKIGIPYYSINFEKEYWDRVfty 93
Cdd:cd01993   10 KILVAVSGGKDSLALLAVLKKLGYNVEALYI-------NLGIGEYSEKSEEVVKkLAEKLNLPLHVVDLKEEYGLGI--- 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 505453482  94 flDEYKKGRTPNPDVICNKeIKFKAFLDYAMDLGADYIATGHYArlqHDE 143
Cdd:cd01993   80 --PELAKKSRRPPCSVCGL-VKRYIMNKFAVENGFDVVATGHNL---DDE 123
NAD_synthase cd00553
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ...
 15-81 2.01e-06

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: 48.71  E-value: 2.01e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505453482  15 RVVVGMSGGVDSSVVALLLKQ--QGYDVVGVFMKnwddtdenGVCTATEDYKDVAKVADKIGIPYYSIN 81
Cdd:cd00553   25 GFVLGLSGGIDSAVVAALAVRalGAENVLALIMP--------SRYSSKETRDDAKALAENLGIEYRTID 85
COG1606 COG1606
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
15-134 3.57e-06

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


Pssm-ID: 441214 [Multi-domain]  Cd Length: 265  Bit Score: 47.80  E-value: 3.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  15 RVVVGMSGGVDSSVVALLLKQQ-GYDVVGVfmknwddtdengvcTAT------EDYKDVAKVADKIGIPYYSINFEkeyw 87
Cdd:COG1606   17 SVLVAFSGGVDSTLLAKVAHDVlGDRVLAV--------------TADspslpeRELEEAKELAKEIGIRHEVIETD---- 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 505453482  88 drvftyFLD--EYKKgrtpNPD---VICNKEIkFKAFLDYAMDLGADYIATG 134
Cdd:COG1606   79 ------ELEdpEFVA----NPPdrcYHCKKEL-FSKLKELAKELGYAVVADG 119
PRK13980 PRK13980
NAD synthetase; Provisional
 14-81 5.60e-06

NAD synthetase; Provisional


Pssm-ID: 184435 [Multi-domain]  Cd Length: 265  Bit Score: 47.51  E-value: 5.60e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  14 TRVVVGMSGGVDSSVVA-LLLKQQGYD-VVGVFMKnwddtdenGVCTATEDYKDVAKVADKIGIPYYSIN 81
Cdd:PRK13980  31 KGVVLGLSGGIDSAVVAyLAVKALGKEnVLALLMP--------SSVSPPEDLEDAELVAEDLGIEYKVIE 92
NAD_synthase pfam02540
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ...
 16-83 6.11e-06

NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is induced by stress factors such as heat shock and glucose limitation.


Pssm-ID: 396888 [Multi-domain]  Cd Length: 241  Bit Score: 46.99  E-value: 6.11e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505453482   16 VVVGMSGGVDSSVVA-----LLLKQQgydVVGVFMKnwddtdenGVCTATEDYKDVAKVADKIGIPYYSINFE 83
Cdd:pfam02540  21 VVLGLSGGIDSSLVAylavkALGKEN---VLALIMP--------SSQSSEEDVQDALALAENLGIEYKTIDIK 82
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 16-53 8.27e-06

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: 43.21  E-value: 8.27e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 505453482  16 VVVGMSGGVDSSVVALLLKQQGYD--VVGVFMKNWDDTDE 53
Cdd:cd01986    1 VVVGYSGGKDSSVALHLASRLGRKaeVAVVHIDHGIGFKE 40
LarE-like cd01990
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ...
 15-200 1.74e-05

Lactate racemization operon protein LarE and similar proteins; This subfamily includes Lactiplantibacillus plantarum LarE, a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family. LarE is part of the lar operon, encoding five Lar proteins (LarA-E) that collaboratively synthesize and incorporate a niacin-derived Ni-containing cofactor into LarA, an Ni-dependent lactate racemase. It catalyzes successive thiolation reactions by donating the sulfur atom of their exclusive cysteine residues to the substrate. The LarE-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. Proteins from this subfamily probably binds ATP. This domain is about 200 amino acids long with a strongly conserved motif SGGxDS at the N-terminus.


Pssm-ID: 467494 [Multi-domain]  Cd Length: 222  Bit Score: 45.33  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  15 RVVVGMSGGVDSSVVALLLKQQGYD-VVGVFMKNwddtdengvCTATEDYKDVAK-VADKIGIPYYSINfekeywdrvFT 92
Cdd:cd01990    1 KVVVAFSGGVDSSLLAKLAKEVLGDnVVAVTADS---------PLVPREELEEAKrIAEEIGIRHEIIK---------TD 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  93 YFLDEYKKGRTPNPDVICNKEIkFKAFLDYAMDLGADYIAtghyarlqhdeDGTmhllrGVDSNKDQT---YFLSQLDSK 169
Cdd:cd01990   63 ELDDEEYVANDPDRCYHCKKAL-YSTLKEIAKERGYDVVL-----------DGT-----NADDLKDYRpglLAAAELGIR 125

                        170       180       190
                 ....*....|....*....|....*....|.
gi 505453482 170 TLqkvmFPLGEMVKPDVRKLALNAGLATAKK 200
Cdd:cd01990  126 SP----LPELGLTKSEIRELARELGLPNWDK 152
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 15-152 2.68e-05

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: 44.51  E-value: 2.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  15 RVVVGMSGGVDSsvVALLLkqqgydvvgvFMKNWDDTDENGVC----------TATEDYKDVAKVADKIGIPYYSINFEK 84
Cdd:cd01992    1 KILVAVSGGPDS--MALLH----------LLKELRPKLGLKLVavhvdhglreESAEEAQFVAKLCKKLGIPLHILTVTE 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505453482  85 EYWDRVFTyfldEyKKGRtpnpdvicnkEIKFKAFLDYAMDLGADYIATGHyarlqH--DEDGT--MHLLRG 152
Cdd:cd01992   69 APKSGGNL----E-AAAR----------EARYAFLERAAKEHGIDVLLTAH-----HldDQAETvlMRLLRG 120
PRK04527 PRK04527
argininosuccinate synthase; Provisional
 12-134 2.90e-05

argininosuccinate synthase; Provisional


Pssm-ID: 235305  Cd Length: 400  Bit Score: 45.60  E-value: 2.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  12 SNTRVVVGMSGGVDSSVVALLLKQQGYDVVGVFmknwddTDENGVCTATEDYkdVAKVADKIGI-PYYSINFEKEYWDRV 90
Cdd:PRK04527   1 SSKDIVLAFSGGLDTSFCIPYLQERGYAVHTVF------ADTGGVDAEERDF--IEKRAAELGAaSHVTVDGGPAIWEGF 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 505453482  91 FTYFL--DEYKKGRTPnpdVIC-NKEIKFKAFLDYAMDLGADYIATG 134
Cdd:PRK04527  73 VKPLVwaGEGYQGQYP---LLVsDRYLIVDAALKRAEELGTRIIAHG 116
nadE TIGR00552
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ...
 16-80 3.35e-05

NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the biosynthesis of the essensial cofactor NAD. The member of this family from Bacillus subtilis is a strictly NH(3)-dependent NAD(+) synthetase of 272 amino acids. Proteins consisting only of the domain modeled here may be named as NH3-dependent NAD+ synthetase. Amidotransferase activity may reside in a separate protein, or not be present. Some other members of the family, such as from Mycobacterium tuberculosis, are considerably longer, contain an apparent amidotransferase domain, and show glutamine-dependent as well as NH(3)-dependent activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]


Pssm-ID: 273132 [Multi-domain]  Cd Length: 250  Bit Score: 45.07  E-value: 3.35e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505453482   16 VVVGMSGGVDSSVVALL-LKQQGYDVVGVFMKNWDDTDEngvctatEDYKDVAKVADKIGIPYYSI 80
Cdd:TIGR00552  25 VVLGLSGGIDSAVVAALcVEALGEQNHALLLPHSVQTPE-------QDVQDALALAEPLGINYKNI 83
QueC-like cd01995
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ...
 15-195 6.46e-05

7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC 6.3.4.20) is also called 7-cyano-7-carbaguanine synthase, preQ(0) synthase, or queuosine biosynthesis protein QueC. It catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)), as part of the biosynthesis pathway of queuosine (Q). Q is one of the most complex modifications occurring at the wobble position of tRNAs with GUN anticodons, and is implicated in a number of biological activities, including accuracy of decoding, virulence, and cellular differentiation. This subfamily belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467499 [Multi-domain]  Cd Length: 208  Bit Score: 43.76  E-value: 6.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  15 RVVVGMSGGVDSSVVALLLKQQGYDVVGVFMkNWddtdenGVCTATEDYKDVAKVADKIGIPYYSIN--FEKEYW----D 88
Cdd:cd01995    2 KAVVLLSGGLDSTTLLYWALKEGYEVHALTF-DY------GQRHAKEELEAAKLIAKLLGIEHKVIDlsFLGELGgsslT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  89 RVFTYFLDEYKKGRTPNPDVICNKEIKFKAF-LDYAMDLGADYIATG-HYARLQHDEDGTMHLLRGVDSnkdqtyfLSQL 166
Cdd:cd01995   75 DEGEEVPDGEYDEESIPSTWVPNRNLIFLSIaAAYAESLGASAIVIGvNAEDASGYPDCRPEFVEAMNS-------ALNL 147

                        170       180
                 ....*....|....*....|....*....
gi 505453482 167 DSKTLQKVMFPLGEMVKPDVRKLALNAGL 195
Cdd:cd01995  148 GTATGVKVVAPLIGLSKAEIVKLGVELGV 176
guaA PRK00074
GMP synthase; Reviewed
 15-35 2.11e-04

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 43.11  E-value: 2.11e-04
                         10        20
                 ....*....|....*....|.
gi 505453482  15 RVVVGMSGGVDSSVVALLLKQ 35
Cdd:PRK00074 217 KVILGLSGGVDSSVAAVLLHK 237
QueC COG0603
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ...
 12-43 2.32e-03

7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; 7-cyano-7-deazaguanine synthase (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440368 [Multi-domain]  Cd Length: 223  Bit Score: 38.99  E-value: 2.32e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 505453482  12 SNTRVVVGMSGGVDSSVVALLLKQQGYDVVGV 43
Cdd:COG0603    1 MMKKAVVLLSGGLDSTTCLAWALARGYEVYAL 32
PPase_ThiI cd01712
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole ...
 12-134 2.45e-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: 38.69  E-value: 2.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  12 SNTRVVVGMSGGVDSSVVALLLKQQGYDVVGVFMKNWDDTDEngvctatedyKDVAKVADKIgipyysinfekeywdRVF 91
Cdd:cd01712    3 TSGKVLVLLSGGIDSPVAAWMMMKRGVEVDFLHFHSGPYTSE----------KAVEKVKDLA---------------RVL 57

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 505453482  92 TYFLDEYKKGRTPNPDVIcNKEIKFKAFLDY----------------AMDLGADYIATG 134
Cdd:cd01712   58 SEYQGGVKLYLVPFTDKI-QKEILEKVPESYrivlmrrmmyriaekiAERLGADALVTG 115
nadE PRK00876
NAD(+) synthase;
16-45 5.49e-03

NAD(+) synthase;


Pssm-ID: 179150 [Multi-domain]  Cd Length: 326  Bit Score: 38.40  E-value: 5.49e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 505453482  16 VVVGMSGGVDSSVV-ALLLKQQGYD-VVGVFM 45
Cdd:PRK00876  36 VVLGLSGGIDSSVTaALCVRALGKErVYGLLM 67
PRK13820 PRK13820
argininosuccinate synthase; Provisional
 13-86 7.25e-03

argininosuccinate synthase; Provisional


Pssm-ID: 237521  Cd Length: 394  Bit Score: 37.99  E-value: 7.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505453482  13 NTRVVVGMSGGVDSSVVALLLKQQ-GYD-VVGVFMKnwddtdengVCTATEDYKDVAKVADKIGIPYYSIN----FEKEY 86
Cdd:PRK13820   2 MKKVVLAYSGGLDTSVCVPLLKEKyGYDeVITVTVD---------VGQPEEEIKEAEEKAKKLGDKHYTIDakeeFAKDY 72
GMP_synthase_C cd01997
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ...
 15-44 8.84e-03

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


Pssm-ID: 467501 [Multi-domain]  Cd Length: 311  Bit Score: 37.52  E-value: 8.84e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 505453482  15 RVVVGMSGGVDSSVVALLLKQQGYD--VVGVF 44
Cdd:cd01997    9 KVLCLVSGGVDSTVCAALLHKALGDerVIAVH 40
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH