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Conserved domains on  [gi|446788497|ref|WP_000865753|]
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MULTISPECIES: tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex dimerization subunit type 1 TsaB [Bacillus]

Protein Classification

tRNA threonylcarbamoyladenosine biosynthesis protein TsaB( domain architecture ID 10003119)

tRNA threonylcarbamoyladenosine biosynthesis protein TsaB (also known as YeaZ) is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine

EC:  2.3.1.234
Gene Ontology:  GO:0002949
PubMed:  22378793

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TsaB COG1214
tRNA A37 threonylcarbamoyladenosine modification protein TsaB [Translation, ribosomal ...
 1-228 6.48e-83

tRNA A37 threonylcarbamoyladenosine modification protein TsaB [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine modification protein TsaB is part of the Pathway/BioSystem: tRNA modification


:

Pssm-ID: 440827  Cd Length: 227  Bit Score: 246.30  E-value: 6.48e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497   1 MKVLAIDTSNYVMGVSLIEEGNVIGEIITNLTKNHSVRLMPAVEKLLKECGVKPKELTKIVVAAGPGSYTGVRIGVTAAK 80
Cdd:COG1214    1 MLILAIDTSTEACSVALLDDGEVLAEREENDGRGHSERLLPMIDELLAEAGLTLSDLDAIAVGIGPGSFTGLRIGVATAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497  81 TLAWSLQIPIVGVSSLEVVAANG-ANFNGLICPLFDGRRGQIYTGLYTYEGEQLTSIEEDRIILIVDWLQMLKDKgqPVL 159
Cdd:COG1214   81 GLALALGIPLVGVSSLEALAAQApRAGAGLVLVAIDARRGEVYWAVYDADDGELERLGEPRVLAPEELAEPLAGG--PVL 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446788497 160 FIGNDVKLHKETIIEHLgdqAVFAPFTkNNPRPSELAFLGLQKEEQ----DVHTFVPSYLRLAEAETKWLESQ 228
Cdd:COG1214  159 FVGDGAEAYAELLAEAL---AVLADAL-ALPSAAALARLAAARLAAgeaeDPADLEPLYLRDPDAEPPAERKA 227
 
Name Accession Description Interval E-value
TsaB COG1214
tRNA A37 threonylcarbamoyladenosine modification protein TsaB [Translation, ribosomal ...
 1-228 6.48e-83

tRNA A37 threonylcarbamoyladenosine modification protein TsaB [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine modification protein TsaB is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440827  Cd Length: 227  Bit Score: 246.30  E-value: 6.48e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497   1 MKVLAIDTSNYVMGVSLIEEGNVIGEIITNLTKNHSVRLMPAVEKLLKECGVKPKELTKIVVAAGPGSYTGVRIGVTAAK 80
Cdd:COG1214    1 MLILAIDTSTEACSVALLDDGEVLAEREENDGRGHSERLLPMIDELLAEAGLTLSDLDAIAVGIGPGSFTGLRIGVATAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497  81 TLAWSLQIPIVGVSSLEVVAANG-ANFNGLICPLFDGRRGQIYTGLYTYEGEQLTSIEEDRIILIVDWLQMLKDKgqPVL 159
Cdd:COG1214   81 GLALALGIPLVGVSSLEALAAQApRAGAGLVLVAIDARRGEVYWAVYDADDGELERLGEPRVLAPEELAEPLAGG--PVL 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446788497 160 FIGNDVKLHKETIIEHLgdqAVFAPFTkNNPRPSELAFLGLQKEEQ----DVHTFVPSYLRLAEAETKWLESQ 228
Cdd:COG1214  159 FVGDGAEAYAELLAEAL---AVLADAL-ALPSAAALARLAAARLAAgeaeDPADLEPLYLRDPDAEPPAERKA 227
T6A_YeaZ TIGR03725
tRNA threonylcarbamoyl adenosine modification protein YeaZ; This family describes a protein ...
 3-216 9.80e-73

tRNA threonylcarbamoyl adenosine modification protein YeaZ; This family describes a protein family, YeaZ, now associated with the threonylcarbamoyl adenosine (t6A) tRNA modification. Members of this family may occur as fusions with ygjD (previously gcp) or the ribosomal protein N-acetyltransferase rimI, and is frequently encoded next to rimI. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274750 [Multi-domain]  Cd Length: 204  Bit Score: 219.83  E-value: 9.80e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497    3 VLAIDTSNYVMGVSLIEEGNVIGEIITNLTKNHSVRLMPAVEKLLKECGVKPKELTKIVVAAGPGSYTGVRIGVTAAKTL 82
Cdd:TIGR03725   1 ILAIDTSTEALSVALLDDGKVLAERTEPAGRNHSERLLPMIEELLAEAGLSLQDLDAIAVGVGPGSFTGLRIGLATAKGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497   83 AWSLQIPIVGVSSLEVVAANGA--NFNGLICPLFDGRRGQIYTGLYtyegeQLTSIEEDRIILIVDWLQMLKDKgqPVLF 160
Cdd:TIGR03725  81 ALALGIPLVGVSSLEALAAQAAaqDGGGPVLVAIDARRGEVYWGLY-----DLKPLEEPAVLSPEELLELLKEL--NVLL 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497  161 IGNDVKLHKEtiiehlgdqAVFAPFTKNNPRPSELAFLGLQK----EEQDVHTFVPSYLR 216
Cdd:TIGR03725 154 VGDGAEAYAL---------ALLAAAADALPDAAALARLALARlkagEPLDVEELEPLYLR 204
ASKHA_NBD_TsaB cd24032
nucleotide-binding domain (NBD) of tRNA threonylcarbamoyladenosine biosynthesis protein TsaB ...
 3-202 4.25e-63

nucleotide-binding domain (NBD) of tRNA threonylcarbamoyladenosine biosynthesis protein TsaB (previously known as YeaZ) and similar proteins; TsaB, also called t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaB, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It may be involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaE. TsaB seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD. In fact, it can act as a protease that specifically degrades TsaD in vitro; therefore, TsaB may post-translationally regulate cellular pools of TsaD via proteolytic degradation. TsaB does not show sialoglycoprotease activity against glycophorin A.


Pssm-ID: 466882 [Multi-domain]  Cd Length: 205  Bit Score: 195.19  E-value: 4.25e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497   3 VLAIDTSNYVMGVSLIEEGNVIGEIITNLTKNHSVRLMPAVEKLLKECGVKPKELTKIVVAAGPGSYTGVRIGVTAAKTL 82
Cdd:cd24032    1 ILAIDTSTSACSVALLKGGKILAEYELDLGRRHSERLLPMIDELLKEAGLSLKDLDAIAVGIGPGSFTGLRIGLATAKGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497  83 AWSLQIPIVGVSSLEVVAANGANFNGLICPLFDGRRGQIYTGLYTYEGEQLTSiEEDRIILIVDWLQMLKDKGQPVLFIG 162
Cdd:cd24032   81 ALALGIPLVGVSTLEALAQNAPRADGRVLPAIDARRGEVYWALYERDKGGLIL-EEEEAVLPPEELEEILLLKKPAILVG 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446788497 163 NDVKLHKETIiehlgDQAVFAPFTKNNPRPSELAFLGLQK 202
Cdd:cd24032  160 DGWDKYPDLI-----KENPVLPIELLLPSAADLAPLALAK 194
TsaD pfam00814
tRNA N6-adenosine threonylcarbamoyltransferase; This domain can be found in Kae1/Qri7/YgjD, ...
 2-224 1.69e-47

tRNA N6-adenosine threonylcarbamoyltransferase; This domain can be found in Kae1/Qri7/YgjD, products of COG0533 that belong to a small group of 60 proteins that are present in all three domains of life. COG0533 proteins are suggest to play a role in a post translational modification of certain tRNAs. For example, YgjD along with YeaZ, YjeE, and YrdC have been deemed necessary and sufficient for the tRNA modification. This modification involves the formation of N6-threonyl carbamoyl adenosine (t6A) at position 37 in the anti-codon stem loop which is critical for translational speed and accuracy. Structural analysis indicate that YeaZ lacks resemblance to any known protease active site. Together with the absence of a putative zinc-binding motif. Thus the likelyhood of it being a protease, as previously thought, has been negated. EC:2.3.1.234


Pssm-ID: 395656  Cd Length: 272  Bit Score: 157.54  E-value: 1.69e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497    2 KVLAIDTSNYVMgvSLIEEGNVIGEIitnLTKNHSVRLMPAVEKLLKECGVKPKELTKIVVAAGPGSYTGVRIGVTAAKT 81
Cdd:pfam00814   1 EILANVILSQKD--LHAPYGGVVPEL---ASRHHSERLMPLIDEALAEAGLSLEDLDAIAVTKGPGLFTGLRVGASFAKG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497   82 LAWSLQIPIVGVSSLEVVAANGANFNGL---ICPLFDGRRGQIYT---GLYTYEGEQLTSIEEDRIILIVDWL------- 148
Cdd:pfam00814  76 LALALNKPLVGVNHLEAHALAARLETGLefpVVLLVSGGHTQVYAakdGRYEILGETLDDAAGEAFDKVARLLglpypgg 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497  149 ----QMLKD---------KGQPVLFIGNDVKLHK----------------ETIIEHLgdqAVFAPFTKNNPRPSELAFLG 199
Cdd:pfam00814 156 pkieKLAKEgafefprpvKGMDFSFSGLKTAVLRliekkepkediaasfqEAVFDHL---AEKTERALKLPGAKELVILG 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 446788497  200 -------LQK------EEQDVHTFVPS--YLRLAEAETKW 224
Cdd:pfam00814 233 gvaankrLREaltemaEERGVKLFAPPleYCTDNGAMIAW 272
PRK09604 PRK09604
tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD;
1-97 9.22e-14

tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD;


Pssm-ID: 236585  Cd Length: 332  Bit Score: 68.94  E-value: 9.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497   1 MKVLAIDTSNYVMGVSLIEEGN-VIGEIITNLTKNHSV---------------RLMPAVEKLLKECGVKPKELTKIVVAA 64
Cdd:PRK09604   1 MLILGIETSCDETSVAVVDDGRgLLSNVVASQIDLHARyggvvpelasrahveNIVPLIEEALKEAGLTLEDIDAIAVTA 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446788497  65 GPGSYTGVRIGVTAAKTLAWSLQIPIVGVSSLE 97
Cdd:PRK09604  81 GPGLVGALLVGVSFAKALALALNKPLIGVNHLE 113
 
Name Accession Description Interval E-value
TsaB COG1214
tRNA A37 threonylcarbamoyladenosine modification protein TsaB [Translation, ribosomal ...
 1-228 6.48e-83

tRNA A37 threonylcarbamoyladenosine modification protein TsaB [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine modification protein TsaB is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440827  Cd Length: 227  Bit Score: 246.30  E-value: 6.48e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497   1 MKVLAIDTSNYVMGVSLIEEGNVIGEIITNLTKNHSVRLMPAVEKLLKECGVKPKELTKIVVAAGPGSYTGVRIGVTAAK 80
Cdd:COG1214    1 MLILAIDTSTEACSVALLDDGEVLAEREENDGRGHSERLLPMIDELLAEAGLTLSDLDAIAVGIGPGSFTGLRIGVATAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497  81 TLAWSLQIPIVGVSSLEVVAANG-ANFNGLICPLFDGRRGQIYTGLYTYEGEQLTSIEEDRIILIVDWLQMLKDKgqPVL 159
Cdd:COG1214   81 GLALALGIPLVGVSSLEALAAQApRAGAGLVLVAIDARRGEVYWAVYDADDGELERLGEPRVLAPEELAEPLAGG--PVL 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446788497 160 FIGNDVKLHKETIIEHLgdqAVFAPFTkNNPRPSELAFLGLQKEEQ----DVHTFVPSYLRLAEAETKWLESQ 228
Cdd:COG1214  159 FVGDGAEAYAELLAEAL---AVLADAL-ALPSAAALARLAAARLAAgeaeDPADLEPLYLRDPDAEPPAERKA 227
T6A_YeaZ TIGR03725
tRNA threonylcarbamoyl adenosine modification protein YeaZ; This family describes a protein ...
 3-216 9.80e-73

tRNA threonylcarbamoyl adenosine modification protein YeaZ; This family describes a protein family, YeaZ, now associated with the threonylcarbamoyl adenosine (t6A) tRNA modification. Members of this family may occur as fusions with ygjD (previously gcp) or the ribosomal protein N-acetyltransferase rimI, and is frequently encoded next to rimI. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274750 [Multi-domain]  Cd Length: 204  Bit Score: 219.83  E-value: 9.80e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497    3 VLAIDTSNYVMGVSLIEEGNVIGEIITNLTKNHSVRLMPAVEKLLKECGVKPKELTKIVVAAGPGSYTGVRIGVTAAKTL 82
Cdd:TIGR03725   1 ILAIDTSTEALSVALLDDGKVLAERTEPAGRNHSERLLPMIEELLAEAGLSLQDLDAIAVGVGPGSFTGLRIGLATAKGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497   83 AWSLQIPIVGVSSLEVVAANGA--NFNGLICPLFDGRRGQIYTGLYtyegeQLTSIEEDRIILIVDWLQMLKDKgqPVLF 160
Cdd:TIGR03725  81 ALALGIPLVGVSSLEALAAQAAaqDGGGPVLVAIDARRGEVYWGLY-----DLKPLEEPAVLSPEELLELLKEL--NVLL 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497  161 IGNDVKLHKEtiiehlgdqAVFAPFTKNNPRPSELAFLGLQK----EEQDVHTFVPSYLR 216
Cdd:TIGR03725 154 VGDGAEAYAL---------ALLAAAADALPDAAALARLALARlkagEPLDVEELEPLYLR 204
ASKHA_NBD_TsaB cd24032
nucleotide-binding domain (NBD) of tRNA threonylcarbamoyladenosine biosynthesis protein TsaB ...
 3-202 4.25e-63

nucleotide-binding domain (NBD) of tRNA threonylcarbamoyladenosine biosynthesis protein TsaB (previously known as YeaZ) and similar proteins; TsaB, also called t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaB, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It may be involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaE. TsaB seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD. In fact, it can act as a protease that specifically degrades TsaD in vitro; therefore, TsaB may post-translationally regulate cellular pools of TsaD via proteolytic degradation. TsaB does not show sialoglycoprotease activity against glycophorin A.


Pssm-ID: 466882 [Multi-domain]  Cd Length: 205  Bit Score: 195.19  E-value: 4.25e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497   3 VLAIDTSNYVMGVSLIEEGNVIGEIITNLTKNHSVRLMPAVEKLLKECGVKPKELTKIVVAAGPGSYTGVRIGVTAAKTL 82
Cdd:cd24032    1 ILAIDTSTSACSVALLKGGKILAEYELDLGRRHSERLLPMIDELLKEAGLSLKDLDAIAVGIGPGSFTGLRIGLATAKGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497  83 AWSLQIPIVGVSSLEVVAANGANFNGLICPLFDGRRGQIYTGLYTYEGEQLTSiEEDRIILIVDWLQMLKDKGQPVLFIG 162
Cdd:cd24032   81 ALALGIPLVGVSTLEALAQNAPRADGRVLPAIDARRGEVYWALYERDKGGLIL-EEEEAVLPPEELEEILLLKKPAILVG 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446788497 163 NDVKLHKETIiehlgDQAVFAPFTKNNPRPSELAFLGLQK 202
Cdd:cd24032  160 DGWDKYPDLI-----KENPVLPIELLLPSAADLAPLALAK 194
TsaD pfam00814
tRNA N6-adenosine threonylcarbamoyltransferase; This domain can be found in Kae1/Qri7/YgjD, ...
 2-224 1.69e-47

tRNA N6-adenosine threonylcarbamoyltransferase; This domain can be found in Kae1/Qri7/YgjD, products of COG0533 that belong to a small group of 60 proteins that are present in all three domains of life. COG0533 proteins are suggest to play a role in a post translational modification of certain tRNAs. For example, YgjD along with YeaZ, YjeE, and YrdC have been deemed necessary and sufficient for the tRNA modification. This modification involves the formation of N6-threonyl carbamoyl adenosine (t6A) at position 37 in the anti-codon stem loop which is critical for translational speed and accuracy. Structural analysis indicate that YeaZ lacks resemblance to any known protease active site. Together with the absence of a putative zinc-binding motif. Thus the likelyhood of it being a protease, as previously thought, has been negated. EC:2.3.1.234


Pssm-ID: 395656  Cd Length: 272  Bit Score: 157.54  E-value: 1.69e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497    2 KVLAIDTSNYVMgvSLIEEGNVIGEIitnLTKNHSVRLMPAVEKLLKECGVKPKELTKIVVAAGPGSYTGVRIGVTAAKT 81
Cdd:pfam00814   1 EILANVILSQKD--LHAPYGGVVPEL---ASRHHSERLMPLIDEALAEAGLSLEDLDAIAVTKGPGLFTGLRVGASFAKG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497   82 LAWSLQIPIVGVSSLEVVAANGANFNGL---ICPLFDGRRGQIYT---GLYTYEGEQLTSIEEDRIILIVDWL------- 148
Cdd:pfam00814  76 LALALNKPLVGVNHLEAHALAARLETGLefpVVLLVSGGHTQVYAakdGRYEILGETLDDAAGEAFDKVARLLglpypgg 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497  149 ----QMLKD---------KGQPVLFIGNDVKLHK----------------ETIIEHLgdqAVFAPFTKNNPRPSELAFLG 199
Cdd:pfam00814 156 pkieKLAKEgafefprpvKGMDFSFSGLKTAVLRliekkepkediaasfqEAVFDHL---AEKTERALKLPGAKELVILG 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 446788497  200 -------LQK------EEQDVHTFVPS--YLRLAEAETKW 224
Cdd:pfam00814 233 gvaankrLREaltemaEERGVKLFAPPleYCTDNGAMIAW 272
ASKHA_NBD_Kae1_TsaB-like cd24001
nucleotide-binding domain (NBD) of the Kae1/TsaB-like domain family; The family includes tRNA ...
 3-108 1.67e-14

nucleotide-binding domain (NBD) of the Kae1/TsaB-like domain family; The family includes tRNA N6-adenosine threonylcarbamoyltransferase Kae1/TsaD, tRNA threonylcarbamoyladenosine biosynthesis protein TsaB (previously known as YeaZ), as well as proteins from the NodU/CmcH subfamily. tRNA N6-adenosine threonylcarbamoyltransferase (EC 2.3.1.234) is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. TsaB is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It may be involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaE. TsaB seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD. The NodU/CmcH family includes NodU from Rhizobium, CmcH from Amycolatopsis lactamdurans, the bifunctional carbamoyltransferase TobZ from Streptoalloteichus tenebrarius, NovN from Streptomyces niveus and NolNO from Sinorhizobium fredii. NodU is a Rhizobium nodulation protein involved in the synthesis of nodulation factors has 6-O-carbamoyltransferase-like activity. 3'-hydroxymethylcephem-O-carbamoyltransferase CmcH (EC 2.1.3.7) is involved in cephamycin (antibiotic) biosynthesis and has 3-hydroxymethylcephem carbamoyltransferase activity. nebramycin 5' synthase TobZ (EC 6.1.2.2) functions as an ATP carbamoyltransferase and tobramycin carbamoyltransferase. Novobiocin biosynthesis protein NovN (EC 2.1.3.12) acts as a carbamoyltransferase that mediates 3'-carbamoylation of the noviosyl ring to produce novobiocin, the final step in the novobiocin biosynthesis pathway. nodulation protein NolNO (EC 2.1.3.-) is involved in the O-carbamoylation of nod factors. The NodU/CmcH subfamily proteins consist of two domains. Only the N-terminal domain shows similarity with Kae1/TsaB-like domain, which belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466851 [Multi-domain]  Cd Length: 186  Bit Score: 69.02  E-value: 1.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497   3 VLAIDTSNYVMGVSLIEEGNVI------------GEIITNLTKNHSVRLMPAVEKLLKECGVKPKELTKIVVAAGPGSYT 70
Cdd:cd24001    1 VLGIEGSAEDTGVAIVDDGGVLanhfetyvtektGGYPPEAARHHARRIVPLIQEALAESGLTLDDIDAIAFGRGPGLGG 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446788497  71 GVRIGVTAAKTLAWSLQIPIVGVSSLEVVAANGANFNG 108
Cdd:cd24001   81 ALRVGATVARGLALAWDKPLIGVNHCIAHAEIAKLKTG 118
TsaD COG0533
tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; ...
 1-97 1.73e-14

tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyltransferase TsaD is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440299  Cd Length: 333  Bit Score: 71.19  E-value: 1.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497   1 MKVLAIDTSNYVMGVSLIEEGnviGEIITNLTK-------------------NHSVRLMPAVEKLLKECGVKPKELTKIV 61
Cdd:COG0533    1 MLILGIETSCDETAAAVVDDG---RGLLSNVVAsqidlharyggvvpelasrAHLENILPLVEEALEEAGVTLKDIDAIA 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446788497  62 VAAGPGSYTGVRIGVTAAKTLAWSLQIPIVGVSSLE 97
Cdd:COG0533   78 VTAGPGLIGALLVGVSFAKALALALGKPLIGVNHLE 113
PRK09604 PRK09604
tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD;
1-97 9.22e-14

tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD;


Pssm-ID: 236585  Cd Length: 332  Bit Score: 68.94  E-value: 9.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497   1 MKVLAIDTSNYVMGVSLIEEGN-VIGEIITNLTKNHSV---------------RLMPAVEKLLKECGVKPKELTKIVVAA 64
Cdd:PRK09604   1 MLILGIETSCDETSVAVVDDGRgLLSNVVASQIDLHARyggvvpelasrahveNIVPLIEEALKEAGLTLEDIDAIAVTA 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446788497  65 GPGSYTGVRIGVTAAKTLAWSLQIPIVGVSSLE 97
Cdd:PRK09604  81 GPGLVGALLVGVSFAKALALALNKPLIGVNHLE 113
ASKHA_NBD_TsaD_bac cd24133
nucleotide-binding domain (NBD) of bacterial tRNA N6-adenosine threonylcarbamoyltransferase ...
 3-97 6.21e-13

nucleotide-binding domain (NBD) of bacterial tRNA N6-adenosine threonylcarbamoyltransferase TsaD and similar proteins; TsaD (EC 2.3.1.234), also called N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD, or tRNA threonylcarbamoyladenosine biosynthesis protein TsaD, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.


Pssm-ID: 466983  Cd Length: 328  Bit Score: 66.74  E-value: 6.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497   3 VLAIDTSNYVMGVSLIEEGnviGEIITNLT-------------------KNHSVRLMPAVEKLLKECGVKPKELTKIVVA 63
Cdd:cd24133    1 ILGIETSCDETAVAVVDDG---GKILSNVVssqidlhakyggvvpeiasRAHLENIIPVVEEALEEAGLTLDDIDAIAVT 77

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446788497  64 AGPGSYTGVRIGVTAAKTLAWSLQIPIVGVSSLE 97
Cdd:cd24133   78 YGPGLIGALLVGVSFAKALAFALNKPLIGVNHLE 111
ASKHA_NBD_Kae1_arch_bac cd24131
nucleotide-binding domain (NBD) of tRNA N6-adenosine threonylcarbamoyltransferase (Kae1) and ...
 1-93 6.64e-11

nucleotide-binding domain (NBD) of tRNA N6-adenosine threonylcarbamoyltransferase (Kae1) and similar proteins mainly from archaea and bacteria; Kae1 (EC 2.3.1.234), also called N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1, or tRNA threonylcarbamoyladenosine biosynthesis protein Kae1, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Kae1 likely plays a direct catalytic role in this reaction but requires other protein(s) of the complex to fulfill this activity. The family also includes bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein (EC 2.3.1.234/EC 2.7.11.1), which contains a Kae1 domain and a Bud32 domain. The Kae1 domain may play a catalytic role and the Bud32 domain probably displays kinase activity that regulates Kae1 function.


Pssm-ID: 466981  Cd Length: 323  Bit Score: 60.75  E-value: 6.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497   1 MKVLAIDTSNYVMGVSLIEEGnviGEIITNLTK----------------NHSVRLMPAVEKLLKECGVKPKELTKIVVAA 64
Cdd:cd24131    1 MIVLGIEGTAHTFGVGIVDSE---GEVLANVTDtyvpekggihpreaaeHHSEVAPELIKKALEEAGVSLNDIDLIAFSQ 77

                         90       100
                 ....*....|....*....|....*....
gi 446788497  65 GPGSYTGVRIGVTAAKTLAWSLQIPIVGV 93
Cdd:cd24131   78 GPGLGPCLRVVATAARALALKLDKPLVGV 106
ASKHA_NBD_Kae1_TsaD cd24031
nucleotide-binding domain (NBD) of the Kae1/TsaD family tRNA N6-adenosine ...
 3-93 1.22e-09

nucleotide-binding domain (NBD) of the Kae1/TsaD family tRNA N6-adenosine threonylcarbamoyltransferase; tRNA N6-adenosine threonylcarbamoyltransferase (EC 2.3.1.234), also called N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein, or tRNA threonylcarbamoyladenosine biosynthesis protein, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The family includes different orthologous of tRNA N6-adenosine threonylcarbamoyltransferase, such as bacterial kinase-associated endopeptidase 1 (Kae1) and TsaD (also known as YgjD) protein, mammalian O-sialoglycoprotein endopeptidase (OSGEP) and yeast protein Kae1, as well as mammalian OSGEP-like protein 1 (OSGEPL1) and yeast protein Qri7, which are the mitochondrial versions of the universal Kae1/TsaD (also known as YgjD) protein and essential for mitochondrial genome maintenance.


Pssm-ID: 466881  Cd Length: 304  Bit Score: 57.10  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497   3 VLAIDTSNYVMGVSLI-EEGNVI------------GEIITNLTKNHSVRLM-PAVEKLLKECGVKPKELTKIVVAAGPGS 68
Cdd:cd24031    1 VLGIEGSADKTGVGIVdDEGKVLanqldtyvtpkaGGIVPEEAARHHARKIvPLIQEALKESGLTAKDIDLIAYTQGPGL 80

                         90       100
                 ....*....|....*....|....*
gi 446788497  69 YTGVRIGVTAAKTLAWSLQIPIVGV 93
Cdd:cd24031   81 GGALRVGATVARTLAVAWNKPIIGV 105
PRK14878 PRK14878
UGMP family protein; Provisional
 4-93 5.37e-09

UGMP family protein; Provisional


Pssm-ID: 184878  Cd Length: 323  Bit Score: 55.31  E-value: 5.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497   4 LAIDTSNYVMGVSLIEEGNVIGEIITNLT------------KNHSVRLMPAVEKLLKECGVKPKELTKIVVAAGPGSYTG 71
Cdd:PRK14878   1 LGIESTAHTLGVGIVKEDKVLANVRDTYVpekggihpreaaQHHAEVAPELLRKALEKAGISIEDIDAVAVSQGPGLGPA 80

                         90       100
                 ....*....|....*....|..
gi 446788497  72 VRIGVTAAKTLAWSLQIPIVGV 93
Cdd:PRK14878  81 LRVGATAARALALKYNKPLVPV 102
ASKHA_NBD_Kae1-like cd24096
nucleotide-binding domain (NBD) of Kae1 and similar proteins; Kae1 (EC 2.3.1.234), also called ...
 3-93 1.74e-08

nucleotide-binding domain (NBD) of Kae1 and similar proteins; Kae1 (EC 2.3.1.234), also called kinase-associated endopeptidase 1, N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, kinase-associated endopeptidase 1 (Kae1), t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1, or tRNA threonylcarbamoyladenosine biosynthesis protein Kae1, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Kae1 likely plays a direct catalytic role in this reaction but requires other protein(s) of the complex to fulfill this activity. OSGEP (EC 2.3.1.234), also called tRNA N6-adenosine threonylcarbamoyltransferase, N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein OSGEP, tRNA threonylcarbamoyladenosine biosynthesis protein OSGEP, is the mammalian orthologue of kinase-associated endopeptidase Kae1. The family also includes bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein (EC 2.3.1.234/EC 2.7.11.1), which contains a Kae1 domain and a Bud32 domain. The Kae1 domain may play a catalytic role and the Bud32 domain probably displays kinase activity that regulates Kae1 function.


Pssm-ID: 466946  Cd Length: 301  Bit Score: 53.59  E-value: 1.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497   3 VLAIDTSNYVMGVSLIE-EGNVI-----------GEIITNLTKNHSVRLMPAV-EKLLKECGVKPKELTKIVVAAGPGSY 69
Cdd:cd24096    2 CLGIEGTAHTFGVGIVDsDGKVLanvrdmytppkGGIHPREAADHHAEVFDKLlSEALEEAGVTINDIDLIAFSQGPGLG 81

                         90       100
                 ....*....|....*....|....
gi 446788497  70 TGVRIGVTAAKTLAWSLQIPIVGV 93
Cdd:cd24096   82 PSLRVTATVARTLAVLLNKPIIGV 105
ASKHA_NBD_OSGEPL1_QRI7_euk cd24134
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase-like protein 1 (OSGEPL1) ...
 3-97 5.80e-08

nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase-like protein 1 (OSGEPL1) and similar proteins from eukayotes; The family includes mammalian OSGEPL1 and yeast QRI7, which are the mitochondrial orthologs of the universal Kae1/ TsaD (also known as YgjD) protein. OSGEPL1/QRI7 (EC 2.3.1.234), also called mitochondrial tRNA N6-adenosine threonylcarbamoyltransferase, N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein, or tRNA threonylcarbamoyladenosine biosynthesis protein, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. It is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. It is involved in mitochondrial genome maintenance.


Pssm-ID: 466984  Cd Length: 330  Bit Score: 52.14  E-value: 5.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497   3 VLAIDTSNYVMGVSLI-EEGNVIGEIITNLTK---------------NHSVRLMPAVEKLLKECGVKPKELTKIVVAAGP 66
Cdd:cd24134    1 VLGIETSCDDTGAAVVdSDGRILGEALASQKEiheqyggivptlaadLHRANIPRVVEEALEQAGLSLSDLDAVAVTVGP 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446788497  67 GSYTGVRIGVTAAKTLAWSLQIPIVGVSSLE 97
Cdd:cd24134   81 GLALCLRVGLEFAKGLAAAHNKPLIPVHHME 111
ASKHA_NBD_TsaD-like cd24097
nucleotide-binding domain (NBD) of TsaD and similar proteins; TsaD (EC 2.3.1.234), also called ...
 3-97 1.15e-07

nucleotide-binding domain (NBD) of TsaD and similar proteins; TsaD (EC 2.3.1.234), also called N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD, or tRNA threonylcarbamoyladenosine biosynthesis protein TsaD, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction. The family also includes mammalian OSGEP-like protein 1 (OSGEPL1) and yeast protein Qri7, which are the mitochondrial versions of the universal Kae1/TsaD (also known as YgjD) protein and essential for mitochondrial genome maintenance.


Pssm-ID: 466947  Cd Length: 313  Bit Score: 51.13  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497   3 VLAIDTSNYVMGVSLIE-EGNVI---------------GEIITNLTKNHSVRLMPAVEKLLKECGVKPKELTKIVVAAGP 66
Cdd:cd24097    1 VLGIETSCDETGIAIYDdEKGLLanqlysqvklhadygGVVPELASRDHVRKTVPLIQAALKESGLTAKDIDAVAYTAGP 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446788497  67 GSYTGVRIGVTAAKTLAWSLQIPIVGVSSLE 97
Cdd:cd24097   81 GLVGALLVGATVGRSLAFAWNVPAIPVHHME 111
PTZ00340 PTZ00340
O-sialoglycoprotein endopeptidase-like protein; Provisional
 3-93 4.75e-06

O-sialoglycoprotein endopeptidase-like protein; Provisional


Pssm-ID: 240369  Cd Length: 345  Bit Score: 46.57  E-value: 4.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497   3 VLAIDTSNYVMGVSLIEEGnviGEIITNL-----------------TKNHSVRLMPAVEKLLKECGVKPKELTKIVVAAG 65
Cdd:PTZ00340   3 ALGIEGSANKLGVGIVTSD---GEILSNVretyitppgtgflpretAQHHREHILSLVKEALEEAKITPSDISLICYTKG 79

                         90       100
                 ....*....|....*....|....*...
gi 446788497  66 PGSYTGVRIGVTAAKTLAWSLQIPIVGV 93
Cdd:PTZ00340  80 PGMGAPLSVGAVVARTLSLLWGKPLVGV 107
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
1-93 5.25e-06

bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 46.81  E-value: 5.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446788497   1 MKVLAIDTSNYVMGVSLIEEGnviGEIITNLTK---------------NHSVRLMPAV-EKLLKECGVKPKELTKIVVAA 64
Cdd:PRK09605   1 MIVLGIEGTAWKTSAGIVDSD---GDVLFNESDpykppsggihpreaaEHHAEAIPKViKEALEEAGLKPEDIDLVAFSQ 77

                         90       100
                 ....*....|....*....|....*....
gi 446788497  65 GPGSYTGVRIGVTAAKTLAWSLQIPIVGV 93
Cdd:PRK09605  78 GPGLGPCLRVVATAARALALSLDVPLIGV 106
ASKHA_NBD_OSGEP_like_euk cd24132
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase (OSGEP) and similar ...
 33-93 2.66e-04

nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase (OSGEP) and similar proteins mainly from eukaryotes; OSGEP (EC 2.3.1.234), also called tRNA N6-adenosine threonylcarbamoyltransferase, N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein OSGEP, tRNA threonylcarbamoyladenosine biosynthesis protein OSGEP, is a component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. OSGEP likely plays a direct catalytic role in this reaction but requires other protein(s) of the complex to fulfill this activity. OSGEP is the mammalian orthologue of kinase-associated endopeptidase Kae1.


Pssm-ID: 466982  Cd Length: 309  Bit Score: 40.99  E-value: 2.66e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446788497  33 KNHSVRLMPAVEKLLKECGVKPKELTKIVVAAGPGSYTGVRIGVTAAKTLAWSLQIPIVGV 93
Cdd:cd24132   46 KHHRAHILDLVKEALKEAGITPSDIDCICYTKGPGMGAPLQSVAVVARTLSQLWNKPLVGV 106
 
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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