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Conserved domains on  [gi|495966361|ref|WP_008690940|]
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MULTISPECIES: L-threonylcarbamoyladenylate synthase [Longicatena]

Protein Classification

L-threonylcarbamoyladenylate synthase( domain architecture ID 10000228)

L-threonylcarbamoyladenylate synthase catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate, and 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

CATH:  3.90.870.10
EC:  2.7.7.87
PubMed:  29650678|19287007
SCOP:  4000384

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
TsaC COG0009
tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC [Translation, ribosomal ...
1-201 1.18e-78

tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC is part of the Pathway/BioSystem: tRNA modification


:

Pssm-ID: 439780 [Multi-domain]  Cd Length: 204  Bit Score: 233.83  E-value: 1.18e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966361   1 METV-RYEAKDIETIADLLKEGKVVAFPTDTVYGLAVIYENEAALEALKKSKGRPENKPIPTMVSNFRQMEEIA-YMSED 78
Cdd:COG0009    1 MATIlKIQPRLIEQAAEALRAGGVVAYPTDTVYGLGCDALNKEAVERIFAIKGRPRDKPLIVLVADLSQLEEYAkEVPDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966361  79 ARKLAEEFMPGGFTMILKKKEHLPAYLTNGFDTVGIRMPDDDIILHLIDLCEKPLLVTSANLSGEEPQETAEGVLKQLDG 158
Cdd:COG0009   81 ARRLAKAFWPGPLTLILPATKEVPDLLTGGRDTVAVRVPDHPVALALLRALGPPLASTSANLSGEPPPTTAEEVREQLGD 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 495966361 159 RIDAIV-VGESGGSKASTIVDMSTDELRIVREGPISEKRIREVL 201
Cdd:COG0009  161 RVDLILdGGPCGVGVPSTIVDLTGGEPEILRPGAIDVEELEEVL 204
 
Name Accession Description Interval E-value
TsaC COG0009
tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC [Translation, ribosomal ...
1-201 1.18e-78

tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439780 [Multi-domain]  Cd Length: 204  Bit Score: 233.83  E-value: 1.18e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966361   1 METV-RYEAKDIETIADLLKEGKVVAFPTDTVYGLAVIYENEAALEALKKSKGRPENKPIPTMVSNFRQMEEIA-YMSED 78
Cdd:COG0009    1 MATIlKIQPRLIEQAAEALRAGGVVAYPTDTVYGLGCDALNKEAVERIFAIKGRPRDKPLIVLVADLSQLEEYAkEVPDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966361  79 ARKLAEEFMPGGFTMILKKKEHLPAYLTNGFDTVGIRMPDDDIILHLIDLCEKPLLVTSANLSGEEPQETAEGVLKQLDG 158
Cdd:COG0009   81 ARRLAKAFWPGPLTLILPATKEVPDLLTGGRDTVAVRVPDHPVALALLRALGPPLASTSANLSGEPPPTTAEEVREQLGD 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 495966361 159 RIDAIV-VGESGGSKASTIVDMSTDELRIVREGPISEKRIREVL 201
Cdd:COG0009  161 RVDLILdGGPCGVGVPSTIVDLTGGEPEILRPGAIDVEELEEVL 204
TIGR00057 TIGR00057
tRNA threonylcarbamoyl adenosine modification protein, Sua5/YciO/YrdC/YwlC family; Has ...
11-201 2.26e-62

tRNA threonylcarbamoyl adenosine modification protein, Sua5/YciO/YrdC/YwlC family; Has paralogs, but YrdC called a tRNA modification protein. Ref 2 authors say probably heteromultimeric complex. Paralogs may mean its does the final binding to the tRNA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 272879 [Multi-domain]  Cd Length: 201  Bit Score: 192.16  E-value: 2.26e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966361   11 IETIADLLKEGKVVAFPTDTVYGLAVIYENEAALEALKKSKGRPENKPIPTMVSNFRQMEEIAYMSEDARKLAEEFMPGG 90
Cdd:TIGR00057  11 IEQAVKILRKGGIVVYPTDTVYGIGADALDEDAVRRLYRIKGRPSNKPLTVLVSDLSEIEKYAYVPDDAKRLMKKFWPGP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966361   91 FTMILKKKEHLPAYLTNGFDTVGIRMPDDDIILHLIDLCEKPLLVTSANLSGEEPQETAEGVLKQLDGRIDAIV-VGESG 169
Cdd:TIGR00057  91 LTLVLKKTPEIPRRVSGKRKTIGIRVPDNPIALELLEELGKPIVATSANLSGKPSATDVEEAVDELGKLVDLIIdAGPCL 170
                         170       180       190
                  ....*....|....*....|....*....|..
gi 495966361  170 GSKASTIVDMSTDELRIVREGPISEkRIREVL 201
Cdd:TIGR00057 171 GGEPSTIIDLTDDTPKVLREGVGSE-PIEKVL 201
Sua5_yciO_yrdC pfam01300
Telomere recombination; This domain has been shown to bind preferentially to dsRNA. The domain ...
16-188 1.39e-58

Telomere recombination; This domain has been shown to bind preferentially to dsRNA. The domain is found in SUA5 as well as HypF and YrdC. It has also been shown to be required for telomere recombniation in yeast.


Pssm-ID: 460153 [Multi-domain]  Cd Length: 176  Bit Score: 181.94  E-value: 1.39e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966361   16 DLLKEGKVVAFPTDTVYGLAVIYENEAALEALKKSKGRPENKPIPTMVSNFRQMEEIAY-MSEDARKLAEEFMPGGFTMI 94
Cdd:pfam01300   1 EALRKGGIVAYPTDTVYGLGCDATNEEAVERLYEIKGRPRDKPLAVMVADLEDLKEYAEeVEEAALRLAERFWPGPLTLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966361   95 LKK-KEHLPAYLTNGFDTVGIRMPDDDIILHLIDLCEKPLLVTSANLSGEEPQETAEGVLKQLDGRIDAIVV-GESGGSK 172
Cdd:pfam01300  81 LKAsKKPLPKLLTPGLGTVGVRLPDHPLALLLLEALGEPLVATSANLSGEPSPTDAEEILEELGGRVDLILDgGRIAGGV 160
                         170
                  ....*....|....*.
gi 495966361  173 ASTIVDMSTDELRIVR 188
Cdd:pfam01300 161 PSTVVDLTGGPPRILR 176
PRK10634 PRK10634
L-threonylcarbamoyladenylate synthase type 1 TsaC;
11-190 1.04e-28

L-threonylcarbamoyladenylate synthase type 1 TsaC;


Pssm-ID: 182603  Cd Length: 190  Bit Score: 105.96  E-value: 1.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966361  11 IETIADLLKEGKVVAFPTDTVYGLAVIYENEAALEALKKSKGRPENKPIPTMVSNFRQME---EIAYMSEDARKLAEEFM 87
Cdd:PRK10634  10 IAAAVDVLNEERVIAYPTEAVFGVGCDPDSETAVMRLLELKQRPVDKGLILIAANYEQLKpyiDDSMLTDAQRETIFSCW 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966361  88 PGGFTMILKKKEHLPAYLTNGFDTVGIRMPDDDIILHLIDLCEKPLLVTSANLSGEEPQETAEGVLKQLDGRIdAIVVGE 167
Cdd:PRK10634  90 PGPVTFVFPAPATTPRWLTGRFDSLAVRVTDHPLVVALCQAYGKPLVSTSANLSGLPPCRTVEEVRAQFGAAF-PVVPGE 168
                        170       180
                 ....*....|....*....|....
gi 495966361 168 SGGSK-ASTIVDMSTDELriVREG 190
Cdd:PRK10634 169 TGGRLnPSEIRDALTGEL--FRQG 190
 
Name Accession Description Interval E-value
TsaC COG0009
tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC [Translation, ribosomal ...
1-201 1.18e-78

tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439780 [Multi-domain]  Cd Length: 204  Bit Score: 233.83  E-value: 1.18e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966361   1 METV-RYEAKDIETIADLLKEGKVVAFPTDTVYGLAVIYENEAALEALKKSKGRPENKPIPTMVSNFRQMEEIA-YMSED 78
Cdd:COG0009    1 MATIlKIQPRLIEQAAEALRAGGVVAYPTDTVYGLGCDALNKEAVERIFAIKGRPRDKPLIVLVADLSQLEEYAkEVPDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966361  79 ARKLAEEFMPGGFTMILKKKEHLPAYLTNGFDTVGIRMPDDDIILHLIDLCEKPLLVTSANLSGEEPQETAEGVLKQLDG 158
Cdd:COG0009   81 ARRLAKAFWPGPLTLILPATKEVPDLLTGGRDTVAVRVPDHPVALALLRALGPPLASTSANLSGEPPPTTAEEVREQLGD 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 495966361 159 RIDAIV-VGESGGSKASTIVDMSTDELRIVREGPISEKRIREVL 201
Cdd:COG0009  161 RVDLILdGGPCGVGVPSTIVDLTGGEPEILRPGAIDVEELEEVL 204
TIGR00057 TIGR00057
tRNA threonylcarbamoyl adenosine modification protein, Sua5/YciO/YrdC/YwlC family; Has ...
11-201 2.26e-62

tRNA threonylcarbamoyl adenosine modification protein, Sua5/YciO/YrdC/YwlC family; Has paralogs, but YrdC called a tRNA modification protein. Ref 2 authors say probably heteromultimeric complex. Paralogs may mean its does the final binding to the tRNA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 272879 [Multi-domain]  Cd Length: 201  Bit Score: 192.16  E-value: 2.26e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966361   11 IETIADLLKEGKVVAFPTDTVYGLAVIYENEAALEALKKSKGRPENKPIPTMVSNFRQMEEIAYMSEDARKLAEEFMPGG 90
Cdd:TIGR00057  11 IEQAVKILRKGGIVVYPTDTVYGIGADALDEDAVRRLYRIKGRPSNKPLTVLVSDLSEIEKYAYVPDDAKRLMKKFWPGP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966361   91 FTMILKKKEHLPAYLTNGFDTVGIRMPDDDIILHLIDLCEKPLLVTSANLSGEEPQETAEGVLKQLDGRIDAIV-VGESG 169
Cdd:TIGR00057  91 LTLVLKKTPEIPRRVSGKRKTIGIRVPDNPIALELLEELGKPIVATSANLSGKPSATDVEEAVDELGKLVDLIIdAGPCL 170
                         170       180       190
                  ....*....|....*....|....*....|..
gi 495966361  170 GSKASTIVDMSTDELRIVREGPISEkRIREVL 201
Cdd:TIGR00057 171 GGEPSTIIDLTDDTPKVLREGVGSE-PIEKVL 201
Sua5_yciO_yrdC pfam01300
Telomere recombination; This domain has been shown to bind preferentially to dsRNA. The domain ...
16-188 1.39e-58

Telomere recombination; This domain has been shown to bind preferentially to dsRNA. The domain is found in SUA5 as well as HypF and YrdC. It has also been shown to be required for telomere recombniation in yeast.


Pssm-ID: 460153 [Multi-domain]  Cd Length: 176  Bit Score: 181.94  E-value: 1.39e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966361   16 DLLKEGKVVAFPTDTVYGLAVIYENEAALEALKKSKGRPENKPIPTMVSNFRQMEEIAY-MSEDARKLAEEFMPGGFTMI 94
Cdd:pfam01300   1 EALRKGGIVAYPTDTVYGLGCDATNEEAVERLYEIKGRPRDKPLAVMVADLEDLKEYAEeVEEAALRLAERFWPGPLTLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966361   95 LKK-KEHLPAYLTNGFDTVGIRMPDDDIILHLIDLCEKPLLVTSANLSGEEPQETAEGVLKQLDGRIDAIVV-GESGGSK 172
Cdd:pfam01300  81 LKAsKKPLPKLLTPGLGTVGVRLPDHPLALLLLEALGEPLVATSANLSGEPSPTDAEEILEELGGRVDLILDgGRIAGGV 160
                         170
                  ....*....|....*.
gi 495966361  173 ASTIVDMSTDELRIVR 188
Cdd:pfam01300 161 PSTVVDLTGGPPRILR 176
PRK10634 PRK10634
L-threonylcarbamoyladenylate synthase type 1 TsaC;
11-190 1.04e-28

L-threonylcarbamoyladenylate synthase type 1 TsaC;


Pssm-ID: 182603  Cd Length: 190  Bit Score: 105.96  E-value: 1.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966361  11 IETIADLLKEGKVVAFPTDTVYGLAVIYENEAALEALKKSKGRPENKPIPTMVSNFRQME---EIAYMSEDARKLAEEFM 87
Cdd:PRK10634  10 IAAAVDVLNEERVIAYPTEAVFGVGCDPDSETAVMRLLELKQRPVDKGLILIAANYEQLKpyiDDSMLTDAQRETIFSCW 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966361  88 PGGFTMILKKKEHLPAYLTNGFDTVGIRMPDDDIILHLIDLCEKPLLVTSANLSGEEPQETAEGVLKQLDGRIdAIVVGE 167
Cdd:PRK10634  90 PGPVTFVFPAPATTPRWLTGRFDSLAVRVTDHPLVVALCQAYGKPLVSTSANLSGLPPCRTVEEVRAQFGAAF-PVVPGE 168
                        170       180
                 ....*....|....*....|....
gi 495966361 168 SGGSK-ASTIVDMSTDELriVREG 190
Cdd:PRK10634 169 TGGRLnPSEIRDALTGEL--FRQG 190
PRK11630 PRK11630
threonylcarbamoyl-AMP synthase;
7-190 8.89e-24

threonylcarbamoyl-AMP synthase;


Pssm-ID: 183245  Cd Length: 206  Bit Score: 93.40  E-value: 8.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966361   7 EAKDIETIADLLKEGKVVAFPTDTVYGLAVIYENEAALEALKKSKGRPENKPIPTMVSNFRQMEEIAYMSEDARKLAEEF 86
Cdd:PRK11630  13 QQRLINQAVEIVRKGGVIVYPTDSGYALGCKIEDKNAMERICRIRQLPDGHNFTLMCRDLSELSTYSFVDNVAFRLMKNN 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966361  87 MPGGFTMILKKKEHLPAYLTN-GFDTVGIRMPDDDIILHLIDLCEKPLLVTSANLSGEEPQET-AEGVLKQLDGRIDAIV 164
Cdd:PRK11630  93 TPGNYTFILKGTKEVPRRLLQeKRKTIGLRVPSNPIALALLEALGEPMLSTSLMLPGSDFTESdPEEIKDRLEKQVDLII 172
                        170       180
                 ....*....|....*....|....*.
gi 495966361 165 VGESGGSKASTIVDMSTDELRIVREG 190
Cdd:PRK11630 173 HGGYLGQQPTTVIDLTDDTPVVVREG 198
HypF COG0068
Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, ...
11-165 2.10e-14

Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 439838 [Multi-domain]  Cd Length: 757  Bit Score: 70.91  E-value: 2.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966361  11 IETIADLLKEGKVVAfptdtVYG-----LAVIYENEAALEALKKSKGRPEnKPIPTMVSNFRQMEEIAYMSEDARKLaee 85
Cdd:COG0068  203 IAAAAELLRAGKIVA-----IKGlggfhLACDATNEEAVARLRRRKRRPA-KPFAVMARDLETARRLCEVSEAEEAL--- 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966361  86 fmpggFT------MILKKKEH--LPAYLTNGFDTVGIrM----PdddiiLH--LIDLCEKPLLVTSANLSGeEPQETAEG 151
Cdd:COG0068  274 -----LTsparpiVLLPKRPDspLAPSVAPGLDTLGV-MlpytP-----LHhlLLDELGRPLVMTSGNLSG-EPICIDNE 341
                        170
                 ....*....|....*
gi 495966361 152 -VLKQLDGRIDAIVV 165
Cdd:COG0068  342 eALERLSGIADYFLL 356
 
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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