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Conserved domains on  [gi|488285414|ref|WP_002356622|]
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MULTISPECIES: L-threonylcarbamoyladenylate synthase [Enterococcus]

Protein Classification

L-threonylcarbamoyladenylate synthase( domain architecture ID 10000243)

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

Graphical summary

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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 ...
21-206 1.74e-94

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: 279.29  E-value: 1.74e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285414  21 GELVAFPTETVYGLGADALNEAAVKKVYQVKGRPSDNPLIVHVNNVEMVKKYVATLPEVATKLVSAFWPGPLTLIFNVpS 100
Cdd:COG0009   22 GGVVAYPTDTVYGLGCDALNKEAVERIFAIKGRPRDKPLIVLVADLSQLEEYAKEVPDAARRLAKAFWPGPLTLILPA-T 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285414 101 DTFSKTVTGGLETVAFRMPDNQATLALIEQANVPLVGPSANTSGKPSPTSAEHVYHDLQGKIAAILDDGPTQIGVESTVL 180
Cdd:COG0009  101 KEVPDLLTGGRDTVAVRVPDHPVALALLRALGPPLASTSANLSGEPPPTTAEEVREQLGDRVDLILDGGPCGVGVPSTIV 180
                        170       180
                 ....*....|....*....|....*.
gi 488285414 181 DLTaeDGVPVILRPGAITKEQLESII 206
Cdd:COG0009  181 DLT--GGEPEILRPGAIDVEELEEVL 204
Sua5_C pfam03481
Threonylcarbamoyl-AMP synthase, C-terminal domain; This domain can be found in the C terminus ...
198-333 2.81e-41

Threonylcarbamoyl-AMP synthase, C-terminal domain; This domain can be found in the C terminus of threonylcarbamoyl-AMP synthases, including Sua5 from Saccharomyces cerevisiae and YwlC from Bacillus subtilis. Threonylcarbamoyl-AMP synthase is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs that read codons beginning with adenine. This domain adopts the Rossmann fold and may be involved in GTP and/or tRNA binding based on structural similarity with both GTP and tRNA binding proteins.


:

Pssm-ID: 460941  Cd Length: 134  Bit Score: 140.53  E-value: 2.81e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285414  198 TKEQLESIIPQVKIDThliSETAAPKAPGMKYKHYSPDAEVWIISGQTAEWQAAI-QQAKEQQEKIGLFLSDEQAAQLDT 276
Cdd:pfam03481   1 TKEELEEVLGEVAVLE---KDGEAPKAPGMKYRHYAPKAPVILVEGDEEEVAALIlAEKKAQGKKVGVLATDETAPAYGA 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 488285414  277 ENafVYSYGA-ETVENATKELFAGLRALDEQGATTIFAQGFAETGLGTAYMNRLKKSA 333
Cdd:pfam03481  78 DL--VLSLGSrGDLEEAARNLFAALRELDELGVDLILVEGFPEEGLGLAIMNRLRKAA 133
 
Name Accession Description Interval E-value
TsaC COG0009
tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC [Translation, ribosomal ...
21-206 1.74e-94

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: 279.29  E-value: 1.74e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285414  21 GELVAFPTETVYGLGADALNEAAVKKVYQVKGRPSDNPLIVHVNNVEMVKKYVATLPEVATKLVSAFWPGPLTLIFNVpS 100
Cdd:COG0009   22 GGVVAYPTDTVYGLGCDALNKEAVERIFAIKGRPRDKPLIVLVADLSQLEEYAKEVPDAARRLAKAFWPGPLTLILPA-T 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285414 101 DTFSKTVTGGLETVAFRMPDNQATLALIEQANVPLVGPSANTSGKPSPTSAEHVYHDLQGKIAAILDDGPTQIGVESTVL 180
Cdd:COG0009  101 KEVPDLLTGGRDTVAVRVPDHPVALALLRALGPPLASTSANLSGEPPPTTAEEVREQLGDRVDLILDGGPCGVGVPSTIV 180
                        170       180
                 ....*....|....*....|....*.
gi 488285414 181 DLTaeDGVPVILRPGAITKEQLESII 206
Cdd:COG0009  181 DLT--GGEPEILRPGAIDVEELEEVL 204
Sua5_yciO_yrdC pfam01300
Telomere recombination; This domain has been shown to bind preferentially to dsRNA. The domain ...
21-193 1.53e-76

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: 232.79  E-value: 1.53e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285414   21 GELVAFPTETVYGLGADALNEAAVKKVYQVKGRPSDNPLIVHVNNVEMVKKYVATLPEVATKLVSAFWPGPLTLIFNVPS 100
Cdd:pfam01300   6 GGIVAYPTDTVYGLGCDATNEEAVERLYEIKGRPRDKPLAVMVADLEDLKEYAEEVEEAALRLAERFWPGPLTLVLKASK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285414  101 DTFSKTVTGGLETVAFRMPDNQATLALIEQANVPLVGPSANTSGKPSPTSAEHVYHDLQGKIAAILDDGPTQIGVESTVL 180
Cdd:pfam01300  86 KPLPKLLTPGLGTVGVRLPDHPLALLLLEALGEPLVATSANLSGEPSPTDAEEILEELGGRVDLILDGGRIAGGVPSTVV 165
                         170
                  ....*....|...
gi 488285414  181 DLTaeDGVPVILR 193
Cdd:pfam01300 166 DLT--GGPPRILR 176
TIGR00057 TIGR00057
tRNA threonylcarbamoyl adenosine modification protein, Sua5/YciO/YrdC/YwlC family; Has ...
21-200 1.81e-69

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: 215.65  E-value: 1.81e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285414   21 GELVAFPTETVYGLGADALNEAAVKKVYQVKGRPSDNPLIVHVNNVEMVKKYvATLPEVATKLVSAFWPGPLTLIFnVPS 100
Cdd:TIGR00057  21 GGIVVYPTDTVYGIGADALDEDAVRRLYRIKGRPSNKPLTVLVSDLSEIEKY-AYVPDDAKRLMKKFWPGPLTLVL-KKT 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285414  101 DTFSKTVTGGLETVAFRMPDNQATLALIEQANVPLVGPSANTSGKPSPTSAEHVYHDLQGKIAAILDDGPTQIGVESTVL 180
Cdd:TIGR00057  99 PEIPRRVSGKRKTIGIRVPDNPIALELLEELGKPIVATSANLSGKPSATDVEEAVDELGKLVDLIIDAGPCLGGEPSTII 178
                         170       180
                  ....*....|....*....|
gi 488285414  181 DLTaeDGVPVILRPGAITKE 200
Cdd:TIGR00057 179 DLT--DDTPKVLREGVGSEP 196
Sua5_C pfam03481
Threonylcarbamoyl-AMP synthase, C-terminal domain; This domain can be found in the C terminus ...
198-333 2.81e-41

Threonylcarbamoyl-AMP synthase, C-terminal domain; This domain can be found in the C terminus of threonylcarbamoyl-AMP synthases, including Sua5 from Saccharomyces cerevisiae and YwlC from Bacillus subtilis. Threonylcarbamoyl-AMP synthase is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs that read codons beginning with adenine. This domain adopts the Rossmann fold and may be involved in GTP and/or tRNA binding based on structural similarity with both GTP and tRNA binding proteins.


Pssm-ID: 460941  Cd Length: 134  Bit Score: 140.53  E-value: 2.81e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285414  198 TKEQLESIIPQVKIDThliSETAAPKAPGMKYKHYSPDAEVWIISGQTAEWQAAI-QQAKEQQEKIGLFLSDEQAAQLDT 276
Cdd:pfam03481   1 TKEELEEVLGEVAVLE---KDGEAPKAPGMKYRHYAPKAPVILVEGDEEEVAALIlAEKKAQGKKVGVLATDETAPAYGA 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 488285414  277 ENafVYSYGA-ETVENATKELFAGLRALDEQGATTIFAQGFAETGLGTAYMNRLKKSA 333
Cdd:pfam03481  78 DL--VLSLGSrGDLEEAARNLFAALRELDELGVDLILVEGFPEEGLGLAIMNRLRKAA 133
PRK10634 PRK10634
L-threonylcarbamoyladenylate synthase type 1 TsaC;
22-154 3.22e-23

L-threonylcarbamoyladenylate synthase type 1 TsaC;


Pssm-ID: 182603  Cd Length: 190  Bit Score: 94.79  E-value: 3.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285414  22 ELVAFPTETVYGLGADALNEAAVKKVYQVKGRPSDNPLIVHVNNVEMVKKYV--ATLPEVATKLVSAFWPGPLTLIFNVP 99
Cdd:PRK10634  21 RVIAYPTEAVFGVGCDPDSETAVMRLLELKQRPVDKGLILIAANYEQLKPYIddSMLTDAQRETIFSCWPGPVTFVFPAP 100
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488285414 100 SDTfSKTVTGGLETVAFRMPDNQATLALIEQANVPLVGPSANTSGKPSPTSAEHV 154
Cdd:PRK10634 101 ATT-PRWLTGRFDSLAVRVTDHPLVVALCQAYGKPLVSTSANLSGLPPCRTVEEV 154
 
Name Accession Description Interval E-value
TsaC COG0009
tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC [Translation, ribosomal ...
21-206 1.74e-94

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: 279.29  E-value: 1.74e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285414  21 GELVAFPTETVYGLGADALNEAAVKKVYQVKGRPSDNPLIVHVNNVEMVKKYVATLPEVATKLVSAFWPGPLTLIFNVpS 100
Cdd:COG0009   22 GGVVAYPTDTVYGLGCDALNKEAVERIFAIKGRPRDKPLIVLVADLSQLEEYAKEVPDAARRLAKAFWPGPLTLILPA-T 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285414 101 DTFSKTVTGGLETVAFRMPDNQATLALIEQANVPLVGPSANTSGKPSPTSAEHVYHDLQGKIAAILDDGPTQIGVESTVL 180
Cdd:COG0009  101 KEVPDLLTGGRDTVAVRVPDHPVALALLRALGPPLASTSANLSGEPPPTTAEEVREQLGDRVDLILDGGPCGVGVPSTIV 180
                        170       180
                 ....*....|....*....|....*.
gi 488285414 181 DLTaeDGVPVILRPGAITKEQLESII 206
Cdd:COG0009  181 DLT--GGEPEILRPGAIDVEELEEVL 204
Sua5_yciO_yrdC pfam01300
Telomere recombination; This domain has been shown to bind preferentially to dsRNA. The domain ...
21-193 1.53e-76

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: 232.79  E-value: 1.53e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285414   21 GELVAFPTETVYGLGADALNEAAVKKVYQVKGRPSDNPLIVHVNNVEMVKKYVATLPEVATKLVSAFWPGPLTLIFNVPS 100
Cdd:pfam01300   6 GGIVAYPTDTVYGLGCDATNEEAVERLYEIKGRPRDKPLAVMVADLEDLKEYAEEVEEAALRLAERFWPGPLTLVLKASK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285414  101 DTFSKTVTGGLETVAFRMPDNQATLALIEQANVPLVGPSANTSGKPSPTSAEHVYHDLQGKIAAILDDGPTQIGVESTVL 180
Cdd:pfam01300  86 KPLPKLLTPGLGTVGVRLPDHPLALLLLEALGEPLVATSANLSGEPSPTDAEEILEELGGRVDLILDGGRIAGGVPSTVV 165
                         170
                  ....*....|...
gi 488285414  181 DLTaeDGVPVILR 193
Cdd:pfam01300 166 DLT--GGPPRILR 176
TIGR00057 TIGR00057
tRNA threonylcarbamoyl adenosine modification protein, Sua5/YciO/YrdC/YwlC family; Has ...
21-200 1.81e-69

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: 215.65  E-value: 1.81e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285414   21 GELVAFPTETVYGLGADALNEAAVKKVYQVKGRPSDNPLIVHVNNVEMVKKYvATLPEVATKLVSAFWPGPLTLIFnVPS 100
Cdd:TIGR00057  21 GGIVVYPTDTVYGIGADALDEDAVRRLYRIKGRPSNKPLTVLVSDLSEIEKY-AYVPDDAKRLMKKFWPGPLTLVL-KKT 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285414  101 DTFSKTVTGGLETVAFRMPDNQATLALIEQANVPLVGPSANTSGKPSPTSAEHVYHDLQGKIAAILDDGPTQIGVESTVL 180
Cdd:TIGR00057  99 PEIPRRVSGKRKTIGIRVPDNPIALELLEELGKPIVATSANLSGKPSATDVEEAVDELGKLVDLIIDAGPCLGGEPSTII 178
                         170       180
                  ....*....|....*....|
gi 488285414  181 DLTaeDGVPVILRPGAITKE 200
Cdd:TIGR00057 179 DLT--DDTPKVLREGVGSEP 196
Sua5_C pfam03481
Threonylcarbamoyl-AMP synthase, C-terminal domain; This domain can be found in the C terminus ...
198-333 2.81e-41

Threonylcarbamoyl-AMP synthase, C-terminal domain; This domain can be found in the C terminus of threonylcarbamoyl-AMP synthases, including Sua5 from Saccharomyces cerevisiae and YwlC from Bacillus subtilis. Threonylcarbamoyl-AMP synthase is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs that read codons beginning with adenine. This domain adopts the Rossmann fold and may be involved in GTP and/or tRNA binding based on structural similarity with both GTP and tRNA binding proteins.


Pssm-ID: 460941  Cd Length: 134  Bit Score: 140.53  E-value: 2.81e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285414  198 TKEQLESIIPQVKIDThliSETAAPKAPGMKYKHYSPDAEVWIISGQTAEWQAAI-QQAKEQQEKIGLFLSDEQAAQLDT 276
Cdd:pfam03481   1 TKEELEEVLGEVAVLE---KDGEAPKAPGMKYRHYAPKAPVILVEGDEEEVAALIlAEKKAQGKKVGVLATDETAPAYGA 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 488285414  277 ENafVYSYGA-ETVENATKELFAGLRALDEQGATTIFAQGFAETGLGTAYMNRLKKSA 333
Cdd:pfam03481  78 DL--VLSLGSrGDLEEAARNLFAALRELDELGVDLILVEGFPEEGLGLAIMNRLRKAA 133
PRK10634 PRK10634
L-threonylcarbamoyladenylate synthase type 1 TsaC;
22-154 3.22e-23

L-threonylcarbamoyladenylate synthase type 1 TsaC;


Pssm-ID: 182603  Cd Length: 190  Bit Score: 94.79  E-value: 3.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285414  22 ELVAFPTETVYGLGADALNEAAVKKVYQVKGRPSDNPLIVHVNNVEMVKKYV--ATLPEVATKLVSAFWPGPLTLIFNVP 99
Cdd:PRK10634  21 RVIAYPTEAVFGVGCDPDSETAVMRLLELKQRPVDKGLILIAANYEQLKPYIddSMLTDAQRETIFSCWPGPVTFVFPAP 100
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488285414 100 SDTfSKTVTGGLETVAFRMPDNQATLALIEQANVPLVGPSANTSGKPSPTSAEHV 154
Cdd:PRK10634 101 ATT-PRWLTGRFDSLAVRVTDHPLVVALCQAYGKPLVSTSANLSGLPPCRTVEEV 154
PRK11630 PRK11630
threonylcarbamoyl-AMP synthase;
21-196 3.30e-09

threonylcarbamoyl-AMP synthase;


Pssm-ID: 183245  Cd Length: 206  Bit Score: 56.03  E-value: 3.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285414  21 GELVAFPTETVYGLGADALNEAAVKKVYQVKGRPSDNPLIVHVNNVEMVKKYvATLPEVATKLVSAFWPGPLTLIFNVPS 100
Cdd:PRK11630  27 GGVIVYPTDSGYALGCKIEDKNAMERICRIRQLPDGHNFTLMCRDLSELSTY-SFVDNVAFRLMKNNTPGNYTFILKGTK 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285414 101 DTFSKTVTGGLETVAFRMPDNQATLALIEQANVPLVGPSANTSGKPSPTSAEHVYHDLQGKIAAILDDGPTQIGVESTVL 180
Cdd:PRK11630 106 EVPRRLLQEKRKTIGLRVPSNPIALALLEALGEPMLSTSLMLPGSDFTESDPEEIKDRLEKQVDLIIHGGYLGQQPTTVI 185
                        170
                 ....*....|....*.
gi 488285414 181 DLTaeDGVPVILRPGA 196
Cdd:PRK11630 186 DLT--DDTPVVVREGV 199
HypF COG0068
Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, ...
21-146 9.15e-03

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


Pssm-ID: 439838 [Multi-domain]  Cd Length: 757  Bit Score: 37.78  E-value: 9.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285414  21 GELVAfptetVYGLG-----ADALNEAAVKKVYQVKGRPsDNPLIVHVNNVEMVKKYVATLPEVATKLVSafWPGPLTLI 95
Cdd:COG0068  213 GKIVA-----IKGLGgfhlaCDATNEEAVARLRRRKRRP-AKPFAVMARDLETARRLCEVSEAEEALLTS--PARPIVLL 284
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488285414  96 FNVPSDTFSKTVTGGLETVAFrMpdnqatLA-------LIEQANVPLVGPSANTSGKP 146
Cdd:COG0068  285 PKRPDSPLAPSVAPGLDTLGV-M------LPytplhhlLLDELGRPLVMTSGNLSGEP 335
 
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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