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Conserved domains on  [gi|499320929|ref|WP_011011421|]
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L-threonylcarbamoyladenylate synthase [Pyrococcus furiosus]

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 ...
1-208 6.10e-108

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: 313.57  E-value: 6.10e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499320929   1 MTIVInmrdRIDERKLRVAARLIREGKLVAFPTETVYGLGADALNEKAARRIFEAKGRPADNPLIVHIAEFSQVYELARE 80
Cdd:COG0009    1 MATIL----KIQPRLIEQAAEALRAGGVVAYPTDTVYGLGCDALNKEAVERIFAIKGRPRDKPLIVLVADLSQLEEYAKE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499320929  81 VPEEAKMLAKKFWPGPLTIVLPRREIVPDVTTGGLDTVAIRMPANEIALKLIKLSGRPIAAPSANISGKPSPTTAEHVAD 160
Cdd:COG0009   77 VPDAARRLAKAFWPGPLTLILPATKEVPDLLTGGRDTVAVRVPDHPVALALLRALGPPLASTSANLSGEPPPTTAEEVRE 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 499320929 161 DFYGKIECIIDGGETKIGVESTVIDLTEWPPVLLRPGGLPLEEIEKVI 208
Cdd:COG0009  157 QLGDRVDLILDGGPCGVGVPSTIVDLTGGEPEILRPGAIDVEELEEVL 204
Sua5_C pfam03481
Threonylcarbamoyl-AMP synthase, C-terminal domain; This domain can be found in the C terminus ...
201-334 2.75e-47

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: 156.32  E-value: 2.75e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499320929  201 LEEIEKVIGEVrihpAVFGKKVDVAKSPGMKYKHYAPDAEVIVVEGPKEKVKRKIAElvkEFKEKGKRVGVIGSES---- 276
Cdd:pfam03481   2 KEELEEVLGEV----AVLEKDGEAPKAPGMKYRHYAPKAPVILVEGDEEEVAALILA---EKKAQGKKVGVLATDEtapa 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499320929  277 YNADEFFYLG--ETVEEVARNLFKALRYMDKAKVDIVLAEGVEEKGLGLAVMNRLRKAAG 334
Cdd:pfam03481  75 YGADLVLSLGsrGDLEEAARNLFAALRELDELGVDLILVEGFPEEGLGLAIMNRLRKAAG 134
 
Name Accession Description Interval E-value
TsaC COG0009
tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC [Translation, ribosomal ...
1-208 6.10e-108

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: 313.57  E-value: 6.10e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499320929   1 MTIVInmrdRIDERKLRVAARLIREGKLVAFPTETVYGLGADALNEKAARRIFEAKGRPADNPLIVHIAEFSQVYELARE 80
Cdd:COG0009    1 MATIL----KIQPRLIEQAAEALRAGGVVAYPTDTVYGLGCDALNKEAVERIFAIKGRPRDKPLIVLVADLSQLEEYAKE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499320929  81 VPEEAKMLAKKFWPGPLTIVLPRREIVPDVTTGGLDTVAIRMPANEIALKLIKLSGRPIAAPSANISGKPSPTTAEHVAD 160
Cdd:COG0009   77 VPDAARRLAKAFWPGPLTLILPATKEVPDLLTGGRDTVAVRVPDHPVALALLRALGPPLASTSANLSGEPPPTTAEEVRE 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 499320929 161 DFYGKIECIIDGGETKIGVESTVIDLTEWPPVLLRPGGLPLEEIEKVI 208
Cdd:COG0009  157 QLGDRVDLILDGGPCGVGVPSTIVDLTGGEPEILRPGAIDVEELEEVL 204
TIGR00057 TIGR00057
tRNA threonylcarbamoyl adenosine modification protein, Sua5/YciO/YrdC/YwlC family; Has ...
7-208 2.43e-81

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: 245.70  E-value: 2.43e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499320929    7 MRDRIDERKLRVAARLIREGKLVAFPTETVYGLGADALNEKAARRIFEAKGRPADNPLIVHIAEFSQVYELAReVPEEAK 86
Cdd:TIGR00057   2 HPENPSQRGIEQAVKILRKGGIVVYPTDTVYGIGADALDEDAVRRLYRIKGRPSNKPLTVLVSDLSEIEKYAY-VPDDAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499320929   87 MLAKKFWPGPLTIVLPRREIVPDVTTGGLDTVAIRMPANEIALKLIKLSGRPIAAPSANISGKPSPTTAEHVADDFYGKI 166
Cdd:TIGR00057  81 RLMKKFWPGPLTLVLKKTPEIPRRVSGKRKTIGIRVPDNPIALELLEELGKPIVATSANLSGKPSATDVEEAVDELGKLV 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 499320929  167 ECIIDGGETKIGVESTVIDLTEWPPVLLRPGGLPlEEIEKVI 208
Cdd:TIGR00057 161 DLIIDAGPCLGGEPSTIIDLTDDTPKVLREGVGS-EPIEKVL 201
Sua5_yciO_yrdC pfam01300
Telomere recombination; This domain has been shown to bind preferentially to dsRNA. The domain ...
21-195 1.86e-79

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: 240.11  E-value: 1.86e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499320929   21 RLIREGKLVAFPTETVYGLGADALNEKAARRIFEAKGRPADNPLIVHIAEFSQVYELAREVPEEAKMLAKKFWPGPLTIV 100
Cdd:pfam01300   1 EALRKGGIVAYPTDTVYGLGCDATNEEAVERLYEIKGRPRDKPLAVMVADLEDLKEYAEEVEEAALRLAERFWPGPLTLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499320929  101 LPR-REIVPDVTTGGLDTVAIRMPANEIALKLIKLSGRPIAAPSANISGKPSPTTAEHVADDFYGKIECIIDGGETKIGV 179
Cdd:pfam01300  81 LKAsKKPLPKLLTPGLGTVGVRLPDHPLALLLLEALGEPLVATSANLSGEPSPTDAEEILEELGGRVDLILDGGRIAGGV 160
                         170
                  ....*....|....*.
gi 499320929  180 ESTVIDLTEWPPVLLR 195
Cdd:pfam01300 161 PSTVVDLTGGPPRILR 176
Sua5_C pfam03481
Threonylcarbamoyl-AMP synthase, C-terminal domain; This domain can be found in the C terminus ...
201-334 2.75e-47

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: 156.32  E-value: 2.75e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499320929  201 LEEIEKVIGEVrihpAVFGKKVDVAKSPGMKYKHYAPDAEVIVVEGPKEKVKRKIAElvkEFKEKGKRVGVIGSES---- 276
Cdd:pfam03481   2 KEELEEVLGEV----AVLEKDGEAPKAPGMKYRHYAPKAPVILVEGDEEEVAALILA---EKKAQGKKVGVLATDEtapa 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499320929  277 YNADEFFYLG--ETVEEVARNLFKALRYMDKAKVDIVLAEGVEEKGLGLAVMNRLRKAAG 334
Cdd:pfam03481  75 YGADLVLSLGsrGDLEEAARNLFAALRELDELGVDLILVEGFPEEGLGLAIMNRLRKAAG 134
PRK10634 PRK10634
L-threonylcarbamoyladenylate synthase type 1 TsaC;
19-162 7.93e-24

L-threonylcarbamoyladenylate synthase type 1 TsaC;


Pssm-ID: 182603  Cd Length: 190  Bit Score: 96.72  E-value: 7.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499320929  19 AARLIREGKLVAFPTETVYGLGADALNEKAARRIFEAKGRPADNPLIVHIAEFSQV--YELAREVPEEAKMLAKKFWPGP 96
Cdd:PRK10634  13 AVDVLNEERVIAYPTEAVFGVGCDPDSETAVMRLLELKQRPVDKGLILIAANYEQLkpYIDDSMLTDAQRETIFSCWPGP 92
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499320929  97 LTIVLPRREIVPDVTTGGLDTVAIRMPANEIALKLIKLSGRPIAAPSANISGKPSPTTAEHVADDF 162
Cdd:PRK10634  93 VTFVFPAPATTPRWLTGRFDSLAVRVTDHPLVVALCQAYGKPLVSTSANLSGLPPCRTVEEVRAQF 158
 
Name Accession Description Interval E-value
TsaC COG0009
tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC [Translation, ribosomal ...
1-208 6.10e-108

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: 313.57  E-value: 6.10e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499320929   1 MTIVInmrdRIDERKLRVAARLIREGKLVAFPTETVYGLGADALNEKAARRIFEAKGRPADNPLIVHIAEFSQVYELARE 80
Cdd:COG0009    1 MATIL----KIQPRLIEQAAEALRAGGVVAYPTDTVYGLGCDALNKEAVERIFAIKGRPRDKPLIVLVADLSQLEEYAKE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499320929  81 VPEEAKMLAKKFWPGPLTIVLPRREIVPDVTTGGLDTVAIRMPANEIALKLIKLSGRPIAAPSANISGKPSPTTAEHVAD 160
Cdd:COG0009   77 VPDAARRLAKAFWPGPLTLILPATKEVPDLLTGGRDTVAVRVPDHPVALALLRALGPPLASTSANLSGEPPPTTAEEVRE 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 499320929 161 DFYGKIECIIDGGETKIGVESTVIDLTEWPPVLLRPGGLPLEEIEKVI 208
Cdd:COG0009  157 QLGDRVDLILDGGPCGVGVPSTIVDLTGGEPEILRPGAIDVEELEEVL 204
TIGR00057 TIGR00057
tRNA threonylcarbamoyl adenosine modification protein, Sua5/YciO/YrdC/YwlC family; Has ...
7-208 2.43e-81

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: 245.70  E-value: 2.43e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499320929    7 MRDRIDERKLRVAARLIREGKLVAFPTETVYGLGADALNEKAARRIFEAKGRPADNPLIVHIAEFSQVYELAReVPEEAK 86
Cdd:TIGR00057   2 HPENPSQRGIEQAVKILRKGGIVVYPTDTVYGIGADALDEDAVRRLYRIKGRPSNKPLTVLVSDLSEIEKYAY-VPDDAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499320929   87 MLAKKFWPGPLTIVLPRREIVPDVTTGGLDTVAIRMPANEIALKLIKLSGRPIAAPSANISGKPSPTTAEHVADDFYGKI 166
Cdd:TIGR00057  81 RLMKKFWPGPLTLVLKKTPEIPRRVSGKRKTIGIRVPDNPIALELLEELGKPIVATSANLSGKPSATDVEEAVDELGKLV 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 499320929  167 ECIIDGGETKIGVESTVIDLTEWPPVLLRPGGLPlEEIEKVI 208
Cdd:TIGR00057 161 DLIIDAGPCLGGEPSTIIDLTDDTPKVLREGVGS-EPIEKVL 201
Sua5_yciO_yrdC pfam01300
Telomere recombination; This domain has been shown to bind preferentially to dsRNA. The domain ...
21-195 1.86e-79

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: 240.11  E-value: 1.86e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499320929   21 RLIREGKLVAFPTETVYGLGADALNEKAARRIFEAKGRPADNPLIVHIAEFSQVYELAREVPEEAKMLAKKFWPGPLTIV 100
Cdd:pfam01300   1 EALRKGGIVAYPTDTVYGLGCDATNEEAVERLYEIKGRPRDKPLAVMVADLEDLKEYAEEVEEAALRLAERFWPGPLTLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499320929  101 LPR-REIVPDVTTGGLDTVAIRMPANEIALKLIKLSGRPIAAPSANISGKPSPTTAEHVADDFYGKIECIIDGGETKIGV 179
Cdd:pfam01300  81 LKAsKKPLPKLLTPGLGTVGVRLPDHPLALLLLEALGEPLVATSANLSGEPSPTDAEEILEELGGRVDLILDGGRIAGGV 160
                         170
                  ....*....|....*.
gi 499320929  180 ESTVIDLTEWPPVLLR 195
Cdd:pfam01300 161 PSTVVDLTGGPPRILR 176
Sua5_C pfam03481
Threonylcarbamoyl-AMP synthase, C-terminal domain; This domain can be found in the C terminus ...
201-334 2.75e-47

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: 156.32  E-value: 2.75e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499320929  201 LEEIEKVIGEVrihpAVFGKKVDVAKSPGMKYKHYAPDAEVIVVEGPKEKVKRKIAElvkEFKEKGKRVGVIGSES---- 276
Cdd:pfam03481   2 KEELEEVLGEV----AVLEKDGEAPKAPGMKYRHYAPKAPVILVEGDEEEVAALILA---EKKAQGKKVGVLATDEtapa 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499320929  277 YNADEFFYLG--ETVEEVARNLFKALRYMDKAKVDIVLAEGVEEKGLGLAVMNRLRKAAG 334
Cdd:pfam03481  75 YGADLVLSLGsrGDLEEAARNLFAALRELDELGVDLILVEGFPEEGLGLAIMNRLRKAAG 134
PRK10634 PRK10634
L-threonylcarbamoyladenylate synthase type 1 TsaC;
19-162 7.93e-24

L-threonylcarbamoyladenylate synthase type 1 TsaC;


Pssm-ID: 182603  Cd Length: 190  Bit Score: 96.72  E-value: 7.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499320929  19 AARLIREGKLVAFPTETVYGLGADALNEKAARRIFEAKGRPADNPLIVHIAEFSQV--YELAREVPEEAKMLAKKFWPGP 96
Cdd:PRK10634  13 AVDVLNEERVIAYPTEAVFGVGCDPDSETAVMRLLELKQRPVDKGLILIAANYEQLkpYIDDSMLTDAQRETIFSCWPGP 92
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499320929  97 LTIVLPRREIVPDVTTGGLDTVAIRMPANEIALKLIKLSGRPIAAPSANISGKPSPTTAEHVADDF 162
Cdd:PRK10634  93 VTFVFPAPATTPRWLTGRFDSLAVRVTDHPLVVALCQAYGKPLVSTSANLSGLPPCRTVEEVRAQF 158
PRK11630 PRK11630
threonylcarbamoyl-AMP synthase;
9-197 4.59e-13

threonylcarbamoyl-AMP synthase;


Pssm-ID: 183245  Cd Length: 206  Bit Score: 67.20  E-value: 4.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499320929   9 DRIDERKLRVAARLIREGKLVAFPTETVYGLGADALNEKAARRIFEAKGRPADNPLIVHIAEFSQVYELArEVPEEAKML 88
Cdd:PRK11630  10 DNPQQRLINQAVEIVRKGGVIVYPTDSGYALGCKIEDKNAMERICRIRQLPDGHNFTLMCRDLSELSTYS-FVDNVAFRL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499320929  89 AKKFWPGPLTIVLPRREIVPD-VTTGGLDTVAIRMPANEIALKLIKLSGRPIAAPSANISGKP-SPTTAEHVADDFYGKI 166
Cdd:PRK11630  89 MKNNTPGNYTFILKGTKEVPRrLLQEKRKTIGLRVPSNPIALALLEALGEPMLSTSLMLPGSDfTESDPEEIKDRLEKQV 168
                        170       180       190
                 ....*....|....*....|....*....|..
gi 499320929 167 ECIIDGGetKIGVE-STVIDLTEWPPVLLRPG 197
Cdd:PRK11630 169 DLIIHGG--YLGQQpTTVIDLTDDTPVVVREG 198
HypF COG0068
Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, ...
16-150 1.16e-07

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


Pssm-ID: 439838 [Multi-domain]  Cd Length: 757  Bit Score: 53.19  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499320929  16 LRVAARLIREGKLVAfptetVYGLG-----ADALNEKAARRIFEAKGRPaDNPLIVHIAEFSQVYELAREVPEEAKML-- 88
Cdd:COG0068  203 IAAAAELLRAGKIVA-----IKGLGgfhlaCDATNEEAVARLRRRKRRP-AKPFAVMARDLETARRLCEVSEAEEALLts 276
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499320929  89 -AKkfwPgpltIVL-PRRE--IVPDVTTGGLDTVAIRMPANEIALKLIKLSGRPIAAPSANISGKP 150
Cdd:COG0068  277 pAR---P----IVLlPKRPdsPLAPSVAPGLDTLGVMLPYTPLHHLLLDELGRPLVMTSGNLSGEP 335
DUF6674 pfam20379
Family of unknown function (DUF6674); This family of proteins is functionally uncharacterized. ...
248-314 2.89e-03

Family of unknown function (DUF6674); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 259 and 297 amino acids in length. There are two conserved sequence motifs: AMKIP and SMN.


Pssm-ID: 466528 [Multi-domain]  Cd Length: 251  Bit Score: 38.74  E-value: 2.89e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499320929  248 KEKVKRKIAELVKEFKEKGKrvgvigSESYNADEFFYLGETVEEVARNLFKALRYMDK--AKVDIVLAE 314
Cdd:pfam20379  86 KDNIIEGAKNAVAAFKEKGK------SALNKVVEFLGIKPALEKIREGVEESIKSMDKtiAKIDAFGTE 148
 
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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