NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1631483904|gb|TJX70546|]
View 

threonylcarbamoyl-AMP synthase [Staphylococcus haemolyticus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
TsaC COG0009
tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC [Translation, ribosomal ...
20-214 1.52e-89

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: 266.96  E-value: 1.52e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904  20 ELENIKQVYNDGGLIAIPTETVYGLGADARNQYAVSNIYQAKGRPSDNPLIVHIHDKSQLDQIVSHLPEEAKCLMDEFWP 99
Cdd:COG0009    11 LIEQAAEALRAGGVVAYPTDTVYGLGCDALNKEAVERIFAIKGRPRDKPLIVLVADLSQLEEYAKEVPDAARRLAKAFWP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904 100 GPISFILPLRQGyLCEKVTGGLQSIAVRMPSHPIGRAILQYIDIPIAAPSANVSGRPSPTTFQHVFNDLNGKIDGIVNGD 179
Cdd:COG0009    91 GPLTLILPATKE-VPDLLTGGRDTVAVRVPDHPVALALLRALGPPLASTSANLSGEPPPTTAEEVREQLGDRVDLILDGG 169
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1631483904 180 QSEEGLESTVLDCTQFPFRIARPGSITQAMLNDVF 214
Cdd:COG0009   170 PCGVGVPSTIVDLTGGEPEILRPGAIDVEELEEVL 204
Sua5_C pfam03481
Threonylcarbamoyl-AMP synthase, C-terminal domain; This domain can be found in the C terminus ...
206-338 2.54e-24

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: 96.23  E-value: 2.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904 206 TQAMLNDVFpGSVEEYHYDvNSQPIAPGMKYKHYAPDTPVTMLMHLSKPIKTI------KEWSKTAFILP-ETLKQYAPS 278
Cdd:pfam03481   1 TKEELEEVL-GEVAVLEKD-GEAPKAPGMKYRHYAPKAPVILVEGDEEEVAALilaekkAQGKKVGVLATdETAPAYGAD 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904 279 DALFIKLCKDEKDIrqAnHNLYQILHSIDENpSIDQAYIYAFDKTDESEAIMNRIIKATG 338
Cdd:pfam03481  79 LVLSLGSRGDLEEA--A-RNLFAALRELDEL-GVDLILVEGFPEEGLGLAIMNRLRKAAG 134
 
Name Accession Description Interval E-value
TsaC COG0009
tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC [Translation, ribosomal ...
20-214 1.52e-89

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: 266.96  E-value: 1.52e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904  20 ELENIKQVYNDGGLIAIPTETVYGLGADARNQYAVSNIYQAKGRPSDNPLIVHIHDKSQLDQIVSHLPEEAKCLMDEFWP 99
Cdd:COG0009    11 LIEQAAEALRAGGVVAYPTDTVYGLGCDALNKEAVERIFAIKGRPRDKPLIVLVADLSQLEEYAKEVPDAARRLAKAFWP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904 100 GPISFILPLRQGyLCEKVTGGLQSIAVRMPSHPIGRAILQYIDIPIAAPSANVSGRPSPTTFQHVFNDLNGKIDGIVNGD 179
Cdd:COG0009    91 GPLTLILPATKE-VPDLLTGGRDTVAVRVPDHPVALALLRALGPPLASTSANLSGEPPPTTAEEVREQLGDRVDLILDGG 169
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1631483904 180 QSEEGLESTVLDCTQFPFRIARPGSITQAMLNDVF 214
Cdd:COG0009   170 PCGVGVPSTIVDLTGGEPEILRPGAIDVEELEEVL 204
Sua5_yciO_yrdC pfam01300
Telomere recombination; This domain has been shown to bind preferentially to dsRNA. The domain ...
29-201 3.73e-74

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: 226.62  E-value: 3.73e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904  29 NDGGLIAIPTETVYGLGADARNQYAVSNIYQAKGRPSDNPLIVHIHDKSQLDQIVSHLPEEAKCLMDEFWPGPISFILPL 108
Cdd:pfam01300   4 RKGGIVAYPTDTVYGLGCDATNEEAVERLYEIKGRPRDKPLAVMVADLEDLKEYAEEVEEAALRLAERFWPGPLTLVLKA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904 109 RQGYLCEKVTGGLQSIAVRMPSHPIGRAILQYIDIPIAAPSANVSGRPSPTTFQHVFNDLNGKIDGIVNGDQSEEGLEST 188
Cdd:pfam01300  84 SKKPLPKLLTPGLGTVGVRLPDHPLALLLLEALGEPLVATSANLSGEPSPTDAEEILEELGGRVDLILDGGRIAGGVPST 163
                         170
                  ....*....|...
gi 1631483904 189 VLDCTQFPFRIAR 201
Cdd:pfam01300 164 VVDLTGGPPRILR 176
TIGR00057 TIGR00057
tRNA threonylcarbamoyl adenosine modification protein, Sua5/YciO/YrdC/YwlC family; Has ...
21-206 2.63e-63

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: 199.86  E-value: 2.63e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904  21 LENIKQVYNDGGLIAIPTETVYGLGADARNQYAVSNIYQAKGRPSDNPLIVHIHDKSQLDQIvSHLPEEAKCLMDEFWPG 100
Cdd:TIGR00057  11 IEQAVKILRKGGIVVYPTDTVYGIGADALDEDAVRRLYRIKGRPSNKPLTVLVSDLSEIEKY-AYVPDDAKRLMKKFWPG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904 101 PISFILPlRQGYLCEKVTGGLQSIAVRMPSHPIGRAILQYIDIPIAAPSANVSGRPSPTTFQHVFNDLNGKIDGIVNGDQ 180
Cdd:TIGR00057  90 PLTLVLK-KTPEIPRRVSGKRKTIGIRVPDNPIALELLEELGKPIVATSANLSGKPSATDVEEAVDELGKLVDLIIDAGP 168
                         170       180
                  ....*....|....*....|....*.
gi 1631483904 181 SEEGLESTVLDCTQFPFRIARPGSIT 206
Cdd:TIGR00057 169 CLGGEPSTIIDLTDDTPKVLREGVGS 194
Sua5_C pfam03481
Threonylcarbamoyl-AMP synthase, C-terminal domain; This domain can be found in the C terminus ...
206-338 2.54e-24

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: 96.23  E-value: 2.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904 206 TQAMLNDVFpGSVEEYHYDvNSQPIAPGMKYKHYAPDTPVTMLMHLSKPIKTI------KEWSKTAFILP-ETLKQYAPS 278
Cdd:pfam03481   1 TKEELEEVL-GEVAVLEKD-GEAPKAPGMKYRHYAPKAPVILVEGDEEEVAALilaekkAQGKKVGVLATdETAPAYGAD 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904 279 DALFIKLCKDEKDIrqAnHNLYQILHSIDENpSIDQAYIYAFDKTDESEAIMNRIIKATG 338
Cdd:pfam03481  79 LVLSLGSRGDLEEA--A-RNLFAALRELDEL-GVDLILVEGFPEEGLGLAIMNRLRKAAG 134
PRK10634 PRK10634
L-threonylcarbamoyladenylate synthase type 1 TsaC;
19-177 1.32e-19

L-threonylcarbamoyladenylate synthase type 1 TsaC;


Pssm-ID: 182603  Cd Length: 190  Bit Score: 85.16  E-value: 1.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904  19 PELENIKQVYNDGGLIAIPTETVYGLGADARNQYAVSNIYQAKGRPSDNPLIVHIHDKSQLDQIV--SHLPEEAKCLMDE 96
Cdd:PRK10634    8 DAIAAAVDVLNEERVIAYPTEAVFGVGCDPDSETAVMRLLELKQRPVDKGLILIAANYEQLKPYIddSMLTDAQRETIFS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904  97 FWPGPISFILPLRQG---YLcekvTGGLQSIAVRMPSHPIGRAILQYIDIPIAAPSANVSGRPSPTTFQHV---FND--- 167
Cdd:PRK10634   88 CWPGPVTFVFPAPATtprWL----TGRFDSLAVRVTDHPLVVALCQAYGKPLVSTSANLSGLPPCRTVEEVraqFGAafp 163
                         170
                  ....*....|.
gi 1631483904 168 -LNGKIDGIVN 177
Cdd:PRK10634  164 vVPGETGGRLN 174
 
Name Accession Description Interval E-value
TsaC COG0009
tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC [Translation, ribosomal ...
20-214 1.52e-89

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: 266.96  E-value: 1.52e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904  20 ELENIKQVYNDGGLIAIPTETVYGLGADARNQYAVSNIYQAKGRPSDNPLIVHIHDKSQLDQIVSHLPEEAKCLMDEFWP 99
Cdd:COG0009    11 LIEQAAEALRAGGVVAYPTDTVYGLGCDALNKEAVERIFAIKGRPRDKPLIVLVADLSQLEEYAKEVPDAARRLAKAFWP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904 100 GPISFILPLRQGyLCEKVTGGLQSIAVRMPSHPIGRAILQYIDIPIAAPSANVSGRPSPTTFQHVFNDLNGKIDGIVNGD 179
Cdd:COG0009    91 GPLTLILPATKE-VPDLLTGGRDTVAVRVPDHPVALALLRALGPPLASTSANLSGEPPPTTAEEVREQLGDRVDLILDGG 169
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1631483904 180 QSEEGLESTVLDCTQFPFRIARPGSITQAMLNDVF 214
Cdd:COG0009   170 PCGVGVPSTIVDLTGGEPEILRPGAIDVEELEEVL 204
Sua5_yciO_yrdC pfam01300
Telomere recombination; This domain has been shown to bind preferentially to dsRNA. The domain ...
29-201 3.73e-74

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: 226.62  E-value: 3.73e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904  29 NDGGLIAIPTETVYGLGADARNQYAVSNIYQAKGRPSDNPLIVHIHDKSQLDQIVSHLPEEAKCLMDEFWPGPISFILPL 108
Cdd:pfam01300   4 RKGGIVAYPTDTVYGLGCDATNEEAVERLYEIKGRPRDKPLAVMVADLEDLKEYAEEVEEAALRLAERFWPGPLTLVLKA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904 109 RQGYLCEKVTGGLQSIAVRMPSHPIGRAILQYIDIPIAAPSANVSGRPSPTTFQHVFNDLNGKIDGIVNGDQSEEGLEST 188
Cdd:pfam01300  84 SKKPLPKLLTPGLGTVGVRLPDHPLALLLLEALGEPLVATSANLSGEPSPTDAEEILEELGGRVDLILDGGRIAGGVPST 163
                         170
                  ....*....|...
gi 1631483904 189 VLDCTQFPFRIAR 201
Cdd:pfam01300 164 VVDLTGGPPRILR 176
TIGR00057 TIGR00057
tRNA threonylcarbamoyl adenosine modification protein, Sua5/YciO/YrdC/YwlC family; Has ...
21-206 2.63e-63

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: 199.86  E-value: 2.63e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904  21 LENIKQVYNDGGLIAIPTETVYGLGADARNQYAVSNIYQAKGRPSDNPLIVHIHDKSQLDQIvSHLPEEAKCLMDEFWPG 100
Cdd:TIGR00057  11 IEQAVKILRKGGIVVYPTDTVYGIGADALDEDAVRRLYRIKGRPSNKPLTVLVSDLSEIEKY-AYVPDDAKRLMKKFWPG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904 101 PISFILPlRQGYLCEKVTGGLQSIAVRMPSHPIGRAILQYIDIPIAAPSANVSGRPSPTTFQHVFNDLNGKIDGIVNGDQ 180
Cdd:TIGR00057  90 PLTLVLK-KTPEIPRRVSGKRKTIGIRVPDNPIALELLEELGKPIVATSANLSGKPSATDVEEAVDELGKLVDLIIDAGP 168
                         170       180
                  ....*....|....*....|....*.
gi 1631483904 181 SEEGLESTVLDCTQFPFRIARPGSIT 206
Cdd:TIGR00057 169 CLGGEPSTIIDLTDDTPKVLREGVGS 194
Sua5_C pfam03481
Threonylcarbamoyl-AMP synthase, C-terminal domain; This domain can be found in the C terminus ...
206-338 2.54e-24

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: 96.23  E-value: 2.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904 206 TQAMLNDVFpGSVEEYHYDvNSQPIAPGMKYKHYAPDTPVTMLMHLSKPIKTI------KEWSKTAFILP-ETLKQYAPS 278
Cdd:pfam03481   1 TKEELEEVL-GEVAVLEKD-GEAPKAPGMKYRHYAPKAPVILVEGDEEEVAALilaekkAQGKKVGVLATdETAPAYGAD 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904 279 DALFIKLCKDEKDIrqAnHNLYQILHSIDENpSIDQAYIYAFDKTDESEAIMNRIIKATG 338
Cdd:pfam03481  79 LVLSLGSRGDLEEA--A-RNLFAALRELDEL-GVDLILVEGFPEEGLGLAIMNRLRKAAG 134
PRK10634 PRK10634
L-threonylcarbamoyladenylate synthase type 1 TsaC;
19-177 1.32e-19

L-threonylcarbamoyladenylate synthase type 1 TsaC;


Pssm-ID: 182603  Cd Length: 190  Bit Score: 85.16  E-value: 1.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904  19 PELENIKQVYNDGGLIAIPTETVYGLGADARNQYAVSNIYQAKGRPSDNPLIVHIHDKSQLDQIV--SHLPEEAKCLMDE 96
Cdd:PRK10634    8 DAIAAAVDVLNEERVIAYPTEAVFGVGCDPDSETAVMRLLELKQRPVDKGLILIAANYEQLKPYIddSMLTDAQRETIFS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904  97 FWPGPISFILPLRQG---YLcekvTGGLQSIAVRMPSHPIGRAILQYIDIPIAAPSANVSGRPSPTTFQHV---FND--- 167
Cdd:PRK10634   88 CWPGPVTFVFPAPATtprWL----TGRFDSLAVRVTDHPLVVALCQAYGKPLVSTSANLSGLPPCRTVEEVraqFGAafp 163
                         170
                  ....*....|.
gi 1631483904 168 -LNGKIDGIVN 177
Cdd:PRK10634  164 vVPGETGGRLN 174
PRK11630 PRK11630
threonylcarbamoyl-AMP synthase;
17-203 1.82e-06

threonylcarbamoyl-AMP synthase;


Pssm-ID: 183245  Cd Length: 206  Bit Score: 47.94  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904  17 DYPELENIKQ---VYNDGGLIAIPTETVYGLGADARNQYAVSNIYQAKGRPSDNPLIVHIHDKSQLdQIVSHLPEEAKCL 93
Cdd:PRK11630   10 DNPQQRLINQaveIVRKGGVIVYPTDSGYALGCKIEDKNAMERICRIRQLPDGHNFTLMCRDLSEL-STYSFVDNVAFRL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904  94 MDEFWPGPISFILPLRQGYLCEKVTGGLQSIAVRMPSHPIGRAILQYIDIPIAAPSANVSGRP-SPTTFQHVFNDLNGKI 172
Cdd:PRK11630   89 MKNNTPGNYTFILKGTKEVPRRLLQEKRKTIGLRVPSNPIALALLEALGEPMLSTSLMLPGSDfTESDPEEIKDRLEKQV 168
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1631483904 173 DGIVNGDQSEEGlESTVLDCTQFPFRIARPG 203
Cdd:PRK11630  169 DLIIHGGYLGQQ-PTTVIDLTDDTPVVVREG 198
HypF COG0068
Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, ...
30-176 1.32e-04

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


Pssm-ID: 439838 [Multi-domain]  Cd Length: 757  Bit Score: 43.94  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631483904  30 DGGLIAIPtetvyGLG-----ADARNQYAVSNIYQAKGRPsDNPLIVHIHDKSQLDQIVSHLPEEAKCLMDefWPGPIsF 104
Cdd:COG0068   212 AGKIVAIK-----GLGgfhlaCDATNEEAVARLRRRKRRP-AKPFAVMARDLETARRLCEVSEAEEALLTS--PARPI-V 282
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1631483904 105 ILPLRQGY-LCEKVTGGLQSIAVRMPSHPIGRAILQYIDIPIAAPSANVSGRPSPTTFQHVFNDLNGKIDGIV 176
Cdd:COG0068   283 LLPKRPDSpLAPSVAPGLDTLGVMLPYTPLHHLLLDELGRPLVMTSGNLSGEPICIDNEEALERLSGIADYFL 355
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH