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Conserved domains on  [gi|7106788|gb|AAF36119|]
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HSPC199 [Homo sapiens]

Protein Classification

Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatB( domain architecture ID 11481027)

Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatB is part of a heterotrimeric complex that forms correctly charged Gln-tRNA(Gln) or Asn-tRNA(Asn) through the transamidation of misacylated Glu-tRNA(Gln) or Asp-tRNA(Asn)

CATH:  1.10.150.380
EC:  6.3.5.-
Gene Ontology:  GO:0006412|GO:0016874|GO:0005524
SCOP:  4001495|4003972

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
gatB PRK05477
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatB;
62-420 6.59e-170

Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatB;


:

Pssm-ID: 235489 [Multi-domain]  Cd Length: 474  Bit Score: 484.57  E-value: 6.59e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788    62 KWAAVVGLEIHAQISSNSKLFSGSQVRFSAPPNSLVSFFDASLPGTLPVLNRRCVEAAVMTGLALNCHINKKSLFDRKHY 141
Cdd:PRK05477   4 NFEVVIGLEVHVQLNTKSKIFSGCSTDFGAEPNTNVCPVCLGLPGALPVLNKEAVEYAIKAGLALNCEIAKRSRFDRKNY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788   142 FYADLPAGYQITQQRLPIAVNGSLIYgvcagkkqsQVIPKTVRIKQIQLEQDSGKSLHDNLRSQTLIDLNRAGVGLLEVV 221
Cdd:PRK05477  84 FYPDLPKGYQISQYDEPIAENGYLEI---------ELGEKRIGIERIHLEEDAGKSVHDQGAGYSLVDYNRAGVPLIEIV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788   222 LEPDMSCGEEAATAVRELQLILQALGTSQANMAEGQLRVDANISVHHPG-EPLGVRTEVKNLNSIRFLAKAIDYEIQRQI 300
Cdd:PRK05477 155 SEPDMRSPEEARAYLKKLRSILRYLGISDGNMEEGSLRCDANVSVRPKGqEEFGTRVEIKNLNSFRFVEKAIEYEIERQI 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788   301 NELENGGEILNETRSFHHKLGCTMSMRDKEGKQDYRFMPEPNLPPLVLYDATslpagadpqqvinIDQIRETLPELPSVT 380
Cdd:PRK05477 235 EILESGGEVVQETRLFDEDKGETRSMRSKEEAHDYRYFPEPDLPPLEISDEW-------------IEEIRAELPELPDAK 301
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 7106788   381 REKLVQQYGMLLEHSFTLLNEVGLLEFFQNVIKETRADKK 420
Cdd:PRK05477 302 RARFVEEYGLSEYDARVLTSDKELADYFEAVVAAGADAKL 341
 
Name Accession Description Interval E-value
gatB PRK05477
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatB;
62-420 6.59e-170

Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatB;


Pssm-ID: 235489 [Multi-domain]  Cd Length: 474  Bit Score: 484.57  E-value: 6.59e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788    62 KWAAVVGLEIHAQISSNSKLFSGSQVRFSAPPNSLVSFFDASLPGTLPVLNRRCVEAAVMTGLALNCHINKKSLFDRKHY 141
Cdd:PRK05477   4 NFEVVIGLEVHVQLNTKSKIFSGCSTDFGAEPNTNVCPVCLGLPGALPVLNKEAVEYAIKAGLALNCEIAKRSRFDRKNY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788   142 FYADLPAGYQITQQRLPIAVNGSLIYgvcagkkqsQVIPKTVRIKQIQLEQDSGKSLHDNLRSQTLIDLNRAGVGLLEVV 221
Cdd:PRK05477  84 FYPDLPKGYQISQYDEPIAENGYLEI---------ELGEKRIGIERIHLEEDAGKSVHDQGAGYSLVDYNRAGVPLIEIV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788   222 LEPDMSCGEEAATAVRELQLILQALGTSQANMAEGQLRVDANISVHHPG-EPLGVRTEVKNLNSIRFLAKAIDYEIQRQI 300
Cdd:PRK05477 155 SEPDMRSPEEARAYLKKLRSILRYLGISDGNMEEGSLRCDANVSVRPKGqEEFGTRVEIKNLNSFRFVEKAIEYEIERQI 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788   301 NELENGGEILNETRSFHHKLGCTMSMRDKEGKQDYRFMPEPNLPPLVLYDATslpagadpqqvinIDQIRETLPELPSVT 380
Cdd:PRK05477 235 EILESGGEVVQETRLFDEDKGETRSMRSKEEAHDYRYFPEPDLPPLEISDEW-------------IEEIRAELPELPDAK 301
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 7106788   381 REKLVQQYGMLLEHSFTLLNEVGLLEFFQNVIKETRADKK 420
Cdd:PRK05477 302 RARFVEEYGLSEYDARVLTSDKELADYFEAVVAAGADAKL 341
GatB COG0064
Asp-tRNAAsn/Glu-tRNAGln amidotransferase B subunit [Translation, ribosomal structure and ...
62-420 6.70e-170

Asp-tRNAAsn/Glu-tRNAGln amidotransferase B subunit [Translation, ribosomal structure and biogenesis]; Asp-tRNAAsn/Glu-tRNAGln amidotransferase B subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439834 [Multi-domain]  Cd Length: 477  Bit Score: 484.53  E-value: 6.70e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788   62 KWAAVVGLEIHAQISSNSKLFSGSQVRFSAPPNSLVSFFDASLPGTLPVLNRRCVEAAVMTGLALNCHINKKSLFDRKHY 141
Cdd:COG0064   2 KYEVVIGLEVHVQLNTKSKIFCGCSTEFGAEPNTNVCPVCLGLPGALPVLNKKAVEYAIKAGLALNCEIAERSKFDRKNY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788  142 FYADLPAGYQITQQRLPIAVNGSLIYGVCAGKKqsqvipKTVRIKQIQLEQDSGKSLHDNLRSQTLIDLNRAGVGLLEVV 221
Cdd:COG0064  82 FYPDLPKGYQISQYDLPICEGGYLEIEVEDGEE------KRIGITRIHLEEDAGKSIHEGGAGYSLVDYNRAGVPLIEIV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788  222 LEPDMSCGEEAATAVRELQLILQALGTSQANMAEGQLRVDANISVHHPG-EPLGVRTEVKNLNSIRFLAKAIDYEIQRQI 300
Cdd:COG0064 156 SEPDMRSPEEARAYLEKLRSILRYLGVSDGNMEEGSLRCDANVSVRPKGsEELGTRVEIKNLNSFRFVERAIEYEIERQI 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788  301 NELENGGEILNETRSFHHKLGCTMSMRDKEGKQDYRFMPEPNLPPLVLYDATslpagadpqqvinIDQIRETLPELPSVT 380
Cdd:COG0064 236 ELLESGGKIVQETRLWDEDKGETRSMRSKEEAHDYRYFPEPDLPPLVISDEW-------------IEEIRATLPELPDAK 302
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 7106788  381 REKLVQQYGMLLEHSFTLLNEVGLLEFFQNVIKETrADKK 420
Cdd:COG0064 303 RERFVEEYGLSEYDARVLTSDKELADYFEAAVKAG-ADPK 341
GatB_N pfam02934
GatB/GatE catalytic domain; This domain is found in the GatB and GatE proteins.
65-348 9.12e-159

GatB/GatE catalytic domain; This domain is found in the GatB and GatE proteins.


Pssm-ID: 460754  Cd Length: 284  Bit Score: 448.76  E-value: 9.12e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788     65 AVVGLEIHAQISSNSKLFSGSQVRFSAPPNSLVSFFDASLPGTLPVLNRRCVEAAVMTGLALNCHINKKSLFDRKHYFYA 144
Cdd:pfam02934   1 LVIGLEIHVQLNTKTKLFCGCPTEFGAEPNTNVCPVDLGLPGTLPVLNKEAVELAIKAGLALNCEINDESKFDRKNYFYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788    145 DLPAGYQITQQRLPIAVNGSLIYGVCAGKkqsqvipKTVRIKQIQLEQDSGKSLHDNLRSQTLIDLNRAGVGLLEVVLEP 224
Cdd:pfam02934  81 DLPKGYQITQYDLPIAKGGYLEIEVEGGT-------KRIGITRIHLEEDAGKSIHDADSGYSLVDLNRAGVPLIEIVTEP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788    225 DMSCGEEAATAVRELQLILQALGTSQANMAEGQLRVDANISVHHPGE-PLGVRTEVKNLNSIRFLAKAIDYEIQRQINEL 303
Cdd:pfam02934 154 DIRSPEEARAYLKKLRSILRYLGVSDGNMEEGSLRCDVNVSVRPKGSeELGTRVEIKNLNSFRFVEKAIEYEIERQIELL 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 7106788    304 ENGGEILNETRSFHHKLGCTMSMRDKEGKQDYRFMPEPNLPPLVL 348
Cdd:pfam02934 234 ESGGKIRQETRGWDEDKGETRSMRSKEEAHDYRYFPEPDLPPIVI 278
gatB TIGR00133
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, B subunit; The heterotrimer GatABC is ...
64-413 1.22e-126

aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, B subunit; The heterotrimer GatABC is responsible for transferring the NH2 group that converts Glu to Gln, or Asp to Asn after the Glu or Asp has been ligated to the tRNA for Gln or Asn, respectively. In Lactobacillus, GatABC is responsible only for tRNA(Gln). In the Archaea, GatABC is responsible only for tRNA(Asn), while GatDE is responsible for tRNA(Gln). In lineages that include Thermus, Chlamydia, or Acidithiobacillus, the GatABC complex catalyzes both. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 272926 [Multi-domain]  Cd Length: 478  Bit Score: 374.44  E-value: 1.22e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788     64 AAVVGLEIHAQISSNSKLFSGSQVRF-SAPPNSLVSFFDASLPGTLPVLNRRCVEAAVMTGLALNCHINK-KSLFDRKHY 141
Cdd:TIGR00133   5 EAKIGLEIHVQLNTKTKLFCSCPNSFgSAPPNTNVCPVCLGLPGALPVLNEEAVKKAIKLALALNSQINQpISVFDRKHY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788    142 FYADLPAGYQITQQRLPIAVNGSLIYGVCAGkkqsqviPKTVRIKQIQLEQDSGKSLHDNLRSQTLIDLNRAGVGLLEVV 221
Cdd:TIGR00133  85 FYPDLPKGYQITQQDRPIAEGGKLEIELDGG-------EKRIGIERVHMEEDTGKSQHFGSDVQSLVDFNRSGAPLIEIV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788    222 LEPDMSCGEEAATAVRELQLILQALGTSQANMAEGQLRVDANISVHHPG-EPLGVRTEVKNLNSIRFLAKAIDYEIQRQI 300
Cdd:TIGR00133 158 TKPDINSPKEARAFLKKLRQILRYLGISDGNLEEGSMRCDVNVSIRLKGqEHLGTRVEIKNINSFKGIEKAIKYEIERQV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788    301 NELENGGEILNETRSFHHKLGCTMSMRDKEGKQDYRFMPEPNLPPLVLYDATslpagadpqqvinIDQIRETLPELPSVT 380
Cdd:TIGR00133 238 KALIRGEEVVQETRTFDEKSNITVSMRSKETSIDYRYFPEPDLPPINIDELL-------------VKEVAGKLPELPSAK 304
                         330       340       350
                  ....*....|....*....|....*....|...
gi 7106788    381 REKLVQQYGMLLEHSFTLLNEVGLLEFFQNVIK 413
Cdd:TIGR00133 305 RIRLKKEYGLSEQDAKVLTSDLTLADYFEEVVK 337
 
Name Accession Description Interval E-value
gatB PRK05477
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatB;
62-420 6.59e-170

Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatB;


Pssm-ID: 235489 [Multi-domain]  Cd Length: 474  Bit Score: 484.57  E-value: 6.59e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788    62 KWAAVVGLEIHAQISSNSKLFSGSQVRFSAPPNSLVSFFDASLPGTLPVLNRRCVEAAVMTGLALNCHINKKSLFDRKHY 141
Cdd:PRK05477   4 NFEVVIGLEVHVQLNTKSKIFSGCSTDFGAEPNTNVCPVCLGLPGALPVLNKEAVEYAIKAGLALNCEIAKRSRFDRKNY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788   142 FYADLPAGYQITQQRLPIAVNGSLIYgvcagkkqsQVIPKTVRIKQIQLEQDSGKSLHDNLRSQTLIDLNRAGVGLLEVV 221
Cdd:PRK05477  84 FYPDLPKGYQISQYDEPIAENGYLEI---------ELGEKRIGIERIHLEEDAGKSVHDQGAGYSLVDYNRAGVPLIEIV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788   222 LEPDMSCGEEAATAVRELQLILQALGTSQANMAEGQLRVDANISVHHPG-EPLGVRTEVKNLNSIRFLAKAIDYEIQRQI 300
Cdd:PRK05477 155 SEPDMRSPEEARAYLKKLRSILRYLGISDGNMEEGSLRCDANVSVRPKGqEEFGTRVEIKNLNSFRFVEKAIEYEIERQI 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788   301 NELENGGEILNETRSFHHKLGCTMSMRDKEGKQDYRFMPEPNLPPLVLYDATslpagadpqqvinIDQIRETLPELPSVT 380
Cdd:PRK05477 235 EILESGGEVVQETRLFDEDKGETRSMRSKEEAHDYRYFPEPDLPPLEISDEW-------------IEEIRAELPELPDAK 301
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 7106788   381 REKLVQQYGMLLEHSFTLLNEVGLLEFFQNVIKETRADKK 420
Cdd:PRK05477 302 RARFVEEYGLSEYDARVLTSDKELADYFEAVVAAGADAKL 341
GatB COG0064
Asp-tRNAAsn/Glu-tRNAGln amidotransferase B subunit [Translation, ribosomal structure and ...
62-420 6.70e-170

Asp-tRNAAsn/Glu-tRNAGln amidotransferase B subunit [Translation, ribosomal structure and biogenesis]; Asp-tRNAAsn/Glu-tRNAGln amidotransferase B subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439834 [Multi-domain]  Cd Length: 477  Bit Score: 484.53  E-value: 6.70e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788   62 KWAAVVGLEIHAQISSNSKLFSGSQVRFSAPPNSLVSFFDASLPGTLPVLNRRCVEAAVMTGLALNCHINKKSLFDRKHY 141
Cdd:COG0064   2 KYEVVIGLEVHVQLNTKSKIFCGCSTEFGAEPNTNVCPVCLGLPGALPVLNKKAVEYAIKAGLALNCEIAERSKFDRKNY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788  142 FYADLPAGYQITQQRLPIAVNGSLIYGVCAGKKqsqvipKTVRIKQIQLEQDSGKSLHDNLRSQTLIDLNRAGVGLLEVV 221
Cdd:COG0064  82 FYPDLPKGYQISQYDLPICEGGYLEIEVEDGEE------KRIGITRIHLEEDAGKSIHEGGAGYSLVDYNRAGVPLIEIV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788  222 LEPDMSCGEEAATAVRELQLILQALGTSQANMAEGQLRVDANISVHHPG-EPLGVRTEVKNLNSIRFLAKAIDYEIQRQI 300
Cdd:COG0064 156 SEPDMRSPEEARAYLEKLRSILRYLGVSDGNMEEGSLRCDANVSVRPKGsEELGTRVEIKNLNSFRFVERAIEYEIERQI 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788  301 NELENGGEILNETRSFHHKLGCTMSMRDKEGKQDYRFMPEPNLPPLVLYDATslpagadpqqvinIDQIRETLPELPSVT 380
Cdd:COG0064 236 ELLESGGKIVQETRLWDEDKGETRSMRSKEEAHDYRYFPEPDLPPLVISDEW-------------IEEIRATLPELPDAK 302
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 7106788  381 REKLVQQYGMLLEHSFTLLNEVGLLEFFQNVIKETrADKK 420
Cdd:COG0064 303 RERFVEEYGLSEYDARVLTSDKELADYFEAAVKAG-ADPK 341
GatB_N pfam02934
GatB/GatE catalytic domain; This domain is found in the GatB and GatE proteins.
65-348 9.12e-159

GatB/GatE catalytic domain; This domain is found in the GatB and GatE proteins.


Pssm-ID: 460754  Cd Length: 284  Bit Score: 448.76  E-value: 9.12e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788     65 AVVGLEIHAQISSNSKLFSGSQVRFSAPPNSLVSFFDASLPGTLPVLNRRCVEAAVMTGLALNCHINKKSLFDRKHYFYA 144
Cdd:pfam02934   1 LVIGLEIHVQLNTKTKLFCGCPTEFGAEPNTNVCPVDLGLPGTLPVLNKEAVELAIKAGLALNCEINDESKFDRKNYFYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788    145 DLPAGYQITQQRLPIAVNGSLIYGVCAGKkqsqvipKTVRIKQIQLEQDSGKSLHDNLRSQTLIDLNRAGVGLLEVVLEP 224
Cdd:pfam02934  81 DLPKGYQITQYDLPIAKGGYLEIEVEGGT-------KRIGITRIHLEEDAGKSIHDADSGYSLVDLNRAGVPLIEIVTEP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788    225 DMSCGEEAATAVRELQLILQALGTSQANMAEGQLRVDANISVHHPGE-PLGVRTEVKNLNSIRFLAKAIDYEIQRQINEL 303
Cdd:pfam02934 154 DIRSPEEARAYLKKLRSILRYLGVSDGNMEEGSLRCDVNVSVRPKGSeELGTRVEIKNLNSFRFVEKAIEYEIERQIELL 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 7106788    304 ENGGEILNETRSFHHKLGCTMSMRDKEGKQDYRFMPEPNLPPLVL 348
Cdd:pfam02934 234 ESGGKIRQETRGWDEDKGETRSMRSKEEAHDYRYFPEPDLPPIVI 278
gatB TIGR00133
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, B subunit; The heterotrimer GatABC is ...
64-413 1.22e-126

aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, B subunit; The heterotrimer GatABC is responsible for transferring the NH2 group that converts Glu to Gln, or Asp to Asn after the Glu or Asp has been ligated to the tRNA for Gln or Asn, respectively. In Lactobacillus, GatABC is responsible only for tRNA(Gln). In the Archaea, GatABC is responsible only for tRNA(Asn), while GatDE is responsible for tRNA(Gln). In lineages that include Thermus, Chlamydia, or Acidithiobacillus, the GatABC complex catalyzes both. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 272926 [Multi-domain]  Cd Length: 478  Bit Score: 374.44  E-value: 1.22e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788     64 AAVVGLEIHAQISSNSKLFSGSQVRF-SAPPNSLVSFFDASLPGTLPVLNRRCVEAAVMTGLALNCHINK-KSLFDRKHY 141
Cdd:TIGR00133   5 EAKIGLEIHVQLNTKTKLFCSCPNSFgSAPPNTNVCPVCLGLPGALPVLNEEAVKKAIKLALALNSQINQpISVFDRKHY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788    142 FYADLPAGYQITQQRLPIAVNGSLIYGVCAGkkqsqviPKTVRIKQIQLEQDSGKSLHDNLRSQTLIDLNRAGVGLLEVV 221
Cdd:TIGR00133  85 FYPDLPKGYQITQQDRPIAEGGKLEIELDGG-------EKRIGIERVHMEEDTGKSQHFGSDVQSLVDFNRSGAPLIEIV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788    222 LEPDMSCGEEAATAVRELQLILQALGTSQANMAEGQLRVDANISVHHPG-EPLGVRTEVKNLNSIRFLAKAIDYEIQRQI 300
Cdd:TIGR00133 158 TKPDINSPKEARAFLKKLRQILRYLGISDGNLEEGSMRCDVNVSIRLKGqEHLGTRVEIKNINSFKGIEKAIKYEIERQV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788    301 NELENGGEILNETRSFHHKLGCTMSMRDKEGKQDYRFMPEPNLPPLVLYDATslpagadpqqvinIDQIRETLPELPSVT 380
Cdd:TIGR00133 238 KALIRGEEVVQETRTFDEKSNITVSMRSKETSIDYRYFPEPDLPPINIDELL-------------VKEVAGKLPELPSAK 304
                         330       340       350
                  ....*....|....*....|....*....|...
gi 7106788    381 REKLVQQYGMLLEHSFTLLNEVGLLEFFQNVIK 413
Cdd:TIGR00133 305 RIRLKKEYGLSEQDAKVLTSDLTLADYFEEVVK 337
PLN02751 PLN02751
glutamyl-tRNA(Gln) amidotransferase
1-420 6.39e-98

glutamyl-tRNA(Gln) amidotransferase


Pssm-ID: 215400 [Multi-domain]  Cd Length: 544  Bit Score: 302.91  E-value: 6.39e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788     1 MAAPMLRwGCRGRrwAFARVDGGSCHRRGAPTGSTSNqiRGESSVAQQPLHTAQKTR---KGEHKWAAVVGLEIHAQISS 77
Cdd:PLN02751   1 MALTLLR-GVQTP--VPSRRGPRLFRRASSRFSVRAT--TATSAAAAESKQAPKKSEaldKIEQDFEAVIGIETHVQLST 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788    78 NSKLFSGSQVRFSAPPNSLVSFFDASLPGTLPVLNRRCVEAAVMTGLALNCHINKKSLFDRKHYFYADLPAGYQITQQRL 157
Cdd:PLN02751  76 LTKAFCSCPYNYGAEPNTTVCPVCMGLPGTLPVLNSKVVEKAVKLGLALNCKISLKSKFDRKQYFYPDLPKGYQISQFDI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788   158 PIAVNGSLiygvcagkkqSQVIP-------KTVRIKQIQLEQDSGKSLH----DNLRSQTLIDLNRAGVGLLEVVLEPDM 226
Cdd:PLN02751 156 PIAEGGYV----------DVDLPvefggghRRFGITRVHMEEDAGKLLHsgngSYSQGSALVDLNRAGVPLLEIVSEPDM 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788   227 SCGEEAATAVRELQLILQALGTSQANMAEGQLRVDANISVHHPG-EPLGVRTEVKNLNSIRFLAKAIDYEIQRQINELEN 305
Cdd:PLN02751 226 RTGIEAAEYGAELQRLVRYLGVSNGNMQEGSLRCDVNVSIRPVGqEEFGTKVEIKNMNSFSAMSRAIDFEISRQILLHRQ 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788   306 G--GEILNETRSFHHKLGCTMSMRDKEGKQDYRFMPEPNLPPLVLYDATslpagadpqqvinIDQIRETLPELPSVTREK 383
Cdd:PLN02751 306 GqgDEIVQETRLWDEGAQKTVTMRKKEGLADYRYFPEPDLPEVVLTEEY-------------VDSIRASMPELPEAKRRR 372
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 7106788   384 LvQQYGMLLEHSFTLLNEVGLLEFFQNVIkETRADKK 420
Cdd:PLN02751 373 Y-ENMGLSMQDVLFLANDKNVAEFFDATL-AKGADAK 407
GatE COG2511
Archaeal Glu-tRNAGln amidotransferase subunit E, contains GAD domain [Translation, ribosomal ...
181-304 4.47e-10

Archaeal Glu-tRNAGln amidotransferase subunit E, contains GAD domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442001 [Multi-domain]  Cd Length: 630  Bit Score: 61.35  E-value: 4.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788  181 KTVRIKQIQLEQDSGKSLHDNlRSQTLIDLNRAGVGLLEVVLEPDMSCGEEAATAVRELQLILQA-------LGTsqanm 253
Cdd:COG2511 150 GKVGIQTICLEEDAARKIEET-GDGVVYSLDRLGIPLVEIATAPDIRSPEQAREVALRIGMLLRStgkvkrgLGT----- 223
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 7106788  254 aegqLRVDANISVhhPGeplGVRTEVKNLNSIRFLAKAIDYEIQRQINELE 304
Cdd:COG2511 224 ----IRQDVNVSI--AG---GARVEIKGVQDLDLIPKIVEYEVKRQVNLLE 265
PRK04028 PRK04028
Glu-tRNA(Gln) amidotransferase subunit GatE;
181-304 7.74e-08

Glu-tRNA(Gln) amidotransferase subunit GatE;


Pssm-ID: 235205 [Multi-domain]  Cd Length: 630  Bit Score: 54.44  E-value: 7.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106788   181 KTVRIKQIQLEQDSGKSLHDNlRSQTLIDLNRAGVGLLEVVLEPDMSCGEEAATAVRELQLILQAlgTSQANMAEGQLRV 260
Cdd:PRK04028 150 GKVGIETICLEEDAARKIEEK-GDGVVYSLDRLGIPLIEISTAPDIHSPEQAKEVALKIGMLLRS--TGKVKRGLGTIRQ 226
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 7106788   261 DANISVHHpgeplGVRTEVKNLNSIRFLAKAIDYEIQRQINELE 304
Cdd:PRK04028 227 DVNVSIAG-----GARVEIKGVQKLDLIPKVVEYEVQRQLNLLK 265
 
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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