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Conserved domains on  [gi|486201804|ref|WP_001549989|]
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MULTISPECIES: tRNA glutamyl-Q(34) synthetase GluQRS [Salmonella]

Protein Classification

glutamyl-Q tRNA(Asp) synthetase( domain architecture ID 10012531)

glutamyl-Q tRNA(Asp) synthetase catalyzes the tRNA-independent activation of glutamate in the presence of ATP and the subsequent transfer of glutamate onto tRNA(Asp)

EC:  6.1.1.-
Gene Ontology:  GO:0004812|GO:0005524|GO:0006400|GO:0006424|GO:0008270

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05710 PRK05710
tRNA glutamyl-Q(34) synthetase GluQRS;
1-293 3.83e-162

tRNA glutamyl-Q(34) synthetase GluQRS;


:

Pssm-ID: 235573  Cd Length: 299  Bit Score: 452.77  E-value: 3.83e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804   1 MTDSHYIGRFAPSPSGELHFGSLIAALGSYLQARAQRGIWRVRIEDIDPPREVPGAAATILRQLEHYGLHWDGEVLWQSQ 80
Cdd:PRK05710   1 MTMTPYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804  81 RHEAYREALAWLHEQGLSYYCTCPRSRIQRL-------GGIYDGHCRTLYHGPENA-AVRIKQQHPVMRFHDALRGDIQA 152
Cdd:PRK05710  81 RHDAYRAALDRLRAQGLVYPCFCSRKEIAAAapappdgGGIYPGTCRDLLHGPRNPpAWRLRVPDAVIAFDDRLQGRQHQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804 153 DPQLASEDFIIHRRDGLFAYNLAVVVDDHFQGVTEIVRGADLIEPTVRQLSLYKQFGWRAPGYVHLPLALNEQGAKLSKQ 232
Cdd:PRK05710 161 DLALAVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRYLHLPLVLNADGQKLSKQ 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 486201804 233 NHAPALATGDPRPVLVQALRFLGQRDVVAWQEMSVEEllRFAVEHWRLAAVPTSANVNPAF 293
Cdd:PRK05710 241 NGAPALDAAGPLPVLAAALRFLGQPPPAADASVEELL--AQAVAHWDLTRLPRQAEINPAF 299
 
Name Accession Description Interval E-value
PRK05710 PRK05710
tRNA glutamyl-Q(34) synthetase GluQRS;
1-293 3.83e-162

tRNA glutamyl-Q(34) synthetase GluQRS;


Pssm-ID: 235573  Cd Length: 299  Bit Score: 452.77  E-value: 3.83e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804   1 MTDSHYIGRFAPSPSGELHFGSLIAALGSYLQARAQRGIWRVRIEDIDPPREVPGAAATILRQLEHYGLHWDGEVLWQSQ 80
Cdd:PRK05710   1 MTMTPYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804  81 RHEAYREALAWLHEQGLSYYCTCPRSRIQRL-------GGIYDGHCRTLYHGPENA-AVRIKQQHPVMRFHDALRGDIQA 152
Cdd:PRK05710  81 RHDAYRAALDRLRAQGLVYPCFCSRKEIAAAapappdgGGIYPGTCRDLLHGPRNPpAWRLRVPDAVIAFDDRLQGRQHQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804 153 DPQLASEDFIIHRRDGLFAYNLAVVVDDHFQGVTEIVRGADLIEPTVRQLSLYKQFGWRAPGYVHLPLALNEQGAKLSKQ 232
Cdd:PRK05710 161 DLALAVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRYLHLPLVLNADGQKLSKQ 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 486201804 233 NHAPALATGDPRPVLVQALRFLGQRDVVAWQEMSVEEllRFAVEHWRLAAVPTSANVNPAF 293
Cdd:PRK05710 241 NGAPALDAAGPLPVLAAALRFLGQPPPAADASVEELL--AQAVAHWDLTRLPRQAEINPAF 299
queuosine_YadB TIGR03838
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ...
 6-271 2.53e-151

glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ligase, but its purpose is to modify tRNA(Asp) at a queuosine position in the anticodon rather than to charge a tRNA with its cognate amino acid. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274810  Cd Length: 271  Bit Score: 424.26  E-value: 2.53e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804    6 YIGRFAPSPSGELHFGSLIAALGSYLQARAQRGIWRVRIEDIDPPREVPGAAATILRQLEHYGLHWDGEVLWQSQRHEAY 85
Cdd:TIGR03838   1 YRGRFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGEVVYQSQRHALY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804   86 REALAWLHEQGLSYYCTCPRSRIQR---LGGIYDGHCRTLYHG--PENAAVRIKQQHPVMRFHDALRGDIQADPQLASED 160
Cdd:TIGR03838  81 QAALDRLLAAGLAYPCQCTRKEIAAardGGGIYPGTCRNGLPGrpGRPAAWRLRVPDGVIAFDDRLQGPQQQDLAAAVGD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804  161 FIIHRRDGLFAYNLAVVVDDHFQGVTEIVRGADLIEPTVRQLSLYKQFGWRAPGYVHLPLALNEQGAKLSKQNHAPALAT 240
Cdd:TIGR03838 161 FVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHLPLVVNADGEKLSKQNGAPALDD 240

                         250       260       270
                  ....*....|....*....|....*....|.
gi 486201804  241 GDPRPVLVQALRFLGQRDVVAWQEMSVEELL 271
Cdd:TIGR03838 241 SRPLPALLAALRFLGLPPPPELAAASPAELL 271
GlnS COG0008
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 9-231 4.52e-61

Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 439779 [Multi-domain]  Cd Length: 467  Bit Score: 200.79  E-value: 4.52e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804   9 RFAPSPSGELHFGSLIAALGSYLQARAQRGIWRVRIEDIDPPREVPGAAATILRQLEHYGLHWDGEVLWQSQRHEAYREA 88
Cdd:COG0008    8 RFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFDIYYEY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804  89 LAWLHEQGLSYYCTCPRSRIQRLGG---------IYDGHCRTL---------YHGpENAAVRIKQQHPVMRFHDALRGDI 150
Cdd:COG0008   88 AEKLIEKGKAYVCFCTPEELEALREtqtapgkppRYDGRCRDLspeelermlAAG-EPPVLRFKIPEEGVVFDDLVRGEI 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804 151 QAD-PQLasEDFIIHRRDGLFAYNLAVVVDDHFQGVTEIVRGADLIEPTVRQLSLYKQFGWRAPGYVHLPLALNEQGAKL 229
Cdd:COG0008  167 TFPnPNL--RDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPLILGPDGTKL 244


                 ..
gi 486201804 230 SK 231
Cdd:COG0008  245 SK 246
tRNA-synt_1c pfam00749
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ...
 9-273 3.91e-54

tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).


Pssm-ID: 395606 [Multi-domain]  Cd Length: 314  Bit Score: 178.67  E-value: 3.91e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804    9 RFAPSPSGELHFGSLIAALGSYLQARAQRGIWRVRIEDIDPPREVPGAAATILRQLEHYGLHWDGEVLWQSQRHEAYREA 88
Cdd:pfam00749   5 RFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIYYKY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804   89 LAWLHEQGLSYYCTCPRSRIQRLGGI-----------YDGHCRTLYH--------GPENAAVRIKQQHP-VMRFHDALRG 148
Cdd:pfam00749  85 AEELIKKGKAYVCFCTPEELEEEREEqealgspsrdrYDEENLHLFEeemkkgsaEGGPATVRAKIPMEsPYVFRDPVRG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804  149 DIQADPQlASEDFIIHRRDGLFAYNLAVVVDDHFQGVTEIVRGADLIEPTVRQLSLYKQFGWRAPGYVHLPLALNEQGAK 228
Cdd:pfam00749 165 RIKFTPQ-EIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNLDGTK 243

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 486201804  229 LSKQnHAPALAT-------GDPRPVLVQALRFLGqrdvvawqeMSVEELLRF 273
Cdd:pfam00749 244 LSKR-KLSWSVDisqvkgwGDPREATLNGLRRRG---------WTPEGIREF 285
GluRS_core cd00808
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ...
 9-231 1.62e-41

catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA synthetase (GluRS) catalytic core domain . The discriminating form of GluRS is only found in bacteria and cellular organelles. GluRS is a monomer that attaches Glu to the appropriate tRNA. Like other class I tRNA synthetases, GluRS aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.


Pssm-ID: 173905 [Multi-domain]  Cd Length: 239  Bit Score: 143.50  E-value: 1.62e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804   9 RFAPSPSGELHFGSLIAALGSYLQARAQRGIWRVRIEDIDPPREVPGAAATILRQLEHYGLHWDGEVLW--------QSQ 80
Cdd:cd00808    5 RFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVggpygpyrQSE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804  81 RHEAYREALAWLHEQGlsyyctcprsriqrlggiydghcrtlyhgpenaavrikqqhpvmrfhdalrgdiqadpqlased 160
Cdd:cd00808   85 RLEIYRKYAEKLLEKG---------------------------------------------------------------- 100

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 486201804 161 fiihrrDGLFAYNLAVVVDDHFQGVTEIVRGADLIEPTVRQLSLYKQFGWRAPGYVHLPLALNEQGAKLSK 231
Cdd:cd00808  101 ------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLPLILNPDGKKLSK 165
 
Name Accession Description Interval E-value
PRK05710 PRK05710
tRNA glutamyl-Q(34) synthetase GluQRS;
1-293 3.83e-162

tRNA glutamyl-Q(34) synthetase GluQRS;


Pssm-ID: 235573  Cd Length: 299  Bit Score: 452.77  E-value: 3.83e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804   1 MTDSHYIGRFAPSPSGELHFGSLIAALGSYLQARAQRGIWRVRIEDIDPPREVPGAAATILRQLEHYGLHWDGEVLWQSQ 80
Cdd:PRK05710   1 MTMTPYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804  81 RHEAYREALAWLHEQGLSYYCTCPRSRIQRL-------GGIYDGHCRTLYHGPENA-AVRIKQQHPVMRFHDALRGDIQA 152
Cdd:PRK05710  81 RHDAYRAALDRLRAQGLVYPCFCSRKEIAAAapappdgGGIYPGTCRDLLHGPRNPpAWRLRVPDAVIAFDDRLQGRQHQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804 153 DPQLASEDFIIHRRDGLFAYNLAVVVDDHFQGVTEIVRGADLIEPTVRQLSLYKQFGWRAPGYVHLPLALNEQGAKLSKQ 232
Cdd:PRK05710 161 DLALAVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRYLHLPLVLNADGQKLSKQ 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 486201804 233 NHAPALATGDPRPVLVQALRFLGQRDVVAWQEMSVEEllRFAVEHWRLAAVPTSANVNPAF 293
Cdd:PRK05710 241 NGAPALDAAGPLPVLAAALRFLGQPPPAADASVEELL--AQAVAHWDLTRLPRQAEINPAF 299
queuosine_YadB TIGR03838
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ...
 6-271 2.53e-151

glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ligase, but its purpose is to modify tRNA(Asp) at a queuosine position in the anticodon rather than to charge a tRNA with its cognate amino acid. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274810  Cd Length: 271  Bit Score: 424.26  E-value: 2.53e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804    6 YIGRFAPSPSGELHFGSLIAALGSYLQARAQRGIWRVRIEDIDPPREVPGAAATILRQLEHYGLHWDGEVLWQSQRHEAY 85
Cdd:TIGR03838   1 YRGRFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGEVVYQSQRHALY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804   86 REALAWLHEQGLSYYCTCPRSRIQR---LGGIYDGHCRTLYHG--PENAAVRIKQQHPVMRFHDALRGDIQADPQLASED 160
Cdd:TIGR03838  81 QAALDRLLAAGLAYPCQCTRKEIAAardGGGIYPGTCRNGLPGrpGRPAAWRLRVPDGVIAFDDRLQGPQQQDLAAAVGD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804  161 FIIHRRDGLFAYNLAVVVDDHFQGVTEIVRGADLIEPTVRQLSLYKQFGWRAPGYVHLPLALNEQGAKLSKQNHAPALAT 240
Cdd:TIGR03838 161 FVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHLPLVVNADGEKLSKQNGAPALDD 240

                         250       260       270
                  ....*....|....*....|....*....|.
gi 486201804  241 GDPRPVLVQALRFLGQRDVVAWQEMSVEELL 271
Cdd:TIGR03838 241 SRPLPALLAALRFLGLPPPPELAAASPAELL 271
gltX_bact TIGR00464
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ...
 9-235 3.42e-66

glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the bacterial and mitochondrial forms of the enzyme. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases may act on both tRNA(gln) and tRNA(glu). This model is highly specific. Proteins with positive scores below the trusted cutoff may be fragments rather than full-length sequences. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273092 [Multi-domain]  Cd Length: 470  Bit Score: 214.14  E-value: 3.42e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804    9 RFAPSPSGELHFGSLIAALGSYLQARAQRGIWRVRIEDIDPPREVPGAAATILRQLEHYGLHWDGEVLWQSQRHEAYREA 88
Cdd:TIGR00464   5 RFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGPYYQSQRLDIYKKY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804   89 LAWLHEQGLSYYCTCPRSRIQRLGGI---------YDGHCRTLyHGPENAAVRIKQQHPVMR----------FHDALRGD 149
Cdd:TIGR00464  85 AKELLEEGLAYRCYCSKERLERLREEqkanketprYDGRCRNL-HEEEIENKLAKGIPPVVRfkipqeavvsFNDQVRGE 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804  150 IQADPQlASEDFIIHRRDGLFAYNLAVVVDDHFQGVTEIVRGADLIEPTVRQLSLYKQFGWRAPGYVHLPLALNEQGAKL 229
Cdd:TIGR00464 164 ITFQNS-ELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLPMILDEDGKKL 242


                  ....*.
gi 486201804  230 SKQNHA 235
Cdd:TIGR00464 243 SKRDGA 248
GlnS COG0008
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 9-231 4.52e-61

Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 439779 [Multi-domain]  Cd Length: 467  Bit Score: 200.79  E-value: 4.52e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804   9 RFAPSPSGELHFGSLIAALGSYLQARAQRGIWRVRIEDIDPPREVPGAAATILRQLEHYGLHWDGEVLWQSQRHEAYREA 88
Cdd:COG0008    8 RFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFDIYYEY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804  89 LAWLHEQGLSYYCTCPRSRIQRLGG---------IYDGHCRTL---------YHGpENAAVRIKQQHPVMRFHDALRGDI 150
Cdd:COG0008   88 AEKLIEKGKAYVCFCTPEELEALREtqtapgkppRYDGRCRDLspeelermlAAG-EPPVLRFKIPEEGVVFDDLVRGEI 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804 151 QAD-PQLasEDFIIHRRDGLFAYNLAVVVDDHFQGVTEIVRGADLIEPTVRQLSLYKQFGWRAPGYVHLPLALNEQGAKL 229
Cdd:COG0008  167 TFPnPNL--RDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPLILGPDGTKL 244


                 ..
gi 486201804 230 SK 231
Cdd:COG0008  245 SK 246
tRNA-synt_1c pfam00749
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ...
 9-273 3.91e-54

tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).


Pssm-ID: 395606 [Multi-domain]  Cd Length: 314  Bit Score: 178.67  E-value: 3.91e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804    9 RFAPSPSGELHFGSLIAALGSYLQARAQRGIWRVRIEDIDPPREVPGAAATILRQLEHYGLHWDGEVLWQSQRHEAYREA 88
Cdd:pfam00749   5 RFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIYYKY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804   89 LAWLHEQGLSYYCTCPRSRIQRLGGI-----------YDGHCRTLYH--------GPENAAVRIKQQHP-VMRFHDALRG 148
Cdd:pfam00749  85 AEELIKKGKAYVCFCTPEELEEEREEqealgspsrdrYDEENLHLFEeemkkgsaEGGPATVRAKIPMEsPYVFRDPVRG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804  149 DIQADPQlASEDFIIHRRDGLFAYNLAVVVDDHFQGVTEIVRGADLIEPTVRQLSLYKQFGWRAPGYVHLPLALNEQGAK 228
Cdd:pfam00749 165 RIKFTPQ-EIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNLDGTK 243

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 486201804  229 LSKQnHAPALAT-------GDPRPVLVQALRFLGqrdvvawqeMSVEELLRF 273
Cdd:pfam00749 244 LSKR-KLSWSVDisqvkgwGDPREATLNGLRRRG---------WTPEGIREF 285
GluRS_core cd00808
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ...
 9-231 1.62e-41

catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA synthetase (GluRS) catalytic core domain . The discriminating form of GluRS is only found in bacteria and cellular organelles. GluRS is a monomer that attaches Glu to the appropriate tRNA. Like other class I tRNA synthetases, GluRS aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.


Pssm-ID: 173905 [Multi-domain]  Cd Length: 239  Bit Score: 143.50  E-value: 1.62e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804   9 RFAPSPSGELHFGSLIAALGSYLQARAQRGIWRVRIEDIDPPREVPGAAATILRQLEHYGLHWDGEVLW--------QSQ 80
Cdd:cd00808    5 RFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVggpygpyrQSE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804  81 RHEAYREALAWLHEQGlsyyctcprsriqrlggiydghcrtlyhgpenaavrikqqhpvmrfhdalrgdiqadpqlased 160
Cdd:cd00808   85 RLEIYRKYAEKLLEKG---------------------------------------------------------------- 100

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 486201804 161 fiihrrDGLFAYNLAVVVDDHFQGVTEIVRGADLIEPTVRQLSLYKQFGWRAPGYVHLPLALNEQGAKLSK 231
Cdd:cd00808  101 ------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLPLILNPDGKKLSK 165
GlxRS_core cd00418
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ...
 9-252 2.82e-33

catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA synthetase(GluRS)/Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Glu or Gln, respectively, to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea, cellular organelles, and some bacteria lack GlnRS. In these cases, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme. The discriminating form of GluRS differs from GlnRS and the non-discriminating form of GluRS in their C-terminal anti-codon binding domains.


Pssm-ID: 185672 [Multi-domain]  Cd Length: 230  Bit Score: 121.81  E-value: 2.82e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804   9 RFAPSPSGELHFGSLIAALGSYLQARAQRGIWRVRIEDIDPPREVPGAAATILRQLEHYGLHWDGEVLWQSQRHEAYREA 88
Cdd:cd00418    5 RFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDLYRAY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804  89 LAWLHEQGlsyyctcprsriqrlggiydghcrtlyhgpenaavrikqqhpvmrfhdalrgdiqadpqlasedfiihrrdG 168
Cdd:cd00418   85 AEELIKKG-----------------------------------------------------------------------G 93

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804 169 LFAYNLAVVVDDHFQGVTEIVRGADLIEPTVRQLSLYKQFGWRAPGYVHLPLALNEQGAKLSKQNHAPALATGDPRPVLV 248
Cdd:cd00418   94 YPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDGTKLSKRKLNTTLRALRRRGYLP 173


                 ....
gi 486201804 249 QALR 252
Cdd:cd00418  174 EALR 177
PLN02627 PLN02627
glutamyl-tRNA synthetase
 9-235 2.43e-31

glutamyl-tRNA synthetase


Pssm-ID: 178234 [Multi-domain]  Cd Length: 535  Bit Score: 122.16  E-value: 2.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804   9 RFAPSPSGELHFGSLIAALGSYLQARAQRGIWRVRIEDIDPPREVPGAAATILRQLEHYGLHWD------GEV--LWQSQ 80
Cdd:PLN02627  49 RFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDegpdvgGEYgpYRQSE 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804  81 RHEAYREALAWLHEQGLSYYCTCP---------RSRIQRLGGIYDGHCRT---------LYHG---------PENAAVRI 133
Cdd:PLN02627 129 RNAIYKQYAEKLLESGHVYPCFCTdeeleamkeEAELKKLPPRYTGKWATasdeevqaeLAKGtpytyrfrvPKEGSVKI 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804 134 kqqhpvmrfHDALRGDIQADPQLASeDFIIHRRDGLFAYNLAVVVDDHFQGVTEIVRGADLIEPTVRQLSLYKQFGWRAP 213
Cdd:PLN02627 209 ---------DDLIRGEVSWNTDTLG-DFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMP 278

                        250       260
                 ....*....|....*....|..
gi 486201804 214 GYVHLPLALNEQGAKLSKQNHA 235
Cdd:PLN02627 279 RFAHVSLILAPDRSKLSKRHGA 300
gltX_arch TIGR00463
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ...
 9-257 4.00e-29

glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the eukaryotic cytosolic and archaeal forms of the enzyme. In some eukaryotes, the glutamyl-tRNA synthetase is part of a longer, multifunctional aminoacyl-tRNA ligase. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases, including all known archaeal enzymes (as of 2010) may act on both tRNA(gln) and tRNA(glu). [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273091 [Multi-domain]  Cd Length: 556  Bit Score: 116.08  E-value: 4.00e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804    9 RFAPSPSGELHFGSLIAALGSYLQARAQRGIWRVRIEDIDPPREVPGAAATILRQLEHYGLHWDgEVLWQSQRHEAYREA 88
Cdd:TIGR00463  97 RFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWD-EVVYQSDRIETYYDY 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804   89 LAWLHEQGLSYYCTCPRS--RIQRLGGIyDGHCRTL------------YHGPE---NAAVRIK----QQHPVMRFHDALR 147
Cdd:TIGR00463 176 TRKLIEMGKAYVCDCRPEefRELRNRGE-ACHCRDRsveenlerweemLEGKEeggSVVVRVKtdlkHKNPAIRDWVIFR 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804  148 GDIQADPQLASEdFIIHRrdglfAYNLAVVVDDHFQGVTEIVRGADLIEPTVRQLSLYKQFGWRAPGYVHLPLALNEQGA 227
Cdd:TIGR00463 255 IVKTPHPRTGDK-YRVYP-----TMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYFGWEPPEFIHWGRLKIDDVR 328

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 486201804  228 KLSKQNHAPALATG------DPRPVLVQALRFLGQR 257
Cdd:TIGR00463 329 ALSTSSARKGILRGeysgwdDPRLPTLRAIRRRGIR 364
gltX PRK04156
glutamyl-tRNA synthetase; Provisional
 9-252 6.33e-29

glutamyl-tRNA synthetase; Provisional


Pssm-ID: 235229 [Multi-domain]  Cd Length: 567  Bit Score: 115.72  E-value: 6.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804   9 RFAPSPSGELHFGSLIAALGSYLQARAQRGIWRVRIEDIDPP--REVPGAAATILRQLEHYGLHWDgEVLWQSQRHEAYR 86
Cdd:PRK04156 105 RFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKWD-EVVIQSDRLEIYY 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804  87 EALAWLHEQGLSYYCTCPRSRIQRL--GGIYDgHCRTlyHGPE-----------------NAAVRIKQ--QHPvmrfhda 145
Cdd:PRK04156 184 EYARKLIEMGGAYVCTCDPEEFKELrdAGKPC-PHRD--KSPEenlelwekmldgeykegEAVVRVKTdlEHP------- 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804 146 lrgdiqaDPqlASEDFII-------HRRDG-------LfaYNLAVVVDDHFQGVTEIVRGADLIEPTVRQLSLYKQFGWR 211
Cdd:PRK04156 254 -------NP--SVRDWVAfrivktpHPRVGdkyrvwpT--YNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYDYFGWE 322

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 486201804 212 APGYVHLPlALNEQGAKLSKQNHAPALATG------DPRPVLVQALR 252
Cdd:PRK04156 323 YPETIHYG-RLKIEGFVLSTSKIRKGIEEGeysgwdDPRLPTLRALR 368
GluRS_non_core cd09287
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ...
 9-252 2.77e-24

catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating Glutamyl-tRNA synthetase (GluRS) cataytic core domain. These enzymes attach Glu to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.


Pssm-ID: 185682 [Multi-domain]  Cd Length: 240  Bit Score: 98.19  E-value: 2.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804   9 RFAPSPSGELHFGSLIAALGSYLQARAQRGIWRVRIEDIDP--PREVPGAAATILRQLEHYGLHWDgEVLWQSQRHEAYR 86
Cdd:cd09287    5 RFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPrtKRPDPEAYDMIPEDLEWLGVKWD-EVVIASDRIELYY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804  87 EALAWLHEQGLSYyctcprsriqrlggiydghcrtlyhgpenaavrikqqhpvmrfhdalrgdiqadpqlasedfiIHRR 166
Cdd:cd09287   84 EYARKLIEMGGAY---------------------------------------------------------------VHPR 100

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804 167 DG-----LFAYNLAVVVDDHFQGVTEIVRGADLIEPTVRQLSLYKQFGWRAPGYVHLPLaLNEQGAKLSKQNHAPALATG 241
Cdd:cd09287  101 TGskyrvWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIHWGR-LKIEGGKLSTSKIRKGIESG 179

                        250
                 ....*....|....*..
gi 486201804 242 ------DPRPVLVQALR 252
Cdd:cd09287  180 eyegwdDPRLPTLRALR 196
PLN03233 PLN03233
putative glutamate-tRNA ligase; Provisional
 7-213 1.59e-10

putative glutamate-tRNA ligase; Provisional


Pssm-ID: 178772 [Multi-domain]  Cd Length: 523  Bit Score: 61.56  E-value: 1.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804   7 IGRFAPSPSGELHFGSLIAALGSYLQARAQRGIWRVRIEDIDPPREVPGAAATILRQLEHYGLHWDgEVLWQSQRHEAYR 86
Cdd:PLN03233  13 VTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPD-SVSFTSDYFEPIR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804  87 EALAWLHEQGLSYYCTCPRSRIQRlGGIYDGHCRTLYHGPENAAVRIKQQHPVMRFHDA--LRG--DIQA------DPQL 156
Cdd:PLN03233  92 CYAIILIEEGLAYMDDTPQEEMKK-ERADRAESKHRNQSPEEALEMFKEMCSGKEEGGAwcLRAkiDMQSdngtlrDPVL 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 486201804 157 ASEDFIIHRRDGLF-----AYNLAVVVDDHFQGVTEIVRGADLIEPTVRQLSLYKQFGWRAP 213
Cdd:PLN03233 171 FRQNTTPHHRSGTAykaypTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRP 232
PTZ00402 PTZ00402
glutamyl-tRNA synthetase; Provisional
 7-114 2.70e-07

glutamyl-tRNA synthetase; Provisional


Pssm-ID: 240404 [Multi-domain]  Cd Length: 601  Bit Score: 51.50  E-value: 2.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804   7 IGRFAPSPSGELHFGSLIAALGSYLQARAQRGIWRVRIEDIDPPREVPGAAATILRQLEHYGLHWDGEVLWQSQRHEAYR 86
Cdd:PTZ00402  54 VTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTYSSDYMDLMY 133

                         90       100       110
                 ....*....|....*....|....*....|
gi 486201804  87 EALAWLHEQGLSYYCTCPRSRIQ--RLGGI 114
Cdd:PTZ00402 134 EKAEELIKKGLAYCDKTPREEMQkcRFDGV 163
PLN02907 PLN02907
glutamate-tRNA ligase
 9-120 1.16e-06

glutamate-tRNA ligase


Pssm-ID: 215492 [Multi-domain]  Cd Length: 722  Bit Score: 49.72  E-value: 1.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804   9 RFAPSPSGELHFGSLIAALGSYLQARAQRGIWRVRIEDIDPPREVPGAAATILRQLEHYGLHWDgEVLWQSQRHEAYREA 88
Cdd:PLN02907 217 RFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYD-AVTYTSDYFPQLMEM 295

                         90       100       110
                 ....*....|....*....|....*....|....
gi 486201804  89 LAWLHEQGLSYYCTCPRS--RIQRLGGIyDGHCR 120
Cdd:PLN02907 296 AEKLIKEGKAYVDDTPREqmRKERMDGI-ESKCR 328
PRK14703 PRK14703
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
 9-116 9.62e-05

glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional


Pssm-ID: 237793 [Multi-domain]  Cd Length: 771  Bit Score: 43.94  E-value: 9.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486201804   9 RFAPSPSGELHFGSLIAALGSYLQARAQRGIWRVRIEDIDPPREVPGAAATILRQLEHYGLHWDGEVLWQSQRHEAYREA 88
Cdd:PRK14703  35 RFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDWGEHLYYASDYFERMYAY 114

                         90       100
                 ....*....|....*....|....*...
gi 486201804  89 LAWLHEQGLSYYCTCPRSRIQRLGGIYD 116
Cdd:PRK14703 115 AEQLIKMGLAYVDSVSEEEIRELRGTVT 142
GlnRS_core cd00807
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ...
 9-72 5.04e-03

catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Gln to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. GlnRS contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.


Pssm-ID: 185676 [Multi-domain]  Cd Length: 238  Bit Score: 37.62  E-value: 5.04e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 486201804   9 RFAPSPSGELHFGSLIAALGSYLQARAQRGIWRVRIEDIDPPREVPGAAATILRQLEHYGLHWD 72
Cdd:cd00807    5 RFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPY 68
 
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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