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Conserved domains on  [gi|116207542|ref|XP_001229580|]
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uncharacterized protein CHGG_03064 [Chaetomium globosum CBS 148.51]

Protein Classification

glutamate--tRNA ligase( domain architecture ID 17564554)

glutamate--tRNA ligase catalyzes the attachment of glutamate to tRNA(Glu)

CATH:  3.40.50.620|3.90.800.10|1.10.1160.10|1.10.10.350|1.10.8.70
EC:  6.1.1.17
Gene Ontology:  GO:0008270|GO:0006424|GO:0004818|GO:0000049|GO:0005524
PubMed:  10704480|12458790|10447505|9746349|8078941|8274143|2053131

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GlnS COG0008
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 9-501 1.82e-78

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: 253.56  E-value: 1.82e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542   9 TNGSRLVSDAEDRLYKDLRWAGLSWDEGePLNSSTagRSgnSQHWQV---LICRGHM-----------GLTGRPTNPGQP 74
Cdd:COG0008   46 TDPERSTEEAVDAILEDLRWLGLDWDEG-PYYQSD--RF--DIYYEYaekLIEKGKAyvcfctpeeleALRETQTAPGKP 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542  75 TLYPGTCRHISLEESDDRAHKGEEFAIRFKSAEEPLMIRDIIYNRFKKKDPE-DDYIIMKRDGFPTYHFANVVDDRHMKI 153
Cdd:COG0008  121 PRYDGRCRDLSPEELERMLAAGEPPVLRFKIPEEGVVFDDLVRGEITFPNPNlRDPVLYRADGYPTYNFAVVVDDHLMGI 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542 154 THVIRGAEWLVSTPKHVELYQAFGWEPPEFAHLGLLVDKNRQKLSKRDNSASMEYYQNGHILPSALLNFAVLLGWrAPPT 233
Cdd:COG0008  201 THVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPLILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGW-SKSD 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542 234 KGDVMTLEEMVENLSL-KFSKGDIIVSLQKLPFLQDKHLNRLfdkptktPTEQqtiEQEFLQPlrtaieqaqqtkdspsp 312
Cdd:COG0008  280 DQEIFSLEELIEAFDLdRVSRSPAVFDPVKLVWLNGPYIRAL-------DDEE---LAELLAP----------------- 332

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542 313 sppstppppatlppssigplrlptphLLENERYRPDLLRLVQGARkisldDPADRFAAALSKLRyYIWDVPRPVLEQAAR 392
Cdd:COG0008  333 --------------------------ELPEAGIREDLERLVPLVR-----ERAKTLSELAELAR-FFFIEREDEKAAKKR 380

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542 393 ALAADNPALLgqgqddgtpalavaaAVMAEKFRAVSEaaWKREGIEEAMHAIGADEVFRGcfaaaadadgvrGNMYAALR 472
Cdd:COG0008  381 LAPEEVRKVL---------------KAALEVLEAVET--WDPETVKGTIHWVSAEAGVKD------------GLLFMPLR 431

                        490       500
                 ....*....|....*....|....*....
gi 116207542 473 WALLGGDKGLPMWTTIEILGRDETLRRLE 501
Cdd:COG0008  432 VALTGRTVEPSLFDVLELLGKERVFERLG 460
 
Name Accession Description Interval E-value
GlnS COG0008
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 9-501 1.82e-78

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: 253.56  E-value: 1.82e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542   9 TNGSRLVSDAEDRLYKDLRWAGLSWDEGePLNSSTagRSgnSQHWQV---LICRGHM-----------GLTGRPTNPGQP 74
Cdd:COG0008   46 TDPERSTEEAVDAILEDLRWLGLDWDEG-PYYQSD--RF--DIYYEYaekLIEKGKAyvcfctpeeleALRETQTAPGKP 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542  75 TLYPGTCRHISLEESDDRAHKGEEFAIRFKSAEEPLMIRDIIYNRFKKKDPE-DDYIIMKRDGFPTYHFANVVDDRHMKI 153
Cdd:COG0008  121 PRYDGRCRDLSPEELERMLAAGEPPVLRFKIPEEGVVFDDLVRGEITFPNPNlRDPVLYRADGYPTYNFAVVVDDHLMGI 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542 154 THVIRGAEWLVSTPKHVELYQAFGWEPPEFAHLGLLVDKNRQKLSKRDNSASMEYYQNGHILPSALLNFAVLLGWrAPPT 233
Cdd:COG0008  201 THVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPLILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGW-SKSD 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542 234 KGDVMTLEEMVENLSL-KFSKGDIIVSLQKLPFLQDKHLNRLfdkptktPTEQqtiEQEFLQPlrtaieqaqqtkdspsp 312
Cdd:COG0008  280 DQEIFSLEELIEAFDLdRVSRSPAVFDPVKLVWLNGPYIRAL-------DDEE---LAELLAP----------------- 332

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542 313 sppstppppatlppssigplrlptphLLENERYRPDLLRLVQGARkisldDPADRFAAALSKLRyYIWDVPRPVLEQAAR 392
Cdd:COG0008  333 --------------------------ELPEAGIREDLERLVPLVR-----ERAKTLSELAELAR-FFFIEREDEKAAKKR 380

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542 393 ALAADNPALLgqgqddgtpalavaaAVMAEKFRAVSEaaWKREGIEEAMHAIGADEVFRGcfaaaadadgvrGNMYAALR 472
Cdd:COG0008  381 LAPEEVRKVL---------------KAALEVLEAVET--WDPETVKGTIHWVSAEAGVKD------------GLLFMPLR 431

                        490       500
                 ....*....|....*....|....*....
gi 116207542 473 WALLGGDKGLPMWTTIEILGRDETLRRLE 501
Cdd:COG0008  432 VALTGRTVEPSLFDVLELLGKERVFERLG 460
gltX_bact TIGR00464
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ...
 9-276 1.08e-64

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: 217.61  E-value: 1.08e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542    9 TNGSRLVSDAEDRLYKDLRWAGLSWDEGEPLNSSTAGRSgnSQHWQVLICRGHM-----------GLTGRPTNPGQPTLY 77
Cdd:TIGR00464  43 TDLERNIEEAEEAILEGLKWLGISWDEGPYYQSQRLDIY--KKYAKELLEEGLAyrcycskerleRLREEQKANKETPRY 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542   78 PGTCRHISLEESDDRAHKGEEFAIRFKSAEE-PLMIRDIIYNRFKKKDPE-DDYIIMKRDGFPTYHFANVVDDRHMKITH 155
Cdd:TIGR00464 121 DGRCRNLHEEEIENKLAKGIPPVVRFKIPQEaVVSFNDQVRGEITFQNSElDDFVILRSDGSPTYNFAVVVDDYLMKITH 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542  156 VIRGAEWLVSTPKHVELYQAFGWEPPEFAHLGLLVDKNRQKLSKRDNSASMEYYQNGHILPSALLNFAVLLGWrAPPTKG 235
Cdd:TIGR00464 201 VIRGEDHISNTPKQILIYQALGWKIPVFAHLPMILDEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGW-SPPDDQ 279

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 116207542  236 DVMTLEEMVENLSL-KFSKGDIIVSLQKLPFLQDKHLNRLFD 276
Cdd:TIGR00464 280 EFFSLEELIEIFSLnRVSKSPAKFDWKKLQWLNAHYIKELPD 321
GluRS_core cd00808
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ...
 9-273 1.12e-63

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: 207.44  E-value: 1.12e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542   9 TNGSRLVSDAEDRLYKDLRWAGLSWDEGeplnsstagrsgnsqhwqvlicrghmgltgrPTNPGQPTLYpgtcrhislEE 88
Cdd:cd00808   43 TDQERSVPEAEEAILEALKWLGLDWDEG-------------------------------PDVGGPYGPY---------RQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542  89 SDdrahkgeefaiRFKsaeeplmirdiIYNRFKKKdpeddyIIMKRDGFPTYHFANVVDDRHMKITHVIRGAEWLVSTPK 168
Cdd:cd00808   83 SE-----------RLE-----------IYRKYAEK------LLEKGDGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPK 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542 169 HVELYQAFGWEPPEFAHLGLLVDKNRQKLSKRDNSASMEYYQNGHILPSALLNFAVLLGWrAPPTKGDVMTLEEMVENLS 248
Cdd:cd00808  135 QILLYEALGWEPPKFAHLPLILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGW-SPPDGEEFFTLEELIELFD 213

                        250       260
                 ....*....|....*....|....*.
gi 116207542 249 L-KFSKGDIIVSLQKLPFLQDKHLNR 273
Cdd:cd00808  214 LeRVSKSPAIFDPEKLDWLNGQYIRE 239
tRNA-synt_1c pfam00749
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ...
 9-256 2.28e-46

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: 164.41  E-value: 2.28e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542    9 TNGSRLVSDAEDRLYKDLRWAGLSWDEGePLNSStagrsgnsQHWQ-------VLICRGH-------------MGLTGRP 68
Cdd:pfam00749  43 TDPERETPEFEESILEDLKWLGIKWDYG-PYYQS--------DRFDiyykyaeELIKKGKayvcfctpeeleeEREEQEA 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542   69 TNPGQPTLYPGTCRHISLEESDDRAHKGEEFAIRFKSAEE-PLMIRDIIYNRFK-KKDPEDDYIIMKRDGFPTYHFANVV 146
Cdd:pfam00749 114 LGSPSRDRYDEENLHLFEEEMKKGSAEGGPATVRAKIPMEsPYVFRDPVRGRIKfTPQEIHDRTGVKWDGYPTYDFAVVI 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542  147 DDRHMKITHVIRGAEWLVSTPKHVELYQAFGWEPPEFAHLGLLVDKNRQKLSKRDNSASM--EYYQNGHILPSALLNFAV 224
Cdd:pfam00749 194 DDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNLDGTKLSKRKLSWSVdiSQVKGWGDPREATLNGLR 273

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 116207542  225 LLGWrAPPTKGDVMTLEEM-----VENLSLKFSKGDI 256
Cdd:pfam00749 274 RRGW-TPEGIREFFTREGViksfdVNRLSKSLEAFDR 309
PLN02627 PLN02627
glutamyl-tRNA synthetase
 9-287 7.18e-36

glutamyl-tRNA synthetase


Pssm-ID: 178234 [Multi-domain]  Cd Length: 535  Bit Score: 140.26  E-value: 7.18e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542   9 TNGSRLVSDAEDRLYKDLRWAGLSWDEGE-------PLNSSTAGrSGNSQHWQVLICRGHM-----------GLTGRPTN 70
Cdd:PLN02627  87 TDLARSTKESEEAVLRDLKWLGLDWDEGPdvggeygPYRQSERN-AIYKQYAEKLLESGHVypcfctdeeleAMKEEAEL 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542  71 PGQPTLYPGTCRHISLEESDDRAHKGEEFAIRFK-SAEEPLMIRDIIYNRFK-KKDPEDDYIIMKRDGFPTYHFANVVDD 148
Cdd:PLN02627 166 KKLPPRYTGKWATASDEEVQAELAKGTPYTYRFRvPKEGSVKIDDLIRGEVSwNTDTLGDFVLLRSNGQPVYNFCVAVDD 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542 149 RHMKITHVIRGAEWLVSTPKHVELYQAFGWEPPEFAHLGLLVDKNRQKLSKRDNSASMEYYQNGHILPSALLNFAVLLGW 228
Cdd:PLN02627 246 ATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHVSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGW 325

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542 229 rAPPTKGDVMTLEEMVENLSL-KFSKGDIIVSLQKLPFLQDKHLNRLfdkptktPTEQQT 287
Cdd:PLN02627 326 -NDGTENEIFTLEELVEKFSIdRINKSGAVFDSTKLKWMNGQHLRLL-------PEEELV 377
 
Name Accession Description Interval E-value
GlnS COG0008
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 9-501 1.82e-78

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: 253.56  E-value: 1.82e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542   9 TNGSRLVSDAEDRLYKDLRWAGLSWDEGePLNSSTagRSgnSQHWQV---LICRGHM-----------GLTGRPTNPGQP 74
Cdd:COG0008   46 TDPERSTEEAVDAILEDLRWLGLDWDEG-PYYQSD--RF--DIYYEYaekLIEKGKAyvcfctpeeleALRETQTAPGKP 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542  75 TLYPGTCRHISLEESDDRAHKGEEFAIRFKSAEEPLMIRDIIYNRFKKKDPE-DDYIIMKRDGFPTYHFANVVDDRHMKI 153
Cdd:COG0008  121 PRYDGRCRDLSPEELERMLAAGEPPVLRFKIPEEGVVFDDLVRGEITFPNPNlRDPVLYRADGYPTYNFAVVVDDHLMGI 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542 154 THVIRGAEWLVSTPKHVELYQAFGWEPPEFAHLGLLVDKNRQKLSKRDNSASMEYYQNGHILPSALLNFAVLLGWrAPPT 233
Cdd:COG0008  201 THVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPLILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGW-SKSD 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542 234 KGDVMTLEEMVENLSL-KFSKGDIIVSLQKLPFLQDKHLNRLfdkptktPTEQqtiEQEFLQPlrtaieqaqqtkdspsp 312
Cdd:COG0008  280 DQEIFSLEELIEAFDLdRVSRSPAVFDPVKLVWLNGPYIRAL-------DDEE---LAELLAP----------------- 332

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542 313 sppstppppatlppssigplrlptphLLENERYRPDLLRLVQGARkisldDPADRFAAALSKLRyYIWDVPRPVLEQAAR 392
Cdd:COG0008  333 --------------------------ELPEAGIREDLERLVPLVR-----ERAKTLSELAELAR-FFFIEREDEKAAKKR 380

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542 393 ALAADNPALLgqgqddgtpalavaaAVMAEKFRAVSEaaWKREGIEEAMHAIGADEVFRGcfaaaadadgvrGNMYAALR 472
Cdd:COG0008  381 LAPEEVRKVL---------------KAALEVLEAVET--WDPETVKGTIHWVSAEAGVKD------------GLLFMPLR 431

                        490       500
                 ....*....|....*....|....*....
gi 116207542 473 WALLGGDKGLPMWTTIEILGRDETLRRLE 501
Cdd:COG0008  432 VALTGRTVEPSLFDVLELLGKERVFERLG 460
gltX_bact TIGR00464
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ...
 9-276 1.08e-64

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: 217.61  E-value: 1.08e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542    9 TNGSRLVSDAEDRLYKDLRWAGLSWDEGEPLNSSTAGRSgnSQHWQVLICRGHM-----------GLTGRPTNPGQPTLY 77
Cdd:TIGR00464  43 TDLERNIEEAEEAILEGLKWLGISWDEGPYYQSQRLDIY--KKYAKELLEEGLAyrcycskerleRLREEQKANKETPRY 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542   78 PGTCRHISLEESDDRAHKGEEFAIRFKSAEE-PLMIRDIIYNRFKKKDPE-DDYIIMKRDGFPTYHFANVVDDRHMKITH 155
Cdd:TIGR00464 121 DGRCRNLHEEEIENKLAKGIPPVVRFKIPQEaVVSFNDQVRGEITFQNSElDDFVILRSDGSPTYNFAVVVDDYLMKITH 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542  156 VIRGAEWLVSTPKHVELYQAFGWEPPEFAHLGLLVDKNRQKLSKRDNSASMEYYQNGHILPSALLNFAVLLGWrAPPTKG 235
Cdd:TIGR00464 201 VIRGEDHISNTPKQILIYQALGWKIPVFAHLPMILDEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGW-SPPDDQ 279

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 116207542  236 DVMTLEEMVENLSL-KFSKGDIIVSLQKLPFLQDKHLNRLFD 276
Cdd:TIGR00464 280 EFFSLEELIEIFSLnRVSKSPAKFDWKKLQWLNAHYIKELPD 321
GluRS_core cd00808
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ...
 9-273 1.12e-63

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: 207.44  E-value: 1.12e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542   9 TNGSRLVSDAEDRLYKDLRWAGLSWDEGeplnsstagrsgnsqhwqvlicrghmgltgrPTNPGQPTLYpgtcrhislEE 88
Cdd:cd00808   43 TDQERSVPEAEEAILEALKWLGLDWDEG-------------------------------PDVGGPYGPY---------RQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542  89 SDdrahkgeefaiRFKsaeeplmirdiIYNRFKKKdpeddyIIMKRDGFPTYHFANVVDDRHMKITHVIRGAEWLVSTPK 168
Cdd:cd00808   83 SE-----------RLE-----------IYRKYAEK------LLEKGDGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPK 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542 169 HVELYQAFGWEPPEFAHLGLLVDKNRQKLSKRDNSASMEYYQNGHILPSALLNFAVLLGWrAPPTKGDVMTLEEMVENLS 248
Cdd:cd00808  135 QILLYEALGWEPPKFAHLPLILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGW-SPPDGEEFFTLEELIELFD 213

                        250       260
                 ....*....|....*....|....*.
gi 116207542 249 L-KFSKGDIIVSLQKLPFLQDKHLNR 273
Cdd:cd00808  214 LeRVSKSPAIFDPEKLDWLNGQYIRE 239
tRNA-synt_1c pfam00749
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ...
 9-256 2.28e-46

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: 164.41  E-value: 2.28e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542    9 TNGSRLVSDAEDRLYKDLRWAGLSWDEGePLNSStagrsgnsQHWQ-------VLICRGH-------------MGLTGRP 68
Cdd:pfam00749  43 TDPERETPEFEESILEDLKWLGIKWDYG-PYYQS--------DRFDiyykyaeELIKKGKayvcfctpeeleeEREEQEA 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542   69 TNPGQPTLYPGTCRHISLEESDDRAHKGEEFAIRFKSAEE-PLMIRDIIYNRFK-KKDPEDDYIIMKRDGFPTYHFANVV 146
Cdd:pfam00749 114 LGSPSRDRYDEENLHLFEEEMKKGSAEGGPATVRAKIPMEsPYVFRDPVRGRIKfTPQEIHDRTGVKWDGYPTYDFAVVI 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542  147 DDRHMKITHVIRGAEWLVSTPKHVELYQAFGWEPPEFAHLGLLVDKNRQKLSKRDNSASM--EYYQNGHILPSALLNFAV 224
Cdd:pfam00749 194 DDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNLDGTKLSKRKLSWSVdiSQVKGWGDPREATLNGLR 273

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 116207542  225 LLGWrAPPTKGDVMTLEEM-----VENLSLKFSKGDI 256
Cdd:pfam00749 274 RRGW-TPEGIREFFTREGViksfdVNRLSKSLEAFDR 309
PLN02627 PLN02627
glutamyl-tRNA synthetase
 9-287 7.18e-36

glutamyl-tRNA synthetase


Pssm-ID: 178234 [Multi-domain]  Cd Length: 535  Bit Score: 140.26  E-value: 7.18e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542   9 TNGSRLVSDAEDRLYKDLRWAGLSWDEGE-------PLNSSTAGrSGNSQHWQVLICRGHM-----------GLTGRPTN 70
Cdd:PLN02627  87 TDLARSTKESEEAVLRDLKWLGLDWDEGPdvggeygPYRQSERN-AIYKQYAEKLLESGHVypcfctdeeleAMKEEAEL 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542  71 PGQPTLYPGTCRHISLEESDDRAHKGEEFAIRFK-SAEEPLMIRDIIYNRFK-KKDPEDDYIIMKRDGFPTYHFANVVDD 148
Cdd:PLN02627 166 KKLPPRYTGKWATASDEEVQAELAKGTPYTYRFRvPKEGSVKIDDLIRGEVSwNTDTLGDFVLLRSNGQPVYNFCVAVDD 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542 149 RHMKITHVIRGAEWLVSTPKHVELYQAFGWEPPEFAHLGLLVDKNRQKLSKRDNSASMEYYQNGHILPSALLNFAVLLGW 228
Cdd:PLN02627 246 ATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHVSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGW 325

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542 229 rAPPTKGDVMTLEEMVENLSL-KFSKGDIIVSLQKLPFLQDKHLNRLfdkptktPTEQQT 287
Cdd:PLN02627 326 -NDGTENEIFTLEELVEKFSIdRINKSGAVFDSTKLKWMNGQHLRLL-------PEEELV 377
GlxRS_core cd00418
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ...
 131-272 7.91e-36

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: 133.37  E-value: 7.91e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542 131 IMKRDGFPTYHFANVVDDRHMKITHVIRGAEWLVSTPKHVELYQAFGWEPPEFAHLGLLVDKNRQKLSKRDNSASMEYYQ 210
Cdd:cd00418   88 LIKKGGYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDGTKLSKRKLNTTLRALR 167

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116207542 211 NGHILPSALLNFAVLLGWrAPPTKGDVMTLEEMVENLSL-KFSKGDIIVSLQKLPFLQDKHLN 272
Cdd:cd00418  168 RRGYLPEALRNYLALIGW-SKPDGHELFTLEEMIAAFSVeRVNSADATFDWAKLEWLNREYIR 229
PRK05710 PRK05710
tRNA glutamyl-Q(34) synthetase GluQRS;
13-242 3.51e-33

tRNA glutamyl-Q(34) synthetase GluQRS;


Pssm-ID: 235573  Cd Length: 299  Bit Score: 128.04  E-value: 3.51e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542  13 RLVSDAEDRLYKDLRWAGLSWDeGEPLNsstagrsgNSQHW----QVLICRGHMGLT------------GRPTNPGQPTL 76
Cdd:PRK05710  51 REVPGAADAILADLEWLGLHWD-GPVLY--------QSQRHdayrAALDRLRAQGLVypcfcsrkeiaaAAPAPPDGGGI 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542  77 YPGTCRHISLEESDDRAhkgeefaIRFKSAEEPLMIRDIIYNRFKKKDPED--DYIIMKRDGFPTYHFANVVDDRHMKIT 154
Cdd:PRK05710 122 YPGTCRDLLHGPRNPPA-------WRLRVPDAVIAFDDRLQGRQHQDLALAvgDFVLRRADGLFAYQLAVVVDDALQGVT 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542 155 HVIRGAEWLVSTPKHVELYQAFGWEPPEFAHLGLLVDKNRQKLSKRDNSASMEyyqNGHILPsALLNFAVLLGWRAPPTK 234
Cdd:PRK05710 195 HVVRGADLLDSTPRQIYLQQLLGLPTPRYLHLPLVLNADGQKLSKQNGAPALD---AAGPLP-VLAAALRFLGQPPPAAD 270


                 ....*...
gi 116207542 235 GDVMTLEE 242
Cdd:PRK05710 271 ASVEELLA 278
queuosine_YadB TIGR03838
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ...
 13-244 6.94e-31

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: 120.72  E-value: 6.94e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542   13 RLVSDAEDRLYKDLRWAGLSWDeGEPLNSSTagrsgNSQHWQVLICR----GHM---GLTGR--PTNPGQPTLYPGTCRH 83
Cdd:TIGR03838  46 REVPGAADDILRTLEAYGLHWD-GEVVYQSQ-----RHALYQAALDRllaaGLAypcQCTRKeiAAARDGGGIYPGTCRN 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542   84 ISLEESDDRAhkgeefAIRFKSAEEPLMIRDII--YNRFKKKDPEDDYIIMKRDGFPTYHFANVVDDRHMKITHVIRGAE 161
Cdd:TIGR03838 120 GLPGRPGRPA------AWRLRVPDGVIAFDDRLqgPQQQDLAAAVGDFVLRRADGLFAYQLAVVVDDAAQGITHVVRGAD 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542  162 WLVSTPKHVELYQAFGWEPPEFAHLGLLVDKNRQKLSKRDNSASMEyyqNGHILPsALLNFAVLLGWrAPPTKGDVMTLE 241
Cdd:TIGR03838 194 LLDSTPRQIYLQRLLGLPPPRYLHLPLVVNADGEKLSKQNGAPALD---DSRPLP-ALLAALRFLGL-PPPPELAAASPA 268


                  ...
gi 116207542  242 EMV 244
Cdd:TIGR03838 269 ELL 271
GluRS_non_core cd09287
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ...
 137-189 1.31e-12

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: 67.38  E-value: 1.31e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 116207542 137 FPTYHFANVVDDRHMKITHVIRGAEWLVSTPKHVELYQAFGWEPPEFAHLGLL 189
Cdd:cd09287  108 WPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIHWGRL 160
gltX PRK04156
glutamyl-tRNA synthetase; Provisional
 127-189 4.95e-12

glutamyl-tRNA synthetase; Provisional


Pssm-ID: 235229 [Multi-domain]  Cd Length: 567  Bit Score: 68.34  E-value: 4.95e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116207542 127 DDYIImkrdgFPTYHFANVVDDRHMKITHVIRGAEWLVSTPKHVELYQAFGWEPPEFAHLGLL 189
Cdd:PRK04156 275 DKYRV-----WPTYNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYDYFGWEYPETIHYGRL 332
gltX_arch TIGR00463
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ...
 9-189 9.96e-12

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: 67.16  E-value: 9.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542    9 TNGSRLVSDAEDRLYKDLRWAGLSWDEgeplnssTAGRSGNSQHW----QVLICRGHMGLTGRPT-------NPGQPTly 77
Cdd:TIGR00463 135 TDPRRVDPEAYDMILEDLEWLGVKWDE-------VVYQSDRIETYydytRKLIEMGKAYVCDCRPeefrelrNRGEAC-- 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542   78 pgTCRHISLEESDDRAHK-------GEEFAIRFKS---AEEPlMIRD-IIYNRFKKKDPE--DDYIImkrdgFPTYHFAN 144
Cdd:TIGR00463 206 --HCRDRSVEENLERWEEmlegkeeGGSVVVRVKTdlkHKNP-AIRDwVIFRIVKTPHPRtgDKYRV-----YPTMDFSV 277

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 116207542  145 VVDDRHMKITHVIRGAEWLVSTPKHVELYQAFGWEPPEFAHLGLL 189
Cdd:TIGR00463 278 AIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYFGWEPPEFIHWGRL 322
Anticodon_2 pfam19269
Anticodon binding domain; This entry represents the anticodon binding domain found at the ...
 422-501 2.61e-05

Anticodon binding domain; This entry represents the anticodon binding domain found at the C-terminus of the class-I glutamyl tRNA synthetase enzyme.


Pssm-ID: 466020 [Multi-domain]  Cd Length: 148  Bit Score: 44.10  E-value: 2.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116207542  422 EKFRAVSEaaWKREGIEEAMHAIGADEvfrgcfaaaadadGVR-GNMYAALRWALLGGDKGLPMWTTIEILGRDETLRRL 500
Cdd:pfam19269  80 PRLEALED--WTAEALEAALKALAEEL-------------GVKnGKVMWPLRVALTGKTVSPGLFEIMEILGKEETLARL 144


                  .
gi 116207542  501 E 501
Cdd:pfam19269 145 R 145
 
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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