|
Name |
Accession |
Description |
Interval |
E-value |
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
2-466 |
0e+00 |
|
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: 804.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDEGPYYQTKRFDR 81
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGPYYQSQRLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 82 YNAVIDQMLEEGTAYKCYCSKERLEALREEQMAKGEKPRYDGRCRHSHEHH-----ADDEPCVVRFANPQEGSVVFDDQI 156
Cdd:TIGR00464 81 YKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEienklAKGIPPVVRFKIPQEAVVSFNDQV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 157 RGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVPVYAHVSMINGDDGK 236
Cdd:TIGR00464 161 RGEITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLPMILDEDGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 237 KLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSHG-DQEIFTREEMIKYFTLNAVSKSASAFNTDKLLWLNHHYINALP 315
Cdd:TIGR00464 241 KLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPdDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQWLNAHYIKELP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 316 PEYVATHLQWHIEQE-NIDTRNGPQLADLVKLLGERCKTLKEMAQSCRYFYEDFAEFDADAAKKHLRPVARQPLEVVRDK 394
Cdd:TIGR00464 321 DEELFELLDPHLKSLvNTDTLNREQLAELLLLFKERLKTLKEIAELIRLFFEDKKEVDEDAFKKHLKKNVKEVLEALKKK 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130330 395 LAAITDWTAENVHHAIQATADELEVGMGKVGMPLRVAVTGAGQSPALDVTVHAIGKTRSIERINKalDFIAE 466
Cdd:TIGR00464 401 LQALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESIKRLKA--QFIAA 470
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
1-465 |
0e+00 |
|
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: 712.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 1 MKIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDEGPYYQTKRFD 80
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 81 RYNAVIDQMLEEGTAYKCYCSKERLEALREEQMAKGEKPRYDGRCRH-SHEHH----ADDEPCVVRFANPQEGsVVFDDQ 155
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDlSPEELermlAAGEPPVLRFKIPEEG-VVFDDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 156 IRGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVPVYAHVSMINGDDG 235
Cdd:COG0008 162 VRGEITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPLILGPDG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 236 KKLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSH-GDQEIFTREEMIKYFTLNAVSKSASAFNTDKLLWLNHHYINAL 314
Cdd:COG0008 242 TKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKsDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLNGPYIRAL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 315 PPEYVATHLQWHIEQENIDTRngpqLADLVKLLGERCKTLKEMAQSCRYFYEDFAefDADAAKKHLRP-VARQPLEVVRD 393
Cdd:COG0008 322 DDEELAELLAPELPEAGIRED----LERLVPLVRERAKTLSELAELARFFFIERE--DEKAAKKRLAPeEVRKVLKAALE 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130330 394 KLAAITDWTAENVHHAIQATADELEVGMGKVGMPLRVAVTGAGQSPALDVTVHAIGKTRSIERINKALDFIA 465
Cdd:COG0008 396 VLEAVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERVFERLGYAIDKLA 467
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
2-305 |
1.50e-168 |
|
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: 476.81 E-value: 1.50e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDEGPYYQTKRFDR 81
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 82 YNAVIDQMLEEGTAYKCYCSKERLEALREEQMAKGEK--PRYDGRCRHSHEH-----HADDEPCVVRFANPQEGSVVFDD 154
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQEALGSPsrDRYDEENLHLFEEemkkgSAEGGPATVRAKIPMESPYVFRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 155 QIRGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVPVYAHVSMINGDD 234
Cdd:pfam00749 161 PVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130330 235 GKKLSKRHGAVSV--MQYRDDGYLPEALLNYLVRLGWS-HGDQEIFTREEMIKYFTLNAVSKSASAFNTDKLLW 305
Cdd:pfam00749 241 GTKLSKRKLSWSVdiSQVKGWGDPREATLNGLRRRGWTpEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLDW 314
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
3-444 |
1.20e-149 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 437.25 E-value: 1.20e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 3 IKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDEGP--------YY 74
Cdd:PLN02627 46 VRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPdvggeygpYR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 75 QTKRFDRYNAVIDQMLEEGTAYKCYCSKERLEALREEQMAKGEKPRYDGRCRHSHEHHADDE-----PCVVRFANPQEGS 149
Cdd:PLN02627 126 QSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAElakgtPYTYRFRVPKEGS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 150 VVFDDQIRGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVPVYAHVSM 229
Cdd:PLN02627 206 VKIDDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHVSL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 230 INGDDGKKLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSHG-DQEIFTREEMIKYFTLNAVSKSASAFNTDKLLWLNH 308
Cdd:PLN02627 286 ILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWNDGtENEIFTLEELVEKFSIDRINKSGAVFDSTKLKWMNG 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 309 HYINALPPEyvathlqwhieqenidtrngpqlaDLVKLLGERCKTLKEMAQSCRYFYE-------DFAEFDADAAkKHLR 381
Cdd:PLN02627 366 QHLRLLPEE------------------------ELVKLVGERWKSAGILKESDGSFVKeavellkDGIELVTDAD-KELL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 382 PVARQPL----------EVVRDKLAAITD----------WTA--ENVHHAIQATADELEVGMGKVG----MPLRVAVTGA 435
Cdd:PLN02627 421 NLLSYPLaatlsspeakTVVEDNFSEVADaliaaydsgeLAAalEEGHDGWQKWVKAFGKALKRKGkrlfMPLRVALTGK 500
|
....*....
gi 16130330 436 GQSPalDVT 444
Cdd:PLN02627 501 MHGP--DVG 507
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
2-312 |
1.38e-135 |
|
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: 390.02 E-value: 1.38e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDE--------GPY 73
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEgpdvggpyGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 74 YQTKRFDRYNAVIDQMLEEGtaykcycskerlealreeqmakgekprydgrcrhshehhaddepcvvrfanpqegsvvfd 153
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 154 dqirgpiefsnqelddliirrtDGSPTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVPVYAHVSMINGD 233
Cdd:cd00808 101 ----------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLPLILNP 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 234 DGKKLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSHGD-QEIFTREEMIKYFTLNAVSKSASAFNTDKLLWLNHHYIN 312
Cdd:cd00808 159 DGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDgEEFFTLEELIELFDLERVSKSPAIFDPEKLDWLNGQYIR 238
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
2-466 |
0e+00 |
|
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: 804.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDEGPYYQTKRFDR 81
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGPYYQSQRLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 82 YNAVIDQMLEEGTAYKCYCSKERLEALREEQMAKGEKPRYDGRCRHSHEHH-----ADDEPCVVRFANPQEGSVVFDDQI 156
Cdd:TIGR00464 81 YKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEienklAKGIPPVVRFKIPQEAVVSFNDQV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 157 RGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVPVYAHVSMINGDDGK 236
Cdd:TIGR00464 161 RGEITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLPMILDEDGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 237 KLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSHG-DQEIFTREEMIKYFTLNAVSKSASAFNTDKLLWLNHHYINALP 315
Cdd:TIGR00464 241 KLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPdDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQWLNAHYIKELP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 316 PEYVATHLQWHIEQE-NIDTRNGPQLADLVKLLGERCKTLKEMAQSCRYFYEDFAEFDADAAKKHLRPVARQPLEVVRDK 394
Cdd:TIGR00464 321 DEELFELLDPHLKSLvNTDTLNREQLAELLLLFKERLKTLKEIAELIRLFFEDKKEVDEDAFKKHLKKNVKEVLEALKKK 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130330 395 LAAITDWTAENVHHAIQATADELEVGMGKVGMPLRVAVTGAGQSPALDVTVHAIGKTRSIERINKalDFIAE 466
Cdd:TIGR00464 401 LQALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESIKRLKA--QFIAA 470
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
1-465 |
0e+00 |
|
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: 712.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 1 MKIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDEGPYYQTKRFD 80
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 81 RYNAVIDQMLEEGTAYKCYCSKERLEALREEQMAKGEKPRYDGRCRH-SHEHH----ADDEPCVVRFANPQEGsVVFDDQ 155
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDlSPEELermlAAGEPPVLRFKIPEEG-VVFDDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 156 IRGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVPVYAHVSMINGDDG 235
Cdd:COG0008 162 VRGEITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPLILGPDG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 236 KKLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSH-GDQEIFTREEMIKYFTLNAVSKSASAFNTDKLLWLNHHYINAL 314
Cdd:COG0008 242 TKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKsDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLNGPYIRAL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 315 PPEYVATHLQWHIEQENIDTRngpqLADLVKLLGERCKTLKEMAQSCRYFYEDFAefDADAAKKHLRP-VARQPLEVVRD 393
Cdd:COG0008 322 DDEELAELLAPELPEAGIRED----LERLVPLVRERAKTLSELAELARFFFIERE--DEKAAKKRLAPeEVRKVLKAALE 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130330 394 KLAAITDWTAENVHHAIQATADELEVGMGKVGMPLRVAVTGAGQSPALDVTVHAIGKTRSIERINKALDFIA 465
Cdd:COG0008 396 VLEAVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERVFERLGYAIDKLA 467
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
2-305 |
1.50e-168 |
|
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: 476.81 E-value: 1.50e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDEGPYYQTKRFDR 81
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 82 YNAVIDQMLEEGTAYKCYCSKERLEALREEQMAKGEK--PRYDGRCRHSHEH-----HADDEPCVVRFANPQEGSVVFDD 154
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQEALGSPsrDRYDEENLHLFEEemkkgSAEGGPATVRAKIPMESPYVFRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 155 QIRGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVPVYAHVSMINGDD 234
Cdd:pfam00749 161 PVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130330 235 GKKLSKRHGAVSV--MQYRDDGYLPEALLNYLVRLGWS-HGDQEIFTREEMIKYFTLNAVSKSASAFNTDKLLW 305
Cdd:pfam00749 241 GTKLSKRKLSWSVdiSQVKGWGDPREATLNGLRRRGWTpEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLDW 314
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
3-444 |
1.20e-149 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 437.25 E-value: 1.20e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 3 IKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDEGP--------YY 74
Cdd:PLN02627 46 VRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPdvggeygpYR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 75 QTKRFDRYNAVIDQMLEEGTAYKCYCSKERLEALREEQMAKGEKPRYDGRCRHSHEHHADDE-----PCVVRFANPQEGS 149
Cdd:PLN02627 126 QSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAElakgtPYTYRFRVPKEGS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 150 VVFDDQIRGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVPVYAHVSM 229
Cdd:PLN02627 206 VKIDDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHVSL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 230 INGDDGKKLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSHG-DQEIFTREEMIKYFTLNAVSKSASAFNTDKLLWLNH 308
Cdd:PLN02627 286 ILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWNDGtENEIFTLEELVEKFSIDRINKSGAVFDSTKLKWMNG 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 309 HYINALPPEyvathlqwhieqenidtrngpqlaDLVKLLGERCKTLKEMAQSCRYFYE-------DFAEFDADAAkKHLR 381
Cdd:PLN02627 366 QHLRLLPEE------------------------ELVKLVGERWKSAGILKESDGSFVKeavellkDGIELVTDAD-KELL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 382 PVARQPL----------EVVRDKLAAITD----------WTA--ENVHHAIQATADELEVGMGKVG----MPLRVAVTGA 435
Cdd:PLN02627 421 NLLSYPLaatlsspeakTVVEDNFSEVADaliaaydsgeLAAalEEGHDGWQKWVKAFGKALKRKGkrlfMPLRVALTGK 500
|
....*....
gi 16130330 436 GQSPalDVT 444
Cdd:PLN02627 501 MHGP--DVG 507
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
2-312 |
1.38e-135 |
|
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: 390.02 E-value: 1.38e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDE--------GPY 73
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEgpdvggpyGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 74 YQTKRFDRYNAVIDQMLEEGtaykcycskerlealreeqmakgekprydgrcrhshehhaddepcvvrfanpqegsvvfd 153
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 154 dqirgpiefsnqelddliirrtDGSPTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVPVYAHVSMINGD 233
Cdd:cd00808 101 ----------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLPLILNP 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 234 DGKKLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSHGD-QEIFTREEMIKYFTLNAVSKSASAFNTDKLLWLNHHYIN 312
Cdd:cd00808 159 DGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDgEEFFTLEELIELFDLERVSKSPAIFDPEKLDWLNGQYIR 238
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
5-270 |
2.34e-91 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 279.43 E-value: 2.34e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 5 TRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDEGPYYQTKRFDRYNA 84
Cdd:PRK05710 8 GRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQRHDAYRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 85 VIDQMLEEGTAYKCYCSKERLEALREEQMAKGekPRYDGRCRhsHEHHADDEPCVVRFANPqEGSVVFDDQIRGPIEF-S 163
Cdd:PRK05710 88 ALDRLRAQGLVYPCFCSRKEIAAAAPAPPDGG--GIYPGTCR--DLLHGPRNPPAWRLRVP-DAVIAFDDRLQGRQHQdL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 164 NQELDDLIIRRTDGSPTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVPVYAHVSMINGDDGKKLSKRHG 243
Cdd:PRK05710 163 ALAVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRYLHLPLVLNADGQKLSKQNG 242
|
250 260
....*....|....*....|....*...
gi 16130330 244 AVSVmqyRDDGylPEALLNYLVR-LGWS 270
Cdd:PRK05710 243 APAL---DAAG--PLPVLAAALRfLGQP 265
|
|
| queuosine_YadB |
TIGR03838 |
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ... |
6-270 |
1.06e-88 |
|
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: 271.72 E-value: 1.06e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 6 RFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDEGPYYQTKRFDRYNAV 85
Cdd:TIGR03838 4 RFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGEVVYQSQRHALYQAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 86 IDQMLEEGTAYKCYCSKERLEALREEQmakgekPRYDGRCRHSHeHHADDEPCVVRFANPqEGSVVFDDQIRGPIEF-SN 164
Cdd:TIGR03838 84 LDRLLAAGLAYPCQCTRKEIAAARDGG------GIYPGTCRNGL-PGRPGRPAAWRLRVP-DGVIAFDDRLQGPQQQdLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 165 QELDDLIIRRTDGSPTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVPVYAHVSMINGDDGKKLSKRHGA 244
Cdd:TIGR03838 156 AAVGDFVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHLPLVVNADGEKLSKQNGA 235
|
250 260
....*....|....*....|....*..
gi 16130330 245 VSVmqyrDDGYlPEALLNYLVR-LGWS 270
Cdd:TIGR03838 236 PAL----DDSR-PLPALLAALRfLGLP 257
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
2-312 |
3.11e-84 |
|
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: 258.94 E-value: 3.11e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDEGPYYQTKRFDR 81
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 82 YNAVIDQMLEEGtaykcycskerlealreeqmakgekprydgrcrhshehhaddepcvvrfanpqegsvvfddqirgpie 161
Cdd:cd00418 81 YRAYAEELIKKG-------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 162 fsnqelddliirrtdGSPTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVPVYAHVSMINGDDGKKLSKR 241
Cdd:cd00418 93 ---------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDGTKLSKR 157
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130330 242 HGAVSVMQYRDDGYLPEALLNYLVRLGWSHGD-QEIFTREEMIKYFTLNAVSKSASAFNTDKLLWLNHHYIN 312
Cdd:cd00418 158 KLNTTLRALRRRGYLPEALRNYLALIGWSKPDgHELFTLEEMIAAFSVERVNSADATFDWAKLEWLNREYIR 229
|
|
| Anticodon_2 |
pfam19269 |
Anticodon binding domain; This entry represents the anticodon binding domain found at the ... |
319-461 |
1.45e-43 |
|
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: 150.42 E-value: 1.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 319 VATHLQWHIEQENIDTRNGPQLADLVKLLGERCKTLKEMAQSCRYFYEDFAEFDADAAKKH----LRPVARQPLEVVRDK 394
Cdd:pfam19269 2 LAELALPYLEEAGLDGLDDEYLKKVVPLLKERAETLSELAELADFFFELPLEYDEEAYAKKkmktNKEESLEVLQELLPR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130330 395 LAAITDWTAENVHHAIQATADELEVGMGKVGMPLRVAVTGAGQSPALDVTVHAIGKTRSIERINKAL 461
Cdd:pfam19269 82 LEALEDWTAEALEAALKALAEELGVKNGKVMWPLRVALTGKTVSPGLFEIMEILGKEETLARLRKAI 148
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
2-268 |
3.02e-41 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 155.01 E-value: 3.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLE--RSTPEAIEAIMDGMNWLSLEWDEgPYYQTKRF 79
Cdd:PRK04156 101 KVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKWDE-VVIQSDRL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 80 DRYNAVIDQMLEEGTAYKCYCSKERLEALREEQmakgekprydgrcrhshehhaddEPCVVRFANPQEGSVVFDDQIRGp 159
Cdd:PRK04156 180 EIYYEYARKLIEMGGAYVCTCDPEEFKELRDAG-----------------------KPCPHRDKSPEENLELWEKMLDG- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 160 iEFSNQE---------------LDDLIIRRTD-------GS-----PTYNFCVVVDDWDMEITHVIRGEDHINNTPRQIN 212
Cdd:PRK04156 236 -EYKEGEavvrvktdlehpnpsVRDWVAFRIVktphprvGDkyrvwPTYNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRY 314
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130330 213 ILKALKAPVPVYAH---VSMingdDGKKLSKR--HGAVSVMQY--RDD------------GYLPEALLNYLVRLG 268
Cdd:PRK04156 315 IYDYFGWEYPETIHygrLKI----EGFVLSTSkiRKGIEEGEYsgWDDprlptlralrrrGILPEAIRELIIEVG 385
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
2-273 |
4.23e-36 |
|
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: 140.34 E-value: 4.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDEgPYYQTKRFDR 81
Cdd:TIGR00463 93 EVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDE-VVYQSDRIET 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 82 YNAVIDQMLEEGTAYKCYCSKERleaLREEQMaKGEKprydgrCRHSHEHHADDEPCVVRFANPQE--GSVVFddQIRGP 159
Cdd:TIGR00463 172 YYDYTRKLIEMGKAYVCDCRPEE---FRELRN-RGEA------CHCRDRSVEENLERWEEMLEGKEegGSVVV--RVKTD 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 160 IEFSNQELDDLIIRRTD-------GS-----PTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVPVYAHV 227
Cdd:TIGR00463 240 LKHKNPAIRDWVIFRIVktphprtGDkyrvyPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYFGWEPPEFIHW 319
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130330 228 SMINGDDGKKLS---KRHGAV-------------SVMQYRDDGYLPEALLNYLVRLGWSHGD 273
Cdd:TIGR00463 320 GRLKIDDVRALStssARKGILrgeysgwddprlpTLRAIRRRGIRPEAIRKFMLSIGVKIND 381
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
2-276 |
3.99e-34 |
|
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: 128.24 E-value: 3.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTP--EAIEAIMDGMNWLSLEWDEgPYYQTKRF 79
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPdpEAYDMIPEDLEWLGVKWDE-VVIASDRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 80 DRYNAVIDQMLEEGTAYkcycskerlealreeqmakgekprydgrcrhshehhaddepcvvrfANPQEGS--VVFddqir 157
Cdd:cd09287 80 ELYYEYARKLIEMGGAY----------------------------------------------VHPRTGSkyRVW----- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 158 gpiefsnqelddliirrtdgsPTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVPVYAHVSMINGDDGK- 236
Cdd:cd09287 109 ---------------------PTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIHWGRLKIEGGKl 167
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 16130330 237 KLSKRHGAVSVMQY--RDD------------GYLPEALLNYLVRLGWSHGDQEI 276
Cdd:cd09287 168 STSKIRKGIESGEYegWDDprlptlralrrrGIRPEAIRDFIIEVGVKQTDATI 221
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
2-147 |
1.00e-20 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 95.56 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDEGPYYQTKRFDR 81
Cdd:PRK14703 31 RVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDWGEHLYYASDYFER 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 82 YNAVIDQMLEEGTAYKCYCSKERLEALR-----------------EE------QMAKGEKPryDG--------------- 123
Cdd:PRK14703 111 MYAYAEQLIKMGLAYVDSVSEEEIRELRgtvtepgtpspyrdrsvEEnldlfrRMRAGEFP--DGahvlrakidmsspnm 188
|
170 180 190
....*....|....*....|....*....|....*
gi 16130330 124 --------RCRHSHEHHADDEPCV---VRFANPQE 147
Cdd:PRK14703 189 klrdpllyRIRHAHHYRTGDEWCIypmYDFAHPLE 223
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
2-318 |
1.86e-18 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 88.10 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDEGPYYQTKRFDR 81
Cdd:PTZ00402 52 KVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTYSSDYMDL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 82 YNAVIDQMLEEGTAykcYCSKerleALREEQmakgEKPRYDGRcrhshehhaddePCVVRFANPQEGSVVFDDQIRG--- 158
Cdd:PTZ00402 132 MYEKAEELIKKGLA---YCDK----TPREEM----QKCRFDGV------------PTKYRDISVEETKRLWNEMKKGsae 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 159 ----------PIEFSNQELDDLIIRRTD------------GSPTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKA 216
Cdd:PTZ00402 189 gqetclrakiSVDNENKAMRDPVIYRVNltpharqgtkykAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 217 LKAPVPVYAHVSMINGD----DGKKLSKRHGAvSVMQYRDDGYLPEalLNYLVRLGwshgdqeiFTREEMIKYFTLNAVS 292
Cdd:PTZ00402 269 LGIRKPIVEDFSRLNMEysvmSKRKLTQLVDT-HVVDGWDDPRFPT--VRALVRRG--------LKMEALRQFVQEQGMS 337
|
330 340
....*....|....*....|....*.
gi 16130330 293 KSASAFNTDKLLWLNHHYINALPPEY 318
Cdd:PTZ00402 338 KTVNFMEWSKLWYFNTQILDPSVPRY 363
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
2-96 |
3.31e-17 |
|
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: 80.76 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDEgPYYQTKRFDR 81
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYK-VTYASDYFDQ 79
|
90
....*....|....*
gi 16130330 82 YNAVIDQMLEEGTAY 96
Cdd:cd00807 80 LYEYAEQLIKKGKAY 94
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
2-126 |
2.39e-13 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 72.45 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDEgPYYQTKRFDR 81
Cdd:PLN02907 213 KVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDA-VTYTSDYFPQ 291
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 16130330 82 YNAVIDQMLEEGtayKCYCSKERLEALREEQMAKGEKprydgRCR 126
Cdd:PLN02907 292 LMEMAEKLIKEG---KAYVDDTPREQMRKERMDGIES-----KCR 328
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
2-241 |
3.09e-12 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 68.50 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDEgPYYQTKRFDR 81
Cdd:PLN03233 11 QIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDS-VSFTSDYFEP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 82 YNAVIDQMLEEGTAYkcycskerLEALREEQMAKgekprydGRCRHSHEHHaddepcvvRFANPQEGSVVFDDQ------ 155
Cdd:PLN03233 90 IRCYAIILIEEGLAY--------MDDTPQEEMKK-------ERADRAESKH--------RNQSPEEALEMFKEMcsgkee 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 156 -----IRGPIEFS--NQELDDLIIRRTDGS------------PTYNF-CVVVDDWDmEITHVIRGEDHINNTPRQINILK 215
Cdd:PLN03233 147 ggawcLRAKIDMQsdNGTLRDPVLFRQNTTphhrsgtaykayPTYDLaCPIVDSIE-GVTHALRTTEYDDRDAQFFWIQK 225
|
250 260
....*....|....*....|....*....
gi 16130330 216 ALKAPVP---VYAHVSMINgddgKKLSKR 241
Cdd:PLN03233 226 ALGLRRPrihAFARMNFMN----TVLSKR 250
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
2-147 |
3.76e-12 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 68.21 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDEGPYYQTKRFDR 81
Cdd:PRK05347 29 RVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWSGELRYASDYFDQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 82 -YNAVIdQMLEEGTAYKCYCSKERLEALR-----------------EE------QMAKGEKPryDG-------------- 123
Cdd:PRK05347 109 lYEYAV-ELIKKGKAYVDDLSAEEIREYRgtltepgknspyrdrsvEEnldlfeRMRAGEFP--EGsavlrakidmaspn 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 16130330 124 ---------RCRHSHEHHADDEPCV---VRFANPQE 147
Cdd:PRK05347 186 inmrdpvlyRIRHAHHHRTGDKWCIypmYDFAHCIS 221
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
2-113 |
7.80e-12 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 67.48 E-value: 7.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEwdegPYYQTKRFDR 81
Cdd:PLN02859 264 KVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMGWE----PFKITYTSDY 339
|
90 100 110
....*....|....*....|....*....|....*
gi 16130330 82 YNAVID---QMLEEGTAYKCYCSKERLEALREEQM 113
Cdd:PLN02859 340 FQELYElavELIRRGHAYVDHQTPEEIKEYREKKM 374
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
6-112 |
1.54e-11 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 66.54 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 6 RFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDeGPYYQTKRFDRYNAV 85
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKPD-WVTFSSDYFDQLHEF 133
|
90 100
....*....|....*....|....*..
gi 16130330 86 IDQMLEEGTAYKCYCSKERLEALREEQ 112
Cdd:PTZ00437 134 AVQLIKDGKAYVDHSTPDELKQQREQR 160
|
|
| lysK |
PRK00750 |
lysyl-tRNA synthetase; Reviewed |
349-461 |
1.97e-03 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234829 [Multi-domain] Cd Length: 510 Bit Score: 40.57 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 349 ERCKTLKEMAQSCRYFYEDFAEfdADAAKKHLRPVARQPLEVVRDKLAAITD-WTAENVHHAIqatadeLEVGMGKVGMP 427
Cdd:PRK00750 397 ETHPRLDRLVEYAINWYRDFVA--PEKKYRAPTEKERAALEDLDDALRELADgADAEEIQNEI------YEVAKKELGVN 468
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 16130330 428 LRVAVT-------GAGQSPALDVTVHAIGKTRSIERINKAL 461
Cdd:PRK00750 469 PRDWFKalyevllGQSQGPRLGSFIALLGIDFVIALIREAL 509
|
|
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
166-243 |
2.88e-03 |
|
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439789 [Multi-domain] Cd Length: 574 Bit Score: 40.13 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 166 ELDDLIIRRTDGSPTY---------------NFCVVVDDWdmeithvirGEDHINNTPRQINILKAL-KAPVPVYAHVS- 228
Cdd:COG0018 299 DDKDRVLVKSDGTYTYfttdiayhlykferyGFDRVIYVV---------GADQHGHFKRLFAALKALgYDPAKDLEHLLf 369
|
90
....*....|....*.
gi 16130330 229 -MINGDDGKKLSKRHG 243
Cdd:COG0018 370 gMVNLRDGEKMSTRAG 385
|
|
| BRCT_Bard1_rpt1 |
cd17734 |
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ... |
184-217 |
3.11e-03 |
|
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the first BRCT domain.
Pssm-ID: 349366 Cd Length: 80 Bit Score: 36.42 E-value: 3.11e-03
10 20 30
....*....|....*....|....*....|....
gi 16130330 184 CVVVDDWDMEITHVIRGEDHINNTPRQINILKAL 217
Cdd:cd17734 25 AKVVTEFSPEVTHVVVPADERGVCPRTMKYLMGI 58
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
169-243 |
7.43e-03 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 38.60 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130330 169 DLIIRRTDGSPTY-------------NFCVVVDDWdmeithvirGEDHINNTPRQINILKAL---KAPVPVYAH--VSMI 230
Cdd:PRK01611 245 DRVLIKSDGTYTYftrdiayhlykfeRFDRVIYVV---------GADHHGHFKRLKAALKALgydPDALEVLLHqmVGLV 315
|
90
....*....|...
gi 16130330 231 NGDDGKKLSKRHG 243
Cdd:PRK01611 316 RGGEGVKMSTRAG 328
|
|
| |
