|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
5-676 |
0e+00 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 845.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 5 LRVSETVAFTDVNSILRYLARIATTSGLYGTNLMEHTEIDHWLEFSATkLSSCDRLTSAINELNHCLSLRTYLVGNSLTL 84
Cdd:PLN02907 41 LLFSSGEKLTGTNVLLRYIARSASLPGFYGQDAFESSQVDEWLDYAPT-FSSGSEFENACEYVDGYLASRTFLVGYSLTI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 85 ADLCVWATLKGSAAWQEHLKQNKTLVHVKRWFGFLEAQQAFRSVGTKWDVSGNRATVAP---------------DKKQDV 149
Cdd:PLN02907 120 ADIAIWSGLAGSGQRWESLRKSKKYQNLVRWFNSISAEYSDILNEVTAAYVGKRGAGKPaaakskekvadagkaDGAKDK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 150 GKF-VELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKP 228
Cdd:PLN02907 200 GSFeVDLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKY 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 229 DQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRTESKHRKNSVEKNLQMWEEMKKGSQFGQSCCLRAKID 308
Cdd:PLN02907 280 DAVTYTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMDGIESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLD 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 309 MSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEY 388
Cdd:PLN02907 360 MQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLRKVHIWEF 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 389 SRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPV 468
Cdd:PLN02907 440 SRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKIIDPV 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 469 APRYVALLKKEVVPVNVLD--AQEEMKEVARHPKNPDVGLKPVWYSPKVFIEGADAETFSEGEMVTFINWGNINITKIHK 546
Cdd:PLN02907 520 CPRHTAVLKEGRVLLTLTDgpETPFVRIIPRHKKYEGAGKKATTFTNRIWLDYADAEAISEGEEVTLMDWGNAIIKEITK 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 547 NADGKITSLDAKLNLENkDYKKTT-KITWLAEsTHALsIPAVCVTYEHLITKPVLGKDEDFKQYINKDSKHEELMLGDPC 625
Cdd:PLN02907 600 DEGGAVTALSGELHLEG-SVKTTKlKLTWLPD-TNEL-VPLSLVEFDYLITKKKLEEDDNFLDVLNPCTKKETAALGDSN 676
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 66267550 626 LKDLKKGDIIQLQRRGFFICDQPYEPVSpyscreAPCILIYIPDGHTKEMP 676
Cdd:PLN02907 677 MRNLKRGEIIQLERKGYYRCDAPFVRSS------KPIVLFAIPDGRQQKSG 721
|
|
| proS_fam_I |
TIGR00408 |
prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ... |
983-1477 |
0e+00 |
|
prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is recognized by pfam model tRNA-synt_2b, which recognizes tRNA synthetases for Gly, His, Ser, and Pro. The prolyl-tRNA synthetases are divided into two widely divergent families. This family includes the archaeal enzyme, the Pro-specific domain of a human multifunctional tRNA ligase, and the enzyme from the spirochete Borrelia burgdorferi. The other family includes enzymes from Escherichia coli, Bacillus subtilis, Synechocystis PCC6803, and one of the two prolyL-tRNA synthetases of Saccharomyces cerevisiae. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273062 [Multi-domain] Cd Length: 472 Bit Score: 567.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 983 AKKEENLAEWYSQVITKSEMIEYYDVSGCYILRPWSYSIWESIKDFFDAEIKKLGVENCYFPIFVSQAALEKEKNHIEDF 1062
Cdd:TIGR00408 2 ASKMQDFSEWYHQILEKAEIIDYYPVKGCYVWLPYGFKIWKNIQKILRNILDEIGHEEVYFPMLIPESELAKEKDHIKGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1063 APEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPVRLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFA 1142
Cdd:TIGR00408 82 EPEVYWITHGGLSKLDEPLALRPTSETAMYPMFKKWVKSYTDLPLKINQWVNVFRYETKHTRPFLRTREFTWQEAHTAHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1143 TFEEAADEVLQILELYARVYEELLAIPVVRGRKTEKEKFAGGDYTTTIEAfISASGRAIQGATSHHLGQNFSKMCEIVFE 1222
Cdd:TIGR00408 162 TAEEAEEQVLRALDIYKEFIENSLAIPYFVGRKPEWEKFAGAEYTWAFET-IMPDGRTLQIATSHNLGQNFAKTFEIKFE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1223 DPKtpGEKQFAYQCSWGLTTRTIGVMVMVHGDSMGLVLPPRVASVQVVVIPCgitnALSEEDREALMAKCNEYRRRLLGA 1302
Cdd:TIGR00408 241 TPT--GDKEYAYQTSYGISTRVIGALIAIHSDEKGLVLPPRVAPIQVVIIPI----IFKKKENEKVMEAAREVRSRLKKA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1303 NIRVRVDLRDNySPGWKFNHWELKGVPVRLEVGPRDMKSCQFVAVRRDTGEKLTIAEKEAEAKLEKVLEDIQLNLFTRAS 1382
Cdd:TIGR00408 315 GFRVHIDDRDN-RPGRKFYQWEIKGIPLRIEVGPNDIEKNIAVISRRDTGEKYQVSLDQLEERVVELLNNIQENLRNRAW 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1383 EDLKTHMVVSNTLEDFQKVL-DAGKVAQIPFCGEIDCEDWIKKMTArdqdvepgapsmgAKSLCIPFnplcELQPGAMCV 1461
Cdd:TIGR00408 394 ERFEQKIVIVETLEEIKQALnEKRGVVLVPWCGEEECEEDLKEKVQ-------------VTILCIPE----DGDVLQLCI 456
|
490
....*....|....*.
gi 66267550 1462 CGKNPAKFYTLFGRSY 1477
Cdd:TIGR00408 457 FCGRKAPDYVLIARTY 472
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
988-1251 |
5.01e-166 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from archaea, the cytoplasm of eukaryotes and some bacteria.
Pssm-ID: 238401 [Multi-domain] Cd Length: 261 Bit Score: 498.66 E-value: 5.01e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 988 NLAEWYSQVITKSEMIEYYDVSGCYILRPWSYSIWESIKDFFDAEIKKLGVENCYFPIFVSQAALEKEKNHIEDFAPEVA 1067
Cdd:cd00778 1 DFSEWYTEVITKAELIDYGPVKGCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPESELEKEKEHIEGFAPEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1068 WVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPVRLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATFEEA 1147
Cdd:cd00778 81 WVTHGGLEELEEPLALRPTSETAIYPMFSKWIRSYRDLPLKINQWVNVFRWETKTTRPFLRTREFLWQEGHTAHATEEEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1148 ADEVLQILELYARVYEELLAIPVVRGRKTEKEKFAGGDYTTTIEAFISaSGRAIQGATSHHLGQNFSKMCEIVFEDPKtp 1227
Cdd:cd00778 161 EEEVLQILDLYKEFYEDLLAIPVVKGRKTEWEKFAGADYTYTIEAMMP-DGRALQSGTSHNLGQNFSKAFDIKYQDKD-- 237
|
250 260
....*....|....*....|....
gi 66267550 1228 GEKQFAYQCSWGLTTRTIGVMVMV 1251
Cdd:cd00778 238 GQKEYVHQTSWGISTRLIGAIIMI 261
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
162-467 |
1.76e-156 |
|
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: 475.66 E-value: 1.76e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 162 KVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPD-QFTYTSDHFET 240
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDyGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 241 IMKYAEKLIQEGKAYVDDTPAEQMKAEREQ--RTESKHRKNSVEKNLQMW-EEMKKGSQFGQSCCLRAKIDMSSnNGCMR 317
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEqeALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMES-PYVFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 318 DPTLYRCKIQP---HPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIR-KPYIWEYSRLNL 393
Cdd:pfam00749 160 DPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66267550 394 NNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSV-VNMEWDKIWAFNKKVIDP 467
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFdVNRLSKSLEAFDRKKLDW 314
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
138-655 |
3.73e-144 |
|
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: 452.74 E-value: 3.73e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 138 RATVAPDKKQDVGKF-VELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKV 216
Cdd:TIGR00463 68 RLGLDIKKKEKKRKGlRELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDM 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 217 ILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRTESKHRKNSVEKNLQMWEEMKKGSQ 296
Cdd:TIGR00463 148 ILEDLEWLGVKWDEVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNRGEACHCRDRSVEENLERWEEMLEGKE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 297 FGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHD--RDEQFYWI 374
Cdd:TIGR00463 228 EGGSVVVRVKTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDnrRKQEYIYR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 375 IEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVnEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEW 454
Cdd:TIGR00463 308 YFGWEPPEFIHWGRLKIDDVRALSTSSARKGIL-RGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSW 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 455 DKIWAFNKKVIDPVAPRYVALlkkeVVPVNV-LDAQEEMKEVAR--HPKNPDVGLKPVWYSPKVFIEGADAETfsEGEMV 531
Cdd:TIGR00463 387 KNIYALNRKIIDEEARRYFFI----WNPVKIeIVGLPEPKRVERplHPDHPEIGERVLILRGEIYVPKDDLEE--GVEPV 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 532 TFINWGNINITKIHknadgkitSLDAKLNLENKDYKKTTKITWLAESThalSIPAVCVTYEHLITKPVLGKDEDFkqyin 611
Cdd:TIGR00463 461 RLMDAVNVIYSKKE--------LRYHSEGLEGARKLGKSIIHWLPAKD---AVKVKVIMPDASIVEGVIEADASE----- 524
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 66267550 612 kdskheelmlgdpclkdLKKGDIIQLQRRGFFICDQPYEPVSPY 655
Cdd:TIGR00463 525 -----------------LEVGDVVQFERFGFARLDSADKDGMVF 551
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
162-471 |
3.43e-135 |
|
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: 415.88 E-value: 3.43e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 162 KVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETI 241
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 242 MKYAEKLIQEGKAYVddtpaeqmkaereqrteskhrknsveknlqmweemkkgsqfgqscclrakidmssnngcmrdptl 321
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 322 yrckiqpHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKR 401
Cdd:cd00807 96 -------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKR 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 402 KLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPR 471
Cdd:cd00807 169 KLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
975-1370 |
6.30e-90 |
|
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440211 [Multi-domain] Cd Length: 564 Bit Score: 304.00 E-value: 6.30e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 975 KQTRLGLEAKKE--ENLAEWYSQVITKSEMIEYYdVSGCYILRPWSYSIWESIKDFFDAEIKKLGVENCYFPIFVSqAAL 1052
Cdd:COG0442 2 RASKLFIPTLKErpADAEVWSHQLMLRAGLIRKL-ASGIYTYLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQP-AEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1053 EKEKNHIEDFAPEVAWVtrsgKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPVRLNQWCNVVRWEFKHPQPFLRTREF 1132
Cdd:COG0442 80 WEESGRWEGFGPELARV----TDRLEREFCLGPTHEEVITDLVRNEIKSYRDLPLLLYQIQTKFRDEIRPRFGLLRTREF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1133 LWQEGHSAFATFEEAADEVLQILELYARVYEElLAIPVVRGRKT-------EKEKFA--------------GGDY----- 1186
Cdd:COG0442 156 LMKDAYSFHATEEELDEEYQKMLDAYERIFER-LGLPVRAVEADsgaiggsESHEFMvladsgedtivycdACDYaanie 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1187 -------------------------TTTIEA------------------------------------------------- 1192
Cdd:COG0442 235 kaealappaeraeptkeleavatpgAKTIEEvaeflgvpaektvktlvykadgelvavlvrgdhelneiklenllgasel 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1193 -----------------FISASG--------------------------------------------------------- 1198
Cdd:COG0442 315 elateeeieaalgavpgFLGPVGlgvpyiadrsvagmsnfvcganeddyhytnvnwgrdfpvdevadlrnvvegdpcpdc 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1199 -------RAIQGATSHHLGQNFSKMCEIVFEDPKtpGEKQFAYQCSWGLT-TRTIGVMVMVHGDSMGLVLPPRVASVQVV 1270
Cdd:COG0442 395 ggllqdgRGIEVGHIFKLGTKYSKAMDATFLDEN--GKEQPVWMGCYGIGvTRLIAAAIEQHHDDKGIIWPPAIAPFQVV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1271 VIPCGITNalseedrEALMAKCNEYRRRLLGANIRVRVDLRDNySPGWKFNHWELKGVPVRLEVGPRDMKSCQFVAVRRD 1350
Cdd:COG0442 473 IVPINMKD-------EAVLEAAEELYAELKAAGIDVLLDDRDE-RPGVKFADAELIGIPLRIVIGPRDLEEGQVEVKRRD 544
|
570 580
....*....|....*....|
gi 66267550 1351 TGEKLTIAEKEAEAKLEKVL 1370
Cdd:COG0442 545 TGEKEEVPLDELVETVKELL 564
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
161-448 |
2.36e-65 |
|
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: 229.68 E-value: 2.36e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 161 GKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQ-FTYTSDHFE 239
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEgPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 240 TIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRTESK--------HRKNSVEKNLQMWEEmkkgsqfGQSCCLRAKI---- 307
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGkpprydgrCRDLSPEELERMLAA-------GEPPVLRFKIpeeg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 308 ----DMSS-----NNGCMRDPTLYRckiqphpRTGnkynvYPTYDFACPIVDSIEGVTHALRT------TEYHDrdeqfy 372
Cdd:COG0008 156 vvfdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGeehlsnTPRQI------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 373 WIIEALGIRKPyiwEYSRLNL----NNTVLSKRKltwfvneGLVdgwddprfpTVRGVLRRGMTVEGLKQFIAAQGSSRS 448
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLilgpDGTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
718-767 |
2.27e-23 |
|
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 94.22 E-value: 2.27e-23
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 66267550 718 LYSRVAVQGDVVRELKAKKAPKEDIDAAVKQLLTLKAEYKEKTGQEYKPG 767
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
|
|
| ProRS-C_1 |
pfam09180 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
1395-1477 |
1.87e-22 |
|
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.
Pssm-ID: 462709 Cd Length: 67 Bit Score: 92.20 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1395 LEDFQKVLDAGKVAQIPFCGEIDCEDWIKKMTardqdvepgapsmGAKSLCIPFNplcELQPGAMCVCGKNPAKFYTLFG 1474
Cdd:pfam09180 1 WEEFKEALEEKGFVLAPWCGDEECEDKIKEET-------------GATSRCIPFD---QEEEGGKCIVCGKPAKKWVLFA 64
|
...
gi 66267550 1475 RSY 1477
Cdd:pfam09180 65 RSY 67
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
718-770 |
2.12e-22 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 91.40 E-value: 2.12e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 66267550 718 LYSRVAVQGDVVRELKAKKAPKEDIDAAVKQLLTLKAEYKEKTGQEYKPGNPS 770
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
791-840 |
1.81e-21 |
|
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 88.83 E-value: 1.81e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 66267550 791 LYNKVAAQGEVVRKLKAEKAPKAKVTEAVECLLSLKAEYKEKTGKDYVPG 840
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
869-921 |
7.93e-21 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 87.16 E-value: 7.93e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 66267550 869 LFDRVACQGEVVRKLKAEKASKDQVDSAVQELLQLKAQYKSLTGIEYKPVSAT 921
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
791-843 |
8.25e-21 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 86.78 E-value: 8.25e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 66267550 791 LYNKVAAQGEVVRKLKAEKAPKAKVTEAVECLLSLKAEYKEKTGKDYVPGQPP 843
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
719-773 |
1.47e-20 |
|
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.
Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 86.24 E-value: 1.47e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 66267550 719 YSRVAVQGDVVRELKAKKAPKEDIDAAVKQLLTLKAEYKEKTGQEYKPGNPSAAA 773
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGDT 55
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
869-917 |
7.05e-20 |
|
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 84.21 E-value: 7.05e-20
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 66267550 869 LFDRVACQGEVVRKLKAEKASKDQVDSAVQELLQLKAQYKSLTGIEYKP 917
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKP 49
|
|
| ProRS-C_1 |
smart00946 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
1395-1477 |
1.66e-19 |
|
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.
Pssm-ID: 198014 Cd Length: 67 Bit Score: 83.77 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1395 LEDFQKVLDAGKVAQIPFCGEIDCEDWIKKMTardqdvepgapsmGAKSLCIPFNplcELQPGAMCVCGKNPAKFYTLFG 1474
Cdd:smart00946 1 LEEFKKALEEGKFVLAPWCGDEECEEKIKEET-------------GATIRCIPFD---QDEEPGKCVVCGKPAKKWVLFA 64
|
...
gi 66267550 1475 RSY 1477
Cdd:smart00946 65 RSY 67
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
792-846 |
3.42e-19 |
|
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.
Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 82.39 E-value: 3.42e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 66267550 792 YNKVAAQGEVVRKLKAEKAPKAKVTEAVECLLSLKAEYKEKTGKDYVPGQPPASQ 846
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGDT 55
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
870-923 |
2.07e-18 |
|
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.
Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 80.08 E-value: 2.07e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 66267550 870 FDRVACQGEVVRKLKAEKASKDQVDSAVQELLQLKAQYKSLTGIEYKPVSATGA 923
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGD 54
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
1242-1370 |
2.80e-11 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 68.19 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1242 TRTIGVMVMVHGDSMGLVLPPRVASVQVVVIPcgiTNALSEEDREAlmakCNEYRRRLLGANIRVRVDLRDNySPGWKFN 1321
Cdd:PRK09194 444 SRLVAAAIEQNHDEKGIIWPKAIAPFDVHIVP---VNMKDEEVKEL----AEKLYAELQAAGIEVLLDDRKE-RPGVKFA 515
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 66267550 1322 HWELKGVPVRLEVGPRDMKSCQFVAVRRDTGEKLTIAEKEAEAKLEKVL 1370
Cdd:PRK09194 516 DADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELVEFLKALK 564
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
716-787 |
3.35e-06 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 51.67 E-value: 3.35e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66267550 716 SVLYSRVAVQGDVVRELKAKKAPKEDIDAAVKQL--LTLKAEYKEKTGQEYKPGNPSAAAVQTVSTKSSSNTVE 787
Cdd:PLN02734 10 AEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLkaLKLEKSALEKELQAAVGAGGDGAASKEAFRQAVVNTLE 83
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
869-923 |
5.24e-04 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 44.74 E-value: 5.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 66267550 869 LFDRVACQGEVVRKLKAEKASKDQVDSAVQELLQLKAQYKSLTGIEYKPVSATGA 923
Cdd:PLN02734 12 KQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELQAAVGAGGD 66
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
781-847 |
6.71e-04 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 44.35 E-value: 6.71e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66267550 781 SSSNTVESTSLYNKVAAQGEVVRKLKAEKAPKAKVTEAVECL--LSLKAEYKEKTGKDYVPGQPPASQN 847
Cdd:PLN02734 2 EDSLRDALAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLkaLKLEKSALEKELQAAVGAGGDGAAS 70
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
5-676 |
0e+00 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 845.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 5 LRVSETVAFTDVNSILRYLARIATTSGLYGTNLMEHTEIDHWLEFSATkLSSCDRLTSAINELNHCLSLRTYLVGNSLTL 84
Cdd:PLN02907 41 LLFSSGEKLTGTNVLLRYIARSASLPGFYGQDAFESSQVDEWLDYAPT-FSSGSEFENACEYVDGYLASRTFLVGYSLTI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 85 ADLCVWATLKGSAAWQEHLKQNKTLVHVKRWFGFLEAQQAFRSVGTKWDVSGNRATVAP---------------DKKQDV 149
Cdd:PLN02907 120 ADIAIWSGLAGSGQRWESLRKSKKYQNLVRWFNSISAEYSDILNEVTAAYVGKRGAGKPaaakskekvadagkaDGAKDK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 150 GKF-VELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKP 228
Cdd:PLN02907 200 GSFeVDLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKY 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 229 DQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRTESKHRKNSVEKNLQMWEEMKKGSQFGQSCCLRAKID 308
Cdd:PLN02907 280 DAVTYTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMDGIESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLD 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 309 MSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEY 388
Cdd:PLN02907 360 MQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLRKVHIWEF 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 389 SRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPV 468
Cdd:PLN02907 440 SRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKIIDPV 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 469 APRYVALLKKEVVPVNVLD--AQEEMKEVARHPKNPDVGLKPVWYSPKVFIEGADAETFSEGEMVTFINWGNINITKIHK 546
Cdd:PLN02907 520 CPRHTAVLKEGRVLLTLTDgpETPFVRIIPRHKKYEGAGKKATTFTNRIWLDYADAEAISEGEEVTLMDWGNAIIKEITK 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 547 NADGKITSLDAKLNLENkDYKKTT-KITWLAEsTHALsIPAVCVTYEHLITKPVLGKDEDFKQYINKDSKHEELMLGDPC 625
Cdd:PLN02907 600 DEGGAVTALSGELHLEG-SVKTTKlKLTWLPD-TNEL-VPLSLVEFDYLITKKKLEEDDNFLDVLNPCTKKETAALGDSN 676
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 66267550 626 LKDLKKGDIIQLQRRGFFICDQPYEPVSpyscreAPCILIYIPDGHTKEMP 676
Cdd:PLN02907 677 MRNLKRGEIIQLERKGYYRCDAPFVRSS------KPIVLFAIPDGRQQKSG 721
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
155-675 |
0e+00 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 599.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 155 LPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYT 234
Cdd:PLN03233 4 LEGAIAGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 235 SDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRTESKHRKNSVEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNG 314
Cdd:PLN03233 84 SDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKERADRAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQSDNG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 315 CMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLN 394
Cdd:PLN03233 164 TLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARMNFM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 395 NTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVA 474
Cdd:PLN03233 244 NTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRFMA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 475 LLKKEVVPVNVLDAQEE----MKEVARHPKNPDVGLKPVWYSPKVFIEGADAETFSEGEMVTFINWGNINITKIHKNADG 550
Cdd:PLN03233 324 IDKADHTALTVTNADEEadfaFSETDCHPKDPGFGKRAMRICDEVLLEKADTEDIQLGEDIVLLRWGVIEISKIDGDLEG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 551 KItsldaklnLENKDYKKTT-KITWLAESTHalSIPAVCVTYEHLITKPVLGKDEDFKQYINKDSKHEELMLGDPCLKDL 629
Cdd:PLN03233 404 HF--------IPDGDFKAAKkKISWIADVSD--NIPVVLSEFDNLIIKEKLEEDDKFEDFINPDTLAETDVIGDAGLKTL 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 66267550 630 KKGDIIQLQRRGFFICDQPYepVSPyscrEAPCILIYIPDGHTKEM 675
Cdd:PLN03233 474 KEHDIIQLERRGFYRVDRPY--MGE----EKPLILFMIPDGKKKAM 513
|
|
| proS_fam_I |
TIGR00408 |
prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ... |
983-1477 |
0e+00 |
|
prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is recognized by pfam model tRNA-synt_2b, which recognizes tRNA synthetases for Gly, His, Ser, and Pro. The prolyl-tRNA synthetases are divided into two widely divergent families. This family includes the archaeal enzyme, the Pro-specific domain of a human multifunctional tRNA ligase, and the enzyme from the spirochete Borrelia burgdorferi. The other family includes enzymes from Escherichia coli, Bacillus subtilis, Synechocystis PCC6803, and one of the two prolyL-tRNA synthetases of Saccharomyces cerevisiae. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273062 [Multi-domain] Cd Length: 472 Bit Score: 567.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 983 AKKEENLAEWYSQVITKSEMIEYYDVSGCYILRPWSYSIWESIKDFFDAEIKKLGVENCYFPIFVSQAALEKEKNHIEDF 1062
Cdd:TIGR00408 2 ASKMQDFSEWYHQILEKAEIIDYYPVKGCYVWLPYGFKIWKNIQKILRNILDEIGHEEVYFPMLIPESELAKEKDHIKGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1063 APEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPVRLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFA 1142
Cdd:TIGR00408 82 EPEVYWITHGGLSKLDEPLALRPTSETAMYPMFKKWVKSYTDLPLKINQWVNVFRYETKHTRPFLRTREFTWQEAHTAHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1143 TFEEAADEVLQILELYARVYEELLAIPVVRGRKTEKEKFAGGDYTTTIEAfISASGRAIQGATSHHLGQNFSKMCEIVFE 1222
Cdd:TIGR00408 162 TAEEAEEQVLRALDIYKEFIENSLAIPYFVGRKPEWEKFAGAEYTWAFET-IMPDGRTLQIATSHNLGQNFAKTFEIKFE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1223 DPKtpGEKQFAYQCSWGLTTRTIGVMVMVHGDSMGLVLPPRVASVQVVVIPCgitnALSEEDREALMAKCNEYRRRLLGA 1302
Cdd:TIGR00408 241 TPT--GDKEYAYQTSYGISTRVIGALIAIHSDEKGLVLPPRVAPIQVVIIPI----IFKKKENEKVMEAAREVRSRLKKA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1303 NIRVRVDLRDNySPGWKFNHWELKGVPVRLEVGPRDMKSCQFVAVRRDTGEKLTIAEKEAEAKLEKVLEDIQLNLFTRAS 1382
Cdd:TIGR00408 315 GFRVHIDDRDN-RPGRKFYQWEIKGIPLRIEVGPNDIEKNIAVISRRDTGEKYQVSLDQLEERVVELLNNIQENLRNRAW 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1383 EDLKTHMVVSNTLEDFQKVL-DAGKVAQIPFCGEIDCEDWIKKMTArdqdvepgapsmgAKSLCIPFnplcELQPGAMCV 1461
Cdd:TIGR00408 394 ERFEQKIVIVETLEEIKQALnEKRGVVLVPWCGEEECEEDLKEKVQ-------------VTILCIPE----DGDVLQLCI 456
|
490
....*....|....*.
gi 66267550 1462 CGKNPAKFYTLFGRSY 1477
Cdd:TIGR00408 457 FCGRKAPDYVLIARTY 472
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
137-702 |
0e+00 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 562.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 137 NRATVAPDKKQDVGKfVELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKV 216
Cdd:PTZ00402 28 NTYFTAANANEENDK-LQLTNAEEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 217 ILEDVAMLHIKPDQF-TYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRTESKHRKNSVEKNLQMWEEMKKGS 295
Cdd:PTZ00402 107 ILDDLATLGVSWDVGpTYSSDYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFDGVPTKYRDISVEETKRLWNEMKKGS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 296 QFGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWII 375
Cdd:PTZ00402 187 AEGQETCLRAKISVDNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFC 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 376 EALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWD 455
Cdd:PTZ00402 267 DALGIRKPIVEDFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWS 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 456 KIWAFNKKVIDPVAPRYVALLKKEVVPVNVlDAQEEMKEVAR--HPKNPDVGLKPVWYSPKVFIEGADAETFSEGEMVTF 533
Cdd:PTZ00402 347 KLWYFNTQILDPSVPRYTVVSNTLKVRCTV-EGQIHLEACEKllHKKVPDMGEKTYYKSDVIFLDAEDVALLKEGDEVTL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 534 INWGNINITKIHK-NADGKITSLDAKLNLENkDYKKTT-KITWLAESTHALSIpaVCVTYEHLITKPVLGKDEDFKQYIN 611
Cdd:PTZ00402 426 MDWGNAYIKNIRRsGEDALITDADIVLHLEG-DVKKTKfKLTWVPESPKAEVM--ELNEYDHLLTKKKPDPEESIDDIIA 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 612 KDSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDQPyepvspyscrEAPCILIYIPDGHTKEMPTSGSKEKTKVeISKK 691
Cdd:PTZ00402 503 PVTKYTQEVYGEEALSVLKKGDIIQLERRGYYIVDDV----------TPKKVLIAIPDGREKVNHLSAKAQYLKT-LPKK 571
|
570
....*....|.
gi 66267550 692 ETSSAPKERPA 702
Cdd:PTZ00402 572 GIASAANDLAA 582
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
988-1251 |
5.01e-166 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from archaea, the cytoplasm of eukaryotes and some bacteria.
Pssm-ID: 238401 [Multi-domain] Cd Length: 261 Bit Score: 498.66 E-value: 5.01e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 988 NLAEWYSQVITKSEMIEYYDVSGCYILRPWSYSIWESIKDFFDAEIKKLGVENCYFPIFVSQAALEKEKNHIEDFAPEVA 1067
Cdd:cd00778 1 DFSEWYTEVITKAELIDYGPVKGCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPESELEKEKEHIEGFAPEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1068 WVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPVRLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATFEEA 1147
Cdd:cd00778 81 WVTHGGLEELEEPLALRPTSETAIYPMFSKWIRSYRDLPLKINQWVNVFRWETKTTRPFLRTREFLWQEGHTAHATEEEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1148 ADEVLQILELYARVYEELLAIPVVRGRKTEKEKFAGGDYTTTIEAFISaSGRAIQGATSHHLGQNFSKMCEIVFEDPKtp 1227
Cdd:cd00778 161 EEEVLQILDLYKEFYEDLLAIPVVKGRKTEWEKFAGADYTYTIEAMMP-DGRALQSGTSHNLGQNFSKAFDIKYQDKD-- 237
|
250 260
....*....|....*....|....
gi 66267550 1228 GEKQFAYQCSWGLTTRTIGVMVMV 1251
Cdd:cd00778 238 GQKEYVHQTSWGISTRLIGAIIMI 261
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
162-467 |
1.76e-156 |
|
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: 475.66 E-value: 1.76e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 162 KVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPD-QFTYTSDHFET 240
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDyGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 241 IMKYAEKLIQEGKAYVDDTPAEQMKAEREQ--RTESKHRKNSVEKNLQMW-EEMKKGSQFGQSCCLRAKIDMSSnNGCMR 317
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEqeALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMES-PYVFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 318 DPTLYRCKIQP---HPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIR-KPYIWEYSRLNL 393
Cdd:pfam00749 160 DPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66267550 394 NNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSV-VNMEWDKIWAFNKKVIDP 467
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFdVNRLSKSLEAFDRKKLDW 314
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
138-655 |
3.73e-144 |
|
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: 452.74 E-value: 3.73e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 138 RATVAPDKKQDVGKF-VELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKV 216
Cdd:TIGR00463 68 RLGLDIKKKEKKRKGlRELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDM 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 217 ILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRTESKHRKNSVEKNLQMWEEMKKGSQ 296
Cdd:TIGR00463 148 ILEDLEWLGVKWDEVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNRGEACHCRDRSVEENLERWEEMLEGKE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 297 FGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHD--RDEQFYWI 374
Cdd:TIGR00463 228 EGGSVVVRVKTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDnrRKQEYIYR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 375 IEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVnEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEW 454
Cdd:TIGR00463 308 YFGWEPPEFIHWGRLKIDDVRALSTSSARKGIL-RGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSW 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 455 DKIWAFNKKVIDPVAPRYVALlkkeVVPVNV-LDAQEEMKEVAR--HPKNPDVGLKPVWYSPKVFIEGADAETfsEGEMV 531
Cdd:TIGR00463 387 KNIYALNRKIIDEEARRYFFI----WNPVKIeIVGLPEPKRVERplHPDHPEIGERVLILRGEIYVPKDDLEE--GVEPV 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 532 TFINWGNINITKIHknadgkitSLDAKLNLENKDYKKTTKITWLAESThalSIPAVCVTYEHLITKPVLGKDEDFkqyin 611
Cdd:TIGR00463 461 RLMDAVNVIYSKKE--------LRYHSEGLEGARKLGKSIIHWLPAKD---AVKVKVIMPDASIVEGVIEADASE----- 524
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 66267550 612 kdskheelmlgdpclkdLKKGDIIQLQRRGFFICDQPYEPVSPY 655
Cdd:TIGR00463 525 -----------------LEVGDVVQFERFGFARLDSADKDGMVF 551
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
161-651 |
3.62e-138 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 436.46 E-value: 3.62e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 161 GKVTVRFPPEASGYLHIGHAKAALLN----QHYQvnfkGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKP-DQFTYTS 235
Cdd:PRK05347 28 TRVHTRFPPEPNGYLHIGHAKSICLNfglaQDYG----GKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWsGELRYAS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 236 DHFETIMKYAEKLIQEGKAYVDDTPAEQMkaeREQR-------TESKHRKNSVEKNLQMWEEMKKGsQF--GqSCCLRAK 306
Cdd:PRK05347 104 DYFDQLYEYAVELIKKGKAYVDDLSAEEI---REYRgtltepgKNSPYRDRSVEENLDLFERMRAG-EFpeG-SAVLRAK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 307 IDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHD-RdeQFY-WIIEALGIR-KP 383
Cdd:PRK05347 179 IDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDhR--PLYdWVLDNLPIPpHP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 384 YIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSR--SVVNM---Ewdkiw 458
Cdd:PRK05347 257 RQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKqdSVIDMsmlE----- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 459 AFNKKVIDPVAPRYVALLK--KeVVPVNVLDAQEEMKEVARHPKNPDVGLKPVWYSPKVFIEGADaetFSE--------- 527
Cdd:PRK05347 332 SCIREDLNENAPRAMAVLDplK-LVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIERED---FMEeppkkyfrl 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 528 --GEMVTFINWGNINITKIHKNADGKITSL------DAKLNLENKDYK-KTTkITWLaESTHAlsIPAVCVTYEHLITKP 598
Cdd:PRK05347 408 vpGKEVRLRNAYVIKCEEVVKDADGNITEIhctydpDTLSGNPADGRKvKGT-IHWV-SAAHA--VPAEVRLYDRLFTVP 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 66267550 599 VLGKDEDFKQYINKDSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDQPYEP 651
Cdd:PRK05347 484 NPAAGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCADKDSTP 536
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
162-471 |
3.43e-135 |
|
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: 415.88 E-value: 3.43e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 162 KVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETI 241
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 242 MKYAEKLIQEGKAYVddtpaeqmkaereqrteskhrknsveknlqmweemkkgsqfgqscclrakidmssnngcmrdptl 321
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 322 yrckiqpHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKR 401
Cdd:cd00807 96 -------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKR 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 402 KLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPR 471
Cdd:cd00807 169 KLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
163-646 |
2.35e-110 |
|
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam model tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273079 [Multi-domain] Cd Length: 522 Bit Score: 359.62 E-value: 2.35e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 163 VTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPD-QFTYTSDHFETI 241
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEgKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 242 MKYAEKLIQEGKAYVDDTPAEQMKAEREQRTE----SKHRKNSVEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMR 317
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDpgknSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 318 DPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGI-RKPYIWEYSRLNLNNT 396
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIfPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 397 VLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALL 476
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 477 KKEVVPVNVLDAQEEMKEVARHPKNPDVGLKPVWYSPKVFIEGADaetFSE-----------GEMVTFINWGNINITKIH 545
Cdd:TIGR00440 321 DPVEVVIENLSDEYELATIPNHPNTPEFGERQVPFTNEFYIDRAD---FREeankqykrlvlGKEVRLRNAYVIKAERVE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 546 KNADGKITSL----DAK-LNLENKDYKKT-TKITWLAESThalSIPAVCVTYEHLITKPVLGKDEDFKQYINKDSKHEEL 619
Cdd:TIGR00440 398 KDAAGKITTIfctyDNKtLGKEPADGRKVkGVIHWVSASS---KYPTETRLYDRLFKVPNPGAPDDFLSVINPESLVIKQ 474
|
490 500
....*....|....*....|....*..
gi 66267550 620 MLGDPCLKDLKKGDIIQLQRRGFFICD 646
Cdd:TIGR00440 475 GFMEHSLGDAVANKRFQFEREGYFCLD 501
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
161-706 |
5.57e-103 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 347.48 E-value: 5.57e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 161 GKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIK-PDQFTYTSDHFE 239
Cdd:PRK14703 30 PRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDwGEHLYYASDYFE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 240 TIMKYAEKLIQEGKAYVDDTPAEQMkaeREQR-------TESKHRKNSVEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSN 312
Cdd:PRK14703 110 RMYAYAEQLIKMGLAYVDSVSEEEI---RELRgtvtepgTPSPYRDRSVEENLDLFRRMRAGEFPDGAHVLRAKIDMSSP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 313 NGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIR--KPYIWEYSR 390
Cdd:PRK14703 187 NMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPWppRPRQYEFAR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 391 LNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAP 470
Cdd:PRK14703 267 LALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGVLEFAIRDDLNRRAP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 471 RYVALLKK-EVVPVNVLDAQEEMKEVARHPKN-PDVGLKPVWYSPKVFIEGADaetFSE-----------GEMVTFINWG 537
Cdd:PRK14703 347 RVMAVLDPlKVVIENLPAGKVEELDLPYWPHDvPKEGSRKVPFTRELYIERDD---FSEdppkgfkrltpGREVRLRGAY 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 538 NINITKIHKNADGKITSLDAKLNLENKDYKKTTK-----ITWLAeSTHALsiPAVCVTYEHLITKPVL-GKDEDFKQYIN 611
Cdd:PRK14703 424 IIRCDEVVRDADGAVTELRCTYDPESAKGEDTGRkaagvIHWVS-AKHAL--PAEVRLYDRLFKVPQPeAADEDFLEFLN 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 612 KDSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDqpyePVSpySCREAPCI--LIYIPD--GHTKEMPTSGSKEKTKVE 687
Cdd:PRK14703 501 PDSLRVAQGRVEPAVRDDPADTRYQFERQGYFWAD----PVD--SRPDALVFnrIITLKDtwGARAREAAREKRAAAPKK 574
|
570
....*....|....*....
gi 66267550 688 ISKKETSSAPKERPAPAVS 706
Cdd:PRK14703 575 TAKPRRSKAEARAEAAALN 593
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
161-651 |
5.96e-101 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 335.41 E-value: 5.96e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 161 GKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFET 240
Cdd:PTZ00437 50 GKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKPDWVTFSSDYFDQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 241 IMKYAEKLIQEGKAYVDDTPAEQMKAEREQRTESKHRKNSVEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPT 320
Cdd:PTZ00437 130 LHEFAVQLIKDGKAYVDHSTPDELKQQREQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRDFI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 321 LYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSK 400
Cdd:PTZ00437 210 AYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWRPHVWEFSRLNVTGSLLSK 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 401 RKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLKKEV 480
Cdd:PTZ00437 290 RKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVIDPIK 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 481 VPVNVLDAQEEMkEVARHPKNPDVGLKPVWYSPKVFIEGADAET---------FSEGEMVTFINW-GNINITKIHKNADG 550
Cdd:PTZ00437 370 VVVDNWKGEREF-ECPNHPRKPELGSRKVMFTDTFYVDRSDFRTednnskfygLAPGPRVVGLKYsGNVVCKGFEVDAAG 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 551 KITSLDAKLNLENKDyKKTTKITWLAESThalSIPAVCVTYEHLITKPVLGKDEDFKQYINKDSKHEELMLGDPCLKDLK 630
Cdd:PTZ00437 449 QPSVIHVDIDFERKD-KPKTNISWVSATA---CTPVEVRLYNALLKDDRAAIDPEFLKFIDEDSEVVSHGYAEKGIENAK 524
|
490 500
....*....|....*....|.
gi 66267550 631 KGDIIQLQRRGFFICDQPYEP 651
Cdd:PTZ00437 525 HFESVQAERFGYFVVDPDTRP 545
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
144-642 |
7.53e-100 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 332.20 E-value: 7.53e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 144 DKKQDVGKFVELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFE--KVILEDV 221
Cdd:PRK04156 83 EKKEEKKGLPPLPNAEKGKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTKRPDPEayDMILEDL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 222 AMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRTESKHRKNSVEKNLQMWEEMKKGSQFGQSC 301
Cdd:PRK04156 163 KWLGVKWDEVVIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELRDAGKPCPHRDKSPEENLELWEKMLDGEYKEGEA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 302 CLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIR 381
Cdd:PRK04156 243 VVRVKTDLEHPNPSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYDYFGWE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 382 KPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFN 461
Cdd:PRK04156 323 YPETIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAIN 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 462 KKVIDPVAPRYVALlkKEVVPVNVLDAQEEMKEVARHPKNPDVGLKPVWYSPKVFIEGADAEtfSEGEMVTFINWGNINI 541
Cdd:PRK04156 403 RKLIDPIANRYFFV--RDPVELEIEGAEPLEAKIPLHPDRPERGEREIPVGGKVYVSSDDLE--AEGKMVRLMDLFNVEI 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 542 TKIHKNAdGKITSLDaklnLENKDYKKTTKITWLAESThalSIPAVCVtyehlitKPVLGKDEDFkqyinkdskheelml 621
Cdd:PRK04156 479 TGVSVDK-ARYHSDD----LEEARKNKAPIIQWVPEDE---SVPVRVL-------KPDGGDIEGL--------------- 528
|
490 500
....*....|....*....|.
gi 66267550 622 GDPCLKDLKKGDIIQLQRRGF 642
Cdd:PRK04156 529 AEPDVADLEVDDIVQFERFGF 549
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
161-651 |
3.96e-95 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 325.56 E-value: 3.96e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 161 GKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFET 240
Cdd:PLN02859 263 GKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMGWEPFKITYTSDYFQE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 241 IMKYAEKLIQEGKAYVDDTPAEQMKAEREQRTESKHRKNSVEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPT 320
Cdd:PLN02859 343 LYELAVELIRRGHAYVDHQTPEEIKEYREKKMNSPWRDRPIEESLKLFEDMRRGLIEEGKATLRMKQDMQNDNFNMYDLI 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 321 LYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSK 400
Cdd:PLN02859 423 AYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGLYQPYVWEYSRLNVTNTVMSK 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 401 RKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRS---VVNMewDKIWAFNKKVIDPVAPRYVALLK 477
Cdd:PLN02859 503 RKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSdnsLIRM--DRLEHHIREELNKTAPRTMVVLH 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 478 KEVVPVNVLDAQEEMK-EVARHPKNPDVGLKP---VWYSPKVFIEGADAET--------FSEGEMVTFINWGNINITK-I 544
Cdd:PLN02859 581 PLKVVITNLESGEVIElDAKRWPDAQNDDPSAfykVPFSRVVYIERSDFRLkdskdyygLAPGKSVLLRYAFPIKCTDvV 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 545 HKNADGKITSLDAKLnlenkDYKKTTK----ITWLAESTHALSIPAVCV-TYEHLITKPVLGKDEDFKQYINKDSKheEL 619
Cdd:PLN02859 661 LADDNETVVEIRAEY-----DPEKKTKpkgvLHWVAEPSPGVEPLKVEVrLFDKLFLSENPAELEDWLEDLNPQSK--EV 733
|
490 500 510
....*....|....*....|....*....|....*
gi 66267550 620 MLGD---PCLKDLKKGDIIQLQRRGFFICDQPYEP 651
Cdd:PLN02859 734 ISGAyavPSLKDAKVGDRFQFERLGYFAVDKDSTP 768
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
975-1370 |
6.30e-90 |
|
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440211 [Multi-domain] Cd Length: 564 Bit Score: 304.00 E-value: 6.30e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 975 KQTRLGLEAKKE--ENLAEWYSQVITKSEMIEYYdVSGCYILRPWSYSIWESIKDFFDAEIKKLGVENCYFPIFVSqAAL 1052
Cdd:COG0442 2 RASKLFIPTLKErpADAEVWSHQLMLRAGLIRKL-ASGIYTYLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQP-AEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1053 EKEKNHIEDFAPEVAWVtrsgKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPVRLNQWCNVVRWEFKHPQPFLRTREF 1132
Cdd:COG0442 80 WEESGRWEGFGPELARV----TDRLEREFCLGPTHEEVITDLVRNEIKSYRDLPLLLYQIQTKFRDEIRPRFGLLRTREF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1133 LWQEGHSAFATFEEAADEVLQILELYARVYEElLAIPVVRGRKT-------EKEKFA--------------GGDY----- 1186
Cdd:COG0442 156 LMKDAYSFHATEEELDEEYQKMLDAYERIFER-LGLPVRAVEADsgaiggsESHEFMvladsgedtivycdACDYaanie 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1187 -------------------------TTTIEA------------------------------------------------- 1192
Cdd:COG0442 235 kaealappaeraeptkeleavatpgAKTIEEvaeflgvpaektvktlvykadgelvavlvrgdhelneiklenllgasel 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1193 -----------------FISASG--------------------------------------------------------- 1198
Cdd:COG0442 315 elateeeieaalgavpgFLGPVGlgvpyiadrsvagmsnfvcganeddyhytnvnwgrdfpvdevadlrnvvegdpcpdc 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1199 -------RAIQGATSHHLGQNFSKMCEIVFEDPKtpGEKQFAYQCSWGLT-TRTIGVMVMVHGDSMGLVLPPRVASVQVV 1270
Cdd:COG0442 395 ggllqdgRGIEVGHIFKLGTKYSKAMDATFLDEN--GKEQPVWMGCYGIGvTRLIAAAIEQHHDDKGIIWPPAIAPFQVV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1271 VIPCGITNalseedrEALMAKCNEYRRRLLGANIRVRVDLRDNySPGWKFNHWELKGVPVRLEVGPRDMKSCQFVAVRRD 1350
Cdd:COG0442 473 IVPINMKD-------EAVLEAAEELYAELKAAGIDVLLDDRDE-RPGVKFADAELIGIPLRIVIGPRDLEEGQVEVKRRD 544
|
570 580
....*....|....*....|
gi 66267550 1351 TGEKLTIAEKEAEAKLEKVL 1370
Cdd:COG0442 545 TGEKEEVPLDELVETVKELL 564
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
1257-1477 |
1.01e-81 |
|
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and archaea. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only, and an additional C-terminal zinc-binding domain specific to this subfamily of aaRSs.
Pssm-ID: 238439 [Multi-domain] Cd Length: 202 Bit Score: 266.86 E-value: 1.01e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1257 GLVLPPRVASVQVVVIPCGITnalsEEDREALMAKCNEYRRRLLGANIRVRVDLRDNYSPGWKFNHWELKGVPVRLEVGP 1336
Cdd:cd00862 1 GLVLPPRVAPIQVVIVPIGIK----DEKREEVLEAADELAERLKAAGIRVHVDDRDNYTPGWKFNDWELKGVPLRIEIGP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1337 RDMKSCQFVAVRRDTGEKLTIAEKEAEAKLEKVLEDIQLNLFTRASEDLK-THMVVsnTLEDFQKVLDAGKVAQIPFCGE 1415
Cdd:cd00862 77 RDLEKNTVVIVRRDTGEKKTVPLAELVEKVPELLDEIQEDLYERALEFRDaTRIVD--TWEEFKEALNEKGIVLAPWCGE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66267550 1416 IDCEDWIKKMTArdqdvepgapsmgAKSLCIPFnPLCELQPGAMCV-CGkNPAKFYTLFGRSY 1477
Cdd:cd00862 155 EECEEEIKEETA-------------ATILCIPF-DEAKLEEGGKCVvCG-RPAKAYARFAKSY 202
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
988-1250 |
1.64e-72 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 243.04 E-value: 1.64e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 988 NLAEWYSQVITKSEMIEYYDVSGCYILRPWSYSIWESIKDFFDAEIKKLGVENCYFPIFVSQAALEKEKNHIEDFAPEVA 1067
Cdd:cd00772 1 DASEKSLEHIGKAELADQGPGRGIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGFSKELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1068 WVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPVRLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATFEEA 1147
Cdd:cd00772 81 VFKDAGDEELEEDFALRPTLEENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIRPRFGFLRAREFIMKDGHSAHADAEEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1148 ADEVLQILELYARVYEELLAIPVVRGRKTEKEKFAGGDYTTTIEAfISASGRAIQGATSHHLGQNFS--KMCEIVFEDPK 1225
Cdd:cd00772 161 DEEFLNMLSAYAEIARDLAAIDFIEGEADEGAKFAGASKSREFEA-LMEDGKAKQAETGHIFGEGFAraFDLKAKFLDKD 239
|
250 260
....*....|....*....|....*.
gi 66267550 1226 tpGEKQFAYQCSWGLT-TRTIGVMVM 1250
Cdd:cd00772 240 --GKEKFFEMGCWGIGiSRFIGAIIE 263
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
161-448 |
2.36e-65 |
|
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: 229.68 E-value: 2.36e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 161 GKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQ-FTYTSDHFE 239
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEgPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 240 TIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRTESK--------HRKNSVEKNLQMWEEmkkgsqfGQSCCLRAKI---- 307
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGkpprydgrCRDLSPEELERMLAA-------GEPPVLRFKIpeeg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 308 ----DMSS-----NNGCMRDPTLYRckiqphpRTGnkynvYPTYDFACPIVDSIEGVTHALRT------TEYHDrdeqfy 372
Cdd:COG0008 156 vvfdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGeehlsnTPRQI------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 373 WIIEALGIRKPyiwEYSRLNL----NNTVLSKRKltwfvneGLVdgwddprfpTVRGVLRRGMTVEGLKQFIAAQGSSRS 448
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLilgpDGTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
162-471 |
3.35e-63 |
|
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: 215.29 E-value: 3.35e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 162 KVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFE--KVILEDVAMLHIKPDQFTYTSDHFE 239
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPDPEayDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 240 TIMKYAEKLIQEGKAYVddtpaeqmkaereqrteskhrknsveknlqmweemkkgsqfgqscclrakidmssnngcmrdp 319
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 320 tlyrckiqpHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLS 399
Cdd:cd09287 98 ---------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIHWGRLKIEGGKLS 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66267550 400 KRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPR 471
Cdd:cd09287 169 TSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRANR 240
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
469-646 |
8.60e-48 |
|
tRNA synthetases class I (E and Q), anti-codon binding 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: 427609 [Multi-domain] Cd Length: 175 Bit Score: 168.60 E-value: 8.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 469 APRYVALLKKEVVPV-NVLDAQEEMKEVARHPKNPDVGLKPVWYSPKVFIEGADAETFSEGEMVTFINWGNINITKIHKN 547
Cdd:pfam03950 1 APRYMAVLDPVKVVIeNYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDFKRLAPGEEVRLMDAYNIKVTEVVKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 548 ADGKITSLDAKLNLENKDY---KKTTKITWLAESThalSIPAVCVTYEHLITkpvlgKDEDFKQYINKDSKHE-ELMLGD 623
Cdd:pfam03950 81 EDGNVTELHCTYDGDDLGGarkVKGKIIHWVSASD---AVPAEVRLYDRLFK-----DEDDADFLLNPDSLKVlTEGLAE 152
|
170 180
....*....|....*....|...
gi 66267550 624 PCLKDLKKGDIIQLQRRGFFICD 646
Cdd:pfam03950 153 PALANLKPGDIVQFERIGYFRVD 175
|
|
| GST_C_GluProRS_N |
cd10309 |
Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional ... |
39-122 |
2.14e-39 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional Glutamyl-Prolyl-tRNA synthetase; Glutathione S-transferase (GST) C-terminal domain family, bifunctional GluRS-Prolyl-tRNA synthetase (GluProRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of GluProRS from higher eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. The GST_C-like domain of GluProRS may be involved in protein-protein interactions, mediating the formation of the multi-aaRS complex in higher eukaryotes. The multi-aaRS complex acts as a molecular hub for protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.
Pssm-ID: 198342 [Multi-domain] Cd Length: 81 Bit Score: 140.92 E-value: 2.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 39 EHTEIDHWLEFSATKLSSCDRLTSAINELNHCLSLRTYLVGNSLTLADLCVWATLKGSAAWQEHlkqNKTLVHVKRWFGF 118
Cdd:cd10309 1 EQTEVDHWISFSAGRLSCDQDFSSALSYLDKALSLRTYLVGNSLTLADFAVWAALRGNGEWLAS---KEKYVNVTRWFKF 77
|
....
gi 66267550 119 LEAQ 122
Cdd:cd10309 78 ISSQ 81
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
162-447 |
7.99e-38 |
|
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: 142.23 E-value: 7.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 162 KVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQ-FTYTSDHFET 240
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEgPYRQSDRFDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 241 IMKYAEKLIQEGkayvddtpaeqmkaereqrteskhrknsveknlqmweemkkgsqfgqscclrakidmssnngcmrdpt 320
Cdd:cd00418 81 YRAYAEELIKKG-------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 321 lyrckiqphprtgnkynVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNL-NNTVLS 399
Cdd:cd00418 93 -----------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLeDGTKLS 155
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 66267550 400 KRKLtwfvneglvdgwddprFPTVRGVLRRGMTVEGLKQFIAAQGSSR 447
Cdd:cd00418 156 KRKL----------------NTTLRALRRRGYLPEALRNYLALIGWSK 187
|
|
| Gly_His_Pro_Ser_Thr_tRS_core |
cd00670 |
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic ... |
1019-1247 |
1.44e-34 |
|
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic domain of tRNA synthetases of the subgroup containing glycyl, histidyl, prolyl, seryl and threonyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. These enzymes belong to class II aminoacyl-tRNA synthetases (aaRS) based upon their structure and the presence of three characteristic sequence motifs in the core domain. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ and the accessory subunit of mitochondrial polymerase gamma (Pol gamma b) . Most class II tRNA synthetases are dimers, with this subgroup consisting of mostly homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238359 [Multi-domain] Cd Length: 235 Bit Score: 132.90 E-value: 1.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1019 YSIWESIKDFFDAEIKKLGVENCYFPIFVSQAALEKEkNHIEDFAPEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKW 1098
Cdd:cd00670 2 TALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKG-GHLDGYRKEMYTFEDKGRELRDTDLVLRPAACEPIYQIFSGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1099 VQSHRDLPVRLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSaFATFEEAADEVLQILELYARVYEElLAIPVVRGRKTEK 1178
Cdd:cd00670 81 ILSYRALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVEYVV-FGEPEEAEEERREWLELAEEIARE-LGLPVRVVVADDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66267550 1179 EKFAGGD--------YTTTIEAFISASGRAIQGATSHHLGQNFSKMCEivFEDPKTPGEKqFAYQCSW-GLTTRTIGV 1247
Cdd:cd00670 159 FFGRGGKrgldagreTVVEFELLLPLPGRAKETAVGSANVHLDHFGAS--FKIDEDGGGR-AHTGCGGaGGEERLVLA 233
|
|
| GST_C_AaRS_like |
cd10289 |
Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA ... |
39-122 |
6.79e-24 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA synthetases and similar domains; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl-tRNA synthetase (AaRS)-like subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of some eukaryotic AaRSs, as well as similar domains found in proteins involved in protein synthesis including Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 2 (AIMP2), AIMP3, and eukaryotic translation Elongation Factor 1 beta (eEF1b). AaRSs comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. AaRSs in this subfamily include GluRS from lower eukaryotes, as well as GluProRS, MetRS, and CysRS from higher eukaryotes. AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex found in higher eukaryotes. The GST_C-like domain is involved in protein-protein interactions, mediating the formation of aaRS complexes such as the MetRS-Arc1p-GluRS ternary complex in lower eukaryotes and the multi-aaRS complex in higher eukaryotes, that act as molecular hubs for protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.
Pssm-ID: 198322 [Multi-domain] Cd Length: 82 Bit Score: 96.61 E-value: 6.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 39 EHTEIDHWLEFsATKLSSCDRLTSAINELNHCLSLRTYLVGNSLTLADLCVWATLKGSAAWQEHlKQNKTLVHVKRWFGF 118
Cdd:cd10289 1 EAAQVDQWLDL-AGSLLKGKELEALLKSLNSYLASRTFLVGYSLTLADVAVFSALYPSGQKLSD-KEKKKFPHVTRWFNH 78
|
....
gi 66267550 119 LEAQ 122
Cdd:cd10289 79 IQNL 82
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
718-767 |
2.27e-23 |
|
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 94.22 E-value: 2.27e-23
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 66267550 718 LYSRVAVQGDVVRELKAKKAPKEDIDAAVKQLLTLKAEYKEKTGQEYKPG 767
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
|
|
| ProRS-C_1 |
pfam09180 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
1395-1477 |
1.87e-22 |
|
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.
Pssm-ID: 462709 Cd Length: 67 Bit Score: 92.20 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1395 LEDFQKVLDAGKVAQIPFCGEIDCEDWIKKMTardqdvepgapsmGAKSLCIPFNplcELQPGAMCVCGKNPAKFYTLFG 1474
Cdd:pfam09180 1 WEEFKEALEEKGFVLAPWCGDEECEDKIKEET-------------GATSRCIPFD---QEEEGGKCIVCGKPAKKWVLFA 64
|
...
gi 66267550 1475 RSY 1477
Cdd:pfam09180 65 RSY 67
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
718-770 |
2.12e-22 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 91.40 E-value: 2.12e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 66267550 718 LYSRVAVQGDVVRELKAKKAPKEDIDAAVKQLLTLKAEYKEKTGQEYKPGNPS 770
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
1268-1368 |
1.28e-21 |
|
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain.
Pssm-ID: 460819 [Multi-domain] Cd Length: 94 Bit Score: 90.72 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1268 QVVVIPCGitnalseEDREALMAKCNEYRRRLLGANIRVRVDLRdNYSPGWKFNHWELKGVPVRLEVGPRDMKSCQFVAV 1347
Cdd:pfam03129 1 QVVVIPLG-------EKAEELEEYAQKLAEELRAAGIRVELDDR-NESIGKKFRRADLIGIPFALVVGEKELEEGTVTVR 72
|
90 100
....*....|....*....|.
gi 66267550 1348 RRDTGEKLTIAEKEAEAKLEK 1368
Cdd:pfam03129 73 RRDTGEQETVSLDELVEKLKE 93
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
791-840 |
1.81e-21 |
|
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 88.83 E-value: 1.81e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 66267550 791 LYNKVAAQGEVVRKLKAEKAPKAKVTEAVECLLSLKAEYKEKTGKDYVPG 840
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
869-921 |
7.93e-21 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 87.16 E-value: 7.93e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 66267550 869 LFDRVACQGEVVRKLKAEKASKDQVDSAVQELLQLKAQYKSLTGIEYKPVSAT 921
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
791-843 |
8.25e-21 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 86.78 E-value: 8.25e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 66267550 791 LYNKVAAQGEVVRKLKAEKAPKAKVTEAVECLLSLKAEYKEKTGKDYVPGQPP 843
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
719-773 |
1.47e-20 |
|
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.
Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 86.24 E-value: 1.47e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 66267550 719 YSRVAVQGDVVRELKAKKAPKEDIDAAVKQLLTLKAEYKEKTGQEYKPGNPSAAA 773
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGDT 55
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
1021-1240 |
1.91e-20 |
|
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 91.41 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1021 IWESIKDFFDAEIKKLGVENCYFPIFVSQAALEKEKNHIEDFAPevawvtrsGKTELAEPIAIRPTSETvmYPAYAkWVQ 1100
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKDLLP--------VGAENEEDLYLRPTLEP--GLVRL-FVS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1101 SHRDLPVRLNQWCNVVRWEfKHPQPFLRTREFLWQEGHSAFATFEEaADEVLQILELYARVYEEL-LAIPVVRGRKTEKE 1179
Cdd:cd00768 70 HIRKLPLRLAEIGPAFRNE-GGRRGLRRVREFTQLEGEVFGEDGEE-ASEFEELIELTEELLRALgIKLDIVFVEKTPGE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66267550 1180 KFAGGdYTTTIEAFI-SASGRAIQGATSHHLGQNFSKMCEIVFEDPktPGEKQFAYQCSWGL 1240
Cdd:cd00768 148 FSPGG-AGPGFEIEVdHPEGRGLEIGSGGYRQDEQARAADLYFLDE--ALEYRYPPTIGFGL 206
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
869-917 |
7.05e-20 |
|
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 84.21 E-value: 7.05e-20
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 66267550 869 LFDRVACQGEVVRKLKAEKASKDQVDSAVQELLQLKAQYKSLTGIEYKP 917
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKP 49
|
|
| ProRS-C_1 |
smart00946 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
1395-1477 |
1.66e-19 |
|
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.
Pssm-ID: 198014 Cd Length: 67 Bit Score: 83.77 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1395 LEDFQKVLDAGKVAQIPFCGEIDCEDWIKKMTardqdvepgapsmGAKSLCIPFNplcELQPGAMCVCGKNPAKFYTLFG 1474
Cdd:smart00946 1 LEEFKKALEEGKFVLAPWCGDEECEEKIKEET-------------GATIRCIPFD---QDEEPGKCVVCGKPAKKWVLFA 64
|
...
gi 66267550 1475 RSY 1477
Cdd:smart00946 65 RSY 67
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
792-846 |
3.42e-19 |
|
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.
Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 82.39 E-value: 3.42e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 66267550 792 YNKVAAQGEVVRKLKAEKAPKAKVTEAVECLLSLKAEYKEKTGKDYVPGQPPASQ 846
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGDT 55
|
|
| GST_C_GluRS_N |
cd10306 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Glutamyl-tRNA synthetase; ... |
39-121 |
9.74e-19 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of Glutamyl-tRNA synthetase; Glutathione S-transferase (GST) C-terminal domain family, Glutamyl-tRNA synthetase (GluRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of GluRS from lower eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. The GST_C-like domain of GluRS is involved in protein-protein interactions. This domain mediates the formation of the MetRS-Arc1p-GluRS ternary complex found in lower eukaryotes, which is considered an evolutionary intermediate between prokaryotic aaRS and the multi-aaRS complex found in higher eukaryotes. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.
Pssm-ID: 198339 [Multi-domain] Cd Length: 87 Bit Score: 82.40 E-value: 9.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 39 EHTEIDHWLEFSATKLSSCD--RLTSAINELNHCLSLRTYLVGNSLTLADLCVWATLKGSAAWQEHLKqNKTLVHVKRWF 116
Cdd:cd10306 3 DKEQVAEWIDFATTLLVLKDfkALSQALEELDSHLTLRTFIVGYSLSLADIAVWGALRGNGVAGSLIK-NKVYVNLSRWF 81
|
....*
gi 66267550 117 GFLEA 121
Cdd:cd10306 82 SFLES 86
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
870-923 |
2.07e-18 |
|
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.
Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 80.08 E-value: 2.07e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 66267550 870 FDRVACQGEVVRKLKAEKASKDQVDSAVQELLQLKAQYKSLTGIEYKPVSATGA 923
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGD 54
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
719-760 |
6.62e-16 |
|
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238605 [Multi-domain] Cd Length: 42 Bit Score: 72.57 E-value: 6.62e-16
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 66267550 719 YSRVAVQGDVVRELKAKKAPKEDIDAAVKQLLTLKAEYKEKT 760
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
792-833 |
7.29e-15 |
|
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238605 [Multi-domain] Cd Length: 42 Bit Score: 69.88 E-value: 7.29e-15
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 66267550 792 YNKVAAQGEVVRKLKAEKAPKAKVTEAVECLLSLKAEYKEKT 833
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
870-911 |
9.49e-15 |
|
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238605 [Multi-domain] Cd Length: 42 Bit Score: 69.49 E-value: 9.49e-15
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 66267550 870 FDRVACQGEVVRKLKAEKASKDQVDSAVQELLQLKAQYKSLT 911
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
1076-1252 |
3.21e-14 |
|
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.
Pssm-ID: 395469 [Multi-domain] Cd Length: 181 Bit Score: 72.44 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1076 ELAEPIAIRPTSETVMYPAYAKWVQSHRDLPVRLNQWCNVVRWEFKHPQ-PFLRTREFLWQEGHSaFATFEEAADEVLQI 1154
Cdd:pfam00587 6 ENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTrGLIRVRQFHQDDAHI-FHAPGQSPDELEDY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1155 LELYARVYEELLaIPVVRGRKTEKEKFAGGDYTTTIEAFISASGRAIQGATSHHLGQNFSKMCEIVFEDPKtpGEKQFAY 1234
Cdd:pfam00587 85 IKLIDRVYSRLG-LEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDED--NESKFPY 161
|
170 180
....*....|....*....|
gi 66267550 1235 QCSWGL--TTRTIGVMVMVH 1252
Cdd:pfam00587 162 MIHRAGlgVERFLAAILENN 181
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
161-417 |
1.02e-13 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 75.93 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 161 GKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYT------ 234
Cdd:PLN02627 44 GPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVggeygp 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 235 ---SDHFETIMKYAEKLIQEGKAY---VDDTPAEQMKAEREQRTE-----SKHRKNSVEknlQMWEEMKKGSQFgqscCL 303
Cdd:PLN02627 124 yrqSERNAIYKQYAEKLLESGHVYpcfCTDEELEAMKEEAELKKLpprytGKWATASDE---EVQAELAKGTPY----TY 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 304 RAKIdmsSNNGCMRDPTLYRCKIQPHPRT-GN----KYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEAL 378
Cdd:PLN02627 197 RFRV---PKEGSVKIDDLIRGEVSWNTDTlGDfvllRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKAL 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 66267550 379 GIRKPyiwEYSRLNL----NNTVLSKR---------KLTWFVNEGLVD-----GWDD 417
Cdd:PLN02627 274 GFPMP---RFAHVSLilapDRSKLSKRhgatsvgqfREMGYLPDAMVNylallGWND 327
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
1267-1366 |
2.28e-11 |
|
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and prolyl tRNA synthetases, which are classified as a group of class II aminoacyl-tRNA synthetases (aaRS). In aaRSs, the anticodon binding domain is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only. This domain is also found in the accessory subunit of mitochondrial polymerase gamma (Pol gamma b).
Pssm-ID: 238379 [Multi-domain] Cd Length: 94 Bit Score: 61.65 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1267 VQVVVIPCGitnalseEDREALMAKCNEYRRRLLGANIRVRVDLRDNySPGWKFNHWELKGVPVRLEVGPRDMKSCQFVA 1346
Cdd:cd00738 2 IDVAIVPLT-------DPRVEAREYAQKLLNALLANGIRVLYDDRER-KIGKKFREADLRGVPFAVVVGEDELENGKVTV 73
|
90 100
....*....|....*....|
gi 66267550 1347 VRRDTGEKLTIAEKEAEAKL 1366
Cdd:cd00738 74 KSRDTGESETLHVDELPEFL 93
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
1242-1370 |
2.80e-11 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 68.19 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1242 TRTIGVMVMVHGDSMGLVLPPRVASVQVVVIPcgiTNALSEEDREAlmakCNEYRRRLLGANIRVRVDLRDNySPGWKFN 1321
Cdd:PRK09194 444 SRLVAAAIEQNHDEKGIIWPKAIAPFDVHIVP---VNMKDEEVKEL----AEKLYAELQAAGIEVLLDDRKE-RPGVKFA 515
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 66267550 1322 HWELKGVPVRLEVGPRDMKSCQFVAVRRDTGEKLTIAEKEAEAKLEKVL 1370
Cdd:PRK09194 516 DADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELVEFLKALK 564
|
|
| GST_C_AIMP3 |
cd10305 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ... |
39-116 |
1.11e-10 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 3; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein (AIMP) 3 subfamily; AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex that functions as a molecular hub to coordinate protein synthesis. There are three AIMPs, named AIMP1-3, which play diverse regulatory roles. AIMP3, also called p18 or eukaryotic translation elongation factor 1 epsilon-1 (EEF1E1), contains a C-terminal domain with similarity to the C-terminal alpha helical domain of GSTs. It specifically interacts with methionyl-tRNA synthetase (MetRS) and is translocated to the nucleus during DNA synthesis or in response to DNA damage and oncogenic stress. In the nucleus, it interacts with ATM and ATR, which are upstream kinase regulators of p53. It appears to work against DNA damage in cooperation with AIMP2, and similar to AIMP2, AIMP3 is also a haploinsufficient tumor suppressor. AIMP3 transgenic mice have shorter lifespans than wild-type mice and they show characteristics of progeria, suggesting that AIMP3 may also be involved in cellular and organismal aging.
Pssm-ID: 198338 [Multi-domain] Cd Length: 101 Bit Score: 59.61 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 39 EHTEIDHWLEFSATKLSSCDR---LTSAINELNHCLSLRTYLVGNSLTLADLCV----WATLKGSAAwQEhlKQNktLVH 111
Cdd:cd10305 3 ERAQVDQWLEYRVTQVAPASDkadAKSLLKELNSYLQDRTYLVGHKLTLADVVLyyglHPIMKDLSP-QE--KEQ--YLN 77
|
....*
gi 66267550 112 VKRWF 116
Cdd:cd10305 78 VSRWF 82
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
869-906 |
2.34e-08 |
|
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238474 [Multi-domain] Cd Length: 45 Bit Score: 51.32 E-value: 2.34e-08
10 20 30
....*....|....*....|....*....|....*...
gi 66267550 869 LFDRVACQGEVVRKLKAEKASKDQVDSAVQELLQLKAQ 906
Cdd:cd00938 3 LEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQ 40
|
|
| GstA |
COG0625 |
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; |
11-132 |
6.88e-08 |
|
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440390 [Multi-domain] Cd Length: 205 Bit Score: 54.52 E-value: 6.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 11 VAFTDVNSILRYLARIATTSGLYGTNLMEHTEIDHWLEFSATKLSSC---------------------DRLTSAINELNH 69
Cdd:COG0625 61 LVLTESLAILEYLAERYPEPPLLPADPAARARVRQWLAWADGDLHPAlrnllerlapekdpaaiararAELARLLAVLEA 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66267550 70 CLSLRTYLVGNSLTLADLCVWATLKGSAAWQEHLKQNKtlvHVKRWFGFLEAQQAFRSVGTKW 132
Cdd:COG0625 141 RLAGGPYLAGDRFSIADIALAPVLRRLDRLGLDLADYP---NLAAWLARLAARPAFQRALAAA 200
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
1085-1366 |
1.74e-07 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 55.64 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1085 PTSETVMYPAYAKWVQSHRDLPVRLNQwcnvVRWEFK---HPQpF--LRTREFLWQEGHSAFATFEEAADEVLQILELYA 1159
Cdd:PRK12325 108 PTNEEMITDIFRSYVKSYKDLPLNLYH----IQWKFRdeiRPR-FgvMRGREFLMKDAYSFDLDEEGARHSYNRMFVAYL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1160 RVYE--ELLAIPV------------------------------------VRGRKTEKEKFAGGDYTTTIEAFISA----- 1196
Cdd:PRK12325 183 RTFArlGLKAIPMradtgpiggdlshefiilaetgestvfydkdfldllVPGEDIDFDVADLQPIVDEWTSLYAAteemh 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1197 --------------SGRAIQGATSHHLGQNFSKMCEIVFEDPKtpGEKQFAYQCSWGL-TTRTIGVMVMVHGDSMGLVLP 1261
Cdd:PRK12325 263 deaafaavpeerrlSARGIEVGHIFYFGTKYSEPMNAKVQGPD--GKEVPVHMGSYGIgVSRLVAAIIEASHDDKGIIWP 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1262 PRVASVQVVVIPCGITNalseedrEALMAKCNEYRRRLLGANIRVRVDLRDNySPGWKFNHWELKGVPVRLEVGPRDMKS 1341
Cdd:PRK12325 341 ESVAPFKVGIINLKQGD-------EACDAACEKLYAALSAAGIDVLYDDTDE-RPGAKFATMDLIGLPWQIIVGPKGLAE 412
|
330 340
....*....|....*....|....*
gi 66267550 1342 CQFVAVRRDTGEKLTIAEKEAEAKL 1366
Cdd:PRK12325 413 GKVELKDRKTGEREELSVEAAINRL 437
|
|
| GST_C_Arc1p_N_like |
cd10304 |
Glutathione S-transferase C-terminal-like, alpha helical domain of the Aminoacyl tRNA ... |
39-128 |
1.01e-06 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of the Aminoacyl tRNA synthetase cofactor 1 and similar proteins; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase cofactor 1 (Arc1p)-like subfamily; Arc1p, also called GU4 nucleic binding protein 1 (G4p1) or p42, is a tRNA-aminoacylation and nuclear-export cofactor. It contains a domain in the N-terminal region with similarity to the C-terminal alpha helical domain of GSTs. This domain mediates the association of the aminoacyl tRNA synthetases (aaRSs), MetRS and GluRS, in yeast to form a stable stoichiometric ternany complex. The GST_C-like domain of Arc1p is a protein-protein interaction domain containing two binding sites which enable it to bind the two aaRSs simultaneously and independently. The MetRS-Arc1p-GluRS complex selectively recruits and aminoacylates its cognate tRNAs without additional cofactors. Arc1p also plays a role in the transport of tRNA from the nucleus to the cytoplasm. It may also control the subcellular distribution of GluRS in the cytoplasm, nucleoplasm, and the mitochondrial matrix.
Pssm-ID: 198337 [Multi-domain] Cd Length: 100 Bit Score: 48.52 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 39 EHTEIDHWLEFSATkLSSCDRLTSAINELNHCLSLRTYLVGNS-LTLADLCVWATLKGSAA-WQEHLKQN-KTLVHVKRW 115
Cdd:cd10304 3 QSAEVAQWLSVAKS-GPVSKDVQETLGQLNLHLRTRTFLLGTGkPSVADVAVFEAVLPVVKeWSDEVKTGyAKYRHILRW 81
|
90
....*....|...
gi 66267550 116 FGFLEAQQAFRSV 128
Cdd:cd10304 82 VDYVQNLLLFIPE 94
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
995-1249 |
1.45e-06 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes.
Pssm-ID: 238402 [Multi-domain] Cd Length: 255 Bit Score: 51.42 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 995 QVITKSEMIeYYDVSGCYILRPWSYSIWESIKDFFDAEIKKLGVENCYFPIfVSQAALEKEKNHIEDFAPEVAWVT-RSG 1073
Cdd:cd00779 8 KLLLRAGFI-RQTSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPI-LQPAELWKESGRWDAYGPELLRLKdRHG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1074 KTELaepiaIRPTSETVMYPAYAKWVQSHRDLPVRLNQwcnvVRWEF---KHPQpF--LRTREFLWQEGHSaFATFEEAA 1148
Cdd:cd00779 86 KEFL-----LGPTHEEVITDLVANEIKSYKQLPLNLYQ----IQTKFrdeIRPR-FglMRGREFLMKDAYS-FDIDEESL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1149 DEV-LQILELYARVYEELLaIPVVrgrktekekfaggdytttieAFISASGrAIQGATSH-------------------- 1207
Cdd:cd00779 155 EETyEKMYQAYSRIFKRLG-LPFV--------------------KVEADSG-AIGGSLSHefhvlsplkitkgievghif 212
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 66267550 1208 HLGQNFSKMCEIVFEDPKtpGEKQFAYQCSWGL-TTRTIGVMV 1249
Cdd:cd00779 213 QLGTKYSKALGATFLDEN--GKPKPLEMGCYGIgVSRLLAAII 253
|
|
| GST_C_EF1Bgamma_like |
cd03181 |
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ... |
39-128 |
2.92e-06 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of Elongation Factor 1B and similar proteins; Glutathione S-transferase (GST) C-terminal domain family, Gamma subunit of Elongation Factor 1B (EF1Bgamma) subfamily; EF1Bgamma is part of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. The EF1B gamma subunit contains a GST fold consisting of an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The GST-like domain of EF1Bgamma is believed to mediate the dimerization of the EF1 complex, which in yeast is a dimer of the heterotrimer EF1A:EF1Balpha:EF1Bgamma. In addition to its role in protein biosynthesis, EF1Bgamma may also display other functions. The recombinant rice protein has been shown to possess GSH conjugating activity. The yeast EF1Bgamma binds to membranes in a calcium dependent manner and is also part of a complex that binds to the msrA (methionine sulfoxide reductase) promoter suggesting a function in the regulation of its gene expression. Also included in this subfamily is the GST_C-like domain at the N-terminus of human valyl-tRNA synthetase (ValRS) and its homologs. Metazoan ValRS forms a stable complex with Elongation Factor-1H (EF-1H), and together, they catalyze consecutive steps in protein biosynthesis, tRNA aminoacylation and its transfer to EF.
Pssm-ID: 198290 [Multi-domain] Cd Length: 123 Bit Score: 47.94 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 39 EHTEIDHWLEFSATKL--SSC---------------------DRLTSAINELNHCLSLRTYLVGNSLTLADLCVWATLKG 95
Cdd:cd03181 1 EAAQVLQWISFANSELlpAAAtwvlpllgiapynkkavdkakEDLKRALGVLEEHLLTRTYLVGERITLADIFVASALLR 80
|
90 100 110
....*....|....*....|....*....|....*
gi 66267550 96 saAWQEHLKQN--KTLVHVKRWFGFLEAQQAFRSV 128
Cdd:cd03181 81 --GFETVLDPEfrKKYPNVTRWFNTVVNQPKFKAV 113
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
716-787 |
3.35e-06 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 51.67 E-value: 3.35e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66267550 716 SVLYSRVAVQGDVVRELKAKKAPKEDIDAAVKQL--LTLKAEYKEKTGQEYKPGNPSAAAVQTVSTKSSSNTVE 787
Cdd:PLN02734 10 AEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLkaLKLEKSALEKELQAAVGAGGDGAASKEAFRQAVVNTLE 83
|
|
| MetRS_RNA |
cd00939 |
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
869-912 |
3.60e-06 |
|
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238475 [Multi-domain] Cd Length: 45 Bit Score: 45.16 E-value: 3.60e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 66267550 869 LFDRVACQGEVVRKLKAEKASKDQVDSAVQELLQLKAQYKSLTG 912
Cdd:cd00939 1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEG 44
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
721-755 |
1.62e-05 |
|
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238474 [Multi-domain] Cd Length: 45 Bit Score: 43.23 E-value: 1.62e-05
10 20 30
....*....|....*....|....*....|....*
gi 66267550 721 RVAVQGDVVRELKAKKAPKEDIDAAVKQLLTLKAE 755
Cdd:cd00938 6 AVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQ 40
|
|
| GST_C_AIMP2 |
cd03200 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ... |
20-93 |
2.09e-05 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 2; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein (AIMP) 2 subfamily; AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex that functions as a molecular hub to coordinate protein synthesis. There are three AIMPs, named AIMP1-3, which play diverse regulatory roles. AIMP2, also called p38 or JTV-1, contains a C-terminal domain with similarity to the C-terminal alpha helical domain of GSTs. It plays an important role in the control of cell fate via antiproliferative (by enhancing the TGF-beta signal) and proapoptotic (activation of p53 and TNF-alpha) activities. Its roles in the control of cell proliferation and death suggest that it is a potent tumor suppressor. AIMP2 heterozygous mice with lower than normal expression of AIMP2 show high susceptibility to tumorigenesis. AIMP2 is also a substrate of Parkin, an E3 ubiquitin ligase that is involved in the ubiquitylation and proteasomal degradation of its substrates. Mutations in the Parkin gene is found in 50% of patients with autosomal-recessive early-onset parkinsonism. The accumulation of AIMP2, due to impaired Parkin function, may play a role in the pathogenesis of Parkinson's disease.
Pssm-ID: 198309 [Multi-domain] Cd Length: 96 Bit Score: 44.81 E-value: 2.09e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66267550 20 LRYLARIAttsGLYGTNLMEHTEIDHWLEFSATKL---SSCDRlTSAINELNHCLSLRTYLVGNSLTLADLCVWATL 93
Cdd:cd03200 1 ARFLFRLL---GDESDDPVNATLIDSWVDTAIFQLlegSSKEK-AAVLRALNSALGRSPWLVGSEPTVADIALWSAV 73
|
|
| MetRS_RNA |
cd00939 |
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
791-835 |
2.32e-05 |
|
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238475 [Multi-domain] Cd Length: 45 Bit Score: 42.84 E-value: 2.32e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 66267550 791 LYNKVAAQGEVVRKLKAEKAPKAKVTEAVECLLSLKAEYKEKTGK 835
Cdd:cd00939 1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEGK 45
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
1260-1368 |
3.79e-05 |
|
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440210 [Multi-domain] Cd Length: 639 Bit Score: 48.10 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1260 LPPRVASVQVVVIPcgITnalseedrEALMAKCNEYRRRLLGANIRVRVDLRDNySPGWKFNHWELKGVPVRLEVGPRDM 1339
Cdd:COG0441 533 FPLWLAPVQVVVLP--IS--------DKHADYAKEVAKKLRAAGIRVEVDLRNE-KIGYKIREAQLQKVPYMLVVGDKEV 601
|
90 100 110
....*....|....*....|....*....|
gi 66267550 1340 KSCQfVAVR-RDTGEKLTIAEKEAEAKLEK 1368
Cdd:COG0441 602 ENGT-VSVRrRGGGDLGTMSLDEFIARLKE 630
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
795-828 |
5.16e-05 |
|
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238474 [Multi-domain] Cd Length: 45 Bit Score: 42.07 E-value: 5.16e-05
10 20 30
....*....|....*....|....*....|....
gi 66267550 795 VAAQGEVVRKLKAEKAPKAKVTEAVECLLSLKAE 828
Cdd:cd00938 7 VKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQ 40
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
1101-1380 |
9.22e-05 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 47.05 E-value: 9.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1101 SHRDLPVRLNQWCNVVRWEFKHP-QPFLRTREFLWQEGHsAFATFEEAADEVLQILELYARVY----------------- 1162
Cdd:PRK12444 350 SYRELPIRMCEFGQVHRHEFSGAlNGLLRVRTFCQDDAH-LFVTPDQIEDEIKSVMAQIDYVYktfgfeyevelstrped 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1163 ----EEL-----LAIPVVRGRKTEKEKFAGGD---YTTTIEAFIS-ASGRAIQGATS------------HHLGQNFSKMC 1217
Cdd:PRK12444 429 smgdDELweqaeASLENVLQSLNYKYRLNEGDgafYGPKIDFHIKdALNRSHQCGTIqldfqmpekfdlNYIDEKNEKRR 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1218 EIVFedpktpgekqfaYQCSWGLTTRTIGVMVmvhgDSMGLVLPPRVASVQVVVIPcgITNALSEEdrealmaKCNEYRR 1297
Cdd:PRK12444 509 PVVI------------HRAVLGSLDRFLAILI----EHFGGAFPAWLAPVQVKVIP--VSNAVHVQ-------YADEVAD 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1298 RLLGANIRVRVDLRDNySPGWKFNHWELKGVPVRLEVGPRDMKScQFVAVRRdTGEkltiaEKEAEAKLEKVLEDIQLNL 1377
Cdd:PRK12444 564 KLAQAGIRVERDERDE-KLGYKIREAQMQKIPYVLVIGDKEMEN-GAVNVRK-YGE-----EKSEVIELDMFVESIKEEI 635
|
...
gi 66267550 1378 FTR 1380
Cdd:PRK12444 636 KNR 638
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
1267-1367 |
1.20e-04 |
|
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238437 [Multi-domain] Cd Length: 91 Bit Score: 42.11 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1267 VQVVVIPcgITNALSEedrealMAKcnEYRRRLLGANIRVRVDLRDNySPGWKFNHWELKGVPVRLEVGPRDMKScQFVA 1346
Cdd:cd00860 2 VQVVVIP--VTDEHLD------YAK--EVAKKLSDAGIRVEVDLRNE-KLGKKIREAQLQKIPYILVVGDKEVET-GTVS 69
|
90 100
....*....|....*....|..
gi 66267550 1347 VR-RDTGEKLTIAEKEAEAKLE 1367
Cdd:cd00860 70 VRtRDGGDLGSMSLDEFIEKLK 91
|
|
| GST_C_Delta_Epsilon |
cd03177 |
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; ... |
48-116 |
1.29e-04 |
|
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The class Delta and Epsilon subfamily is made up primarily of insect GSTs, which play major roles in insecticide resistance by facilitating reductive dehydrochlorination of insecticides or conjugating them with GSH to produce water-soluble metabolites that are easily excreted. They are also implicated in protection against cellular damage by oxidative stress.
Pssm-ID: 198287 [Multi-domain] Cd Length: 117 Bit Score: 42.91 E-value: 1.29e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66267550 48 EFSATKLsscDRLTSAINELNHCLSLRTYLVGNSLTLADLCVWATLkGSAAWQEHLKqnKTLVHVKRWF 116
Cdd:cd03177 34 EPPEEKL---DKLEEALEFLETFLEGSDYVAGDQLTIADLSLVATV-STLEVVGFDL--SKYPNVAAWY 96
|
|
| MetRS_RNA |
cd00939 |
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
722-761 |
1.85e-04 |
|
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238475 [Multi-domain] Cd Length: 45 Bit Score: 40.53 E-value: 1.85e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 66267550 722 VAVQGDVVRELKAKKAPKEDIDAAVKQLLTLKAEYKEKTG 761
Cdd:cd00939 5 VAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEG 44
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
1268-1367 |
2.42e-04 |
|
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238438 [Multi-domain] Cd Length: 94 Bit Score: 41.42 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 1268 QVVVIPcgiTNALSEEDREAlmakCNEYRRRLLGANIRVRVDLRDNySPGWKFNHWELKGVPVRLEVGPRDMKSCQFVAV 1347
Cdd:cd00861 3 DVVIIP---MNMKDEVQQEL----AEKLYAELQAAGVDVLLDDRNE-RPGVKFADADLIGIPYRIVVGKKSAAEGIVEIK 74
|
90 100
....*....|....*....|
gi 66267550 1348 RRDTGEKLTIAEKEAEAKLE 1367
Cdd:cd00861 75 VRKTGEKEEISIDELLEFLQ 94
|
|
| GlyRS_RNA |
cd00935 |
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS ... |
718-759 |
4.36e-04 |
|
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix-turn-helix structure , which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238472 [Multi-domain] Cd Length: 51 Bit Score: 39.39 E-value: 4.36e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 66267550 718 LYSRVAVQGDVVRELKAKKAPKEDIDAAVKQLLTLKAEYKEK 759
Cdd:cd00935 4 LRAAVKEQGDLVRKLKEEGAPDVDIKKAVAELKARKKLLEDK 45
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
869-923 |
5.24e-04 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 44.74 E-value: 5.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 66267550 869 LFDRVACQGEVVRKLKAEKASKDQVDSAVQELLQLKAQYKSLTGIEYKPVSATGA 923
Cdd:PLN02734 12 KQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELQAAVGAGGD 66
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
781-847 |
6.71e-04 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 44.35 E-value: 6.71e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66267550 781 SSSNTVESTSLYNKVAAQGEVVRKLKAEKAPKAKVTEAVECL--LSLKAEYKEKTGKDYVPGQPPASQN 847
Cdd:PLN02734 2 EDSLRDALAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLkaLKLEKSALEKELQAAVGAGGDGAAS 70
|
|
| GST_C_ValRS_N |
cd10294 |
Glutathione S-transferase C-terminal-like, alpha helical domain of vertebrate Valyl-tRNA ... |
60-128 |
7.80e-04 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of vertebrate Valyl-tRNA synthetase; Glutathione S-transferase (GST) C-terminal domain family, Valyl-tRNA synthetase (ValRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of human ValRS and its homologs from other vertebrates such as frog and zebrafish. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. They typically form large stable complexes with other proteins. ValRS forms a stable complex with Elongation Factor-1H (EF-1H), and together, they catalyze consecutive steps in protein biosynthesis, tRNA aminoacylation and its transfer to EF. The GST_C-like domain of ValRS from higher eukaryotes is likely involved in protein-protein interactions, to mediate the formation of the multi-aaRS complex that acts as a molecular hub to coordinate protein synthesis. ValRSs from prokaryotes and lower eukaryotes, such as fungi and plants, do not appear to contain this GST_C-like domain.
Pssm-ID: 198327 [Multi-domain] Cd Length: 123 Bit Score: 40.98 E-value: 7.80e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66267550 60 LTSAINELNHCLSLRTYLVGNSLTLADLCVWATLKGSAAWQEHLKQNKTLVHVKRWFGFLEAQQAFRSV 128
Cdd:cd10294 45 LQRVLKVLDCYLKLRTYLVGEAITLADIAVACALLLPFKYVLDPARRESLLNVTRWFLTCVNQPEFLAV 113
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
164-247 |
1.62e-03 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate 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: 173901 [Multi-domain] Cd Length: 143 Bit Score: 40.54 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66267550 164 TVRFPPEASGYLHIGHAKAALLN---QHY--QVNFKGKLIMRFDDTNPEKEK------EDFEKVILEDVAMLHikpDQFT 232
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFdflAQAyrKLGYKVRCIALIDDAGGLIGDpankkgENAKAFVERWIERIK---EDVE 77
|
90
....*....|....*
gi 66267550 233 YTSDHFETIMKYAEK 247
Cdd:cd00802 78 YMFLQAADFLLLYET 92
|
|
| GlyRS_RNA |
cd00935 |
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS ... |
869-910 |
2.23e-03 |
|
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix-turn-helix structure , which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238472 [Multi-domain] Cd Length: 51 Bit Score: 37.47 E-value: 2.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 66267550 869 LFDRVACQGEVVRKLKAEKASKDQVDSAVQEllqLKAQYKSL 910
Cdd:cd00935 4 LRAAVKEQGDLVRKLKEEGAPDVDIKKAVAE---LKARKKLL 42
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| GlyRS_RNA |
cd00935 |
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS ... |
790-832 |
3.31e-03 |
|
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix-turn-helix structure , which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238472 [Multi-domain] Cd Length: 51 Bit Score: 37.08 E-value: 3.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 66267550 790 SLYNKVAAQGEVVRKLKAEKAPKAKVTEAVECLLSLKAEYKEK 832
Cdd:cd00935 3 PLRAAVKEQGDLVRKLKEEGAPDVDIKKAVAELKARKKLLEDK 45
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| GST_C_eEF1b_like |
cd10308 |
Glutathione S-transferase C-terminal-like, alpha helical domain of eukaryotic translation ... |
41-116 |
3.92e-03 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of eukaryotic translation Elongation Factor 1 beta; Glutathione S-transferase (GST) C-terminal domain family, eukaryotic translation Elongation Factor 1 beta (eEF1b) subfamily; eEF1b is a component of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. eEF1b contains a GST_C-like alpha helical domain at the N-terminal region and a C-terminal guanine nucleotide exchange domain. The GST_C-like domain likely functions as a protein-protein interaction domain, similar to the function of the GST_C-like domains of EF1Bgamma and various aminoacyl-tRNA synthetases (aaRSs) from higher eukaryotes.
Pssm-ID: 198341 Cd Length: 82 Bit Score: 37.79 E-value: 3.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66267550 41 TEIDHWLEFSATKLSSCDRLTSAIN--ELNHCLSLRTYLVGNSLTLADLCVWATLKGSAAWQEHlkqnktlVHVKRWF 116
Cdd:cd10308 6 TESKHKLLLGVSLDGSFADLKTDKGleALNEYLADRSYISGYSPSQADVEVFDKLKKAPDATKF-------PHLARWY 76
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