|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
90-730 |
0e+00 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 722.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 90 PPLGALLAVEhvKGDVSI----SLEEGKENILYVSENVVFTDINSILRYLARVATTAGLYGSNLLEHTEIDHWLEFSATk 165
Cdd:PLN02907 12 PPLAVIAAAK--VAGVPLtidpSLKSGSAPTLLFSSGEKLTGTNVLLRYIARSASLPGFYGQDAFESSQVDEWLDYAPT- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 166 LSSCNLFTSAINELNHCLSLRTYLVGNSLSLADLCVWATLKGSAAWQEQLKQNKAPVHVKRWFGFLEAQ----------- 234
Cdd:PLN02907 89 FSSGSEFENACEYVDGYLASRTFLVGYSLTIADIAIWSGLAGSGQRWESLRKSKKYQNLVRWFNSISAEysdilnevtaa 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 235 -------------QAFQSVGTKWNVSATKAKVHYQVN--------------------------------------FKGKL 263
Cdd:PLN02907 169 yvgkrgagkpaaaKSKEKVADAGKADGAKDKGSFEVDlpgaeegkvctrfppepsgylhighakaallnqyfarrYKGKL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 264 IMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAE---------- 333
Cdd:PLN02907 249 IVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKErmdgieskcr 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 334 --PIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTH 411
Cdd:PLN02907 329 nnSVEENLRLWKEMIAGSERGLQCCVRGKLDMQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTH 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 412 ALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLK 491
Cdd:PLN02907 409 ALRSSEYHDRNAQYYRILEDMGLRKVHIWEFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALK 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 492 QFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLKKEVIPV---NIPEaQEEMKEVAKHPKNPDVGLKPVWYSPK 568
Cdd:PLN02907 489 QFILSQGASKNLNLMEWDKLWTINKKIIDPVCPRHTAVLKEGRVLLtltDGPE-TPFVRIIPRHKKYEGAGKKATTFTNR 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 569 VFIEGADAETLSEGEMVTFINWGNINITKINKNADGKIVSLDAKLNLENkDYKKTT-KITWLAETAHALPIPaiCVTYEH 647
Cdd:PLN02907 568 IWLDYADAEAISEGEEVTLMDWGNAIIKEITKDEGGAVTALSGELHLEG-SVKTTKlKLTWLPDTNELVPLS--LVEFDY 644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 648 LITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDQPYEPVSpysckeAPCVLIYVPDGHTK 727
Cdd:PLN02907 645 LITKKKLEEDDNFLDVLNPCTKKETAALGDSNMRNLKRGEIIQLERKGYYRCDAPFVRSS------KPIVLFAIPDGRQQ 718
|
...
gi 1826797428 728 EMP 730
Cdd:PLN02907 719 KSG 721
|
|
| proS_fam_I |
TIGR00408 |
prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ... |
1034-1528 |
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: 567.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1034 AKKEENLADWYSQVITKSELIEYYDVSGCYILRPWAYSIWESIKDFFDAEIKKLGVENCYFPMFVSQGALEKEKTHIADF 1113
Cdd:TIGR00408 2 ASKMQDFSEWYHQILEKAEIIDYYPVKGCYVWLPYGFKIWKNIQKILRNILDEIGHEEVYFPMLIPESELAKEKDHIKGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1114 APEVAWVTRSGKTELAEPIAVRPTSETVMYPAYAKWVQSHRDLPIRLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFA 1193
Cdd:TIGR00408 82 EPEVYWITHGGLSKLDEPLALRPTSETAMYPMFKKWVKSYTDLPLKINQWVNVFRYETKHTRPFLRTREFTWQEAHTAHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1194 TFEEAAEEVLQILDLYAQVYEELLAIPVVKGRKTEKEKFAGGDYTTTLEVfISASGRAIQGATSHHLGQNFSKMFEIIFE 1273
Cdd:TIGR00408 162 TAEEAEEQVLRALDIYKEFIENSLAIPYFVGRKPEWEKFAGAEYTWAFET-IMPDGRTLQIATSHNLGQNFAKTFEIKFE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1274 DPKmpGEKQFAYQNSWGLTTRTIGVMTMVHGDNMGLVLPPRVASVQVMVIPCgitnALSEEDREALIAKCNDYRRRLLSV 1353
Cdd:TIGR00408 241 TPT--GDKEYAYQTSYGISTRVIGALIAIHSDEKGLVLPPRVAPIQVVIIPI----IFKKKENEKVMEAAREVRSRLKKA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1354 NIRVRVDLRENySPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVADNEAETKLHALLEDIHVNLFTRAS 1433
Cdd:TIGR00408 315 GFRVHIDDRDN-RPGRKFYQWEIKGIPLRIEVGPNDIEKNIAVISRRDTGEKYQVSLDQLEERVVELLNNIQENLRNRAW 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1434 EDLKTHMVVANTMEDFQKML-DSGKIAQIPFCGEIDCEDWIKKTTArdqdlepgapsmgAKSLCVPFKPlcelQPGARCV 1512
Cdd:TIGR00408 394 ERFEQKIVIVETLEEIKQALnEKRGVVLVPWCGEEECEEDLKEKVQ-------------VTILCIPEDG----DVLQLCI 456
|
490
....*....|....*..
gi 1826797428 1513 -CGRnAAKYYTLFGRSY 1528
Cdd:TIGR00408 457 fCGR-KAPDYVLIARTY 472
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
1039-1302 |
9.50e-168 |
|
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: 504.44 E-value: 9.50e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1039 NLADWYSQVITKSELIEYYDVSGCYILRPWAYSIWESIKDFFDAEIKKLGVENCYFPMFVSQGALEKEKTHIADFAPEVA 1118
Cdd:cd00778 1 DFSEWYTEVITKAELIDYGPVKGCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPESELEKEKEHIEGFAPEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1119 WVTRSGKTELAEPIAVRPTSETVMYPAYAKWVQSHRDLPIRLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATFEEA 1198
Cdd:cd00778 81 WVTHGGLEELEEPLALRPTSETAIYPMFSKWIRSYRDLPLKINQWVNVFRWETKTTRPFLRTREFLWQEGHTAHATEEEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1199 AEEVLQILDLYAQVYEELLAIPVVKGRKTEKEKFAGGDYTTTLEVFISaSGRAIQGATSHHLGQNFSKMFEIIFEDPKmp 1278
Cdd:cd00778 161 EEEVLQILDLYKEFYEDLLAIPVVKGRKTEWEKFAGADYTYTIEAMMP-DGRALQSGTSHNLGQNFSKAFDIKYQDKD-- 237
|
250 260
....*....|....*....|....
gi 1826797428 1279 GEKQFAYQNSWGLTTRTIGVMTMV 1302
Cdd:cd00778 238 GQKEYVHQTSWGISTRLIGAIIMI 261
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
254-521 |
6.39e-129 |
|
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: 402.85 E-value: 6.39e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 254 HYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPD-QFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKA 332
Cdd:pfam00749 27 LYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDyGPYYQSDRFDIYYKYAEELIKKGKAYVCFCTPEELEE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 333 E--------------PIEKNLQMW-EEMKKGSQFGQSCCLRAKIDMSSNnGCMRDPTLYRCKIQP---HPRTGNKYNVYP 394
Cdd:pfam00749 107 EreeqealgspsrdrYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVFRDPVRGRIKFTPqeiHDRTGVKWDGYP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 395 TYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIR-KPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPR 473
Cdd:pfam00749 186 TYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLNLDGTKLSKRKLSWSVDISQVKGWGDPR 265
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1826797428 474 FPTVRGVLRRGMTVEGLKQFIAAQGSSRSV-VNMEWDKIWAFNKKVIDP 521
Cdd:pfam00749 266 EATLNGLRRRGWTPEGIREFFTREGVIKSFdVNRLSKSLEAFDRKKLDW 314
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
254-709 |
3.34e-116 |
|
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: 377.63 E-value: 3.34e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 254 HYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAE 333
Cdd:TIGR00463 119 EYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFREL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 334 ------------PIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACP 401
Cdd:TIGR00463 199 rnrgeachcrdrSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVA 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 402 IVDSIEGVTHALRTTEYHD--RDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVnEGLVDGWDDPRFPTVRG 479
Cdd:TIGR00463 279 IDDHLLGVTHVLRGKDHIDnrRKQEYIYRYFGWEPPEFIHWGRLKIDDVRALSTSSARKGIL-RGEYSGWDDPRLPTLRA 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 480 VLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLK-KEVIPVNIPEAQEEMKevAKHPKNPDV 558
Cdd:TIGR00463 358 IRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIIDEEARRYFFIWNpVKIEIVGLPEPKRVER--PLHPDHPEI 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 559 GLKPVWYSPKVFIEGADAETLSegEMVTFINWGNINITKINknadgkivSLDAKLNLENKDYKKTTKITWLAETAhalPI 638
Cdd:TIGR00463 436 GERVLILRGEIYVPKDDLEEGV--EPVRLMDAVNVIYSKKE--------LRYHSEGLEGARKLGKSIIHWLPAKD---AV 502
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1826797428 639 PAICVTYEHLITKPVLGKDEDFkqyvnknskheelmlgdpclkdLKKGDIIQLQRRGFFICDQPYEPVSPY 709
Cdd:TIGR00463 503 KVKVIMPDASIVEGVIEADASE----------------------LEVGDVVQFERFGFARLDSADKDGMVF 551
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
255-525 |
1.28e-115 |
|
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: 363.50 E-value: 1.28e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 255 YQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVddtpaeqmkaep 334
Cdd:cd00807 28 YAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQLYEYAEQLIKKGKAYV------------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 335 ieknlqmweemkkgsqfgqscclrakidmssnngcmrdptlyrckiqpHPRTGNKYNVYPTYDFACPIVDSIEGVTHALR 414
Cdd:cd00807 96 ------------------------------------------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLC 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 415 TTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFI 494
Cdd:cd00807 128 TLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFI 207
|
250 260 270
....*....|....*....|....*....|.
gi 1826797428 495 AAQGSSRSVVNMEWDKIWAFNKKVIDPVAPR 525
Cdd:cd00807 208 LRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
1043-1421 |
6.16e-84 |
|
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: 287.05 E-value: 6.16e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1043 WYSQVITKSELIEYYdVSGCYILRPWAYSIWESIKDFFDAEIKKLGVENCYFPMFVSqGALEKEKTHIADFAPEVAWVtr 1122
Cdd:COG0442 21 WSHQLMLRAGLIRKL-ASGIYTYLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQP-AELWEESGRWEGFGPELARV-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1123 sgKTELAEPIAVRPTSETVMYPAYAKWVQSHRDLPIRLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATFEEAAEEV 1202
Cdd:COG0442 97 --TDRLEREFCLGPTHEEVITDLVRNEIKSYRDLPLLLYQIQTKFRDEIRPRFGLLRTREFLMKDAYSFHATEEELDEEY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1203 LQILDLYAQVYEElLAIPVVKGRKT-------EKEKFA--------------GGDYTTTLEV------------------ 1243
Cdd:COG0442 175 QKMLDAYERIFER-LGLPVRAVEADsgaiggsESHEFMvladsgedtivycdACDYAANIEKaealappaeraeptkele 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1244 ------------------------------------------------------------------------------FI 1245
Cdd:COG0442 254 avatpgaktieevaeflgvpaektvktlvykadgelvavlvrgdhelneiklenllgaselelateeeieaalgavpgFL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1246 SASG----------------------------------------------------------------RAIQGATSHHLG 1261
Cdd:COG0442 334 GPVGlgvpyiadrsvagmsnfvcganeddyhytnvnwgrdfpvdevadlrnvvegdpcpdcggllqdgRGIEVGHIFKLG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1262 QNFSKMFEIIFEDPKmpGEKQFAYQNSWGLT-TRTIGVMTMVHGDNMGLVLPPRVASVQVMVIPCGITNalseedrEALI 1340
Cdd:COG0442 414 TKYSKAMDATFLDEN--GKEQPVWMGCYGIGvTRLIAAAIEQHHDDKGIIWPPAIAPFQVVIVPINMKD-------EAVL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1341 AKCNDYRRRLLSVNIRVRVDLRENySPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVADNEAETKLHAL 1420
Cdd:COG0442 485 EAAEELYAELKAAGIDVLLDDRDE-RPGVKFADAELIGIPLRIVIGPRDLEEGQVEVKRRDTGEKEEVPLDELVETVKEL 563
|
.
gi 1826797428 1421 L 1421
Cdd:COG0442 564 L 564
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
259-502 |
6.62e-45 |
|
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: 169.97 E-value: 6.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 259 FKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQ-FTYTSDHFETIMKYAEKLIQEGKAYVDDTPAE---QMKAEP 334
Cdd:COG0008 35 YGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEgPYYQSDRFDIYYEYAEKLIEKGKAYVCFCTPEeleALRETQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 335 IEKNLQMW----------EEMKKGSQFGQSCCLRAKI--------DMSS-----NNGCMRDPTLYRckiqphpRTGnkyn 391
Cdd:COG0008 115 TAPGKPPRydgrcrdlspEELERMLAAGEPPVLRFKIpeegvvfdDLVRgeitfPNPNLRDPVLYR-------ADG---- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 392 vYPTYDFACPIVDSIEGVTHALRT------TEYHDrdeqfyWIIEALGIRKPyiwEYSRLNL----NNTVLSKRKltwfv 461
Cdd:COG0008 184 -YPTYNFAVVVDDHLMGITHVIRGeehlsnTPRQI------WLYEALGWEPP---EFAHLPLilgpDGTKLSKRK----- 248
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1826797428 462 neGLVdgwddprfpTVRGVLRRGMTVEGLKQFIAAQGSSRS 502
Cdd:COG0008 249 --GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
772-821 |
9.26e-25 |
|
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: 98.08 E-value: 9.26e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1826797428 772 LYNRVAAQGDVVRELKAKKAAKEDIDAAVKQLLALKAEYKEKTGQEYKPG 821
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
772-824 |
1.94e-24 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 97.18 E-value: 1.94e-24
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1826797428 772 LYNRVAAQGDVVRELKAKKAAKEDIDAAVKQLLALKAEYKEKTGQEYKPGNPP 824
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 ... |
773-825 |
3.22e-22 |
|
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: 91.25 E-value: 3.22e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1826797428 773 YNRVAAQGDVVRELKAKKAAKEDIDAAVKQLLALKAEYKEKTGQEYKPGNPPA 825
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPG 53
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
844-893 |
2.74e-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: 88.45 E-value: 2.74e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1826797428 844 LYDEVAAQGEVVRKLKAEKAPKAKVNEAVECLLSLKAQYKEKTGKEYIPG 893
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
920-972 |
4.67e-21 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 87.55 E-value: 4.67e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1826797428 920 LFDEVASQGEVVRKLKAEKASKDQVDTAVQELLQLKAQYKSLTGIEYKPVSAT 972
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
920-968 |
1.85e-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: 85.75 E-value: 1.85e-20
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1826797428 920 LFDEVASQGEVVRKLKAEKASKDQVDTAVQELLQLKAQYKSLTGIEYKP 968
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKP 49
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
1319-1417 |
3.06e-20 |
|
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: 86.87 E-value: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1319 QVMVIPCGitnalseEDREALIAKCNDYRRRLLSVNIRVRVDLReNYSPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAV 1398
Cdd:pfam03129 1 QVVVIPLG-------EKAEELEEYAQKLAEELRAAGIRVELDDR-NESIGKKFRRADLIGIPFALVVGEKELEEGTVTVR 72
|
90
....*....|....*....
gi 1826797428 1399 RRDTGEKLTVADNEAETKL 1417
Cdd:pfam03129 73 RRDTGEQETVSLDELVEKL 91
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
844-896 |
3.54e-20 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 85.24 E-value: 3.54e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1826797428 844 LYDEVAAQGEVVRKLKAEKAPKAKVNEAVECLLSLKAQYKEKTGKEYIPGQPP 896
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
|
|
| ProRS-C_1 |
smart00946 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
1446-1528 |
1.15e-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: 84.16 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1446 MEDFQKMLDSGKIAQIPFCGEIDCEDWIKKTTardqdlepgapsmGAKSLCVPFKplcELQPGARCVCGRNAAKYYTLFG 1525
Cdd:smart00946 1 LEEFKKALEEGKFVLAPWCGDEECEEKIKEET-------------GATIRCIPFD---QDEEPGKCVVCGKPAKKWVLFA 64
|
...
gi 1826797428 1526 RSY 1528
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 ... |
921-974 |
2.59e-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: 82.77 E-value: 2.59e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1826797428 921 FDEVASQGEVVRKLKAEKASKDQVDTAVQELLQLKAQYKSLTGIEYKPVSATGA 974
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGD 54
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
845-896 |
3.64e-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: 3.64e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1826797428 845 YDEVAAQGEVVRKLKAEKAPKAKVNEAVECLLSLKAQYKEKTGKEYIPGQPP 896
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPP 52
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
1260-1421 |
1.35e-08 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 59.33 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1260 LGQNFSKMFEIIFEDPKmpGEKQFAYQNSWGlttrtIGVMTMV------HGDNMGLVLPPRVASVQVMVIPcgiTNALSE 1333
Cdd:PRK09194 412 LGTKYSEAMNATVLDEN--GKAQPLIMGCYG-----IGVSRLVaaaieqNHDEKGIIWPKAIAPFDVHIVP---VNMKDE 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1334 EDREA---LIAKcndyrrrLLSVNIRVRVDLReNYSPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVAD 1410
Cdd:PRK09194 482 EVKELaekLYAE-------LQAAGIEVLLDDR-KERPGVKFADADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPV 553
|
170
....*....|.
gi 1826797428 1411 NEAETKLHALL 1421
Cdd:PRK09194 554 DELVEFLKALK 564
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
776-813 |
2.01e-05 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 49.36 E-value: 2.01e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1826797428 776 VAAQGDVVRELKAKKAAKEDIDAAVKQLLALKAEYKEK 813
Cdd:PLN02734 16 VTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSAL 53
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
920-974 |
8.53e-05 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 47.05 E-value: 8.53e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1826797428 920 LFDEVASQGEVVRKLKAEKASKDQVDTAVQELLQLKAQYKSLTGIEYKPVSATGA 974
Cdd:PLN02734 12 KQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELQAAVGAGGD 66
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
846-890 |
2.23e-03 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 42.42 E-value: 2.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1826797428 846 DEVAAQGEVVRKLKAEKAPKAKVNEAVECLLSLKAQyKEKTGKEY 890
Cdd:PLN02734 14 AAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLE-KSALEKEL 57
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
90-730 |
0e+00 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 722.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 90 PPLGALLAVEhvKGDVSI----SLEEGKENILYVSENVVFTDINSILRYLARVATTAGLYGSNLLEHTEIDHWLEFSATk 165
Cdd:PLN02907 12 PPLAVIAAAK--VAGVPLtidpSLKSGSAPTLLFSSGEKLTGTNVLLRYIARSASLPGFYGQDAFESSQVDEWLDYAPT- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 166 LSSCNLFTSAINELNHCLSLRTYLVGNSLSLADLCVWATLKGSAAWQEQLKQNKAPVHVKRWFGFLEAQ----------- 234
Cdd:PLN02907 89 FSSGSEFENACEYVDGYLASRTFLVGYSLTIADIAIWSGLAGSGQRWESLRKSKKYQNLVRWFNSISAEysdilnevtaa 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 235 -------------QAFQSVGTKWNVSATKAKVHYQVN--------------------------------------FKGKL 263
Cdd:PLN02907 169 yvgkrgagkpaaaKSKEKVADAGKADGAKDKGSFEVDlpgaeegkvctrfppepsgylhighakaallnqyfarrYKGKL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 264 IMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAE---------- 333
Cdd:PLN02907 249 IVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKErmdgieskcr 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 334 --PIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTH 411
Cdd:PLN02907 329 nnSVEENLRLWKEMIAGSERGLQCCVRGKLDMQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTH 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 412 ALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLK 491
Cdd:PLN02907 409 ALRSSEYHDRNAQYYRILEDMGLRKVHIWEFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALK 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 492 QFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLKKEVIPV---NIPEaQEEMKEVAKHPKNPDVGLKPVWYSPK 568
Cdd:PLN02907 489 QFILSQGASKNLNLMEWDKLWTINKKIIDPVCPRHTAVLKEGRVLLtltDGPE-TPFVRIIPRHKKYEGAGKKATTFTNR 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 569 VFIEGADAETLSEGEMVTFINWGNINITKINKNADGKIVSLDAKLNLENkDYKKTT-KITWLAETAHALPIPaiCVTYEH 647
Cdd:PLN02907 568 IWLDYADAEAISEGEEVTLMDWGNAIIKEITKDEGGAVTALSGELHLEG-SVKTTKlKLTWLPDTNELVPLS--LVEFDY 644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 648 LITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDQPYEPVSpysckeAPCVLIYVPDGHTK 727
Cdd:PLN02907 645 LITKKKLEEDDNFLDVLNPCTKKETAALGDSNMRNLKRGEIIQLERKGYYRCDAPFVRSS------KPIVLFAIPDGRQQ 718
|
...
gi 1826797428 728 EMP 730
Cdd:PLN02907 719 KSG 721
|
|
| proS_fam_I |
TIGR00408 |
prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ... |
1034-1528 |
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: 567.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1034 AKKEENLADWYSQVITKSELIEYYDVSGCYILRPWAYSIWESIKDFFDAEIKKLGVENCYFPMFVSQGALEKEKTHIADF 1113
Cdd:TIGR00408 2 ASKMQDFSEWYHQILEKAEIIDYYPVKGCYVWLPYGFKIWKNIQKILRNILDEIGHEEVYFPMLIPESELAKEKDHIKGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1114 APEVAWVTRSGKTELAEPIAVRPTSETVMYPAYAKWVQSHRDLPIRLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFA 1193
Cdd:TIGR00408 82 EPEVYWITHGGLSKLDEPLALRPTSETAMYPMFKKWVKSYTDLPLKINQWVNVFRYETKHTRPFLRTREFTWQEAHTAHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1194 TFEEAAEEVLQILDLYAQVYEELLAIPVVKGRKTEKEKFAGGDYTTTLEVfISASGRAIQGATSHHLGQNFSKMFEIIFE 1273
Cdd:TIGR00408 162 TAEEAEEQVLRALDIYKEFIENSLAIPYFVGRKPEWEKFAGAEYTWAFET-IMPDGRTLQIATSHNLGQNFAKTFEIKFE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1274 DPKmpGEKQFAYQNSWGLTTRTIGVMTMVHGDNMGLVLPPRVASVQVMVIPCgitnALSEEDREALIAKCNDYRRRLLSV 1353
Cdd:TIGR00408 241 TPT--GDKEYAYQTSYGISTRVIGALIAIHSDEKGLVLPPRVAPIQVVIIPI----IFKKKENEKVMEAAREVRSRLKKA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1354 NIRVRVDLRENySPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVADNEAETKLHALLEDIHVNLFTRAS 1433
Cdd:TIGR00408 315 GFRVHIDDRDN-RPGRKFYQWEIKGIPLRIEVGPNDIEKNIAVISRRDTGEKYQVSLDQLEERVVELLNNIQENLRNRAW 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1434 EDLKTHMVVANTMEDFQKML-DSGKIAQIPFCGEIDCEDWIKKTTArdqdlepgapsmgAKSLCVPFKPlcelQPGARCV 1512
Cdd:TIGR00408 394 ERFEQKIVIVETLEEIKQALnEKRGVVLVPWCGEEECEEDLKEKVQ-------------VTILCIPEDG----DVLQLCI 456
|
490
....*....|....*..
gi 1826797428 1513 -CGRnAAKYYTLFGRSY 1528
Cdd:TIGR00408 457 fCGR-KAPDYVLIARTY 472
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
254-729 |
1.57e-168 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 517.26 E-value: 1.57e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 254 HYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAE 333
Cdd:PLN03233 37 YYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 334 PIEKN------------LQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACP 401
Cdd:PLN03233 117 RADRAeskhrnqspeeaLEMFKEMCSGKEEGGAWCLRAKIDMQSDNGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 402 IVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVL 481
Cdd:PLN03233 197 IVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARMNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGIS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 482 RRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLKKEVIPVNIPEAQEE----MKEVAKHPKNPD 557
Cdd:PLN03233 277 RRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRFMAIDKADHTALTVTNADEEadfaFSETDCHPKDPG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 558 VGLKPVWYSPKVFIEGADAETLSEGEMVTFINWGNINITKINKNADGKIVSldaklnleNKDYKKTT-KITWLAETAHAl 636
Cdd:PLN03233 357 FGKRAMRICDEVLLEKADTEDIQLGEDIVLLRWGVIEISKIDGDLEGHFIP--------DGDFKAAKkKISWIADVSDN- 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 637 pIPAICVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDQPYepVSPysckEAPC 716
Cdd:PLN03233 428 -IPVVLSEFDNLIIKEKLEEDDKFEDFINPDTLAETDVIGDAGLKTLKEHDIIQLERRGFYRVDRPY--MGE----EKPL 500
|
490
....*....|...
gi 1826797428 717 VLIYVPDGHTKEM 729
Cdd:PLN03233 501 ILFMIPDGKKKAM 513
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
1039-1302 |
9.50e-168 |
|
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: 504.44 E-value: 9.50e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1039 NLADWYSQVITKSELIEYYDVSGCYILRPWAYSIWESIKDFFDAEIKKLGVENCYFPMFVSQGALEKEKTHIADFAPEVA 1118
Cdd:cd00778 1 DFSEWYTEVITKAELIDYGPVKGCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPESELEKEKEHIEGFAPEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1119 WVTRSGKTELAEPIAVRPTSETVMYPAYAKWVQSHRDLPIRLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATFEEA 1198
Cdd:cd00778 81 WVTHGGLEELEEPLALRPTSETAIYPMFSKWIRSYRDLPLKINQWVNVFRWETKTTRPFLRTREFLWQEGHTAHATEEEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1199 AEEVLQILDLYAQVYEELLAIPVVKGRKTEKEKFAGGDYTTTLEVFISaSGRAIQGATSHHLGQNFSKMFEIIFEDPKmp 1278
Cdd:cd00778 161 EEEVLQILDLYKEFYEDLLAIPVVKGRKTEWEKFAGADYTYTIEAMMP-DGRALQSGTSHNLGQNFSKAFDIKYQDKD-- 237
|
250 260
....*....|....*....|....
gi 1826797428 1279 GEKQFAYQNSWGLTTRTIGVMTMV 1302
Cdd:cd00778 238 GQKEYVHQTSWGISTRLIGAIIMI 261
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
259-802 |
8.03e-157 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 489.09 E-value: 8.03e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 259 FKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQF-TYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKA----- 332
Cdd:PTZ00402 83 YKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGpTYSSDYMDLMYEKAEELIKKGLAYCDKTPREEMQKcrfdg 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 333 -------EPIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDS 405
Cdd:PTZ00402 163 vptkyrdISVEETKRLWNEMKKGSAEGQETCLRAKISVDNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDS 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 406 IEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGM 485
Cdd:PTZ00402 243 VEGVTHALRTNEYHDRNDQYYWFCDALGIRKPIVEDFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 486 TVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLKKEVIPVNIpEAQEEMKEVAK--HPKNPDVGLKPV 563
Cdd:PTZ00402 323 KMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILDPSVPRYTVVSNTLKVRCTV-EGQIHLEACEKllHKKVPDMGEKTY 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 564 WYSPKVFIEGADAETLSEGEMVTFINWGNINITKINK-NADGKIVSLDAKLNLENkDYKKTT-KITWLAETAHALPIPai 641
Cdd:PTZ00402 402 YKSDVIFLDAEDVALLKEGDEVTLMDWGNAYIKNIRRsGEDALITDADIVLHLEG-DVKKTKfKLTWVPESPKAEVME-- 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 642 CVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDQpyepvspyscKEAPCVLIYV 721
Cdd:PTZ00402 479 LNEYDHLLTKKKPDPEESIDDIIAPVTKYTQEVYGEEALSVLKKGDIIQLERRGYYIVDD----------VTPKKVLIAI 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 722 PDGhtkemptsgsREKTKVETTKNEPTTPFKERPGPSLDNtcapsedslvlynrvaaqgdvvrELKAKKAAKEDIDAAVK 801
Cdd:PTZ00402 549 PDG----------REKVNHLSAKAQYLKTLPKKGIASAAN-----------------------DLAAKRAAKAAKKAAQK 595
|
.
gi 1826797428 802 Q 802
Cdd:PTZ00402 596 Q 596
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
254-521 |
6.39e-129 |
|
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: 402.85 E-value: 6.39e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 254 HYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPD-QFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKA 332
Cdd:pfam00749 27 LYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDyGPYYQSDRFDIYYKYAEELIKKGKAYVCFCTPEELEE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 333 E--------------PIEKNLQMW-EEMKKGSQFGQSCCLRAKIDMSSNnGCMRDPTLYRCKIQP---HPRTGNKYNVYP 394
Cdd:pfam00749 107 EreeqealgspsrdrYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVFRDPVRGRIKFTPqeiHDRTGVKWDGYP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 395 TYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIR-KPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPR 473
Cdd:pfam00749 186 TYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLNLDGTKLSKRKLSWSVDISQVKGWGDPR 265
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1826797428 474 FPTVRGVLRRGMTVEGLKQFIAAQGSSRSV-VNMEWDKIWAFNKKVIDP 521
Cdd:pfam00749 266 EATLNGLRRRGWTPEGIREFFTREGVIKSFdVNRLSKSLEAFDRKKLDW 314
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
259-715 |
1.44e-120 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 389.46 E-value: 1.44e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 259 FKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKP-DQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKA----- 332
Cdd:PRK05347 60 YGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWsGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREyrgtl 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 333 -EP----------IEKNLQMWEEMKKGsQF--GqSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFA 399
Cdd:PRK05347 140 tEPgknspyrdrsVEENLDLFERMRAG-EFpeG-SAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 400 CPIVDSIEGVTHALRTTEYHD-RdeQFY-WIIEALGIR-KPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPT 476
Cdd:PRK05347 218 HCISDAIEGITHSLCTLEFEDhR--PLYdWVLDNLPIPpHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 477 VRGVLRRGMTVEGLKQFIAAQGSSR--SVVNM---EwdkiwAFNKKVIDPVAPRYVALLK--KEVIpVNIPEAQEEMKEV 549
Cdd:PRK05347 296 ISGLRRRGYTPESIREFCERIGVTKqdSVIDMsmlE-----SCIREDLNENAPRAMAVLDplKLVI-TNYPEGQVEELEA 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 550 AKHPKNPDVGLKPVWYSPKVFIEGAD-AET-------LSEGEMVTFINWGNINITKINKNADGKIVSL------DAKLNL 615
Cdd:PRK05347 370 PNHPEDPEMGTREVPFSRELYIEREDfMEEppkkyfrLVPGKEVRLRNAYVIKCEEVVKDADGNITEIhctydpDTLSGN 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 616 ENKDYK-KTTkITWLaETAHAlpIPAICVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQLQRR 694
Cdd:PRK05347 450 PADGRKvKGT-IHWV-SAAHA--VPAEVRLYDRLFTVPNPAAGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFERE 525
|
490 500
....*....|....*....|.
gi 1826797428 695 GFFICDqpyepvsPYSCKEAP 715
Cdd:PRK05347 526 GYFCAD-------KDSTPGKL 539
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
254-709 |
3.34e-116 |
|
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: 377.63 E-value: 3.34e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 254 HYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAE 333
Cdd:TIGR00463 119 EYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFREL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 334 ------------PIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACP 401
Cdd:TIGR00463 199 rnrgeachcrdrSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVA 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 402 IVDSIEGVTHALRTTEYHD--RDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVnEGLVDGWDDPRFPTVRG 479
Cdd:TIGR00463 279 IDDHLLGVTHVLRGKDHIDnrRKQEYIYRYFGWEPPEFIHWGRLKIDDVRALSTSSARKGIL-RGEYSGWDDPRLPTLRA 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 480 VLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLK-KEVIPVNIPEAQEEMKevAKHPKNPDV 558
Cdd:TIGR00463 358 IRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIIDEEARRYFFIWNpVKIEIVGLPEPKRVER--PLHPDHPEI 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 559 GLKPVWYSPKVFIEGADAETLSegEMVTFINWGNINITKINknadgkivSLDAKLNLENKDYKKTTKITWLAETAhalPI 638
Cdd:TIGR00463 436 GERVLILRGEIYVPKDDLEEGV--EPVRLMDAVNVIYSKKE--------LRYHSEGLEGARKLGKSIIHWLPAKD---AV 502
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1826797428 639 PAICVTYEHLITKPVLGKDEDFkqyvnknskheelmlgdpclkdLKKGDIIQLQRRGFFICDQPYEPVSPY 709
Cdd:TIGR00463 503 KVKVIMPDASIVEGVIEADASE----------------------LEVGDVVQFERFGFARLDSADKDGMVF 551
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
255-525 |
1.28e-115 |
|
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: 363.50 E-value: 1.28e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 255 YQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVddtpaeqmkaep 334
Cdd:cd00807 28 YAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQLYEYAEQLIKKGKAYV------------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 335 ieknlqmweemkkgsqfgqscclrakidmssnngcmrdptlyrckiqpHPRTGNKYNVYPTYDFACPIVDSIEGVTHALR 414
Cdd:cd00807 96 ------------------------------------------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLC 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 415 TTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFI 494
Cdd:cd00807 128 TLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFI 207
|
250 260 270
....*....|....*....|....*....|.
gi 1826797428 495 AAQGSSRSVVNMEWDKIWAFNKKVIDPVAPR 525
Cdd:cd00807 208 LRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
255-700 |
1.46e-89 |
|
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: 301.84 E-value: 1.46e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 255 YQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPD-QFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMK-- 331
Cdd:TIGR00440 27 YAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEgKIRYSSDYFDELYRYAEELIKKGLAYVDELTPEEIRey 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 332 ----AEP----------IEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYD 397
Cdd:TIGR00440 107 rgtlTDPgknspyrdrsIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMRDPVAYRIKFAPHHQTGTKWCIYPMYD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 398 FACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGI-RKPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPT 476
Cdd:TIGR00440 187 FTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIfPRPAQYEFSRLNLEGTVLSKRKLAQLVDDKFVRGWDDPRMPT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 477 VRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLKKEVIPVNIPEAQEEMKEVAKHPKNP 556
Cdd:TIGR00440 267 ISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVIDPVEVVIENLSDEYELATIPNHPNTP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 557 DVGLKPVWYSPKVFIEGADAET--------LSEGEMVTFINWGNINITKINKNADGKIVSL----DAK-LNLENKDYKKT 623
Cdd:TIGR00440 347 EFGERQVPFTNEFYIDRADFREeankqykrLVLGKEVRLRNAYVIKAERVEKDAAGKITTIfctyDNKtLGKEPADGRKV 426
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1826797428 624 -TKITWLAeTAHALPIPAicVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICD 700
Cdd:TIGR00440 427 kGVIHWVS-ASSKYPTET--RLYDRLFKVPNPGAPDDFLSVINPESLVIKQGFMEHSLGDAVANKRFQFEREGYFCLD 501
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
1043-1421 |
6.16e-84 |
|
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: 287.05 E-value: 6.16e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1043 WYSQVITKSELIEYYdVSGCYILRPWAYSIWESIKDFFDAEIKKLGVENCYFPMFVSqGALEKEKTHIADFAPEVAWVtr 1122
Cdd:COG0442 21 WSHQLMLRAGLIRKL-ASGIYTYLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQP-AELWEESGRWEGFGPELARV-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1123 sgKTELAEPIAVRPTSETVMYPAYAKWVQSHRDLPIRLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATFEEAAEEV 1202
Cdd:COG0442 97 --TDRLEREFCLGPTHEEVITDLVRNEIKSYRDLPLLLYQIQTKFRDEIRPRFGLLRTREFLMKDAYSFHATEEELDEEY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1203 LQILDLYAQVYEElLAIPVVKGRKT-------EKEKFA--------------GGDYTTTLEV------------------ 1243
Cdd:COG0442 175 QKMLDAYERIFER-LGLPVRAVEADsgaiggsESHEFMvladsgedtivycdACDYAANIEKaealappaeraeptkele 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1244 ------------------------------------------------------------------------------FI 1245
Cdd:COG0442 254 avatpgaktieevaeflgvpaektvktlvykadgelvavlvrgdhelneiklenllgaselelateeeieaalgavpgFL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1246 SASG----------------------------------------------------------------RAIQGATSHHLG 1261
Cdd:COG0442 334 GPVGlgvpyiadrsvagmsnfvcganeddyhytnvnwgrdfpvdevadlrnvvegdpcpdcggllqdgRGIEVGHIFKLG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1262 QNFSKMFEIIFEDPKmpGEKQFAYQNSWGLT-TRTIGVMTMVHGDNMGLVLPPRVASVQVMVIPCGITNalseedrEALI 1340
Cdd:COG0442 414 TKYSKAMDATFLDEN--GKEQPVWMGCYGIGvTRLIAAAIEQHHDDKGIIWPPAIAPFQVVIVPINMKD-------EAVL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1341 AKCNDYRRRLLSVNIRVRVDLRENySPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVADNEAETKLHAL 1420
Cdd:COG0442 485 EAAEELYAELKAAGIDVLLDDRDE-RPGVKFADAELIGIPLRIVIGPRDLEEGQVEVKRRDTGEKEEVPLDELVETVKEL 563
|
.
gi 1826797428 1421 L 1421
Cdd:COG0442 564 L 564
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
259-765 |
1.86e-82 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 288.93 E-value: 1.86e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 259 FKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIK-PDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKA----- 332
Cdd:PRK14703 62 YGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDwGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRElrgtv 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 333 -----------EPIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACP 401
Cdd:PRK14703 142 tepgtpspyrdRSVEENLDLFRRMRAGEFPDGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHP 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 402 IVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIR--KPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRG 479
Cdd:PRK14703 222 LEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPWppRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 480 VLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLKK-EVIPVNIPEAQEEMKEVAKHPKN-PD 557
Cdd:PRK14703 302 QRRRGVTPEAIRDFADQIGVAKTNSTVDIGVLEFAIRDDLNRRAPRVMAVLDPlKVVIENLPAGKVEELDLPYWPHDvPK 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 558 VGLKPVWYSPKVFIEGAD-AET-------LSEGEMVTFINWGNINITKINKNADGKIVSLDAKLNLENKDYKKTTK---- 625
Cdd:PRK14703 382 EGSRKVPFTRELYIERDDfSEDppkgfkrLTPGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDTGRkaag 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 626 -ITWLAeTAHALPIPAicVTYEHLITKPVL-GKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDqpy 703
Cdd:PRK14703 462 vIHWVS-AKHALPAEV--RLYDRLFKVPQPeAADEDFLEFLNPDSLRVAQGRVEPAVRDDPADTRYQFERQGYFWAD--- 535
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1826797428 704 ePVSpySCKEAPCVLIYVPdghTKEMPTSGSREKTKVETTKNEPTTPFKERPGPSLDNTCAP 765
Cdd:PRK14703 536 -PVD--SRPDALVFNRIIT---LKDTWGARAREAAREKRAAAPKKTAKPRRSKAEARAEAAA 591
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
1308-1528 |
2.53e-82 |
|
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: 268.78 E-value: 2.53e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1308 GLVLPPRVASVQVMVIPCGITnalsEEDREALIAKCNDYRRRLLSVNIRVRVDLRENYSPGWKFNHWELKGVPIRLEVGP 1387
Cdd:cd00862 1 GLVLPPRVAPIQVVIVPIGIK----DEKREEVLEAADELAERLKAAGIRVHVDDRDNYTPGWKFNDWELKGVPLRIEIGP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1388 RDMKSCQFVAVRRDTGEKLTVADNEAETKLHALLEDIHVNLFTRASEDLK-THMVVanTMEDFQKMLDSGKIAQIPFCGE 1466
Cdd:cd00862 77 RDLEKNTVVIVRRDTGEKKTVPLAELVEKVPELLDEIQEDLYERALEFRDaTRIVD--TWEEFKEALNEKGIVLAPWCGE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1826797428 1467 IDCEDWIKKTTArdqdlepgapsmgAKSLCVPFkPLCELQPGARCV-CGRNaAKYYTLFGRSY 1528
Cdd:cd00862 155 EECEEEIKEETA-------------ATILCIPF-DEAKLEEGGKCVvCGRP-AKAYARFAKSY 202
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
213-705 |
6.02e-81 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 278.79 E-value: 6.02e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 213 EQLKQNKAPVHVKRWFGFLEAQQAFQSVG--TKWNVSATKAKVHyqvnfKGKLIMRFDDTNPEKEKEDFEKVILEDVAML 290
Cdd:PTZ00437 39 ELLEKHEAVTGGKPYFRFPPEPNGFLHIGhaKSMNLNFGSARAH-----GGKCYLRYDDTNPETEEQVYIDAIMEMVKWM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 291 HIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAE------------PIEKNLQMWEEMKKGSQFGQSCCLR 358
Cdd:PTZ00437 114 GWKPDWVTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQreqredspwrnrSVEENLLLFEHMRQGRYAEGEATLR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 359 AKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPY 438
Cdd:PTZ00437 194 VKADMKSDNPNMRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWRPH 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 439 IWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKV 518
Cdd:PTZ00437 274 VWEFSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLRED 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 519 IDPVAPRYVALLkkEVIPVNIPEAQEEMK-EVAKHPKNPDVGLKPVWYSPKVFIEGADAET---------LSEGEMVTFI 588
Cdd:PTZ00437 354 LDERCERRLMVI--DPIKVVVDNWKGEREfECPNHPRKPELGSRKVMFTDTFYVDRSDFRTednnskfygLAPGPRVVGL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 589 NW-GNINITKINKNADGKIVSLDAKLNLENKDyKKTTKITWLAETAhalPIPAICVTYEHLITKPVLGKDEDFKQYVNKN 667
Cdd:PTZ00437 432 KYsGNVVCKGFEVDAAGQPSVIHVDIDFERKD-KPKTNISWVSATA---CTPVEVRLYNALLKDDRAAIDPEFLKFIDED 507
|
490 500 510
....*....|....*....|....*....|....*...
gi 1826797428 668 SKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDQPYEP 705
Cdd:PTZ00437 508 SEVVSHGYAEKGIENAKHFESVQAERFGYFVVDPDTRP 545
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
261-705 |
2.58e-80 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 282.80 E-value: 2.58e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 261 GKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKA-------- 332
Cdd:PLN02859 297 GCCYLRFDDTNPEAEKKEYIDHIEEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEyrekkmns 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 333 ----EPIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEG 408
Cdd:PLN02859 377 pwrdRPIEESLKLFEDMRRGLIEEGKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLEN 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 409 VTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVE 488
Cdd:PLN02859 457 ITHSLCTLEFETRRASYYWLLDSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPT 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 489 GLKQFIAAQGSSRS---VVNMewDKIWAFNKKVIDPVAPRYVALLKK-EVIPVNIPEAQEEMKEVAKHPKNPDVGLKP-- 562
Cdd:PLN02859 537 AINAFCRGIGITRSdnsLIRM--DRLEHHIREELNKTAPRTMVVLHPlKVVITNLESGEVIELDAKRWPDAQNDDPSAfy 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 563 -VWYSPKVFIEGADAET--------LSEGEMVTFINWGNINITK-INKNADGKIVSLDAKLnlenkDYKKTTK----ITW 628
Cdd:PLN02859 615 kVPFSRVVYIERSDFRLkdskdyygLAPGKSVLLRYAFPIKCTDvVLADDNETVVEIRAEY-----DPEKKTKpkgvLHW 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 629 LAETAHAL-PIPAICVTYEHLITKPVLGKDEDFKQYVNKNSKheELMLGD---PCLKDLKKGDIIQLQRRGFFICDQPYE 704
Cdd:PLN02859 690 VAEPSPGVePLKVEVRLFDKLFLSENPAELEDWLEDLNPQSK--EVISGAyavPSLKDAKVGDRFQFERLGYFAVDKDST 767
|
.
gi 1826797428 705 P 705
Cdd:PLN02859 768 P 768
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
255-696 |
3.22e-75 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 261.71 E-value: 3.22e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 255 YQVNFKGKLIMRFDDTNPEKEKEDFE--KVILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKA 332
Cdd:PRK04156 128 YAKMYGGKFILRFEDTDPRTKRPDPEayDMILEDLKWLGVKWDEVVIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 333 ------------EPIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFAC 400
Cdd:PRK04156 208 lrdagkpcphrdKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPNPSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 401 PIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGV 480
Cdd:PRK04156 288 AVDDHLLGVTHVLRGKDHIDNTEKQRYIYDYFGWEYPETIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRAL 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 481 LRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALlkKEVIPVNIPEAQEEMKEVAKHPKNPDVGL 560
Cdd:PRK04156 368 RRRGILPEAIRELIIEVGVKETDATISWENLYAINRKLIDPIANRYFFV--RDPVELEIEGAEPLEAKIPLHPDRPERGE 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 561 KPVWYSPKVFIEGADAETLseGEMVTFINWGNINITKINKNAdGKIVSLDaklnLENKDYKKTTKITWLAETaHALPIPA 640
Cdd:PRK04156 446 REIPVGGKVYVSSDDLEAE--GKMVRLMDLFNVEITGVSVDK-ARYHSDD----LEEARKNKAPIIQWVPED-ESVPVRV 517
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1826797428 641 IcvtyehlitKPVLGKDEDFkqyvnknskheelmlGDPCLKDLKKGDIIQLQRRGF 696
Cdd:PRK04156 518 L---------KPDGGDIEGL---------------AEPDVADLEVDDIVQFERFGF 549
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
1039-1301 |
6.17e-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: 241.50 E-value: 6.17e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1039 NLADWYSQVITKSELIEYYDVSGCYILRPWAYSIWESIKDFFDAEIKKLGVENCYFPMFVSQGALEKEKTHIADFAPEVA 1118
Cdd:cd00772 1 DASEKSLEHIGKAELADQGPGRGIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGFSKELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1119 WVTRSGKTELAEPIAVRPTSETVMYPAYAKWVQSHRDLPIRLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATFEEA 1198
Cdd:cd00772 81 VFKDAGDEELEEDFALRPTLEENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIRPRFGFLRAREFIMKDGHSAHADAEEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1199 AEEVLQILDLYAQVYEELLAIPVVKGRKTEKEKFAGGDYTTTLEVfISASGRAIQGATSHHLGQNFSKMFEIIFEDPKMP 1278
Cdd:cd00772 161 DEEFLNMLSAYAEIARDLAAIDFIEGEADEGAKFAGASKSREFEA-LMEDGKAKQAETGHIFGEGFARAFDLKAKFLDKD 239
|
250 260
....*....|....*....|....
gi 1826797428 1279 GEKQFAYQNSWGLT-TRTIGVMTM 1301
Cdd:cd00772 240 GKEKFFEMGCWGIGiSRFIGAIIE 263
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
255-525 |
9.16e-53 |
|
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: 185.63 E-value: 9.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 255 YQVNFKGKLIMRFDDTNPEKEKEDFE--KVILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVddtpaeqmka 332
Cdd:cd09287 28 YAKMYGGKFILRFDDTDPRTKRPDPEayDMIPEDLEWLGVKWDEVVIASDRIELYYEYARKLIEMGGAYV---------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 333 epieknlqmweemkkgsqfgqscclrakidmssnngcmrdptlyrckiqpHPRTGNKYNVYPTYDFACPIVDSIEGVTHA 412
Cdd:cd09287 98 --------------------------------------------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 413 LRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQ 492
Cdd:cd09287 128 LRGKDHIDNTEKQRYIYEYFGWEYPETIHWGRLKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRD 207
|
250 260 270
....*....|....*....|....*....|...
gi 1826797428 493 FIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPR 525
Cdd:cd09287 208 FIIEVGVKQTDATISWENLYAINRKLIDPRANR 240
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
523-700 |
1.28e-47 |
|
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: 168.22 E-value: 1.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 523 APRYVALLKKEVIPV-NIPEAQEEMKEVAKHPKNPDVGLKPVWYSPKVFIEGADAETLSEGEMVTFINWGNINITKINKN 601
Cdd:pfam03950 1 APRYMAVLDPVKVVIeNYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDFKRLAPGEEVRLMDAYNIKVTEVVKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 602 ADGKIVSLDAKLNLENKDY---KKTTKITWLAETAhalPIPAICVTYEHLITkpvlgKDEDFKQYVNKNSKHE-ELMLGD 677
Cdd:pfam03950 81 EDGNVTELHCTYDGDDLGGarkVKGKIIHWVSASD---AVPAEVRLYDRLFK-----DEDDADFLLNPDSLKVlTEGLAE 152
|
170 180
....*....|....*....|...
gi 1826797428 678 PCLKDLKKGDIIQLQRRGFFICD 700
Cdd:pfam03950 153 PALANLKPGDIVQFERIGYFRVD 175
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
259-502 |
6.62e-45 |
|
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: 169.97 E-value: 6.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 259 FKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQ-FTYTSDHFETIMKYAEKLIQEGKAYVDDTPAE---QMKAEP 334
Cdd:COG0008 35 YGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEgPYYQSDRFDIYYEYAEKLIEKGKAYVCFCTPEeleALRETQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 335 IEKNLQMW----------EEMKKGSQFGQSCCLRAKI--------DMSS-----NNGCMRDPTLYRckiqphpRTGnkyn 391
Cdd:COG0008 115 TAPGKPPRydgrcrdlspEELERMLAAGEPPVLRFKIpeegvvfdDLVRgeitfPNPNLRDPVLYR-------ADG---- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 392 vYPTYDFACPIVDSIEGVTHALRT------TEYHDrdeqfyWIIEALGIRKPyiwEYSRLNL----NNTVLSKRKltwfv 461
Cdd:COG0008 184 -YPTYNFAVVVDDHLMGITHVIRGeehlsnTPRQI------WLYEALGWEPP---EFAHLPLilgpDGTKLSKRK----- 248
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1826797428 462 neGLVdgwddprfpTVRGVLRRGMTVEGLKQFIAAQGSSRS 502
Cdd:COG0008 249 --GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
|
| GST_C_GluProRS_N |
cd10309 |
Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional ... |
151-234 |
3.66e-38 |
|
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: 137.45 E-value: 3.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 151 EHTEIDHWLEFSATKLSSCNLFTSAINELNHCLSLRTYLVGNSLSLADLCVWATLKGSAAWQEqlkQNKAPVHVKRWFGF 230
Cdd:cd10309 1 EQTEVDHWISFSAGRLSCDQDFSSALSYLDKALSLRTYLVGNSLTLADFAVWAALRGNGEWLA---SKEKYVNVTRWFKF 77
|
....
gi 1826797428 231 LEAQ 234
Cdd:cd10309 78 ISSQ 81
|
|
| 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 ... |
1069-1265 |
3.77e-30 |
|
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: 120.19 E-value: 3.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1069 AYSIWESIKDFFDAEIKKLGVENCYFPMFVSQGALEKEKtHIADFAPEVAWVTRSGKTELAEPIAVRPTSETVMYPAYAK 1148
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGG-HLDGYRKEMYTFEDKGRELRDTDLVLRPAACEPIYQIFSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1149 WVQSHRDLPIRLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSaFATFEEAAEEVLQILDLYAQVYEElLAIPVVKGRKTE 1228
Cdd:cd00670 80 EILSYRALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVEYVV-FGEPEEAEEERREWLELAEEIARE-LGLPVRVVVADD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1826797428 1229 KEKFAGGD--------YTTTLEVFISASGRAIQGATSHHLGQNFS 1265
Cdd:cd00670 158 PFFGRGGKrgldagreTVVEFELLLPLPGRAKETAVGSANVHLDH 202
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
772-821 |
9.26e-25 |
|
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: 98.08 E-value: 9.26e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1826797428 772 LYNRVAAQGDVVRELKAKKAAKEDIDAAVKQLLALKAEYKEKTGQEYKPG 821
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
259-501 |
1.81e-24 |
|
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: 103.71 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 259 FKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQ-FTYTSDHFETIMKYAEKLIQEGkayvddtpaeqmkaepiek 337
Cdd:cd00418 32 YGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEgPYRQSDRFDLYRAYAEELIKKG------------------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 338 nlqmweemkkgsqfgqscclrakidmssnngcmrdptlyrckiqphprtgnkynVYPTYDFACPIVDSIEGVTHALRTTE 417
Cdd:cd00418 93 ------------------------------------------------------GYPLYNFVHPVDDALMGITHVLRGED 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 418 YHDRDEQFYWIIEALGIRKPYIWEYSRLNL-NNTVLSKRKLtwfvneglvdgwddprFPTVRGVLRRGMTVEGLKQFIAA 496
Cdd:cd00418 119 HLDNTPIQDWLYEALGWEPPRFYHFPRLLLeDGTKLSKRKL----------------NTTLRALRRRGYLPEALRNYLAL 182
|
....*
gi 1826797428 497 QGSSR 501
Cdd:cd00418 183 IGWSK 187
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
772-824 |
1.94e-24 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 97.18 E-value: 1.94e-24
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1826797428 772 LYNRVAAQGDVVRELKAKKAAKEDIDAAVKQLLALKAEYKEKTGQEYKPGNPP 824
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
|
|
| GST_C_AaRS_like |
cd10289 |
Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA ... |
151-234 |
5.12e-23 |
|
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: 94.30 E-value: 5.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 151 EHTEIDHWLEFsATKLSSCNLFTSAINELNHCLSLRTYLVGNSLSLADLCVWATLKGSAAWQEQLKQNKaPVHVKRWFGF 230
Cdd:cd10289 1 EAAQVDQWLDL-AGSLLKGKELEALLKSLNSYLASRTFLVGYSLTLADVAVFSALYPSGQKLSDKEKKK-FPHVTRWFNH 78
|
....
gi 1826797428 231 LEAQ 234
Cdd:cd10289 79 IQNL 82
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
773-825 |
3.22e-22 |
|
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: 91.25 E-value: 3.22e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1826797428 773 YNRVAAQGDVVRELKAKKAAKEDIDAAVKQLLALKAEYKEKTGQEYKPGNPPA 825
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPG 53
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
844-893 |
2.74e-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: 88.45 E-value: 2.74e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1826797428 844 LYDEVAAQGEVVRKLKAEKAPKAKVNEAVECLLSLKAQYKEKTGKEYIPG 893
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
920-972 |
4.67e-21 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 87.55 E-value: 4.67e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1826797428 920 LFDEVASQGEVVRKLKAEKASKDQVDTAVQELLQLKAQYKSLTGIEYKPVSAT 972
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
920-968 |
1.85e-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: 85.75 E-value: 1.85e-20
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1826797428 920 LFDEVASQGEVVRKLKAEKASKDQVDTAVQELLQLKAQYKSLTGIEYKP 968
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKP 49
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
1319-1417 |
3.06e-20 |
|
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: 86.87 E-value: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1319 QVMVIPCGitnalseEDREALIAKCNDYRRRLLSVNIRVRVDLReNYSPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAV 1398
Cdd:pfam03129 1 QVVVIPLG-------EKAEELEEYAQKLAEELRAAGIRVELDDR-NESIGKKFRRADLIGIPFALVVGEKELEEGTVTVR 72
|
90
....*....|....*....
gi 1826797428 1399 RRDTGEKLTVADNEAETKL 1417
Cdd:pfam03129 73 RRDTGEQETVSLDELVEKL 91
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
844-896 |
3.54e-20 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 85.24 E-value: 3.54e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1826797428 844 LYDEVAAQGEVVRKLKAEKAPKAKVNEAVECLLSLKAQYKEKTGKEYIPGQPP 896
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
|
|
| ProRS-C_1 |
smart00946 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
1446-1528 |
1.15e-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: 84.16 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1446 MEDFQKMLDSGKIAQIPFCGEIDCEDWIKKTTardqdlepgapsmGAKSLCVPFKplcELQPGARCVCGRNAAKYYTLFG 1525
Cdd:smart00946 1 LEEFKKALEEGKFVLAPWCGDEECEEKIKEET-------------GATIRCIPFD---QDEEPGKCVVCGKPAKKWVLFA 64
|
...
gi 1826797428 1526 RSY 1528
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 ... |
921-974 |
2.59e-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: 82.77 E-value: 2.59e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1826797428 921 FDEVASQGEVVRKLKAEKASKDQVDTAVQELLQLKAQYKSLTGIEYKPVSATGA 974
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGD 54
|
|
| ProRS-C_1 |
pfam09180 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
1446-1528 |
2.73e-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: 462709 Cd Length: 67 Bit Score: 82.95 E-value: 2.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1446 MEDFQKMLDSGKIAQIPFCGEIDCEDWIKKTTardqdlepgapsmGAKSLCVPFKplcELQPGARCV-CGRNaAKYYTLF 1524
Cdd:pfam09180 1 WEEFKEALEEKGFVLAPWCGDEECEDKIKEET-------------GATSRCIPFD---QEEEGGKCIvCGKP-AKKWVLF 63
|
....
gi 1826797428 1525 GRSY 1528
Cdd:pfam09180 64 ARSY 67
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
845-896 |
3.64e-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: 3.64e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1826797428 845 YDEVAAQGEVVRKLKAEKAPKAKVNEAVECLLSLKAQYKEKTGKEYIPGQPP 896
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPP 52
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
1072-1291 |
6.85e-19 |
|
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: 86.79 E-value: 6.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1072 IWESIKDFFDAEIKKLGVENCYFPMFVSQGALEKEKTHIADFAPevawvtrsGKTELAEPIAVRPTSETvmYPAYAkWVQ 1151
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKDLLP--------VGAENEEDLYLRPTLEP--GLVRL-FVS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1152 SHRDLPIRLNQWCNVVRWEfKHPQPFLRTREFLWQEGHSAFATFEEaAEEVLQILDLYAQVYEEL-LAIPVVKGRKTEKE 1230
Cdd:cd00768 70 HIRKLPLRLAEIGPAFRNE-GGRRGLRRVREFTQLEGEVFGEDGEE-ASEFEELIELTEELLRALgIKLDIVFVEKTPGE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1826797428 1231 KFAGGdYTTTLEVFI-SASGRAIQGATSHHLGQNFSKMFEIIFEDPkmPGEKQFAYQNSWGL 1291
Cdd:cd00768 148 FSPGG-AGPGFEIEVdHPEGRGLEIGSGGYRQDEQARAADLYFLDE--ALEYRYPPTIGFGL 206
|
|
| GST_C_GluRS_N |
cd10306 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Glutamyl-tRNA synthetase; ... |
151-233 |
2.68e-17 |
|
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: 78.16 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 151 EHTEIDHWLEFSATKLSSCNL--FTSAINELNHCLSLRTYLVGNSLSLADLCVWATLKGSAAWQEQLKQNKAPvHVKRWF 228
Cdd:cd10306 3 DKEQVAEWIDFATTLLVLKDFkaLSQALEELDSHLTLRTFIVGYSLSLADIAVWGALRGNGVAGSLIKNKVYV-NLSRWF 81
|
....*
gi 1826797428 229 GFLEA 233
Cdd:cd10306 82 SFLES 86
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
773-814 |
4.29e-17 |
|
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: 76.04 E-value: 4.29e-17
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1826797428 773 YNRVAAQGDVVRELKAKKAAKEDIDAAVKQLLALKAEYKEKT 814
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
845-886 |
2.06e-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: 71.42 E-value: 2.06e-15
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1826797428 845 YDEVAAQGEVVRKLKAEKAPKAKVNEAVECLLSLKAQYKEKT 886
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
921-962 |
2.87e-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: 71.03 E-value: 2.87e-15
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1826797428 921 FDEVASQGEVVRKLKAEKASKDQVDTAVQELLQLKAQYKSLT 962
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 ... |
1127-1303 |
1.21e-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: 73.60 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1127 ELAEPIAVRPTSETVMYPAYAKWVQSHRDLPIRLNQWCNVVRWEFKHPQ-PFLRTREFLWQEGHSaFATFEEAAEEVLQI 1205
Cdd:pfam00587 6 ENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTrGLIRVRQFHQDDAHI-FHAPGQSPDELEDY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1206 LDLYAQVYEELLaIPVVKGRKTEKEKFAGGDYTTTLEVFISASGRAIQGATSHHLGQNFSKMFEIIFEDpkMPGEKQFAY 1285
Cdd:pfam00587 85 IKLIDRVYSRLG-LEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKD--EDNESKFPY 161
|
170 180
....*....|....*....|
gi 1826797428 1286 QNSWGL--TTRTIGVMTMVH 1303
Cdd:pfam00587 162 MIHRAGlgVERFLAAILENN 181
|
|
| GST_C_AIMP3 |
cd10305 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ... |
150-228 |
2.42e-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: 58.84 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 150 LEHTEIDHWLEFSATKLSSC---NLFTSAINELNHCLSLRTYLVGNSLSLADLCVWATLKG-----SAAWQEQLKqnkap 221
Cdd:cd10305 2 EERAQVDQWLEYRVTQVAPAsdkADAKSLLKELNSYLQDRTYLVGHKLTLADVVLYYGLHPimkdlSPQEKEQYL----- 76
|
....*..
gi 1826797428 222 vHVKRWF 228
Cdd:cd10305 77 -NVSRWF 82
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
1318-1417 |
1.07e-09 |
|
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: 56.64 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1318 VQVMVIPCGitnalseEDREALIAKCNDYRRRLLSVNIRVRVDLRENySPGWKFNHWELKGVPIRLEVGPRDMKSCQFVA 1397
Cdd:cd00738 2 IDVAIVPLT-------DPRVEAREYAQKLLNALLANGIRVLYDDRER-KIGKKFREADLRGVPFAVVVGEDELENGKVTV 73
|
90 100
....*....|....*....|
gi 1826797428 1398 VRRDTGEKLTVADNEAETKL 1417
Cdd:cd00738 74 KSRDTGESETLHVDELPEFL 93
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
1260-1421 |
1.35e-08 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 59.33 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1260 LGQNFSKMFEIIFEDPKmpGEKQFAYQNSWGlttrtIGVMTMV------HGDNMGLVLPPRVASVQVMVIPcgiTNALSE 1333
Cdd:PRK09194 412 LGTKYSEAMNATVLDEN--GKAQPLIMGCYG-----IGVSRLVaaaieqNHDEKGIIWPKAIAPFDVHIVP---VNMKDE 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1334 EDREA---LIAKcndyrrrLLSVNIRVRVDLReNYSPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVAD 1410
Cdd:PRK09194 482 EVKELaekLYAE-------LQAAGIEVLLDDR-KERPGVKFADADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPV 553
|
170
....*....|.
gi 1826797428 1411 NEAETKLHALL 1421
Cdd:PRK09194 554 DELVEFLKALK 564
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
924-957 |
3.68e-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: 50.93 E-value: 3.68e-08
10 20 30
....*....|....*....|....*....|....
gi 1826797428 924 VASQGEVVRKLKAEKASKDQVDTAVQELLQLKAQ 957
Cdd:cd00938 7 VKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQ 40
|
|
| GstA |
COG0625 |
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; |
121-244 |
4.34e-08 |
|
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440390 [Multi-domain] Cd Length: 205 Bit Score: 55.29 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 121 ENVVFTDINSILRYLARVATTAGLYGSNLLEHTEIDHWLEFSATKLSSC--NLFTS-------------------AINEL 179
Cdd:COG0625 59 DGLVLTESLAILEYLAERYPEPPLLPADPAARARVRQWLAWADGDLHPAlrNLLERlapekdpaaiararaelarLLAVL 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1826797428 180 NHCLSLRTYLVGNSLSLADLCVWATLKGSAAWQEQLKQNKapvHVKRWFGFLEAQQAFQSVGTKW 244
Cdd:COG0625 139 EARLAGGPYLAGDRFSIADIALAPVLRRLDRLGLDLADYP---NLAAWLARLAARPAFQRALAAA 200
|
|
| GST_C_Arc1p_N_like |
cd10304 |
Glutathione S-transferase C-terminal-like, alpha helical domain of the Aminoacyl tRNA ... |
151-246 |
1.55e-07 |
|
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: 50.83 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 151 EHTEIDHWLEFSATKLSSCNLFTSaINELNHCLSLRTYLVGNS-LSLADLCVWATLKGSAA-WQEQLKQNKAPV-HVKRW 227
Cdd:cd10304 3 QSAEVAQWLSVAKSGPVSKDVQET-LGQLNLHLRTRTFLLGTGkPSVADVAVFEAVLPVVKeWSDEVKTGYAKYrHILRW 81
|
90
....*....|....*....
gi 1826797428 228 FGFLEAQQAFQSVGTKWNV 246
Cdd:cd10304 82 VDYVQNLLLFIPEADKIEV 100
|
|
| MetRS_RNA |
cd00939 |
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
920-963 |
3.90e-07 |
|
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: 47.85 E-value: 3.90e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1826797428 920 LFDEVASQGEVVRKLKAEKASKDQVDTAVQELLQLKAQYKSLTG 963
Cdd:cd00939 1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEG 44
|
|
| GST_C_AIMP2 |
cd03200 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ... |
132-234 |
4.28e-07 |
|
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: 49.44 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 132 LRYLARVAttaGLYGSNLLEHTEIDHWLEFSATKL--SSCNLFTSAINELNHCLSLRTYLVGNSLSLADLCVWATLkgsa 209
Cdd:cd03200 1 ARFLFRLL---GDESDDPVNATLIDSWVDTAIFQLleGSSKEKAAVLRALNSALGRSPWLVGSEPTVADIALWSAV---- 73
|
90 100
....*....|....*....|....*
gi 1826797428 210 awQEQLKQNKAPVHVKRWFGFLEAQ 234
Cdd:cd03200 74 --LQTGLASGAPANVQRWMKSCENL 96
|
|
| MetRS_RNA |
cd00939 |
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
844-888 |
6.49e-07 |
|
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: 47.47 E-value: 6.49e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1826797428 844 LYDEVAAQGEVVRKLKAEKAPKAKVNEAVECLLSLKAQYKEKTGK 888
Cdd:cd00939 1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEGK 45
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
842-881 |
5.69e-06 |
|
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: 44.77 E-value: 5.69e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1826797428 842 RSLYDEVAAQGEVVRKLKAEKAPKAKVNEAVECLLSLKAQ 881
Cdd:cd00938 1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQ 40
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
775-809 |
9.38e-06 |
|
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: 44.00 E-value: 9.38e-06
10 20 30
....*....|....*....|....*....|....*
gi 1826797428 775 RVAAQGDVVRELKAKKAAKEDIDAAVKQLLALKAE 809
Cdd:cd00938 6 AVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQ 40
|
|
| GST_C_EF1Bgamma_like |
cd03181 |
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ... |
151-240 |
1.01e-05 |
|
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: 46.40 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 151 EHTEIDHWLEFSATKL--SSCNLF--------------TSAINELNHC-------LSLRTYLVGNSLSLADLCVWATLKG 207
Cdd:cd03181 1 EAAQVLQWISFANSELlpAAATWVlpllgiapynkkavDKAKEDLKRAlgvleehLLTRTYLVGERITLADIFVASALLR 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1826797428 208 ------SAAWQEQLkqnkapVHVKRWFGFLEAQQAFQSV 240
Cdd:cd03181 81 gfetvlDPEFRKKY------PNVTRWFNTVVNQPKFKAV 113
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
776-813 |
2.01e-05 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 49.36 E-value: 2.01e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1826797428 776 VAAQGDVVRELKAKKAAKEDIDAAVKQLLALKAEYKEK 813
Cdd:PLN02734 16 VTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSAL 53
|
|
| MetRS_RNA |
cd00939 |
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
776-815 |
2.18e-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: 2.18e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1826797428 776 VAAQGDVVRELKAKKAAKEDIDAAVKQLLALKAEYKEKTG 815
Cdd:cd00939 5 VAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEG 44
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
1152-1431 |
2.86e-05 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 48.59 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1152 SHRDLPIRLNQWCNVVRWEFKHP-QPFLRTREFLWQEGHsAFATFEEAAEEVLQILDLYAQVYE--------ELlaipvv 1222
Cdd:PRK12444 350 SYRELPIRMCEFGQVHRHEFSGAlNGLLRVRTFCQDDAH-LFVTPDQIEDEIKSVMAQIDYVYKtfgfeyevEL------ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1223 kgrKTEKEKFAGGDY-----TTTLEVFISASGRAIQ-----GA---------------TSHHLGQnfskmfeiIFEDPKM 1277
Cdd:PRK12444 423 ---STRPEDSMGDDElweqaEASLENVLQSLNYKYRlnegdGAfygpkidfhikdalnRSHQCGT--------IQLDFQM 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1278 PGEKQFAYQNS--------------WGLTTRTIGVMTmvhgDNMGLVLPPRVASVQVMVIPcgITNALSEEdrealiaKC 1343
Cdd:PRK12444 492 PEKFDLNYIDEknekrrpvvihravLGSLDRFLAILI----EHFGGAFPAWLAPVQVKVIP--VSNAVHVQ-------YA 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1344 NDYRRRLLSVNIRVRVDLReNYSPGWKFNHWELKGVPIRLEVGPRDMKScQFVAVRRdTGEKltvadNEAETKLHALLED 1423
Cdd:PRK12444 559 DEVADKLAQAGIRVERDER-DEKLGYKIREAQMQKIPYVLVIGDKEMEN-GAVNVRK-YGEE-----KSEVIELDMFVES 630
|
....*...
gi 1826797428 1424 IHVNLFTR 1431
Cdd:PRK12444 631 IKEEIKNR 638
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
1136-1419 |
3.67e-05 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 47.93 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1136 PTSETVMYPAYAKWVQSHRDLPIRLNQwcnvVRWEFK---HPQpF--LRTREFLWQEGHSAFATFEEAAEEVLQILDLYA 1210
Cdd:PRK12325 108 PTNEEMITDIFRSYVKSYKDLPLNLYH----IQWKFRdeiRPR-FgvMRGREFLMKDAYSFDLDEEGARHSYNRMFVAYL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1211 QVYE--ELLAIPV------------------------------------VKGRKTEKEKFAGGD--------YTTTLEVF 1244
Cdd:PRK12325 183 RTFArlGLKAIPMradtgpiggdlshefiilaetgestvfydkdfldllVPGEDIDFDVADLQPivdewtslYAATEEMH 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1245 ISA-----------SGRAIQGATSHHLGQNFSKMFEIIFEDPKmpGEKQFAYQNSWGlttrtIGVMTMV-------HGDN 1306
Cdd:PRK12325 263 DEAafaavpeerrlSARGIEVGHIFYFGTKYSEPMNAKVQGPD--GKEVPVHMGSYG-----IGVSRLVaaiieasHDDK 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1307 mGLVLPPRVASVQVMVIPCGITNalseedrEALIAKCNDYRRRLLSVNIRVRVDLRENySPGWKFNHWELKGVPIRLEVG 1386
Cdd:PRK12325 336 -GIIWPESVAPFKVGIINLKQGD-------EACDAACEKLYAALSAAGIDVLYDDTDE-RPGAKFATMDLIGLPWQIIVG 406
|
330 340 350
....*....|....*....|....*....|...
gi 1826797428 1387 PRDMKSCQFVAVRRDTGEKLTVADNEAETKLHA 1419
Cdd:PRK12325 407 PKGLAEGKVELKDRKTGEREELSVEAAINRLTA 439
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
920-974 |
8.53e-05 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 47.05 E-value: 8.53e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1826797428 920 LFDEVASQGEVVRKLKAEKASKDQVDTAVQELLQLKAQYKSLTGIEYKPVSATGA 974
Cdd:PLN02734 12 KQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELQAAVGAGGD 66
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
1060-1298 |
2.16e-04 |
|
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: 44.87 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1060 SGCYILRPWAYSIWESIKDFFDAEIKKLGVENCYFPmFVSQGALEKEKTHIADFAPEVAWVT-RSGKTELaepiaVRPTS 1138
Cdd:cd00779 21 SGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMP-ILQPAELWKESGRWDAYGPELLRLKdRHGKEFL-----LGPTH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1139 ETVMYPAYAKWVQSHRDLPIRLNQwcnvVRWEF---KHPQpF--LRTREFLWQEGHSaFATFEEAAEEVlqildlYAQVY 1213
Cdd:cd00779 95 EEVITDLVANEIKSYKQLPLNLYQ----IQTKFrdeIRPR-FglMRGREFLMKDAYS-FDIDEESLEET------YEKMY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1214 E------ELLAIPVVKgrktekekfaggdytttlevfISASGRAIQGATSH--------------------HLGQNFSKM 1267
Cdd:cd00779 163 QaysrifKRLGLPFVK---------------------VEADSGAIGGSLSHefhvlsplkitkgievghifQLGTKYSKA 221
|
250 260 270
....*....|....*....|....*....|..
gi 1826797428 1268 FEIIFEDPKmpGEKQFAYQNSWGL-TTRTIGV 1298
Cdd:cd00779 222 LGATFLDEN--GKPKPLEMGCYGIgVSRLLAA 251
|
|
| GlyRS_RNA |
cd00935 |
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS ... |
772-813 |
7.82e-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: 39.01 E-value: 7.82e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1826797428 772 LYNRVAAQGDVVRELKAKKAAKEDIDAAVKQLLALKAEYKEK 813
Cdd:cd00935 4 LRAAVKEQGDLVRKLKEEGAPDVDIKKAVAELKARKKLLEDK 45
|
|
| GST_C_Delta_Epsilon |
cd03177 |
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; ... |
179-228 |
1.18e-03 |
|
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: 40.21 E-value: 1.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1826797428 179 LNHCLSLRTYLVGNSLSLADLCVWATLkGSAAWQEqLKQNKAPvHVKRWF 228
Cdd:cd03177 50 LETFLEGSDYVAGDQLTIADLSLVATV-STLEVVG-FDLSKYP-NVAAWY 96
|
|
| GlyRS_RNA |
cd00935 |
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS ... |
920-961 |
1.69e-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: 37.85 E-value: 1.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1826797428 920 LFDEVASQGEVVRKLKAEKASKDQVDTAVQEllqLKAQYKSL 961
Cdd:cd00935 4 LRAAVKEQGDLVRKLKEEGAPDVDIKKAVAE---LKARKKLL 42
|
|
| GlyRS_RNA |
cd00935 |
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS ... |
843-885 |
1.72e-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: 37.85 E-value: 1.72e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1826797428 843 SLYDEVAAQGEVVRKLKAEKAPKAKVNEAVECLLSLKAQYKEK 885
Cdd:cd00935 3 PLRAAVKEQGDLVRKLKEEGAPDVDIKKAVAELKARKKLLEDK 45
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
846-890 |
2.23e-03 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 42.42 E-value: 2.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1826797428 846 DEVAAQGEVVRKLKAEKAPKAKVNEAVECLLSLKAQyKEKTGKEY 890
Cdd:PLN02734 14 AAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLE-KSALEKEL 57
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
1318-1417 |
2.31e-03 |
|
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: 38.64 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1318 VQVMVIPcgITNalseedrealiaKCNDY----RRRLLSVNIRVRVDLRENySPGWKFNHWELKGVPIRLEVGPRDMKSc 1393
Cdd:cd00860 2 VQVVVIP--VTD------------EHLDYakevAKKLSDAGIRVEVDLRNE-KLGKKIREAQLQKIPYILVVGDKEVET- 65
|
90 100
....*....|....*....|....*
gi 1826797428 1394 QFVAVR-RDTGEKLTVADNEAETKL 1417
Cdd:cd00860 66 GTVSVRtRDGGDLGSMSLDEFIEKL 90
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
1311-1408 |
2.33e-03 |
|
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: 42.33 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1311 LPPRVASVQVMVIPcgITnalseedrEALIAKCNDYRRRLLSVNIRVRVDLReNYSPGWKFNHWELKGVPIRLEVGPRDM 1390
Cdd:COG0441 533 FPLWLAPVQVVVLP--IS--------DKHADYAKEVAKKLRAAGIRVEVDLR-NEKIGYKIREAQLQKVPYMLVVGDKEV 601
|
90
....*....|....*...
gi 1826797428 1391 KSCQfVAVRRDTGEKLTV 1408
Cdd:COG0441 602 ENGT-VSVRRRGGGDLGT 618
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
1348-1417 |
7.47e-03 |
|
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: 37.18 E-value: 7.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826797428 1348 RRLLSVNIRVRVDLRENySPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVADNEAETKL 1417
Cdd:cd00861 25 AELQAAGVDVLLDDRNE-RPGVKFADADLIGIPYRIVVGKKSAAEGIVEIKVRKTGEKEEISIDELLEFL 93
|
|
| |
