|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
13-711 |
0e+00 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 843.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 13 PPLGALLA--VEHVKDDVSISVEEGKENILHVSENVIFTDVNSILRYLARVATTAGLYGSNLMEHTEIDHWLEFSATkLS 90
Cdd:PLN02907 12 PPLAVIAAakVAGVPLTIDPSLKSGSAPTLLFSSGEKLTGTNVLLRYIARSASLPGFYGQDAFESSQVDEWLDYAPT-FS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 91 SCDSFTSTINELNHCLSLRTYLVGNSLSLADLCVWATLKGNAAWQEQLKQKKAPVHVKRWFGFLEAQQAFQSVGTKWDVS 170
Cdd:PLN02907 91 SGSEFENACEYVDGYLASRTFLVGYSLTIADIAIWSGLAGSGQRWESLRKSKKYQNLVRWFNSISAEYSDILNEVTAAYV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 171 TTK---ARVAPEKKQDV------------GKF-VELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIM 234
Cdd:PLN02907 171 GKRgagKPAAAKSKEKVadagkadgakdkGSFeVDLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 235 RFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIDSKHRKN 314
Cdd:PLN02907 251 RFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMDGIESKCRNN 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 315 PIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHAL 394
Cdd:PLN02907 331 SVEENLRLWKEMIAGSERGLQCCVRGKLDMQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHAL 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 395 RTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQF 474
Cdd:PLN02907 411 RSSEYHDRNAQYYRILEDMGLRKVHIWEFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQF 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 475 IAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLKKEVIPV---NVPEaQEEMKEVAKHPKNPEVGLKPVWYSPKVF 551
Cdd:PLN02907 491 ILSQGASKNLNLMEWDKLWTINKKIIDPVCPRHTAVLKEGRVLLtltDGPE-TPFVRIIPRHKKYEGAGKKATTFTNRIW 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 552 IEGADAETFSEGEMVTFINWGNLNITKIHKNADGKIISLDAKLNLENkDYKKTT-KVTWLAETTHAlpIPVICVTYEHLI 630
Cdd:PLN02907 570 LDYADAEAISEGEEVTLMDWGNAIIKEITKDEGGAVTALSGELHLEG-SVKTTKlKLTWLPDTNEL--VPLSLVEFDYLI 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 631 TKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDQPYEPVSpysckeAPCVLIYIPDGHTKEM 710
Cdd:PLN02907 647 TKKKLEEDDNFLDVLNPCTKKETAALGDSNMRNLKRGEIIQLERKGYYRCDAPFVRSS------KPIVLFAIPDGRQQKS 720
|
.
gi 62241042 711 P 711
Cdd:PLN02907 721 G 721
|
|
| proS_fam_I |
TIGR00408 |
prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ... |
1018-1512 |
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: 565.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1018 AKKEENLADWYSQVITKSEMIEYHDISGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKTHVADF 1097
Cdd:TIGR00408 2 ASKMQDFSEWYHQILEKAEIIDYYPVKGCYVWLPYGFKIWKNIQKILRNILDEIGHEEVYFPMLIPESELAKEKDHIKGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1098 APEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFA 1177
Cdd:TIGR00408 82 EPEVYWITHGGLSKLDEPLALRPTSETAMYPMFKKWVKSYTDLPLKINQWVNVFRYETKHTRPFLRTREFTWQEAHTAHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1178 TMEEAAEEVLQILDLYAQVYEELLAIPVVKGRKTEKEKFAGGDYTTTIEAFISaSGRAIQGGTSHHLGQNFSKMFEIVFE 1257
Cdd:TIGR00408 162 TAEEAEEQVLRALDIYKEFIENSLAIPYFVGRKPEWEKFAGAEYTWAFETIMP-DGRTLQIATSHNLGQNFAKTFEIKFE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1258 DPKipGEKQFAYQNSWGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCgitnALSEEDKEALIAKCNDYRRRLLSV 1337
Cdd:TIGR00408 241 TPT--GDKEYAYQTSYGISTRVIGALIAIHSDEKGLVLPPRVAPIQVVIIPI----IFKKKENEKVMEAAREVRSRLKKA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1338 NIRVRADLRDNySPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVAENEAETKLQAILEDIQVTLFTRAS 1417
Cdd:TIGR00408 315 GFRVHIDDRDN-RPGRKFYQWEIKGIPLRIEVGPNDIEKNIAVISRRDTGEKYQVSLDQLEERVVELLNNIQENLRNRAW 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1418 EDLKTHMVVANTMEDFQKIL-DSGKIVQIPFCGEIDCEDWIKKTTArdqdlepgapsmgAKSLCIPFKPlcelQPGAKCV 1496
Cdd:TIGR00408 394 ERFEQKIVIVETLEEIKQALnEKRGVVLVPWCGEEECEEDLKEKVQ-------------VTILCIPEDG----DVLQLCI 456
|
490
....*....|....*.
gi 62241042 1497 CGKNPAKYYTLFGRSY 1512
Cdd:TIGR00408 457 FCGRKAPDYVLIARTY 472
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
1023-1286 |
2.91e-170 |
|
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: 510.60 E-value: 2.91e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1023 NLADWYSQVITKSEMIEYHDISGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKTHVADFAPEVA 1102
Cdd:cd00778 1 DFSEWYTEVITKAELIDYGPVKGCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPESELEKEKEHIEGFAPEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1103 WVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATMEEA 1182
Cdd:cd00778 81 WVTHGGLEELEEPLALRPTSETAIYPMFSKWIRSYRDLPLKINQWVNVFRWETKTTRPFLRTREFLWQEGHTAHATEEEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1183 AEEVLQILDLYAQVYEELLAIPVVKGRKTEKEKFAGGDYTTTIEAFISaSGRAIQGGTSHHLGQNFSKMFEIVFEDPKip 1262
Cdd:cd00778 161 EEEVLQILDLYKEFYEDLLAIPVVKGRKTEWEKFAGADYTYTIEAMMP-DGRALQSGTSHNLGQNFSKAFDIKYQDKD-- 237
|
250 260
....*....|....*....|....
gi 62241042 1263 GEKQFAYQNSWGLTTRTIGVMTMV 1286
Cdd:cd00778 238 GQKEYVHQTSWGISTRLIGAIIMI 261
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
197-502 |
1.11e-156 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 476.81 E-value: 1.11e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 197 KVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPD-QFTYTSDHFET 275
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDyGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 276 IMKYAEKLIQEGKAYVDDTPAEQMKAEREQ--RIDSKHRKNPIEKNLQMW-EEMKKGSQFGQSCCLRAKIDMSSnNGCMR 352
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEqeALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMES-PYVFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 353 DPTLYRCKIQP---HPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIR-KPYIWEYSRLNL 428
Cdd:pfam00749 160 DPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62241042 429 NNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSV-VNMEWDKIWAFNKKVIDP 502
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFdVNRLSKSLEAFDRKKLDW 314
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
173-690 |
6.62e-144 |
|
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the eukaryotic cytosolic and archaeal forms of the enzyme. In some eukaryotes, the glutamyl-tRNA synthetase is part of a longer, multifunctional aminoacyl-tRNA ligase. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases, including all known archaeal enzymes (as of 2010) may act on both tRNA(gln) and tRNA(glu). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273091 [Multi-domain] Cd Length: 556 Bit Score: 452.74 E-value: 6.62e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 173 KARVAPEKKQDVGKF-VELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKV 251
Cdd:TIGR00463 68 RLGLDIKKKEKKRKGlRELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDM 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 252 ILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIDSKHRKNPIEKNLQMWEEMKKGSQ 331
Cdd:TIGR00463 148 ILEDLEWLGVKWDEVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNRGEACHCRDRSVEENLERWEEMLEGKE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 332 FGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHD--RDEQFYWI 409
Cdd:TIGR00463 228 EGGSVVVRVKTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDnrRKQEYIYR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 410 IEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVnEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEW 489
Cdd:TIGR00463 308 YFGWEPPEFIHWGRLKIDDVRALSTSSARKGIL-RGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSW 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 490 DKIWAFNKKVIDPVAPRYVALLK-KEVIPVNVPEAQEEMKevAKHPKNPEVGLKPVWYSPKVFIEGADAETfsEGEMVTF 568
Cdd:TIGR00463 387 KNIYALNRKIIDEEARRYFFIWNpVKIEIVGLPEPKRVER--PLHPDHPEIGERVLILRGEIYVPKDDLEE--GVEPVRL 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 569 INWGNLNITKIHknadgkiiSLDAKLNLENKDYKKTTKVTWLAETThalPIPVICVTYEHLITKPVLGKDEDFkqyvnkn 648
Cdd:TIGR00463 463 MDAVNVIYSKKE--------LRYHSEGLEGARKLGKSIIHWLPAKD---AVKVKVIMPDASIVEGVIEADASE------- 524
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 62241042 649 skheelmlgdpclkdLKKGDIIQLQRRGFFICDQPYEPVSPY 690
Cdd:TIGR00463 525 ---------------LEVGDVVQFERFGFARLDSADKDGMVF 551
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
197-506 |
5.37e-135 |
|
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Gln to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. GlnRS contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185676 [Multi-domain] Cd Length: 238 Bit Score: 415.88 E-value: 5.37e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 197 KVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETI 276
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 277 MKYAEKLIQEGKAYVddtpaeqmkaereqridskhrknpieknlqmweemkkgsqfgqscclrakidmssnngcmrdptl 356
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 357 yrckiqpHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKR 436
Cdd:cd00807 96 -------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKR 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 437 KLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPR 506
Cdd:cd00807 169 KLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
1027-1405 |
9.35e-90 |
|
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440211 [Multi-domain] Cd Length: 564 Bit Score: 303.62 E-value: 9.35e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1027 WYSQVITKSEMIEYHdISGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPMFVSQSaLEKEKTHVADFAPEVAWVtr 1106
Cdd:COG0442 21 WSHQLMLRAGLIRKL-ASGIYTYLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQPAE-LWEESGRWEGFGPELARV-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1107 sgKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATMEEAAEEV 1186
Cdd:COG0442 97 --TDRLEREFCLGPTHEEVITDLVRNEIKSYRDLPLLLYQIQTKFRDEIRPRFGLLRTREFLMKDAYSFHATEEELDEEY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1187 LQILDLYAQVYEElLAIPVVKGRKT-------EKEKFA--------------GGDY------------------------ 1221
Cdd:COG0442 175 QKMLDAYERIFER-LGLPVRAVEADsgaiggsESHEFMvladsgedtivycdACDYaaniekaealappaeraeptkele 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1222 ------TTTIEA------------------------------------------------------------------FI 1229
Cdd:COG0442 254 avatpgAKTIEEvaeflgvpaektvktlvykadgelvavlvrgdhelneiklenllgaselelateeeieaalgavpgFL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1230 SASG----------------------------------------------------------------RAIQGGTSHHLG 1245
Cdd:COG0442 334 GPVGlgvpyiadrsvagmsnfvcganeddyhytnvnwgrdfpvdevadlrnvvegdpcpdcggllqdgRGIEVGHIFKLG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1246 QNFSKMFEIVFEDPKipGEKQFAYQNSWGLT-TRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCGItnalseeDKEALI 1324
Cdd:COG0442 414 TKYSKAMDATFLDEN--GKEQPVWMGCYGIGvTRLIAAAIEQHHDDKGIIWPPAIAPFQVVIVPINM-------KDEAVL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1325 AKCNDYRRRLLSVNIRVRADLRDNySPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVAENEAETKLQAI 1404
Cdd:COG0442 485 EAAEELYAELKAAGIDVLLDDRDE-RPGVKFADAELIGIPLRIVIGPRDLEEGQVEVKRRDTGEKEEVPLDELVETVKEL 563
|
.
gi 62241042 1405 L 1405
Cdd:COG0442 564 L 564
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
196-483 |
8.56e-65 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 228.14 E-value: 8.56e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 196 GKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQ-FTYTSDHFE 274
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEgPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 275 TIMKYAEKLIQEGKAYVDDTPAEQMKAEREQ--------RIDSKHRKNPIEKNLQMWEEmkkgsqfGQSCCLRAKI---- 342
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETqtapgkppRYDGRCRDLSPEELERMLAA-------GEPPVLRFKIpeeg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 343 ----DMSS-----NNGCMRDPTLYRckiqphpRTGnkynvYPTYDFACPIVDSIEGVTHALRT------TEYHDrdeqfy 407
Cdd:COG0008 156 vvfdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGeehlsnTPRQI------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 408 WIIEALGIRKPyiwEYSRLNL----NNTVLSKRKltwfvneGLVdgwddprfpTVRGVLRRGMTVEGLKQFIAAQGSSRS 483
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLilgpDGTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
753-802 |
1.00e-23 |
|
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 94.99 E-value: 1.00e-23
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 62241042 753 LYNRVAVQGDVVRELKAKKAPKEDVDAAVKQLLSLKAEYKEKTGQEYKPG 802
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
|
|
| ProRS-C_1 |
pfam09180 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
1430-1512 |
2.92e-23 |
|
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: 94.51 E-value: 2.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1430 MEDFQKILDSGKIVQIPFCGEIDCEDWIKKTTardqdlepgapsmGAKSLCIPFKplcELQPGAKCVCGKNPAKYYTLFG 1509
Cdd:pfam09180 1 WEEFKEALEEKGFVLAPWCGDEECEDKIKEET-------------GATSRCIPFD---QEEEGGKCIVCGKPAKKWVLFA 64
|
...
gi 62241042 1510 RSY 1512
Cdd:pfam09180 65 RSY 67
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
753-805 |
3.73e-23 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 93.71 E-value: 3.73e-23
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 62241042 753 LYNRVAVQGDVVRELKAKKAPKEDVDAAVKQLLSLKAEYKEKTGQEYKPGNPP 805
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
|
|
| ProRS-C_1 |
smart00946 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
1430-1512 |
3.18e-22 |
|
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.
Pssm-ID: 198014 Cd Length: 67 Bit Score: 91.48 E-value: 3.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1430 MEDFQKILDSGKIVQIPFCGEIDCEDWIKKTTardqdlepgapsmGAKSLCIPFKplcELQPGAKCVCGKNPAKYYTLFG 1509
Cdd:smart00946 1 LEEFKKALEEGKFVLAPWCGDEECEEKIKEET-------------GATIRCIPFD---QDEEPGKCVVCGKPAKKWVLFA 64
|
...
gi 62241042 1510 RSY 1512
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 ... |
754-806 |
4.41e-21 |
|
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: 87.78 E-value: 4.41e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 62241042 754 YNRVAVQGDVVRELKAKKAPKEDVDAAVKQLLSLKAEYKEKTGQEYKPGNPPA 806
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPG 53
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
826-875 |
1.50e-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: 86.14 E-value: 1.50e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 62241042 826 LYDEVAAQGEVVRKLKAEKSPKAKINEAVECLLSLKAQYKEKTGKEYIPG 875
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
904-952 |
5.49e-20 |
|
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 84.59 E-value: 5.49e-20
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 62241042 904 LFDKVASQGEVVRKLKTEKAPKDQVDIAVQELLQLKAQYKSLIGVEYKP 952
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKP 49
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
826-878 |
2.73e-19 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 82.54 E-value: 2.73e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 62241042 826 LYDEVAAQGEVVRKLKAEKSPKAKINEAVECLLSLKAQYKEKTGKEYIPGQPP 878
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
904-956 |
4.45e-19 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 82.16 E-value: 4.45e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 62241042 904 LFDKVASQGEVVRKLKTEKAPKDQVDIAVQELLQLKAQYKSLIGVEYKPVSAT 956
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 ... |
827-878 |
2.61e-18 |
|
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.
Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 80.08 E-value: 2.61e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 62241042 827 YDEVAAQGEVVRKLKAEKSPKAKINEAVECLLSLKAQYKEKTGKEYIPGQPP 878
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPP 52
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
905-958 |
6.38e-17 |
|
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: 75.84 E-value: 6.38e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 62241042 905 FDKVASQGEVVRKLKTEKAPKDQVDIAVQELLQLKAQYKSLIGVEYKPVSATGA 958
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGD 54
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
1244-1405 |
1.99e-09 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 62.02 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1244 LGQNFSKMFEIVFEDPKipGEKQFAYQNSWGlttrtIGVMTMV------HGDNMGLVLPPRVACVQVVIIPcgiTNALSE 1317
Cdd:PRK09194 412 LGTKYSEAMNATVLDEN--GKAQPLIMGCYG-----IGVSRLVaaaieqNHDEKGIIWPKAIAPFDVHIVP---VNMKDE 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1318 EDKEA---LIAKcndyrrrLLSVNIRVRADLRDNySPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVAE 1394
Cdd:PRK09194 482 EVKELaekLYAE-------LQAAGIEVLLDDRKE-RPGVKFADADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPV 553
|
170
....*....|.
gi 62241042 1395 NEAETKLQAIL 1405
Cdd:PRK09194 554 DELVEFLKALK 564
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
757-827 |
1.40e-04 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 46.66 E-value: 1.40e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62241042 757 VAVQGDVVRELKAKKAPKEDVDAAVKQL--LSLKAEYKEKTGQEYKPGNPPAEIGQNISSNSSASILESKSLY 827
Cdd:PLN02734 16 VTAQGNAVRALKASKADKAEIDAAIEKLkaLKLEKSALEKELQAAVGAGGDGAASKEAFRQAVVNTLERRLFY 88
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
904-958 |
2.82e-04 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 45.51 E-value: 2.82e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 62241042 904 LFDKVASQGEVVRKLKTEKAPKDQVDIAVQELLQLKAQyKSLIGVEYKPVSATGA 958
Cdd:PLN02734 12 KQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLE-KSALEKELQAAVGAGG 65
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
828-889 |
1.17e-03 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 43.58 E-value: 1.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62241042 828 DEVAAQGEVVRKLKAEKSPKAKINEAVECLLSLKAQyKEKTGKEYipgQPPLSQSSDSSPTR 889
Cdd:PLN02734 14 AAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLE-KSALEKEL---QAAVGAGGDGAASK 71
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
13-711 |
0e+00 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 843.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 13 PPLGALLA--VEHVKDDVSISVEEGKENILHVSENVIFTDVNSILRYLARVATTAGLYGSNLMEHTEIDHWLEFSATkLS 90
Cdd:PLN02907 12 PPLAVIAAakVAGVPLTIDPSLKSGSAPTLLFSSGEKLTGTNVLLRYIARSASLPGFYGQDAFESSQVDEWLDYAPT-FS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 91 SCDSFTSTINELNHCLSLRTYLVGNSLSLADLCVWATLKGNAAWQEQLKQKKAPVHVKRWFGFLEAQQAFQSVGTKWDVS 170
Cdd:PLN02907 91 SGSEFENACEYVDGYLASRTFLVGYSLTIADIAIWSGLAGSGQRWESLRKSKKYQNLVRWFNSISAEYSDILNEVTAAYV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 171 TTK---ARVAPEKKQDV------------GKF-VELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIM 234
Cdd:PLN02907 171 GKRgagKPAAAKSKEKVadagkadgakdkGSFeVDLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 235 RFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIDSKHRKN 314
Cdd:PLN02907 251 RFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMDGIESKCRNN 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 315 PIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHAL 394
Cdd:PLN02907 331 SVEENLRLWKEMIAGSERGLQCCVRGKLDMQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHAL 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 395 RTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQF 474
Cdd:PLN02907 411 RSSEYHDRNAQYYRILEDMGLRKVHIWEFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQF 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 475 IAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLKKEVIPV---NVPEaQEEMKEVAKHPKNPEVGLKPVWYSPKVF 551
Cdd:PLN02907 491 ILSQGASKNLNLMEWDKLWTINKKIIDPVCPRHTAVLKEGRVLLtltDGPE-TPFVRIIPRHKKYEGAGKKATTFTNRIW 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 552 IEGADAETFSEGEMVTFINWGNLNITKIHKNADGKIISLDAKLNLENkDYKKTT-KVTWLAETTHAlpIPVICVTYEHLI 630
Cdd:PLN02907 570 LDYADAEAISEGEEVTLMDWGNAIIKEITKDEGGAVTALSGELHLEG-SVKTTKlKLTWLPDTNEL--VPLSLVEFDYLI 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 631 TKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDQPYEPVSpysckeAPCVLIYIPDGHTKEM 710
Cdd:PLN02907 647 TKKKLEEDDNFLDVLNPCTKKETAALGDSNMRNLKRGEIIQLERKGYYRCDAPFVRSS------KPIVLFAIPDGRQQKS 720
|
.
gi 62241042 711 P 711
Cdd:PLN02907 721 G 721
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
190-710 |
0e+00 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 592.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 190 LPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYT 269
Cdd:PLN03233 4 LEGAIAGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 270 SDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIDSKHRKNPIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNG 349
Cdd:PLN03233 84 SDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKERADRAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQSDNG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 350 CMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLN 429
Cdd:PLN03233 164 TLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARMNFM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 430 NTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVA 509
Cdd:PLN03233 244 NTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRFMA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 510 LLKKEVIPVNVPEAQEE----MKEVAKHPKNPEVGLKPVWYSPKVFIEGADAETFSEGEMVTFINWGNLNITKIHKNADG 585
Cdd:PLN03233 324 IDKADHTALTVTNADEEadfaFSETDCHPKDPGFGKRAMRICDEVLLEKADTEDIQLGEDIVLLRWGVIEISKIDGDLEG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 586 KIISldaklnleNKDYKKTT-KVTWLAETTHAlpIPVICVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDL 664
Cdd:PLN03233 404 HFIP--------DGDFKAAKkKISWIADVSDN--IPVVLSEFDNLIIKEKLEEDDKFEDFINPDTLAETDVIGDAGLKTL 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 62241042 665 KKGDIIQLQRRGFFICDQPYepVSPysckEAPCVLIYIPDGHTKEM 710
Cdd:PLN03233 474 KEHDIIQLERRGFYRVDRPY--MGE----EKPLILFMIPDGKKKAM 513
|
|
| proS_fam_I |
TIGR00408 |
prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ... |
1018-1512 |
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: 565.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1018 AKKEENLADWYSQVITKSEMIEYHDISGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKTHVADF 1097
Cdd:TIGR00408 2 ASKMQDFSEWYHQILEKAEIIDYYPVKGCYVWLPYGFKIWKNIQKILRNILDEIGHEEVYFPMLIPESELAKEKDHIKGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1098 APEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFA 1177
Cdd:TIGR00408 82 EPEVYWITHGGLSKLDEPLALRPTSETAMYPMFKKWVKSYTDLPLKINQWVNVFRYETKHTRPFLRTREFTWQEAHTAHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1178 TMEEAAEEVLQILDLYAQVYEELLAIPVVKGRKTEKEKFAGGDYTTTIEAFISaSGRAIQGGTSHHLGQNFSKMFEIVFE 1257
Cdd:TIGR00408 162 TAEEAEEQVLRALDIYKEFIENSLAIPYFVGRKPEWEKFAGAEYTWAFETIMP-DGRTLQIATSHNLGQNFAKTFEIKFE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1258 DPKipGEKQFAYQNSWGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCgitnALSEEDKEALIAKCNDYRRRLLSV 1337
Cdd:TIGR00408 241 TPT--GDKEYAYQTSYGISTRVIGALIAIHSDEKGLVLPPRVAPIQVVIIPI----IFKKKENEKVMEAAREVRSRLKKA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1338 NIRVRADLRDNySPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVAENEAETKLQAILEDIQVTLFTRAS 1417
Cdd:TIGR00408 315 GFRVHIDDRDN-RPGRKFYQWEIKGIPLRIEVGPNDIEKNIAVISRRDTGEKYQVSLDQLEERVVELLNNIQENLRNRAW 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1418 EDLKTHMVVANTMEDFQKIL-DSGKIVQIPFCGEIDCEDWIKKTTArdqdlepgapsmgAKSLCIPFKPlcelQPGAKCV 1496
Cdd:TIGR00408 394 ERFEQKIVIVETLEEIKQALnEKRGVVLVPWCGEEECEEDLKEKVQ-------------VTILCIPEDG----DVLQLCI 456
|
490
....*....|....*.
gi 62241042 1497 CGKNPAKYYTLFGRSY 1512
Cdd:TIGR00408 457 FCGRKAPDYVLIARTY 472
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
177-730 |
0e+00 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 556.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 177 APEKKQDVGKfVELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDV 256
Cdd:PTZ00402 33 AANANEENDK-LQLTNAEEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 257 AMLHIKPDQF-TYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIDSKHRKNPIEKNLQMWEEMKKGSQFGQS 335
Cdd:PTZ00402 112 ATLGVSWDVGpTYSSDYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFDGVPTKYRDISVEETKRLWNEMKKGSAEGQE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 336 CCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGI 415
Cdd:PTZ00402 192 TCLRAKISVDNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGI 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 416 RKPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAF 495
Cdd:PTZ00402 272 RKPIVEDFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYF 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 496 NKKVIDPVAPRYVALLKKEVIPVNVpEAQEEMKEVAK--HPKNPEVGLKPVWYSPKVFIEGADAETFSEGEMVTFINWGN 573
Cdd:PTZ00402 352 NTQILDPSVPRYTVVSNTLKVRCTV-EGQIHLEACEKllHKKVPDMGEKTYYKSDVIFLDAEDVALLKEGDEVTLMDWGN 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 574 LNITKIHK-NADGKIISLDAKLNLENkDYKKTT-KVTWLAETTHALPIPVicVTYEHLITKPVLGKDEDFKQYVNKNSKH 651
Cdd:PTZ00402 431 AYIKNIRRsGEDALITDADIVLHLEG-DVKKTKfKLTWVPESPKAEVMEL--NEYDHLLTKKKPDPEESIDDIIAPVTKY 507
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62241042 652 EELMLGDPCLKDLKKGDIIQLQRRGFFICDQpyepvspyscKEAPCVLIYIPDGHTKEMPTSGSKEKTKVEATKNETSA 730
Cdd:PTZ00402 508 TQEVYGEEALSVLKKGDIIQLERRGYYIVDD----------VTPKKVLIAIPDGREKVNHLSAKAQYLKTLPKKGIASA 576
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
1023-1286 |
2.91e-170 |
|
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: 510.60 E-value: 2.91e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1023 NLADWYSQVITKSEMIEYHDISGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKTHVADFAPEVA 1102
Cdd:cd00778 1 DFSEWYTEVITKAELIDYGPVKGCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPESELEKEKEHIEGFAPEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1103 WVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATMEEA 1182
Cdd:cd00778 81 WVTHGGLEELEEPLALRPTSETAIYPMFSKWIRSYRDLPLKINQWVNVFRWETKTTRPFLRTREFLWQEGHTAHATEEEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1183 AEEVLQILDLYAQVYEELLAIPVVKGRKTEKEKFAGGDYTTTIEAFISaSGRAIQGGTSHHLGQNFSKMFEIVFEDPKip 1262
Cdd:cd00778 161 EEEVLQILDLYKEFYEDLLAIPVVKGRKTEWEKFAGADYTYTIEAMMP-DGRALQSGTSHNLGQNFSKAFDIKYQDKD-- 237
|
250 260
....*....|....*....|....
gi 62241042 1263 GEKQFAYQNSWGLTTRTIGVMTMV 1286
Cdd:cd00778 238 GQKEYVHQTSWGISTRLIGAIIMI 261
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
197-502 |
1.11e-156 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 476.81 E-value: 1.11e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 197 KVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPD-QFTYTSDHFET 275
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDyGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 276 IMKYAEKLIQEGKAYVDDTPAEQMKAEREQ--RIDSKHRKNPIEKNLQMW-EEMKKGSQFGQSCCLRAKIDMSSnNGCMR 352
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEqeALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMES-PYVFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 353 DPTLYRCKIQP---HPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIR-KPYIWEYSRLNL 428
Cdd:pfam00749 160 DPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62241042 429 NNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSV-VNMEWDKIWAFNKKVIDP 502
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFdVNRLSKSLEAFDRKKLDW 314
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
173-690 |
6.62e-144 |
|
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the eukaryotic cytosolic and archaeal forms of the enzyme. In some eukaryotes, the glutamyl-tRNA synthetase is part of a longer, multifunctional aminoacyl-tRNA ligase. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases, including all known archaeal enzymes (as of 2010) may act on both tRNA(gln) and tRNA(glu). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273091 [Multi-domain] Cd Length: 556 Bit Score: 452.74 E-value: 6.62e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 173 KARVAPEKKQDVGKF-VELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKV 251
Cdd:TIGR00463 68 RLGLDIKKKEKKRKGlRELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDM 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 252 ILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIDSKHRKNPIEKNLQMWEEMKKGSQ 331
Cdd:TIGR00463 148 ILEDLEWLGVKWDEVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNRGEACHCRDRSVEENLERWEEMLEGKE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 332 FGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHD--RDEQFYWI 409
Cdd:TIGR00463 228 EGGSVVVRVKTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDnrRKQEYIYR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 410 IEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVnEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEW 489
Cdd:TIGR00463 308 YFGWEPPEFIHWGRLKIDDVRALSTSSARKGIL-RGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSW 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 490 DKIWAFNKKVIDPVAPRYVALLK-KEVIPVNVPEAQEEMKevAKHPKNPEVGLKPVWYSPKVFIEGADAETfsEGEMVTF 568
Cdd:TIGR00463 387 KNIYALNRKIIDEEARRYFFIWNpVKIEIVGLPEPKRVER--PLHPDHPEIGERVLILRGEIYVPKDDLEE--GVEPVRL 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 569 INWGNLNITKIHknadgkiiSLDAKLNLENKDYKKTTKVTWLAETThalPIPVICVTYEHLITKPVLGKDEDFkqyvnkn 648
Cdd:TIGR00463 463 MDAVNVIYSKKE--------LRYHSEGLEGARKLGKSIIHWLPAKD---AVKVKVIMPDASIVEGVIEADASE------- 524
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 62241042 649 skheelmlgdpclkdLKKGDIIQLQRRGFFICDQPYEPVSPY 690
Cdd:TIGR00463 525 ---------------LEVGDVVQFERFGFARLDSADKDGMVF 551
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
196-696 |
1.63e-137 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 435.30 E-value: 1.63e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 196 GKVTVRFPPEASGYLHIGHAKAALLN----QHYQvnfkGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKP-DQFTYTS 270
Cdd:PRK05347 28 TRVHTRFPPEPNGYLHIGHAKSICLNfglaQDYG----GKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWsGELRYAS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 271 DHFETIMKYAEKLIQEGKAYVDDTPAEQMkaeREQR-------IDSKHRKNPIEKNLQMWEEMKKGsQF--GqSCCLRAK 341
Cdd:PRK05347 104 DYFDQLYEYAVELIKKGKAYVDDLSAEEI---REYRgtltepgKNSPYRDRSVEENLDLFERMRAG-EFpeG-SAVLRAK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 342 IDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHD-RdeQFY-WIIEALGIR-KP 418
Cdd:PRK05347 179 IDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDhR--PLYdWVLDNLPIPpHP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 419 YIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSR--SVVNM---Ewdkiw 493
Cdd:PRK05347 257 RQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKqdSVIDMsmlE----- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 494 AFNKKVIDPVAPRYVALLK--KEVIpVNVPEAQEEMKEVAKHPKNPEVGLKPVWYSPKVFIEGADaetFSE--------- 562
Cdd:PRK05347 332 SCIREDLNENAPRAMAVLDplKLVI-TNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIERED---FMEeppkkyfrl 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 563 --GEMVTFINWGNLNITKIHKNADGKIISL----DAK-LNLENKDYKKTTKV-TWLaETTHALPIPVicVTYEHLITKPV 634
Cdd:PRK05347 408 vpGKEVRLRNAYVIKCEEVVKDADGNITEIhctyDPDtLSGNPADGRKVKGTiHWV-SAAHAVPAEV--RLYDRLFTVPN 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62241042 635 LGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDqpyepvsPYSCKEAP 696
Cdd:PRK05347 485 PAAGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCAD-------KDSTPGKL 539
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
197-506 |
5.37e-135 |
|
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Gln to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. GlnRS contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185676 [Multi-domain] Cd Length: 238 Bit Score: 415.88 E-value: 5.37e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 197 KVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETI 276
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 277 MKYAEKLIQEGKAYVddtpaeqmkaereqridskhrknpieknlqmweemkkgsqfgqscclrakidmssnngcmrdptl 356
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 357 yrckiqpHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKR 436
Cdd:cd00807 96 -------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKR 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 437 KLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPR 506
Cdd:cd00807 169 KLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
198-681 |
6.97e-108 |
|
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: 353.07 E-value: 6.97e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 198 VTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPD-QFTYTSDHFETI 276
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEgKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 277 MKYAEKLIQEGKAYVDDTPAEQMKAEREQRID----SKHRKNPIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMR 352
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDpgknSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 353 DPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGI-RKPYIWEYSRLNLNNT 431
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIfPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 432 VLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALL 511
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 512 KKEVIPVNVPEAQEEMKEVAKHPKNPEVGLKPVWYSPKVFIEGADaetFSE-----------GEMVTFINWGNLNITKIH 580
Cdd:TIGR00440 321 DPVEVVIENLSDEYELATIPNHPNTPEFGERQVPFTNEFYIDRAD---FREeankqykrlvlGKEVRLRNAYVIKAERVE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 581 KNADGKIISL----DAK-LNLENKDYKKTTKVTWLAETTHALPIPVicVTYEHLITKPVLGKDEDFKQYVNKNSKHEELM 655
Cdd:TIGR00440 398 KDAAGKITTIfctyDNKtLGKEPADGRKVKGVIHWVSASSKYPTET--RLYDRLFKVPNPGAPDDFLSVINPESLVIKQG 475
|
490 500
....*....|....*....|....*.
gi 62241042 656 LGDPCLKDLKKGDIIQLQRRGFFICD 681
Cdd:TIGR00440 476 FMEHSLGDAVANKRFQFEREGYFCLD 501
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
196-741 |
8.64e-102 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 344.40 E-value: 8.64e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 196 GKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIK-PDQFTYTSDHFE 274
Cdd:PRK14703 30 PRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDwGEHLYYASDYFE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 275 TIMKYAEKLIQEGKAYVDDTPAEQMkaeREQR-------IDSKHRKNPIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSN 347
Cdd:PRK14703 110 RMYAYAEQLIKMGLAYVDSVSEEEI---RELRgtvtepgTPSPYRDRSVEENLDLFRRMRAGEFPDGAHVLRAKIDMSSP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 348 NGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIR--KPYIWEYSR 425
Cdd:PRK14703 187 NMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPWppRPRQYEFAR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 426 LNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAP 505
Cdd:PRK14703 267 LALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGVLEFAIRDDLNRRAP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 506 RYVALLKK-EVIPVNVPEAQEEMKEVAKHPKN-PEVGLKPVWYSPKVFIEGADaetFSE-----------GEMVTFINWG 572
Cdd:PRK14703 347 RVMAVLDPlKVVIENLPAGKVEELDLPYWPHDvPKEGSRKVPFTRELYIERDD---FSEdppkgfkrltpGREVRLRGAY 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 573 NLNITKIHKNADGKIISLDAKLNLENKDYKKTTKVT-----WLAeTTHALPIPVicVTYEHLITKPVL-GKDEDFKQYVN 646
Cdd:PRK14703 424 IIRCDEVVRDADGAVTELRCTYDPESAKGEDTGRKAagvihWVS-AKHALPAEV--RLYDRLFKVPQPeAADEDFLEFLN 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 647 KNSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDqpyePVSpySCKEAPCV--LIYIPD--GHTKEMPTSGSKEKTKVE 722
Cdd:PRK14703 501 PDSLRVAQGRVEPAVRDDPADTRYQFERQGYFWAD----PVD--SRPDALVFnrIITLKDtwGARAREAAREKRAAAPKK 574
|
570
....*....|....*....
gi 62241042 723 ATKNETSAPFKERPTPSLN 741
Cdd:PRK14703 575 TAKPRRSKAEARAEAAALN 593
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
196-686 |
6.59e-99 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 330.02 E-value: 6.59e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 196 GKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFET 275
Cdd:PTZ00437 50 GKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKPDWVTFSSDYFDQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 276 IMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIDSKHRKNPIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPT 355
Cdd:PTZ00437 130 LHEFAVQLIKDGKAYVDHSTPDELKQQREQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRDFI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 356 LYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSK 435
Cdd:PTZ00437 210 AYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWRPHVWEFSRLNVTGSLLSK 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 436 RKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLkkEV 515
Cdd:PTZ00437 290 RKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVI--DP 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 516 IPVNVPEAQEEMK-EVAKHPKNPEVGLKPVWYSPKVFIEGADAET---------FSEGEMVTFINW-GNLNITKIHKNAD 584
Cdd:PTZ00437 368 IKVVVDNWKGEREfECPNHPRKPELGSRKVMFTDTFYVDRSDFRTednnskfygLAPGPRVVGLKYsGNVVCKGFEVDAA 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 585 GKIISLDAKLNLENKDyKKTTKVTWLAETThalPIPVICVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDL 664
Cdd:PTZ00437 448 GQPSVIHVDIDFERKD-KPKTNISWVSATA---CTPVEVRLYNALLKDDRAAIDPEFLKFIDEDSEVVSHGYAEKGIENA 523
|
490 500
....*....|....*....|..
gi 62241042 665 KKGDIIQLQRRGFFICDQPYEP 686
Cdd:PTZ00437 524 KHFESVQAERFGYFVVDPDTRP 545
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
179-677 |
3.10e-98 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 327.58 E-value: 3.10e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 179 EKKQDVGKFVELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFE--KVILEDV 256
Cdd:PRK04156 83 EKKEEKKGLPPLPNAEKGKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTKRPDPEayDMILEDL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 257 AMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIDSKHRKNPIEKNLQMWEEMKKGSQFGQSC 336
Cdd:PRK04156 163 KWLGVKWDEVVIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELRDAGKPCPHRDKSPEENLELWEKMLDGEYKEGEA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 337 CLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIR 416
Cdd:PRK04156 243 VVRVKTDLEHPNPSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYDYFGWE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 417 KPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFN 496
Cdd:PRK04156 323 YPETIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAIN 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 497 KKVIDPVAPRYVALlkKEVIPVNVPEAQEEMKEVAKHPKNPEVGLKPVWYSPKVFIEGADAEtfSEGEMVTFINWGNLNI 576
Cdd:PRK04156 403 RKLIDPIANRYFFV--RDPVELEIEGAEPLEAKIPLHPDRPERGEREIPVGGKVYVSSDDLE--AEGKMVRLMDLFNVEI 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 577 TKIHKNAdGKIISLDaklnLENKDYKKTTKVTWLAEtTHALPIPVIcvtyehlitKPVLGKDEDFkqyvnknskheelml 656
Cdd:PRK04156 479 TGVSVDK-ARYHSDD----LEEARKNKAPIIQWVPE-DESVPVRVL---------KPDGGDIEGL--------------- 528
|
490 500
....*....|....*....|.
gi 62241042 657 GDPCLKDLKKGDIIQLQRRGF 677
Cdd:PRK04156 529 AEPDVADLEVDDIVQFERFGF 549
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
160-686 |
1.32e-97 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 332.88 E-value: 1.32e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 160 FQSVGTKWDVSTTKARVAPEKKqdvgkfvelpgAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDT 239
Cdd:PLN02859 238 FFSDGSVLRPSNTKEILEKHLK-----------ATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDT 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 240 NPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIDSKHRKNPIEKN 319
Cdd:PLN02859 307 NPEAEKKEYIDHIEEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKKMNSPWRDRPIEES 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 320 LQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEY 399
Cdd:PLN02859 387 LKLFEDMRRGLIEEGKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEF 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 400 HDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQG 479
Cdd:PLN02859 467 ETRRASYYWLLDSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIG 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 480 SSRS---VVNMewDKIWAFNKKVIDPVAPRYVALLKK-EVIPVNVPEAQEEMKEVAKHPKNPEVGLKP---VWYSPKVFI 552
Cdd:PLN02859 547 ITRSdnsLIRM--DRLEHHIREELNKTAPRTMVVLHPlKVVITNLESGEVIELDAKRWPDAQNDDPSAfykVPFSRVVYI 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 553 EGADAET--------FSEGEMVTFINWGNLNITK-IHKNADGKIISLDAKLnlenkDYKKTTK----VTWLAETTHAL-P 618
Cdd:PLN02859 625 ERSDFRLkdskdyygLAPGKSVLLRYAFPIKCTDvVLADDNETVVEIRAEY-----DPEKKTKpkgvLHWVAEPSPGVeP 699
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62241042 619 IPVICVTYEHLITKPVLGKDEDFKQYVNKNSKheELMLGD---PCLKDLKKGDIIQLQRRGFFICDQPYEP 686
Cdd:PLN02859 700 LKVEVRLFDKLFLSENPAELEDWLEDLNPQSK--EVISGAyavPSLKDAKVGDRFQFERLGYFAVDKDSTP 768
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
1027-1405 |
9.35e-90 |
|
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440211 [Multi-domain] Cd Length: 564 Bit Score: 303.62 E-value: 9.35e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1027 WYSQVITKSEMIEYHdISGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPMFVSQSaLEKEKTHVADFAPEVAWVtr 1106
Cdd:COG0442 21 WSHQLMLRAGLIRKL-ASGIYTYLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQPAE-LWEESGRWEGFGPELARV-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1107 sgKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATMEEAAEEV 1186
Cdd:COG0442 97 --TDRLEREFCLGPTHEEVITDLVRNEIKSYRDLPLLLYQIQTKFRDEIRPRFGLLRTREFLMKDAYSFHATEEELDEEY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1187 LQILDLYAQVYEElLAIPVVKGRKT-------EKEKFA--------------GGDY------------------------ 1221
Cdd:COG0442 175 QKMLDAYERIFER-LGLPVRAVEADsgaiggsESHEFMvladsgedtivycdACDYaaniekaealappaeraeptkele 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1222 ------TTTIEA------------------------------------------------------------------FI 1229
Cdd:COG0442 254 avatpgAKTIEEvaeflgvpaektvktlvykadgelvavlvrgdhelneiklenllgaselelateeeieaalgavpgFL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1230 SASG----------------------------------------------------------------RAIQGGTSHHLG 1245
Cdd:COG0442 334 GPVGlgvpyiadrsvagmsnfvcganeddyhytnvnwgrdfpvdevadlrnvvegdpcpdcggllqdgRGIEVGHIFKLG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1246 QNFSKMFEIVFEDPKipGEKQFAYQNSWGLT-TRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCGItnalseeDKEALI 1324
Cdd:COG0442 414 TKYSKAMDATFLDEN--GKEQPVWMGCYGIGvTRLIAAAIEQHHDDKGIIWPPAIAPFQVVIVPINM-------KDEAVL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1325 AKCNDYRRRLLSVNIRVRADLRDNySPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVAENEAETKLQAI 1404
Cdd:COG0442 485 EAAEELYAELKAAGIDVLLDDRDE-RPGVKFADAELIGIPLRIVIGPRDLEEGQVEVKRRDTGEKEEVPLDELVETVKEL 563
|
.
gi 62241042 1405 L 1405
Cdd:COG0442 564 L 564
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
1292-1512 |
6.45e-86 |
|
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: 278.80 E-value: 6.45e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1292 GLVLPPRVACVQVVIIPCGITnalsEEDKEALIAKCNDYRRRLLSVNIRVRADLRDNYSPGWKFNHWELKGVPIRLEVGP 1371
Cdd:cd00862 1 GLVLPPRVAPIQVVIVPIGIK----DEKREEVLEAADELAERLKAAGIRVHVDDRDNYTPGWKFNDWELKGVPLRIEIGP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1372 RDMKSCQFVAVRRDTGEKLTVAENEAETKLQAILEDIQVTLFTRASEDLK-THMVVanTMEDFQKILDSGKIVQIPFCGE 1450
Cdd:cd00862 77 RDLEKNTVVIVRRDTGEKKTVPLAELVEKVPELLDEIQEDLYERALEFRDaTRIVD--TWEEFKEALNEKGIVLAPWCGE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62241042 1451 IDCEDWIKKTTArdqdlepgapsmgAKSLCIPFkPLCELQPGAKCV-CGkNPAKYYTLFGRSY 1512
Cdd:cd00862 155 EECEEEIKEETA-------------ATILCIPF-DEAKLEEGGKCVvCG-RPAKAYARFAKSY 202
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
1023-1285 |
2.68e-73 |
|
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: 245.36 E-value: 2.68e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1023 NLADWYSQVITKSEMIEYHDISGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKTHVADFAPEVA 1102
Cdd:cd00772 1 DASEKSLEHIGKAELADQGPGRGIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGFSKELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1103 WVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATMEEA 1182
Cdd:cd00772 81 VFKDAGDEELEEDFALRPTLEENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIRPRFGFLRAREFIMKDGHSAHADAEEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1183 AEEVLQILDLYAQVYEELLAIPVVKGRKTEKEKFAGGDYTTTIEAfISASGRAIQGGTSHHLGQNFSKMFE--IVFEDPK 1260
Cdd:cd00772 161 DEEFLNMLSAYAEIARDLAAIDFIEGEADEGAKFAGASKSREFEA-LMEDGKAKQAETGHIFGEGFARAFDlkAKFLDKD 239
|
250 260
....*....|....*....|....*.
gi 62241042 1261 ipGEKQFAYQNSWGLT-TRTIGVMTM 1285
Cdd:cd00772 240 --GKEKFFEMGCWGIGiSRFIGAIIE 263
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
196-483 |
8.56e-65 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 228.14 E-value: 8.56e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 196 GKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQ-FTYTSDHFE 274
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEgPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 275 TIMKYAEKLIQEGKAYVDDTPAEQMKAEREQ--------RIDSKHRKNPIEKNLQMWEEmkkgsqfGQSCCLRAKI---- 342
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETqtapgkppRYDGRCRDLSPEELERMLAA-------GEPPVLRFKIpeeg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 343 ----DMSS-----NNGCMRDPTLYRckiqphpRTGnkynvYPTYDFACPIVDSIEGVTHALRT------TEYHDrdeqfy 407
Cdd:COG0008 156 vvfdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGeehlsnTPRQI------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 408 WIIEALGIRKPyiwEYSRLNL----NNTVLSKRKltwfvneGLVdgwddprfpTVRGVLRRGMTVEGLKQFIAAQGSSRS 483
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLilgpDGTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
197-506 |
3.75e-63 |
|
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating Glutamyl-tRNA synthetase (GluRS) cataytic core domain. These enzymes attach Glu to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185682 [Multi-domain] Cd Length: 240 Bit Score: 215.29 E-value: 3.75e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 197 KVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFE--KVILEDVAMLHIKPDQFTYTSDHFE 274
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPDPEayDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 275 TIMKYAEKLIQEGKAYVddtpaeqmkaereqridskhrknpieknlqmweemkkgsqfgqscclrakidmssnngcmrdp 354
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 355 tlyrckiqpHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLS 434
Cdd:cd09287 98 ---------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIHWGRLKIEGGKLS 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62241042 435 KRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPR 506
Cdd:cd09287 169 TSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRANR 240
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
504-681 |
4.94e-46 |
|
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: 163.60 E-value: 4.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 504 APRYVALLKKEVIPV-NVPEAQEEMKEVAKHPKNPEVGLKPVWYSPKVFIEGADAETFSEGEMVTFINWGNLNITKIHKN 582
Cdd:pfam03950 1 APRYMAVLDPVKVVIeNYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDFKRLAPGEEVRLMDAYNIKVTEVVKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 583 ADGKIISLDAKLNLENKDY---KKTTKVTWLAETThalPIPVICVTYEHLITkpvlgKDEDFKQYVNKNSKHE-ELMLGD 658
Cdd:pfam03950 81 EDGNVTELHCTYDGDDLGGarkVKGKIIHWVSASD---AVPAEVRLYDRLFK-----DEDDADFLLNPDSLKVlTEGLAE 152
|
170 180
....*....|....*....|...
gi 62241042 659 PCLKDLKKGDIIQLQRRGFFICD 681
Cdd:pfam03950 153 PALANLKPGDIVQFERIGYFRVD 175
|
|
| GST_C_GluProRS_N |
cd10309 |
Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional ... |
74-157 |
5.95e-39 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional Glutamyl-Prolyl-tRNA synthetase; Glutathione S-transferase (GST) C-terminal domain family, bifunctional GluRS-Prolyl-tRNA synthetase (GluProRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of GluProRS from higher eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. The GST_C-like domain of GluProRS may be involved in protein-protein interactions, mediating the formation of the multi-aaRS complex in higher eukaryotes. The multi-aaRS complex acts as a molecular hub for protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.
Pssm-ID: 198342 [Multi-domain] Cd Length: 81 Bit Score: 139.76 E-value: 5.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 74 EHTEIDHWLEFSATKLSSCDSFTSTINELNHCLSLRTYLVGNSLSLADLCVWATLKGNAAWQEqlkQKKAPVHVKRWFGF 153
Cdd:cd10309 1 EQTEVDHWISFSAGRLSCDQDFSSALSYLDKALSLRTYLVGNSLTLADFAVWAALRGNGEWLA---SKEKYVNVTRWFKF 77
|
....
gi 62241042 154 LEAQ 157
Cdd:cd10309 78 ISSQ 81
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
197-482 |
8.21e-38 |
|
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA synthetase(GluRS)/Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Glu or Gln, respectively, to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea, cellular organelles, and some bacteria lack GlnRS. In these cases, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme. The discriminating form of GluRS differs from GlnRS and the non-discriminating form of GluRS in their C-terminal anti-codon binding domains.
Pssm-ID: 185672 [Multi-domain] Cd Length: 230 Bit Score: 142.23 E-value: 8.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 197 KVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQ-FTYTSDHFET 275
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEgPYRQSDRFDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 276 IMKYAEKLIQEGkayvddtpaeqmkaereqridskhrknpieknlqmweemkkgsqfgqscclrakidmssnngcmrdpt 355
Cdd:cd00418 81 YRAYAEELIKKG-------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 356 lyrckiqphprtgnkynVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNL-NNTVLS 434
Cdd:cd00418 93 -----------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLeDGTKLS 155
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 62241042 435 KRKLtwfvneglvdgwddprFPTVRGVLRRGMTVEGLKQFIAAQGSSR 482
Cdd:cd00418 156 KRKL----------------NTTLRALRRRGYLPEALRNYLALIGWSK 187
|
|
| Gly_His_Pro_Ser_Thr_tRS_core |
cd00670 |
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic ... |
1053-1249 |
4.32e-33 |
|
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: 128.66 E-value: 4.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1053 AYAIWEAIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKtHVADFAPEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAK 1132
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGG-HLDGYRKEMYTFEDKGRELRDTDLVLRPAACEPIYQIFSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1133 WVQSHRDLPIKLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSaFATMEEAAEEVLQILDLYAQVYEElLAIPVVKGRKTE 1212
Cdd:cd00670 80 EILSYRALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVEYVV-FGEPEEAEEERREWLELAEEIARE-LGLPVRVVVADD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 62241042 1213 KEKFAGGD--------YTTTIEAFISASGRAIQGGTSHHLGQNFS 1249
Cdd:cd00670 158 PFFGRGGKrgldagreTVVEFELLLPLPGRAKETAVGSANVHLDH 202
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
753-802 |
1.00e-23 |
|
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 94.99 E-value: 1.00e-23
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 62241042 753 LYNRVAVQGDVVRELKAKKAPKEDVDAAVKQLLSLKAEYKEKTGQEYKPG 802
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
|
|
| ProRS-C_1 |
pfam09180 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
1430-1512 |
2.92e-23 |
|
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: 94.51 E-value: 2.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1430 MEDFQKILDSGKIVQIPFCGEIDCEDWIKKTTardqdlepgapsmGAKSLCIPFKplcELQPGAKCVCGKNPAKYYTLFG 1509
Cdd:pfam09180 1 WEEFKEALEEKGFVLAPWCGDEECEDKIKEET-------------GATSRCIPFD---QEEEGGKCIVCGKPAKKWVLFA 64
|
...
gi 62241042 1510 RSY 1512
Cdd:pfam09180 65 RSY 67
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
753-805 |
3.73e-23 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 93.71 E-value: 3.73e-23
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 62241042 753 LYNRVAVQGDVVRELKAKKAPKEDVDAAVKQLLSLKAEYKEKTGQEYKPGNPP 805
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
|
|
| GST_C_AaRS_like |
cd10289 |
Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA ... |
74-157 |
6.52e-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: 93.92 E-value: 6.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 74 EHTEIDHWLEFsATKLSSCDSFTSTINELNHCLSLRTYLVGNSLSLADLCVWATLKGNAAWQEQLKQKKaPVHVKRWFGF 153
Cdd:cd10289 1 EAAQVDQWLDL-AGSLLKGKELEALLKSLNSYLASRTFLVGYSLTLADVAVFSALYPSGQKLSDKEKKK-FPHVTRWFNH 78
|
....
gi 62241042 154 LEAQ 157
Cdd:cd10289 79 IQNL 82
|
|
| ProRS-C_1 |
smart00946 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
1430-1512 |
3.18e-22 |
|
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.
Pssm-ID: 198014 Cd Length: 67 Bit Score: 91.48 E-value: 3.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1430 MEDFQKILDSGKIVQIPFCGEIDCEDWIKKTTardqdlepgapsmGAKSLCIPFKplcELQPGAKCVCGKNPAKYYTLFG 1509
Cdd:smart00946 1 LEEFKKALEEGKFVLAPWCGDEECEEKIKEET-------------GATIRCIPFD---QDEEPGKCVVCGKPAKKWVLFA 64
|
...
gi 62241042 1510 RSY 1512
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 ... |
754-806 |
4.41e-21 |
|
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: 87.78 E-value: 4.41e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 62241042 754 YNRVAVQGDVVRELKAKKAPKEDVDAAVKQLLSLKAEYKEKTGQEYKPGNPPA 806
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPG 53
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
1303-1404 |
1.30e-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: 88.03 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1303 QVVIIPCGitnalseEDKEALIAKCNDYRRRLLSVNIRVRADLRdNYSPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAV 1382
Cdd:pfam03129 1 QVVVIPLG-------EKAEELEEYAQKLAEELRAAGIRVELDDR-NESIGKKFRRADLIGIPFALVVGEKELEEGTVTVR 72
|
90 100
....*....|....*....|..
gi 62241042 1383 RRDTGEKLTVAENEAETKLQAI 1404
Cdd:pfam03129 73 RRDTGEQETVSLDELVEKLKEL 94
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
826-875 |
1.50e-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: 86.14 E-value: 1.50e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 62241042 826 LYDEVAAQGEVVRKLKAEKSPKAKINEAVECLLSLKAQYKEKTGKEYIPG 875
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
904-952 |
5.49e-20 |
|
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 84.59 E-value: 5.49e-20
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 62241042 904 LFDKVASQGEVVRKLKTEKAPKDQVDIAVQELLQLKAQYKSLIGVEYKP 952
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKP 49
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
826-878 |
2.73e-19 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 82.54 E-value: 2.73e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 62241042 826 LYDEVAAQGEVVRKLKAEKSPKAKINEAVECLLSLKAQYKEKTGKEYIPGQPP 878
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
904-956 |
4.45e-19 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 82.16 E-value: 4.45e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 62241042 904 LFDKVASQGEVVRKLKTEKAPKDQVDIAVQELLQLKAQYKSLIGVEYKPVSAT 956
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 ... |
827-878 |
2.61e-18 |
|
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.
Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 80.08 E-value: 2.61e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 62241042 827 YDEVAAQGEVVRKLKAEKSPKAKINEAVECLLSLKAQYKEKTGKEYIPGQPP 878
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 ... |
1056-1275 |
3.09e-18 |
|
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: 84.86 E-value: 3.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1056 IWEAIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKTHVADFAPevawvtrsGKTELAEPIAIRPTSETvmYPAYAkWVQ 1135
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKDLLP--------VGAENEEDLYLRPTLEP--GLVRL-FVS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1136 SHRDLPIKLNQWCNVVRWEfKHPQPFLRTREFLWQEGHSAFATMEEaAEEVLQILDLYAQVYEEL-LAIPVVKGRKTEKE 1214
Cdd:cd00768 70 HIRKLPLRLAEIGPAFRNE-GGRRGLRRVREFTQLEGEVFGEDGEE-ASEFEELIELTEELLRALgIKLDIVFVEKTPGE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62241042 1215 KFAGGdYTTTIEAFI-SASGRAIQGGTSHHLGQNFSKMFEIVFEDPkiPGEKQFAYQNSWGL 1275
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; ... |
74-156 |
3.56e-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: 77.78 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 74 EHTEIDHWLEFSATKLSSCD--SFTSTINELNHCLSLRTYLVGNSLSLADLCVWATLKGNAAWQEQLKQKKAPvHVKRWF 151
Cdd:cd10306 3 DKEQVAEWIDFATTLLVLKDfkALSQALEELDSHLTLRTFIVGYSLSLADIAVWGALRGNGVAGSLIKNKVYV-NLSRWF 81
|
....*
gi 62241042 152 GFLEA 156
Cdd:cd10306 82 SFLES 86
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
905-958 |
6.38e-17 |
|
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: 75.84 E-value: 6.38e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 62241042 905 FDKVASQGEVVRKLKTEKAPKDQVDIAVQELLQLKAQYKSLIGVEYKPVSATGA 958
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGD 54
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
754-795 |
2.66e-16 |
|
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238605 [Multi-domain] Cd Length: 42 Bit Score: 73.73 E-value: 2.66e-16
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 62241042 754 YNRVAVQGDVVRELKAKKAPKEDVDAAVKQLLSLKAEYKEKT 795
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 ... |
1111-1287 |
5.60e-15 |
|
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: 74.76 E-value: 5.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1111 ELAEPIAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVRWEFKHPQ-PFLRTREFLWQEGHSaFATMEEAAEEVLQI 1189
Cdd:pfam00587 6 ENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTrGLIRVRQFHQDDAHI-FHAPGQSPDELEDY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1190 LDLYAQVYEELLaIPVVKGRKTEKEKFAGGDYTTTIEAFISASGRAIQGGTSHHLGQNFSKMFEIVFEDPKipGEKQFAY 1269
Cdd:pfam00587 85 IKLIDRVYSRLG-LEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDED--NESKFPY 161
|
170 180
....*....|....*....|
gi 62241042 1270 QNSWGL--TTRTIGVMTMVH 1287
Cdd:pfam00587 162 MIHRAGlgVERFLAAILENN 181
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
827-868 |
9.72e-15 |
|
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238605 [Multi-domain] Cd Length: 42 Bit Score: 69.49 E-value: 9.72e-15
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 62241042 827 YDEVAAQGEVVRKLKAEKSPKAKINEAVECLLSLKAQYKEKT 868
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
905-945 |
2.10e-14 |
|
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: 68.34 E-value: 2.10e-14
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 62241042 905 FDKVASQGEVVRKLKTEKAPKDQVDIAVQELLQLKAQYKSL 945
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEA 41
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
196-452 |
6.96e-13 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 73.24 E-value: 6.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 196 GKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYT------ 269
Cdd:PLN02627 44 GPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVggeygp 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 270 ---SDHFETIMKYAEKLIQEGKAY---VDDTPAEQMKAEREQ-----RIDSKHRKNPIEknlQMWEEMKKGSQFgqscCL 338
Cdd:PLN02627 124 yrqSERNAIYKQYAEKLLESGHVYpcfCTDEELEAMKEEAELkklppRYTGKWATASDE---EVQAELAKGTPY----TY 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 339 RAKIdmsSNNGCMRDPTLYRCKIQPHPRT-GN----KYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEAL 413
Cdd:PLN02627 197 RFRV---PKEGSVKIDDLIRGEVSWNTDTlGDfvllRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKAL 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 62241042 414 GIRKPyiwEYSRLNL----NNTVLSKR---------KLTWFVNEGLVD-----GWDD 452
Cdd:PLN02627 274 GFPMP---RFAHVSLilapDRSKLSKRhgatsvgqfREMGYLPDAMVNylallGWND 327
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
1302-1402 |
3.34e-11 |
|
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and prolyl tRNA synthetases, which are classified as a group of class II aminoacyl-tRNA synthetases (aaRS). In aaRSs, the anticodon binding domain is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only. This domain is also found in the accessory subunit of mitochondrial polymerase gamma (Pol gamma b).
Pssm-ID: 238379 [Multi-domain] Cd Length: 94 Bit Score: 61.26 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1302 VQVVIIPCGitnalseEDKEALIAKCNDYRRRLLSVNIRVRADLRDNySPGWKFNHWELKGVPIRLEVGPRDMKSCQFVA 1381
Cdd:cd00738 2 IDVAIVPLT-------DPRVEAREYAQKLLNALLANGIRVLYDDRER-KIGKKFREADLRGVPFAVVVGEDELENGKVTV 73
|
90 100
....*....|....*....|.
gi 62241042 1382 VRRDTGEKLTVAENEAETKLQ 1402
Cdd:cd00738 74 KSRDTGESETLHVDELPEFLV 94
|
|
| GST_C_AIMP3 |
cd10305 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ... |
74-151 |
5.87e-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: 57.69 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 74 EHTEIDHWLEFSATKLSSCDS---FTSTINELNHCLSLRTYLVGNSLSLADLCVWATLKgNAAWQEQLKQKKAPVHVKRW 150
Cdd:cd10305 3 ERAQVDQWLEYRVTQVAPASDkadAKSLLKELNSYLQDRTYLVGHKLTLADVVLYYGLH-PIMKDLSPQEKEQYLNVSRW 81
|
.
gi 62241042 151 F 151
Cdd:cd10305 82 F 82
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
1244-1405 |
1.99e-09 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 62.02 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1244 LGQNFSKMFEIVFEDPKipGEKQFAYQNSWGlttrtIGVMTMV------HGDNMGLVLPPRVACVQVVIIPcgiTNALSE 1317
Cdd:PRK09194 412 LGTKYSEAMNATVLDEN--GKAQPLIMGCYG-----IGVSRLVaaaieqNHDEKGIIWPKAIAPFDVHIVP---VNMKDE 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1318 EDKEA---LIAKcndyrrrLLSVNIRVRADLRDNySPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVAE 1394
Cdd:PRK09194 482 EVKELaekLYAE-------LQAAGIEVLLDDRKE-RPGVKFADADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPV 553
|
170
....*....|.
gi 62241042 1395 NEAETKLQAIL 1405
Cdd:PRK09194 554 DELVEFLKALK 564
|
|
| GstA |
COG0625 |
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; |
44-167 |
6.48e-08 |
|
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440390 [Multi-domain] Cd Length: 205 Bit Score: 54.52 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 44 ENVIFTDVNSILRYLARVATTAGLYGSNLMEHTEIDHWLEFSATKLSSC---------------------DSFTSTINEL 102
Cdd:COG0625 59 DGLVLTESLAILEYLAERYPEPPLLPADPAARARVRQWLAWADGDLHPAlrnllerlapekdpaaiararAELARLLAVL 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62241042 103 NHCLSLRTYLVGNSLSLADLCVWATLkGNAAWQEqLKQKKAPvHVKRWFGFLEAQQAFQSVGTKW 167
Cdd:COG0625 139 EARLAGGPYLAGDRFSIADIALAPVL-RRLDRLG-LDLADYP-NLAAWLARLAARPAFQRALAAA 200
|
|
| GST_C_AIMP2 |
cd03200 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ... |
55-157 |
1.45e-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: 50.98 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 55 LRYLARVAttaGLYGSNLMEHTEIDHWLEFSATKL--SSCDSFTSTINELNHCLSLRTYLVGNSLSLADLCVWATLK--G 130
Cdd:cd03200 1 ARFLFRLL---GDESDDPVNATLIDSWVDTAIFQLleGSSKEKAAVLRALNSALGRSPWLVGSEPTVADIALWSAVLqtG 77
|
90 100
....*....|....*....|....*..
gi 62241042 131 NAAwqeqlkqkKAPVHVKRWFGFLEAQ 157
Cdd:cd03200 78 LAS--------GAPANVQRWMKSCENL 96
|
|
| MetRS_RNA |
cd00939 |
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
826-870 |
1.33e-06 |
|
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238475 [Multi-domain] Cd Length: 45 Bit Score: 46.31 E-value: 1.33e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 62241042 826 LYDEVAAQGEVVRKLKAEKSPKAKINEAVECLLSLKAQYKEKTGK 870
Cdd:cd00939 1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEGK 45
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
1120-1403 |
1.94e-06 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 52.17 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1120 PTSETVMYPAYAKWVQSHRDLPIKLNQwcnvVRWEFK---HPQpF--LRTREFLWQEGHSAFATMEEAAEEVLQILDLYA 1194
Cdd:PRK12325 108 PTNEEMITDIFRSYVKSYKDLPLNLYH----IQWKFRdeiRPR-FgvMRGREFLMKDAYSFDLDEEGARHSYNRMFVAYL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1195 QVYE--ELLAIPV------------------------------------VKGRKTEKEKFAGGDYTTTIEAFISA----- 1231
Cdd:PRK12325 183 RTFArlGLKAIPMradtgpiggdlshefiilaetgestvfydkdfldllVPGEDIDFDVADLQPIVDEWTSLYAAteemh 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1232 --------------SGRAIQGGTSHHLGQNFSKMFEIVFEDPKipGEKQFAYQNSWGlttrtIGVMTMV-------HGDN 1290
Cdd:PRK12325 263 deaafaavpeerrlSARGIEVGHIFYFGTKYSEPMNAKVQGPD--GKEVPVHMGSYG-----IGVSRLVaaiieasHDDK 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1291 mGLVLPPRVACVQVVIIPCGITNalseedkEALIAKCNDYRRRLLSVNIRVRADLRDNySPGWKFNHWELKGVPIRLEVG 1370
Cdd:PRK12325 336 -GIIWPESVAPFKVGIINLKQGD-------EACDAACEKLYAALSAAGIDVLYDDTDE-RPGAKFATMDLIGLPWQIIVG 406
|
330 340 350
....*....|....*....|....*....|...
gi 62241042 1371 PRDMKSCQFVAVRRDTGEKLTVAENEAETKLQA 1403
Cdd:PRK12325 407 PKGLAEGKVELKDRKTGEREELSVEAAINRLTA 439
|
|
| GST_C_Arc1p_N_like |
cd10304 |
Glutathione S-transferase C-terminal-like, alpha helical domain of the Aminoacyl tRNA ... |
74-163 |
2.61e-06 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of the Aminoacyl tRNA synthetase cofactor 1 and similar proteins; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase cofactor 1 (Arc1p)-like subfamily; Arc1p, also called GU4 nucleic binding protein 1 (G4p1) or p42, is a tRNA-aminoacylation and nuclear-export cofactor. It contains a domain in the N-terminal region with similarity to the C-terminal alpha helical domain of GSTs. This domain mediates the association of the aminoacyl tRNA synthetases (aaRSs), MetRS and GluRS, in yeast to form a stable stoichiometric ternany complex. The GST_C-like domain of Arc1p is a protein-protein interaction domain containing two binding sites which enable it to bind the two aaRSs simultaneously and independently. The MetRS-Arc1p-GluRS complex selectively recruits and aminoacylates its cognate tRNAs without additional cofactors. Arc1p also plays a role in the transport of tRNA from the nucleus to the cytoplasm. It may also control the subcellular distribution of GluRS in the cytoplasm, nucleoplasm, and the mitochondrial matrix.
Pssm-ID: 198337 [Multi-domain] Cd Length: 100 Bit Score: 47.37 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 74 EHTEIDHWLEFSATKLSSCDSFTsTINELNHCLSLRTYLVGNS-LSLADLCVWATLKGNAA-WQEQLKQKKAPV-HVKRW 150
Cdd:cd10304 3 QSAEVAQWLSVAKSGPVSKDVQE-TLGQLNLHLRTRTFLLGTGkPSVADVAVFEAVLPVVKeWSDEVKTGYAKYrHILRW 81
|
90
....*....|...
gi 62241042 151 FGFLEAQQAFQSV 163
Cdd:cd10304 82 VDYVQNLLLFIPE 94
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
908-941 |
3.65e-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: 45.15 E-value: 3.65e-06
10 20 30
....*....|....*....|....*....|....
gi 62241042 908 VASQGEVVRKLKTEKAPKDQVDIAVQELLQLKAQ 941
Cdd:cd00938 7 VKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQ 40
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
830-863 |
1.08e-05 |
|
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238474 [Multi-domain] Cd Length: 45 Bit Score: 44.00 E-value: 1.08e-05
10 20 30
....*....|....*....|....*....|....
gi 62241042 830 VAAQGEVVRKLKAEKSPKAKINEAVECLLSLKAQ 863
Cdd:cd00938 7 VKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQ 40
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
1044-1282 |
2.85e-05 |
|
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: 47.57 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1044 SGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPmFVSQSALEKEKTHVADFAPEVAWVT-RSGKTELaepiaIRPTS 1122
Cdd:cd00779 21 SGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMP-ILQPAELWKESGRWDAYGPELLRLKdRHGKEFL-----LGPTH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1123 ETVMYPAYAKWVQSHRDLPIKLNQwcnvVRWEF---KHPQpF--LRTREFLWQEGHSaFATMEEAAEEVlqildlYAQVY 1197
Cdd:cd00779 95 EEVITDLVANEIKSYKQLPLNLYQ----IQTKFrdeIRPR-FglMRGREFLMKDAYS-FDIDEESLEET------YEKMY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1198 E------ELLAIPVVKgrktekekfaggdytttIEAfisASGrAIQGGTSH--------------------HLGQNFSKM 1251
Cdd:cd00779 163 QaysrifKRLGLPFVK-----------------VEA---DSG-AIGGSLSHefhvlsplkitkgievghifQLGTKYSKA 221
|
250 260 270
....*....|....*....|....*....|..
gi 62241042 1252 FEIVFEDPKipGEKQFAYQNSWGL-TTRTIGV 1282
Cdd:cd00779 222 LGATFLDEN--GKPKPLEMGCYGIgVSRLLAA 251
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
756-790 |
5.66e-05 |
|
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238474 [Multi-domain] Cd Length: 45 Bit Score: 41.69 E-value: 5.66e-05
10 20 30
....*....|....*....|....*....|....*
gi 62241042 756 RVAVQGDVVRELKAKKAPKEDVDAAVKQLLSLKAE 790
Cdd:cd00938 6 AVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQ 40
|
|
| MetRS_RNA |
cd00939 |
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
904-948 |
6.23e-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: 41.69 E-value: 6.23e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 62241042 904 LFDKVASQGEVVRKLKTEKAPKDQVDIAVQELLQLKAQYKSLIGV 948
Cdd:cd00939 1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEGK 45
|
|
| MetRS_RNA |
cd00939 |
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
757-796 |
1.02e-04 |
|
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238475 [Multi-domain] Cd Length: 45 Bit Score: 41.30 E-value: 1.02e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 62241042 757 VAVQGDVVRELKAKKAPKEDVDAAVKQLLSLKAEYKEKTG 796
Cdd:cd00939 5 VAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEG 44
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
757-827 |
1.40e-04 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 46.66 E-value: 1.40e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62241042 757 VAVQGDVVRELKAKKAPKEDVDAAVKQL--LSLKAEYKEKTGQEYKPGNPPAEIGQNISSNSSASILESKSLY 827
Cdd:PLN02734 16 VTAQGNAVRALKASKADKAEIDAAIEKLkaLKLEKSALEKELQAAVGAGGDGAASKEAFRQAVVNTLERRLFY 88
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
1303-1402 |
1.94e-04 |
|
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238438 [Multi-domain] Cd Length: 94 Bit Score: 41.81 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1303 QVVIIPCGITNALSEEDKEALIAkcndyrrRLLSVNIRVRADLRDNySPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAV 1382
Cdd:cd00861 3 DVVIIPMNMKDEVQQELAEKLYA-------ELQAAGVDVLLDDRNE-RPGVKFADADLIGIPYRIVVGKKSAAEGIVEIK 74
|
90 100
....*....|....*....|
gi 62241042 1383 RRDTGEKLTVAENEAETKLQ 1402
Cdd:cd00861 75 VRKTGEKEEISIDELLEFLQ 94
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
904-958 |
2.82e-04 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 45.51 E-value: 2.82e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 62241042 904 LFDKVASQGEVVRKLKTEKAPKDQVDIAVQELLQLKAQyKSLIGVEYKPVSATGA 958
Cdd:PLN02734 12 KQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLE-KSALEKELQAAVGAGG 65
|
|
| GlyRS_RNA |
cd00935 |
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS ... |
753-794 |
3.52e-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: 39.78 E-value: 3.52e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 62241042 753 LYNRVAVQGDVVRELKAKKAPKEDVDAAVKQLLSLKAEYKEK 794
Cdd:cd00935 4 LRAAVKEQGDLVRKLKEEGAPDVDIKKAVAELKARKKLLEDK 45
|
|
| GST_C_EF1Bgamma_like |
cd03181 |
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ... |
74-163 |
4.86e-04 |
|
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: 41.39 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 74 EHTEIDHWLEFSATKL--SSC--------------DSFTSTINELNHC-------LSLRTYLVGNSLSLADLCVWATLKG 130
Cdd:cd03181 1 EAAQVLQWISFANSELlpAAAtwvlpllgiapynkKAVDKAKEDLKRAlgvleehLLTRTYLVGERITLADIFVASALLR 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 62241042 131 ------NAAWQEQLkqkkapVHVKRWFGFLEAQQAFQSV 163
Cdd:cd03181 81 gfetvlDPEFRKKY------PNVTRWFNTVVNQPKFKAV 113
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
1278-1403 |
5.14e-04 |
|
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: 44.64 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1278 RTIGVMTMVHGDNMGLVLPPrvacVQVVIIPcgITnalseedkEALIAKCNDYRRRLLSVNIRVRADLRDNySPGWKFNH 1357
Cdd:COG0441 520 RFIGILIEHYAGAFPLWLAP----VQVVVLP--IS--------DKHADYAKEVAKKLRAAGIRVEVDLRNE-KIGYKIRE 584
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 62241042 1358 WELKGVPIRLEVGPRDMKSCQfVAVR-RDTGEKLTVAENEAETKLQA 1403
Cdd:COG0441 585 AQLQKVPYMLVVGDKEVENGT-VSVRrRGGGDLGTMSLDEFIARLKE 630
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
828-889 |
1.17e-03 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 43.58 E-value: 1.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62241042 828 DEVAAQGEVVRKLKAEKSPKAKINEAVECLLSLKAQyKEKTGKEYipgQPPLSQSSDSSPTR 889
Cdd:PLN02734 14 AAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLE-KSALEKEL---QAAVGAGGDGAASK 71
|
|
| GlyRS_RNA |
cd00935 |
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS ... |
904-945 |
1.19e-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: 38.24 E-value: 1.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 62241042 904 LFDKVASQGEVVRKLKTEKAPKDQVDIAVQEllqLKAQYKSL 945
Cdd:cd00935 4 LRAAVKEQGDLVRKLKEEGAPDVDIKKAVAE---LKARKKLL 42
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
199-282 |
1.66e-03 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 40.54 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 199 TVRFPPEASGYLHIGHAKAALLN---QHY--QVNFKGKLIMRFDDTNPEKEK------EDFEKVILEDVAMLHikpDQFT 267
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFdflAQAyrKLGYKVRCIALIDDAGGLIGDpankkgENAKAFVERWIERIK---EDVE 77
|
90
....*....|....*
gi 62241042 268 YTSDHFETIMKYAEK 282
Cdd:cd00802 78 YMFLQAADFLLLYET 92
|
|
| GST_C_Delta_Epsilon |
cd03177 |
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; ... |
102-151 |
2.38e-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: 39.44 E-value: 2.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 62241042 102 LNHCLSLRTYLVGNSLSLADLCVWATLkGNAAWQEqLKQKKAPvHVKRWF 151
Cdd:cd03177 50 LETFLEGSDYVAGDQLTIADLSLVATV-STLEVVG-FDLSKYP-NVAAWY 96
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
1302-1402 |
2.60e-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: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241042 1302 VQVVIIPcgITNalseedkealiaKCNDY----RRRLLSVNIRVRADLRDNySPGWKFNHWELKGVPIRLEVGPRDMKSc 1377
Cdd:cd00860 2 VQVVVIP--VTD------------EHLDYakevAKKLSDAGIRVEVDLRNE-KLGKKIREAQLQKIPYILVVGDKEVET- 65
|
90 100
....*....|....*....|....*.
gi 62241042 1378 QFVAVR-RDTGEKLTVAENEAETKLQ 1402
Cdd:cd00860 66 GTVSVRtRDGGDLGSMSLDEFIEKLK 91
|
|
| GST_C_8 |
cd03207 |
C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; ... |
93-159 |
5.72e-03 |
|
C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 8; composed of Agrobacterium tumefaciens GST and other uncharacterized bacterial proteins with similarity to GSTs. 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 three-dimensional structure of Agrobacterium tumefaciens GST has been determined but there is no information on its functional characterization.
Pssm-ID: 198316 [Multi-domain] Cd Length: 101 Bit Score: 38.05 E-value: 5.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62241042 93 DSFTSTINELNHCLSLRTYLVGNSLSLADLCVWATLkgnaAWQEQLKQKKAPVHVKRWFGFLEAQQA 159
Cdd:cd03207 39 GDLDERLAALEAALAGRPYLVGERFSAADLLLASVL----RWARAFGLLPEYPALRAYVARCTARPA 101
|
|
| GlyRS_RNA |
cd00935 |
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS ... |
825-867 |
5.83e-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: 36.31 E-value: 5.83e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 62241042 825 SLYDEVAAQGEVVRKLKAEKSPKAKINEAVECLLSLKAQYKEK 867
Cdd:cd00935 3 PLRAAVKEQGDLVRKLKEEGAPDVDIKKAVAELKARKKLLEDK 45
|
|
| GST_C |
pfam00043 |
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ... |
106-151 |
9.52e-03 |
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Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants. Stringent starvation proteins in E. coli are also included in the alignment but are not known to have GST activity. The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed to reside in the N-terminal domain. In plants, GSTs are encoded by a large gene family (48 GST genes in Arabidopsis) and can be divided into the phi, tau, theta, zeta, and lambda classes.
Pssm-ID: 459647 [Multi-domain] Cd Length: 93 Bit Score: 36.88 E-value: 9.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 62241042 106 LSLRTYLVGNSLSLADLCVWATLKGNAAWQEQLKQKKAPvHVKRWF 151
Cdd:pfam00043 42 LKGQTYLVGDKLTLADIALAPALLWLYELDPACLREKFP-NLKAWF 86
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