|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
13-686 |
0e+00 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 748.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 13 PPLGALLAVEHVKDNVSIF--VEEGKENILRVSENVVFTDINSILRYLARVAMTARLYGSNLMEHTEIDHWLEFSATkLS 90
Cdd:PLN02907 12 PPLAVIAAAKVAGVPLTIDpsLKSGSAPTLLFSSGEKLTGTNVLLRYIARSASLPGFYGQDAFESSQVDEWLDYAPT-FS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 91 SCDLFPSAINELNHCLSLRTYLVGNSLSLADLCVWATLKGNVAWQEQLQQNRAPVHVKRWFGFLEAQQAFQSVGTKWNVS 170
Cdd:PLN02907 91 SGSEFENACEYVDGYLASRTFLVGYSLTIADIAIWSGLAGSGQRWESLRKSKKYQNLVRWFNSISAEYSDILNEVTAAYV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 171 ATKAKG---APQKKPDV------------GKF-VELPGAEMGKVTVRFPPEASGF------------KFMAETHtdyvlg 222
Cdd:PLN02907 171 GKRGAGkpaAAKSKEKVadagkadgakdkGSFeVDLPGAEEGKVCTRFPPEPSGYlhighakaallnQYFARRY------ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 223 NGKVI-------------------LEDVAMLHIEPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAERMKAEREQRTE 283
Cdd:PLN02907 245 KGKLIvrfddtnpskesdefveniLKDIETLGIKYDAVTYTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMDGIE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 284 SKHRNNSVEKNLQMWEEMKKGSPFGQSCCLRAKIDMNSNNGCMRDPTLYRCKIQPHPRTGNRYNVYPTYDFACPIVDSIE 363
Cdd:PLN02907 325 SKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDMQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 364 GVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVDEGLVDGWDDPRFPTVRGVLRRGMTV 443
Cdd:PLN02907 405 GVTHALRSSEYHDRNAQYYRILEDMGLRKVHIWEFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKI 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 444 EGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLKKEVIPVHV---PgAQEEMKEVAKHPKNPDVGLKPVW 520
Cdd:PLN02907 485 EALKQFILSQGASKNLNLMEWDKLWTINKKIIDPVCPRHTAVLKEGRVLLTLtdgP-ETPFVRIIPRHKKYEGAGKKATT 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 521 YSPRVFIEGADAETLSEGEMVTFINWGNLNITKIHKNANGKIVSLDAKLNLENkDYKKTT-KITWLAETAHALPIPaiCV 599
Cdd:PLN02907 564 FTNRIWLDYADAEAISEGEEVTLMDWGNAIIKEITKDEGGAVTALSGELHLEG-SVKTTKlKLTWLPDTNELVPLS--LV 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 600 TYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDQPYEPVSphscreAPCVLIYIPD 679
Cdd:PLN02907 641 EFDYLITKKKLEEDDNFLDVLNPCTKKETAALGDSNMRNLKRGEIIQLERKGYYRCDAPFVRSS------KPIVLFAIPD 714
|
....*..
gi 940746979 680 GHTKEMP 686
Cdd:PLN02907 715 GRQQKSG 721
|
|
| proS_fam_I |
TIGR00408 |
prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ... |
993-1487 |
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: 559.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 993 AKKEENLADWYSQVITKSEMIEYYDVSGCYILRPWAFSIWESIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKTHVADF 1072
Cdd:TIGR00408 2 ASKMQDFSEWYHQILEKAEIIDYYPVKGCYVWLPYGFKIWKNIQKILRNILDEIGHEEVYFPMLIPESELAKEKDHIKGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1073 APEVAWVTRSGKTELAEPIAVRPTSETVMYPAYAKWVQSHRDLPIRLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFA 1152
Cdd:TIGR00408 82 EPEVYWITHGGLSKLDEPLALRPTSETAMYPMFKKWVKSYTDLPLKINQWVNVFRYETKHTRPFLRTREFTWQEAHTAHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1153 TFEEAAAEVLQILDLYAQVYEELLAIPVVKGRKTEKEKFAGGDYTTTVEAFISaSGRAIQGATSHHLGQNFSKMFEIIFE 1232
Cdd:TIGR00408 162 TAEEAEEQVLRALDIYKEFIENSLAIPYFVGRKPEWEKFAGAEYTWAFETIMP-DGRTLQIATSHNLGQNFAKTFEIKFE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1233 DPKtpGEKQFAYQNSWGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVVIPCgitnALSEEDRDALIAKCNDYRRRLLSV 1312
Cdd:TIGR00408 241 TPT--GDKEYAYQTSYGISTRVIGALIAIHSDEKGLVLPPRVAPIQVVIIPI----IFKKKENEKVMEAAREVRSRLKKA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1313 NIRARADLRDNySPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVTENEAETKLKALLEDIHANLFRKAS 1392
Cdd:TIGR00408 315 GFRVHIDDRDN-RPGRKFYQWEIKGIPLRIEVGPNDIEKNIAVISRRDTGEKYQVSLDQLEERVVELLNNIQENLRNRAW 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1393 EDLKTHMVVANSMEDFQKLL-DSGKIVQIPFCGEIDCEDWIKKTTArdqdlepgapsmgAKSLCIPFKPlcelQPGARCV 1471
Cdd:TIGR00408 394 ERFEQKIVIVETLEEIKQALnEKRGVVLVPWCGEEECEEDLKEKVQ-------------VTILCIPEDG----DVLQLCI 456
|
490
....*....|....*.
gi 940746979 1472 CGKNPAKYYTLFGRSY 1487
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 ... |
998-1261 |
1.01e-160 |
|
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: 484.79 E-value: 1.01e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 998 NLADWYSQVITKSEMIEYYDVSGCYILRPWAFSIWESIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKTHVADFAPEVA 1077
Cdd:cd00778 1 DFSEWYTEVITKAELIDYGPVKGCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPESELEKEKEHIEGFAPEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1078 WVTRSGKTELAEPIAVRPTSETVMYPAYAKWVQSHRDLPIRLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATFEEA 1157
Cdd:cd00778 81 WVTHGGLEELEEPLALRPTSETAIYPMFSKWIRSYRDLPLKINQWVNVFRWETKTTRPFLRTREFLWQEGHTAHATEEEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1158 AAEVLQILDLYAQVYEELLAIPVVKGRKTEKEKFAGGDYTTTVEAFISaSGRAIQGATSHHLGQNFSKMFEIIFEDPKtp 1237
Cdd:cd00778 161 EEEVLQILDLYKEFYEDLLAIPVVKGRKTEWEKFAGADYTYTIEAMMP-DGRALQSGTSHNLGQNFSKAFDIKYQDKD-- 237
|
250 260
....*....|....*....|....
gi 940746979 1238 GEKQFAYQNSWGLTTRTIGVMTMV 1261
Cdd:cd00778 238 GQKEYVHQTSWGISTRLIGAIIMI 261
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
197-477 |
3.13e-120 |
|
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: 378.59 E-value: 3.13e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 197 KVTVRFPPEASG-----------FKFM-AETH----------TD---YVLGNGKVILEDVAMLHIEPD-QFTYTSDHFET 250
Cdd:pfam00749 1 KVRTRFAPSPTGylhighakaalFNYLyAKNHngkfilrfedTDperETPEFEESILEDLKWLGIKWDyGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 251 IMKYAEKLIQEGKAYVDDTPAERMKAEREQ--RTESKHRNNSVEKNLQMW-EEMKKGSPFGQSCCLRAKIDMNSnNGCMR 327
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEqeALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMES-PYVFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 328 DPTLYRCKIQP---HPRTGNRYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIR-KPYIWEYSRLNL 403
Cdd:pfam00749 160 DPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 940746979 404 NNTVLSKRKLTWFVDEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSV-VNMEWDKIWAFNKKVIDP 477
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFdVNRLSKSLEAFDRKKLDW 314
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
141-661 |
3.43e-115 |
|
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: 374.16 E-value: 3.43e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 141 NRAPVHVKRWFGFLEAQQAFQSVGTKWNVSATKAK-----GAPQKKPDVGKFVELPGAEMGKVTVRFPPEASGFKFMAet 215
Cdd:TIGR00463 32 NNPELRKKAKEVLEAVEAAVEEVNSLSPEEQKELMkrlglDIKKKEKKRKGLRELPGAKMGEVVMRFAPNPSGPLHIG-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 216 HTDYVLGN--------GKVIL-------------------EDVAMLHIEPDQFTYTSDHFETIMKYAEKLIQEGKAYVDD 268
Cdd:TIGR00463 110 HARAAILNheyakkydGKLIIrfddtdprrvdpeaydmilEDLEWLGVKWDEVVYQSDRIETYYDYTRKLIEMGKAYVCD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 269 TPAERMKAEREQRTESKHRNNSVEKNLQMWEEMKKGSPFGQSCCLRAKIDMNSNNGCMRDPTLYRCKIQPHPRTGNRYNV 348
Cdd:TIGR00463 190 CRPEEFRELRNRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 349 YPTYDFACPIVDSIEGVTHALRTTEYHD--RDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVDeGLVDGWD 426
Cdd:TIGR00463 270 YPTMDFSVAIDDHLLGVTHVLRGKDHIDnrRKQEYIYRYFGWEPPEFIHWGRLKIDDVRALSTSSARKGILR-GEYSGWD 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 427 DPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLK-KEVIPVHVPGAQEEMKev 505
Cdd:TIGR00463 349 DPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIIDEEARRYFFIWNpVKIEIVGLPEPKRVER-- 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 506 AKHPKNPDVGLKPVWYSPRVFIEGADAETLSegEMVTFINWGNLNITKIHknangkivSLDAKLNLENKDYKKTTKITWL 585
Cdd:TIGR00463 427 PLHPDHPEIGERVLILRGEIYVPKDDLEEGV--EPVRLMDAVNVIYSKKE--------LRYHSEGLEGARKLGKSIIHWL 496
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940746979 586 AETAhalPIPAICVTYEHLITKPVLGKDEDFkqyvnknskheelmlgdpclkdLKKGDIIQLQRRGFFICDQPYEP 661
Cdd:TIGR00463 497 PAKD---AVKVKVIMPDASIVEGVIEADASE----------------------LEVGDVVQFERFGFARLDSADKD 547
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
197-481 |
1.11e-100 |
|
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: 321.89 E-value: 1.11e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 197 KVTVRFPPEASGF-----------------KFMAETH-----TDYVLGNGK---VILEDVAMLHIEPDQFTYTSDHFETI 251
Cdd:cd00807 1 KVVTRFPPEPNGYlhighakaillnfgyakKYGGRCNlrfddTNPEKEEEEyvdSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 252 MKYAEKLIQEGKAYVddtpaermkaereqrteskhrnnsveknlqmweemkkgspfgqscclrakidmnsnngcmrdptl 331
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 332 yrckiqpHPRTGNRYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKR 411
Cdd:cd00807 96 -------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKR 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 412 KLTWFVDEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPR 481
Cdd:cd00807 169 KLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
1002-1380 |
1.68e-77 |
|
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: 268.18 E-value: 1.68e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1002 WYSQVITKSEMIEYYdVSGCYILRPWAFSIWESIKDFFDAEIKKLGVENCYFPMFVSQSaLEKEKTHVADFAPEVAWVtr 1081
Cdd:COG0442 21 WSHQLMLRAGLIRKL-ASGIYTYLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQPAE-LWEESGRWEGFGPELARV-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1082 sgKTELAEPIAVRPTSETVMYPAYAKWVQSHRDLPIRLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATFEEAAAEV 1161
Cdd:COG0442 97 --TDRLEREFCLGPTHEEVITDLVRNEIKSYRDLPLLLYQIQTKFRDEIRPRFGLLRTREFLMKDAYSFHATEEELDEEY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1162 LQILDLYAQVYEElLAIPVVKGRKT-------EKEKFA--------------GGDYTTTVEA------------------ 1202
Cdd:COG0442 175 QKMLDAYERIFER-LGLPVRAVEADsgaiggsESHEFMvladsgedtivycdACDYAANIEKaealappaeraeptkele 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1203 ------------------------------------------------------------------------------FI 1204
Cdd:COG0442 254 avatpgaktieevaeflgvpaektvktlvykadgelvavlvrgdhelneiklenllgaselelateeeieaalgavpgFL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1205 SASG----------------------------------------------------------------RAIQGATSHHLG 1220
Cdd:COG0442 334 GPVGlgvpyiadrsvagmsnfvcganeddyhytnvnwgrdfpvdevadlrnvvegdpcpdcggllqdgRGIEVGHIFKLG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1221 QNFSKMFEIIFEDPKtpGEKQFAYQNSWGLT-TRTIGVMTMVHGDNMGLVLPPRVACVQVVVIPCGITNalseedrDALI 1299
Cdd:COG0442 414 TKYSKAMDATFLDEN--GKEQPVWMGCYGIGvTRLIAAAIEQHHDDKGIIWPPAIAPFQVVIVPINMKD-------EAVL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1300 AKCNDYRRRLLSVNIRARADLRDNySPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVTENEAETKLKAL 1379
Cdd:COG0442 485 EAAEELYAELKAAGIDVLLDDRDE-RPGVKFADAELIGIPLRIVIGPRDLEEGQVEVKRRDTGEKEEVPLDELVETVKEL 563
|
.
gi 940746979 1380 L 1380
Cdd:COG0442 564 L 564
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
196-458 |
2.52e-39 |
|
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: 153.41 E-value: 2.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 196 GKVTVRFPPEASGF---------------------KFM-------AETHT-DYVlgngKVILEDVAMLHIEPDQ-FTYTS 245
Cdd:COG0008 3 MKVRTRFAPSPTGYlhighartalfnwlfarkyggKFIlriedtdPERSTeEAV----DAILEDLRWLGLDWDEgPYYQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 246 DHFETIMKYAEKLIQEGKAYVDDTPAERMKAEREQRTESK--------HRNNSVEKNLQMWEEmkkgspfGQSCCLRAKI 317
Cdd:COG0008 79 DRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGkpprydgrCRDLSPEELERMLAA-------GEPPVLRFKI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 318 --------DMNS-----NNGCMRDPTLYRckiqphpRTGnrynvYPTYDFACPIVDSIEGVTHALRT------TEYHDrd 378
Cdd:COG0008 152 peegvvfdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGeehlsnTPRQI-- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 379 eqfyWIIEALGIRKPyiwEYSRLNL----NNTVLSKRKltwfvdeGLVdgwddprfpTVRGVLRRGMTVEGLKQFIAAQG 454
Cdd:COG0008 218 ----WLYEALGWEPP---EFAHLPLilgpDGTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLG 274
|
....
gi 940746979 455 SSRS 458
Cdd:COG0008 275 WSKS 278
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
728-777 |
4.65e-25 |
|
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 98.85 E-value: 4.65e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 940746979 728 LYNKVAAQGDVVRELKAKKAAKEDVDAAVKQLLALKAEYKEKTGQEYKPG 777
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
728-780 |
2.14e-24 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 97.18 E-value: 2.14e-24
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 940746979 728 LYNKVAAQGDVVRELKAKKAAKEDVDAAVKQLLALKAEYKEKTGQEYKPGSPP 780
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 ... |
729-784 |
1.30e-22 |
|
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.
Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 92.02 E-value: 1.30e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 940746979 729 YNKVAAQGDVVRELKAKKAAKEDVDAAVKQLLALKAEYKEKTGQEYKPGSPPAAAA 784
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGDTP 56
|
|
| ProRS-C_1 |
pfam09180 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
1405-1487 |
1.42e-22 |
|
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.
Pssm-ID: 462709 Cd Length: 67 Bit Score: 92.58 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1405 MEDFQKLLDSGKIVQIPFCGEIDCEDWIKKTTardqdlepgapsmGAKSLCIPFKplcELQPGARCVCGKNPAKYYTLFG 1484
Cdd:pfam09180 1 WEEFKEALEEKGFVLAPWCGDEECEDKIKEET-------------GATSRCIPFD---QEEEGGKCIVCGKPAKKWVLFA 64
|
...
gi 940746979 1485 RSY 1487
Cdd:pfam09180 65 RSY 67
|
|
| ProRS-C_1 |
smart00946 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
1405-1487 |
7.37e-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: 90.32 E-value: 7.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1405 MEDFQKLLDSGKIVQIPFCGEIDCEDWIKKTTardqdlepgapsmGAKSLCIPFKplcELQPGARCVCGKNPAKYYTLFG 1484
Cdd:smart00946 1 LEEFKKALEEGKFVLAPWCGDEECEEKIKEET-------------GATIRCIPFD---QDEEPGKCVVCGKPAKKWVLFA 64
|
...
gi 940746979 1485 RSY 1487
Cdd:smart00946 65 RSY 67
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
878-930 |
1.63e-21 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 89.09 E-value: 1.63e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 940746979 878 LFDQVASQGEVVRKLKAEKASKDQVDAAVQELLQRKAQYKSLTGVEYKPVSAT 930
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
878-926 |
1.55e-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: 1.55e-20
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 940746979 878 LFDQVASQGEVVRKLKAEKASKDQVDAAVQELLQRKAQYKSLTGVEYKP 926
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKP 49
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
879-932 |
2.50e-19 |
|
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.
Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 82.77 E-value: 2.50e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 940746979 879 FDQVASQGEVVRKLKAEKASKDQVDAAVQELLQRKAQYKSLTGVEYKPVSATGA 932
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGD 54
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
801-845 |
1.03e-18 |
|
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: 80.74 E-value: 1.03e-18
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 940746979 801 LYDEVAAQGEVVRKLKAEKAPKAKVNEAVECLLSLKAQYKEKTGQ 845
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQ 45
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
801-853 |
4.85e-17 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 76.38 E-value: 4.85e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 940746979 801 LYDEVAAQGEVVRKLKAEKAPKAKVNEAVECLLSLKAQYKEKTGQNTCLGQPP 853
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 ... |
802-857 |
3.07e-16 |
|
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: 73.92 E-value: 3.07e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 940746979 802 YDEVAAQGEVVRKLKAEKAPKAKVNEAVECLLSLKAQYKEKTGQNTCLGQPPSLTA 857
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGDTP 56
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
1219-1380 |
1.03e-07 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 56.63 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1219 LGQNFSKMFEIIFEDPKtpGEKQFAYQNSWGlttrtIGVMTMV------HGDNMGLVLPPRVACVQVVVIPcgiTNALSE 1292
Cdd:PRK09194 412 LGTKYSEAMNATVLDEN--GKAQPLIMGCYG-----IGVSRLVaaaieqNHDEKGIIWPKAIAPFDVHIVP---VNMKDE 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1293 EDRDA---LIAKcndyrrrLLSVNIRARADLRDNySPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVTE 1369
Cdd:PRK09194 482 EVKELaekLYAE-------LQAAGIEVLLDDRKE-RPGVKFADADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPV 553
|
170
....*....|.
gi 940746979 1370 NEAETKLKALL 1380
Cdd:PRK09194 554 DELVEFLKALK 564
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
731-786 |
3.23e-06 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 51.67 E-value: 3.23e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 940746979 731 KVAAQGDVVRELKAKKAAKEDVDAAVKQLLALK--AEYKEKTGQEYKPGSPPAAAAQA 786
Cdd:PLN02734 15 AVTAQGNAVRALKASKADKAEIDAAIEKLKALKleKSALEKELQAAVGAGGDGAASKE 72
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
878-932 |
2.24e-04 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 45.89 E-value: 2.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 940746979 878 LFDQVASQGEVVRKLKAEKASKDQVDAAVQELLQRKAQYKSLTGVEYKPVSATGA 932
Cdd:PLN02734 12 KQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELQAAVGAGGD 66
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
803-836 |
2.70e-03 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 42.42 E-value: 2.70e-03
10 20 30
....*....|....*....|....*....|....
gi 940746979 803 DEVAAQGEVVRKLKAEKAPKAKVNEAVECLLSLK 836
Cdd:PLN02734 14 AAVTAQGNAVRALKASKADKAEIDAAIEKLKALK 47
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
13-686 |
0e+00 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 748.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 13 PPLGALLAVEHVKDNVSIF--VEEGKENILRVSENVVFTDINSILRYLARVAMTARLYGSNLMEHTEIDHWLEFSATkLS 90
Cdd:PLN02907 12 PPLAVIAAAKVAGVPLTIDpsLKSGSAPTLLFSSGEKLTGTNVLLRYIARSASLPGFYGQDAFESSQVDEWLDYAPT-FS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 91 SCDLFPSAINELNHCLSLRTYLVGNSLSLADLCVWATLKGNVAWQEQLQQNRAPVHVKRWFGFLEAQQAFQSVGTKWNVS 170
Cdd:PLN02907 91 SGSEFENACEYVDGYLASRTFLVGYSLTIADIAIWSGLAGSGQRWESLRKSKKYQNLVRWFNSISAEYSDILNEVTAAYV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 171 ATKAKG---APQKKPDV------------GKF-VELPGAEMGKVTVRFPPEASGF------------KFMAETHtdyvlg 222
Cdd:PLN02907 171 GKRGAGkpaAAKSKEKVadagkadgakdkGSFeVDLPGAEEGKVCTRFPPEPSGYlhighakaallnQYFARRY------ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 223 NGKVI-------------------LEDVAMLHIEPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAERMKAEREQRTE 283
Cdd:PLN02907 245 KGKLIvrfddtnpskesdefveniLKDIETLGIKYDAVTYTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMDGIE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 284 SKHRNNSVEKNLQMWEEMKKGSPFGQSCCLRAKIDMNSNNGCMRDPTLYRCKIQPHPRTGNRYNVYPTYDFACPIVDSIE 363
Cdd:PLN02907 325 SKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDMQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 364 GVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVDEGLVDGWDDPRFPTVRGVLRRGMTV 443
Cdd:PLN02907 405 GVTHALRSSEYHDRNAQYYRILEDMGLRKVHIWEFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKI 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 444 EGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLKKEVIPVHV---PgAQEEMKEVAKHPKNPDVGLKPVW 520
Cdd:PLN02907 485 EALKQFILSQGASKNLNLMEWDKLWTINKKIIDPVCPRHTAVLKEGRVLLTLtdgP-ETPFVRIIPRHKKYEGAGKKATT 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 521 YSPRVFIEGADAETLSEGEMVTFINWGNLNITKIHKNANGKIVSLDAKLNLENkDYKKTT-KITWLAETAHALPIPaiCV 599
Cdd:PLN02907 564 FTNRIWLDYADAEAISEGEEVTLMDWGNAIIKEITKDEGGAVTALSGELHLEG-SVKTTKlKLTWLPDTNELVPLS--LV 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 600 TYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDQPYEPVSphscreAPCVLIYIPD 679
Cdd:PLN02907 641 EFDYLITKKKLEEDDNFLDVLNPCTKKETAALGDSNMRNLKRGEIIQLERKGYYRCDAPFVRSS------KPIVLFAIPD 714
|
....*..
gi 940746979 680 GHTKEMP 686
Cdd:PLN02907 715 GRQQKSG 721
|
|
| proS_fam_I |
TIGR00408 |
prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ... |
993-1487 |
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: 559.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 993 AKKEENLADWYSQVITKSEMIEYYDVSGCYILRPWAFSIWESIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKTHVADF 1072
Cdd:TIGR00408 2 ASKMQDFSEWYHQILEKAEIIDYYPVKGCYVWLPYGFKIWKNIQKILRNILDEIGHEEVYFPMLIPESELAKEKDHIKGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1073 APEVAWVTRSGKTELAEPIAVRPTSETVMYPAYAKWVQSHRDLPIRLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFA 1152
Cdd:TIGR00408 82 EPEVYWITHGGLSKLDEPLALRPTSETAMYPMFKKWVKSYTDLPLKINQWVNVFRYETKHTRPFLRTREFTWQEAHTAHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1153 TFEEAAAEVLQILDLYAQVYEELLAIPVVKGRKTEKEKFAGGDYTTTVEAFISaSGRAIQGATSHHLGQNFSKMFEIIFE 1232
Cdd:TIGR00408 162 TAEEAEEQVLRALDIYKEFIENSLAIPYFVGRKPEWEKFAGAEYTWAFETIMP-DGRTLQIATSHNLGQNFAKTFEIKFE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1233 DPKtpGEKQFAYQNSWGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVVIPCgitnALSEEDRDALIAKCNDYRRRLLSV 1312
Cdd:TIGR00408 241 TPT--GDKEYAYQTSYGISTRVIGALIAIHSDEKGLVLPPRVAPIQVVIIPI----IFKKKENEKVMEAAREVRSRLKKA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1313 NIRARADLRDNySPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVTENEAETKLKALLEDIHANLFRKAS 1392
Cdd:TIGR00408 315 GFRVHIDDRDN-RPGRKFYQWEIKGIPLRIEVGPNDIEKNIAVISRRDTGEKYQVSLDQLEERVVELLNNIQENLRNRAW 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1393 EDLKTHMVVANSMEDFQKLL-DSGKIVQIPFCGEIDCEDWIKKTTArdqdlepgapsmgAKSLCIPFKPlcelQPGARCV 1471
Cdd:TIGR00408 394 ERFEQKIVIVETLEEIKQALnEKRGVVLVPWCGEEECEEDLKEKVQ-------------VTILCIPEDG----DVLQLCI 456
|
490
....*....|....*.
gi 940746979 1472 CGKNPAKYYTLFGRSY 1487
Cdd:TIGR00408 457 FCGRKAPDYVLIARTY 472
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
190-685 |
8.04e-167 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 511.86 E-value: 8.04e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 190 LPGAEMGKVTVRFPPEASGFKFMAetHTDYVLGN--------GKV-------------------ILEDVAMLHIEPDQFT 242
Cdd:PLN03233 4 LEGAIAGQIVTRFPPEPSGYLHIG--HAKAALLNdyyarrykGRLilrfddtnpskekaefeesIIEDLGKIEIKPDSVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 243 YTSDHFETIMKYAEKLIQEGKAYVDDTPAERMKAEREQRTESKHRNNSVEKNLQMWEEMKKGSPFGQSCCLRAKIDMNSN 322
Cdd:PLN03233 82 FTSDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKERADRAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQSD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 323 NGCMRDPTLYRCKIQPHPRTGNRYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLN 402
Cdd:PLN03233 162 NGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARMN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 403 LNNTVLSKRKLTWFVDEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRY 482
Cdd:PLN03233 242 FMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 483 VALLKKEVIPVHVPGAQEE----MKEVAKHPKNPDVGLKPVWYSPRVFIEGADAETLSEGEMVTFINWGNLNITKIHKNA 558
Cdd:PLN03233 322 MAIDKADHTALTVTNADEEadfaFSETDCHPKDPGFGKRAMRICDEVLLEKADTEDIQLGEDIVLLRWGVIEISKIDGDL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 559 NGKIVSldaklnleNKDYKKTT-KITWLAETAHAlpIPAICVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLK 637
Cdd:PLN03233 402 EGHFIP--------DGDFKAAKkKISWIADVSDN--IPVVLSEFDNLIIKEKLEEDDKFEDFINPDTLAETDVIGDAGLK 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 940746979 638 DLKKGDIIQLQRRGFFICDQPYepVSPhscrEAPCVLIYIPDGHTKEM 685
Cdd:PLN03233 472 TLKEHDIIQLERRGFYRVDRPY--MGE----EKPLILFMIPDGKKKAM 513
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
998-1261 |
1.01e-160 |
|
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: 484.79 E-value: 1.01e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 998 NLADWYSQVITKSEMIEYYDVSGCYILRPWAFSIWESIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKTHVADFAPEVA 1077
Cdd:cd00778 1 DFSEWYTEVITKAELIDYGPVKGCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPESELEKEKEHIEGFAPEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1078 WVTRSGKTELAEPIAVRPTSETVMYPAYAKWVQSHRDLPIRLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATFEEA 1157
Cdd:cd00778 81 WVTHGGLEELEEPLALRPTSETAIYPMFSKWIRSYRDLPLKINQWVNVFRWETKTTRPFLRTREFLWQEGHTAHATEEEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1158 AAEVLQILDLYAQVYEELLAIPVVKGRKTEKEKFAGGDYTTTVEAFISaSGRAIQGATSHHLGQNFSKMFEIIFEDPKtp 1237
Cdd:cd00778 161 EEEVLQILDLYKEFYEDLLAIPVVKGRKTEWEKFAGADYTYTIEAMMP-DGRALQSGTSHNLGQNFSKAFDIKYQDKD-- 237
|
250 260
....*....|....*....|....
gi 940746979 1238 GEKQFAYQNSWGLTTRTIGVMTMV 1261
Cdd:cd00778 238 GQKEYVHQTSWGISTRLIGAIIMI 261
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
177-758 |
1.63e-155 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 484.85 E-value: 1.63e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 177 APQKKPDVGKfVELPGAEMGKVTVRFPPEASGFKFMAetHTDYVLGN--------GKV-------------------ILE 229
Cdd:PTZ00402 33 AANANEENDK-LQLTNAEEGKVVTRFPPEASGFLHIG--HAKAALINsmladkykGKLvfrfddtnpskekehfeqaILD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 230 DVAMLHIEPDQF-TYTSDHFETIMKYAEKLIQEGKAYVDDTPAERMKAEREQRTESKHRNNSVEKNLQMWEEMKKGSPFG 308
Cdd:PTZ00402 110 DLATLGVSWDVGpTYSSDYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFDGVPTKYRDISVEETKRLWNEMKKGSAEG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 309 QSCCLRAKIDMNSNNGCMRDPTLYRCKIQPHPRTGNRYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEAL 388
Cdd:PTZ00402 190 QETCLRAKISVDNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDAL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 389 GIRKPYIWEYSRLNLNNTVLSKRKLTWFVDEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIW 468
Cdd:PTZ00402 270 GIRKPIVEDFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLW 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 469 AFNKKVIDPVAPRYVALLKKEVIPVHVPGaQEEMKEVAK--HPKNPDVGLKPVWYSPRVFIEGADAETLSEGEMVTFINW 546
Cdd:PTZ00402 350 YFNTQILDPSVPRYTVVSNTLKVRCTVEG-QIHLEACEKllHKKVPDMGEKTYYKSDVIFLDAEDVALLKEGDEVTLMDW 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 547 GNLNITKIHK-NANGKIVSLDAKLNLENkDYKKTT-KITWLAETAHALPIPaiCVTYEHLITKPVLGKDEDFKQYVNKNS 624
Cdd:PTZ00402 429 GNAYIKNIRRsGEDALITDADIVLHLEG-DVKKTKfKLTWVPESPKAEVME--LNEYDHLLTKKKPDPEESIDDIIAPVT 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 625 KHEELMLGDPCLKDLKKGDIIQLQRRGFFICDQPyepvsphscrEAPCVLIYIPDGHTKEMPTSGskektKVETLKnetT 704
Cdd:PTZ00402 506 KYTQEVYGEEALSVLKKGDIIQLERRGYYIVDDV----------TPKKVLIAIPDGREKVNHLSA-----KAQYLK---T 567
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 940746979 705 TPVKERPAApltntsaasegpvvlynkvaaqgdvVRELKAKKAAKEDVDAAVKQ 758
Cdd:PTZ00402 568 LPKKGIASA-------------------------ANDLAAKRAAKAAKKAAQKQ 596
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
197-477 |
3.13e-120 |
|
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: 378.59 E-value: 3.13e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 197 KVTVRFPPEASG-----------FKFM-AETH----------TD---YVLGNGKVILEDVAMLHIEPD-QFTYTSDHFET 250
Cdd:pfam00749 1 KVRTRFAPSPTGylhighakaalFNYLyAKNHngkfilrfedTDperETPEFEESILEDLKWLGIKWDyGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 251 IMKYAEKLIQEGKAYVDDTPAERMKAEREQ--RTESKHRNNSVEKNLQMW-EEMKKGSPFGQSCCLRAKIDMNSnNGCMR 327
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEqeALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMES-PYVFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 328 DPTLYRCKIQP---HPRTGNRYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIR-KPYIWEYSRLNL 403
Cdd:pfam00749 160 DPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 940746979 404 NNTVLSKRKLTWFVDEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSV-VNMEWDKIWAFNKKVIDP 477
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFdVNRLSKSLEAFDRKKLDW 314
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
141-661 |
3.43e-115 |
|
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: 374.16 E-value: 3.43e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 141 NRAPVHVKRWFGFLEAQQAFQSVGTKWNVSATKAK-----GAPQKKPDVGKFVELPGAEMGKVTVRFPPEASGFKFMAet 215
Cdd:TIGR00463 32 NNPELRKKAKEVLEAVEAAVEEVNSLSPEEQKELMkrlglDIKKKEKKRKGLRELPGAKMGEVVMRFAPNPSGPLHIG-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 216 HTDYVLGN--------GKVIL-------------------EDVAMLHIEPDQFTYTSDHFETIMKYAEKLIQEGKAYVDD 268
Cdd:TIGR00463 110 HARAAILNheyakkydGKLIIrfddtdprrvdpeaydmilEDLEWLGVKWDEVVYQSDRIETYYDYTRKLIEMGKAYVCD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 269 TPAERMKAEREQRTESKHRNNSVEKNLQMWEEMKKGSPFGQSCCLRAKIDMNSNNGCMRDPTLYRCKIQPHPRTGNRYNV 348
Cdd:TIGR00463 190 CRPEEFRELRNRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 349 YPTYDFACPIVDSIEGVTHALRTTEYHD--RDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVDeGLVDGWD 426
Cdd:TIGR00463 270 YPTMDFSVAIDDHLLGVTHVLRGKDHIDnrRKQEYIYRYFGWEPPEFIHWGRLKIDDVRALSTSSARKGILR-GEYSGWD 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 427 DPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLK-KEVIPVHVPGAQEEMKev 505
Cdd:TIGR00463 349 DPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIIDEEARRYFFIWNpVKIEIVGLPEPKRVER-- 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 506 AKHPKNPDVGLKPVWYSPRVFIEGADAETLSegEMVTFINWGNLNITKIHknangkivSLDAKLNLENKDYKKTTKITWL 585
Cdd:TIGR00463 427 PLHPDHPEIGERVLILRGEIYVPKDDLEEGV--EPVRLMDAVNVIYSKKE--------LRYHSEGLEGARKLGKSIIHWL 496
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940746979 586 AETAhalPIPAICVTYEHLITKPVLGKDEDFkqyvnknskheelmlgdpclkdLKKGDIIQLQRRGFFICDQPYEP 661
Cdd:TIGR00463 497 PAKD---AVKVKVIMPDASIVEGVIEADASE----------------------LEVGDVVQFERFGFARLDSADKD 547
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
196-661 |
2.92e-109 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 357.88 E-value: 2.92e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 196 GKVTVRFPPEASGF-----------------KFMAETH------------TDYVlgngKVILEDVAMLHIEP-DQFTYTS 245
Cdd:PRK05347 28 TRVHTRFPPEPNGYlhighaksiclnfglaqDYGGKCNlrfddtnpekedQEYV----DSIKEDVRWLGFDWsGELRYAS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 246 DHFETIMKYAEKLIQEGKAYVDDTPAERMkaeREQR-------TESKHRNNSVEKNLQMWEEMKKGS-PFGqSCCLRAKI 317
Cdd:PRK05347 104 DYFDQLYEYAVELIKKGKAYVDDLSAEEI---REYRgtltepgKNSPYRDRSVEENLDLFERMRAGEfPEG-SAVLRAKI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 318 DMNSNNGCMRDPTLYRCKIQPHPRTGNRYNVYPTYDFACPIVDSIEGVTHALRTTEYHD-RdeQFY-WIIEALGIR-KPY 394
Cdd:PRK05347 180 DMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDhR--PLYdWVLDNLPIPpHPR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 395 IWEYSRLNLNNTVLSKRKLTWFVDEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSR--SVVNM---EwdkiwA 469
Cdd:PRK05347 258 QYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKqdSVIDMsmlE-----S 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 470 FNKKVIDPVAPRYVALLKkeviPVHV-----PGAQEEMKEVAKHPKNPDVGLKPVWYSPRVFIEGAD-AET-------LS 536
Cdd:PRK05347 333 CIREDLNENAPRAMAVLD----PLKLvitnyPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDfMEEppkkyfrLV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 537 EGEMVTFINWGNLNITKIHKNANGKIVSL------DAKLNLENKDYK-KTTkITWLaETAHAlpIPAICVTYEHLITKPV 609
Cdd:PRK05347 409 PGKEVRLRNAYVIKCEEVVKDADGNITEIhctydpDTLSGNPADGRKvKGT-IHWV-SAAHA--VPAEVRLYDRLFTVPN 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 940746979 610 LGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDQPYEP 661
Cdd:PRK05347 485 PAAGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCADKDSTP 536
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
197-481 |
1.11e-100 |
|
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: 321.89 E-value: 1.11e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 197 KVTVRFPPEASGF-----------------KFMAETH-----TDYVLGNGK---VILEDVAMLHIEPDQFTYTSDHFETI 251
Cdd:cd00807 1 KVVTRFPPEPNGYlhighakaillnfgyakKYGGRCNlrfddTNPEKEEEEyvdSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 252 MKYAEKLIQEGKAYVddtpaermkaereqrteskhrnnsveknlqmweemkkgspfgqscclrakidmnsnngcmrdptl 331
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 332 yrckiqpHPRTGNRYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKR 411
Cdd:cd00807 96 -------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKR 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 412 KLTWFVDEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPR 481
Cdd:cd00807 169 KLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
1267-1487 |
1.69e-85 |
|
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: 277.64 E-value: 1.69e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1267 GLVLPPRVACVQVVVIPCGITnalsEEDRDALIAKCNDYRRRLLSVNIRARADLRDNYSPGWKFNHWELKGVPIRLEVGP 1346
Cdd:cd00862 1 GLVLPPRVAPIQVVIVPIGIK----DEKREEVLEAADELAERLKAAGIRVHVDDRDNYTPGWKFNDWELKGVPLRIEIGP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1347 RDMKSCQFVAVRRDTGEKLTVTENEAETKLKALLEDIHANLFRKASEDLK-THMVVanSMEDFQKLLDSGKIVQIPFCGE 1425
Cdd:cd00862 77 RDLEKNTVVIVRRDTGEKKTVPLAELVEKVPELLDEIQEDLYERALEFRDaTRIVD--TWEEFKEALNEKGIVLAPWCGE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 940746979 1426 IDCEDWIKKTTArdqdlepgapsmgAKSLCIPFkPLCELQPGARCV-CGkNPAKYYTLFGRSY 1487
Cdd:cd00862 155 EECEEEIKEETA-------------ATILCIPF-DEAKLEEGGKCVvCG-RPAKAYARFAKSY 202
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
227-656 |
4.24e-84 |
|
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: 286.05 E-value: 4.24e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 227 ILEDVAMLHIEPD-QFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAERMKAEREQRTE----SKHRNNSVEKNLQMWEEM 301
Cdd:TIGR00440 55 IKRDVEWLGFKWEgKIRYSSDYFDELYRYAEELIKKGLAYVDELTPEEIREYRGTLTDpgknSPYRDRSIEENLALFEKM 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 302 KKGSPFGQSCCLRAKIDMNSNNGCMRDPTLYRCKIQPHPRTGNRYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQF 381
Cdd:TIGR00440 135 RDGKFKEGKAILRAKIDMASPFPVMRDPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLY 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 382 YWIIEALGI-RKPYIWEYSRLNLNNTVLSKRKLTWFVDEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVV 460
Cdd:TIGR00440 215 DWVLDNIHIfPRPAQYEFSRLNLEGTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDN 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 461 NMEWDKIWAFNKKVIDPVAPRYVALLKKEVIPVHVPGAQEEMKEVAKHPKNPDVGLKPVWYSPRVFIEGADAET------ 534
Cdd:TIGR00440 295 NIEVVRLESCIREDLNENAPRAMAVIDPVEVVIENLSDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREeankqy 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 535 --LSEGEMVTFINWGNLNITKIHKNANGKIVSL----DAK-LNLENKDYKKT-TKITWLAeTAHALPIPAicVTYEHLIT 606
Cdd:TIGR00440 375 krLVLGKEVRLRNAYVIKAERVEKDAAGKITTIfctyDNKtLGKEPADGRKVkGVIHWVS-ASSKYPTET--RLYDRLFK 451
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 940746979 607 KPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICD 656
Cdd:TIGR00440 452 VPNPGAPDDFLSVINPESLVIKQGFMEHSLGDAVANKRFQFEREGYFCLD 501
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
196-721 |
1.28e-81 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 286.23 E-value: 1.28e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 196 GKVTVRFPPEASGF-----------------KFMAETH------------TDYVlgngKVILEDVAMLHIE-PDQFTYTS 245
Cdd:PRK14703 30 PRVVTRFPPEPNGYlhighaksillnfgiarDYGGRCHlrmddtnpetedTEYV----EAIKDDVRWLGFDwGEHLYYAS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 246 DHFETIMKYAEKLIQEGKAYVDDTPAERMkaeREQR-------TESKHRNNSVEKNLQMWEEMKKGS-PFGQSCcLRAKI 317
Cdd:PRK14703 106 DYFERMYAYAEQLIKMGLAYVDSVSEEEI---RELRgtvtepgTPSPYRDRSVEENLDLFRRMRAGEfPDGAHV-LRAKI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 318 DMNSNNGCMRDPTLYRCKIQPHPRTGNRYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIR--KPYI 395
Cdd:PRK14703 182 DMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPWppRPRQ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 396 WEYSRLNLNNTVLSKRKLTWFVDEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVI 475
Cdd:PRK14703 262 YEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGVLEFAIRDDL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 476 DPVAPRYVALLKK-EVIPVHVPGAQEEMKEVAKHPKN-PDVGLKPVWYSPRVFIEGAD-AET-------LSEGEMVTFIN 545
Cdd:PRK14703 342 NRRAPRVMAVLDPlKVVIENLPAGKVEELDLPYWPHDvPKEGSRKVPFTRELYIERDDfSEDppkgfkrLTPGREVRLRG 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 546 WGNLNITKIHKNANGKIVSLDAKLNLENKDYKKTTK-----ITWLAeTAHALPIPAicVTYEHLITKPVL-GKDEDFKQY 619
Cdd:PRK14703 422 AYIIRCDEVVRDADGAVTELRCTYDPESAKGEDTGRkaagvIHWVS-AKHALPAEV--RLYDRLFKVPQPeAADEDFLEF 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 620 VNKNSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDqpyePVSphSCREAPCV--LIYIPD--GHTKEMPTSGSKEKTK 695
Cdd:PRK14703 499 LNPDSLRVAQGRVEPAVRDDPADTRYQFERQGYFWAD----PVD--SRPDALVFnrIITLKDtwGARAREAAREKRAAAP 572
|
570 580
....*....|....*....|....*.
gi 940746979 696 VETLKNETTTPVKERPAAPLTNTSAA 721
Cdd:PRK14703 573 KKTAKPRRSKAEARAEAAALNPEQRA 598
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
196-661 |
1.81e-80 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 277.25 E-value: 1.81e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 196 GKVTVRFPPEASGF------KFMAETHTDYVLGNGK-------------------VILEDVAMLHIEPDQFTYTSDHFET 250
Cdd:PTZ00437 50 GKPYFRFPPEPNGFlhighaKSMNLNFGSARAHGGKcylryddtnpeteeqvyidAIMEMVKWMGWKPDWVTFSSDYFDQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 251 IMKYAEKLIQEGKAYVDDTPAERMKAEREQRTESKHRNNSVEKNLQMWEEMKKGSPFGQSCCLRAKIDMNSNNGCMRDPT 330
Cdd:PTZ00437 130 LHEFAVQLIKDGKAYVDHSTPDELKQQREQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRDFI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 331 LYRCKIQPHPRTGNRYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSK 410
Cdd:PTZ00437 210 AYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWRPHVWEFSRLNVTGSLLSK 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 411 RKLTWFVDEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLkkEV 490
Cdd:PTZ00437 290 RKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVI--DP 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 491 IPVHVPGAQEEMK-EVAKHPKNPDVGLKPVWYSPRVFIEGADAET---------LSEGEMVTFINW-GNLNITKIHKNAN 559
Cdd:PTZ00437 368 IKVVVDNWKGEREfECPNHPRKPELGSRKVMFTDTFYVDRSDFRTednnskfygLAPGPRVVGLKYsGNVVCKGFEVDAA 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 560 GKIVSLDAKLNLENKDyKKTTKITWLAETAhalPIPAICVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDL 639
Cdd:PTZ00437 448 GQPSVIHVDIDFERKD-KPKTNISWVSATA---CTPVEVRLYNALLKDDRAAIDPEFLKFIDEDSEVVSHGYAEKGIENA 523
|
490 500
....*....|....*....|..
gi 940746979 640 KKGDIIQLQRRGFFICDQPYEP 661
Cdd:PTZ00437 524 KHFESVQAERFGYFVVDPDTRP 545
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
1002-1380 |
1.68e-77 |
|
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: 268.18 E-value: 1.68e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1002 WYSQVITKSEMIEYYdVSGCYILRPWAFSIWESIKDFFDAEIKKLGVENCYFPMFVSQSaLEKEKTHVADFAPEVAWVtr 1081
Cdd:COG0442 21 WSHQLMLRAGLIRKL-ASGIYTYLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQPAE-LWEESGRWEGFGPELARV-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1082 sgKTELAEPIAVRPTSETVMYPAYAKWVQSHRDLPIRLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATFEEAAAEV 1161
Cdd:COG0442 97 --TDRLEREFCLGPTHEEVITDLVRNEIKSYRDLPLLLYQIQTKFRDEIRPRFGLLRTREFLMKDAYSFHATEEELDEEY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1162 LQILDLYAQVYEElLAIPVVKGRKT-------EKEKFA--------------GGDYTTTVEA------------------ 1202
Cdd:COG0442 175 QKMLDAYERIFER-LGLPVRAVEADsgaiggsESHEFMvladsgedtivycdACDYAANIEKaealappaeraeptkele 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1203 ------------------------------------------------------------------------------FI 1204
Cdd:COG0442 254 avatpgaktieevaeflgvpaektvktlvykadgelvavlvrgdhelneiklenllgaselelateeeieaalgavpgFL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1205 SASG----------------------------------------------------------------RAIQGATSHHLG 1220
Cdd:COG0442 334 GPVGlgvpyiadrsvagmsnfvcganeddyhytnvnwgrdfpvdevadlrnvvegdpcpdcggllqdgRGIEVGHIFKLG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1221 QNFSKMFEIIFEDPKtpGEKQFAYQNSWGLT-TRTIGVMTMVHGDNMGLVLPPRVACVQVVVIPCGITNalseedrDALI 1299
Cdd:COG0442 414 TKYSKAMDATFLDEN--GKEQPVWMGCYGIGvTRLIAAAIEQHHDDKGIIWPPAIAPFQVVIVPINMKD-------EAVL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1300 AKCNDYRRRLLSVNIRARADLRDNySPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVTENEAETKLKAL 1379
Cdd:COG0442 485 EAAEELYAELKAAGIDVLLDDRDE-RPGVKFADAELIGIPLRIVIGPRDLEEGQVEVKRRDTGEKEEVPLDELVETVKEL 563
|
.
gi 940746979 1380 L 1380
Cdd:COG0442 564 L 564
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
160-661 |
6.14e-77 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 272.79 E-value: 6.14e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 160 FQSVGTKWNVSATKAKGAPQKKpdvgkfvelpgAEMGKVTVRFPPEASGFKFMAETHTDYV-LG-----NGKVIL----- 228
Cdd:PLN02859 238 FFSDGSVLRPSNTKEILEKHLK-----------ATGGKVYTRFPPEPNGYLHIGHAKAMFVdFGlakerGGCCYLrfddt 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 229 --------------EDVAMLHIEPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAERMKAEREQRTESKHRNNSVEKN 294
Cdd:PLN02859 307 npeaekkeyidhieEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKKMNSPWRDRPIEES 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 295 LQMWEEMKKGS-PFGQSCcLRAKIDMNSNNGCMRDPTLYRCKIQPHPRTGNRYNVYPTYDFACPIVDSIEGVTHALRTTE 373
Cdd:PLN02859 387 LKLFEDMRRGLiEEGKAT-LRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 374 YHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVDEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQ 453
Cdd:PLN02859 466 FETRRASYYWLLDSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGI 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 454 GSSRS---VVNMewDKIWAFNKKVIDPVAPRYVALLK--KEVIPVHVPGAQEEMkEVAKHPKNPDVGLKP---VWYSPRV 525
Cdd:PLN02859 546 GITRSdnsLIRM--DRLEHHIREELNKTAPRTMVVLHplKVVITNLESGEVIEL-DAKRWPDAQNDDPSAfykVPFSRVV 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 526 FIEGADAET--------LSEGEMVTFINWGNLNITK-IHKNANGKIVSLDAKLnlenkDYKKTTK----ITWLAETAHAL 592
Cdd:PLN02859 623 YIERSDFRLkdskdyygLAPGKSVLLRYAFPIKCTDvVLADDNETVVEIRAEY-----DPEKKTKpkgvLHWVAEPSPGV 697
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 940746979 593 -PIPAICVTYEHLITKPVLGKDEDFKQYVNKNSKheELMLGD---PCLKDLKKGDIIQLQRRGFFICDQPYEP 661
Cdd:PLN02859 698 ePLKVEVRLFDKLFLSENPAELEDWLEDLNPQSK--EVISGAyavPSLKDAKVGDRFQFERLGYFAVDKDSTP 768
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
179-652 |
3.44e-76 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 264.41 E-value: 3.44e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 179 QKKPDVGKFVELPGAEMGKVTVRFPPEASG---------------FKFMaethtdYvlgNGKVIL--------------- 228
Cdd:PRK04156 83 EKKEEKKGLPPLPNAEKGKVVMRFAPNPSGplhlgharaailndeYAKM------Y---GGKFILrfedtdprtkrpdpe 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 229 ------EDVAMLHIEPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAERMKAEREQRTESKHRNNSVEKNLQMWEEMK 302
Cdd:PRK04156 154 aydmilEDLKWLGVKWDEVVIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELRDAGKPCPHRDKSPEENLELWEKML 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 303 KGSPFGQSCCLRAKIDMNSNNGCMRDPTLYRCKIQPHPRTGNRYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFY 382
Cdd:PRK04156 234 DGEYKEGEAVVRVKTDLEHPNPSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDNTEKQR 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 383 WIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVDEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNM 462
Cdd:PRK04156 314 YIYDYFGWEYPETIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATI 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 463 EWDKIWAFNKKVIDPVAPRYVALlkKEVIPVHVPGAQEEMKEVAKHPKNPDVGLKPVWYSPRVFIEGADAETLseGEMVT 542
Cdd:PRK04156 394 SWENLYAINRKLIDPIANRYFFV--RDPVELEIEGAEPLEAKIPLHPDRPERGEREIPVGGKVYVSSDDLEAE--GKMVR 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 543 FINWGNLNITKIHKNAnGKIVSLDAKLNLENKdykktTKIT-WLAETaHALPIPAIcvtyehlitKPVLGKDEDFkqyvn 621
Cdd:PRK04156 470 LMDLFNVEITGVSVDK-ARYHSDDLEEARKNK-----APIIqWVPED-ESVPVRVL---------KPDGGDIEGL----- 528
|
490 500 510
....*....|....*....|....*....|.
gi 940746979 622 knskheelmlGDPCLKDLKKGDIIQLQRRGF 652
Cdd:PRK04156 529 ----------AEPDVADLEVDDIVQFERFGF 549
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
998-1260 |
8.21e-68 |
|
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: 229.56 E-value: 8.21e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 998 NLADWYSQVITKSEMIEYYDVSGCYILRPWAFSIWESIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKTHVADFAPEVA 1077
Cdd:cd00772 1 DASEKSLEHIGKAELADQGPGRGIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGFSKELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1078 WVTRSGKTELAEPIAVRPTSETVMYPAYAKWVQSHRDLPIRLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATFEEA 1157
Cdd:cd00772 81 VFKDAGDEELEEDFALRPTLEENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIRPRFGFLRAREFIMKDGHSAHADAEEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1158 AAEVLQILDLYAQVYEELLAIPVVKGRKTEKEKFAGGDYTTTVEAfISASGRAIQGATSHHLGQNFSKMFEIIFEDPKTP 1237
Cdd:cd00772 161 DEEFLNMLSAYAEIARDLAAIDFIEGEADEGAKFAGASKSREFEA-LMEDGKAKQAETGHIFGEGFARAFDLKAKFLDKD 239
|
250 260
....*....|....*....|....
gi 940746979 1238 GEKQFAYQNSWGLT-TRTIGVMTM 1260
Cdd:cd00772 240 GKEKFFEMGCWGIGiSRFIGAIIE 263
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
479-656 |
1.61e-45 |
|
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: 162.06 E-value: 1.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 479 APRYVALLKKEVIPVH-VPGAQEEMKEVAKHPKNPDVGLKPVWYSPRVFIEGADAETLSEGEMVTFINWGNLNITKIHKN 557
Cdd:pfam03950 1 APRYMAVLDPVKVVIEnYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDFKRLAPGEEVRLMDAYNIKVTEVVKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 558 ANGKIVSLDAKLNLENKDY---KKTTKITWLAETAhalPIPAICVTYEHLITkpvlgKDEDFKQYVNKNSKHE-ELMLGD 633
Cdd:pfam03950 81 EDGNVTELHCTYDGDDLGGarkVKGKIIHWVSASD---AVPAEVRLYDRLFK-----DEDDADFLLNPDSLKVlTEGLAE 152
|
170 180
....*....|....*....|...
gi 940746979 634 PCLKDLKKGDIIQLQRRGFFICD 656
Cdd:pfam03950 153 PALANLKPGDIVQFERIGYFRVD 175
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
227-481 |
3.17e-42 |
|
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: 155.20 E-value: 3.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 227 ILEDVAMLHIEPDQFTYTSDHFETIMKYAEKLIQEGKAYVddtpaermkaereqrteskhrnnsveknlqmweemkkgsp 306
Cdd:cd09287 58 IPEDLEWLGVKWDEVVIASDRIELYYEYARKLIEMGGAYV---------------------------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 307 fgqscclrakidmnsnngcmrdptlyrckiqpHPRTGNRYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIE 386
Cdd:cd09287 98 --------------------------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 387 ALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVDEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDK 466
Cdd:cd09287 146 YFGWEYPETIHWGRLKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWEN 225
|
250
....*....|....*
gi 940746979 467 IWAFNKKVIDPVAPR 481
Cdd:cd09287 226 LYAINRKLIDPRANR 240
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
196-458 |
2.52e-39 |
|
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: 153.41 E-value: 2.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 196 GKVTVRFPPEASGF---------------------KFM-------AETHT-DYVlgngKVILEDVAMLHIEPDQ-FTYTS 245
Cdd:COG0008 3 MKVRTRFAPSPTGYlhighartalfnwlfarkyggKFIlriedtdPERSTeEAV----DAILEDLRWLGLDWDEgPYYQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 246 DHFETIMKYAEKLIQEGKAYVDDTPAERMKAEREQRTESK--------HRNNSVEKNLQMWEEmkkgspfGQSCCLRAKI 317
Cdd:COG0008 79 DRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGkpprydgrCRDLSPEELERMLAA-------GEPPVLRFKI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 318 --------DMNS-----NNGCMRDPTLYRckiqphpRTGnrynvYPTYDFACPIVDSIEGVTHALRT------TEYHDrd 378
Cdd:COG0008 152 peegvvfdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGeehlsnTPRQI-- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 379 eqfyWIIEALGIRKPyiwEYSRLNL----NNTVLSKRKltwfvdeGLVdgwddprfpTVRGVLRRGMTVEGLKQFIAAQG 454
Cdd:COG0008 218 ----WLYEALGWEPP---EFAHLPLilgpDGTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLG 274
|
....
gi 940746979 455 SSRS 458
Cdd:COG0008 275 WSKS 278
|
|
| GST_C_GluProRS_N |
cd10309 |
Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional ... |
74-157 |
2.99e-37 |
|
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: 134.75 E-value: 2.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 74 EHTEIDHWLEFSATKLSSCDLFPSAINELNHCLSLRTYLVGNSLSLADLCVWATLKGNVAWQEqlqQNRAPVHVKRWFGF 153
Cdd:cd10309 1 EQTEVDHWISFSAGRLSCDQDFSSALSYLDKALSLRTYLVGNSLTLADFAVWAALRGNGEWLA---SKEKYVNVTRWFKF 77
|
....
gi 940746979 154 LEAQ 157
Cdd:cd10309 78 ISSQ 81
|
|
| Gly_His_Pro_Ser_Thr_tRS_core |
cd00670 |
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic ... |
1031-1259 |
6.99e-27 |
|
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: 110.56 E-value: 6.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1031 IWESIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKtHVADFAPEVAWVTRSGKTELAEPIAVRPTSETVMYPAYAKWVQ 1110
Cdd:cd00670 4 LWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGG-HLDGYRKEMYTFEDKGRELRDTDLVLRPAACEPIYQIFSGEIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1111 SHRDLPIRLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSaFATFEEAAAEVLQILDLYAQVYEElLAIPVVKGRKTEKEK 1190
Cdd:cd00670 83 SYRALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVEYVV-FGEPEEAEEERREWLELAEEIARE-LGLPVRVVVADDPFF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 940746979 1191 FAGGD--------YTTTVEAFISASGRAIQGATSHHLGQNFSkmFEIIFEDPKTPGEKQFAYQNSWGLTTRTIGVMT 1259
Cdd:cd00670 161 GRGGKrgldagreTVVEFELLLPLPGRAKETAVGSANVHLDH--FGASFKIDEDGGGRAHTGCGGAGGEERLVLALL 235
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
728-777 |
4.65e-25 |
|
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 98.85 E-value: 4.65e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 940746979 728 LYNKVAAQGDVVRELKAKKAAKEDVDAAVKQLLALKAEYKEKTGQEYKPG 777
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
728-780 |
2.14e-24 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 97.18 E-value: 2.14e-24
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 940746979 728 LYNKVAAQGDVVRELKAKKAAKEDVDAAVKQLLALKAEYKEKTGQEYKPGSPP 780
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 ... |
729-784 |
1.30e-22 |
|
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.
Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 92.02 E-value: 1.30e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 940746979 729 YNKVAAQGDVVRELKAKKAAKEDVDAAVKQLLALKAEYKEKTGQEYKPGSPPAAAA 784
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGDTP 56
|
|
| ProRS-C_1 |
pfam09180 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
1405-1487 |
1.42e-22 |
|
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.
Pssm-ID: 462709 Cd Length: 67 Bit Score: 92.58 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1405 MEDFQKLLDSGKIVQIPFCGEIDCEDWIKKTTardqdlepgapsmGAKSLCIPFKplcELQPGARCVCGKNPAKYYTLFG 1484
Cdd:pfam09180 1 WEEFKEALEEKGFVLAPWCGDEECEDKIKEET-------------GATSRCIPFD---QEEEGGKCIVCGKPAKKWVLFA 64
|
...
gi 940746979 1485 RSY 1487
Cdd:pfam09180 65 RSY 67
|
|
| ProRS-C_1 |
smart00946 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
1405-1487 |
7.37e-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: 90.32 E-value: 7.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1405 MEDFQKLLDSGKIVQIPFCGEIDCEDWIKKTTardqdlepgapsmGAKSLCIPFKplcELQPGARCVCGKNPAKYYTLFG 1484
Cdd:smart00946 1 LEEFKKALEEGKFVLAPWCGDEECEEKIKEET-------------GATIRCIPFD---QDEEPGKCVVCGKPAKKWVLFA 64
|
...
gi 940746979 1485 RSY 1487
Cdd:smart00946 65 RSY 67
|
|
| GST_C_AaRS_like |
cd10289 |
Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA ... |
74-157 |
1.39e-21 |
|
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: 90.06 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 74 EHTEIDHWLEFsATKLSSCDLFPSAINELNHCLSLRTYLVGNSLSLADLCVWATLKGNVAWQEQLQQNRaPVHVKRWFGF 153
Cdd:cd10289 1 EAAQVDQWLDL-AGSLLKGKELEALLKSLNSYLASRTFLVGYSLTLADVAVFSALYPSGQKLSDKEKKK-FPHVTRWFNH 78
|
....
gi 940746979 154 LEAQ 157
Cdd:cd10289 79 IQNL 82
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
878-930 |
1.63e-21 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 89.09 E-value: 1.63e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 940746979 878 LFDQVASQGEVVRKLKAEKASKDQVDAAVQELLQRKAQYKSLTGVEYKPVSAT 930
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
1278-1379 |
4.82e-21 |
|
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain.
Pssm-ID: 460819 [Multi-domain] Cd Length: 94 Bit Score: 89.18 E-value: 4.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1278 QVVVIPCGitnalseEDRDALIAKCNDYRRRLLSVNIRARADLRdNYSPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAV 1357
Cdd:pfam03129 1 QVVVIPLG-------EKAEELEEYAQKLAEELRAAGIRVELDDR-NESIGKKFRRADLIGIPFALVVGEKELEEGTVTVR 72
|
90 100
....*....|....*....|..
gi 940746979 1358 RRDTGEKLTVTENEAETKLKAL 1379
Cdd:pfam03129 73 RRDTGEQETVSLDELVEKLKEL 94
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
878-926 |
1.55e-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: 1.55e-20
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 940746979 878 LFDQVASQGEVVRKLKAEKASKDQVDAAVQELLQRKAQYKSLTGVEYKP 926
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKP 49
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
879-932 |
2.50e-19 |
|
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.
Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 82.77 E-value: 2.50e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 940746979 879 FDQVASQGEVVRKLKAEKASKDQVDAAVQELLQRKAQYKSLTGVEYKPVSATGA 932
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGD 54
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
801-845 |
1.03e-18 |
|
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: 80.74 E-value: 1.03e-18
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 940746979 801 LYDEVAAQGEVVRKLKAEKAPKAKVNEAVECLLSLKAQYKEKTGQ 845
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQ 45
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
729-770 |
3.06e-17 |
|
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238605 [Multi-domain] Cd Length: 42 Bit Score: 76.42 E-value: 3.06e-17
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 940746979 729 YNKVAAQGDVVRELKAKKAAKEDVDAAVKQLLALKAEYKEKT 770
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
348-457 |
4.48e-17 |
|
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: 82.13 E-value: 4.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 348 VYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNL-NNTVLSKRKLtwfvdeglvdgwd 426
Cdd:cd00418 93 GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLeDGTKLSKRKL------------- 159
|
90 100 110
....*....|....*....|....*....|.
gi 940746979 427 dprFPTVRGVLRRGMTVEGLKQFIAAQGSSR 457
Cdd:cd00418 160 ---NTTLRALRRRGYLPEALRNYLALIGWSK 187
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
801-853 |
4.85e-17 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 76.38 E-value: 4.85e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 940746979 801 LYDEVAAQGEVVRKLKAEKAPKAKVNEAVECLLSLKAQYKEKTGQNTCLGQPP 853
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 ... |
802-857 |
3.07e-16 |
|
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: 73.92 E-value: 3.07e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 940746979 802 YDEVAAQGEVVRKLKAEKAPKAKVNEAVECLLSLKAQYKEKTGQNTCLGQPPSLTA 857
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGDTP 56
|
|
| GST_C_GluRS_N |
cd10306 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Glutamyl-tRNA synthetase; ... |
74-156 |
3.76e-16 |
|
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: 74.70 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 74 EHTEIDHWLEFSATKLSSCDlFPS---AINELNHCLSLRTYLVGNSLSLADLCVWATLKGNVAWQEQLQQNRAPvHVKRW 150
Cdd:cd10306 3 DKEQVAEWIDFATTLLVLKD-FKAlsqALEELDSHLTLRTFIVGYSLSLADIAVWGALRGNGVAGSLIKNKVYV-NLSRW 80
|
....*.
gi 940746979 151 FGFLEA 156
Cdd:cd10306 81 FSFLES 86
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
879-920 |
8.59e-16 |
|
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238605 [Multi-domain] Cd Length: 42 Bit Score: 72.19 E-value: 8.59e-16
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 940746979 879 FDQVASQGEVVRKLKAEKASKDQVDAAVQELLQRKAQYKSLT 920
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
802-843 |
1.48e-15 |
|
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238605 [Multi-domain] Cd Length: 42 Bit Score: 71.80 E-value: 1.48e-15
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 940746979 802 YDEVAAQGEVVRKLKAEKAPKAKVNEAVECLLSLKAQYKEKT 843
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
1031-1250 |
1.29e-14 |
|
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: 74.46 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1031 IWESIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKTHVADFAPevawvtrsGKTELAEPIAVRPTSETvmYPAYAkWVQ 1110
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKDLLP--------VGAENEEDLYLRPTLEP--GLVRL-FVS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1111 SHRDLPIRLNQWCNVVRWEfKHPQPFLRTREFLWQEGHSaFATFEEAAAEVLQILDLYAQVYEEL-LAIPVVKGRKTEKE 1189
Cdd:cd00768 70 HIRKLPLRLAEIGPAFRNE-GGRRGLRRVREFTQLEGEV-FGEDGEEASEFEELIELTEELLRALgIKLDIVFVEKTPGE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940746979 1190 KFAGGdYTTTVEAFI-SASGRAIQGATSHHLGQNFSKMFEIIFEDPktPGEKQFAYQNSWGL 1250
Cdd:cd00768 148 FSPGG-AGPGFEIEVdHPEGRGLEIGSGGYRQDEQARAADLYFLDE--ALEYRYPPTIGFGL 206
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
1086-1262 |
3.11e-11 |
|
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: 63.97 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1086 ELAEPIAVRPTSETVMYPAYAKWVQSHRDLPIRLNQWCNVVRWEFKHPQ-PFLRTREFLWQEGHSaFATFEEAAAEVLQI 1164
Cdd:pfam00587 6 ENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTrGLIRVRQFHQDDAHI-FHAPGQSPDELEDY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1165 LDLYAQVYEELLaIPVVKGRKTEKEKFAGGDYTTTVEAFISASGRAIQGATSHHLGQNFSKMFEIIFEDPKtpGEKQFAY 1244
Cdd:pfam00587 85 IKLIDRVYSRLG-LEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDED--NESKFPY 161
|
170 180
....*....|....*....|
gi 940746979 1245 QNSWGL--TTRTIGVMTMVH 1262
Cdd:pfam00587 162 MIHRAGlgVERFLAAILENN 181
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
1277-1377 |
4.15e-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: 60.88 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1277 VQVVVIPCGitnalseEDRDALIAKCNDYRRRLLSVNIRARADLRDNySPGWKFNHWELKGVPIRLEVGPRDMKSCQFVA 1356
Cdd:cd00738 2 IDVAIVPLT-------DPRVEAREYAQKLLNALLANGIRVLYDDRER-KIGKKFREADLRGVPFAVVVGEDELENGKVTV 73
|
90 100
....*....|....*....|.
gi 940746979 1357 VRRDTGEKLTVTENEAETKLK 1377
Cdd:cd00738 74 KSRDTGESETLHVDELPEFLV 94
|
|
| GST_C_AIMP3 |
cd10305 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ... |
74-151 |
1.86e-10 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 3; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein (AIMP) 3 subfamily; AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex that functions as a molecular hub to coordinate protein synthesis. There are three AIMPs, named AIMP1-3, which play diverse regulatory roles. AIMP3, also called p18 or eukaryotic translation elongation factor 1 epsilon-1 (EEF1E1), contains a C-terminal domain with similarity to the C-terminal alpha helical domain of GSTs. It specifically interacts with methionyl-tRNA synthetase (MetRS) and is translocated to the nucleus during DNA synthesis or in response to DNA damage and oncogenic stress. In the nucleus, it interacts with ATM and ATR, which are upstream kinase regulators of p53. It appears to work against DNA damage in cooperation with AIMP2, and similar to AIMP2, AIMP3 is also a haploinsufficient tumor suppressor. AIMP3 transgenic mice have shorter lifespans than wild-type mice and they show characteristics of progeria, suggesting that AIMP3 may also be involved in cellular and organismal aging.
Pssm-ID: 198338 [Multi-domain] Cd Length: 101 Bit Score: 59.23 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 74 EHTEIDHWLEFSATKLSSCD---LFPSAINELNHCLSLRTYLVGNSLSLADLCVWATLKGNVAwQEQLQQNRAPVHVKRW 150
Cdd:cd10305 3 ERAQVDQWLEYRVTQVAPASdkaDAKSLLKELNSYLQDRTYLVGHKLTLADVVLYYGLHPIMK-DLSPQEKEQYLNVSRW 81
|
.
gi 940746979 151 F 151
Cdd:cd10305 82 F 82
|
|
| GstA |
COG0625 |
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; |
44-167 |
7.83e-08 |
|
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440390 [Multi-domain] Cd Length: 205 Bit Score: 54.52 E-value: 7.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 44 ENVVFTDINSILRYLARVAMTARLYGSNLMEHTEIDHWLEFSATKLSSC------DLFPSAINE---------------L 102
Cdd:COG0625 59 DGLVLTESLAILEYLAERYPEPPLLPADPAARARVRQWLAWADGDLHPAlrnlleRLAPEKDPAaiararaelarllavL 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940746979 103 NHCLSLRTYLVGNSLSLADLCVWATLkgnvAWQEQLQQNRAPV-HVKRWFGFLEAQQAFQSVGTKW 167
Cdd:COG0625 139 EARLAGGPYLAGDRFSIADIALAPVL----RRLDRLGLDLADYpNLAAWLARLAARPAFQRALAAA 200
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
1219-1380 |
1.03e-07 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 56.63 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1219 LGQNFSKMFEIIFEDPKtpGEKQFAYQNSWGlttrtIGVMTMV------HGDNMGLVLPPRVACVQVVVIPcgiTNALSE 1292
Cdd:PRK09194 412 LGTKYSEAMNATVLDEN--GKAQPLIMGCYG-----IGVSRLVaaaieqNHDEKGIIWPKAIAPFDVHIVP---VNMKDE 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1293 EDRDA---LIAKcndyrrrLLSVNIRARADLRDNySPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVTE 1369
Cdd:PRK09194 482 EVKELaekLYAE-------LQAAGIEVLLDDRKE-RPGVKFADADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPV 553
|
170
....*....|.
gi 940746979 1370 NEAETKLKALL 1380
Cdd:PRK09194 554 DELVEFLKALK 564
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
878-915 |
1.29e-07 |
|
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: 49.39 E-value: 1.29e-07
10 20 30
....*....|....*....|....*....|....*...
gi 940746979 878 LFDQVASQGEVVRKLKAEKASKDQVDAAVQELLQRKAQ 915
Cdd:cd00938 3 LEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQ 40
|
|
| GST_C_Arc1p_N_like |
cd10304 |
Glutathione S-transferase C-terminal-like, alpha helical domain of the Aminoacyl tRNA ... |
74-169 |
6.19e-07 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of the Aminoacyl tRNA synthetase cofactor 1 and similar proteins; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase cofactor 1 (Arc1p)-like subfamily; Arc1p, also called GU4 nucleic binding protein 1 (G4p1) or p42, is a tRNA-aminoacylation and nuclear-export cofactor. It contains a domain in the N-terminal region with similarity to the C-terminal alpha helical domain of GSTs. This domain mediates the association of the aminoacyl tRNA synthetases (aaRSs), MetRS and GluRS, in yeast to form a stable stoichiometric ternany complex. The GST_C-like domain of Arc1p is a protein-protein interaction domain containing two binding sites which enable it to bind the two aaRSs simultaneously and independently. The MetRS-Arc1p-GluRS complex selectively recruits and aminoacylates its cognate tRNAs without additional cofactors. Arc1p also plays a role in the transport of tRNA from the nucleus to the cytoplasm. It may also control the subcellular distribution of GluRS in the cytoplasm, nucleoplasm, and the mitochondrial matrix.
Pssm-ID: 198337 [Multi-domain] Cd Length: 100 Bit Score: 49.29 E-value: 6.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 74 EHTEIDHWLEFSATkLSSCDLFPSAINELNHCLSLRTYLVGNS-LSLADLCVWATLKGNVA-WQEQLQQNRAPV-HVKRW 150
Cdd:cd10304 3 QSAEVAQWLSVAKS-GPVSKDVQETLGQLNLHLRTRTFLLGTGkPSVADVAVFEAVLPVVKeWSDEVKTGYAKYrHILRW 81
|
90
....*....|....*....
gi 940746979 151 FGFLEAQQAFQSVGTKWNV 169
Cdd:cd10304 82 VDYVQNLLLFIPEADKIEV 100
|
|
| GST_C_AIMP2 |
cd03200 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ... |
55-157 |
2.27e-06 |
|
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: 47.51 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 55 LRYLARVAMTarlYGSNLMEHTEIDHWLEFSATKL--SSCDLFPSAINELNHCLSLRTYLVGNSLSLADLCVWATLkgnv 132
Cdd:cd03200 1 ARFLFRLLGD---ESDDPVNATLIDSWVDTAIFQLleGSSKEKAAVLRALNSALGRSPWLVGSEPTVADIALWSAV---- 73
|
90 100
....*....|....*....|....*
gi 940746979 133 awQEQLQQNRAPVHVKRWFGFLEAQ 157
Cdd:cd03200 74 --LQTGLASGAPANVQRWMKSCENL 96
|
|
| MetRS_RNA |
cd00939 |
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
801-844 |
2.45e-06 |
|
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238475 [Multi-domain] Cd Length: 45 Bit Score: 45.54 E-value: 2.45e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 940746979 801 LYDEVAAQGEVVRKLKAEKAPKAKVNEAVECLLSLKAQYKEKTG 844
Cdd:cd00939 1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEG 44
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
731-786 |
3.23e-06 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 51.67 E-value: 3.23e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 940746979 731 KVAAQGDVVRELKAKKAAKEDVDAAVKQLLALK--AEYKEKTGQEYKPGSPPAAAAQA 786
Cdd:PLN02734 15 AVTAQGNAVRALKASKADKAEIDAAIEKLKALKleKSALEKELQAAVGAGGDGAASKE 72
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
799-838 |
3.96e-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: 3.96e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 940746979 799 RSLYDEVAAQGEVVRKLKAEKAPKAKVNEAVECLLSLKAQ 838
Cdd:cd00938 1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQ 40
|
|
| MetRS_RNA |
cd00939 |
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
878-922 |
8.26e-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: 44.00 E-value: 8.26e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 940746979 878 LFDQVASQGEVVRKLKAEKASKDQVDAAVQELLQRKAQYKSLTGV 922
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 ... |
728-771 |
1.52e-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: 43.62 E-value: 1.52e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 940746979 728 LYNKVAAQGDVVRELKAKKAAKEDVDAAVKQLLALKAEYKEKTG 771
Cdd:cd00939 1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEG 44
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
1218-1378 |
2.63e-05 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 48.32 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1218 HLGQNFSKMFEIIFEDPKtpGEKQFAYQNSWGlttrtIGVMTMV-------HGDNmGLVLPPRVACVQVVVIPCGITNAl 1290
Cdd:PRK12325 288 YFGTKYSEPMNAKVQGPD--GKEVPVHMGSYG-----IGVSRLVaaiieasHDDK-GIIWPESVAPFKVGIINLKQGDE- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1291 seedrdALIAKCNDYRRRLLSVNIRARADLRDNySPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVTEN 1370
Cdd:PRK12325 359 ------ACDAACEKLYAALSAAGIDVLYDDTDE-RPGAKFATMDLIGLPWQIIVGPKGLAEGKVELKDRKTGEREELSVE 431
|
....*...
gi 940746979 1371 EAETKLKA 1378
Cdd:PRK12325 432 AAINRLTA 439
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
732-765 |
5.30e-05 |
|
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238474 [Multi-domain] Cd Length: 45 Bit Score: 42.07 E-value: 5.30e-05
10 20 30
....*....|....*....|....*....|....
gi 940746979 732 VAAQGDVVRELKAKKAAKEDVDAAVKQLLALKAE 765
Cdd:cd00938 7 VKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQ 40
|
|
| GST_C_EF1Bgamma_like |
cd03181 |
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ... |
74-163 |
6.24e-05 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of Elongation Factor 1B and similar proteins; Glutathione S-transferase (GST) C-terminal domain family, Gamma subunit of Elongation Factor 1B (EF1Bgamma) subfamily; EF1Bgamma is part of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. The EF1B gamma subunit contains a GST fold consisting of an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The GST-like domain of EF1Bgamma is believed to mediate the dimerization of the EF1 complex, which in yeast is a dimer of the heterotrimer EF1A:EF1Balpha:EF1Bgamma. In addition to its role in protein biosynthesis, EF1Bgamma may also display other functions. The recombinant rice protein has been shown to possess GSH conjugating activity. The yeast EF1Bgamma binds to membranes in a calcium dependent manner and is also part of a complex that binds to the msrA (methionine sulfoxide reductase) promoter suggesting a function in the regulation of its gene expression. Also included in this subfamily is the GST_C-like domain at the N-terminus of human valyl-tRNA synthetase (ValRS) and its homologs. Metazoan ValRS forms a stable complex with Elongation Factor-1H (EF-1H), and together, they catalyze consecutive steps in protein biosynthesis, tRNA aminoacylation and its transfer to EF.
Pssm-ID: 198290 [Multi-domain] Cd Length: 123 Bit Score: 44.09 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 74 EHTEIDHWLEFSATKL--SSCDLF-PS-------------AINELNHC-------LSLRTYLVGNSLSLADLCVWATLKG 130
Cdd:cd03181 1 EAAQVLQWISFANSELlpAAATWVlPLlgiapynkkavdkAKEDLKRAlgvleehLLTRTYLVGERITLADIFVASALLR 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 940746979 131 nvawqeQLQQN-----RAP-VHVKRWFGFLEAQQAFQSV 163
Cdd:cd03181 81 ------GFETVldpefRKKyPNVTRWFNTVVNQPKFKAV 113
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
878-932 |
2.24e-04 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 45.89 E-value: 2.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 940746979 878 LFDQVASQGEVVRKLKAEKASKDQVDAAVQELLQRKAQYKSLTGVEYKPVSATGA 932
Cdd:PLN02734 12 KQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELQAAVGAGGD 66
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
1253-1378 |
2.55e-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: 45.41 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1253 RTIGVMTMVHGDNMGLVLPPrvacVQVVVIPcgITnalseedrDALIAKCNDYRRRLLSVNIRARADLRDNySPGWKFNH 1332
Cdd:COG0441 520 RFIGILIEHYAGAFPLWLAP----VQVVVLP--IS--------DKHADYAKEVAKKLRAAGIRVEVDLRNE-KIGYKIRE 584
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 940746979 1333 WELKGVPIRLEVGPRDMKSCQfVAVR-RDTGEKLTVTENEAETKLKA 1378
Cdd:COG0441 585 AQLQKVPYMLVVGDKEVENGT-VSVRrRGGGDLGTMSLDEFIARLKE 630
|
|
| GlyRS_RNA |
cd00935 |
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS ... |
878-913 |
2.66e-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: 40.16 E-value: 2.66e-04
10 20 30
....*....|....*....|....*....|....*.
gi 940746979 878 LFDQVASQGEVVRKLKAEKASKDQVDAAVQELLQRK 913
Cdd:cd00935 4 LRAAVKEQGDLVRKLKEEGAPDVDIKKAVAELKARK 39
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
674-779 |
3.00e-04 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 45.37 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 674 LIYIpdgHTKEMPTS---GSKEKTKVETLKNETttpvkERPAAPLTNTSAASEGPVVLYNKVAAQ-GDVVRELKAKKAAK 749
Cdd:PLN02221 190 FLYI---HTPIITTSdceGAGEMFQVTTLINYT-----ERLEQDLIDNPPPTEADVEAARLIVKErGEVVAQLKAAKASK 261
|
90 100 110
....*....|....*....|....*....|.
gi 940746979 750 EDVDAAVKQLLALKAEYKE-KTGQEYKPGSP 779
Cdd:PLN02221 262 EEITAAVAELKIAKESLAHiEERSKLKPGLP 292
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
1277-1377 |
4.95e-04 |
|
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238437 [Multi-domain] Cd Length: 91 Bit Score: 40.56 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940746979 1277 VQVVVIPcgITNalseedrdaliaKCNDY----RRRLLSVNIRARADLRDNySPGWKFNHWELKGVPIRLEVGPRDMKSc 1352
Cdd:cd00860 2 VQVVVIP--VTD------------EHLDYakevAKKLSDAGIRVEVDLRNE-KLGKKIREAQLQKIPYILVVGDKEVET- 65
|
90 100
....*....|....*....|....*.
gi 940746979 1353 QFVAVR-RDTGEKLTVTENEAETKLK 1377
Cdd:cd00860 66 GTVSVRtRDGGDLGSMSLDEFIEKLK 91
|
|
| GlyRS_RNA |
cd00935 |
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS ... |
728-769 |
6.83e-04 |
|
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix-turn-helix structure , which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238472 [Multi-domain] Cd Length: 51 Bit Score: 39.01 E-value: 6.83e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 940746979 728 LYNKVAAQGDVVRELKAKKAAKEDVDAAVKQLLALKAEYKEK 769
Cdd:cd00935 4 LRAAVKEQGDLVRKLKEEGAPDVDIKKAVAELKARKKLLEDK 45
|
|
| GlyRS_RNA |
cd00935 |
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS ... |
800-842 |
1.46e-03 |
|
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix-turn-helix structure , which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238472 [Multi-domain] Cd Length: 51 Bit Score: 37.85 E-value: 1.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 940746979 800 SLYDEVAAQGEVVRKLKAEKAPKAKVNEAVECLLSLKAQYKEK 842
Cdd:cd00935 3 PLRAAVKEQGDLVRKLKEEGAPDVDIKKAVAELKARKKLLEDK 45
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
803-836 |
2.70e-03 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 42.42 E-value: 2.70e-03
10 20 30
....*....|....*....|....*....|....
gi 940746979 803 DEVAAQGEVVRKLKAEKAPKAKVNEAVECLLSLK 836
Cdd:PLN02734 14 AAVTAQGNAVRALKASKADKAEIDAAIEKLKALK 47
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