|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
282-1264 |
0e+00 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 1417.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 282 LPTPPGEKKDVSGTMPDSYSPQYVEAAWYPWWERQGFFKPEYGRPSVSAPNPrgvFMMCIPPPNVTGSLHLGHALTNAIQ 361
Cdd:PTZ00419 10 SKDEKKNKKRNISSMAASYDPKEVESGWYEWWEKSGFFKPAEDAKSLNSGKK---FVIVLPPPNVTGYLHIGHALTGAIQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 362 DSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKKLWKERGLNRHQLGREAFLQEVWKWKAEKGDRIYHQLKKLGSSLDWD 441
Cdd:PTZ00419 87 DSLIRYHRMKGDETLWVPGTDHAGIATQVVVEKKLMKEENKTRHDLGREEFLKKVWEWKDKHGNNICNQLRRLGSSLDWS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 442 RACFTMDPKLSATVTEAFVRLHEEGVIYRSTRLVNWSCTLNSAISDIEVDKKELTGRTLLSVPGYKEKVEFGVLVSFAYK 521
Cdd:PTZ00419 167 REVFTMDEQRSKAVKEAFVRLYEDGLIYRDTRLVNWCCYLKTAISDIEVEFEEIEKPTKITIPGYDKKVEVGVLWHFAYP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 522 VQGSDsDEEVVVATTRIETMLGDVAVAVHPKDPRYQHLKGKSVVHPFLS-RSLPIVFDD-FVDMEFGTGAVKITPAHDQN 599
Cdd:PTZ00419 247 LEDSG-QEEIVVATTRIETMLGDVAVAVHPKDERYKKLHGKELIHPFIPdRKIPIIADDeLVDMEFGTGAVKITPAHDPN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 600 DYEVGQRHRLEAISIMDSKGALVNVPPPFLGLPRFEARKAVLAALKEQGLFRGIKDNPMVVPLCNRSKDVVEPLLRPQWY 679
Cdd:PTZ00419 326 DYEIAKRHNLPFINIFTLDGKINENGGEFAGMHRFDCRRKIEEELKEMGLLRDKVPNPMRLPRCSRSGDIVEPMLIPQWY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 680 VRCGEMAQAASAAVTRGDLRILPEAHQRTWHSWMDNIRDWCISRQLWWGHRIPAYFITVHD-PAVPPGEDPdgryWVSGR 758
Cdd:PTZ00419 406 VNCKDMAKRAVEAVRNGELKIIPSSHENVWYHWLENIQDWCISRQLWWGHRIPAYRVISKGpETDPSDEEP----WVVAR 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 759 TEAEAREKAAREFGVSPDKISLQQDEDVLDTWFSSGLFPFSIFGWPNQSEDLSVFYPGTLLETGHDILFFWVARMVMLGL 838
Cdd:PTZ00419 482 SEEEALEKAKKKFGLSEEDFELEQDEDVLDTWFSSGLFPFSTLGWPDQTDDLQRFFPTSLLETGSDILFFWVARMVMMSL 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 839 KLTEKLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVIHGVSLQGLHDQLLNSNLDPSEVEKAKEGQRADFPAGIPECG 918
Cdd:PTZ00419 562 HLTDKLPFKTVFLHAMVRDSQGEKMSKSKGNVIDPLEVIEGISLQDLNQKLYEGNLPEKEIKRAIELQKKEFPNGIPECG 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 919 TDALRFGLCAYTSQGRDINLDVNRILGYRHFCNKLWNATKFALRGLGKGFVPSPT--SKPEGHESL--VDRWIRSRLAEA 994
Cdd:PTZ00419 642 TDALRFGLLAYTQQGRNINLDINRVVGYRHFCNKLWNAVKFALMKLLKDFNLPNStlFKPNNVESLpwEDKWILHRLNVA 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 995 VRLSNEGFQAYDFPAVTTAQYSFWLYELCDVYLECLKPVLN-GVDQVAADCARQTLYTCLDVGLRLLSPFMPFVTEELFQ 1073
Cdd:PTZ00419 722 IKEVTEGFKEYDFSEATQATYNFWLYELCDVYLELIKPRLSkQSDGERKQHAQDVLHTVLDIGLRLLHPMMPFITEELYQ 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 1074 RLPRRtPNAPASLCVTPYPEPSeCSWKDPEAEAALELALSITRAVRSLRADYNLT-RTRPDCFLEVADEATGALASAVSA 1152
Cdd:PTZ00419 802 RLPNY-LRKSESISIAKYPQPN-PGWNNEALDEEMKIIMSIVKSIRSLIATLGIPnKTKPDCYVTAKDAELIELIESAEN 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 1153 YVQTLASAG---VVAVLALGAPAPQGCAVAVASDRCSIHLQLQGLVDPARELGKLQAKRSEAQRQAQRLQERRAASGYSA 1229
Cdd:PTZ00419 880 LISTLAKIGsvsVIPPIEEEAEVPKGCGFDVVDNKVIIYLNLDEFIDLKKELAKLEKKLAKLQKSLESYLKKISIPNYED 959
|
970 980 990
....*....|....*....|....*....|....*
gi 564396916 1230 KVPLEVQEADEVKLQQTEAELRKVDEAIALFQKML 1264
Cdd:PTZ00419 960 KVPEDVRKLNDEKIDELNEEIKQLEQAIEELKSLL 994
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
296-1258 |
0e+00 |
|
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440291 [Multi-domain] Cd Length: 877 Bit Score: 1194.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 296 MPDSYSPQYVEAAWYPWWERQGFFKPEygrPSVSAPNprgvFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETT 375
Cdd:COG0525 3 LPKTYDPKEVEAKWYQYWEENGYFKAD---PDSDKEP----FTIVIPPPNVTGSLHMGHALNNTLQDILIRYKRMQGYNT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 376 LWNPGCDHAGIATQVVVEKKLwKERGLNRHQLGREAFLQEVWKWKAEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSATV 455
Cdd:COG0525 76 LWQPGTDHAGIATQAVVERQL-AEEGKSRHDLGREKFLERVWEWKEESGGTITNQLRRLGASCDWSRERFTMDEGLSKAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 456 TEAFVRLHEEGVIYRSTRLVNWSCTLNSAISDIEVDkkeltgrtllsvpgYKEKVefGVLVSFAYKVqgSDSDEEVVVAT 535
Cdd:COG0525 155 REVFVRLYEKGLIYRGKRLVNWDPKLKTALSDLEVE--------------HEEVK--GHLWHIRYPL--ADGSGYIVVAT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 536 TRIETMLGDVAVAVHPKDPRYQHLKGKSVVHPFLSRSLPIVFDDFVDMEFGTGAVKITPAHDQNDYEVGQRHRLEAISIM 615
Cdd:COG0525 217 TRPETMLGDTAVAVHPEDERYKHLIGKTVILPLVGREIPIIADEYVDPEFGTGAVKITPAHDPNDFEVGKRHNLPMINIL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 616 DSKGALVNVPPPFLGLPRFEARKAVLAALKEQGLFRGIKDNPMVVPLCNRSKDVVEPLLRPQWYVRCGEMAQAASAAVTR 695
Cdd:COG0525 297 DEDGTINENAGKYRGLDRFEARKAIVADLEELGLLVKVEPHKHSVGHSDRSGTVIEPYLSDQWFVKMKPLAKPAIEAVED 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 696 GDLRILPEAHQRTWHSWMDNIRDWCISRQLWWGHRIPAYFitvhdpavppgeDPDGRYWVSgRTEAEAREKAarefgvsp 775
Cdd:COG0525 377 GEIKFVPERWEKTYFHWMENIRDWCISRQLWWGHRIPAWY------------CPDGEVYVA-RTEPEACAKA-------- 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 776 DKISLQQDEDVLDTWFSSGLFPFSIFGWPNQSEDLSVFYPGTLLETGHDILFFWVARMVMLGLKLTEKLPFREVYLHAIV 855
Cdd:COG0525 436 GSVNLTQDEDVLDTWFSSALWPFSTLGWPEKTEDLKYFYPTSVLVTGFDIIFFWVARMIMMGLHFTGEVPFKDVYIHGLV 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 856 RDAHGRKMSKSLGNVIDPLDVIhgvslqglhDQLlnsnldpsevekakegqradfpagipecGTDALRFGLCAYTSQGRD 935
Cdd:COG0525 516 RDEQGRKMSKSKGNVIDPLDLI---------DKY----------------------------GADALRFTLAALASPGRD 558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 936 INLDVNRILGYRHFCNKLWNATKFALrGLGKGFVPSPTSKPEgHESLVDRWIRSRLAEAVRLSNEGFQAYDFPAVTTAQY 1015
Cdd:COG0525 559 IKFDEERVEGYRNFANKLWNASRFVL-MNLEGFDPGLDPDPE-ELSLADRWILSRLNKTIAEVTEALEKYRFDEAAQALY 636
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 1016 SF-WlYELCDVYLECLKPVLNGVDQVAADCARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRTPNapASLCVTPYPEP 1094
Cdd:COG0525 637 DFvW-NEFCDWYLELAKPRLYGGDEAAKRETRATLVYVLEQILRLLHPFMPFITEEIWQKLPPRKEG--ESIMLAPWPEA 713
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 1095 SEcSWKDPEAEAALELALSITRAVRSLRADYNLT-RTRPDCFLEVADEATGALASAVSAYVQTLASAGVVAVLAlgAPAP 1173
Cdd:COG0525 714 DE-ELIDEEAEAEFEWLKEVISAIRNIRAEMNIPpSKKLPLLLKGADEADRARLEENAAYIKRLARLEEITILV--DEKP 790
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 1174 QGCAVAVASDrCSIHLQLQGLVDPARELGKLQAKRSEAQRQAQRLQERRAASGYSAKVPLEVQEADEVKLQQTEAELRKV 1253
Cdd:COG0525 791 EGAASAVVGG-AEVFLPLEGLIDVEAERARLEKELAKLEKEIARVEKKLSNEGFVAKAPAEVVEKEREKLAEAEAKLEKL 869
|
....*
gi 564396916 1254 DEAIA 1258
Cdd:COG0525 870 EEQLA 874
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
295-1262 |
0e+00 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 1164.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 295 TMPDSYSPQYVEAAWYPWWERQGFFKPEygrpsvsaPNPRGVFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGET 374
Cdd:PRK05729 4 ELPKTYDPKEVEAKWYQKWEEKGYFKPD--------DNSKKPFSIVIPPPNVTGSLHMGHALNNTLQDILIRYKRMQGYN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 375 TLWNPGCDHAGIATQVVVEKKLWKErGLNRHQLGREAFLQEVWKWKAEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSAT 454
Cdd:PRK05729 76 TLWLPGTDHAGIATQMVVERQLAAE-GKSRHDLGREKFLEKVWEWKEESGGTITNQLRRLGASCDWSRERFTMDEGLSKA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 455 VTEAFVRLHEEGVIYRSTRLVNWSCTLNSAISDIEVDkkeltgrtllsvpgYKEkVEfGVLVSFAYKVqgSDSDEEVVVA 534
Cdd:PRK05729 155 VREVFVRLYEKGLIYRGKRLVNWDPKLQTALSDLEVE--------------YKE-VK-GKLWHIRYPL--ADGSDYLVVA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 535 TTRIETMLGDVAVAVHPKDPRYQHLKGKSVVHPFLSRSLPIVFDDFVDMEFGTGAVKITPAHDQNDYEVGQRHRLEAISI 614
Cdd:PRK05729 217 TTRPETMLGDTAVAVNPEDERYKHLIGKTVILPLVGREIPIIADEYVDPEFGTGAVKITPAHDPNDFEVGKRHNLPMINI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 615 MDSKGALVNVPPPFLGLPRFEARKAVLAALKEQGLFRGIKDNPMVVPLCNRSKDVVEPLLRPQWYVRCGEMAQAASAAVT 694
Cdd:PRK05729 297 MDEDGTINENPGEYQGLDRFEARKAIVADLEELGLLVKIEPHTHSVGHSDRSGVVIEPYLSDQWFVKMKPLAKPALEAVE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 695 RGDLRILPEAHQRTWHSWMDNIRDWCISRQLWWGHRIPAYFitvhdpavppgeDPDGRYWVsGRTEAEAREKAArefgvs 774
Cdd:PRK05729 377 NGEIKFVPERWEKTYFHWMENIQDWCISRQLWWGHRIPAWY------------DEDGEVYV-GREEPEAREKAL------ 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 775 pdkisLQQDEDVLDTWFSSGLFPFSIFGWPNQSEDLSVFYPGTLLETGHDILFFWVARMVMLGLKLTEKLPFREVYLHAI 854
Cdd:PRK05729 438 -----LTQDEDVLDTWFSSALWPFSTLGWPEKTEDLKRFYPTSVLVTGFDIIFFWVARMIMMGLHFTGQVPFKDVYIHGL 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 855 VRDAHGRKMSKSLGNVIDPLDVIhgvslqglhDQLlnsnldpsevekakegqradfpagipecGTDALRFGLCAYTSQGR 934
Cdd:PRK05729 513 VRDEQGRKMSKSKGNVIDPLDLI---------DKY----------------------------GADALRFTLAALASPGR 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 935 DINLDVNRILGYRHFCNKLWNATKFALrgLGKGFVPSPTSKPEGHESLVDRWIRSRLAEAVRLSNEGFQAYDFPAVTTAQ 1014
Cdd:PRK05729 556 DIRFDEERVEGYRNFANKLWNASRFVL--MNLEGADVGELPDPEELSLADRWILSRLNRTVAEVTEALDKYRFDEAARAL 633
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 1015 YSFWLYELCDVYLECLKPVLNGVDQVAadcARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRtpNAPASLCVTPYPEP 1094
Cdd:PRK05729 634 YEFIWNEFCDWYLELAKPVLQEAAKRA---TRATLAYVLEQILRLLHPFMPFITEELWQKLAPL--GIEESIMLAPWPEA 708
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 1095 SECswKDPEAEAALELALSITRAVRSLRADYNLT-RTRPDCFLEVADEATGALASAVSAYVQTLASAGVVAVLALGAPAP 1173
Cdd:PRK05729 709 DEA--IDEAAEAEFEWLKELITAIRNIRAEMNIPpSKKLPLLLKGADAEDRARLEANEAYIKRLARLESLEILADDEEAP 786
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 1174 QGCAVAVASDrCSIHLQLQGLVDPARELGKLQAKRSEAQRQAQRLQERRAASGYSAKVPLEVQEADEVKLQQTEAELRKV 1253
Cdd:PRK05729 787 EGAASAVVGG-AELFLPLEGLIDVEAELARLEKELAKLEKEIERVEKKLSNEGFVAKAPEEVVEKEREKLAEYEEKLAKL 865
|
....*....
gi 564396916 1254 DEAIALFQK 1262
Cdd:PRK05729 866 KERLARLKA 874
|
|
| PLN02381 |
PLN02381 |
valyl-tRNA synthetase |
213-1256 |
0e+00 |
|
valyl-tRNA synthetase
Pssm-ID: 215214 [Multi-domain] Cd Length: 1066 Bit Score: 1146.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 213 ARSVTQQPGSEITAPQKTAAQLKKEAKKREK-------------LEKFQQKQKTQQQQPAHGEKKPKPEKKEKRDPGVIT 279
Cdd:PLN02381 1 GSRTESEAEKKILTEEELERKKKKEEKAKEKelkklkaaqkeakAKLQAQQASDGTNVPKKSEKKSRKRDVEDENPEDFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 280 yDLPTPPGEKKDVSGTMPDSYSPQYVEAAWYPWWERQGFFKPEygrPSVSAPNprgvFMMCIPPPNVTGSLHLGHALTNA 359
Cdd:PLN02381 81 -DPDTPFGQKKRLSSQMAKQYSPSAVEKSWYAWWEKSGYFGAD---AKSSKPP----FVIVLPPPNVTGALHIGHALTAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 360 IQDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKKLWKERGLNRHQLGREAFLQEVWKWKAEKGDRIYHQLKKLGSSLD 439
Cdd:PLN02381 153 IEDTIIRWKRMSGYNALWVPGVDHAGIATQVVVEKKLMRERHLTRHDIGREEFVSEVWKWKDEYGGTILNQLRRLGASLD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 440 WDRACFTMDPKLSATVTEAFVRLHEEGVIYRSTRLVNWSCTLNSAISDIEVDKKELTGRTLLSVPGYKEKVEFGVLVSFA 519
Cdd:PLN02381 233 WSRECFTMDEQRSKAVTEAFVRLYKEGLIYRDIRLVNWDCTLRTAISDVEVDYIDIKERTLLKVPGYDKPVEFGVLTSFA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 520 YKVQGSDSdeEVVVATTRIETMLGDVAVAVHPKDPRYQHLKGKSVVHPFLSRSLPIVFD-DFVDMEFGTGAVKITPAHDQ 598
Cdd:PLN02381 313 YPLEGGLG--EIVVATTRIETMLGDTAIAIHPDDERYKHLHGKFAVHPFNGRKLPIICDaILVDPNFGTGAVKITPAHDP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 599 NDYEVGQRHRLEAISIMDSKGAL-VNVPPPFLGLPRFEARKAVLAALKEQGLFRGIKDNPMVVPLCNRSKDVVEPLLRPQ 677
Cdd:PLN02381 391 NDFEVGKRHNLEFINIFTDDGKInSNGGSEFAGMPRFAAREAVIEALQKKGLYRGAKNNEMRLGLCSRTNDVVEPMIKPQ 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 678 WYVRCGEMAQAASAAVTRGD---LRILPEAHQRTWHSWMDNIRDWCISRQLWWGHRIPAYFITVHDPAvppgEDPDGRY- 753
Cdd:PLN02381 471 WFVNCSSMAKQALDAAIDGEnkkLEFIPKQYLAEWKRWLENIRDWCISRQLWWGHRIPAWYVTLEDDQ----LKELGSYn 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 754 --WVSGRTEAEAREKAAREFgvSPDKISLQQDEDVLDTWFSSGLFPFSIFGWPNQSEDLSVFYPGTLLETGHDILFFWVA 831
Cdd:PLN02381 547 dhWVVARNESDALLEASQKF--PGKKFELSQDPDVLDTWFSSGLFPLSVLGWPDDTDDLKAFYPTSVLETGHDILFFWVA 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 832 RMVMLGLKLTEKLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVIHGVSLQGLHDQLLNSNLDPSEVEKAKEGQRADFP 911
Cdd:PLN02381 625 RMVMMGMQLGGDVPFRKVYLHPMIRDAHGRKMSKSLGNVIDPLEVINGISLEGLHKRLEEGNLDPKELVVAKEGQKKDFP 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 912 AGIPECGTDALRFGLCAYTSQGRDINLDVNRILGYRHFCNKLWNATKFALRGLGKGFVPSPTSKPEGHESLVdRWIRSRL 991
Cdd:PLN02381 705 NGIAECGTDALRFALVSYTAQSDKINLDILRVVGYRQWCNKLWNAVRFAMSKLGDDYTPPATLSVETMPFSC-KWILSVL 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 992 AEAVRLSNEGFQAYDFPAVTTAQYSFWLYELCDVYLECLKPVLNGVDQ---VAADCARQTLYTCLDVGLRLLSPFMPFVT 1068
Cdd:PLN02381 784 NKAISKTVSSLDAYEFSDAASTVYSWWQYQFCDVFIEAIKPYFAGDNPefaSERAAAQDTLWICLDTGLRLLHPFMPFVT 863
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 1069 EELFQRLPR-RTPNAPASLCVTPYPEPSEcSWKDPEAEAALELALSITRAVRSLRADYNLTRT--RPDCFLEVADEATGA 1145
Cdd:PLN02381 864 EELWQRLPQpKDHTRKDSIMISEYPSAVE-AWTNEKVEYEMDLVLSTVKCLRSLRAEVLEKQKneRLPAFALCRNQEIAA 942
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 1146 LASAVSAYVQTLASAGVVAVLALGAPA-PQGCAVAVASDRCSIHLQLQGLVDPARELGKLQAKRSEAQRQAQRLQERRAA 1224
Cdd:PLN02381 943 IIKSHQLEILTLANLSSLKVLLSENDApPAGCAFENVNENLKVYLQAQGAVNAEAELEKLRNKMDEIQKQQEKLEKKMNA 1022
|
1050 1060 1070
....*....|....*....|....*....|..
gi 564396916 1225 SGYSAKVPLEVQEADEVKLQQTEAELRKVDEA 1256
Cdd:PLN02381 1023 SGYKEKVPANIQEEDARKLTKLLQELEFFEKE 1054
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
296-1243 |
0e+00 |
|
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase and is particularly closely related to the isoleucyl tRNA synthetase. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273070 [Multi-domain] Cd Length: 861 Bit Score: 977.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 296 MPDSYSPQYVEAAWYPWWERQGFFKPEYGRPSVSapnprgvFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETT 375
Cdd:TIGR00422 1 MPKDYDPHEVEKKWYKKWEKSGFFKPDGNSNKPP-------FCIDIPPPNVTGSLHIGHALNWSIQDIIARYKRMKGYNV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 376 LWNPGCDHAGIATQVVVEKKLWKErGLNRHQLGREAFLQEVWKWKAEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSATV 455
Cdd:TIGR00422 74 LWLPGTDHAGIATQVKVEKKLGAE-GKTKHDLGREEFREKIWEWKEESGGTIKNQIKRLGASLDWSRERFTMDEGLSKAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 456 TEAFVRLHEEGVIYRSTRLVNWSCTLNSAISDIEVDKKELTGrtllSVPGYKEKVEFGvlvsfaykvqgsdSDEEVVVAT 535
Cdd:TIGR00422 153 KEAFVRLYEKGLIYRGEYLVNWDPKLNTAISDIEVEYKEVKG----KLYYIRYPLANG-------------SKDYLVVAT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 536 TRIETMLGDVAVAVHPKDPRYQHLKGKSVVHPFLSRSLPIVFDDFVDMEFGTGAVKITPAHDQNDYEVGQRHRLEAISIM 615
Cdd:TIGR00422 216 TRPETMFGDTAVAVHPEDERYKHLIGKKVILPLTGRKIPIIADEYVDMEFGTGAVKVTPAHDFNDYEWGKRHNLEFINIL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 616 DSKGALVNVPPPFLGLPRFEARKAVLAALKEQGLFRGIKDNPMVVPLCNRSKDVVEPLLRPQWYVRCGEMAQAASAAVTR 695
Cdd:TIGR00422 296 DEDGLLNENAGKYQGLTRFEARKKIVEDLKEEGLLVKIEPHTHNVGTCWRSGTVVEPLLSKQWFVKVEKLADKALEAAEE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 696 GDLRILPEAHQRTWHSWMDNIRDWCISRQLWWGHRIPAYFItvhdpavppgeDPDGRYWVsGRTEAEAREKAAREFGVSp 775
Cdd:TIGR00422 376 GEIKFVPKRMEKRYLNWLRNIKDWCISRQLIWGHRIPVWYC-----------KECGEVYV-AKEEPLPDDKTNTGPSVE- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 776 dkisLQQDEDVLDTWFSSGLFPFSIFGWPNQSEDLSVFYPGTLLETGHDILFFWVARMVMLGLKLTEKLPFREVYLHAIV 855
Cdd:TIGR00422 443 ----LEQDTDVLDTWFSSSLWPFSTLGWPDETKDLKKFYPTDLLVTGYDIIFFWVARMIFRSLALTGQVPFKEVYIHGLV 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 856 RDAHGRKMSKSLGNVIDPLDVIHgvslqglhdqllnsnldpsevekakegqradfpagipECGTDALRFGLCAYTSQGRD 935
Cdd:TIGR00422 519 RDEQGRKMSKSLGNVIDPLDVIE-------------------------------------KYGADALRFTLASLVTPGDD 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 936 INLDVNRILGYRHFCNKLWNATKFALRGLGKgfvPSPTSKPEGHESLVDRWIRSRLAEAVRLSNEGFQAYDFPAVTTAQY 1015
Cdd:TIGR00422 562 INFDWKRVESARNFLNKLWNASRFVLMNLSD---DLELSGGEEKLSLADRWILSKLNRTIKEVRKALDKYRFAEAAKALY 638
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 1016 SFWLYELCDVYLECLKPVLNGVDQVAADCARQTLYTCLDVGLRLLSPFMPFVTEELFQRLprrtPNAPASLCVTPYPEPS 1095
Cdd:TIGR00422 639 EFIWNDFCDWYIELVKYRLYNGNEAEKKAARDTLYYVLDKALRLLHPFMPFITEEIWQHF----KEGADSIMLQSYPVVD 714
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 1096 EcSWKDPEAEAALELALSITRAVRSLRADYNLTRTRPDCFLEVADEATGALASAVSA-YVQTLASAGVVAVLAlGAPaPQ 1174
Cdd:TIGR00422 715 A-EFVDEEAEKAFELLKEIIVSIRNLKAESNIPPNAPLKVLLIYTEAETAERLKLNAvDIKGAINFSEVEVVI-EKP-EV 791
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564396916 1175 GCAVAVASDRCSIHLQLQGLVDPARELGKLQAKRSEAQRQAQRLQERRAASGYSAKVPLEVQEADEVKL 1243
Cdd:TIGR00422 792 TEAVVELVPGFEIIIPVKGLINKAKELARLQKQLDKEKKEVIRIEGKLENEGFVKKAPKEVIEKEKEKL 860
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
300-1259 |
0e+00 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 856.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 300 YSPQYVEAAWYPWWERQGFFKPEygrpsvSAPNPRGVFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNP 379
Cdd:PRK14900 19 YEHREVEARWYPFWQERGYFHGD------EHDRTRPPFSIVLPPPNVTGSLHLGHALTATLQDVLIRWKRMSGFNTLWLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 380 GCDHAGIATQVVVEKKLWKERGLNRHQLGREAFLQEVWKWKAEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSATVTEAF 459
Cdd:PRK14900 93 GTDHAGIATQMIVEKELKKTEKKSRHDLGREAFLERVWAWKEQYGSRIGEQHKALGASLDWQRERFTMDEGLSRAVREVF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 460 VRLHEEGVIYRSTRLVNWSCTLNSAISDIEVDKKEltgrtllsvpgykekVEFGVLVSFAYKVqgSDSDEEVVVATTRIE 539
Cdd:PRK14900 173 VRLHEEGLIYREKKLINWCPDCRTALSDLEVEHEE---------------AHQGELWSFAYPL--ADGSGEIVVATTRPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 540 TMLGDVAVAVHPKDPRYQHLKGKSVVHPFLSRSLPIVFD-DFVDMEFGTGAVKITPAHDQNDYEVGQRHRLEAISIMDSK 618
Cdd:PRK14900 236 TMLGDTAVAVHPLDPRYMALHGKKVRHPITGRTFPIVADaILVDPKFGTGAVKVTPAHDFNDFEVGKRHGLEMITVIGPD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 619 GALVNVPPPFLGLPRFEARKAVLAALKEQGLFRGIKDNPMVVPLCNRSKDVVEPLLRPQWYVRCGEMAQAASAAVTRGDL 698
Cdd:PRK14900 316 GRMTAEAGPLAGLDRFEARKEVKRLLAEQGLDRGAKPHVLPLGRCQRSATILEPLLSDQWYVRIEPLARPAIEAVEQGRT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 699 RILPEAHQRTWHSWMDNIRDWCISRQLWWGHRIPAYFItvhdpavppgedPDGRYWVSGRTEAEAREKAAREFgvspdki 778
Cdd:PRK14900 396 RFIPEQWTNTYMAWMRNIHDWCISRQLWWGHQIPAWYC------------PDGHVTVARETPEACSTCGKAEL------- 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 779 slQQDEDVLDTWFSSGLFPFSIFGWPNQSEDLSVFYPGTLLETGHDILFFWVARMVMLGLKLTEKLPFREVYLHAIVRDA 858
Cdd:PRK14900 457 --RQDEDVLDTWFSSGLWPFSTMGWPEQTDTLRTFYPTSVMETGHDIIFFWVARMMMMGLHFMGEVPFRTVYLHPMVRDE 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 859 HGRKMSKSLGNVIDPLDVihgvslqglhdqllnsnldpsevekakegqradfpagIPECGTDALRFGLCAYTSQGRDINL 938
Cdd:PRK14900 535 KGQKMSKTKGNVIDPLVI-------------------------------------TEQYGADALRFTLAALTAQGRDIKL 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 939 DVNRILGYRHFCNKLWNATKFALRGLGkGFVPSPTSKPEGHESLVDRWIRSRLAEAVRLSNEGFQAYDFPAVTTAQYSFW 1018
Cdd:PRK14900 578 AKERIEGYRAFANKLWNASRFALMNLS-GYQERGEDPARLARTPADRWILARLQRAVNETVEALEAFRFNDAANAVYAFV 656
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 1019 LYELCDVYLECLKPVLNGVDQVAADCARQTLYTCLDVGLRLLSPFMPFVTEELFQRLP--RRTPNAPASLCVTPYPEPSE 1096
Cdd:PRK14900 657 WHELCDWYIELAKEALASEDPEARRSVQAVLVHCLQTSYRLLHPFMPFITEELWHVLRaqVGASAWADSVLAAEYPRKGE 736
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 1097 CswkDPEAEAALELALSITRAVRSLRADYNLT-----RTRPDCFLEVADEATGALASAVS-AYVQTLASAGVVAVLALGA 1170
Cdd:PRK14900 737 A---DEAAEAAFRPVLGIIDAVRNIRGEMGIPwkvklGAQAPVEIAVADPALRDLLQAGElARVHRVAGVEGSRLVVAAA 813
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 1171 PAPQGCAVAVASDRCSIHLQLQGLVDPARELGKLQAKRSEAQRQAQRLQERRAASGYSAKVPLEVQEADEVKLQQTEAEL 1250
Cdd:PRK14900 814 TAPAPQSAVGVGPGFEVRVPLAGVIDLAAETARVDKEIGKVDQDLAVLERKLQNPSFVQNAPPAVVEKDRARAEELREKR 893
|
....*....
gi 564396916 1251 RKVDEAIAL 1259
Cdd:PRK14900 894 GKLEAHRAM 902
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
310-1263 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 715.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 310 YPWWERQGFFKPEYGRPSvsapNPrgvFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQ 389
Cdd:PLN02943 70 YNWWESQGYFKPNFDRGG----DP---FVIPMPPPNVTGSLHMGHAMFVTLEDIMVRYNRMKGRPTLWIPGTDHAGIATQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 390 VVVEKKLWKErGLNRHQLGREAFLQEVWKWKAEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSATVTEAFVRLHEEGVIY 469
Cdd:PLN02943 143 LVVEKMLASE-GIKRTDLGRDEFTKRVWEWKEKYGGTITNQIKRLGASCDWSRERFTLDEQLSRAVVEAFVRLHEKGLIY 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 470 RSTRLVNWSCTLNSAISDIEVDKKEltgrtllsvpgykekvEFGVLVSFAYKVQGSdSDEEVVVATTRIETMLGDVAVAV 549
Cdd:PLN02943 222 QGSYMVNWSPNLQTAVSDLEVEYSE----------------EPGTLYYIKYRVAGG-SEDFLTIATTRPETLFGDVAIAV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 550 HPKDPRYQHLKGKSVVHPF-LSRSLPIVFDDFVDMEFGTGAVKITPAHDQNDYEVGQRHRLEAISIMDSKGALVNVPppf 628
Cdd:PLN02943 285 NPEDDRYSKYIGKMAIVPMtYGRHVPIIADRYVDKDFGTGVLKISPGHDHNDYLLARKLGLPILNVMNKDGTLNEVA--- 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 629 lGLPRFEARKAVLAALKEQGLfrGIKDNP--MVVPLCNRSKDVVEPLLRPQWYVRCGEMAQAASAAVTRGDLRILPEAHQ 706
Cdd:PLN02943 362 -GLYWFEAREKLWSDLEETGL--AVKKEPhtLRVPRSQRGGEVIEPLVSKQWFVTMEPLAEKALKAVENGELTIIPERFE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 707 RTWHSWMDNIRDWCISRQLWWGHRIPAYFITvhdpavppGEDPDGRYWVSgRTEAEAREKAAREFGVSpdkISLQQDEDV 786
Cdd:PLN02943 439 KIYNHWLSNIKDWCISRQLWWGHRIPVWYIV--------GKDCEEDYIVA-RSAEEALEKAREKYGKD---VEIYQDPDV 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 787 LDTWFSSGLFPFSIFGWPNQS-EDLSVFYPGTLLETGHDILFFWVARMVMLGLKLTEKLPFREVYLHAIVRDAHGRKMSK 865
Cdd:PLN02943 507 LDTWFSSALWPFSTLGWPDVSaEDFKKFYPTTVLETGHDILFFWVARMVMMGIEFTGTVPFSYVYLHGLIRDSQGRKMSK 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 866 SLGNVIDPLDVIHgvslqglhdqllnsnldpsevekakegqradfpagipECGTDALRFGLCAYTSqGRDINLDVNRILG 945
Cdd:PLN02943 587 TLGNVIDPLDTIK-------------------------------------EFGTDALRFTLALGTA-GQDLNLSTERLTS 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 946 YRHFCNKLWNATKFALRGLgkgfvPSPTS----------KPEGHESLV-----DRWIRSRLAEAVRLSNEGFQAYDFPAV 1010
Cdd:PLN02943 629 NKAFTNKLWNAGKFVLQNL-----PSQSDtsawehilacKFDKEESLLslplpECWVVSKLHELIDSVTTSYDKYFFGDV 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 1011 TTAQYSFWLYELCDVYLECLKPVLNGV-DQVAADCARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRTpnapASLCVT 1089
Cdd:PLN02943 704 GREIYDFFWSDFADWYIEASKTRLYHSgDNSALSRAQAVLLYVFENILKLLHPFMPFVTEELWQALPYRK----EALIVS 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 1090 PYPEPSECswKDPEAEAALELALSITRAVRSLRADYNLTRTRPDCFLEVADEATGALASAVSAYVQTLASAGVVAVLALG 1169
Cdd:PLN02943 780 PWPQTSLP--KDLKSIKRFENLQSLTRAIRNARAEYSVEPAKRISASIVASAEVIEYISKEKEVLALLSRLDLQNVHFTD 857
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 1170 AP---APQGCAVaVASDRCSIHLQLQGLVDPARELGKLQAKRSEAQRQAQRLQERRAASGYSAKVPLEVQEADEVKLQQT 1246
Cdd:PLN02943 858 SPpgdANQSVHL-VASEGLEAYLPLADMVDISAEVERLSKRLSKMQTEYDALAARLSSPKFVEKAPEDVVRGVREKAAEA 936
|
970
....*....|....*..
gi 564396916 1247 EAELRKVDEAIALFQKM 1263
Cdd:PLN02943 937 EEKIKLTKNRLAFLKST 953
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
308-939 |
0e+00 |
|
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.
Pssm-ID: 459685 [Multi-domain] Cd Length: 602 Bit Score: 684.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 308 AWYPWWERQGFFKPEygrpsVSAPNPRGVFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIA 387
Cdd:pfam00133 1 QIYEFWDEQGYFKPE-----LEKRKGKPSFTIHDGPPNATGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 388 TQVVVEKKLWKERGLNRHQLGREAFLQEVWKWKAEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSATVTEAFVRLHEEGV 467
Cdd:pfam00133 76 TEQVVEKKLGIKEKKTRHKYGREEFREKCREWKMEYADEIRKQFRRLGRSIDWDREYFTMDPELEAAVWEVFVRLHDKGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 468 IYRSTRLVNWSCTLNSAISDIEVDKKELTgrtllsvpgykekvefGVLVSFAYKVQGsDSDEEVVVATTRIETMLGDVAV 547
Cdd:pfam00133 156 IYRGKKLVNWSPALNTALSNLEVEYKDVK----------------GPSIHVAFPLAD-DEGASLVIWTTTPWTLPGNTAV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 548 AVHP-------------------------------KDPRYQHLKGKSVVHPFLSRSLPIVFDDFVDMEFGTGAVKITPAH 596
Cdd:pfam00133 219 AVNPefdyvitgegyilaeallkslykkgtdkkilEDFRGKELEGKEAIHPFVNREIPIITDDYVDMEFGTGAVHIAPAH 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 597 DQNDYEVGQRHRLEAISIMDSKGALVNVPPPFLGLPRFEARKAVLAALKEQGLFRGIKDNPMVVPLCNRSKDVVEPLLRP 676
Cdd:pfam00133 299 GENDYEVGQRHNLEVINPVDDDGTFTEEAPDFQGVYRFDARKKIVELLTEKGLLLKIEPFTHSYPFCWRSGTPIIPRATP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 677 QWYVRCGEMAQAASAAVTrgDLRILPEAHQRTWHSWMDNIRDWCISRQLWWGHRIPAYFITVHDPAVPPGEdpdGRYWVS 756
Cdd:pfam00133 379 QWFVRMDELADQALEAVE--KVQFVPKSGEKRYFNWLANIQDWCISRQRWWGHPIPAWVSKDTEEVVCRGE---LFELVA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 757 GRTEAEAREKA-AREFG--VSPDKISLQQDEDVLDTWFSSGLFPFSIFGWPNQS-EDLSVFYPGTLLETGHDILFFWVAR 832
Cdd:pfam00133 454 GRFEEEGSIKWlHREAKdkLGYGKGTLEQDEDVLDTWFSSGSWPFSTLGWPFVNtEEFKKFFPADMLLEGSDQTRGWFYR 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 833 MVMLGLKLTEKLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVIHgvslqglhdqllnsnldpsevekakegqradfpa 912
Cdd:pfam00133 534 MIMLSTALTGSVPFKNVLVHGLVRDEQGRKMSKSLGNVIDPLDVID---------------------------------- 579
|
650 660
....*....|....*....|....*..
gi 564396916 913 gipECGTDALRFGLCaYTSQGRDINLD 939
Cdd:pfam00133 580 ---KYGADALRLWLA-NSDYGRDINLS 602
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
335-938 |
0e+00 |
|
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) catalytic core domain. This enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. ValRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 185677 [Multi-domain] Cd Length: 382 Bit Score: 611.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 335 GVFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKKLWKERGlNRHQLGREAFLQ 414
Cdd:cd00817 1 PVFVIDTPPPNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGIATQVVVEKKLGIEGK-TRHDLGREEFLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 415 EVWKWKAEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSATVTEAFVRLHEEGVIYRSTRLVNWSCTLNSAISDIEVdkke 494
Cdd:cd00817 80 KCWEWKEESGGKIREQLKRLGASVDWSREYFTMDPGLSRAVQEAFVRLYEKGLIYRDNRLVNWCPKLRTAISDIEV---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 495 ltgrtllsvpgykekvefgvlvsfaykvqgsdsdeevvvattrietmlgdvavavhpkdpryqhlkgksvvhpflsrslp 574
Cdd:cd00817 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 575 ivfddfvdmefgtgavkitpahdqndyevgqrhrleaisimdskgalvnvpppflglprfearkavlaalkeqglfrgik 654
Cdd:cd00817 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 655 dnpmvvplCNRSKDVVEPLLRPQWYVRCGEMAQAASAAVTRGDLRILPEAHQRTWHSWMDNIRDWCISRQLWWGHRIPAY 734
Cdd:cd00817 156 --------CSRSGDVIEPLLKPQWFVKVKDLAKKALEAVKEGDIKFVPERMEKRYENWLENIRDWCISRQLWWGHRIPAW 227
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 735 FItvhdpavppgedPDGRYWVSGRTEAEAREKAAREFGVSPDKISLQQDEDVLDTWFSSGLFPFSIFGWPNQSEDLSVFY 814
Cdd:cd00817 228 YC------------KDGGHWVVAREEDEAIDKAAPEACVPCGGEELKQDEDVLDTWFSSSLWPFSTLGWPEETKDLKKFY 295
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 815 PGTLLETGHDILFFWVARMVMLGLKLTEKLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVihgvslqglhdqllnsnl 894
Cdd:cd00817 296 PTSLLVTGHDIIFFWVARMIMRGLKLTGKLPFKEVYLHGLVRDEDGRKMSKSLGNVIDPLDV------------------ 357
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 564396916 895 dpsevekakegqradfpagIPECGTDALRFGLCAYTSQGRDINL 938
Cdd:cd00817 358 -------------------IDGYGADALRFTLASAATQGRDINL 382
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
295-1174 |
1.39e-137 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 439.24 E-value: 1.39e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 295 TMPDSYSPQYVEAAWYPWWERQG--FFKPEYGRPsvsapnprgVFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRG 372
Cdd:PRK13208 5 ELPKKYDPEELEEKWQKIWEEEGtyKFDPDERKP---------VYSIDTPPPTVSGSLHIGHVFSYTHTDFIARYQRMRG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 373 ETTLWNPGCDHAGIATQVVVEKKLwkerGLNRHQLGREAFLQ--EVWKWKAEKGDRiyHQLKKLGSSLDWDRACFTMDPK 450
Cdd:PRK13208 76 YNVFFPQGWDDNGLPTERKVEKYY----GIRKDDISREEFIElcRELTDEDEKKFR--ELWRRLGLSVDWSLEYQTISPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 451 LSATVTEAFVRLHEEGVIYRSTRLVNWSCTLNSAISDIEVDKKELTGRtllsvpgykekvefgvLVSFAYKVQGsdsDEE 530
Cdd:PRK13208 150 YRRISQKSFLDLYKKGLIYRAEAPVLWCPRCETAIAQAEVEYREREGK----------------LNYIKFPVED---GEE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 531 VVVATTRIETMLGDVAVAVHPKDPRYQHLKGKSVVHPFLSRSLPIVFDDFVDMEFGTGAVKITPAHDQNDYEVGQRHRLE 610
Cdd:PRK13208 211 IEIATTRPELLPACVAVVVHPDDERYKHLVGKTAIVPLFGVEVPILADPLVDPDFGTGAVMICTFGDKTDVTWWRELNLP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 611 AISIMDSKGALVNVPPPFLGLPRFEARKAVLAALKEQGLFRGIKDNPMVVPLCNRSKDVVEPLLRPQWYVRCGEMAQAAs 690
Cdd:PRK13208 291 TRIIIDEDGRMTEAAGKLAGLTIEEARKKIVEDLKSGGLLGKQEPIKHNVKFCERCDTPLEILVTRQWFIKVLDLKEEL- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 691 aaVTRGD-LRILPEAHQRTWHSWMDNIR-DWCISRQ--------LWW----GHRIPA----YFItvhDPA--VPPGEDPD 750
Cdd:PRK13208 370 --LERGKeINWYPEHMRVRLENWIEGLNwDWCISRQryfgtpipVWYckdcGHPILPdeedLPV---DPTkdEPPGYKCP 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 751 GRywvsGRTEAEArekaarefgvspdkislqqDEDVLDTWFSSGLFPFSIFGWPNQSEDLSVFYPGTLLETGHDILFFW- 829
Cdd:PRK13208 445 QC----GSPGFEG-------------------ETDVMDTWATSSITPLIVTGWERDEDLFEKVFPMDLRPQGHDIIRTWl 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 830 ---VARMVMLglklTEKLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVIhgvslqglhdqllnsnldpsevekakegq 906
Cdd:PRK13208 502 fytILRAYLL----TGKLPWKNIMISGMVLDPDGKKMSKSKGNVVTPEELL----------------------------- 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 907 radfpagiPECGTDALRFGLcAYTSQGRDINLDVNRI-LGYRhFCNKLWNATKFALrGLGKGFVPSPTSKPEghesLVDR 985
Cdd:PRK13208 549 --------EKYGADAVRYWA-ASARLGSDTPFDEKQVkIGRR-LLTKLWNASRFVL-HFSADPEPDKAEVLE----PLDR 613
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 986 WIRSRLAEAVRLSNEGFQAYDFPAVTTAQYSFWLYELCDVYLECLKPVL-NGVDQVAADCARQTLYTCLDVGLRLLSPFM 1064
Cdd:PRK13208 614 WILAKLAKVVEKATEALENYDFAKALEEIESFFWHVFCDDYLELVKSRAyGEDEEEEQKSARYTLYTVLDTLLRLLAPFL 693
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 1065 PFVTEELFQRLPRRtpnapaSLCVTPYPEPSEcSWKDPEAEAALELALSITRAVRSLRADYNLTRTRPdcfLEVADEATG 1144
Cdd:PRK13208 694 PFITEEVWSWLYGG------SVHRASWPEPDE-ELIDEEDEELGELAKEILSAVRKYKSEAGLSLNAP---LKKVEVYGP 763
|
890 900 910
....*....|....*....|....*....|
gi 564396916 1145 ALASAVSAYVQTLASAGVVAVLALGAPAPQ 1174
Cdd:PRK13208 764 ADLELLEAAEEDLKAAGNIEELELVEGDPE 793
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
343-1149 |
1.59e-84 |
|
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439830 [Multi-domain] Cd Length: 931 Bit Score: 296.61 E-value: 1.59e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 343 PPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCD-HaGIATQVVVEKKLwkerGLNR---HQLGREAFLQE--- 415
Cdd:COG0060 54 PPYANGDIHIGHALNKILKDIIVRYKTMRGFDVPYVPGWDcH-GLPIELKVEKEL----GIKKkdiEKVGIAEFREKcre 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 416 -VWKWKAEKGDriyhQLKKLGSSLDWDRACFTMDPKLSATVTEAFVRLHEEGVIYRSTRLVNWSCTLNSAISDIEVdkke 494
Cdd:COG0060 129 yALKYVDEQRE----DFKRLGVWGDWDNPYLTMDPEYEESIWWALKKLYEKGLLYKGLKPVPWCPRCGTALAEAEV---- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 495 ltgrtllsvpGYKEKVEFGVLVSFayKVQGS-----DSDEEVVVATTRIETMLGDVAVAVHP---------KDPRY---- 556
Cdd:COG0060 201 ----------EYKDVTSPSIYVKF--PVKDEkalllLEDAYLVIWTTTPWTLPANLAVAVHPdidyvlvevTGGERlila 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 557 ------------------------QHLKGKSVVHPFL-----SRSLPIVFDDFVDMEFGTGAVKITPAHDQNDYEVGQRH 607
Cdd:COG0060 269 ealveavlkelgiedyevlatfkgAELEGLRYEHPFYyvvgyDRAHPVILGDYVTTEDGTGIVHTAPGHGEDDFEVGKKY 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 608 RLEAISIMDSKGALVNVPPPFLGLPRFEARKAVLAALKEQG-LFRGIKdnpmVV---PLCNRSKdvvEPLL---RPQWYV 680
Cdd:COG0060 349 GLPVLNPVDDDGRFTEEAPLFAGLFVKDANPAIIEDLKERGaLLAREK----IThsyPHCWRCK---TPLIyraTPQWFI 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 681 RCGEMAQAASAAVTR-------GDLRIlpeahqrtwHSWMDNIRDWCISRQLWWGHRIPAYfitVHDPavpPGEDPDGRY 753
Cdd:COG0060 422 SMDKLRDRALEAIEKvnwipewGEGRF---------GNMLENRPDWCISRQRYWGVPIPIW---VCED---CGELHRTEE 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 754 WVSGRTEAEAREKAAREFGVSPDKISLQQD-------------EDVLDTWFSSGLFPFSIFgwpNQSEDLSvfYPGTL-L 819
Cdd:COG0060 487 VIGSVAELLEEEGADAWFELDLHRPFLDETlkcpkcggtmrrvPDVLDVWFDSGSMHFAVL---ENREELH--FPADFyL 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 820 EtGHD---------ILffwvarmvmLGLKLTEKLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVIhgvslqglhDQLl 890
Cdd:COG0060 562 E-GSDqtrgwfyssLL---------TSTALFGRAPYKNVLTHGFVLDEDGRKMSKSLGNVVDPQEVI---------DKY- 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 891 nsnldpsevekakegqradfpagipecGTDALRFgLCAYTSQGRDINLDVNRILGYRHFCNKLWNATKFALRGLGkGFVP 970
Cdd:COG0060 622 ---------------------------GADILRL-WVASSDYWGDLRFSDEILKEVRDVYRRLRNTYRFLLANLD-DFDP 672
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 971 SPTSKPEGHESLVDRWIRSRLAEAVRLSNEGFQAYDFPAVTTAqysfwLYELCDV-----YLECLKPVL--NGVDQVAAD 1043
Cdd:COG0060 673 AEDAVPYEDLPELDRWILSRLNELIKEVTEAYDNYDFHRAYRA-----LHNFCVEdlsnwYLDISKDRLytEAADSLDRR 747
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 1044 CARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRrtpNAPASLCVTPYPEPSEcSWKDPeaeaalelalsitravrSLRA 1123
Cdd:COG0060 748 AAQTTLYEVLETLVRLLAPILPFTAEEIWQNLPG---EAEESVHLADWPEVDE-ELIDE-----------------ELEA 806
|
890 900
....*....|....*....|....*.
gi 564396916 1124 DYNLTRtrpdcflEVADEATGALASA 1149
Cdd:COG0060 807 KWDLVR-------EVRSAVLKALEAA 825
|
|
| Anticodon_Ia_Val |
cd07962 |
Anticodon-binding domain of valyl tRNA synthetases; This domain is found in valyl tRNA ... |
938-1075 |
1.57e-61 |
|
Anticodon-binding domain of valyl tRNA synthetases; This domain is found in valyl tRNA synthetases (ValRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. ValRS catalyzes the transfer of valine to the 3'-end of its tRNA.
Pssm-ID: 153416 [Multi-domain] Cd Length: 135 Bit Score: 206.25 E-value: 1.57e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 938 LDVNRILGYRHFCNKLWNATKFALRGLGKGFVPSPTSKPEgheSLVDRWIRSRLAEAVRLSNEGFQAYDFPAVTTAQYSF 1017
Cdd:cd07962 1 FDEKRVEGGRNFCNKLWNAARFVLMNLEDDDEPEEDPESL---SLADRWILSRLNKTVEEVTEALENYRFSEAATALYEF 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 564396916 1018 WLYELCDVYLECLKPVLNGVDQVAADCARQTLYTCLDVGLRLLSPFMPFVTEELFQRL 1075
Cdd:cd07962 78 FWNDFCDWYLELVKPRLYGEDEEEKKAARATLYYVLETILRLLHPFMPFITEELWQRL 135
|
|
| GST_C_ValRS_N |
cd10294 |
Glutathione S-transferase C-terminal-like, alpha helical domain of vertebrate Valyl-tRNA ... |
92-213 |
3.59e-60 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of vertebrate Valyl-tRNA synthetase; Glutathione S-transferase (GST) C-terminal domain family, Valyl-tRNA synthetase (ValRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of human ValRS and its homologs from other vertebrates such as frog and zebrafish. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. They typically form large stable complexes with other proteins. ValRS forms a stable complex with Elongation Factor-1H (EF-1H), and together, they catalyze consecutive steps in protein biosynthesis, tRNA aminoacylation and its transfer to EF. The GST_C-like domain of ValRS from higher eukaryotes is likely involved in protein-protein interactions, to mediate the formation of the multi-aaRS complex that acts as a molecular hub to coordinate protein synthesis. ValRSs from prokaryotes and lower eukaryotes, such as fungi and plants, do not appear to contain this GST_C-like domain.
Pssm-ID: 198327 [Multi-domain] Cd Length: 123 Bit Score: 201.60 E-value: 3.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 92 AAVLVQQWVSYADTELTPAACGATLPALGLRG-PGQDPQAALGALGKALNPLEEWLRLHTYLAGDAPTLADLAAVTALLL 170
Cdd:cd10294 1 ACALVWQWVSFADNELTPAACAAAFPLLGLSGsDKQNQQRSLAELQRVLKVLDCYLKLRTYLVGEAITLADIAVACALLL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 564396916 171 PFRYVLDPSARRIWGNVTRWFNTCVRQPEFRAVLGEVVLYSGA 213
Cdd:cd10294 81 PFKYVLDPARRESLLNVTRWFLTCVNQPEFLAVLGEVSLCEKA 123
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
336-877 |
8.88e-50 |
|
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases. These class I enzymes are all monomers. However, in some species, MetRS functions as a homodimer, as a result of an additional C-terminal domain. These enzymes aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. Enzymes in this subfamily share an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. MetRS has a significantly shorter insertion, which lacks the editing function.
Pssm-ID: 185674 [Multi-domain] Cd Length: 312 Bit Score: 179.15 E-value: 8.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 336 VFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKKLwkerGLNRHQLGREAFLQE 415
Cdd:cd00668 1 KFYVTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKG----GRKKKTIWIEEFRED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 416 VWKWKAEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSATVTEAFVRLHEEGviyrstrlvnwsctlnsaisdievdkkel 495
Cdd:cd00668 77 PKEFVEEMSGEHKEDFRRLGISYDWSDEYITTEPEYSKAVELIFSRLYEKG----------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 496 tgrtllsvpgykekvefgvlvsFAYKvqgsdsDEEVVVATtrietmlgdvavavhpkdpryqhlkgksvvhpflsrslpi 575
Cdd:cd00668 128 ----------------------LIYR------GTHPVRIT---------------------------------------- 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 576 vfddfvdmefgtgavkitpahdqndyevgqrhrleaisimdskgalvnvpppflglprfearkavlaalkeqglfrgikd 655
Cdd:cd00668 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 656 npmvvplcnrskdvvepllrPQWYVRCGEMAQAASAAVTRGDlrILPEAHQRTWHSWMDNIRDWCISRQLWWGHRIPayf 735
Cdd:cd00668 140 --------------------EQWFFDMPKFKEKLLKALRRGK--IVPEHVKNRMEAWLESLLDWAISRQRYWGTPLP--- 194
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 736 itvhdpavppgedpdgrywvsgrteaearekaarefgvspdkislqqdEDVLDTWFSSGLFPFSIFGWPNQSEDLSVFYP 815
Cdd:cd00668 195 ------------------------------------------------EDVFDVWFDSGIGPLGSLGYPEEKEWFKDSYP 226
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564396916 816 GTLLETGHDILFFWVARMVMLGLKLTEKLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVI 877
Cdd:cd00668 227 ADWHLIGKDILRGWANFWITMLVALFGEIPPKNLLVHGFVLDEGGQKMSKSKGNVIDPSDVV 288
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
312-1099 |
5.10e-46 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 180.35 E-value: 5.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 312 WWERQGFFKpeygrpSVSAPNPRGVFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVV 391
Cdd:PLN02843 15 LWEENQVYK------RVSDRNNGESFTLHDGPPYANGDLHIGHALNKILKDFINRYQLLQGKKVHYVPGWDCHGLPIELK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 392 VEKKLWKERglnRHQLGREAFLQEVWKWKAEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSATVTEAFVRLHEEGVIYRS 471
Cdd:PLN02843 89 VLQSLDQEA---RKELTPIKLRAKAAKFAKKTVDTQRESFKRYGVWGDWENPYLTLDPEYEAAQIEVFGQMFLNGYIYRG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 472 TRLVNWSCTLNSAISDIEVDKKEltgrtllsvpGYKEKVEFGVL-VSFAYKVQGSDSDE-----EVVVATTRIETMLGDV 545
Cdd:PLN02843 166 RKPVHWSPSSRTALAEAELEYPE----------GHVSKSIYVAFpVVSPSETSPEELEEflpglSLAIWTTTPWTMPANA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 546 AVAVHPK-------------------------------DPRYQHL------------------------KGKSVV----- 565
Cdd:PLN02843 236 AVAVNDKlqysvvevqsfsedestsggnkkkrpgnvlkEQQKLFLivatdlvpaleakwgvklvvlktfPGSDLEgcryi 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 566 HPFLSRSLPIVFD-DFVDMEFGTGAVKITPAHDQNDYEVGQRHRLEAISIMDSKGALVNVPPPFLGLPRF-EARKAVLAA 643
Cdd:PLN02843 316 HPLYNRESPVVIGgDYITTESGTGLVHTAPGHGQEDYITGLKYGLPLLSPVDDAGKFTEEAGQFSGLSVLgEGNAAVVEA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 644 LKEQGLFrgIKDNPMV--VPLCNRSKdvvEP-LLRP--QWYVRCGEMAQAASAAVtrGDLRILPEAHQRTWHSWMDNIRD 718
Cdd:PLN02843 396 LDEAGSL--LMEEAYGhkYPYDWRTK---KPtIFRAteQWFASVEGFRQAALDAI--DKVKWIPAQGENRIRAMVSGRSD 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 719 WCISRQLWWGHRIPAYF------------ITVHDPAVPPGEDPDGrYW---VSGRTEAEAREKAARefgvspdkisLQQD 783
Cdd:PLN02843 469 WCISRQRTWGVPIPVFYhvetkeplmneeTIAHVKSIVAQKGSDA-WWymdVEDLLPEKYRDKASD----------YEKG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 784 EDVLDTWFSSGlfpFSIFGWPNQSEDLSvfYPGTLLETGHDILFFWVARMVMLGLKLTEKLPFREVYLHAIVRDAHGRKM 863
Cdd:PLN02843 538 TDTMDVWFDSG---SSWAGVLGSREGLS--YPADLYLEGSDQHRGWFQSSLLTSVATKGKAPYKSVLTHGFVLDEKGFKM 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 864 SKSLGNVIDPLDVIHGVSlqglhdqllNSNLDPSEvekakegqradfpagipecGTDALRFGLCA--YTSqgrDINLDVN 941
Cdd:PLN02843 613 SKSLGNVVDPRLVIEGGK---------NQKQEPAY-------------------GADVLRLWVASvdYTG---DVLIGPQ 661
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 942 rIL-----GYRhfcnKLWNATKFALRGLGKgFVPSPTSKpegHESL--VDRWIRSRLAEAVRLSNEGFQAYDFPAVTTAQ 1014
Cdd:PLN02843 662 -ILkqmsdIYR----KLRGTLRYLLGNLHD-WKPDNAVP---YEDLpsIDKYALFQLENVVNEIEESYDNYQFFKIFQIL 732
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 1015 YSFWLYELCDVYLECLKPVL--NGVDQVAADCARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRTPNAPA-SLCVTPY 1091
Cdd:PLN02843 733 QRFTIVDLSNFYLDVAKDRLyvGGTTSFTRRSCQTVLAAHLLSLLRAIAPILPHLAEDAWQNLPFQEDGSAAeSVFEAGW 812
|
....*...
gi 564396916 1092 PEPSEcSW 1099
Cdd:PLN02843 813 PTPNE-EW 819
|
|
| PLN02882 |
PLN02882 |
aminoacyl-tRNA ligase |
343-1096 |
1.27e-42 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215477 [Multi-domain] Cd Length: 1159 Bit Score: 170.29 E-value: 1.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 343 PPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKKLWKERGLNRHQLGREAFLQE----VWK 418
Cdd:PLN02882 46 PPFATGLPHYGHILAGTIKDIVTRYQSMTGHHVTRRFGWDCHGLPVEYEIDKKLGIKRRDDVLKMGIDKYNEEcrsiVTR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 419 WKAEKGDRIyhqlKKLGSSLDWDRACFTMDPKLSATVTEAFVRLHEEGVIYRSTRLVNWSCTLNSAISDIEVDKKeltgr 498
Cdd:PLN02882 126 YSKEWEKTV----TRTGRWIDFENDYKTMDPKFMESVWWVFKQLFEKGLVYKGFKVMPYSTACKTPLSNFEAGLN----- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 499 tllsvpgYKEKVEFGVLVSFAykVQGsDSDEEVVVA-TTRIETMLGDVAVAVHPK------------------DPRYQHL 559
Cdd:PLN02882 197 -------YKDVSDPAVMVSFP--IVG-DPDNASFVAwTTTPWTLPSNLALCVNPNftyvkvrnkytgkvyivaESRLSAL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 560 --------------------------KGKSVV-------HPFLSRSLPIVF----DDFVDMEFGTGAVKITPAHDQNDYE 602
Cdd:PLN02882 267 ptakpkskkgskpenaaegyevlakvPGSSLVgkkyeplFDYFSEFSDTAFrvvaDDYVTDDSGTGVVHCAPAFGEDDYR 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 603 VGQRHRL-----EAISIMDSKGALVNVPPPFLGLPRFEARKAVLAALKEQGlfRGIKDNPMV--VPLCNRSKdvvEPLLR 675
Cdd:PLN02882 347 VCLANGIiekggNLPVPVDDDGCFTEKVTDFSGRYVKDADKDIIAAIKAKG--RLVKSGSIThsYPFCWRSD---TPLIY 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 676 ---PQWYVRCGEMAQaasaavtrgdlRILPEAHQRTW----------HSWMDNIRDWCISRQLWWGHRIPAYFitvhdpa 742
Cdd:PLN02882 422 ravPSWFVKVEEIKD-----------RLLENNKQTYWvpdyvkekrfHNWLENARDWAVSRSRFWGTPLPIWI------- 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 743 vppgeDPDGRYWVSGRTEAEARE---------------------KAAREFGVspdkisLQQDEDVLDTWFSSGLFPFSIF 801
Cdd:PLN02882 484 -----SDDGEEVVVIGSIAELEKlsgvkvtdlhrhfidhitipsSRGPEFGV------LRRVDDVFDCWFESGSMPYAYI 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 802 GWPNQSEDLsvF---YPGTLLETGHDILFFWVARMVMLGLKLTEKLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVIH 878
Cdd:PLN02882 553 HYPFENKEL--FeknFPADFVAEGLDQTRGWFYTLMVLSTALFDKPAFKNLICNGLVLAEDGKKMSKSLKNYPDPNEVID 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 879 GVSLQGLHDQLLNSnldpsevekakegqradfpagiPECGTDALRFGLCAYTSQGRDINLD-VNrilGYRHFcnkLWNAT 957
Cdd:PLN02882 631 KYGADALRLYLINS----------------------PVVRAEPLRFKEEGVFGVVKDVFLPwYN---AYRFL---VQNAK 682
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 958 KFALRGLGKgFVPSPTSKPEGHESLVDRWIRSRLAEAVRLSNEGFQAYDFPAVTTAQYSFwLYELCDVYLECLKPVLNGV 1037
Cdd:PLN02882 683 RLEVEGGAP-FVPLDLAKLQNSANVLDRWINSATQSLVKFVREEMGAYRLYTVVPYLVKF-IDNLTNIYVRFNRKRLKGR 760
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 1038 DQVA-ADCARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRTPNAPASLCVTPYPEPSE 1096
Cdd:PLN02882 761 TGEEdCRTALSTLYNVLLTSCKVMAPFTPFFTEVLYQNLRKVLPGSEESIHYCSFPQVDE 820
|
|
| GST_C_EF1Bgamma_like |
cd03181 |
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ... |
92-209 |
8.96e-41 |
|
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: 146.17 E-value: 8.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 92 AAVLVQQWVSYADTELTPAACGATLPALGLRGPG-QDPQAALGALGKALNPLEEWLRLHTYLAGDAPTLADLAAVTALLL 170
Cdd:cd03181 1 EAAQVLQWISFANSELLPAAATWVLPLLGIAPYNkKAVDKAKEDLKRALGVLEEHLLTRTYLVGERITLADIFVASALLR 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 564396916 171 PFRYVLDPSARRIWGNVTRWFNTCVRQPEFRAVLGEVVL 209
Cdd:cd03181 81 GFETVLDPEFRKKYPNVTRWFNTVVNQPKFKAVFGEVKL 119
|
|
| PTZ00427 |
PTZ00427 |
isoleucine-tRNA ligase, putative; Provisional |
343-1077 |
9.94e-36 |
|
isoleucine-tRNA ligase, putative; Provisional
Pssm-ID: 173617 [Multi-domain] Cd Length: 1205 Bit Score: 148.19 E-value: 9.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 343 PPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIAtqvvVEKKLWKERGLNRhqlgREAFLQEVWKWKAE 422
Cdd:PTZ00427 110 PPFATGLPHYGHLLAGIIKDCVTRYFYQCGFSVERKFGWDCHGLP----IEYEIEKENNINK----KEDILKMGIDVYNE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 423 KGDRIYHQ--------LKKLGSSLDWDRACFTMDPKLSATVTEAFVRLHEEGVIYRSTRLVNWSCTLNSAISDIEV---- 490
Cdd:PTZ00427 182 KCRGIVLKysnewvktVERIGRWIDFKNDYKTMDKTFMESVWWVFSELYKNNYVYKSFKVMPYSCKCNTPISNFELnlny 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 491 ----------------------------DKKELTGRTLlsVPGYKEKVEFG----------------------------- 513
Cdd:PTZ00427 262 kdtpdpsiiisfvlcsdfpkveeecnieEDKQLLGEKY--SVLYNNKRENSnngnnnstnnvcyaqhseilawtttpwtl 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 514 -------VLVSFAY-KVQGSDSDEEVVVATTRIETMLGDVAVAV------------HPKDPRYQHLKGKSV-VHPFLSRS 572
Cdd:PTZ00427 340 psnlalcVNEHFTYlRIHHVKSNRVVIVGECRLEWIMKELKWNVedlkivnrfkgkELKGLRYKPLFTNFYeKYNFKERA 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 573 LPIVFDDFVDMEFGTGAVKITPAHDQNDYEVGQRHRL----EAISI--MDSKGALVNVPPPFLGLPRFEARKAVLAALKE 646
Cdd:PTZ00427 420 YKILADDFVTDDAGTGIVHCAPTYGEDDFRVCKKNGVidpeKNIFIdpLDANGYFTNEVEEVQNLYIKEADNVIKKKLKN 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 647 QGlfRGIKDNPMV--VPLCNRSKdvvEPLLR---PQWYVRcgeMAQAASAAVTRGDLRILPEAH--QRTWHSWMDNIRDW 719
Cdd:PTZ00427 500 EN--RLLSNNTIVhsYPFCWRSD---TPLIYraiPAWFIR---VSNSTNELVKNNETTYWIPAHikEKKFHNWIKDAKDW 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 720 CISRQLWWGHRIPAY-------FITVHdpAVPPGEDPDG--------RYWVSgrtEAEAREKAAREFGvspdkiSLQQDE 784
Cdd:PTZ00427 572 CISRNRYWGTPIPIWadekmetVICVE--SIKHLEELSGvknindlhRHFID---HIEIKNPKGKTYP------KLKRIP 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 785 DVLDTWFSSGLFPFSIFGWP--NQSEDLSVFYPGTLLETGHDILFFWVARMVMLGLKLTEKLPFREVYLHAIVRDAHGRK 862
Cdd:PTZ00427 641 EVFDCWFESGSMPYAKVHYPfsTEKEDFHKIFPADFIAEGLDQTRGWFYTLLVISTLLFDKAPFKNLICNGLVLASDGKK 720
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 863 MSKSLGNVIDPLDVIHGVSLQGLHDQLLNSNLDPSEVEKAKEgqradfpAGIPEcgtdALRFGLCAYTSQGRDINLDVNR 942
Cdd:PTZ00427 721 MSKRLKNYPDPLYILDKYGADSLRLYLINSVAVRAENLKFQE-------KGVNE----VVKSFILPFYHSFRFFSQEVTR 789
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 943 IlgyrhfcnKLWNATKFALRglgkgfvpspTSKPEGHESLVDRWIRSRLAEAVRLSNEGFQAYDFPAVTTAQYSFwLYEL 1022
Cdd:PTZ00427 790 Y--------ECLNKKQFLFN----------TDYIYKNDNIMDQWIFSSVQSLTKSVHTEMKAYKLYNVLPKLLQF-IENL 850
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 564396916 1023 CDVYLECLKPVLNGVdQVAADCARQ--TLYTCLDVGLRLLSPFMPFVTEELFQRLPR 1077
Cdd:PTZ00427 851 TNWYIRLNRDRMRGS-LGEENCLQSlcTTYRTLHLFTVLMAPFTPFITEYIYQQLRR 906
|
|
| leuS_bact |
TIGR00396 |
leucyl-tRNA synthetase, eubacterial and mitochondrial family; The leucyl-tRNA synthetases ... |
300-1075 |
1.12e-30 |
|
leucyl-tRNA synthetase, eubacterial and mitochondrial family; The leucyl-tRNA synthetases belong to two families so broadly different that they are represented by separate models. This model includes both eubacterial and mitochondrial leucyl-tRNA synthetases. It generates higher scores for some valyl-tRNA synthetases than for any archaeal or eukaryotic cytosolic leucyl-tRNA synthetase. Note that the enzyme from Aquifex aeolicus is split into alpha and beta chains; neither chain is long enough to score above the trusted cutoff, but the alpha chain scores well above the noise cutoff. The beta chain must be found by a model and search designed for partial length matches. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273057 [Multi-domain] Cd Length: 842 Bit Score: 131.03 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 300 YSPQYVEAAWYPWWERQGFFKPEygrpsvSAPNPRGVFMMCI-PPPnvTGSLHLGHALTNAIQDSLTRWHRMRGETTLWN 378
Cdd:TIGR00396 1 YNHIEIEEKWQQKWDENKTFKVT------DDSSKPKYYILSMfPYP--SGALHMGHVRNYTITDVLSRYYRMKGYNVLHP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 379 PGCDHAGI-ATQVVVEkklwkeRGLNRHqlgreaflqevwKWKAEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSATVTE 457
Cdd:TIGR00396 73 IGWDAFGLpAENAAIK------RGIHPA------------KWTYENIANMKKQLQALGFSYDWDREIATCDPEYYKWTQW 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 458 AFVRLHEEGVIYRSTRLVNWSCTLNSAI-------------SDIEVDKKELTgRTLLSVPGYKEKV-------------- 510
Cdd:TIGR00396 135 IFLELFEKGLAYVKEADVNWCPNDGTVLaneqvdsdgrswrGDTPVEKKELK-QWFLKITAYAEELlndleeldhwpesv 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 511 ----------EFGVLVSFAYKvqgsDSDEEVVVATTRIETMLGDVAVAVHPKDPRYQH---------------------- 558
Cdd:TIGR00396 214 kemqrnwigkSEGVEITFKIA----DHDEKITVFTTRPDTIFGVTYLALAPEHPLVEKaaennpkvaafikkilnktvae 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 559 -----------LKGKSVVHPFLSRSLPIVFDDFVDMEFGTGAVKITPAHDQNDYEVGQRHRLEAISIMDS---------- 617
Cdd:TIGR00396 290 rtkatkekkgvDTGIKAIHPLTGEKIPIWVANYVLMEYGTGAVMGVPAHDERDFEFAQKYGLPIKPVIDPaekdlsltaa 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 618 ---KGALVNvPPPFLGLPRFEARKAVLAALKEQGLfrgikdnpmvvplcnrSKDVVEpllrpqwYvrcgemaqaasaavt 694
Cdd:TIGR00396 370 yteDGVLVN-SGEFNGLNSSEARNAIIDMLEKEGK----------------GKRKVN-------Y--------------- 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 695 rgdlrilpeahqrtwhswmdNIRDWCISRQLWWGHRIPAYFITVHDPAVPPGED------------PDG-------RYWV 755
Cdd:TIGR00396 411 --------------------RLRDWGFSRQRYWGEPIPIIHCEDGGVVPVPEEDlpvilpedvvydGDGgsplsriPEWV 470
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 756 SgRTEAEAREKAAREfgvspdkislqqdEDVLDTWFSSG--LFPFSIFGWPNQSED---LSVFYPGTLLETG--HDILF- 827
Cdd:TIGR00396 471 N-VTCPSCGKPALRE-------------TDTMDTFAGSSwyYLRYLDPKNTDGPFDkekAEYWLPVDLYIGGieHAILHl 536
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 828 ----FWVARMVMLGLkLTEKLPFREVYLHAIV-----------------------RDAHGR--------KMSKSLGNVID 872
Cdd:TIGR00396 537 lyarFFHKFLRDIGY-VNTKEPFKKLINQGMVlgfyyppngkvpadvlterdekgKDKAGGelvyvgyeKMSKSKGNGID 615
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 873 PLDVIHgvslqglhdqllnsnldpsevekakegqradfpagipECGTDALRFGLCAYTSQGRDINLDVNRILGYRHFCNK 952
Cdd:TIGR00396 616 PQEIVE-------------------------------------SYGADALRLFIMFMGPIAASLEWNESGLEGARRFLDR 658
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 953 LWNatkFALRGLGKGFVPSPTSKPeghESLVDRWIRSRLAEAVRLSNEGFQ-AYDFPAVTTAQYSF----WLYELCDVYL 1027
Cdd:TIGR00396 659 VWN---LVYEITGELDAASLTVTA---LEEAQKELRRDVHKFLKKVTEDLEkRESFNTAISAMMELlnklYKAKKEALML 732
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 564396916 1028 ECLKPVlngvdqvaadcarqtlytcldvgLRLLSPFMPFVTEELFQRL 1075
Cdd:TIGR00396 733 EYLKGF-----------------------VTVLSPFAPHLAEELWEKL 757
|
|
| Anticodon_1 |
pfam08264 |
Anticodon-binding domain of tRNA ligase; This domain is found mainly hydrophobic tRNA ... |
984-1127 |
1.11e-29 |
|
Anticodon-binding domain of tRNA ligase; This domain is found mainly hydrophobic tRNA synthetases. The domain binds to the anticodon of the tRNA ligase.
Pssm-ID: 400523 [Multi-domain] Cd Length: 141 Bit Score: 115.19 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 984 DRWIRSRLAEAVRLSNEGFQAYDFPAVTTAQYSFWLYELCDVYLECLKPVLNGVDqvAADCARQTLYTCLDVGLRLLSPF 1063
Cdd:pfam08264 1 DRWILSRLNKLIKEVTEAYENYRFNTAAQALYEFFWNDLSDWYLELIKDRLYGEE--PDSRAQTTLYEVLETLLRLLAPF 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564396916 1064 MPFVTEELFQRLprrtpnapaSLCVTPYPEPSECSwkDPEAEAALELALSITRAVRSLRADYNL 1127
Cdd:pfam08264 79 MPFITEELWQKE---------SIHLAPWPEDAELE--EAELEEAFELRQEIVQAIRKLRSELKI 131
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
343-878 |
1.74e-29 |
|
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases (IleRS) catalytic core domain . This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. IleRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173909 [Multi-domain] Cd Length: 338 Bit Score: 120.80 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 343 PPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKKLWKERGLNRHQLGREAFLQEVWKWKAE 422
Cdd:cd00818 9 PPYANGLPHYGHALNKILKDIINRYKTMQGYYVPRRPGWDCHGLPIELKVEKELGISGKKDIEKMGIAEFNAKCREFALR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 423 KGDRIYHQLKKLGSSLDWDRACFTMDPKLSATVTEAFVRLHEEGVIYRSTRLVNWsctlnsaisdievdkkeltgrtlls 502
Cdd:cd00818 89 YVDEQEEQFQRLGVWVDWENPYKTMDPEYMESVWWVFKQLHEKGLLYRGYKVVPW------------------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 503 vpgykekvefgvlvsfaykvqgsdsdeevvvattrietmlgdvavavhpkdpryqhlkgksvvhpflsrslPIVFddfvd 582
Cdd:cd00818 144 -----------------------------------------------------------------------PLIY----- 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 583 mefgtgavkitpahdqndyevgqrhrleaisimdskgalvnvpppflglprfearKAVlaalkeqglfrgikdnpmvvpl 662
Cdd:cd00818 148 -------------------------------------------------------RAT---------------------- 150
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 663 cnrskdvvepllrPQWYVRCGEMAQAASAAVTRgdLRILPEAHQRTWHSWMDNIRDWCISRQLWWGHRIPAyfitvhdpa 742
Cdd:cd00818 151 -------------PQWFIRVTKIKDRLLEANDK--VNWIPEWVKNRFGNWLENRRDWCISRQRYWGTPIPV--------- 206
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 743 vppgedpdgryWVSgrteaearekaarefgVSPDKISLQQDEDVLDTWFSSGLFPFSIFGWPNQSEDLSVFYPGTLLETG 822
Cdd:cd00818 207 -----------WYC----------------EDCGEVLVRRVPDVLDVWFDSGSMPYAQLHYPFENEDFEELFPADFILEG 259
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 564396916 823 HDILFFWVARMVMLGLKLTEKLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVIH 878
Cdd:cd00818 260 SDQTRGWFYSLLLLSTALFGKAPYKNVIVHGFVLDEDGRKMSKSLGNYVDPQEVVD 315
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
296-877 |
9.54e-27 |
|
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440261 [Multi-domain] Cd Length: 826 Bit Score: 118.23 E-value: 9.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 296 MPDSYSPQYVEAAWYPWWERQGFFKpeygrpsvsAPNPRG-----VFMMcIPPPnvTGSLHLGHALTNAIQDSLTRWHRM 370
Cdd:COG0495 1 MQERYNPKEIEKKWQKYWEENGTFK---------ADEDSSkpkyyVLDM-FPYP--SGRLHMGHVRNYTIGDVVARYKRM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 371 RGETTLwNP-GCD-------HAGIATQVvvekklwkerglnrHqlgrEAflqevwKWKAEKGDRIYHQLKKLGSSLDWDR 442
Cdd:COG0495 69 QGYNVL-HPmGWDafglpaeNAAIKNGV--------------H----PA------EWTYENIANMRRQLKRLGLSYDWSR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 443 ACFTMDP-------KLsatvteaFVRLHEEGVIYRSTRLVNWSCTLN------------SAISDIEVDKKELTG------ 497
Cdd:COG0495 124 EIATCDPeyykwtqWI-------FLQLYEKGLAYRKEAPVNWCPVDQtvlaneqvidgrCWRCGAPVEKKELPQwflkit 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 498 ----RtLLS----VPGYKEKV----------EFGVLVSFAYKvqgsDSDEEVVVATTRIETMLGD--VAVAV-HP----- 551
Cdd:COG0495 197 dyadE-LLDdldkLDGWPEKVktmqrnwigrSEGAEVDFPVE----GSDEKITVFTTRPDTLFGAtfMVLAPeHPlvkel 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 552 -KDPRYQHLK--------------------------GKSVVHPFLSRSLPIVFDDFVDMEFGTGAVKITPAHDQNDYEVG 604
Cdd:COG0495 272 aTPEQNAAVAafieeakkkseiertsetkektgvftGLYAINPLTGEKIPIWIADYVLMDYGTGAVMAVPAHDQRDFEFA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 605 QRHRL-----------EAISIMDS----KGALVNvPPPFLGLPRFEARKAVLAALKEQGLfrgikdnpmvvplcnrskdv 669
Cdd:COG0495 352 KKYGLpikqviapedgDDPDILEEaytgDGVLIN-SGEFDGLDSEEAKEAIIEWLEEKGL-------------------- 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 670 vepllrpqwyvrcGEmaqaasAAVT-RgdlrilpeahqrtwhswmdnIRDWCISRQLWWGHRIPAyfitVHDP-----AV 743
Cdd:COG0495 411 -------------GK------RKVNyR--------------------LRDWLISRQRYWGEPIPI----IHCEdcgvvPV 447
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 744 P----------------PGEDPDGRY--WVS------GRteaeareKAAREFgvspdkislqqdeDVLDTWF-SSglfpf 798
Cdd:COG0495 448 PedqlpvelpedvdfdpTGGSPLARApeWVNvtcpkcGG-------PARRET-------------DTMDTFVdSS----- 502
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 799 sifgW-------PNQSE--------------DLsvfYPGtlletG--HDIL------FFWvarMVM--LGLkLTEKLPFR 847
Cdd:COG0495 503 ----WyylrytdPHNDEapfdpeaanywlpvDQ---YIG-----GieHAILhllyarFFT---KVLrdLGL-VSFDEPFK 566
|
730 740 750
....*....|....*....|....*....|....*....
gi 564396916 848 ---------EVYLHAIVRDAHGrKMSKSLGNVIDPLDVI 877
Cdd:COG0495 567 rlltqgmvlEVGKDGVVIGGIE-KMSKSKGNVVDPDEII 604
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
350-1102 |
9.14e-24 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 108.80 E-value: 9.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 350 LHLGHALTNAIQDSLTRWHRMRGETTLWnPGCDHA------GIATQV----------------VVEKKLWKerglnrhqL 407
Cdd:PRK12300 1 LHVGHGRTYTIGDVIARYKRMRGYNVLF-PMAFHVtgtpilGIAERIargdpetielykslygIPEEELEK--------F 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 408 GREAFLQEVWKWKAEKgdriyhQLKKLGSSLDWDRACFTMDPKLSATVTEAFVRLHEEGVIYRSTRLVNWSCTLNSAISD 487
Cdd:PRK12300 72 KDPEYIVEYFSEEAKE------DMKRIGYSIDWRREFTTTDPEYSKFIEWQFRKLKEKGLIVKGSHPVRYCPNDNNPVGD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 488 ieVDKKELTGrtllsvpgyKEKVEFgVLVSFAykvqgsDSDEEV-VVATTRIETMLGDVAVAVHPKDP------------ 554
Cdd:PRK12300 146 --HDLLDGEE---------PEIVEY-TLIKFE------ESEDLIlPAATLRPETIFGVTNLWVNPDATyvkaevdgekwi 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 555 ---------RYQH-------------LKGKSVVHPFLSRSLPIVFDDFVDMEFGTGAVKITPAHDQNDY----EVGQRHR 608
Cdd:PRK12300 208 vskeaaeklSFQDrdveiieeikgseLIGKKVKNPVTGKEVPILPADFVDPDNGTGVVMSVPAHAPYDYvalrDLKKNKE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 609 L----EAISIMD--------------------------------------SKGALVNVPPPFLGLPRFEARKAVLAALKE 646
Cdd:PRK12300 288 LldviEPIPLIEvegygefpakevveklgiksqedpeleeatkevyraefHKGVLKENTGEYAGKPVREAREKITKDLIE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 647 QGLfrGIK----DNPMVVPLCNrSKDVVEpLLRPQWYVRCGEMAQAASA--AVTRgdLRILPEAHQRTWHSWMDNIRDWC 720
Cdd:PRK12300 368 KGI--ADImyefSNRPVYCRCG-TECVVK-VVKDQWFIDYSDPEWKELAhkALDN--MEIIPEEYRKEFENTIDWLKDRA 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 721 ISRQLWWGHRIP-----------------AYFITVHdpavppgedpdgrywvsgrteaearekAAREFGVSPDKIslqqD 783
Cdd:PRK12300 442 CARRRGLGTRLPwdeewiieslsdstiymAYYTIAH---------------------------KIREYGIKPEQL----T 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 784 EDVLDTWFSSGLFPFSIF---GWPNQ-----SEDLSVFYPGTLLETGHD-----ILFF------------WVARMVMLGL 838
Cdd:PRK12300 491 PEFFDYVFLGKGDPEEVSkktGIPKEileemREEFLYWYPVDWRHSGKDlipnhLTFFifnhvaifpeekWPRGIVVNGF 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 839 KLTEklpfrevylhaivrdahGRKMSKSLGNVIdPLdvihgvslqglhdqllnsnldpsevEKAKEgqradfpagipECG 918
Cdd:PRK12300 571 VLLE-----------------GKKMSKSKGNVI-PL-------------------------RKAIE-----------EYG 596
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 919 TDALRFGLCAYTSQGRDINLDVNRILGYRHFCNKLWNatkFALRGLGKGfvpsptskPEGHESLVDRWIRSRLAEAVRLS 998
Cdd:PRK12300 597 ADVVRLYLTSSAELLQDADWREKEVESVRRQLERFYE---LAKELIEIG--------GEEELRFIDKWLLSRLNRIIKET 665
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 999 NEGFQAYDF-PAVTTAQYSfwLYELCDVYLEcLKPVLNgvdqvaadcaRQTLYTCLDVGLRLLSPFMPFVTEELFQRLPR 1077
Cdd:PRK12300 666 TEAMESFQTrDAVQEAFYE--LLNDLRWYLR-RVGEAN----------NKVLREVLEIWIRLLAPFTPHLAEELWHKLGG 732
|
890 900
....*....|....*....|....*
gi 564396916 1078 RTpnaPASLcvTPYPEPSEcSWKDP 1102
Cdd:PRK12300 733 EG---FVSL--EKWPEPDE-SKIDE 751
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
305-748 |
1.52e-20 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 98.36 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 305 VEAAWYPWWERQGFFK-PEygrpSVSAPNPRGVFMMCIPPPNVTGsLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDH 383
Cdd:PLN02563 85 IEPKWQRYWEENRTFRtPD----DVDTSKPKFYVLDMFPYPSGAG-LHVGHPEGYTATDILARYKRMQGYNVLHPMGWDA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 384 AGI-ATQVVVEK----KLWKERGLNRHQLgreaflqevwkwkaekgdriyhQLKKLGSSLDWDRACFTMDPKLSATVTEA 458
Cdd:PLN02563 160 FGLpAEQYAIETgthpKITTLKNIARFRS----------------------QLKSLGFSYDWDREISTTEPEYYKWTQWI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 459 FVRLHEEGVIYRSTRLVNWSCTLNSAISDIEVDK--KELTGRTLLSVP--------------------------GYKE-- 508
Cdd:PLN02563 218 FLQLLKRGLAYQAEVPVNWCPALGTVLANEEVVDglSERGGHPVIRKPmrqwmlkitayadrlledlddldwpeSIKEmq 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 509 ----------KVEFGVLvsfayKVQGSDSDEEVVVATTRIETMLGDVAVAVHPKDP------------------------ 554
Cdd:PLN02563 298 rnwigrsegaELDFSVL-----DGEGKERDEKITVYTTRPDTLFGATYLVVAPEHPllsslttaeqkeaveeyvdaasrk 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 555 ----RYQHLKGKSVV-------HPFLSRSLPIVFDDFVDMEFGTGAVKITPAHDQNDYEVGQRHRLEAISIMDS------ 617
Cdd:PLN02563 373 sdleRTELQKEKTGVftgsyaiNPATGEAIPIWVADYVLGSYGTGAIMAVPAHDTRDFEFAQKFDLPIKWVVKPadgned 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 618 --------KGALVNVPPPFL---GLPRFEARKAVLAALKEQGlfrgikdnpmvvplcNRSKDVVEPLlrpqwyvrcgema 686
Cdd:PLN02563 453 daekaytgEGVIVNSSSSGLdinGLSSKEAAKKVIEWLEETG---------------NGKKKVNYKL------------- 504
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564396916 687 qaasaavtrgdlrilpeahqrtwhswmdniRDWCISRQLWWGHRIPAYFITVHDPAVPPGED 748
Cdd:PLN02563 505 ------------------------------RDWLFARQRYWGEPIPVVFLEDSGEPVPVPES 536
|
|
| Anticodon_Ia_Ile_ABEc |
cd07961 |
Anticodon-binding domain of archaeal, bacterial, and eukaryotic cytoplasmic isoleucyl tRNA ... |
947-1096 |
4.44e-18 |
|
Anticodon-binding domain of archaeal, bacterial, and eukaryotic cytoplasmic isoleucyl tRNA synthetases; This domain is found in isoleucyl tRNA synthetases (IleRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. This family includes bacterial, archaeal, and eukaryotic cytoplasmic members. IleRS catalyzes the transfer of isoleucine to the 3'-end of its tRNA.
Pssm-ID: 153415 [Multi-domain] Cd Length: 183 Bit Score: 83.37 E-value: 4.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 947 RHFCNKLWNATKFAL--RGLgKGFVPSPTSKPEGHESLVDRWIRSRLAEAVRLSNEGFQAYDFPAVTTAQYSFWLyELCD 1024
Cdd:cd07961 11 RKVLLPLWNAYRFFVtyANL-DGFDPGKDDDAVASLNVLDRWILSRLNSLIKEVTEEMEAYDLYTAVRALLEFID-ELTN 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564396916 1025 VYL----ECLKPVLNGVDQVAAdcaRQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRTPNAPASLCVTPYPEPSE 1096
Cdd:cd07961 89 WYIrrnrKRFWGEEGDDDKLAA---YATLYEVLLTLSRLMAPFTPFITEEIYQNLRRELGDAPESVHLLDWPEVDE 161
|
|
| GST_C |
pfam00043 |
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ... |
107-198 |
2.85e-15 |
|
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants. Stringent starvation proteins in E. coli are also included in the alignment but are not known to have GST activity. The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed to reside in the N-terminal domain. In plants, GSTs are encoded by a large gene family (48 GST genes in Arabidopsis) and can be divided into the phi, tau, theta, zeta, and lambda classes.
Pssm-ID: 459647 [Multi-domain] Cd Length: 93 Bit Score: 72.32 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 107 LTPAACGATLPALGLR--GPGQDPQAALGALGKALNPLEEWLRLHTYLAGDAPTLADLAAVTALLLPFRYVLDPSaRRIW 184
Cdd:pfam00043 1 LMDLRMQIALLPYVPPeeKKEPEVDEALEKVARVLSALEEVLKGQTYLVGDKLTLADIALAPALLWLYELDPACL-REKF 79
|
90
....*....|....
gi 564396916 185 GNVTRWFNTCVRQP 198
Cdd:pfam00043 80 PNLKAWFERVAARP 93
|
|
| Anticodon_Ia_Ile_BEm |
cd07960 |
Anticodon-binding domain of bacterial and eukaryotic mitochondrial isoleucyl tRNA synthetases; ... |
946-1102 |
3.28e-13 |
|
Anticodon-binding domain of bacterial and eukaryotic mitochondrial isoleucyl tRNA synthetases; This domain is found in isoleucyl tRNA synthetases (IleRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. This family includes bacterial and eukaryotic mitochondrial members. IleRS catalyzes the transfer of isoleucine to the 3'-end of its tRNA.
Pssm-ID: 153414 [Multi-domain] Cd Length: 180 Bit Score: 69.09 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 946 YRhfcnKLWNATKFALRGLGkGFVPSPTSKPEGHESLVDRWIRSRLAEAVRLSNEGFQAYDFPAVTTAQYSFWLYELCDV 1025
Cdd:cd07960 13 YR----KIRNTFRFLLGNLN-DFDPAKDAVPYEELLELDRYALHRLNELIKEVREAYENYEFHKVYQALNNFCTVDLSAF 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564396916 1026 YLECLKPVL--NGVDQVAADCARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRTPNAPASLcvTPYPEPSEcSWKDP 1102
Cdd:cd07960 88 YLDIIKDRLycDAKDSLERRSAQTVLYHILDALLKLLAPILPFTAEEVWEHLPGEKKEESVFL--EDWPELPE-EWKDE 163
|
|
| GstA |
COG0625 |
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; |
56-206 |
9.55e-13 |
|
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440390 [Multi-domain] Cd Length: 205 Bit Score: 68.38 E-value: 9.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 56 RLPALEqgPGGLWVWGAPAVAQLLwpAGLGG-----PGGSRAAVLVQQWVSYADTELTPAAcgatLPALGLRGPGQDP-- 128
Cdd:COG0625 52 KVPVLV--DDGLVLTESLAILEYL--AERYPeppllPADPAARARVRQWLAWADGDLHPAL----RNLLERLAPEKDPaa 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564396916 129 -QAALGALGKALNPLEEWLRLHTYLAGDAPTLADLAAVTALLLPFRYVLDPSArriWGNVTRWFNTCVRQPEFRAVLGE 206
Cdd:COG0625 124 iARARAELARLLAVLEARLAGGPYLAGDRFSIADIALAPVLRRLDRLGLDLAD---YPNLAAWLARLAARPAFQRALAA 199
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
337-477 |
3.96e-12 |
|
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173906 [Multi-domain] Cd Length: 314 Bit Score: 68.81 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 337 FMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAG-----IATQVVVEKKLWKERGLNrhqlgrea 411
Cdd:cd00812 2 FYILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGlpaenAAIKIGRDPEDWTEYNIK-------- 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564396916 412 flqevwKWKAekgdriyhQLKKLGSSLDWDRACFTMDPKLSATVTEAFVRLHEEGVIYRSTRLVNW 477
Cdd:cd00812 74 ------KMKE--------QLKRMGFSYDWRREFTTCDPEYYKFTQWLFLKLYEKGLAYKKEAPVNW 125
|
|
| tRNA-synt_1_2 |
pfam13603 |
Leucyl-tRNA synthetase, Domain 2; This is a family of the conserved region of Leucine-tRNA ... |
513-640 |
1.17e-11 |
|
Leucyl-tRNA synthetase, Domain 2; This is a family of the conserved region of Leucine-tRNA ligase or Leucyl-tRNA synthetase, EC:6.1.1.4.
Pssm-ID: 433342 [Multi-domain] Cd Length: 185 Bit Score: 64.88 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 513 GVLVSFAYKvqgsDSDEEVVVATTRIETMLGD--VAVAV-HP-------KDP-------RYQHLK--------------- 560
Cdd:pfam13603 9 GAEITFPVE----GTDEKIEVFTTRPDTLMGVtfVALAPeHPlveklaeKNPevaafieECKNTSeiertsetkekegvf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 561 -GKSVVHPFLSRSLPIVFDDFVDMEFGTGAVKITPAHDQNDYEVGQRHRL------------EAISIMDS----KGALVN 623
Cdd:pfam13603 85 tGLYAIHPITGEKIPIWIANFVLMEYGTGAVMAVPAHDQRDFEFAKKYNLpikpviqpedgdLDLDIMTEayteEGILVN 164
|
170
....*....|....*..
gi 564396916 624 vPPPFLGLPRFEARKAV 640
Cdd:pfam13603 165 -SGEFDGLDSEEAKEAI 180
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
711-1075 |
1.18e-11 |
|
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439913 [Multi-domain] Cd Length: 544 Bit Score: 68.99 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 711 SWMDN-IRDWCISRQLWWGhrIPayfitvhdpaVPpgEDPDGRYWVsgrteaearekaarefgvspdkislqqdedvldt 789
Cdd:COG0143 217 SWLKEgLQDLSISRDFDWG--IP----------VP--GDPGKVFYV---------------------------------- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 790 WF-------SSglfpfsIFGWP---NQSEDLSVFYPGTLLETGH----DILFF----WVArMVM-LGLKLTEKLPfrevy 850
Cdd:COG0143 249 WFdaligyiSA------TKGYAddrGLPEDFEKYWPAPDTELVHfigkDIIRFhaiiWPA-MLMaAGLPLPKKVF----- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 851 lhaivrdAH------GRKMSKSLGNVIDPLDVIhgvslqglhdqllnsnldpsevekakegqrADFPAgipecgtDALRF 924
Cdd:COG0143 317 -------AHgfltveGEKMSKSRGNVIDPDDLL------------------------------DRYGP-------DALRY 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 925 GLCAYTSQGRDINLD-------------------VNRILGyrhFCNKLWNatkfalrglgkGFVPSPtskpeGHESLVDR 985
Cdd:COG0143 353 YLLREVPFGQDGDFSwedfvarvnsdlandlgnlASRTLS---MIHKYFD-----------GKVPEP-----GELTEADE 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 986 WIRSRLAEAVRLSNEGFQAYDFPAVTTAqysfwLYELCDV---YLECLKP-VLngVDQVAADCARQTLYTCLDVgLR--- 1058
Cdd:COG0143 414 ELLAEAEAALEEVAEAMEAFEFRKALEE-----IMALARAankYIDETAPwKL--AKDEDPERLATVLYTLLEA-LRila 485
|
410
....*....|....*...
gi 564396916 1059 -LLSPFMPFVTEELFQRL 1075
Cdd:COG0143 486 iLLKPFLPETAEKILEQL 503
|
|
| GST_C_family |
cd00299 |
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ... |
96-194 |
5.12e-09 |
|
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione S-transferase (GST) family, C-terminal alpha helical domain; a large, diverse group of cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. In addition, GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. This family, also referred to as soluble GSTs, is the largest family of GSH transferases and is only distantly related to the mitochondrial GSTs (GSTK). Soluble GSTs bear no structural similarity to microsomal GSTs (MAPEG family) and display additional activities unique to their group, such as catalyzing thiolysis, reduction and isomerization of certain compounds. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Based on sequence similarity, different classes of GSTs have been identified, which display varying tissue distribution, substrate specificities and additional specific activities. In humans, GSTs display polymorphisms which may influence individual susceptibility to diseases such as cancer, arthritis, allergy and sclerosis. Some GST family members with non-GST functions include glutaredoxin 2, the CLIC subfamily of anion channels, prion protein Ure2p, crystallins, metaxins, stringent starvation protein A, and aminoacyl-tRNA synthetases.
Pssm-ID: 198286 [Multi-domain] Cd Length: 100 Bit Score: 54.81 E-value: 5.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 96 VQQWVSYADTELTPAACGATLPALGLRGPGQDPQ-AALGALGKALNPLEEWLRLHTYLAGDAPTLADLAAVTALLLPFRY 174
Cdd:cd00299 1 VRALEDWADATLAPPLVRLLYLEKVPLPKDEAAVeAAREELPALLAALEQLLAGRPYLAGDQFSLADVALAPVLARLEAL 80
|
90 100
....*....|....*....|
gi 564396916 175 VLDPSARRIWGNVTRWFNTC 194
Cdd:cd00299 81 GPYYDLLDEYPRLKAWYDRL 100
|
|
| Anticodon_Ia_like |
cd07375 |
Anticodon-binding domain of class Ia aminoacyl tRNA synthetases and similar domains; This ... |
941-1064 |
1.52e-08 |
|
Anticodon-binding domain of class Ia aminoacyl tRNA synthetases and similar domains; This domain is found in a variety of class Ia aminoacyl tRNA synthetases, C-terminal to the catalytic core domain. It recognizes and specifically binds to the anticodon of the tRNA. Aminoacyl tRNA synthetases catalyze the transfer of cognate amino acids to the 3'-end of their tRNAs by specifically recognizing cognate from non-cognate amino acids. Members include valyl-, leucyl-, isoleucyl-, cysteinyl-, arginyl-, and methionyl-tRNA synthethases. This superfamily also includes a domain from MshC, an enzyme in the mycothiol biosynthetic pathway.
Pssm-ID: 153408 [Multi-domain] Cd Length: 117 Bit Score: 54.05 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 941 NRILGYRHFCNKLWNATKFALRGLGKGFVPSPTSKPEGheslVDRWIRSRLAEAVRLSNEGFQAYDFPAVTTAQYSFWLY 1020
Cdd:cd07375 2 ERLKQARAFLNRLYRLLSFFRKALGGTQPKWDNELLEE----ADRELLARLQEFIKRTTNALEALDPTTAVQELFKFTNE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 564396916 1021 ElcDVYLECLKPVLNGVDQVAAdcARQTLYTCLDVGLRLLSPFM 1064
Cdd:cd07375 78 L--NWYLDELKPALQTEELREA--VLAVLRAALVVLTKLLAPFT 117
|
|
| GST_C_AaRS_like |
cd10289 |
Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA ... |
93-194 |
1.11e-07 |
|
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: 50.39 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 93 AVLVQQWVSYADTeltpaacgatlpalGLRGPGQDPQAalgalgKALNPLeewLRLHTYLAGDAPTLADLaAVTALLLPF 172
Cdd:cd10289 2 AAQVDQWLDLAGS--------------LLKGKELEALL------KSLNSY---LASRTFLVGYSLTLADV-AVFSALYPS 57
|
90 100
....*....|....*....|..
gi 564396916 173 RYVLDPSARRIWGNVTRWFNTC 194
Cdd:cd10289 58 GQKLSDKEKKKFPHVTRWFNHI 79
|
|
| Anticodon_Ia_Leu_AEc |
cd07959 |
Anticodon-binding domain of archaeal and eukaryotic cytoplasmic leucyl tRNA synthetases; This ... |
971-1075 |
5.35e-07 |
|
Anticodon-binding domain of archaeal and eukaryotic cytoplasmic leucyl tRNA synthetases; This domain is found in leucyl tRNA synthetases (LeuRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain. In contrast to other class Ia enzymes, the anticodon is not used as an identity element in LeuRS (with exceptions such as Saccharomyces cerevisiae and some other eukaryotes). No anticodon-binding site can be defined for this family, which includes archaeal and eukaryotic cytoplasmic members. LeuRS catalyzes the transfer of leucine to the 3'-end of its tRNA.
Pssm-ID: 153413 [Multi-domain] Cd Length: 117 Bit Score: 49.51 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 971 SPTSKPEGHESLVDRWIRSRLAEAVRLSNEGFQAYDF-PAVTTAQYSFwlYELCDVYLEclkpvlngvdQVAADCARQTL 1049
Cdd:cd07959 24 IETEGELEELTFIDRWLLSRLNRLIKETTEAYENMQFrEALKEGLYEL--QNDLDWYRE----------RGGAGMNKDLL 91
|
90 100
....*....|....*....|....*.
gi 564396916 1050 YTCLDVGLRLLSPFMPFVTEELFQRL 1075
Cdd:cd07959 92 RRFIEVWTRLLAPFAPHLAEEIWHEL 117
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
778-1075 |
6.24e-07 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 53.73 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 778 ISLQQDED-VLDTWFSsGLFPF-SIFGWPNQSEDLSV----FYPGTLLETGHDILFF----WVARMVMLGLKLTEKlpfr 847
Cdd:PRK11893 212 IPVPGDPKhVIYVWFD-ALTNYlTALGYPDDEELLAElfnkYWPADVHLIGKDILRFhavyWPAFLMAAGLPLPKR---- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 848 eVYLHA-IVRDahGRKMSKSLGNVIDPLDVIHgvslqglhdqllnsnldpsevekakegqradfpagipECGTDALRFGL 926
Cdd:PRK11893 287 -VFAHGfLTLD--GEKMSKSLGNVIDPFDLVD-------------------------------------EYGVDAVRYFL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 927 CAYTSQGRDINLDVNRILGYR--HFCNKLWN---ATKFALRGLGKGFVPSPTSKPEGHESLVDrwirsRLAEAVRLSNEG 1001
Cdd:PRK11893 327 LREIPFGQDGDFSREAFINRInaDLANDLGNlaqRTLSMIAKNFDGKVPEPGALTEADEALLE-----AAAALLERVRAA 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 1002 FQAYDFpavTTAQYSFW-LYELCDVYLECLKPVLngvdQVAADCAR--QTLYTCLDvGLR----LLSPFMPFVTEELFQR 1074
Cdd:PRK11893 402 MDNLAF---DKALEAILaLVRAANKYIDEQAPWS----LAKTDPERlaTVLYTLLE-VLRgiavLLQPVMPELAAKILDQ 473
|
.
gi 564396916 1075 L 1075
Cdd:PRK11893 474 L 474
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
802-877 |
1.93e-06 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 52.11 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 802 GWPNQSEDLS-VFYPGTLLETGHDIL-F---FWVARMVMLGLKLteklpFREVYLHA-IVRDahGRKMSKSLGNVIDPLD 875
Cdd:PRK12267 240 GYGSDDDELFkKFWPADVHLVGKDILrFhaiYWPIMLMALGLPL-----PKKVFAHGwWLMK--DGKMSKSKGNVVDPEE 312
|
..
gi 564396916 876 VI 877
Cdd:PRK12267 313 LV 314
|
|
| GST_C_AIMP3 |
cd10305 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ... |
95-201 |
3.54e-06 |
|
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: 46.90 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 95 LVQQWVSYADTELTPAACGATLPALglrgpgqdpqaalgalgkaLNPLEEWLRLHTYLAGDAPTLADlAAVTALLLPFRY 174
Cdd:cd10305 6 QVDQWLEYRVTQVAPASDKADAKSL-------------------LKELNSYLQDRTYLVGHKLTLAD-VVLYYGLHPIMK 65
|
90 100
....*....|....*....|....*..
gi 564396916 175 VLDPSARRIWGNVTRWFNTCVRQPEFR 201
Cdd:cd10305 66 DLSPQEKEQYLNVSRWFDHVQHLPGIR 92
|
|
| GST_C_7 |
cd03206 |
C-terminal, alpha helical domain of an unknown subfamily 7 of Glutathione S-transferases; ... |
96-192 |
4.80e-06 |
|
C-terminal, alpha helical domain of an unknown subfamily 7 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 7; composed of uncharacterized proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain.
Pssm-ID: 198315 [Multi-domain] Cd Length: 100 Bit Score: 46.45 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 96 VQQWVSYADTELTPAACGATLpaLGLRGPGQDPQAALGALGKALNPLEEWLRLHTYLAGDAPTLADLAAvtalllpFRYV 175
Cdd:cd03206 1 VQRWLSFAAGEIAHGPAAARL--IHLFGAPLDPERARAISHRLLRLLDQHLAGRDWLAGDRPTIADVAC-------YPYI 71
|
90 100
....*....|....*....|....*.
gi 564396916 176 ---------LDPsarriWGNVTRWFN 192
Cdd:cd03206 72 alapeggvsLEP-----YPAIRAWLA 92
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
344-472 |
7.40e-06 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 49.98 E-value: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 344 PNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKklwkeRGLNRHQLGreaflqevwkwkAEK 423
Cdd:pfam09334 8 PYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEK-----EGITPEELV------------DRY 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 564396916 424 GDRIYHQLKKLGSSLD-WDRacfTMDPKLSATVTEAFVRLHEEGVIYRST 472
Cdd:pfam09334 71 HEIHREDFKKFNISFDdYGR---TTSERHHELVQEFFLKLYENGYIYEKE 117
|
|
| GST_C_Delta_Epsilon |
cd03177 |
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; ... |
121-198 |
8.74e-06 |
|
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The class Delta and Epsilon subfamily is made up primarily of insect GSTs, which play major roles in insecticide resistance by facilitating reductive dehydrochlorination of insecticides or conjugating them with GSH to produce water-soluble metabolites that are easily excreted. They are also implicated in protection against cellular damage by oxidative stress.
Pssm-ID: 198287 [Multi-domain] Cd Length: 117 Bit Score: 45.99 E-value: 8.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 121 LRGPGQDPQAALGALGKALNPLEEWLRLHTYLAGDAPTLADLAAVTAL----LLPFryvlDPSArriWGNVTRWFNTCVR 196
Cdd:cd03177 29 LFGGAEPPEEKLDKLEEALEFLETFLEGSDYVAGDQLTIADLSLVATVstleVVGF----DLSK---YPNVAAWYERLKA 101
|
..
gi 564396916 197 QP 198
Cdd:cd03177 102 LP 103
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
344-469 |
1.29e-05 |
|
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. 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. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function.
Pssm-ID: 173907 [Multi-domain] Cd Length: 319 Bit Score: 48.68 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 344 PNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEkklwkERGLNRHQLGRE--AFLQEVWKWka 421
Cdd:cd00814 9 PYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAE-----EEGVTPQELCDKyhEIFKDLFKW-- 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 564396916 422 ekgdriyhqlkkLGssLDWDRACFTMDPKLSATVTEAFVRLHEEGVIY 469
Cdd:cd00814 82 ------------LN--ISFDYFIRTTSPRHKEIVQEFFKKLYENGYIY 115
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
341-469 |
1.63e-05 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 49.11 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 341 IPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGiatqvvvEKKLWKERglnrhQLGREAflQEvwkWK 420
Cdd:PRK11893 7 TPIYYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFFLTGTDEHG-------QKIQRKAE-----EAGISP--QE---LA 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 564396916 421 AEKGDRIYHQLKKLGSSLDwdraCF--TMDPKLSATVTEAFVRLHEEGVIY 469
Cdd:PRK11893 70 DRNSAAFKRLWEALNISYD----DFirTTDPRHKEAVQEIFQRLLANGDIY 116
|
|
| GST_C_5 |
cd03196 |
C-terminal, alpha helical domain of an unknown subfamily 5 of Glutathione S-transferases; ... |
139-203 |
1.74e-05 |
|
C-terminal, alpha helical domain of an unknown subfamily 5 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 5; composed of uncharacterized bacterial proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain.
Pssm-ID: 198305 [Multi-domain] Cd Length: 115 Bit Score: 45.22 E-value: 1.74e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564396916 139 LNPLEEWLRLHTYLAGDAPTLADLAavtalLLPF----------RYVLDPsarriWGNVTRWFNTCVRQPEFRAV 203
Cdd:cd03196 50 LAELEARLSQHAYLFGDRPSLADYA-----IFPFvrqfahvdrdWFDASP-----YPNLRRWLNRFLQSPLFSKI 114
|
|
| Val_tRNA-synt_C |
pfam10458 |
Valyl tRNA synthetase tRNA binding arm; This domain is found at the C-terminus of Valyl tRNA ... |
1196-1258 |
2.56e-05 |
|
Valyl tRNA synthetase tRNA binding arm; This domain is found at the C-terminus of Valyl tRNA synthetases.
Pssm-ID: 431296 [Multi-domain] Cd Length: 66 Bit Score: 43.41 E-value: 2.56e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564396916 1196 DPARELGKLQAKRSEAQRQAQRLQERRAASGYSAKVPLEVQEADEVKLQQTEAELRKVDEAIA 1258
Cdd:pfam10458 1 DVEKERARLEKELAKLQKEIERVQGKLANPGFVAKAPAEVVEEEKAKLAELEEQAEKLRERLS 63
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
346-428 |
3.14e-05 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 48.26 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 346 VTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCD-H----------AGIATQVVVE------KKLWKERGL------ 402
Cdd:PRK12267 15 PNGKPHIGHAYTTIAADALARYKRLQGYDVFFLTGTDeHgqkiqqaaekAGKTPQEYVDeisagfKELWKKLDIsydkfi 94
|
90 100 110
....*....|....*....|....*....|
gi 564396916 403 ----NRHQLGREAFLQEVWkwkaEKGDrIY 428
Cdd:PRK12267 95 rttdERHKKVVQKIFEKLY----EQGD-IY 119
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
337-471 |
1.67e-04 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 45.86 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 337 FMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAG--IATQVVVEkklwkerglnrhqlGREAflq 414
Cdd:PLN02224 71 FVLTTPLYYVNAPPHMGSAYTTIAADSIARFQRLLGKKVIFITGTDEHGekIATSAAAN--------------GRNP--- 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 564396916 415 evwkwkAEKGDRIYHQLKKLGSSLD--WDRACFTMDPKLSATVTEAFVRLHEEGVIYRS 471
Cdd:PLN02224 134 ------PEHCDIISQSYRTLWKDLDiaYDKFIRTTDPKHEAIVKEFYARVFANGDIYRA 186
|
|
| GST_C_GluRS_N |
cd10306 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Glutamyl-tRNA synthetase; ... |
130-193 |
4.60e-04 |
|
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: 40.41 E-value: 4.60e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564396916 130 AALGALGKALNPLEEWLRLHTYLAGDAPTLADLaAVTALLLPFRYVLDPSARRIWGNVTRWFNT 193
Cdd:cd10306 21 KDFKALSQALEELDSHLTLRTFIVGYSLSLADI-AVWGALRGNGVAGSLIKNKVYVNLSRWFSF 83
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
674-877 |
7.34e-04 |
|
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173906 [Multi-domain] Cd Length: 314 Bit Score: 43.01 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 674 LRPQWYVRCGEMAQAASAAVTRGDLRILPEAHQRTWHSWMDnirdwcISRQLWWGHRIPayfitvhdpavppgedpdgry 753
Cdd:cd00812 128 LLDQWFLKYSETEWKEKLLKDLEKLDGWPEEVRAMQENWIG------CSRQRYWGTPIP--------------------- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 754 WvsgrteaearekaarefgvspdkislqqdEDVLDTWFSSGLFP--FSIFGWPNQ---------SEDLSVFYPGTLLETG 822
Cdd:cd00812 181 W-----------------------------TDTMESLSDSTWYYarYTDAHNLEQpyegdlefdREEFEYWYPVDIYIGG 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564396916 823 HD-----ILF--FWVArmVMLGLKLTEKLPFREVYLHAIVRdAHGRKMSKSLGNVIDPLDVI 877
Cdd:cd00812 232 KEhapnhLLYsrFNHK--ALFDEGLVTDEPPKGLIVQGMVL-LEGEKMSKSKGNVVTPDEAI 290
|
|
| GST_C_GluProRS_N |
cd10309 |
Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional ... |
125-192 |
9.33e-04 |
|
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: 39.22 E-value: 9.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564396916 125 GQDPQAALGALGKALNPLEEWLRLHTYLAGDAPTLADLAAVTALllpFRYVLDPSARRIWGNVTRWFN 192
Cdd:cd10309 12 SAGRLSCDQDFSSALSYLDKALSLRTYLVGNSLTLADFAVWAAL---RGNGEWLASKEKYVNVTRWFK 76
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
305-376 |
1.30e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 43.13 E-value: 1.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564396916 305 VEAAWYPWWERQGFFKPEygrPSVSAPNPRGVFMMCIPPPNVTGSLHLGHALtnaiqdSLTR------WHRMRGETTL 376
Cdd:PLN02959 18 IEVAVQKWWEEEKVFEAE---AGDEPPKPGEKFFGNFPYPYMNGLLHLGHAF------SLSKlefaaaYHRLRGANVL 86
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
754-878 |
1.59e-03 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 42.78 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 754 WVSGRTEAEAREKAAREFGVS-PDkislqQDEDVLDTWFSSGLFPFSIFGWPNQSEDL----SVFYPGTLLETGHDILFF 828
Cdd:PLN02224 260 WIKSGLRDFSISRALVDWGIPvPD-----DDKQTIYVWFDALLGYISALTEDNKQQNLetavSFGWPASLHLIGKDILRF 334
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 564396916 829 ----WVARMVMLGLKLTeKLPFREVYLhaiVRDahGRKMSKSLGNVIDPLDVIH 878
Cdd:PLN02224 335 havyWPAMLMSAGLELP-KMVFGHGFL---TKD--GMKMGKSLGNTLEPFELVQ 382
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
711-877 |
2.48e-03 |
|
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. 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. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function.
Pssm-ID: 173907 [Multi-domain] Cd Length: 319 Bit Score: 41.36 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 711 SWMDN-IRDWCISRQLW-WGhrIPayfitvhdpaVPpgEDPDGRYWVsgrteaearekaarefgvspdkislqqdedvld 788
Cdd:cd00814 173 SWLKEgLKDLSITRDLFdWG--IP----------VP--LDPGKVIYV--------------------------------- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 789 tWF-------SSGLFPFSIFG-----WPNQSEDLSVFypgtlletGHDILFF----WVArMVM-LGLKLTEKLPfrevyl 851
Cdd:cd00814 206 -WFdaligyiSATGYYNEEWGnswwwKDGWPELVHFI--------GKDIIRFhaiyWPA-MLLgAGLPLPTRIV------ 269
|
170 180 190
....*....|....*....|....*....|..
gi 564396916 852 haivrdAH------GRKMSKSLGNVIDPLDVI 877
Cdd:cd00814 270 ------AHgyltveGKKMSKSRGNVVDPDDLL 295
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
133-233 |
3.07e-03 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 42.02 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 133 GALGKALNPLEEWLRLHTYLAGDAPTLADLAAVTALL--LPFRYVLDPSARriWGNVTRWFNTCVRQPEfrAVLGEVVL- 209
Cdd:PLN02907 93 SEFENACEYVDGYLASRTFLVGYSLTIADIAIWSGLAgsGQRWESLRKSKK--YQNLVRWFNSISAEYS--DILNEVTAa 168
|
90 100
....*....|....*....|....
gi 564396916 210 YSGARSvtqqPGSEITAPQKTAAQ 233
Cdd:PLN02907 169 YVGKRG----AGKPAAAKSKEKVA 188
|
|
| GST_C_Phi |
cd03187 |
C-terminal, alpha helical domain of Class Phi Glutathione S-transferases; Glutathione ... |
95-204 |
5.61e-03 |
|
C-terminal, alpha helical domain of Class Phi Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related fungal and bacterial proteins. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The class Phi GST subfamily has experience extensive gene duplication. The Arabidopsis and Oryza genomes contain 13 and 16 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Tau GSTs, showing class specificity in substrate preference. Phi enzymes are highly reactive toward chloroacetanilide and thiocarbamate herbicides. Some Phi GSTs have other functions including transport of flavonoid pigments to the vacuole, shoot regeneration and GSH peroxidase activity.
Pssm-ID: 198296 [Multi-domain] Cd Length: 118 Bit Score: 37.98 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396916 95 LVQQWVSYADTELTPAACGATL-----PALGLRGpgqDPQAA---LGALGKALNPLEEWLRLHTYLAGDAPTLADLA--A 164
Cdd:cd03187 5 LVEQWLEVEAHQFDPPASKLVFelvfkPMLGLKT---DEAVVeenEAKLKKVLDVYEARLSKSKYLAGDSFTLADLShlP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 564396916 165 VTALLL--PFRYVLDpsARRiwgNVTRWFNTCVRQPEFRAVL 204
Cdd:cd03187 82 NLHYLMatPSKKLFD--SRP---HVKAWWEDISARPAWKKVL 118
|
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