|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
281-1263 |
0e+00 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 1417.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 281 LPTPPGEKKDVSGAMPDSYSPQYVEAAWYPWWERQGFFKPEYGRPSVSAPNPrgvFMMCIPPPNVTGSLHLGHALTNAIQ 360
Cdd:PTZ00419 10 SKDEKKNKKRNISSMAASYDPKEVESGWYEWWEKSGFFKPAEDAKSLNSGKK---FVIVLPPPNVTGYLHIGHALTGAIQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 361 DSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKKLWKERGLNRHQLGREAFLEEVWKWKAEKGDRIYHQLKKLGSSLDWD 440
Cdd:PTZ00419 87 DSLIRYHRMKGDETLWVPGTDHAGIATQVVVEKKLMKEENKTRHDLGREEFLKKVWEWKDKHGNNICNQLRRLGSSLDWS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 441 RACFTMDPKLSATVTEAFVRLHEEGVIYRSTRLVNWSCTLNSAISDIEVDKKELTGRTLLPVPGYKEKVEFGVLVSFAYK 520
Cdd:PTZ00419 167 REVFTMDEQRSKAVKEAFVRLYEDGLIYRDTRLVNWCCYLKTAISDIEVEFEEIEKPTKITIPGYDKKVEVGVLWHFAYP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 521 VQGSDsDEEVVVATTRIETMLGDVAVAVHPKDPRYQHLKGKCVVHPFLS-RSLPIVFDD-FVDMEFGTGAVKITPAHDQN 598
Cdd:PTZ00419 247 LEDSG-QEEIVVATTRIETMLGDVAVAVHPKDERYKKLHGKELIHPFIPdRKIPIIADDeLVDMEFGTGAVKITPAHDPN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 599 DYEVGQRHRLEAISIMDSKGALINVPPPFLGLPRFEARKAVLAALKERGLFRGIKDNPMVVPLCNRSKDVVEPLLRPQWY 678
Cdd:PTZ00419 326 DYEIAKRHNLPFINIFTLDGKINENGGEFAGMHRFDCRRKIEEELKEMGLLRDKVPNPMRLPRCSRSGDIVEPMLIPQWY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 679 VRCGEMAQAASAAVTRGDLRILPEAHQRTWHSWMDNIRDWCISRQLWWGHRIPAYFITVHD-PAVPPGEDPdgryWVSGR 757
Cdd:PTZ00419 406 VNCKDMAKRAVEAVRNGELKIIPSSHENVWYHWLENIQDWCISRQLWWGHRIPAYRVISKGpETDPSDEEP----WVVAR 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 758 TEAEAREKAAREFGVSPDKISLQQDEDVLDTWFSSGLFPFSIFGWPNQSEDLSVFYPGTLLETGHDILFFWVARMVMLGL 837
Cdd:PTZ00419 482 SEEEALEKAKKKFGLSEEDFELEQDEDVLDTWFSSGLFPFSTLGWPDQTDDLQRFFPTSLLETGSDILFFWVARMVMMSL 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 838 KLTGKLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVIHGVSLQGLYDQLLNSNLDPSEVEKAKEGQKADFPAGIPECG 917
Cdd:PTZ00419 562 HLTDKLPFKTVFLHAMVRDSQGEKMSKSKGNVIDPLEVIEGISLQDLNQKLYEGNLPEKEIKRAIELQKKEFPNGIPECG 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 918 TDALRFGLCAYTSQGRDINLDVNRILGYRHFCNKLWNATKFALRGLGKGFVP--SATSKPEGHESL--VDRWIRSRLTEA 993
Cdd:PTZ00419 642 TDALRFGLLAYTQQGRNINLDINRVVGYRHFCNKLWNAVKFALMKLLKDFNLpnSTLFKPNNVESLpwEDKWILHRLNVA 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 994 VRLSNEGFQAYDFPAITTAQYSFWLYELCDVYLECLKPVLN-GVDQVAAECARQTLYTCLDVGLRLLSPFMPFVTEELFQ 1072
Cdd:PTZ00419 722 IKEVTEGFKEYDFSEATQATYNFWLYELCDVYLELIKPRLSkQSDGERKQHAQDVLHTVLDIGLRLLHPMMPFITEELYQ 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 1073 RLPRRTPKAPaSLCVTPYPEPSeCSWKDPEAEAALELALSITRAVRSLRADYNLT-RTRPDCFLEVADEATGALASAVSG 1151
Cdd:PTZ00419 802 RLPNYLRKSE-SISIAKYPQPN-PGWNNEALDEEMKIIMSIVKSIRSLIATLGIPnKTKPDCYVTAKDAELIELIESAEN 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 1152 YVQALASAG---VVAVLALGAPAPQGCAVAVASDRCSIHLQLQGLVDPARELGKLQAKRSEAQRQAQRLQERRAASSYSA 1228
Cdd:PTZ00419 880 LISTLAKIGsvsVIPPIEEEAEVPKGCGFDVVDNKVIIYLNLDEFIDLKKELAKLEKKLAKLQKSLESYLKKISIPNYED 959
|
970 980 990
....*....|....*....|....*....|....*
gi 31565370 1229 KVPLEVQEADEAKLQQTEAELRKVDEAIALFQKML 1263
Cdd:PTZ00419 960 KVPEDVRKLNDEKIDELNEEIKQLEQAIEELKSLL 994
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
295-1257 |
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: 1194.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 295 MPDSYSPQYVEAAWYPWWERQGFFKPEygrPSVSAPNprgvFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETT 374
Cdd:COG0525 3 LPKTYDPKEVEAKWYQYWEENGYFKAD---PDSDKEP----FTIVIPPPNVTGSLHMGHALNNTLQDILIRYKRMQGYNT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 375 LWNPGCDHAGIATQVVVEKKLwKERGLNRHQLGREAFLEEVWKWKAEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSATV 454
Cdd:COG0525 76 LWQPGTDHAGIATQAVVERQL-AEEGKSRHDLGREKFLERVWEWKEESGGTITNQLRRLGASCDWSRERFTMDEGLSKAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 455 TEAFVRLHEEGVIYRSTRLVNWSCTLNSAISDIEVDkkeltgrtllpvpgYKEKVefGVLVSFAYKVqgSDSDEEVVVAT 534
Cdd:COG0525 155 REVFVRLYEKGLIYRGKRLVNWDPKLKTALSDLEVE--------------HEEVK--GHLWHIRYPL--ADGSGYIVVAT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 535 TRIETMLGDVAVAVHPKDPRYQHLKGKCVVHPFLSRSLPIVFDDFVDMEFGTGAVKITPAHDQNDYEVGQRHRLEAISIM 614
Cdd:COG0525 217 TRPETMLGDTAVAVHPEDERYKHLIGKTVILPLVGREIPIIADEYVDPEFGTGAVKITPAHDPNDFEVGKRHNLPMINIL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 615 DSKGALINVPPPFLGLPRFEARKAVLAALKERGLFRGIKDNPMVVPLCNRSKDVVEPLLRPQWYVRCGEMAQAASAAVTR 694
Cdd:COG0525 297 DEDGTINENAGKYRGLDRFEARKAIVADLEELGLLVKVEPHKHSVGHSDRSGTVIEPYLSDQWFVKMKPLAKPAIEAVED 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 695 GDLRILPEAHQRTWHSWMDNIRDWCISRQLWWGHRIPAYFitvhdpavppgeDPDGRYWVSgRTEAEAREKAarefgvsp 774
Cdd:COG0525 377 GEIKFVPERWEKTYFHWMENIRDWCISRQLWWGHRIPAWY------------CPDGEVYVA-RTEPEACAKA-------- 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 775 DKISLQQDEDVLDTWFSSGLFPFSIFGWPNQSEDLSVFYPGTLLETGHDILFFWVARMVMLGLKLTGKLPFREVYLHAIV 854
Cdd:COG0525 436 GSVNLTQDEDVLDTWFSSALWPFSTLGWPEKTEDLKYFYPTSVLVTGFDIIFFWVARMIMMGLHFTGEVPFKDVYIHGLV 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 855 RDAHGRKMSKSLGNVIDPLDVIhgvslqglyDQLlnsnldpsevekakegqkadfpagipecGTDALRFGLCAYTSQGRD 934
Cdd:COG0525 516 RDEQGRKMSKSKGNVIDPLDLI---------DKY----------------------------GADALRFTLAALASPGRD 558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 935 INLDVNRILGYRHFCNKLWNATKFALrGLGKGFVPSATSKPEgHESLVDRWIRSRLTEAVRLSNEGFQAYDFPAITTAQY 1014
Cdd:COG0525 559 IKFDEERVEGYRNFANKLWNASRFVL-MNLEGFDPGLDPDPE-ELSLADRWILSRLNKTIAEVTEALEKYRFDEAAQALY 636
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 1015 SF-WlYELCDVYLECLKPVLNGVDQVAAECARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRTPKapASLCVTPYPEP 1093
Cdd:COG0525 637 DFvW-NEFCDWYLELAKPRLYGGDEAAKRETRATLVYVLEQILRLLHPFMPFITEEIWQKLPPRKEG--ESIMLAPWPEA 713
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 1094 SEcSWKDPEAEAALELALSITRAVRSLRADYNLT-RTRPDCFLEVADEATGALASAVSGYVQALASAGVVAVLAlgAPAP 1172
Cdd:COG0525 714 DE-ELIDEEAEAEFEWLKEVISAIRNIRAEMNIPpSKKLPLLLKGADEADRARLEENAAYIKRLARLEEITILV--DEKP 790
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 1173 QGCAVAVASDrCSIHLQLQGLVDPARELGKLQAKRSEAQRQAQRLQERRAASSYSAKVPLEVQEADEAKLQQTEAELRKV 1252
Cdd:COG0525 791 EGAASAVVGG-AEVFLPLEGLIDVEAERARLEKELAKLEKEIARVEKKLSNEGFVAKAPAEVVEKEREKLAEAEAKLEKL 869
|
....*
gi 31565370 1253 DEAIA 1257
Cdd:COG0525 870 EEQLA 874
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
295-1261 |
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 31565370 295 MPDSYSPQYVEAAWYPWWERQGFFKPEygrpsvsaPNPRGVFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETT 374
Cdd:PRK05729 5 LPKTYDPKEVEAKWYQKWEEKGYFKPD--------DNSKKPFSIVIPPPNVTGSLHMGHALNNTLQDILIRYKRMQGYNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 375 LWNPGCDHAGIATQVVVEKKLWKErGLNRHQLGREAFLEEVWKWKAEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSATV 454
Cdd:PRK05729 77 LWLPGTDHAGIATQMVVERQLAAE-GKSRHDLGREKFLEKVWEWKEESGGTITNQLRRLGASCDWSRERFTMDEGLSKAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 455 TEAFVRLHEEGVIYRSTRLVNWSCTLNSAISDIEVDkkeltgrtllpvpgYKEkVEfGVLVSFAYKVqgSDSDEEVVVAT 534
Cdd:PRK05729 156 REVFVRLYEKGLIYRGKRLVNWDPKLQTALSDLEVE--------------YKE-VK-GKLWHIRYPL--ADGSDYLVVAT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 535 TRIETMLGDVAVAVHPKDPRYQHLKGKCVVHPFLSRSLPIVFDDFVDMEFGTGAVKITPAHDQNDYEVGQRHRLEAISIM 614
Cdd:PRK05729 218 TRPETMLGDTAVAVNPEDERYKHLIGKTVILPLVGREIPIIADEYVDPEFGTGAVKITPAHDPNDFEVGKRHNLPMINIM 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 615 DSKGALINVPPPFLGLPRFEARKAVLAALKERGLFRGIKDNPMVVPLCNRSKDVVEPLLRPQWYVRCGEMAQAASAAVTR 694
Cdd:PRK05729 298 DEDGTINENPGEYQGLDRFEARKAIVADLEELGLLVKIEPHTHSVGHSDRSGVVIEPYLSDQWFVKMKPLAKPALEAVEN 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 695 GDLRILPEAHQRTWHSWMDNIRDWCISRQLWWGHRIPAYFitvhdpavppgeDPDGRYWVsGRTEAEAREKAArefgvsp 774
Cdd:PRK05729 378 GEIKFVPERWEKTYFHWMENIQDWCISRQLWWGHRIPAWY------------DEDGEVYV-GREEPEAREKAL------- 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 775 dkisLQQDEDVLDTWFSSGLFPFSIFGWPNQSEDLSVFYPGTLLETGHDILFFWVARMVMLGLKLTGKLPFREVYLHAIV 854
Cdd:PRK05729 438 ----LTQDEDVLDTWFSSALWPFSTLGWPEKTEDLKRFYPTSVLVTGFDIIFFWVARMIMMGLHFTGQVPFKDVYIHGLV 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 855 RDAHGRKMSKSLGNVIDPLDVIhgvslqglyDQLlnsnldpsevekakegqkadfpagipecGTDALRFGLCAYTSQGRD 934
Cdd:PRK05729 514 RDEQGRKMSKSKGNVIDPLDLI---------DKY----------------------------GADALRFTLAALASPGRD 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 935 INLDVNRILGYRHFCNKLWNATKFALrgLGKGFVPSATSKPEGHESLVDRWIRSRLTEAVRLSNEGFQAYDFPAITTAQY 1014
Cdd:PRK05729 557 IRFDEERVEGYRNFANKLWNASRFVL--MNLEGADVGELPDPEELSLADRWILSRLNRTVAEVTEALDKYRFDEAARALY 634
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 1015 SFWLYELCDVYLECLKPVLNGVDQVAaecARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRTPKapASLCVTPYPEPS 1094
Cdd:PRK05729 635 EFIWNEFCDWYLELAKPVLQEAAKRA---TRATLAYVLEQILRLLHPFMPFITEELWQKLAPLGIE--ESIMLAPWPEAD 709
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 1095 ECswKDPEAEAALELALSITRAVRSLRADYNLT-RTRPDCFLEVADEATGALASAVSGYVQALASAGVVAVLALGAPAPQ 1173
Cdd:PRK05729 710 EA--IDEAAEAEFEWLKELITAIRNIRAEMNIPpSKKLPLLLKGADAEDRARLEANEAYIKRLARLESLEILADDEEAPE 787
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 1174 GCAVAVASDrCSIHLQLQGLVDPARELGKLQAKRSEAQRQAQRLQERRAASSYSAKVPLEVQEADEAKLQQTEAELRKVD 1253
Cdd:PRK05729 788 GAASAVVGG-AELFLPLEGLIDVEAELARLEKELAKLEKEIERVEKKLSNEGFVAKAPEEVVEKEREKLAEYEEKLAKLK 866
|
....*...
gi 31565370 1254 EAIALFQK 1261
Cdd:PRK05729 867 ERLARLKA 874
|
|
| PLN02381 |
PLN02381 |
valyl-tRNA synthetase |
213-1255 |
0e+00 |
|
valyl-tRNA synthetase
Pssm-ID: 215214 [Multi-domain] Cd Length: 1066 Bit Score: 1144.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 213 ARSVTQQPGSEVIAPQKTPAQLKKEAKKREK-------LEKFQQKQKTQQQPPHGEKKPKPEKKEKRDPGV------ITY 279
Cdd:PLN02381 1 GSRTESEAEKKILTEEELERKKKKEEKAKEKelkklkaAQKEAKAKLQAQQASDGTNVPKKSEKKSRKRDVedenpeDFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 280 DLPTPPGEKKDVSGAMPDSYSPQYVEAAWYPWWERQGFFKPEygrPSVSAPNprgvFMMCIPPPNVTGSLHLGHALTNAI 359
Cdd:PLN02381 81 DPDTPFGQKKRLSSQMAKQYSPSAVEKSWYAWWEKSGYFGAD---AKSSKPP----FVIVLPPPNVTGALHIGHALTAAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 360 QDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKKLWKERGLNRHQLGREAFLEEVWKWKAEKGDRIYHQLKKLGSSLDW 439
Cdd:PLN02381 154 EDTIIRWKRMSGYNALWVPGVDHAGIATQVVVEKKLMRERHLTRHDIGREEFVSEVWKWKDEYGGTILNQLRRLGASLDW 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 440 DRACFTMDPKLSATVTEAFVRLHEEGVIYRSTRLVNWSCTLNSAISDIEVDKKELTGRTLLPVPGYKEKVEFGVLVSFAY 519
Cdd:PLN02381 234 SRECFTMDEQRSKAVTEAFVRLYKEGLIYRDIRLVNWDCTLRTAISDVEVDYIDIKERTLLKVPGYDKPVEFGVLTSFAY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 520 KVQGSDSdeEVVVATTRIETMLGDVAVAVHPKDPRYQHLKGKCVVHPFLSRSLPIVFD-DFVDMEFGTGAVKITPAHDQN 598
Cdd:PLN02381 314 PLEGGLG--EIVVATTRIETMLGDTAIAIHPDDERYKHLHGKFAVHPFNGRKLPIICDaILVDPNFGTGAVKITPAHDPN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 599 DYEVGQRHRLEAISIMDSKGAL-INVPPPFLGLPRFEARKAVLAALKERGLFRGIKDNPMVVPLCNRSKDVVEPLLRPQW 677
Cdd:PLN02381 392 DFEVGKRHNLEFINIFTDDGKInSNGGSEFAGMPRFAAREAVIEALQKKGLYRGAKNNEMRLGLCSRTNDVVEPMIKPQW 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 678 YVRCGEMAQAASAAVTRGD---LRILPEAHQRTWHSWMDNIRDWCISRQLWWGHRIPAYFITVHDPAvppgEDPDGRY-- 752
Cdd:PLN02381 472 FVNCSSMAKQALDAAIDGEnkkLEFIPKQYLAEWKRWLENIRDWCISRQLWWGHRIPAWYVTLEDDQ----LKELGSYnd 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 753 -WVSGRTEAEAREKAAREFgvSPDKISLQQDEDVLDTWFSSGLFPFSIFGWPNQSEDLSVFYPGTLLETGHDILFFWVAR 831
Cdd:PLN02381 548 hWVVARNESDALLEASQKF--PGKKFELSQDPDVLDTWFSSGLFPLSVLGWPDDTDDLKAFYPTSVLETGHDILFFWVAR 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 832 MVMLGLKLTGKLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVIHGVSLQGLYDQLLNSNLDPSEVEKAKEGQKADFPA 911
Cdd:PLN02381 626 MVMMGMQLGGDVPFRKVYLHPMIRDAHGRKMSKSLGNVIDPLEVINGISLEGLHKRLEEGNLDPKELVVAKEGQKKDFPN 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 912 GIPECGTDALRFGLCAYTSQGRDINLDVNRILGYRHFCNKLWNATKFALRGLGKGFVPSATSKPEGHESLVdRWIRSRLT 991
Cdd:PLN02381 706 GIAECGTDALRFALVSYTAQSDKINLDILRVVGYRQWCNKLWNAVRFAMSKLGDDYTPPATLSVETMPFSC-KWILSVLN 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 992 EAVRLSNEGFQAYDFPAITTAQYSFWLYELCDVYLECLKPVLNGVDQ---VAAECARQTLYTCLDVGLRLLSPFMPFVTE 1068
Cdd:PLN02381 785 KAISKTVSSLDAYEFSDAASTVYSWWQYQFCDVFIEAIKPYFAGDNPefaSERAAAQDTLWICLDTGLRLLHPFMPFVTE 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 1069 ELFQRLPR-RTPKAPASLCVTPYPEPSEcSWKDPEAEAALELALSITRAVRSLRADYNLTRT--RPDCFLEVADEATGAL 1145
Cdd:PLN02381 865 ELWQRLPQpKDHTRKDSIMISEYPSAVE-AWTNEKVEYEMDLVLSTVKCLRSLRAEVLEKQKneRLPAFALCRNQEIAAI 943
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 1146 ASAVSGYVQALASAGVVAVLALGAPA-PQGCAVAVASDRCSIHLQLQGLVDPARELGKLQAKRSEAQRQAQRLQERRAAS 1224
Cdd:PLN02381 944 IKSHQLEILTLANLSSLKVLLSENDApPAGCAFENVNENLKVYLQAQGAVNAEAELEKLRNKMDEIQKQQEKLEKKMNAS 1023
|
1050 1060 1070
....*....|....*....|....*....|.
gi 31565370 1225 SYSAKVPLEVQEADEAKLQQTEAELRKVDEA 1255
Cdd:PLN02381 1024 GYKEKVPANIQEEDARKLTKLLQELEFFEKE 1054
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
295-1242 |
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: 976.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 295 MPDSYSPQYVEAAWYPWWERQGFFKPEYGRPSVSapnprgvFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETT 374
Cdd:TIGR00422 1 MPKDYDPHEVEKKWYKKWEKSGFFKPDGNSNKPP-------FCIDIPPPNVTGSLHIGHALNWSIQDIIARYKRMKGYNV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 375 LWNPGCDHAGIATQVVVEKKLWKErGLNRHQLGREAFLEEVWKWKAEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSATV 454
Cdd:TIGR00422 74 LWLPGTDHAGIATQVKVEKKLGAE-GKTKHDLGREEFREKIWEWKEESGGTIKNQIKRLGASLDWSRERFTMDEGLSKAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 455 TEAFVRLHEEGVIYRSTRLVNWSCTLNSAISDIEVDKKELTGRtllpVPGYKEKVEFGvlvsfaykvqgsdSDEEVVVAT 534
Cdd:TIGR00422 153 KEAFVRLYEKGLIYRGEYLVNWDPKLNTAISDIEVEYKEVKGK----LYYIRYPLANG-------------SKDYLVVAT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 535 TRIETMLGDVAVAVHPKDPRYQHLKGKCVVHPFLSRSLPIVFDDFVDMEFGTGAVKITPAHDQNDYEVGQRHRLEAISIM 614
Cdd:TIGR00422 216 TRPETMFGDTAVAVHPEDERYKHLIGKKVILPLTGRKIPIIADEYVDMEFGTGAVKVTPAHDFNDYEWGKRHNLEFINIL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 615 DSKGALINVPPPFLGLPRFEARKAVLAALKERGLFRGIKDNPMVVPLCNRSKDVVEPLLRPQWYVRCGEMAQAASAAVTR 694
Cdd:TIGR00422 296 DEDGLLNENAGKYQGLTRFEARKKIVEDLKEEGLLVKIEPHTHNVGTCWRSGTVVEPLLSKQWFVKVEKLADKALEAAEE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 695 GDLRILPEAHQRTWHSWMDNIRDWCISRQLWWGHRIPAYFItvhdpavppgeDPDGRYWVsGRTEAEAREKAAREFGVSp 774
Cdd:TIGR00422 376 GEIKFVPKRMEKRYLNWLRNIKDWCISRQLIWGHRIPVWYC-----------KECGEVYV-AKEEPLPDDKTNTGPSVE- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 775 dkisLQQDEDVLDTWFSSGLFPFSIFGWPNQSEDLSVFYPGTLLETGHDILFFWVARMVMLGLKLTGKLPFREVYLHAIV 854
Cdd:TIGR00422 443 ----LEQDTDVLDTWFSSSLWPFSTLGWPDETKDLKKFYPTDLLVTGYDIIFFWVARMIFRSLALTGQVPFKEVYIHGLV 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 855 RDAHGRKMSKSLGNVIDPLDVIHgvslqglydqllnsnldpsevekakegqkadfpagipECGTDALRFGLCAYTSQGRD 934
Cdd:TIGR00422 519 RDEQGRKMSKSLGNVIDPLDVIE-------------------------------------KYGADALRFTLASLVTPGDD 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 935 INLDVNRILGYRHFCNKLWNATKFALRGLGKgfvPSATSKPEGHESLVDRWIRSRLTEAVRLSNEGFQAYDFPAITTAQY 1014
Cdd:TIGR00422 562 INFDWKRVESARNFLNKLWNASRFVLMNLSD---DLELSGGEEKLSLADRWILSKLNRTIKEVRKALDKYRFAEAAKALY 638
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 1015 SFWLYELCDVYLECLKPVLNGVDQVAAECARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRTpkapASLCVTPYPEPS 1094
Cdd:TIGR00422 639 EFIWNDFCDWYIELVKYRLYNGNEAEKKAARDTLYYVLDKALRLLHPFMPFITEEIWQHFKEGA----DSIMLQSYPVVD 714
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 1095 EcSWKDPEAEAALELALSITRAVRSLRADYNLTRTRPDCFLEVADEATGALA-SAVSGYVQALASAGVVAVLAlGAPaPQ 1173
Cdd:TIGR00422 715 A-EFVDEEAEKAFELLKEIIVSIRNLKAESNIPPNAPLKVLLIYTEAETAERlKLNAVDIKGAINFSEVEVVI-EKP-EV 791
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31565370 1174 GCAVAVASDRCSIHLQLQGLVDPARELGKLQAKRSEAQRQAQRLQERRAASSYSAKVPLEVQEADEAKL 1242
Cdd:TIGR00422 792 TEAVVELVPGFEIIIPVKGLINKAKELARLQKQLDKEKKEVIRIEGKLENEGFVKKAPKEVIEKEKEKL 860
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
299-1258 |
0e+00 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 860.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 299 YSPQYVEAAWYPWWERQGFFKPEygrpsvSAPNPRGVFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNP 378
Cdd:PRK14900 19 YEHREVEARWYPFWQERGYFHGD------EHDRTRPPFSIVLPPPNVTGSLHLGHALTATLQDVLIRWKRMSGFNTLWLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 379 GCDHAGIATQVVVEKKLWKERGLNRHQLGREAFLEEVWKWKAEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSATVTEAF 458
Cdd:PRK14900 93 GTDHAGIATQMIVEKELKKTEKKSRHDLGREAFLERVWAWKEQYGSRIGEQHKALGASLDWQRERFTMDEGLSRAVREVF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 459 VRLHEEGVIYRSTRLVNWSCTLNSAISDIEVDKKEltgrtllpvpgykekVEFGVLVSFAYKVqgSDSDEEVVVATTRIE 538
Cdd:PRK14900 173 VRLHEEGLIYREKKLINWCPDCRTALSDLEVEHEE---------------AHQGELWSFAYPL--ADGSGEIVVATTRPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 539 TMLGDVAVAVHPKDPRYQHLKGKCVVHPFLSRSLPIVFD-DFVDMEFGTGAVKITPAHDQNDYEVGQRHRLEAISIMDSK 617
Cdd:PRK14900 236 TMLGDTAVAVHPLDPRYMALHGKKVRHPITGRTFPIVADaILVDPKFGTGAVKVTPAHDFNDFEVGKRHGLEMITVIGPD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 618 GALINVPPPFLGLPRFEARKAVLAALKERGLFRGIKDNPMVVPLCNRSKDVVEPLLRPQWYVRCGEMAQAASAAVTRGDL 697
Cdd:PRK14900 316 GRMTAEAGPLAGLDRFEARKEVKRLLAEQGLDRGAKPHVLPLGRCQRSATILEPLLSDQWYVRIEPLARPAIEAVEQGRT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 698 RILPEAHQRTWHSWMDNIRDWCISRQLWWGHRIPAYFItvhdpavppgedPDGRYWVSGRTEAEAREKAAREFgvspdki 777
Cdd:PRK14900 396 RFIPEQWTNTYMAWMRNIHDWCISRQLWWGHQIPAWYC------------PDGHVTVARETPEACSTCGKAEL------- 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 778 slQQDEDVLDTWFSSGLFPFSIFGWPNQSEDLSVFYPGTLLETGHDILFFWVARMVMLGLKLTGKLPFREVYLHAIVRDA 857
Cdd:PRK14900 457 --RQDEDVLDTWFSSGLWPFSTMGWPEQTDTLRTFYPTSVMETGHDIIFFWVARMMMMGLHFMGEVPFRTVYLHPMVRDE 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 858 HGRKMSKSLGNVIDPLDVihgvslqglydqllnsnldpsevekakegqkadfpagIPECGTDALRFGLCAYTSQGRDINL 937
Cdd:PRK14900 535 KGQKMSKTKGNVIDPLVI-------------------------------------TEQYGADALRFTLAALTAQGRDIKL 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 938 DVNRILGYRHFCNKLWNATKFALRGLGkGFVPSATSKPEGHESLVDRWIRSRLTEAVRLSNEGFQAYDFPAITTAQYSFW 1017
Cdd:PRK14900 578 AKERIEGYRAFANKLWNASRFALMNLS-GYQERGEDPARLARTPADRWILARLQRAVNETVEALEAFRFNDAANAVYAFV 656
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 1018 LYELCDVYLECLKPVLNGVDQVAAECARQTLYTCLDVGLRLLSPFMPFVTEELFQRLP--RRTPKAPASLCVTPYPEPSE 1095
Cdd:PRK14900 657 WHELCDWYIELAKEALASEDPEARRSVQAVLVHCLQTSYRLLHPFMPFITEELWHVLRaqVGASAWADSVLAAEYPRKGE 736
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 1096 CswkDPEAEAALELALSITRAVRSLRADYNLT-----RTRPDCFLEVADEATGALASAVS-GYVQALASAGVVAVLALGA 1169
Cdd:PRK14900 737 A---DEAAEAAFRPVLGIIDAVRNIRGEMGIPwkvklGAQAPVEIAVADPALRDLLQAGElARVHRVAGVEGSRLVVAAA 813
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 1170 PAPQGCAVAVASDRCSIHLQLQGLVDPARELGKLQAKRSEAQRQAQRLQERRAASSYSAKVPLEVQEADEAKLQQTEAEL 1249
Cdd:PRK14900 814 TAPAPQSAVGVGPGFEVRVPLAGVIDLAAETARVDKEIGKVDQDLAVLERKLQNPSFVQNAPPAVVEKDRARAEELREKR 893
|
....*....
gi 31565370 1250 RKVDEAIAL 1258
Cdd:PRK14900 894 GKLEAHRAM 902
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
309-1262 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 719.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 309 YPWWERQGFFKPEYGRPSvsapNPrgvFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQ 388
Cdd:PLN02943 70 YNWWESQGYFKPNFDRGG----DP---FVIPMPPPNVTGSLHMGHAMFVTLEDIMVRYNRMKGRPTLWIPGTDHAGIATQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 389 VVVEKKLWKErGLNRHQLGREAFLEEVWKWKAEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSATVTEAFVRLHEEGVIY 468
Cdd:PLN02943 143 LVVEKMLASE-GIKRTDLGRDEFTKRVWEWKEKYGGTITNQIKRLGASCDWSRERFTLDEQLSRAVVEAFVRLHEKGLIY 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 469 RSTRLVNWSCTLNSAISDIEVDKKEltgrtllpvpgykekvEFGVLVSFAYKVQGSdSDEEVVVATTRIETMLGDVAVAV 548
Cdd:PLN02943 222 QGSYMVNWSPNLQTAVSDLEVEYSE----------------EPGTLYYIKYRVAGG-SEDFLTIATTRPETLFGDVAIAV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 549 HPKDPRYQHLKGKCVVHPF-LSRSLPIVFDDFVDMEFGTGAVKITPAHDQNDYEVGQRHRLEAISIMDSKGALINVPppf 627
Cdd:PLN02943 285 NPEDDRYSKYIGKMAIVPMtYGRHVPIIADRYVDKDFGTGVLKISPGHDHNDYLLARKLGLPILNVMNKDGTLNEVA--- 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 628 lGLPRFEARKAVLAALKERGLfrGIKDNP--MVVPLCNRSKDVVEPLLRPQWYVRCGEMAQAASAAVTRGDLRILPEAHQ 705
Cdd:PLN02943 362 -GLYWFEAREKLWSDLEETGL--AVKKEPhtLRVPRSQRGGEVIEPLVSKQWFVTMEPLAEKALKAVENGELTIIPERFE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 706 RTWHSWMDNIRDWCISRQLWWGHRIPAYFITvhdpavppGEDPDGRYWVSgRTEAEAREKAAREFGVSpdkISLQQDEDV 785
Cdd:PLN02943 439 KIYNHWLSNIKDWCISRQLWWGHRIPVWYIV--------GKDCEEDYIVA-RSAEEALEKAREKYGKD---VEIYQDPDV 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 786 LDTWFSSGLFPFSIFGWPNQS-EDLSVFYPGTLLETGHDILFFWVARMVMLGLKLTGKLPFREVYLHAIVRDAHGRKMSK 864
Cdd:PLN02943 507 LDTWFSSALWPFSTLGWPDVSaEDFKKFYPTTVLETGHDILFFWVARMVMMGIEFTGTVPFSYVYLHGLIRDSQGRKMSK 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 865 SLGNVIDPLDVIHgvslqglydqllnsnldpsevekakegqkadfpagipECGTDALRFGLCAYTSqGRDINLDVNRILG 944
Cdd:PLN02943 587 TLGNVIDPLDTIK-------------------------------------EFGTDALRFTLALGTA-GQDLNLSTERLTS 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 945 YRHFCNKLWNATKFALRGLGKGFVPSA-----TSKPEGHESLV-----DRWIRSRLTEAVRLSNEGFQAYDFPAITTAQY 1014
Cdd:PLN02943 629 NKAFTNKLWNAGKFVLQNLPSQSDTSAwehilACKFDKEESLLslplpECWVVSKLHELIDSVTTSYDKYFFGDVGREIY 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 1015 SFWLYELCDVYLECLKPVLNGV-DQVAAECARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRTpkapASLCVTPYPEP 1093
Cdd:PLN02943 709 DFFWSDFADWYIEASKTRLYHSgDNSALSRAQAVLLYVFENILKLLHPFMPFVTEELWQALPYRK----EALIVSPWPQT 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 1094 SECswKDPEAEAALELALSITRAVRSLRADYNLTRTRPDCFLEVADEATGALASAVSGYVQALASAGVVAVLALGAP--- 1170
Cdd:PLN02943 785 SLP--KDLKSIKRFENLQSLTRAIRNARAEYSVEPAKRISASIVASAEVIEYISKEKEVLALLSRLDLQNVHFTDSPpgd 862
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 1171 APQGCAVaVASDRCSIHLQLQGLVDPARELGKLQAKRSEAQRQAQRLQERRAASSYSAKVPLEVQEADEAKLQQTEAELR 1250
Cdd:PLN02943 863 ANQSVHL-VASEGLEAYLPLADMVDISAEVERLSKRLSKMQTEYDALAARLSSPKFVEKAPEDVVRGVREKAAEAEEKIK 941
|
970
....*....|..
gi 31565370 1251 KVDEAIALFQKM 1262
Cdd:PLN02943 942 LTKNRLAFLKST 953
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
307-938 |
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: 687.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 307 AWYPWWERQGFFKPEygrpsVSAPNPRGVFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIA 386
Cdd:pfam00133 1 QIYEFWDEQGYFKPE-----LEKRKGKPSFTIHDGPPNATGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 387 TQVVVEKKLWKERGLNRHQLGREAFLEEVWKWKAEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSATVTEAFVRLHEEGV 466
Cdd:pfam00133 76 TEQVVEKKLGIKEKKTRHKYGREEFREKCREWKMEYADEIRKQFRRLGRSIDWDREYFTMDPELEAAVWEVFVRLHDKGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 467 IYRSTRLVNWSCTLNSAISDIEVDKKELTgrtllpvpgykekvefGVLVSFAYKVQGsDSDEEVVVATTRIETMLGDVAV 546
Cdd:pfam00133 156 IYRGKKLVNWSPALNTALSNLEVEYKDVK----------------GPSIHVAFPLAD-DEGASLVIWTTTPWTLPGNTAV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 547 AVHP-------------------------------KDPRYQHLKGKCVVHPFLSRSLPIVFDDFVDMEFGTGAVKITPAH 595
Cdd:pfam00133 219 AVNPefdyvitgegyilaeallkslykkgtdkkilEDFRGKELEGKEAIHPFVNREIPIITDDYVDMEFGTGAVHIAPAH 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 596 DQNDYEVGQRHRLEAISIMDSKGALINVPPPFLGLPRFEARKAVLAALKERGLFRGIKDNPMVVPLCNRSKDVVEPLLRP 675
Cdd:pfam00133 299 GENDYEVGQRHNLEVINPVDDDGTFTEEAPDFQGVYRFDARKKIVELLTEKGLLLKIEPFTHSYPFCWRSGTPIIPRATP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 676 QWYVRCGEMAQAASAAVTrgDLRILPEAHQRTWHSWMDNIRDWCISRQLWWGHRIPAYFITVHDPAVPPGEdpdGRYWVS 755
Cdd:pfam00133 379 QWFVRMDELADQALEAVE--KVQFVPKSGEKRYFNWLANIQDWCISRQRWWGHPIPAWVSKDTEEVVCRGE---LFELVA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 756 GRTEAEAREKA-AREFG--VSPDKISLQQDEDVLDTWFSSGLFPFSIFGWPNQS-EDLSVFYPGTLLETGHDILFFWVAR 831
Cdd:pfam00133 454 GRFEEEGSIKWlHREAKdkLGYGKGTLEQDEDVLDTWFSSGSWPFSTLGWPFVNtEEFKKFFPADMLLEGSDQTRGWFYR 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 832 MVMLGLKLTGKLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVIHgvslqglydqllnsnldpsevekakegqkadfpa 911
Cdd:pfam00133 534 MIMLSTALTGSVPFKNVLVHGLVRDEQGRKMSKSLGNVIDPLDVID---------------------------------- 579
|
650 660
....*....|....*....|....*..
gi 31565370 912 gipECGTDALRFGLCaYTSQGRDINLD 938
Cdd:pfam00133 580 ---KYGADALRLWLA-NSDYGRDINLS 602
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
334-937 |
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: 615.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 334 GVFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKKLWKERGlNRHQLGREAFLE 413
Cdd:cd00817 1 PVFVIDTPPPNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGIATQVVVEKKLGIEGK-TRHDLGREEFLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 414 EVWKWKAEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSATVTEAFVRLHEEGVIYRSTRLVNWSCTLNSAISDIEVdkke 493
Cdd:cd00817 80 KCWEWKEESGGKIREQLKRLGASVDWSREYFTMDPGLSRAVQEAFVRLYEKGLIYRDNRLVNWCPKLRTAISDIEV---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 494 ltgrtllpvpgykekvefgvlvsfaykvqgsdsdeevvvattrietmlgdvavavhpkdpryqhlkgkcvvhpflsrslp 573
Cdd:cd00817 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 574 ivfddfvdmefgtgavkitpahdqndyevgqrhrleaisimdskgalinvpppflglprfearkavlaalkerglfrgik 653
Cdd:cd00817 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 654 dnpmvvplCNRSKDVVEPLLRPQWYVRCGEMAQAASAAVTRGDLRILPEAHQRTWHSWMDNIRDWCISRQLWWGHRIPAY 733
Cdd:cd00817 156 --------CSRSGDVIEPLLKPQWFVKVKDLAKKALEAVKEGDIKFVPERMEKRYENWLENIRDWCISRQLWWGHRIPAW 227
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 734 FItvhdpavppgedPDGRYWVSGRTEAEAREKAAREFGVSPDKISLQQDEDVLDTWFSSGLFPFSIFGWPNQSEDLSVFY 813
Cdd:cd00817 228 YC------------KDGGHWVVAREEDEAIDKAAPEACVPCGGEELKQDEDVLDTWFSSSLWPFSTLGWPEETKDLKKFY 295
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 814 PGTLLETGHDILFFWVARMVMLGLKLTGKLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVihgvslqglydqllnsnl 893
Cdd:cd00817 296 PTSLLVTGHDIIFFWVARMIMRGLKLTGKLPFKEVYLHGLVRDEDGRKMSKSLGNVIDPLDV------------------ 357
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 31565370 894 dpsevekakegqkadfpagIPECGTDALRFGLCAYTSQGRDINL 937
Cdd:cd00817 358 -------------------IDGYGADALRFTLASAATQGRDINL 382
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
294-1173 |
3.56e-136 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 435.39 E-value: 3.56e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 294 AMPDSYSPQYVEAAWYPWWERQG--FFKPEYGRPsvsapnprgVFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRG 371
Cdd:PRK13208 5 ELPKKYDPEELEEKWQKIWEEEGtyKFDPDERKP---------VYSIDTPPPTVSGSLHIGHVFSYTHTDFIARYQRMRG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 372 ETTLWNPGCDHAGIATQVVVEKKLwkerGLNRHQLGREAFLE--EVWKWKAEKGDRiyHQLKKLGSSLDWDRACFTMDPK 449
Cdd:PRK13208 76 YNVFFPQGWDDNGLPTERKVEKYY----GIRKDDISREEFIElcRELTDEDEKKFR--ELWRRLGLSVDWSLEYQTISPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 450 LSATVTEAFVRLHEEGVIYRSTRLVNWSCTLNSAISDIEVDKKELTGRtllpvpgykekvefgvLVSFAYKVQGsdsDEE 529
Cdd:PRK13208 150 YRRISQKSFLDLYKKGLIYRAEAPVLWCPRCETAIAQAEVEYREREGK----------------LNYIKFPVED---GEE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 530 VVVATTRIETMLGDVAVAVHPKDPRYQHLKGKCVVHPFLSRSLPIVFDDFVDMEFGTGAVKITPAHDQNDYEVGQRHRLE 609
Cdd:PRK13208 211 IEIATTRPELLPACVAVVVHPDDERYKHLVGKTAIVPLFGVEVPILADPLVDPDFGTGAVMICTFGDKTDVTWWRELNLP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 610 AISIMDSKGALINVPPPFLGLPRFEARKAVLAALKERGLFRGIKDNPMVVPLCNRSKDVVEPLLRPQWYVRCGEMAQAAs 689
Cdd:PRK13208 291 TRIIIDEDGRMTEAAGKLAGLTIEEARKKIVEDLKSGGLLGKQEPIKHNVKFCERCDTPLEILVTRQWFIKVLDLKEEL- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 690 aaVTRGD-LRILPEAHQRTWHSWMDNIR-DWCISRQ--------LWW----GHRIPA----YFItvhDPA--VPPGEDPD 749
Cdd:PRK13208 370 --LERGKeINWYPEHMRVRLENWIEGLNwDWCISRQryfgtpipVWYckdcGHPILPdeedLPV---DPTkdEPPGYKCP 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 750 GRywvsGRTEAEArekaarefgvspdkislqqDEDVLDTWFSSGLFPFSIFGWPNQSEDLSVFYPGTLLETGHDILFFW- 828
Cdd:PRK13208 445 QC----GSPGFEG-------------------ETDVMDTWATSSITPLIVTGWERDEDLFEKVFPMDLRPQGHDIIRTWl 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 829 ---VARMVMLglklTGKLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVIhgvslqglydqllnsnldpsevekakegq 905
Cdd:PRK13208 502 fytILRAYLL----TGKLPWKNIMISGMVLDPDGKKMSKSKGNVVTPEELL----------------------------- 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 906 kadfpagiPECGTDALRFGLcAYTSQGRDINLDVNRI-LGYRhFCNKLWNATKFALrGLGKGFVPSATSKPEghesLVDR 984
Cdd:PRK13208 549 --------EKYGADAVRYWA-ASARLGSDTPFDEKQVkIGRR-LLTKLWNASRFVL-HFSADPEPDKAEVLE----PLDR 613
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 985 WIRSRLTEAVRLSNEGFQAYDFPAITTAQYSFWLYELCDVYLECLKPVL-NGVDQVAAECARQTLYTCLDVGLRLLSPFM 1063
Cdd:PRK13208 614 WILAKLAKVVEKATEALENYDFAKALEEIESFFWHVFCDDYLELVKSRAyGEDEEEEQKSARYTLYTVLDTLLRLLAPFL 693
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 1064 PFVTEELFQRLPRRtpkapaSLCVTPYPEPSEcSWKDPEAEAALELALSITRAVRSLRADYNLTRTRPdcfLEVADEATG 1143
Cdd:PRK13208 694 PFITEEVWSWLYGG------SVHRASWPEPDE-ELIDEEDEELGELAKEILSAVRKYKSEAGLSLNAP---LKKVEVYGP 763
|
890 900 910
....*....|....*....|....*....|
gi 31565370 1144 ALASAVSGYVQALASAGVVAVLALGAPAPQ 1173
Cdd:PRK13208 764 ADLELLEAAEEDLKAAGNIEELELVEGDPE 793
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
342-1148 |
3.49e-86 |
|
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: 301.61 E-value: 3.49e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 342 PPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCD-HaGIATQVVVEKKLwkerGLNR---HQLGREAFLEE--- 414
Cdd:COG0060 54 PPYANGDIHIGHALNKILKDIIVRYKTMRGFDVPYVPGWDcH-GLPIELKVEKEL----GIKKkdiEKVGIAEFREKcre 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 415 -VWKWKAEKGDriyhQLKKLGSSLDWDRACFTMDPKLSATVTEAFVRLHEEGVIYRSTRLVNWSCTLNSAISDIEVdkke 493
Cdd:COG0060 129 yALKYVDEQRE----DFKRLGVWGDWDNPYLTMDPEYEESIWWALKKLYEKGLLYKGLKPVPWCPRCGTALAEAEV---- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 494 ltgrtllpvpGYKEKVEFGVLVSFayKVQGS-----DSDEEVVVATTRIETMLGDVAVAVHP---------KDPRY---- 555
Cdd:COG0060 201 ----------EYKDVTSPSIYVKF--PVKDEkalllLEDAYLVIWTTTPWTLPANLAVAVHPdidyvlvevTGGERlila 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 556 ------------------------QHLKGKCVVHPFL-----SRSLPIVFDDFVDMEFGTGAVKITPAHDQNDYEVGQRH 606
Cdd:COG0060 269 ealveavlkelgiedyevlatfkgAELEGLRYEHPFYyvvgyDRAHPVILGDYVTTEDGTGIVHTAPGHGEDDFEVGKKY 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 607 RLEAISIMDSKGALINVPPPFLGLPRFEARKAVLAALKERG-LFRGIKdnpmVV---PLCNRSKdvvEPLL---RPQWYV 679
Cdd:COG0060 349 GLPVLNPVDDDGRFTEEAPLFAGLFVKDANPAIIEDLKERGaLLAREK----IThsyPHCWRCK---TPLIyraTPQWFI 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 680 RCGEMAQAASAAVTR-------GDLRIlpeahqrtwHSWMDNIRDWCISRQLWWGHRIPAYfitVHDPavpPGEDPDGRY 752
Cdd:COG0060 422 SMDKLRDRALEAIEKvnwipewGEGRF---------GNMLENRPDWCISRQRYWGVPIPIW---VCED---CGELHRTEE 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 753 WVSGRTEAEAREKAAREFGVSPDKISLQQD-------------EDVLDTWFSSGLFPFSIFgwpNQSEDLSvfYPGTL-L 818
Cdd:COG0060 487 VIGSVAELLEEEGADAWFELDLHRPFLDETlkcpkcggtmrrvPDVLDVWFDSGSMHFAVL---ENREELH--FPADFyL 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 819 EtGHD---------ILffwvarmvmLGLKLTGKLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVIhgvslqglyDQLl 889
Cdd:COG0060 562 E-GSDqtrgwfyssLL---------TSTALFGRAPYKNVLTHGFVLDEDGRKMSKSLGNVVDPQEVI---------DKY- 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 890 nsnldpsevekakegqkadfpagipecGTDALRFgLCAYTSQGRDINLDVNRILGYRHFCNKLWNATKFALRGLGkGFVP 969
Cdd:COG0060 622 ---------------------------GADILRL-WVASSDYWGDLRFSDEILKEVRDVYRRLRNTYRFLLANLD-DFDP 672
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 970 SATSKPEGHESLVDRWIRSRLTEAVRLSNEGFQAYDFPAITTAqysfwLYELCDV-----YLECLKPVL--NGVDQVAAE 1042
Cdd:COG0060 673 AEDAVPYEDLPELDRWILSRLNELIKEVTEAYDNYDFHRAYRA-----LHNFCVEdlsnwYLDISKDRLytEAADSLDRR 747
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 1043 CARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRrtpKAPASLCVTPYPEPSEcSWKDPeaeaalelalsitravrSLRA 1122
Cdd:COG0060 748 AAQTTLYEVLETLVRLLAPILPFTAEEIWQNLPG---EAEESVHLADWPEVDE-ELIDE-----------------ELEA 806
|
890 900
....*....|....*....|....*.
gi 31565370 1123 DYNLTRtrpdcflEVADEATGALASA 1148
Cdd:COG0060 807 KWDLVR-------EVRSAVLKALEAA 825
|
|
| Anticodon_Ia_Val |
cd07962 |
Anticodon-binding domain of valyl tRNA synthetases; This domain is found in valyl tRNA ... |
937-1074 |
6.26e-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: 204.33 E-value: 6.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 937 LDVNRILGYRHFCNKLWNATKFALRGLGKGFVPSATSKPEgheSLVDRWIRSRLTEAVRLSNEGFQAYDFPAITTAQYSF 1016
Cdd:cd07962 1 FDEKRVEGGRNFCNKLWNAARFVLMNLEDDDEPEEDPESL---SLADRWILSRLNKTVEEVTEALENYRFSEAATALYEF 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 31565370 1017 WLYELCDVYLECLKPVLNGVDQVAAECARQTLYTCLDVGLRLLSPFMPFVTEELFQRL 1074
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 |
2.36e-59 |
|
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: 199.29 E-value: 2.36e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 92 AAVLVQQWVSYADTELIPAACGATLPALGLRG-PGQDPQAALGALGKALNPLEDWLRLHTYLAGDAPTLADLAAVTALLL 170
Cdd:cd10294 1 ACALVWQWVSFADNELTPAACAAAFPLLGLSGsDKQNQQRSLAELQRVLKVLDCYLKLRTYLVGEAITLADIAVACALLL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 31565370 171 PFRYVLDPSARRIWGNVTRWFNTCVRQPEFRAVLGEVALYSGA 213
Cdd:cd10294 81 PFKYVLDPARRESLLNVTRWFLTCVNQPEFLAVLGEVSLCEKA 123
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
335-876 |
5.65e-51 |
|
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: 182.62 E-value: 5.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 335 VFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKKLwkerGLNRHQLGREAFLEE 414
Cdd:cd00668 1 KFYVTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKG----GRKKKTIWIEEFRED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 415 VWKWKAEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSATVTEAFVRLHEEGviyrstrlvnwsctlnsaisdievdkkel 494
Cdd:cd00668 77 PKEFVEEMSGEHKEDFRRLGISYDWSDEYITTEPEYSKAVELIFSRLYEKG----------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 495 tgrtllpvpgykekvefgvlvsFAYKvqgsdsDEEVVVATtrietmlgdvavavhpkdpryqhlkgkcvvhpflsrslpi 574
Cdd:cd00668 128 ----------------------LIYR------GTHPVRIT---------------------------------------- 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 575 vfddfvdmefgtgavkitpahdqndyevgqrhrleaisimdskgalinvpppflglprfearkavlaalkerglfrgikd 654
Cdd:cd00668 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 655 npmvvplcnrskdvvepllrPQWYVRCGEMAQAASAAVTRGDlrILPEAHQRTWHSWMDNIRDWCISRQLWWGHRIPayf 734
Cdd:cd00668 140 --------------------EQWFFDMPKFKEKLLKALRRGK--IVPEHVKNRMEAWLESLLDWAISRQRYWGTPLP--- 194
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 735 itvhdpavppgedpdgrywvsgrteaearekaarefgvspdkislqqdEDVLDTWFSSGLFPFSIFGWPNQSEDLSVFYP 814
Cdd:cd00668 195 ------------------------------------------------EDVFDVWFDSGIGPLGSLGYPEEKEWFKDSYP 226
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31565370 815 GTLLETGHDILFFWVARMVMLGLKLTGKLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVI 876
Cdd:cd00668 227 ADWHLIGKDILRGWANFWITMLVALFGEIPPKNLLVHGFVLDEGGQKMSKSKGNVIDPSDVV 288
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
311-1098 |
4.47e-47 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 183.82 E-value: 4.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 311 WWERQGFFKpeygrpSVSAPNPRGVFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVV 390
Cdd:PLN02843 15 LWEENQVYK------RVSDRNNGESFTLHDGPPYANGDLHIGHALNKILKDFINRYQLLQGKKVHYVPGWDCHGLPIELK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 391 VEKKLWKERglnRHQLGREAFLEEVWKWKAEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSATVTEAFVRLHEEGVIYRS 470
Cdd:PLN02843 89 VLQSLDQEA---RKELTPIKLRAKAAKFAKKTVDTQRESFKRYGVWGDWENPYLTLDPEYEAAQIEVFGQMFLNGYIYRG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 471 TRLVNWSCTLNSAISDIEVDKKEltgrtllpvpGYKEKVEFGVL-VSFAYKVQGSDSDE-----EVVVATTRIETMLGDV 544
Cdd:PLN02843 166 RKPVHWSPSSRTALAEAELEYPE----------GHVSKSIYVAFpVVSPSETSPEELEEflpglSLAIWTTTPWTMPANA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 545 AVAVHPK----------------------DPRYQHL-----KGKCVV--------------------------------- 564
Cdd:PLN02843 236 AVAVNDKlqysvvevqsfsedestsggnkKKRPGNVlkeqqKLFLIVatdlvpaleakwgvklvvlktfpgsdlegcryi 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 565 HPFLSRSLPIVFD-DFVDMEFGTGAVKITPAHDQNDYEVGQRHRLEAISIMDSKGALINVPPPFLGLPRF-EARKAVLAA 642
Cdd:PLN02843 316 HPLYNRESPVVIGgDYITTESGTGLVHTAPGHGQEDYITGLKYGLPLLSPVDDAGKFTEEAGQFSGLSVLgEGNAAVVEA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 643 LKERGLFrgIKDNPMV--VPLCNRSKdvvEP-LLRP--QWYVRCGEMAQAASAAVtrGDLRILPEAHQRTWHSWMDNIRD 717
Cdd:PLN02843 396 LDEAGSL--LMEEAYGhkYPYDWRTK---KPtIFRAteQWFASVEGFRQAALDAI--DKVKWIPAQGENRIRAMVSGRSD 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 718 WCISRQLWWGHRIPAYF------------ITVHDPAVPPGEDPDGrYW---VSGRTEAEAREKAARefgvspdkisLQQD 782
Cdd:PLN02843 469 WCISRQRTWGVPIPVFYhvetkeplmneeTIAHVKSIVAQKGSDA-WWymdVEDLLPEKYRDKASD----------YEKG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 783 EDVLDTWFSSGlfpFSIFGWPNQSEDLSvfYPGTLLETGHDILFFWVARMVMLGLKLTGKLPFREVYLHAIVRDAHGRKM 862
Cdd:PLN02843 538 TDTMDVWFDSG---SSWAGVLGSREGLS--YPADLYLEGSDQHRGWFQSSLLTSVATKGKAPYKSVLTHGFVLDEKGFKM 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 863 SKSLGNVIDPLDVIHGvslqglydqllnsnldpsevekaKEGQKADfpagiPECGTDALRFGLCA--YTSqgrDINLDVN 940
Cdd:PLN02843 613 SKSLGNVVDPRLVIEG-----------------------GKNQKQE-----PAYGADVLRLWVASvdYTG---DVLIGPQ 661
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 941 rIL-----GYRhfcnKLWNATKFALRGLGKgFVPSATSKpegHESL--VDRWIRSRLTEAVRLSNEGFQAYDFPAITTAQ 1013
Cdd:PLN02843 662 -ILkqmsdIYR----KLRGTLRYLLGNLHD-WKPDNAVP---YEDLpsIDKYALFQLENVVNEIEESYDNYQFFKIFQIL 732
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 1014 YSFWLYELCDVYLECLKPVL--NGVDQVAAECARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRTPKAPA-SLCVTPY 1090
Cdd:PLN02843 733 QRFTIVDLSNFYLDVAKDRLyvGGTTSFTRRSCQTVLAAHLLSLLRAIAPILPHLAEDAWQNLPFQEDGSAAeSVFEAGW 812
|
....*...
gi 31565370 1091 PEPSEcSW 1098
Cdd:PLN02843 813 PTPNE-EW 819
|
|
| PLN02882 |
PLN02882 |
aminoacyl-tRNA ligase |
342-1095 |
3.72e-44 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215477 [Multi-domain] Cd Length: 1159 Bit Score: 175.30 E-value: 3.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 342 PPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKKLWKERGLNRHQLGREAFLEE----VWK 417
Cdd:PLN02882 46 PPFATGLPHYGHILAGTIKDIVTRYQSMTGHHVTRRFGWDCHGLPVEYEIDKKLGIKRRDDVLKMGIDKYNEEcrsiVTR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 418 WKAEKGDRIyhqlKKLGSSLDWDRACFTMDPKLSATVTEAFVRLHEEGVIYRSTRLVNWSCTLNSAISDIEVDKKeltgr 497
Cdd:PLN02882 126 YSKEWEKTV----TRTGRWIDFENDYKTMDPKFMESVWWVFKQLFEKGLVYKGFKVMPYSTACKTPLSNFEAGLN----- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 498 tllpvpgYKEKVEFGVLVSFAykVQGsDSDEEVVVA-TTRIETMLGDVAVAVHPK------------------DPRYQHL 558
Cdd:PLN02882 197 -------YKDVSDPAVMVSFP--IVG-DPDNASFVAwTTTPWTLPSNLALCVNPNftyvkvrnkytgkvyivaESRLSAL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 559 --------KGK---------CVVHPFLSRSL------PI--------------VFDDFVDMEFGTGAVKITPAHDQNDYE 601
Cdd:PLN02882 267 ptakpkskKGSkpenaaegyEVLAKVPGSSLvgkkyePLfdyfsefsdtafrvVADDYVTDDSGTGVVHCAPAFGEDDYR 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 602 VGQRHRL-----EAISIMDSKGALINVPPPFLGLPRFEARKAVLAALKERGlfRGIKDNPMV--VPLCNRSKdvvEPLLR 674
Cdd:PLN02882 347 VCLANGIiekggNLPVPVDDDGCFTEKVTDFSGRYVKDADKDIIAAIKAKG--RLVKSGSIThsYPFCWRSD---TPLIY 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 675 ---PQWYVRCGEMAQaasaavtrgdlRILPEAHQRTW----------HSWMDNIRDWCISRQLWWGHRIPAYFitvhdpa 741
Cdd:PLN02882 422 ravPSWFVKVEEIKD-----------RLLENNKQTYWvpdyvkekrfHNWLENARDWAVSRSRFWGTPLPIWI------- 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 742 vppgeDPDGRYWVSGRTEAEARE---------------------KAAREFGVspdkisLQQDEDVLDTWFSSGLFPFSIF 800
Cdd:PLN02882 484 -----SDDGEEVVVIGSIAELEKlsgvkvtdlhrhfidhitipsSRGPEFGV------LRRVDDVFDCWFESGSMPYAYI 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 801 GWPNQSEDLsvF---YPGTLLETGHDILFFWVARMVMLGLKLTGKLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVIH 877
Cdd:PLN02882 553 HYPFENKEL--FeknFPADFVAEGLDQTRGWFYTLMVLSTALFDKPAFKNLICNGLVLAEDGKKMSKSLKNYPDPNEVID 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 878 GVSLQGLYDQLLNSnldpsevekakegqkadfpagiPECGTDALRFGLCAYTSQGRDINLD-VNrilGYRHFcnkLWNAT 956
Cdd:PLN02882 631 KYGADALRLYLINS----------------------PVVRAEPLRFKEEGVFGVVKDVFLPwYN---AYRFL---VQNAK 682
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 957 KFALRGLGKgFVPSATSKPEGHESLVDRWIRSRLTEAVRLSNEGFQAYDFPAITTAQYSFwLYELCDVYLECLKPVLNGV 1036
Cdd:PLN02882 683 RLEVEGGAP-FVPLDLAKLQNSANVLDRWINSATQSLVKFVREEMGAYRLYTVVPYLVKF-IDNLTNIYVRFNRKRLKGR 760
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 1037 DQVA-AECARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRTPKAPASLCVTPYPEPSE 1095
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 |
1.52e-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: 148.48 E-value: 1.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 92 AAVLVQQWVSYADTELIPAACGATLPALGLRGPG-QDPQAALGALGKALNPLEDWLRLHTYLAGDAPTLADLAAVTALLL 170
Cdd:cd03181 1 EAAQVLQWISFANSELLPAAATWVLPLLGIAPYNkKAVDKAKEDLKRALGVLEEHLLTRTYLVGERITLADIFVASALLR 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 31565370 171 PFRYVLDPSARRIWGNVTRWFNTCVRQPEFRAVLGEVAL 209
Cdd:cd03181 81 GFETVLDPEFRKKYPNVTRWFNTVVNQPKFKAVFGEVKL 119
|
|
| PTZ00427 |
PTZ00427 |
isoleucine-tRNA ligase, putative; Provisional |
342-1076 |
2.35e-35 |
|
isoleucine-tRNA ligase, putative; Provisional
Pssm-ID: 173617 [Multi-domain] Cd Length: 1205 Bit Score: 147.04 E-value: 2.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 342 PPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIAtqvvVEKKLWKERGLNRHQ----LGREAFLEEVWK 417
Cdd:PTZ00427 110 PPFATGLPHYGHLLAGIIKDCVTRYFYQCGFSVERKFGWDCHGLP----IEYEIEKENNINKKEdilkMGIDVYNEKCRG 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 418 WKAEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSATVTEAFVRLHEEGVIYRSTRLVNWSCTLNSAISDIEV-------- 489
Cdd:PTZ00427 186 IVLKYSNEWVKTVERIGRWIDFKNDYKTMDKTFMESVWWVFSELYKNNYVYKSFKVMPYSCKCNTPISNFELnlnykdtp 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 490 ------------------------DKKELTGRTLLPVpgYKEKVEFG--------------------------------- 512
Cdd:PTZ00427 266 dpsiiisfvlcsdfpkveeecnieEDKQLLGEKYSVL--YNNKRENSnngnnnstnnvcyaqhseilawtttpwtlpsnl 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 513 ---VLVSFAY-KVQGSDSDEEVVVATTRIETMLGDVAVAV------------HPKDPRYQHLKGKCV-VHPFLSRSLPIV 575
Cdd:PTZ00427 344 alcVNEHFTYlRIHHVKSNRVVIVGECRLEWIMKELKWNVedlkivnrfkgkELKGLRYKPLFTNFYeKYNFKERAYKIL 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 576 FDDFVDMEFGTGAVKITPAHDQNDYEVGQRHRL----EAISI--MDSKGALINVPPPFLGLPRFEARKAVLAALKERGlf 649
Cdd:PTZ00427 424 ADDFVTDDAGTGIVHCAPTYGEDDFRVCKKNGVidpeKNIFIdpLDANGYFTNEVEEVQNLYIKEADNVIKKKLKNEN-- 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 650 RGIKDNPMV--VPLCNRSKdvvEPLLR---PQWYVRcgeMAQAASAAVTRGDLRILPEAH--QRTWHSWMDNIRDWCISR 722
Cdd:PTZ00427 502 RLLSNNTIVhsYPFCWRSD---TPLIYraiPAWFIR---VSNSTNELVKNNETTYWIPAHikEKKFHNWIKDAKDWCISR 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 723 QLWWGHRIPAY-------FITVHdpAVPPGEDPDG--------RYWVSgrtEAEAREKAAREFGvspdkiSLQQDEDVLD 787
Cdd:PTZ00427 576 NRYWGTPIPIWadekmetVICVE--SIKHLEELSGvknindlhRHFID---HIEIKNPKGKTYP------KLKRIPEVFD 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 788 TWFSSGLFPFSIFGWP--NQSEDLSVFYPGTLLETGHDILFFWVARMVMLGLKLTGKLPFREVYLHAIVRDAHGRKMSKS 865
Cdd:PTZ00427 645 CWFESGSMPYAKVHYPfsTEKEDFHKIFPADFIAEGLDQTRGWFYTLLVISTLLFDKAPFKNLICNGLVLASDGKKMSKR 724
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 866 LGNVIDPLDVIHGVSLQGLYDQLLNSNLDPSEVEKAKEgqkadfpAGIPEcgtdALRFGLCAYTSQGRDINLDVNRIlgy 945
Cdd:PTZ00427 725 LKNYPDPLYILDKYGADSLRLYLINSVAVRAENLKFQE-------KGVNE----VVKSFILPFYHSFRFFSQEVTRY--- 790
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 946 rhfcnKLWNATKFALRglgkgfvpsaTSKPEGHESLVDRWIRSRLTEAVRLSNEGFQAYDFPAITTAQYSFwLYELCDVY 1025
Cdd:PTZ00427 791 -----ECLNKKQFLFN----------TDYIYKNDNIMDQWIFSSVQSLTKSVHTEMKAYKLYNVLPKLLQF-IENLTNWY 854
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 31565370 1026 LECLKPVLNGV----DQVAAECarqTLYTCLDVGLRLLSPFMPFVTEELFQRLPR 1076
Cdd:PTZ00427 855 IRLNRDRMRGSlgeeNCLQSLC---TTYRTLHLFTVLMAPFTPFITEYIYQQLRR 906
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
342-892 |
2.35e-30 |
|
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: 123.50 E-value: 2.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 342 PPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKKLWKERGLNRHQLGREAFLEEVWKWKAE 421
Cdd:cd00818 9 PPYANGLPHYGHALNKILKDIINRYKTMQGYYVPRRPGWDCHGLPIELKVEKELGISGKKDIEKMGIAEFNAKCREFALR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 422 KGDRIYHQLKKLGSSLDWDRACFTMDPKLSATVTEAFVRLHEEGVIYRSTRLVNWsctlnsaisdievdkkeltgrtllp 501
Cdd:cd00818 89 YVDEQEEQFQRLGVWVDWENPYKTMDPEYMESVWWVFKQLHEKGLLYRGYKVVPW------------------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 502 vpgykekvefgvlvsfaykvqgsdsdeevvvattrietmlgdvavavhpkdpryqhlkgkcvvhpflsrslPIVFddfvd 581
Cdd:cd00818 144 -----------------------------------------------------------------------PLIY----- 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 582 mefgtgavkitpahdqndyevgqrhrleaisimdskgalinvpppflglprfearKAVlaalkerglfrgikdnpmvvpl 661
Cdd:cd00818 148 -------------------------------------------------------RAT---------------------- 150
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 662 cnrskdvvepllrPQWYVRCGEMAQAASAAVTRgdLRILPEAHQRTWHSWMDNIRDWCISRQLWWGHRIPAyfitvhdpa 741
Cdd:cd00818 151 -------------PQWFIRVTKIKDRLLEANDK--VNWIPEWVKNRFGNWLENRRDWCISRQRYWGTPIPV--------- 206
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 742 vppgedpdgryWVSgrteaearekaarefgVSPDKISLQQDEDVLDTWFSSGLFPFSIFGWPNQSEDLSVFYPGTLLETG 821
Cdd:cd00818 207 -----------WYC----------------EDCGEVLVRRVPDVLDVWFDSGSMPYAQLHYPFENEDFEELFPADFILEG 259
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31565370 822 HDILFFWVARMVMLGLKLTGKLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVI--HGVSLQGLYdqLLNSN 892
Cdd:cd00818 260 SDQTRGWFYSLLLLSTALFGKAPYKNVIVHGFVLDEDGRKMSKSLGNYVDPQEVVdkYGADALRLW--VASSD 330
|
|
| leuS_bact |
TIGR00396 |
leucyl-tRNA synthetase, eubacterial and mitochondrial family; The leucyl-tRNA synthetases ... |
299-1074 |
7.27e-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: 128.33 E-value: 7.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 299 YSPQYVEAAWYPWWERQGFFKPEygrpsvSAPNPRGVFMMCI-PPPnvTGSLHLGHALTNAIQDSLTRWHRMRGETTLWN 377
Cdd:TIGR00396 1 YNHIEIEEKWQQKWDENKTFKVT------DDSSKPKYYILSMfPYP--SGALHMGHVRNYTITDVLSRYYRMKGYNVLHP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 378 PGCDHAGI-ATQVVVEkklwkeRGLNRHqlgreafleevwKWKAEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSATVTE 456
Cdd:TIGR00396 73 IGWDAFGLpAENAAIK------RGIHPA------------KWTYENIANMKKQLQALGFSYDWDREIATCDPEYYKWTQW 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 457 AFVRLHEEGVIYRSTRLVNWSCTLNSAI-------------SDIEVDKKELTgRTLLPVPGYKEKV-------------- 509
Cdd:TIGR00396 135 IFLELFEKGLAYVKEADVNWCPNDGTVLaneqvdsdgrswrGDTPVEKKELK-QWFLKITAYAEELlndleeldhwpesv 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 510 ----------EFGVLVSFAYKvqgsDSDEEVVVATTRIETMLGDVAVAVHPKDPRYQH---------------------- 557
Cdd:TIGR00396 214 kemqrnwigkSEGVEITFKIA----DHDEKITVFTTRPDTIFGVTYLALAPEHPLVEKaaennpkvaafikkilnktvae 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 558 -----------LKGKCVVHPFLSRSLPIVFDDFVDMEFGTGAVKITPAHDQNDYEVGQRHRLEAISIMDS---------- 616
Cdd:TIGR00396 290 rtkatkekkgvDTGIKAIHPLTGEKIPIWVANYVLMEYGTGAVMGVPAHDERDFEFAQKYGLPIKPVIDPaekdlsltaa 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 617 ---KGALINvPPPFLGLPRFEARKAVLAALKERGLfrgikdnpmvvplcnrSKDVVEpllrpqwYvrcgemaqaasaavt 693
Cdd:TIGR00396 370 yteDGVLVN-SGEFNGLNSSEARNAIIDMLEKEGK----------------GKRKVN-------Y--------------- 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 694 rgdlrilpeahqrtwhswmdNIRDWCISRQLWWGHRIPAYFITVHDPAVPPGED------------PDG-------RYWV 754
Cdd:TIGR00396 411 --------------------RLRDWGFSRQRYWGEPIPIIHCEDGGVVPVPEEDlpvilpedvvydGDGgsplsriPEWV 470
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 755 SgRTEAEAREKAAREfgvspdkislqqdEDVLDTWFSSG--LFPFSIFGWPNQSED---LSVFYPGTLLETG--HDILF- 826
Cdd:TIGR00396 471 N-VTCPSCGKPALRE-------------TDTMDTFAGSSwyYLRYLDPKNTDGPFDkekAEYWLPVDLYIGGieHAILHl 536
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 827 ----FWVARMVMLGLkLTGKLPFREVYLHAIV-----------------------RDAHGR--------KMSKSLGNVID 871
Cdd:TIGR00396 537 lyarFFHKFLRDIGY-VNTKEPFKKLINQGMVlgfyyppngkvpadvlterdekgKDKAGGelvyvgyeKMSKSKGNGID 615
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 872 PLDVIHgvslqglydqllnsnldpsevekakegqkadfpagipECGTDALRFGLCAYTSQGRDINLDVNRILGYRHFCNK 951
Cdd:TIGR00396 616 PQEIVE-------------------------------------SYGADALRLFIMFMGPIAASLEWNESGLEGARRFLDR 658
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 952 LWNatkFALRGLGKgfvPSATSKPEGHESLVDRWIRSRLTEAVRLSNEGFQ-AYDF-PAIttAQYSFWLYEL-----CDV 1024
Cdd:TIGR00396 659 VWN---LVYEITGE---LDAASLTVTALEEAQKELRRDVHKFLKKVTEDLEkRESFnTAI--SAMMELLNKLykakkEAL 730
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 31565370 1025 YLECLKPVlngvdqvaaecarqtlytcldvgLRLLSPFMPFVTEELFQRL 1074
Cdd:TIGR00396 731 MLEYLKGF-----------------------VTVLSPFAPHLAEELWEKL 757
|
|
| Anticodon_1 |
pfam08264 |
Anticodon-binding domain of tRNA ligase; This domain is found mainly hydrophobic tRNA ... |
983-1126 |
1.39e-28 |
|
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: 112.11 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 983 DRWIRSRLTEAVRLSNEGFQAYDFPAITTAQYSFWLYELCDVYLECLKPVLNGVDqvAAECARQTLYTCLDVGLRLLSPF 1062
Cdd:pfam08264 1 DRWILSRLNKLIKEVTEAYENYRFNTAAQALYEFFWNDLSDWYLELIKDRLYGEE--PDSRAQTTLYEVLETLLRLLAPF 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31565370 1063 MPFVTEELFQRLprrtpkapaSLCVTPYPEPSECSwkDPEAEAALELALSITRAVRSLRADYNL 1126
Cdd:pfam08264 79 MPFITEELWQKE---------SIHLAPWPEDAELE--EAELEEAFELRQEIVQAIRKLRSELKI 131
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
295-876 |
3.65e-26 |
|
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: 116.30 E-value: 3.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 295 MPDSYSPQYVEAAWYPWWERQGFFKpeygrpsvsAPNPRG-----VFMMcIPPPnvTGSLHLGHALTNAIQDSLTRWHRM 369
Cdd:COG0495 1 MQERYNPKEIEKKWQKYWEENGTFK---------ADEDSSkpkyyVLDM-FPYP--SGRLHMGHVRNYTIGDVVARYKRM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 370 RGETTLwNP-GCD-------HAGIATQVvvekklwkerglnrHqlgrEAfleevwKWKAEKGDRIYHQLKKLGSSLDWDR 441
Cdd:COG0495 69 QGYNVL-HPmGWDafglpaeNAAIKNGV--------------H----PA------EWTYENIANMRRQLKRLGLSYDWSR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 442 ACFTMDP-------KLsatvteaFVRLHEEGVIYRSTRLVNWSCTLN------------SAISDIEVDKKELTG------ 496
Cdd:COG0495 124 EIATCDPeyykwtqWI-------FLQLYEKGLAYRKEAPVNWCPVDQtvlaneqvidgrCWRCGAPVEKKELPQwflkit 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 497 ----RtLL----PVPGYKEKV----------EFGVLVSFAYKvqgsDSDEEVVVATTRIETMLGD--VAVAV-HP----- 550
Cdd:COG0495 197 dyadE-LLddldKLDGWPEKVktmqrnwigrSEGAEVDFPVE----GSDEKITVFTTRPDTLFGAtfMVLAPeHPlvkel 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 551 ----KDPRYQHLKGKC-----------------------VVHPFLSRSLPIVFDDFVDMEFGTGAVKITPAHDQNDYEVG 603
Cdd:COG0495 272 atpeQNAAVAAFIEEAkkkseiertsetkektgvftglyAINPLTGEKIPIWIADYVLMDYGTGAVMAVPAHDQRDFEFA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 604 QRHRL-----------EAISIMDS----KGALINvPPPFLGLPRFEARKAVLAALKERGLfrgikdnpmvvplcnrskdv 668
Cdd:COG0495 352 KKYGLpikqviapedgDDPDILEEaytgDGVLIN-SGEFDGLDSEEAKEAIIEWLEEKGL-------------------- 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 669 vepllrpqwyvrcGEmaqaasAAVT-RgdlrilpeahqrtwhswmdnIRDWCISRQLWWGHRIPAyfitVHDP-----AV 742
Cdd:COG0495 411 -------------GK------RKVNyR--------------------LRDWLISRQRYWGEPIPI----IHCEdcgvvPV 447
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 743 P----------------PGEDPDGRY--WVS------GRteaeareKAAREFgvspdkislqqdeDVLDTWF-SSglfpf 797
Cdd:COG0495 448 PedqlpvelpedvdfdpTGGSPLARApeWVNvtcpkcGG-------PARRET-------------DTMDTFVdSS----- 502
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 798 sifgW-------PNQSE--------------DLsvfYPGtlletG--HDIL------FFWvarMVM--LGLkLTGKLPFR 846
Cdd:COG0495 503 ----WyylrytdPHNDEapfdpeaanywlpvDQ---YIG-----GieHAILhllyarFFT---KVLrdLGL-VSFDEPFK 566
|
730 740 750
....*....|....*....|....*....|....*....
gi 31565370 847 ---------EVYLHAIVRDAHGrKMSKSLGNVIDPLDVI 876
Cdd:COG0495 567 rlltqgmvlEVGKDGVVIGGIE-KMSKSKGNVVDPDEII 604
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
349-1101 |
2.64e-23 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 107.26 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 349 LHLGHALTNAIQDSLTRWHRMRGETTLWnPGCDHA------GIATQV----------------VVEKKLWKerglnrhqL 406
Cdd:PRK12300 1 LHVGHGRTYTIGDVIARYKRMRGYNVLF-PMAFHVtgtpilGIAERIargdpetielykslygIPEEELEK--------F 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 407 GREAFLEEVWKWKAEKgdriyhQLKKLGSSLDWDRACFTMDPKLSATVTEAFVRLHEEGVIYRSTRLVNWSCTLNSAISD 486
Cdd:PRK12300 72 KDPEYIVEYFSEEAKE------DMKRIGYSIDWRREFTTTDPEYSKFIEWQFRKLKEKGLIVKGSHPVRYCPNDNNPVGD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 487 ieVDKKELTGrtllpvpgyKEKVEFgVLVSFAykvqgsDSDEEV-VVATTRIETMLGDVAVAVHPKDP------------ 553
Cdd:PRK12300 146 --HDLLDGEE---------PEIVEY-TLIKFE------ESEDLIlPAATLRPETIFGVTNLWVNPDATyvkaevdgekwi 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 554 ---------RYQH-------------LKGKCVVHPFLSRSLPIVFDDFVDMEFGTGAVKITPAHDQNDY----EVGQRHR 607
Cdd:PRK12300 208 vskeaaeklSFQDrdveiieeikgseLIGKKVKNPVTGKEVPILPADFVDPDNGTGVVMSVPAHAPYDYvalrDLKKNKE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 608 L----EAISIMD--------------------------------------SKGALINVPPPFLGLPRFEARKAVLAALKE 645
Cdd:PRK12300 288 LldviEPIPLIEvegygefpakevveklgiksqedpeleeatkevyraefHKGVLKENTGEYAGKPVREAREKITKDLIE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 646 RGLfrGIK----DNPMVVPLCNrSKDVVEpLLRPQWYVRCGEMAQAASA--AVTRgdLRILPEAHQRTWHSWMDNIRDWC 719
Cdd:PRK12300 368 KGI--ADImyefSNRPVYCRCG-TECVVK-VVKDQWFIDYSDPEWKELAhkALDN--MEIIPEEYRKEFENTIDWLKDRA 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 720 ISRQLWWGHRIP-----------------AYFITVHdpavppgedpdgrywvsgrteaearekAAREFGVSPDKIslqqD 782
Cdd:PRK12300 442 CARRRGLGTRLPwdeewiieslsdstiymAYYTIAH---------------------------KIREYGIKPEQL----T 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 783 EDVLDTWFSSGLFPFSIfgwpnqSEDLSVfyPGTLLETGHDILFFWVArmvmLGLKLTGK------LPFReVYLH-AIVR 855
Cdd:PRK12300 491 PEFFDYVFLGKGDPEEV------SKKTGI--PKEILEEMREEFLYWYP----VDWRHSGKdlipnhLTFF-IFNHvAIFP 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 856 DAH--------------GRKMSKSLGNVIdPLdvihgvslqglydqllnsnldpsevEKAKEgqkadfpagipECGTDAL 921
Cdd:PRK12300 558 EEKwprgivvngfvlleGKKMSKSKGNVI-PL-------------------------RKAIE-----------EYGADVV 600
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 922 RFGLCAYTSQGRDINLDVNRILGYRHFCNKLWNatkFALRGLGKGfvpsatskPEGHESLVDRWIRSRLTEAVRLSNEGF 1001
Cdd:PRK12300 601 RLYLTSSAELLQDADWREKEVESVRRQLERFYE---LAKELIEIG--------GEEELRFIDKWLLSRLNRIIKETTEAM 669
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 1002 QAYDF-PAITTAQYSfwLYELCDVYLEcLKPVLNgvdqvaaecaRQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRTpk 1080
Cdd:PRK12300 670 ESFQTrDAVQEAFYE--LLNDLRWYLR-RVGEAN----------NKVLREVLEIWIRLLAPFTPHLAEELWHKLGGEG-- 734
|
890 900
....*....|....*....|.
gi 31565370 1081 aPASLcvTPYPEPSEcSWKDP 1101
Cdd:PRK12300 735 -FVSL--EKWPEPDE-SKIDE 751
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
286-747 |
2.11e-20 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 97.97 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 286 GEKKDVSGAMPDSYSPQYVEAAWYPWWERQGFFK-PEygrpSVSAPNPRGVFMMCIPPPNVTGsLHLGHALTNAIQDSLT 364
Cdd:PLN02563 67 STTAKTTPAAKRAYPFHEIEPKWQRYWEENRTFRtPD----DVDTSKPKFYVLDMFPYPSGAG-LHVGHPEGYTATDILA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 365 RWHRMRGETTLWNPGCDHAGI-ATQVVVEK----KLWKERGLNRHQLgreafleevwkwkaekgdriyhQLKKLGSSLDW 439
Cdd:PLN02563 142 RYKRMQGYNVLHPMGWDAFGLpAEQYAIETgthpKITTLKNIARFRS----------------------QLKSLGFSYDW 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 440 DRACFTMDPKLSATVTEAFVRLHEEGVIYRSTRLVNWSCTLNSAISDIEVDK--KELTGRTLLPVP-------------- 503
Cdd:PLN02563 200 DREISTTEPEYYKWTQWIFLQLLKRGLAYQAEVPVNWCPALGTVLANEEVVDglSERGGHPVIRKPmrqwmlkitayadr 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 504 ------------GYKE------------KVEFGVLvsfayKVQGSDSDEEVVVATTRIETMLGDVAVAVHPKDP------ 553
Cdd:PLN02563 280 lledlddldwpeSIKEmqrnwigrsegaELDFSVL-----DGEGKERDEKITVYTTRPDTLFGATYLVVAPEHPllsslt 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 554 ----------------------RYQHLKGKCVV-------HPFLSRSLPIVFDDFVDMEFGTGAVKITPAHDQNDYEVGQ 604
Cdd:PLN02563 355 taeqkeaveeyvdaasrksdleRTELQKEKTGVftgsyaiNPATGEAIPIWVADYVLGSYGTGAIMAVPAHDTRDFEFAQ 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 605 RHRLEAISIMDS--------------KGALINVPPPFL---GLPRFEARKAVLAALKERGlfrgikdnpmvvplcNRSKD 667
Cdd:PLN02563 435 KFDLPIKWVVKPadgneddaekaytgEGVIVNSSSSGLdinGLSSKEAAKKVIEWLEETG---------------NGKKK 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 668 VVEPLlrpqwyvrcgemaqaasaavtrgdlrilpeahqrtwhswmdniRDWCISRQLWWGHRIPAYFITVHDPAVPPGED 747
Cdd:PLN02563 500 VNYKL-------------------------------------------RDWLFARQRYWGEPIPVVFLEDSGEPVPVPES 536
|
|
| Anticodon_Ia_Ile_ABEc |
cd07961 |
Anticodon-binding domain of archaeal, bacterial, and eukaryotic cytoplasmic isoleucyl tRNA ... |
946-1095 |
1.56e-17 |
|
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: 81.83 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 946 RHFCNKLWNATKFAL--RGLgKGFVPSATSKPEGHESLVDRWIRSRLTEAVRLSNEGFQAYDFPAITTAQYSFWLyELCD 1023
Cdd:cd07961 11 RKVLLPLWNAYRFFVtyANL-DGFDPGKDDDAVASLNVLDRWILSRLNSLIKEVTEEMEAYDLYTAVRALLEFID-ELTN 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31565370 1024 VYL----ECLKPVLNGVDQVAAecaRQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRTPKAPASLCVTPYPEPSE 1095
Cdd:cd07961 89 WYIrrnrKRFWGEEGDDDKLAA---YATLYEVLLTLSRLMAPFTPFITEEIYQNLRRELGDAPESVHLLDWPEVDE 161
|
|
| GST_C |
pfam00043 |
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ... |
107-198 |
2.50e-14 |
|
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: 69.62 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 107 LIPAACGATLPALGLR--GPGQDPQAALGALGKALNPLEDWLRLHTYLAGDAPTLADLAAVTALLLPFRYVLDPSaRRIW 184
Cdd:pfam00043 1 LMDLRMQIALLPYVPPeeKKEPEVDEALEKVARVLSALEEVLKGQTYLVGDKLTLADIALAPALLWLYELDPACL-REKF 79
|
90
....*....|....
gi 31565370 185 GNVTRWFNTCVRQP 198
Cdd:pfam00043 80 PNLKAWFERVAARP 93
|
|
| Anticodon_Ia_Ile_BEm |
cd07960 |
Anticodon-binding domain of bacterial and eukaryotic mitochondrial isoleucyl tRNA synthetases; ... |
945-1101 |
9.49e-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: 67.94 E-value: 9.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 945 YRhfcnKLWNATKFALRGLGkGFVPSATSKPEGHESLVDRWIRSRLTEAVRLSNEGFQAYDFPAITTAQYSFWLYELCDV 1024
Cdd:cd07960 13 YR----KIRNTFRFLLGNLN-DFDPAKDAVPYEELLELDRYALHRLNELIKEVREAYENYEFHKVYQALNNFCTVDLSAF 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31565370 1025 YLECLKPVL--NGVDQVAAECARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRTPKAPASLcvTPYPEPSEcSWKDP 1101
Cdd:cd07960 88 YLDIIKDRLycDAKDSLERRSAQTVLYHILDALLKLLAPILPFTAEEVWEHLPGEKKEESVFL--EDWPELPE-EWKDE 163
|
|
| GstA |
COG0625 |
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; |
56-206 |
2.84e-12 |
|
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440390 [Multi-domain] Cd Length: 205 Bit Score: 67.23 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 56 RLPALEqgPGGLWVWGAPAVAQLLwpAGLGG-----PGGSRAAVLVQQWVSYADTELIPAAcgatLPALGLRGPGQDP-- 128
Cdd:COG0625 52 KVPVLV--DDGLVLTESLAILEYL--AERYPeppllPADPAARARVRQWLAWADGDLHPAL----RNLLERLAPEKDPaa 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31565370 129 -QAALGALGKALNPLEDWLRLHTYLAGDAPTLADLAAVTALLLPFRYVLDPSArriWGNVTRWFNTCVRQPEFRAVLGE 206
Cdd:COG0625 124 iARARAELARLLAVLEARLAGGPYLAGDRFSIADIALAPVLRRLDRLGLDLAD---YPNLAAWLARLAARPAFQRALAA 199
|
|
| tRNA-synt_1_2 |
pfam13603 |
Leucyl-tRNA synthetase, Domain 2; This is a family of the conserved region of Leucine-tRNA ... |
512-639 |
3.44e-12 |
|
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: 66.42 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 512 GVLVSFAYKvqgsDSDEEVVVATTRIETMLGD--VAVAV-HP-------KDPRYQHLKGKC------------------- 562
Cdd:pfam13603 9 GAEITFPVE----GTDEKIEVFTTRPDTLMGVtfVALAPeHPlveklaeKNPEVAAFIEECkntseiertsetkekegvf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 563 ----VVHPFLSRSLPIVFDDFVDMEFGTGAVKITPAHDQNDYEVGQRHRL------------EAISIMDS----KGALIN 622
Cdd:pfam13603 85 tglyAIHPITGEKIPIWIANFVLMEYGTGAVMAVPAHDQRDFEFAKKYNLpikpviqpedgdLDLDIMTEayteEGILVN 164
|
170
....*....|....*..
gi 31565370 623 vPPPFLGLPRFEARKAV 639
Cdd:pfam13603 165 -SGEFDGLDSEEAKEAI 180
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
336-476 |
4.33e-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: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 336 FMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAG-----IATQVVVEKKLWKERGLNrhqlgrea 410
Cdd:cd00812 2 FYILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGlpaenAAIKIGRDPEDWTEYNIK-------- 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31565370 411 fleevwKWKAekgdriyhQLKKLGSSLDWDRACFTMDPKLSATVTEAFVRLHEEGVIYRSTRLVNW 476
Cdd:cd00812 74 ------KMKE--------QLKRMGFSYDWRREFTTCDPEYYKFTQWLFLKLYEKGLAYKKEAPVNW 125
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
710-1074 |
1.24e-10 |
|
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: 65.52 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 710 SWMDN-IRDWCISRQLWWGhrIPayfitvhdpaVPpgEDPDGRYWVsgrteaearekaarefgvspdkislqqdedvldt 788
Cdd:COG0143 217 SWLKEgLQDLSISRDFDWG--IP----------VP--GDPGKVFYV---------------------------------- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 789 WF-------SSglfpfsIFGWP---NQSEDLSVFYPGTLLETGH----DILFF----WVArMVM-LGLKLTGKLPfrevy 849
Cdd:COG0143 249 WFdaligyiSA------TKGYAddrGLPEDFEKYWPAPDTELVHfigkDIIRFhaiiWPA-MLMaAGLPLPKKVF----- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 850 lhaivrdAH------GRKMSKSLGNVIDPLDVIhgvslqglydqllnsnldpsevekakegqkADFPAgipecgtDALRF 923
Cdd:COG0143 317 -------AHgfltveGEKMSKSRGNVIDPDDLL------------------------------DRYGP-------DALRY 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 924 GLCAYTSQGRDINLD-------------------VNRILGyrhFCNKLWNatkfalrglgkGFVPSAtskpeGHESLVDR 984
Cdd:COG0143 353 YLLREVPFGQDGDFSwedfvarvnsdlandlgnlASRTLS---MIHKYFD-----------GKVPEP-----GELTEADE 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 985 WIRSRLTEAVRLSNEGFQAYDFPAITTAqysfwLYELCDV---YLECLKP-VLngVDQVAAECARQTLYTCLDVgLR--- 1057
Cdd:COG0143 414 ELLAEAEAALEEVAEAMEAFEFRKALEE-----IMALARAankYIDETAPwKL--AKDEDPERLATVLYTLLEA-LRila 485
|
410
....*....|....*...
gi 31565370 1058 -LLSPFMPFVTEELFQRL 1074
Cdd:COG0143 486 iLLKPFLPETAEKILEQL 503
|
|
| GST_C_family |
cd00299 |
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ... |
96-194 |
1.14e-08 |
|
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: 54.04 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 96 VQQWVSYADTELIPAACGATLPALGLRGPGQDPQ-AALGALGKALNPLEDWLRLHTYLAGDAPTLADLAAVTALLLPFRY 174
Cdd:cd00299 1 VRALEDWADATLAPPLVRLLYLEKVPLPKDEAAVeAAREELPALLAALEQLLAGRPYLAGDQFSLADVALAPVLARLEAL 80
|
90 100
....*....|....*....|
gi 31565370 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 ... |
940-1063 |
1.20e-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: 54.43 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 940 NRILGYRHFCNKLWNATKFALRGLGKGFVPSATSKPEGheslVDRWIRSRLTEAVRLSNEGFQAYDFPAITTAQYSFWLY 1019
Cdd:cd07375 2 ERLKQARAFLNRLYRLLSFFRKALGGTQPKWDNELLEE----ADRELLARLQEFIKRTTNALEALDPTTAVQELFKFTNE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 31565370 1020 ElcDVYLECLKPVLNgvDQVAAECARQTLYTCLDVGLRLLSPFM 1063
Cdd:cd07375 78 L--NWYLDELKPALQ--TEELREAVLAVLRAALVVLTKLLAPFT 117
|
|
| Anticodon_Ia_Leu_AEc |
cd07959 |
Anticodon-binding domain of archaeal and eukaryotic cytoplasmic leucyl tRNA synthetases; This ... |
970-1074 |
7.54e-08 |
|
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: 51.82 E-value: 7.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 970 SATSKPEGHESLVDRWIRSRLTEAVRLSNEGFQAYDF-PAITTAQYSFwlYELCDVYLEclkpvlngvdQVAAECARQTL 1048
Cdd:cd07959 24 IETEGELEELTFIDRWLLSRLNRLIKETTEAYENMQFrEALKEGLYEL--QNDLDWYRE----------RGGAGMNKDLL 91
|
90 100
....*....|....*....|....*.
gi 31565370 1049 YTCLDVGLRLLSPFMPFVTEELFQRL 1074
Cdd:cd07959 92 RRFIEVWTRLLAPFAPHLAEEIWHEL 117
|
|
| GST_C_AaRS_like |
cd10289 |
Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA ... |
93-194 |
9.34e-08 |
|
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: 50.77 E-value: 9.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 93 AVLVQQWVSYADTelipaacgatlpalGLRGPGQDPQAalgalgKALNPLedwLRLHTYLAGDAPTLADLaAVTALLLPF 172
Cdd:cd10289 2 AAQVDQWLDLAGS--------------LLKGKELEALL------KSLNSY---LASRTFLVGYSLTLADV-AVFSALYPS 57
|
90 100
....*....|....*....|..
gi 31565370 173 RYVLDPSARRIWGNVTRWFNTC 194
Cdd:cd10289 58 GQKLSDKEKKKFPHVTRWFNHI 79
|
|
| GST_C_AIMP3 |
cd10305 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ... |
95-201 |
5.96e-07 |
|
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: 48.83 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 95 LVQQWVSYADTELIPAACGATLPALglrgpgqdpqaalgalgkaLNPLEDWLRLHTYLAGDAPTLADlAAVTALLLPFRY 174
Cdd:cd10305 6 QVDQWLEYRVTQVAPASDKADAKSL-------------------LKELNSYLQDRTYLVGHKLTLAD-VVLYYGLHPIMK 65
|
90 100
....*....|....*....|....*..
gi 31565370 175 VLDPSARRIWGNVTRWFNTCVRQPEFR 201
Cdd:cd10305 66 DLSPQEKEQYLNVSRWFDHVQHLPGIR 92
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
777-1074 |
1.51e-06 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 52.19 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 777 ISLQQDED-VLDTWFSsGLFPF-SIFGWPNQSEDLSV----FYPGTLLETGHDILFF----WVARMVMLGLKLTGKlpfr 846
Cdd:PRK11893 212 IPVPGDPKhVIYVWFD-ALTNYlTALGYPDDEELLAElfnkYWPADVHLIGKDILRFhavyWPAFLMAAGLPLPKR---- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 847 eVYLHA-IVRDahGRKMSKSLGNVIDPLDVIHgvslqglydqllnsnldpsevekakegqkadfpagipECGTDALRFGL 925
Cdd:PRK11893 287 -VFAHGfLTLD--GEKMSKSLGNVIDPFDLVD-------------------------------------EYGVDAVRYFL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 926 CAYTSQGRDINLDVNRILGYR--HFCNKLWN---ATKFALRGLGKGFVPSATSKPEGHESLVDRWIRSRltEAVRlsneg 1000
Cdd:PRK11893 327 LREIPFGQDGDFSREAFINRInaDLANDLGNlaqRTLSMIAKNFDGKVPEPGALTEADEALLEAAAALL--ERVR----- 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 1001 fQAYDFPAITTAQYSFW-LYELCDVYLECLKP-VLNGVDQvaaECARQTLYTCLDvGLR----LLSPFMPFVTEELFQRL 1074
Cdd:PRK11893 400 -AAMDNLAFDKALEAILaLVRAANKYIDEQAPwSLAKTDP---ERLATVLYTLLE-VLRgiavLLQPVMPELAAKILDQL 474
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
801-876 |
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 31565370 801 GWPNQSEDLS-VFYPGTLLETGHDIL-F---FWVARMVMLGLKLtgklpFREVYLHA-IVRDahGRKMSKSLGNVIDPLD 874
Cdd:PRK12267 240 GYGSDDDELFkKFWPADVHLVGKDILrFhaiYWPIMLMALGLPL-----PKKVFAHGwWLMK--DGKMSKSKGNVVDPEE 312
|
..
gi 31565370 875 VI 876
Cdd:PRK12267 313 LV 314
|
|
| GST_C_Delta_Epsilon |
cd03177 |
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; ... |
121-198 |
3.35e-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: 47.14 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 121 LRGPGQDPQAALGALGKALNPLEDWLRLHTYLAGDAPTLADLAAVTAL----LLPFryvlDPSArriWGNVTRWFNTCVR 196
Cdd:cd03177 29 LFGGAEPPEEKLDKLEEALEFLETFLEGSDYVAGDQLTIADLSLVATVstleVVGF----DLSK---YPNVAAWYERLKA 101
|
..
gi 31565370 197 QP 198
Cdd:cd03177 102 LP 103
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
343-471 |
7.39e-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: 7.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 343 PNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKklwkeRGLNRHQLGreafleevwkwkAEK 422
Cdd:pfam09334 8 PYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEK-----EGITPEELV------------DRY 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 31565370 423 GDRIYHQLKKLGSSLD-WDRacfTMDPKLSATVTEAFVRLHEEGVIYRST 471
Cdd:pfam09334 71 HEIHREDFKKFNISFDdYGR---TTSERHHELVQEFFLKLYENGYIYEKE 117
|
|
| GST_C_7 |
cd03206 |
C-terminal, alpha helical domain of an unknown subfamily 7 of Glutathione S-transferases; ... |
96-192 |
1.70e-05 |
|
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: 44.91 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 96 VQQWVSYADTELIPAACGATLpaLGLRGPGQDPQAALGALGKALNPLEDWLRLHTYLAGDAPTLADLAAvtalllpFRYV 175
Cdd:cd03206 1 VQRWLSFAAGEIAHGPAAARL--IHLFGAPLDPERARAISHRLLRLLDQHLAGRDWLAGDRPTIADVAC-------YPYI 71
|
90 100
....*....|....*....|....*.
gi 31565370 176 ---------LDPsarriWGNVTRWFN 192
Cdd:cd03206 72 alapeggvsLEP-----YPAIRAWLA 92
|
|
| GST_C_5 |
cd03196 |
C-terminal, alpha helical domain of an unknown subfamily 5 of Glutathione S-transferases; ... |
139-203 |
2.24e-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: 44.84 E-value: 2.24e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31565370 139 LNPLEDWLRLHTYLAGDAPTLADLAavtalLLPF----------RYVLDPsarriWGNVTRWFNTCVRQPEFRAV 203
Cdd:cd03196 50 LAELEARLSQHAYLFGDRPSLADYA-----IFPFvrqfahvdrdWFDASP-----YPNLRRWLNRFLQSPLFSKI 114
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
340-468 |
2.42e-05 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 48.34 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 340 IPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGiatqvvvEKKLWK--ERGLNRHQLGReafleevwk 417
Cdd:PRK11893 7 TPIYYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFFLTGTDEHG-------QKIQRKaeEAGISPQELAD--------- 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 31565370 418 wkaEKGDRIYHQLKKLGSSLDwdraCF--TMDPKLSATVTEAFVRLHEEGVIY 468
Cdd:PRK11893 71 ---RNSAAFKRLWEALNISYD----DFirTTDPRHKEAVQEIFQRLLANGDIY 116
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
345-427 |
3.82e-05 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 47.87 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 345 VTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCD-H----------AGIATQVVVE------KKLWKERGL------ 401
Cdd:PRK12267 15 PNGKPHIGHAYTTIAADALARYKRLQGYDVFFLTGTDeHgqkiqqaaekAGKTPQEYVDeisagfKELWKKLDIsydkfi 94
|
90 100 110
....*....|....*....|....*....|
gi 31565370 402 ----NRHQLGREAFLEEVWkwkaEKGDrIY 427
Cdd:PRK12267 95 rttdERHKKVVQKIFEKLY----EQGD-IY 119
|
|
| Val_tRNA-synt_C |
pfam10458 |
Valyl tRNA synthetase tRNA binding arm; This domain is found at the C-terminus of Valyl tRNA ... |
1195-1257 |
3.95e-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: 42.64 E-value: 3.95e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31565370 1195 DPARELGKLQAKRSEAQRQAQRLQERRAASSYSAKVPLEVQEADEAKLQQTEAELRKVDEAIA 1257
Cdd:pfam10458 1 DVEKERARLEKELAKLQKEIERVQGKLANPGFVAKAPAEVVEEEKAKLAELEEQAEKLRERLS 63
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
343-468 |
3.99e-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: 47.14 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 343 PNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEkklwkERGLNRHQLGRE--AFLEEVWKWka 420
Cdd:cd00814 9 PYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAE-----EEGVTPQELCDKyhEIFKDLFKW-- 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 31565370 421 ekgdriyhqlkkLGssLDWDRACFTMDPKLSATVTEAFVRLHEEGVIY 468
Cdd:cd00814 82 ------------LN--ISFDYFIRTTSPRHKEIVQEFFKKLYENGYIY 115
|
|
| GST_C_GluRS_N |
cd10306 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Glutamyl-tRNA synthetase; ... |
130-193 |
9.06e-05 |
|
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: 42.34 E-value: 9.06e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31565370 130 AALGALGKALNPLEDWLRLHTYLAGDAPTLADLaAVTALLLPFRYVLDPSARRIWGNVTRWFNT 193
Cdd:cd10306 21 KDFKALSQALEELDSHLTLRTFIVGYSLSLADI-AVWGALRGNGVAGSLIKNKVYVNLSRWFSF 83
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
336-470 |
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 31565370 336 FMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAG--IATQVVVEkklwkerglnrhqlGREAfle 413
Cdd:PLN02224 71 FVLTTPLYYVNAPPHMGSAYTTIAADSIARFQRLLGKKVIFITGTDEHGekIATSAAAN--------------GRNP--- 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 31565370 414 evwkwkAEKGDRIYHQLKKLGSSLD--WDRACFTMDPKLSATVTEAFVRLHEEGVIYRS 470
Cdd:PLN02224 134 ------PEHCDIISQSYRTLWKDLDiaYDKFIRTTDPKHEAIVKEFYARVFANGDIYRA 186
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
673-876 |
9.55e-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: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 673 LRPQWYVRCGEMAQAASAAVTRGDLRILPEAHQRTWHSWMDnirdwcISRQLWWGHRIPayfitvhdpavppgedpdgry 752
Cdd:cd00812 128 LLDQWFLKYSETEWKEKLLKDLEKLDGWPEEVRAMQENWIG------CSRQRYWGTPIP--------------------- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 753 WvsgrteaearekaarefgvspdkislqqdEDVLDTWFSSGLFP--FSIFGWPNQ---------SEDLSVFYPGTLLETG 821
Cdd:cd00812 181 W-----------------------------TDTMESLSDSTWYYarYTDAHNLEQpyegdlefdREEFEYWYPVDIYIGG 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31565370 822 HD-----ILF--FWVArmVMLGLKLTGKLPFREVYLHAIVRdAHGRKMSKSLGNVIDPLDVI 876
Cdd:cd00812 232 KEhapnhLLYsrFNHK--ALFDEGLVTDEPPKGLIVQGMVL-LEGEKMSKSKGNVVTPDEAI 290
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
304-375 |
1.32e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 43.13 E-value: 1.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31565370 304 VEAAWYPWWERQGFFKPEygrPSVSAPNPRGVFMMCIPPPNVTGSLHLGHALtnaiqdSLTR------WHRMRGETTL 375
Cdd:PLN02959 18 IEVAVQKWWEEEKVFEAE---AGDEPPKPGEKFFGNFPYPYMNGLLHLGHAF------SLSKlefaaaYHRLRGANVL 86
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
753-877 |
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 31565370 753 WVSGRTEAEAREKAAREFGVS-PDkislqQDEDVLDTWFSSGLFPFSIFGWPNQSEDL----SVFYPGTLLETGHDILFF 827
Cdd:PLN02224 260 WIKSGLRDFSISRALVDWGIPvPD-----DDKQTIYVWFDALLGYISALTEDNKQQNLetavSFGWPASLHLIGKDILRF 334
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 31565370 828 ----WVARMVMLGLKLTgKLPFREVYLhaiVRDahGRKMSKSLGNVIDPLDVIH 877
Cdd:PLN02224 335 havyWPAMLMSAGLELP-KMVFGHGFL---TKD--GMKMGKSLGNTLEPFELVQ 382
|
|
| GST_C_GluProRS_N |
cd10309 |
Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional ... |
125-192 |
2.34e-03 |
|
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: 38.07 E-value: 2.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31565370 125 GQDPQAALGALGKALNPLEDWLRLHTYLAGDAPTLADLAAVTALllpFRYVLDPSARRIWGNVTRWFN 192
Cdd:cd10309 12 SAGRLSCDQDFSSALSYLDKALSLRTYLVGNSLTLADFAVWAAL---RGNGEWLASKEKYVNVTRWFK 76
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
133-214 |
4.98e-03 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 41.25 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 133 GALGKALNPLEDWLRLHTYLAGDAPTLADLAAVTALL--LPFRYVLDPSARriWGNVTRWFNTCVRQPEFRAVlGEVALY 210
Cdd:PLN02907 93 SEFENACEYVDGYLASRTFLVGYSLTIADIAIWSGLAgsGQRWESLRKSKK--YQNLVRWFNSISAEYSDILN-EVTAAY 169
|
....
gi 31565370 211 SGAR 214
Cdd:PLN02907 170 VGKR 173
|
|
| GST_C_MetRS_N |
cd10307 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Methionyl-tRNA synthetase ... |
95-193 |
8.00e-03 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of Methionyl-tRNA synthetase from higher eukaryotes; Glutathione S-transferase (GST) C-terminal domain family, Methionyl-tRNA synthetase (MetRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of MetRS 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. MetRS is a class I aaRS, containing a Rossman fold catalytic core. It recognizes the initiator tRNA as well as the Met-tRNA for protein chain elongation. The GST_C-like domain of MetRS 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. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.
Pssm-ID: 198340 [Multi-domain] Cd Length: 102 Bit Score: 37.09 E-value: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31565370 95 LVQQWVSYADTELIPAacgaTLPALGL-RGPGQDPQAALGALGKALNPL-EDWLRLHTYLAGDAPTLADLaAVTALLLPF 172
Cdd:cd10307 4 LSNQWLEWEAWLLQPA----LSLALALtHVQGKKSEADLNTVLNALVHLdQSLLKKSTPLLGDKLSSADV-VVWSALYPL 78
|
90 100
....*....|....*....|.
gi 31565370 173 rYVLDPSARRIWGNVTRWFNT 193
Cdd:cd10307 79 -GTDKSALPENLDNLRRWFQN 98
|
|
| |
