|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
283-1265 |
0e+00 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 1420.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 283 LPTPPGEKKDVSGPMPDSYSPRYVEAAWYPWWEQQGFFKPEYGRPNVSAANPrgvFMMCIPPPNVTGSLHLGHALTNAIQ 362
Cdd:PTZ00419 10 SKDEKKNKKRNISSMAASYDPKEVESGWYEWWEKSGFFKPAEDAKSLNSGKK---FVIVLPPPNVTGYLHIGHALTGAIQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 363 DSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKKLWREQGLSRHQLGREAFLQEVWKWKEEKGDRIYHQLKKLGSSLDWD 442
Cdd:PTZ00419 87 DSLIRYHRMKGDETLWVPGTDHAGIATQVVVEKKLMKEENKTRHDLGREEFLKKVWEWKDKHGNNICNQLRRLGSSLDWS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 443 RACFTMDPKLSAAVTEAFVRLHEEGIIYRSTRLVNWSCTLNSAISDIEVDKKELTGRTLLSVPGYKEKVEFGVLVSFAYK 522
Cdd:PTZ00419 167 REVFTMDEQRSKAVKEAFVRLYEDGLIYRDTRLVNWCCYLKTAISDIEVEFEEIEKPTKITIPGYDKKVEVGVLWHFAYP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 523 VQGSDsDEEVVVATTRIETMLGDVAVAVHPKDTRYQHLKGKNVIHPFLS-RSLPIVFDE-FVDMDFGTGAVKITPAHDQN 600
Cdd:PTZ00419 247 LEDSG-QEEIVVATTRIETMLGDVAVAVHPKDERYKKLHGKELIHPFIPdRKIPIIADDeLVDMEFGTGAVKITPAHDPN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 601 DYEVGQRHGLEAISIMDSRGALINVPPPFLGLPRFEARKAVLVALKERGLFRGIEDNPMVVPLCNRSKDVVEPLLRPQWY 680
Cdd:PTZ00419 326 DYEIAKRHNLPFINIFTLDGKINENGGEFAGMHRFDCRRKIEEELKEMGLLRDKVPNPMRLPRCSRSGDIVEPMLIPQWY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 681 VRCGEMAQAASAAVTRGDLRILPEAHQRTWHAWMDNIREWCISRQLWWGHRIPAYFVTVSD-PAVPPGEDPdgryWVSGR 759
Cdd:PTZ00419 406 VNCKDMAKRAVEAVRNGELKIIPSSHENVWYHWLENIQDWCISRQLWWGHRIPAYRVISKGpETDPSDEEP----WVVAR 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 760 NEAEAREKAAKEFGVSPDKISLQQDEDVLDTWFSSGLFPLSILGWPNQSEDLSVFYPGTLLETGHDILFFWVARMVMLGL 839
Cdd:PTZ00419 482 SEEEALEKAKKKFGLSEEDFELEQDEDVLDTWFSSGLFPFSTLGWPDQTDDLQRFFPTSLLETGSDILFFWVARMVMMSL 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 840 KLTGRLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVIYGISLQGLHNQLLNSNLDPSEVEKAKEGQKADFPAGIPECG 919
Cdd:PTZ00419 562 HLTDKLPFKTVFLHAMVRDSQGEKMSKSKGNVIDPLEVIEGISLQDLNQKLYEGNLPEKEIKRAIELQKKEFPNGIPECG 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 920 TDALRFGLCAYMSQGRDINLDVNRILGYRHFCNKLWNATKFALRGLGKGFVPSPT--SQPGGHESL--VDRWIRSRLTEA 995
Cdd:PTZ00419 642 TDALRFGLLAYTQQGRNINLDINRVVGYRHFCNKLWNAVKFALMKLLKDFNLPNStlFKPNNVESLpwEDKWILHRLNVA 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 996 VRLSNQGFQAYDFPAVTTAQYSFWLYELCDVYLECLKPVLN-GVDQVAAECARQTLYTCLDVGLRLLSPFMPFVTEELFQ 1074
Cdd:PTZ00419 722 IKEVTEGFKEYDFSEATQATYNFWLYELCDVYLELIKPRLSkQSDGERKQHAQDVLHTVLDIGLRLLHPMMPFITEELYQ 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 1075 RLPRRmPQAPPSLCVTPYPEPSeCSWKDPEAEAALELALSITRAVRSLRADYNLT-RIRPDCFLEVADEATGALASAVSG 1153
Cdd:PTZ00419 802 RLPNY-LRKSESISIAKYPQPN-PGWNNEALDEEMKIIMSIVKSIRSLIATLGIPnKTKPDCYVTAKDAELIELIESAEN 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 1154 YVQALASAG---VVAVLALGAPAPQGCAVALASDRCSIHLQLQGLVDPARELGKLQAKRVEAQRQAQRLRERRAASGYPV 1230
Cdd:PTZ00419 880 LISTLAKIGsvsVIPPIEEEAEVPKGCGFDVVDNKVIIYLNLDEFIDLKKELAKLEKKLAKLQKSLESYLKKISIPNYED 959
|
970 980 990
....*....|....*....|....*....|....*
gi 530382523 1231 KVPLEVQEADEAKLQQTEAELRKVDEAIALFQKML 1265
Cdd:PTZ00419 960 KVPEDVRKLNDEKIDELNEEIKQLEQAIEELKSLL 994
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
297-1259 |
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: 1179.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 297 MPDSYSPRYVEAAWYPWWEQQGFFKPEygrPNvSAANPrgvFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETT 376
Cdd:COG0525 3 LPKTYDPKEVEAKWYQYWEENGYFKAD---PD-SDKEP---FTIVIPPPNVTGSLHMGHALNNTLQDILIRYKRMQGYNT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 377 LWNPGCDHAGIATQVVVEKKLwREQGLSRHQLGREAFLQEVWKWKEEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSAAV 456
Cdd:COG0525 76 LWQPGTDHAGIATQAVVERQL-AEEGKSRHDLGREKFLERVWEWKEESGGTITNQLRRLGASCDWSRERFTMDEGLSKAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 457 TEAFVRLHEEGIIYRSTRLVNWSCTLNSAISDIEVDkkeltgrtllsvpgYKEKVefGVLVSFAYKVqgSDSDEEVVVAT 536
Cdd:COG0525 155 REVFVRLYEKGLIYRGKRLVNWDPKLKTALSDLEVE--------------HEEVK--GHLWHIRYPL--ADGSGYIVVAT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 537 TRIETMLGDVAVAVHPKDTRYQHLKGKNVIHPFLSRSLPIVFDEFVDMDFGTGAVKITPAHDQNDYEVGQRHGLEAISIM 616
Cdd:COG0525 217 TRPETMLGDTAVAVHPEDERYKHLIGKTVILPLVGREIPIIADEYVDPEFGTGAVKITPAHDPNDFEVGKRHNLPMINIL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 617 DSRGALINVPPPFLGLPRFEARKAVLVALKERGLFRGIEDNPMVVPLCNRSKDVVEPLLRPQWYVRCGEMAQAASAAVTR 696
Cdd:COG0525 297 DEDGTINENAGKYRGLDRFEARKAIVADLEELGLLVKVEPHKHSVGHSDRSGTVIEPYLSDQWFVKMKPLAKPAIEAVED 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 697 GDLRILPEAHQRTWHAWMDNIREWCISRQLWWGHRIPAYFvtvsdpavppgeDPDGRYWVSgRNEAEAREKAAKEfgvsp 776
Cdd:COG0525 377 GEIKFVPERWEKTYFHWMENIRDWCISRQLWWGHRIPAWY------------CPDGEVYVA-RTEPEACAKAGSV----- 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 777 dkiSLQQDEDVLDTWFSSGLFPLSILGWPNQSEDLSVFYPGTLLETGHDILFFWVARMVMLGLKLTGRLPFREVYLHAIV 856
Cdd:COG0525 439 ---NLTQDEDVLDTWFSSALWPFSTLGWPEKTEDLKYFYPTSVLVTGFDIIFFWVARMIMMGLHFTGEVPFKDVYIHGLV 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 857 RDAHGRKMSKSLGNVIDPLDVI--YgislqglhnqllnsnldpsevekakegqkadfpagipecGTDALRFGLCAYMSQG 934
Cdd:COG0525 516 RDEQGRKMSKSKGNVIDPLDLIdkY---------------------------------------GADALRFTLAALASPG 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 935 RDINLDVNRILGYRHFCNKLWNATKFALrGLGKGFVPSPTSQPgGHESLVDRWIRSRLTEAVRLSNQGFQAYDFPAVTTA 1014
Cdd:COG0525 557 RDIKFDEERVEGYRNFANKLWNASRFVL-MNLEGFDPGLDPDP-EELSLADRWILSRLNKTIAEVTEALEKYRFDEAAQA 634
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 1015 QYSF-WlYELCDVYLECLKPVLNGVDQVAAECARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRmpQAPPSLCVTPYP 1093
Cdd:COG0525 635 LYDFvW-NEFCDWYLELAKPRLYGGDEAAKRETRATLVYVLEQILRLLHPFMPFITEEIWQKLPPR--KEGESIMLAPWP 711
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 1094 EPSEcSWKDPEAEAALELALSITRAVRSLRADYNL---TRIrpDCFLEVADEATGALASAVSGYVQALASAGVVAVLAlg 1170
Cdd:COG0525 712 EADE-ELIDEEAEAEFEWLKEVISAIRNIRAEMNIppsKKL--PLLLKGADEADRARLEENAAYIKRLARLEEITILV-- 786
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 1171 APAPQGCAVALASDrCSIHLQLQGLVDPARELGKLQAKRVEAQRQAQRLRERRAASGYPVKVPLEVQEADEAKLQQTEAE 1250
Cdd:COG0525 787 DEKPEGAASAVVGG-AEVFLPLEGLIDVEAERARLEKELAKLEKEIARVEKKLSNEGFVAKAPAEVVEKEREKLAEAEAK 865
|
....*....
gi 530382523 1251 LRKVDEAIA 1259
Cdd:COG0525 866 LEKLEEQLA 874
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
297-1263 |
0e+00 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 1143.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 297 MPDSYSPRYVEAAWYPWWEQQGFFKPEygrpnvsaANPRGVFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETT 376
Cdd:PRK05729 5 LPKTYDPKEVEAKWYQKWEEKGYFKPD--------DNSKKPFSIVIPPPNVTGSLHMGHALNNTLQDILIRYKRMQGYNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 377 LWNPGCDHAGIATQVVVEKKLwREQGLSRHQLGREAFLQEVWKWKEEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSAAV 456
Cdd:PRK05729 77 LWLPGTDHAGIATQMVVERQL-AAEGKSRHDLGREKFLEKVWEWKEESGGTITNQLRRLGASCDWSRERFTMDEGLSKAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 457 TEAFVRLHEEGIIYRSTRLVNWSCTLNSAISDIEVDkkeltgrtllsvpgYKEkVEfGVLVSFAYKVqgSDSDEEVVVAT 536
Cdd:PRK05729 156 REVFVRLYEKGLIYRGKRLVNWDPKLQTALSDLEVE--------------YKE-VK-GKLWHIRYPL--ADGSDYLVVAT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 537 TRIETMLGDVAVAVHPKDTRYQHLKGKNVIHPFLSRSLPIVFDEFVDMDFGTGAVKITPAHDQNDYEVGQRHGLEAISIM 616
Cdd:PRK05729 218 TRPETMLGDTAVAVNPEDERYKHLIGKTVILPLVGREIPIIADEYVDPEFGTGAVKITPAHDPNDFEVGKRHNLPMINIM 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 617 DSRGALINVPPPFLGLPRFEARKAVLVALKERGLFRGIEDNPMVVPLCNRSKDVVEPLLRPQWYVRCGEMAQAASAAVTR 696
Cdd:PRK05729 298 DEDGTINENPGEYQGLDRFEARKAIVADLEELGLLVKIEPHTHSVGHSDRSGVVIEPYLSDQWFVKMKPLAKPALEAVEN 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 697 GDLRILPEAHQRTWHAWMDNIREWCISRQLWWGHRIPAYFvtvsdpavppgeDPDGRYWVsGRNEAEAREKAAkefgvsp 776
Cdd:PRK05729 378 GEIKFVPERWEKTYFHWMENIQDWCISRQLWWGHRIPAWY------------DEDGEVYV-GREEPEAREKAL------- 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 777 dkisLQQDEDVLDTWFSSGLFPLSILGWPNQSEDLSVFYPGTLLETGHDILFFWVARMVMLGLKLTGRLPFREVYLHAIV 856
Cdd:PRK05729 438 ----LTQDEDVLDTWFSSALWPFSTLGWPEKTEDLKRFYPTSVLVTGFDIIFFWVARMIMMGLHFTGQVPFKDVYIHGLV 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 857 RDAHGRKMSKSLGNVIDPLDVI--YgislqglhnqllnsnldpsevekakegqkadfpagipecGTDALRFGLCAYMSQG 934
Cdd:PRK05729 514 RDEQGRKMSKSKGNVIDPLDLIdkY---------------------------------------GADALRFTLAALASPG 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 935 RDINLDVNRILGYRHFCNKLWNATKFALrgLGKGFVPSPTSQPGGHESLVDRWIRSRLTEAVRLSNQGFQAYDFPAVTTA 1014
Cdd:PRK05729 555 RDIRFDEERVEGYRNFANKLWNASRFVL--MNLEGADVGELPDPEELSLADRWILSRLNRTVAEVTEALDKYRFDEAARA 632
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 1015 QYSFWLYELCDVYLECLKPVLNGVDQVAaecARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRmpQAPPSLCVTPYPE 1094
Cdd:PRK05729 633 LYEFIWNEFCDWYLELAKPVLQEAAKRA---TRATLAYVLEQILRLLHPFMPFITEELWQKLAPL--GIEESIMLAPWPE 707
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 1095 PSECswKDPEAEAALELALSITRAVRSLRADYNLT-RIRPDCFLEVADEATGALASAVSGYVQALASAGVVAVLALGAPA 1173
Cdd:PRK05729 708 ADEA--IDEAAEAEFEWLKELITAIRNIRAEMNIPpSKKLPLLLKGADAEDRARLEANEAYIKRLARLESLEILADDEEA 785
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 1174 PQGCAVALASDrCSIHLQLQGLVDPARELGKLQAKRVEAQRQAQRLRERRAASGYPVKVPLEVQEADEAKLQQTEAELRK 1253
Cdd:PRK05729 786 PEGAASAVVGG-AELFLPLEGLIDVEAELARLEKELAKLEKEIERVEKKLSNEGFVAKAPEEVVEKEREKLAEYEEKLAK 864
|
970
....*....|
gi 530382523 1254 VDEAIALFQK 1263
Cdd:PRK05729 865 LKERLARLKA 874
|
|
| PLN02381 |
PLN02381 |
valyl-tRNA synthetase |
282-1257 |
0e+00 |
|
valyl-tRNA synthetase
Pssm-ID: 215214 [Multi-domain] Cd Length: 1066 Bit Score: 1138.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 282 DLPTPPGEKKDVSGPMPDSYSPRYVEAAWYPWWEQQGFFKPEygrpnvsAANPRGVFMMCIPPPNVTGSLHLGHALTNAI 361
Cdd:PLN02381 81 DPDTPFGQKKRLSSQMAKQYSPSAVEKSWYAWWEKSGYFGAD-------AKSSKPPFVIVLPPPNVTGALHIGHALTAAI 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 362 QDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKKLWREQGLSRHQLGREAFLQEVWKWKEEKGDRIYHQLKKLGSSLDW 441
Cdd:PLN02381 154 EDTIIRWKRMSGYNALWVPGVDHAGIATQVVVEKKLMRERHLTRHDIGREEFVSEVWKWKDEYGGTILNQLRRLGASLDW 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 442 DRACFTMDPKLSAAVTEAFVRLHEEGIIYRSTRLVNWSCTLNSAISDIEVDKKELTGRTLLSVPGYKEKVEFGVLVSFAY 521
Cdd:PLN02381 234 SRECFTMDEQRSKAVTEAFVRLYKEGLIYRDIRLVNWDCTLRTAISDVEVDYIDIKERTLLKVPGYDKPVEFGVLTSFAY 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 522 KVQGSDSdeEVVVATTRIETMLGDVAVAVHPKDTRYQHLKGKNVIHPFLSRSLPIVFD-EFVDMDFGTGAVKITPAHDQN 600
Cdd:PLN02381 314 PLEGGLG--EIVVATTRIETMLGDTAIAIHPDDERYKHLHGKFAVHPFNGRKLPIICDaILVDPNFGTGAVKITPAHDPN 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 601 DYEVGQRHGLEAISIMDSRGAL-INVPPPFLGLPRFEARKAVLVALKERGLFRGIEDNPMVVPLCNRSKDVVEPLLRPQW 679
Cdd:PLN02381 392 DFEVGKRHNLEFINIFTDDGKInSNGGSEFAGMPRFAAREAVIEALQKKGLYRGAKNNEMRLGLCSRTNDVVEPMIKPQW 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 680 YVRCGEMAQAASAAVTRGD---LRILPEAHQRTWHAWMDNIREWCISRQLWWGHRIPAYFVTVSDPAvppgEDPDGRY-- 754
Cdd:PLN02381 472 FVNCSSMAKQALDAAIDGEnkkLEFIPKQYLAEWKRWLENIRDWCISRQLWWGHRIPAWYVTLEDDQ----LKELGSYnd 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 755 -WVSGRNEAEAREKAAKEFgvSPDKISLQQDEDVLDTWFSSGLFPLSILGWPNQSEDLSVFYPGTLLETGHDILFFWVAR 833
Cdd:PLN02381 548 hWVVARNESDALLEASQKF--PGKKFELSQDPDVLDTWFSSGLFPLSVLGWPDDTDDLKAFYPTSVLETGHDILFFWVAR 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 834 MVMLGLKLTGRLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVIYGISLQGLHNQLLNSNLDPSEVEKAKEGQKADFPA 913
Cdd:PLN02381 626 MVMMGMQLGGDVPFRKVYLHPMIRDAHGRKMSKSLGNVIDPLEVINGISLEGLHKRLEEGNLDPKELVVAKEGQKKDFPN 705
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 914 GIPECGTDALRFGLCAYMSQGRDINLDVNRILGYRHFCNKLWNATKFALRGLGKGFVPSPTSQPGGHESLVdRWIRSRLT 993
Cdd:PLN02381 706 GIAECGTDALRFALVSYTAQSDKINLDILRVVGYRQWCNKLWNAVRFAMSKLGDDYTPPATLSVETMPFSC-KWILSVLN 784
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 994 EAVRLSNQGFQAYDFPAVTTAQYSFWLYELCDVYLECLKPVLNGVDQ---VAAECARQTLYTCLDVGLRLLSPFMPFVTE 1070
Cdd:PLN02381 785 KAISKTVSSLDAYEFSDAASTVYSWWQYQFCDVFIEAIKPYFAGDNPefaSERAAAQDTLWICLDTGLRLLHPFMPFVTE 864
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 1071 ELFQRLPR-RMPQAPPSLCVTPYPEPSEcSWKDPEAEAALELALSITRAVRSLRADYNLTRI--RPDCFLEVADEATGAL 1147
Cdd:PLN02381 865 ELWQRLPQpKDHTRKDSIMISEYPSAVE-AWTNEKVEYEMDLVLSTVKCLRSLRAEVLEKQKneRLPAFALCRNQEIAAI 943
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 1148 ASAVSGYVQALASAGVVAVLALGAPA-PQGCAVALASDRCSIHLQLQGLVDPARELGKLQAKRVEAQRQAQRLRERRAAS 1226
Cdd:PLN02381 944 IKSHQLEILTLANLSSLKVLLSENDApPAGCAFENVNENLKVYLQAQGAVNAEAELEKLRNKMDEIQKQQEKLEKKMNAS 1023
|
970 980 990
....*....|....*....|....*....|.
gi 530382523 1227 GYPVKVPLEVQEADEAKLQQTEAELRKVDEA 1257
Cdd:PLN02381 1024 GYKEKVPANIQEEDARKLTKLLQELEFFEKE 1054
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
297-1244 |
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: 958.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 297 MPDSYSPRYVEAAWYPWWEQQGFFKPEYGRPNVSaanprgvFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETT 376
Cdd:TIGR00422 1 MPKDYDPHEVEKKWYKKWEKSGFFKPDGNSNKPP-------FCIDIPPPNVTGSLHIGHALNWSIQDIIARYKRMKGYNV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 377 LWNPGCDHAGIATQVVVEKKLWrEQGLSRHQLGREAFLQEVWKWKEEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSAAV 456
Cdd:TIGR00422 74 LWLPGTDHAGIATQVKVEKKLG-AEGKTKHDLGREEFREKIWEWKEESGGTIKNQIKRLGASLDWSRERFTMDEGLSKAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 457 TEAFVRLHEEGIIYRSTRLVNWSCTLNSAISDIEVDKKELTGrtllSVPGYKEKVEFGvlvsfaykvqgsdSDEEVVVAT 536
Cdd:TIGR00422 153 KEAFVRLYEKGLIYRGEYLVNWDPKLNTAISDIEVEYKEVKG----KLYYIRYPLANG-------------SKDYLVVAT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 537 TRIETMLGDVAVAVHPKDTRYQHLKGKNVIHPFLSRSLPIVFDEFVDMDFGTGAVKITPAHDQNDYEVGQRHGLEAISIM 616
Cdd:TIGR00422 216 TRPETMFGDTAVAVHPEDERYKHLIGKKVILPLTGRKIPIIADEYVDMEFGTGAVKVTPAHDFNDYEWGKRHNLEFINIL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 617 DSRGALINVPPPFLGLPRFEARKAVLVALKERGLFRGIEDNPMVVPLCNRSKDVVEPLLRPQWYVRCGEMAQAASAAVTR 696
Cdd:TIGR00422 296 DEDGLLNENAGKYQGLTRFEARKKIVEDLKEEGLLVKIEPHTHNVGTCWRSGTVVEPLLSKQWFVKVEKLADKALEAAEE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 697 GDLRILPEAHQRTWHAWMDNIREWCISRQLWWGHRIPAYFvtvsdpavppgEDPDGRYWVsGRNEAEAREKAAKEFGVSp 776
Cdd:TIGR00422 376 GEIKFVPKRMEKRYLNWLRNIKDWCISRQLIWGHRIPVWY-----------CKECGEVYV-AKEEPLPDDKTNTGPSVE- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 777 dkisLQQDEDVLDTWFSSGLFPLSILGWPNQSEDLSVFYPGTLLETGHDILFFWVARMVMLGLKLTGRLPFREVYLHAIV 856
Cdd:TIGR00422 443 ----LEQDTDVLDTWFSSSLWPFSTLGWPDETKDLKKFYPTDLLVTGYDIIFFWVARMIFRSLALTGQVPFKEVYIHGLV 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 857 RDAHGRKMSKSLGNVIDPLDVIygislqglhnqllnsnldpsevekakegqkadfpagiPECGTDALRFGLCAYMSQGRD 936
Cdd:TIGR00422 519 RDEQGRKMSKSLGNVIDPLDVI-------------------------------------EKYGADALRFTLASLVTPGDD 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 937 INLDVNRILGYRHFCNKLWNATKFALRGLGKgfvPSPTSQPGGHESLVDRWIRSRLTEAVRLSNQGFQAYDFPAVTTAQY 1016
Cdd:TIGR00422 562 INFDWKRVESARNFLNKLWNASRFVLMNLSD---DLELSGGEEKLSLADRWILSKLNRTIKEVRKALDKYRFAEAAKALY 638
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 1017 SFWLYELCDVYLECLKPVLNGVDQVAAECARQTLYTCLDVGLRLLSPFMPFVTEELFQRLprrmPQAPPSLCVTPYPEPS 1096
Cdd:TIGR00422 639 EFIWNDFCDWYIELVKYRLYNGNEAEKKAARDTLYYVLDKALRLLHPFMPFITEEIWQHF----KEGADSIMLQSYPVVD 714
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 1097 EcSWKDPEAEAALELALSITRAVRSLRADYNLTRIRPDCFLEVADEATGALA-SAVSGYVQALASAGVVAVLAlGAPaPQ 1175
Cdd:TIGR00422 715 A-EFVDEEAEKAFELLKEIIVSIRNLKAESNIPPNAPLKVLLIYTEAETAERlKLNAVDIKGAINFSEVEVVI-EKP-EV 791
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530382523 1176 GCAVALASDRCSIHLQLQGLVDPARELGKLQAKRVEAQRQAQRLRERRAASGYPVKVPLEVQEADEAKL 1244
Cdd:TIGR00422 792 TEAVVELVPGFEIIIPVKGLINKAKELARLQKQLDKEKKEVIRIEGKLENEGFVKKAPKEVIEKEKEKL 860
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
301-1260 |
0e+00 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 848.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 301 YSPRYVEAAWYPWWEQQGFFKPEygrpnvSAANPRGVFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNP 380
Cdd:PRK14900 19 YEHREVEARWYPFWQERGYFHGD------EHDRTRPPFSIVLPPPNVTGSLHLGHALTATLQDVLIRWKRMSGFNTLWLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 381 GCDHAGIATQVVVEKKLWREQGLSRHQLGREAFLQEVWKWKEEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSAAVTEAF 460
Cdd:PRK14900 93 GTDHAGIATQMIVEKELKKTEKKSRHDLGREAFLERVWAWKEQYGSRIGEQHKALGASLDWQRERFTMDEGLSRAVREVF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 461 VRLHEEGIIYRSTRLVNWSCTLNSAISDIEVDKKEltgrtllsvpgykekVEFGVLVSFAYKVqgSDSDEEVVVATTRIE 540
Cdd:PRK14900 173 VRLHEEGLIYREKKLINWCPDCRTALSDLEVEHEE---------------AHQGELWSFAYPL--ADGSGEIVVATTRPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 541 TMLGDVAVAVHPKDTRYQHLKGKNVIHPFLSRSLPIVFD-EFVDMDFGTGAVKITPAHDQNDYEVGQRHGLEAISIMDSR 619
Cdd:PRK14900 236 TMLGDTAVAVHPLDPRYMALHGKKVRHPITGRTFPIVADaILVDPKFGTGAVKVTPAHDFNDFEVGKRHGLEMITVIGPD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 620 GALINVPPPFLGLPRFEARKAVLVALKERGLFRGIEDNPMVVPLCNRSKDVVEPLLRPQWYVRCGEMAQAASAAVTRGDL 699
Cdd:PRK14900 316 GRMTAEAGPLAGLDRFEARKEVKRLLAEQGLDRGAKPHVLPLGRCQRSATILEPLLSDQWYVRIEPLARPAIEAVEQGRT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 700 RILPEAHQRTWHAWMDNIREWCISRQLWWGHRIPAYFVTVSDPAVppgedpdgrywvsGRNEAEAREKAAKEfgvspdki 779
Cdd:PRK14900 396 RFIPEQWTNTYMAWMRNIHDWCISRQLWWGHQIPAWYCPDGHVTV-------------ARETPEACSTCGKA-------- 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 780 SLQQDEDVLDTWFSSGLFPLSILGWPNQSEDLSVFYPGTLLETGHDILFFWVARMVMLGLKLTGRLPFREVYLHAIVRDA 859
Cdd:PRK14900 455 ELRQDEDVLDTWFSSGLWPFSTMGWPEQTDTLRTFYPTSVMETGHDIIFFWVARMMMMGLHFMGEVPFRTVYLHPMVRDE 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 860 HGRKMSKSLGNVIDPLDViygislqglhnqllnsnldpsevekakegqkadfpagIPECGTDALRFGLCAYMSQGRDINL 939
Cdd:PRK14900 535 KGQKMSKTKGNVIDPLVI-------------------------------------TEQYGADALRFTLAALTAQGRDIKL 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 940 DVNRILGYRHFCNKLWNATKFALRGLGkGFVPSPTSQPGGHESLVDRWIRSRLTEAVRLSNQGFQAYDFPAVTTAQYSFW 1019
Cdd:PRK14900 578 AKERIEGYRAFANKLWNASRFALMNLS-GYQERGEDPARLARTPADRWILARLQRAVNETVEALEAFRFNDAANAVYAFV 656
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 1020 LYELCDVYLECLKPVLNGVDQVAAECARQTLYTCLDVGLRLLSPFMPFVTEELFQRLP--RRMPQAPPSLCVTPYPEPSE 1097
Cdd:PRK14900 657 WHELCDWYIELAKEALASEDPEARRSVQAVLVHCLQTSYRLLHPFMPFITEELWHVLRaqVGASAWADSVLAAEYPRKGE 736
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 1098 CswkDPEAEAALELALSITRAVRSLRADYNLT-----RIRPDCFLEVADEATGALASAVS-GYVQALASAGVVAVLALGA 1171
Cdd:PRK14900 737 A---DEAAEAAFRPVLGIIDAVRNIRGEMGIPwkvklGAQAPVEIAVADPALRDLLQAGElARVHRVAGVEGSRLVVAAA 813
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 1172 PAPQGCAVALASDRCSIHLQLQGLVDPARELGKLQAKRVEAQRQAQRLRERRAASGYPVKVPLEVQEADEAKLQQTEAEL 1251
Cdd:PRK14900 814 TAPAPQSAVGVGPGFEVRVPLAGVIDLAAETARVDKEIGKVDQDLAVLERKLQNPSFVQNAPPAVVEKDRARAEELREKR 893
|
....*....
gi 530382523 1252 RKVDEAIAL 1260
Cdd:PRK14900 894 GKLEAHRAM 902
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
311-1264 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 720.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 311 YPWWEQQGFFKPEYGRpnvsAANPrgvFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQ 390
Cdd:PLN02943 70 YNWWESQGYFKPNFDR----GGDP---FVIPMPPPNVTGSLHMGHAMFVTLEDIMVRYNRMKGRPTLWIPGTDHAGIATQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 391 VVVEKKLwREQGLSRHQLGREAFLQEVWKWKEEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSAAVTEAFVRLHEEGIIY 470
Cdd:PLN02943 143 LVVEKML-ASEGIKRTDLGRDEFTKRVWEWKEKYGGTITNQIKRLGASCDWSRERFTLDEQLSRAVVEAFVRLHEKGLIY 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 471 RSTRLVNWSCTLNSAISDIEVDKKEltgrtllsvpgykekvEFGVLVSFAYKVQGSdSDEEVVVATTRIETMLGDVAVAV 550
Cdd:PLN02943 222 QGSYMVNWSPNLQTAVSDLEVEYSE----------------EPGTLYYIKYRVAGG-SEDFLTIATTRPETLFGDVAIAV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 551 HPKDTRYQHLKGKNVIHPF-LSRSLPIVFDEFVDMDFGTGAVKITPAHDQNDYEVGQRHGLEAISIMDSRGALINVPppf 629
Cdd:PLN02943 285 NPEDDRYSKYIGKMAIVPMtYGRHVPIIADRYVDKDFGTGVLKISPGHDHNDYLLARKLGLPILNVMNKDGTLNEVA--- 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 630 lGLPRFEARKAVLVALKERGLFRGIEDNPMVVPLCNRSKDVVEPLLRPQWYVRCGEMAQAASAAVTRGDLRILPEAHQRT 709
Cdd:PLN02943 362 -GLYWFEAREKLWSDLEETGLAVKKEPHTLRVPRSQRGGEVIEPLVSKQWFVTMEPLAEKALKAVENGELTIIPERFEKI 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 710 WHAWMDNIREWCISRQLWWGHRIPAYFVTvsdpavppGEDPDGRYWVSgRNEAEAREKAAKEFGVSpdkISLQQDEDVLD 789
Cdd:PLN02943 441 YNHWLSNIKDWCISRQLWWGHRIPVWYIV--------GKDCEEDYIVA-RSAEEALEKAREKYGKD---VEIYQDPDVLD 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 790 TWFSSGLFPLSILGWPNQS-EDLSVFYPGTLLETGHDILFFWVARMVMLGLKLTGRLPFREVYLHAIVRDAHGRKMSKSL 868
Cdd:PLN02943 509 TWFSSALWPFSTLGWPDVSaEDFKKFYPTTVLETGHDILFFWVARMVMMGIEFTGTVPFSYVYLHGLIRDSQGRKMSKTL 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 869 GNVIDPLDViygislqglhnqllnsnldpsevekakegqkadfpagIPECGTDALRFGLcAYMSQGRDINLDVNRILGYR 948
Cdd:PLN02943 589 GNVIDPLDT-------------------------------------IKEFGTDALRFTL-ALGTAGQDLNLSTERLTSNK 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 949 HFCNKLWNATKFALRGLgkgfvpSPTSQPGGHESLVD----------------RWIRSRLTEAVRLSNQGFQAYDFPAVT 1012
Cdd:PLN02943 631 AFTNKLWNAGKFVLQNL------PSQSDTSAWEHILAckfdkeesllslplpeCWVVSKLHELIDSVTTSYDKYFFGDVG 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 1013 TAQYSFWLYELCDVYLECLKPVLNGV-DQVAAECARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRmpqaPPSLCVTP 1091
Cdd:PLN02943 705 REIYDFFWSDFADWYIEASKTRLYHSgDNSALSRAQAVLLYVFENILKLLHPFMPFVTEELWQALPYR----KEALIVSP 780
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 1092 YPEPSECswKDPEAEAALELALSITRAVRSLRADYNltrIRPDCFLEVADEATGALASAVSGYVQALASAGVVAVLAL-- 1169
Cdd:PLN02943 781 WPQTSLP--KDLKSIKRFENLQSLTRAIRNARAEYS---VEPAKRISASIVASAEVIEYISKEKEVLALLSRLDLQNVhf 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 1170 --GAPAPQGCAVAL-ASDRCSIHLQLQGLVDPARELGKLQAKRVEAQRQAQRLRERRAASGYPVKVPLEVQEADEAKLQQ 1246
Cdd:PLN02943 856 tdSPPGDANQSVHLvASEGLEAYLPLADMVDISAEVERLSKRLSKMQTEYDALAARLSSPKFVEKAPEDVVRGVREKAAE 935
|
970
....*....|....*...
gi 530382523 1247 TEAELRKVDEAIALFQKM 1264
Cdd:PLN02943 936 AEEKIKLTKNRLAFLKST 953
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
309-940 |
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: 679.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 309 AWYPWWEQQGFFKPEygrpnVSAANPRGVFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIA 388
Cdd:pfam00133 1 QIYEFWDEQGYFKPE-----LEKRKGKPSFTIHDGPPNATGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 389 TQVVVEKKLWREQGLSRHQLGREAFLQEVWKWKEEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSAAVTEAFVRLHEEGI 468
Cdd:pfam00133 76 TEQVVEKKLGIKEKKTRHKYGREEFREKCREWKMEYADEIRKQFRRLGRSIDWDREYFTMDPELEAAVWEVFVRLHDKGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 469 IYRSTRLVNWSCTLNSAISDIEVDKKELTgrtllsvpgykekvefGVLVSFAYKVQGsDSDEEVVVATTRIETMLGDVAV 548
Cdd:pfam00133 156 IYRGKKLVNWSPALNTALSNLEVEYKDVK----------------GPSIHVAFPLAD-DEGASLVIWTTTPWTLPGNTAV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 549 AVHP-------------------------------KDTRYQHLKGKNVIHPFLSRSLPIVFDEFVDMDFGTGAVKITPAH 597
Cdd:pfam00133 219 AVNPefdyvitgegyilaeallkslykkgtdkkilEDFRGKELEGKEAIHPFVNREIPIITDDYVDMEFGTGAVHIAPAH 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 598 DQNDYEVGQRHGLEAISIMDSRGALINVPPPFLGLPRFEARKAVLVALKERGLFRGIEDNPMVVPLCNRSKDVVEPLLRP 677
Cdd:pfam00133 299 GENDYEVGQRHNLEVINPVDDDGTFTEEAPDFQGVYRFDARKKIVELLTEKGLLLKIEPFTHSYPFCWRSGTPIIPRATP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 678 QWYVRCGEMAQAASAAVTrgDLRILPEAHQRTWHAWMDNIREWCISRQLWWGHRIPAYFVTVSDPAVPPGEdpdGRYWVS 757
Cdd:pfam00133 379 QWFVRMDELADQALEAVE--KVQFVPKSGEKRYFNWLANIQDWCISRQRWWGHPIPAWVSKDTEEVVCRGE---LFELVA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 758 GRNEAEAREKA-AKEFG--VSPDKISLQQDEDVLDTWFSSGLFPLSILGWPNQS-EDLSVFYPGTLLETGHDILFFWVAR 833
Cdd:pfam00133 454 GRFEEEGSIKWlHREAKdkLGYGKGTLEQDEDVLDTWFSSGSWPFSTLGWPFVNtEEFKKFFPADMLLEGSDQTRGWFYR 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 834 MVMLGLKLTGRLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDViygislqglhnqllnsnldpsevekakegqkadfpa 913
Cdd:pfam00133 534 MIMLSTALTGSVPFKNVLVHGLVRDEQGRKMSKSLGNVIDPLDV------------------------------------ 577
|
650 660
....*....|....*....|....*..
gi 530382523 914 gIPECGTDALRFGLCaYMSQGRDINLD 940
Cdd:pfam00133 578 -IDKYGADALRLWLA-NSDYGRDINLS 602
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
336-939 |
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: 616.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 336 GVFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKKLWREQGlSRHQLGREAFLQ 415
Cdd:cd00817 1 PVFVIDTPPPNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGIATQVVVEKKLGIEGK-TRHDLGREEFLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 416 EVWKWKEEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSAAVTEAFVRLHEEGIIYRSTRLVNWSCTLNSAISDIEVdkke 495
Cdd:cd00817 80 KCWEWKEESGGKIREQLKRLGASVDWSREYFTMDPGLSRAVQEAFVRLYEKGLIYRDNRLVNWCPKLRTAISDIEV---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 496 ltgrtllsvpgykekvefgvlvsfaykvqgsdsdeevvvattrietmlgdvavavhpkdtryqhlkgknvihpflsrslp 575
Cdd:cd00817 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 576 ivfdefvdmdfgtgavkitpahdqndyevgqrhgleaisimdsrgalinvpppflglprfearkavlvalkerglfrgie 655
Cdd:cd00817 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 656 dnpmvvplCNRSKDVVEPLLRPQWYVRCGEMAQAASAAVTRGDLRILPEAHQRTWHAWMDNIREWCISRQLWWGHRIPAY 735
Cdd:cd00817 156 --------CSRSGDVIEPLLKPQWFVKVKDLAKKALEAVKEGDIKFVPERMEKRYENWLENIRDWCISRQLWWGHRIPAW 227
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 736 FVtvsdpavppgedPDGRYWVSGRNEAEAREKAAKEFGVSPDKISLQQDEDVLDTWFSSGLFPLSILGWPNQSEDLSVFY 815
Cdd:cd00817 228 YC------------KDGGHWVVAREEDEAIDKAAPEACVPCGGEELKQDEDVLDTWFSSSLWPFSTLGWPEETKDLKKFY 295
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 816 PGTLLETGHDILFFWVARMVMLGLKLTGRLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVIYGIslqglhnqllnsnl 895
Cdd:cd00817 296 PTSLLVTGHDIIFFWVARMIMRGLKLTGKLPFKEVYLHGLVRDEDGRKMSKSLGNVIDPLDVIDGY-------------- 361
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 530382523 896 dpsevekakegqkadfpagipecGTDALRFGLCAYMSQGRDINL 939
Cdd:cd00817 362 -----------------------GADALRFTLASAATQGRDINL 382
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
297-1150 |
1.72e-134 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 430.77 E-value: 1.72e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 297 MPDSYSPRYVEAAWYPWWEQQG--FFKPEYGRPnvsaanprgVFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGE 374
Cdd:PRK13208 6 LPKKYDPEELEEKWQKIWEEEGtyKFDPDERKP---------VYSIDTPPPTVSGSLHIGHVFSYTHTDFIARYQRMRGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 375 TTLWNPGCDHAGIATQVVVEKKLwreqGLSRHQLGREAFLQEVWKWKEEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSA 454
Cdd:PRK13208 77 NVFFPQGWDDNGLPTERKVEKYY----GIRKDDISREEFIELCRELTDEDEKKFRELWRRLGLSVDWSLEYQTISPEYRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 455 AVTEAFVRLHEEGIIYRSTRLVNWSCTLNSAISDIEVDKKELTGRtllsvpgykekvefgvLVSFAYKVQGsdsDEEVVV 534
Cdd:PRK13208 153 ISQKSFLDLYKKGLIYRAEAPVLWCPRCETAIAQAEVEYREREGK----------------LNYIKFPVED---GEEIEI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 535 ATTRIETMLGDVAVAVHPKDTRYQHLKGKNVIHPFLSRSLPIVFDEFVDMDFGTGAVKITPAHDQNDYEVGQRHGLEAIS 614
Cdd:PRK13208 214 ATTRPELLPACVAVVVHPDDERYKHLVGKTAIVPLFGVEVPILADPLVDPDFGTGAVMICTFGDKTDVTWWRELNLPTRI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 615 IMDSRGALINVPPPFLGLPRFEARKAVLVALKERGLFRGIEDNPMVVPLCNRSKDVVEPLLRPQWYVRCGEMAQAAsaaV 694
Cdd:PRK13208 294 IIDEDGRMTEAAGKLAGLTIEEARKKIVEDLKSGGLLGKQEPIKHNVKFCERCDTPLEILVTRQWFIKVLDLKEEL---L 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 695 TRGD-LRILPEAHQRTWHAWMDNIR-EWCISRQ--------LWW----GHRIPA----YFVtvsDPA--VPPGEDPDGRy 754
Cdd:PRK13208 371 ERGKeINWYPEHMRVRLENWIEGLNwDWCISRQryfgtpipVWYckdcGHPILPdeedLPV---DPTkdEPPGYKCPQC- 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 755 wvsGRNEAEArekaakefgvspdkislqqDEDVLDTWFSSGLFPLSILGWPNQSEDLSVFYPGTLLETGHDILFFW---- 830
Cdd:PRK13208 447 ---GSPGFEG-------------------ETDVMDTWATSSITPLIVTGWERDEDLFEKVFPMDLRPQGHDIIRTWlfyt 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 831 VARMVMLglklTGRLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVIygislqglhnqllnsnldpsevekakegqkad 910
Cdd:PRK13208 505 ILRAYLL----TGKLPWKNIMISGMVLDPDGKKMSKSKGNVVTPEELL-------------------------------- 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 911 fpagiPECGTDALRFGLcAYMSQGRDINLDVNRI-LGYRhFCNKLWNATKFALrglgkGFVPSPTSQPGGHESLVDRWIR 989
Cdd:PRK13208 549 -----EKYGADAVRYWA-ASARLGSDTPFDEKQVkIGRR-LLTKLWNASRFVL-----HFSADPEPDKAEVLEPLDRWIL 616
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 990 SRLTEAVRLSNQGFQAYDFPAVTTAQYSFWLYELCDVYLECLKPVL-NGVDQVAAECARQTLYTCLDVGLRLLSPFMPFV 1068
Cdd:PRK13208 617 AKLAKVVEKATEALENYDFAKALEEIESFFWHVFCDDYLELVKSRAyGEDEEEEQKSARYTLYTVLDTLLRLLAPFLPFI 696
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 1069 TEELFQRLPRRmpqappSLCVTPYPEPSEcSWKDPEAEAALELALSITRAVR--------SLRADYNLTRIRPDCFLEVA 1140
Cdd:PRK13208 697 TEEVWSWLYGG------SVHRASWPEPDE-ELIDEEDEELGELAKEILSAVRkykseaglSLNAPLKKVEVYGPADLELL 769
|
890
....*....|
gi 530382523 1141 DEATGALASA 1150
Cdd:PRK13208 770 EAAEEDLKAA 779
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
344-1150 |
9.75e-83 |
|
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: 291.60 E-value: 9.75e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 344 PPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCD-HaGIATQVVVEKKLwreqGLSR---HQLGREAFLQE--- 416
Cdd:COG0060 54 PPYANGDIHIGHALNKILKDIIVRYKTMRGFDVPYVPGWDcH-GLPIELKVEKEL----GIKKkdiEKVGIAEFREKcre 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 417 -VWKWKEEKGDriyhQLKKLGSSLDWDRACFTMDPKLSAAVTEAFVRLHEEGIIYRSTRLVNWSCTLNSAISDIEVdkke 495
Cdd:COG0060 129 yALKYVDEQRE----DFKRLGVWGDWDNPYLTMDPEYEESIWWALKKLYEKGLLYKGLKPVPWCPRCGTALAEAEV---- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 496 ltgrtllsvpGYKEKVEFGVLVSFayKVQGS-----DSDEEVVVATTRIETMLGDVAVAVHP------------------ 552
Cdd:COG0060 201 ----------EYKDVTSPSIYVKF--PVKDEkalllLEDAYLVIWTTTPWTLPANLAVAVHPdidyvlvevtggerlila 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 553 --------KDTRYQH-----------LKGKNVIHPFL-----SRSLPIVFDEFVDMDFGTGAVKITPAHDQNDYEVGQRH 608
Cdd:COG0060 269 ealveavlKELGIEDyevlatfkgaeLEGLRYEHPFYyvvgyDRAHPVILGDYVTTEDGTGIVHTAPGHGEDDFEVGKKY 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 609 GLEAISIMDSRGALINVPPPFLGLPRFEARKAVLVALKERG-LFRgIEDnpmVV---PLCNRSKdvvEPLL---RPQWYV 681
Cdd:COG0060 349 GLPVLNPVDDDGRFTEEAPLFAGLFVKDANPAIIEDLKERGaLLA-REK---IThsyPHCWRCK---TPLIyraTPQWFI 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 682 RCGEMAQAASAAVTR-------GDLRIlpeahqrtwHAWMDNIREWCISRQLWWGHRIPAyFVTVSdpavpPGEDPDGRY 754
Cdd:COG0060 422 SMDKLRDRALEAIEKvnwipewGEGRF---------GNMLENRPDWCISRQRYWGVPIPI-WVCED-----CGELHRTEE 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 755 WVSGRNEAEAREKAAKEFGVSPDKISLQQD-------------EDVLDTWFSSGLFPLSILgwpNQSEDLSvfYPGTL-L 820
Cdd:COG0060 487 VIGSVAELLEEEGADAWFELDLHRPFLDETlkcpkcggtmrrvPDVLDVWFDSGSMHFAVL---ENREELH--FPADFyL 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 821 EtGHD---------ILffwvarmvmLGLKLTGRLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVIygislqglhNQLl 891
Cdd:COG0060 562 E-GSDqtrgwfyssLL---------TSTALFGRAPYKNVLTHGFVLDEDGRKMSKSLGNVVDPQEVI---------DKY- 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 892 nsnldpsevekakegqkadfpagipecGTDALRFgLCAYMSQGRDINLDVNRILGYRHFCNKLWNATKFALRGLGkGFVP 971
Cdd:COG0060 622 ---------------------------GADILRL-WVASSDYWGDLRFSDEILKEVRDVYRRLRNTYRFLLANLD-DFDP 672
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 972 SPTSQPGGHESLVDRWIRSRLTEAVRLSNQGFQAYDFPAVTTAqysfwLYELCDV-----YLECLKPVL--NGVDQVAAE 1044
Cdd:COG0060 673 AEDAVPYEDLPELDRWILSRLNELIKEVTEAYDNYDFHRAYRA-----LHNFCVEdlsnwYLDISKDRLytEAADSLDRR 747
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 1045 CARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRrmpQAPPSLCVTPYPEPSEcSWKDPeaeaalelalsitravrSLRA 1124
Cdd:COG0060 748 AAQTTLYEVLETLVRLLAPILPFTAEEIWQNLPG---EAEESVHLADWPEVDE-ELIDE-----------------ELEA 806
|
890 900
....*....|....*....|....*.
gi 530382523 1125 DYNLTRirpdcflEVADEATGALASA 1150
Cdd:COG0060 807 KWDLVR-------EVRSAVLKALEAA 825
|
|
| GST_C_ValRS_N |
cd10294 |
Glutathione S-transferase C-terminal-like, alpha helical domain of vertebrate Valyl-tRNA ... |
92-213 |
2.83e-63 |
|
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: 210.46 E-value: 2.83e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 92 AAVLVQQWVSYADTELIPAACGATLPALGL-RSSAQDPQAVLGALGRALSPLEEWLRLHTYLAGEAPTLADLAAVTALLL 170
Cdd:cd10294 1 ACALVWQWVSFADNELTPAACAAAFPLLGLsGSDKQNQQRSLAELQRVLKVLDCYLKLRTYLVGEAITLADIAVACALLL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 530382523 171 PFRYVLDPPARRIWNNVTRWFVTCVRQPEFRAVLGEVVLYSGA 213
Cdd:cd10294 81 PFKYVLDPARRESLLNVTRWFLTCVNQPEFLAVLGEVSLCEKA 123
|
|
| Anticodon_Ia_Val |
cd07962 |
Anticodon-binding domain of valyl tRNA synthetases; This domain is found in valyl tRNA ... |
939-1076 |
6.99e-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: 6.99e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 939 LDVNRILGYRHFCNKLWNATKFALRGLGKGFVPSPTSQPgghESLVDRWIRSRLTEAVRLSNQGFQAYDFPAVTTAQYSF 1018
Cdd:cd07962 1 FDEKRVEGGRNFCNKLWNAARFVLMNLEDDDEPEEDPES---LSLADRWILSRLNKTVEEVTEALENYRFSEAATALYEF 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 530382523 1019 WLYELCDVYLECLKPVLNGVDQVAAECARQTLYTCLDVGLRLLSPFMPFVTEELFQRL 1076
Cdd:cd07962 78 FWNDFCDWYLELVKPRLYGEDEEEKKAARATLYYVLETILRLLHPFMPFITEELWQRL 135
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
337-878 |
8.06e-53 |
|
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: 188.01 E-value: 8.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 337 VFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKKLWREQGLSRhqlgREAFLQE 416
Cdd:cd00668 1 KFYVTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGGRKKKTIW----IEEFRED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 417 VWKWKEEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSAAVTEAFVRLHEEGIIYRSTRLVnwsctlnsaisdievdkkEL 496
Cdd:cd00668 77 PKEFVEEMSGEHKEDFRRLGISYDWSDEYITTEPEYSKAVELIFSRLYEKGLIYRGTHPV------------------RI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 497 TGRTLLSVPGYKEKvefgvlvsfaykvqgsdsdeevvvattrietmlgdvavavhpkdtryqhlkgknvihpflsrslpi 576
Cdd:cd00668 139 TEQWFFDMPKFKEK------------------------------------------------------------------ 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 577 vfdefvdmdfgtgavkitpahdqndyevgqrhgleaisimdsrgalinvpppflglprfearkavlvalkergLFRGIED 656
Cdd:cd00668 153 -------------------------------------------------------------------------LLKALRR 159
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 657 NPMVVplcnrskdvvepllrPQWYVRCGEmaqaasaavtrgdlrilpeahqrtwhaWMDNIREWCISRQLWWGHRIPayf 736
Cdd:cd00668 160 GKIVP---------------EHVKNRMEA---------------------------WLESLLDWAISRQRYWGTPLP--- 194
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 737 vtvsdpavppgedpdgrywvsgrneaearekaakefgvspdkislqqdEDVLDTWFSSGLFPLSILGWPNQSEDLSVFYP 816
Cdd:cd00668 195 ------------------------------------------------EDVFDVWFDSGIGPLGSLGYPEEKEWFKDSYP 226
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530382523 817 GTLLETGHDILFFWVARMVMLGLKLTGRLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVI 878
Cdd:cd00668 227 ADWHLIGKDILRGWANFWITMLVALFGEIPPKNLLVHGFVLDEGGQKMSKSKGNVIDPSDVV 288
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
313-1077 |
2.80e-45 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 178.04 E-value: 2.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 313 WWEQQGFFKpeygrpNVSAANPRGVFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVV 392
Cdd:PLN02843 15 LWEENQVYK------RVSDRNNGESFTLHDGPPYANGDLHIGHALNKILKDFINRYQLLQGKKVHYVPGWDCHGLPIELK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 393 VEKKLWREqglSRHQLGREAFLQEVWKWKEEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSAAVTEAFVRLHEEGIIYRS 472
Cdd:PLN02843 89 VLQSLDQE---ARKELTPIKLRAKAAKFAKKTVDTQRESFKRYGVWGDWENPYLTLDPEYEAAQIEVFGQMFLNGYIYRG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 473 TRLVNWSCTLNSAISDIEVDKKEltgrtllsvpGYKEKVEFGVL-VSFAYKVQGSDSDE-----EVVVATTRIETMLGDV 546
Cdd:PLN02843 166 RKPVHWSPSSRTALAEAELEYPE----------GHVSKSIYVAFpVVSPSETSPEELEEflpglSLAIWTTTPWTMPANA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 547 AVAVHPK----------------------DTRYQH--------------------------------------LKGKNVI 566
Cdd:PLN02843 236 AVAVNDKlqysvvevqsfsedestsggnkKKRPGNvlkeqqklflivatdlvpaleakwgvklvvlktfpgsdLEGCRYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 567 HPFLSRSLPIVFD-EFVDMDFGTGAVKITPAHDQNDYEVGQRHGLEAISIMDSRGALINVPPPFLGLPRF-EARKAVLVA 644
Cdd:PLN02843 316 HPLYNRESPVVIGgDYITTESGTGLVHTAPGHGQEDYITGLKYGLPLLSPVDDAGKFTEEAGQFSGLSVLgEGNAAVVEA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 645 LKERGLFRGIEDNPMVVPLCNRSKdvvEP-LLRP--QWYVRCGEMAQAASAAVtrGDLRILPEAHQRTWHAWMDNIREWC 721
Cdd:PLN02843 396 LDEAGSLLMEEAYGHKYPYDWRTK---KPtIFRAteQWFASVEGFRQAALDAI--DKVKWIPAQGENRIRAMVSGRSDWC 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 722 ISRQLWWGHRIPAYFVTVSDPAV--------------PPGEDPdgrYWVSGRNE---AEAREKAAKefgvspdkisLQQD 784
Cdd:PLN02843 471 ISRQRTWGVPIPVFYHVETKEPLmneetiahvksivaQKGSDA---WWYMDVEDllpEKYRDKASD----------YEKG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 785 EDVLDTWFSSGLFPLSILGwpnQSEDLSvfYPGTLLETGHDILFFWVARMVMLGLKLTGRLPFREVYLHAIVRDAHGRKM 864
Cdd:PLN02843 538 TDTMDVWFDSGSSWAGVLG---SREGLS--YPADLYLEGSDQHRGWFQSSLLTSVATKGKAPYKSVLTHGFVLDEKGFKM 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 865 SKSLGNVIDPLDVIYGislqglhnqllnsnldpsevekaKEGQKADfpagiPECGTDALRFGLCA--YMSqgrDINLDVN 942
Cdd:PLN02843 613 SKSLGNVVDPRLVIEG-----------------------GKNQKQE-----PAYGADVLRLWVASvdYTG---DVLIGPQ 661
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 943 rIL-----GYRhfcnKLWNATKFALRGLGKgFVPSpTSQPggHESL--VDRWIRSRLTEAVRLSNQGFQAYDFPAVTTAQ 1015
Cdd:PLN02843 662 -ILkqmsdIYR----KLRGTLRYLLGNLHD-WKPD-NAVP--YEDLpsIDKYALFQLENVVNEIEESYDNYQFFKIFQIL 732
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530382523 1016 YSFWLYELCDVYLECLKPVL--NGVDQVAAECARQTLYTCLDVGLRLLSPFMPFVTEELFQRLP 1077
Cdd:PLN02843 733 QRFTIVDLSNFYLDVAKDRLyvGGTTSFTRRSCQTVLAAHLLSLLRAIAPILPHLAEDAWQNLP 796
|
|
| PLN02882 |
PLN02882 |
aminoacyl-tRNA ligase |
344-1151 |
1.12e-43 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215477 [Multi-domain] Cd Length: 1159 Bit Score: 173.76 E-value: 1.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 344 PPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKKL---WREQGLsrhQLGREAFLQE---- 416
Cdd:PLN02882 46 PPFATGLPHYGHILAGTIKDIVTRYQSMTGHHVTRRFGWDCHGLPVEYEIDKKLgikRRDDVL---KMGIDKYNEEcrsi 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 417 VWKWKEEKGDRIyhqlKKLGSSLDWDRACFTMDPKLSAAVTEAFVRLHEEGIIYRSTRLVNWSCTLNSAISDIEVDKKel 496
Cdd:PLN02882 123 VTRYSKEWEKTV----TRTGRWIDFENDYKTMDPKFMESVWWVFKQLFEKGLVYKGFKVMPYSTACKTPLSNFEAGLN-- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 497 tgrtllsvpgYKEKVEFGVLVSFAykVQGsDSDEEVVVA-TTRIETMLGDVAVAVHPK------------------DTRY 557
Cdd:PLN02882 197 ----------YKDVSDPAVMVSFP--IVG-DPDNASFVAwTTTPWTLPSNLALCVNPNftyvkvrnkytgkvyivaESRL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 558 QHL--------KGKN---------VIHPFLSRSL------PI--------------VFDEFVDMDFGTGAVKITPAHDQN 600
Cdd:PLN02882 264 SALptakpkskKGSKpenaaegyeVLAKVPGSSLvgkkyePLfdyfsefsdtafrvVADDYVTDDSGTGVVHCAPAFGED 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 601 DYEVGQRHGL-----EAISIMDSRGALINVPPPFLGLPRFEARKAVLVALKERGlfRGIEDNPMV--VPLCNRSKdvvEP 673
Cdd:PLN02882 344 DYRVCLANGIiekggNLPVPVDDDGCFTEKVTDFSGRYVKDADKDIIAAIKAKG--RLVKSGSIThsYPFCWRSD---TP 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 674 LLR---PQWYVRCGEMAQaasaavtrgdlRILPEAHQRTW----------HAWMDNIREWCISRQLWWGHRIPayfVTVS 740
Cdd:PLN02882 419 LIYravPSWFVKVEEIKD-----------RLLENNKQTYWvpdyvkekrfHNWLENARDWAVSRSRFWGTPLP---IWIS 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 741 DpavppgedpDGRYWVSGRNEAEAREKAAK---------------------EFGVspdkisLQQDEDVLDTWFSSGLFPL 799
Cdd:PLN02882 485 D---------DGEEVVVIGSIAELEKLSGVkvtdlhrhfidhitipssrgpEFGV------LRRVDDVFDCWFESGSMPY 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 800 SILGWPNQSEDLsvF---YPGTLLETGHDILFFWVARMVMLGLKLTGRLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLD 876
Cdd:PLN02882 550 AYIHYPFENKEL--FeknFPADFVAEGLDQTRGWFYTLMVLSTALFDKPAFKNLICNGLVLAEDGKKMSKSLKNYPDPNE 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 877 VI--YGISLQGLHnqLLNSnldpsevekakegqkadfpagiPECGTDALRFGLCAYMSQGRDINLD-VNrilGYRHFcnk 953
Cdd:PLN02882 628 VIdkYGADALRLY--LINS----------------------PVVRAEPLRFKEEGVFGVVKDVFLPwYN---AYRFL--- 677
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 954 LWNATKFALRGLGKgFVPSPTSQPGGHESLVDRWIRSRLTEAVRLSNQGFQAYDFPAVTTAQYSFwLYELCDVYLECLKP 1033
Cdd:PLN02882 678 VQNAKRLEVEGGAP-FVPLDLAKLQNSANVLDRWINSATQSLVKFVREEMGAYRLYTVVPYLVKF-IDNLTNIYVRFNRK 755
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 1034 VLNGVDQVA-AECARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRMPQAPPSLCVTPYPEPSEcSWKDPEAEAALELA 1112
Cdd:PLN02882 756 RLKGRTGEEdCRTALSTLYNVLLTSCKVMAPFTPFFTEVLYQNLRKVLPGSEESIHYCSFPQVDE-GELDERIEQSVSRM 834
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 530382523 1113 LSITRAVRSLRADYN---------LTRIRPDcfLEVADEATGALASAV 1151
Cdd:PLN02882 835 QTVIELARNIRERHNkplktplkeMVVVHPD--AEFLDDITGKLKEYV 880
|
|
| GST_C_EF1Bgamma_like |
cd03181 |
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ... |
92-209 |
1.69e-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: 1.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 92 AAVLVQQWVSYADTELIPAACGATLPALGLR-SSAQDPQAVLGALGRALSPLEEWLRLHTYLAGEAPTLADLAAVTALLL 170
Cdd:cd03181 1 EAAQVLQWISFANSELLPAAATWVLPLLGIApYNKKAVDKAKEDLKRALGVLEEHLLTRTYLVGERITLADIFVASALLR 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 530382523 171 PFRYVLDPPARRIWNNVTRWFVTCVRQPEFRAVLGEVVL 209
Cdd:cd03181 81 GFETVLDPEFRKKYPNVTRWFNTVVNQPKFKAVFGEVKL 119
|
|
| PTZ00427 |
PTZ00427 |
isoleucine-tRNA ligase, putative; Provisional |
344-1078 |
2.76e-34 |
|
isoleucine-tRNA ligase, putative; Provisional
Pssm-ID: 173617 [Multi-domain] Cd Length: 1205 Bit Score: 143.57 E-value: 2.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 344 PPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKklwrEQGLSRhqlgREAFLQEVWKWKEE 423
Cdd:PTZ00427 110 PPFATGLPHYGHLLAGIIKDCVTRYFYQCGFSVERKFGWDCHGLPIEYEIEK----ENNINK----KEDILKMGIDVYNE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 424 KGDRIYHQ--------LKKLGSSLDWDRACFTMDPKLSAAVTEAFVRLHEEGIIYRSTRLVNWSCTLNSAISDIEV---- 491
Cdd:PTZ00427 182 KCRGIVLKysnewvktVERIGRWIDFKNDYKTMDKTFMESVWWVFSELYKNNYVYKSFKVMPYSCKCNTPISNFELnlny 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 492 ----------------------------DKKELTGRTLlsVPGYKEKVEFG----------------------------- 514
Cdd:PTZ00427 262 kdtpdpsiiisfvlcsdfpkveeecnieEDKQLLGEKY--SVLYNNKRENSnngnnnstnnvcyaqhseilawtttpwtl 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 515 -------VLVSFAY-KVQGSDSDEEVVVATTRIETMLGDVAVAV------------HPKDTRYQHLKGKNV-IHPFLSRS 573
Cdd:PTZ00427 340 psnlalcVNEHFTYlRIHHVKSNRVVIVGECRLEWIMKELKWNVedlkivnrfkgkELKGLRYKPLFTNFYeKYNFKERA 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 574 LPIVFDEFVDMDFGTGAVKITPAHDQNDYEVGQRHGL----EAISI--MDSRGALINVPPPFLGLPRFEARKAVLVALKE 647
Cdd:PTZ00427 420 YKILADDFVTDDAGTGIVHCAPTYGEDDFRVCKKNGVidpeKNIFIdpLDANGYFTNEVEEVQNLYIKEADNVIKKKLKN 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 648 RGlfRGIEDNPMV--VPLCNRSKdvvEPLLR---PQWYVRcgeMAQAASAAVTRGDLRILPEAH--QRTWHAWMDNIREW 720
Cdd:PTZ00427 500 EN--RLLSNNTIVhsYPFCWRSD---TPLIYraiPAWFIR---VSNSTNELVKNNETTYWIPAHikEKKFHNWIKDAKDW 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 721 CISRQLWWGHRIPAYF-----VTVSDPAVPPGEDPDG--------RYWVsgrNEAEAREKAAKEFGvspdkiSLQQDEDV 787
Cdd:PTZ00427 572 CISRNRYWGTPIPIWAdekmeTVICVESIKHLEELSGvknindlhRHFI---DHIEIKNPKGKTYP------KLKRIPEV 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 788 LDTWFSSGLFPLSILGWP--NQSEDLSVFYPGTLLETGHDILFFWVARMVMLGLKLTGRLPFREVYLHAIVRDAHGRKMS 865
Cdd:PTZ00427 643 FDCWFESGSMPYAKVHYPfsTEKEDFHKIFPADFIAEGLDQTRGWFYTLLVISTLLFDKAPFKNLICNGLVLASDGKKMS 722
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 866 KSLGNVIDPLDVIYGISLQGLHNQLLNSNLDPSEVEKAKEgqkadfpAGIPEcgtdALRFGLCAYMSQGRDINLDVNRIl 945
Cdd:PTZ00427 723 KRLKNYPDPLYILDKYGADSLRLYLINSVAVRAENLKFQE-------KGVNE----VVKSFILPFYHSFRFFSQEVTRY- 790
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 946 gyrhfcnKLWNATKFALRglgkgfvpspTSQPGGHESLVDRWIRSRLTEAVRLSNQGFQAYDFPAVTTAQYSFwLYELCD 1025
Cdd:PTZ00427 791 -------ECLNKKQFLFN----------TDYIYKNDNIMDQWIFSSVQSLTKSVHTEMKAYKLYNVLPKLLQF-IENLTN 852
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 530382523 1026 VYLECLKPVLNGV----DQVAAECarqTLYTCLDVGLRLLSPFMPFVTEELFQRLPR 1078
Cdd:PTZ00427 853 WYIRLNRDRMRGSlgeeNCLQSLC---TTYRTLHLFTVLMAPFTPFITEYIYQQLRR 906
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
344-880 |
5.66e-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: 122.34 E-value: 5.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 344 PPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKKLWREQGLSRHQLGREAFLQE----VWK 419
Cdd:cd00818 9 PPYANGLPHYGHALNKILKDIINRYKTMQGYYVPRRPGWDCHGLPIELKVEKELGISGKKDIEKMGIAEFNAKcrefALR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 420 WKEEKGdriyHQLKKLGSSLDWDRACFTMDPKLSAAVTEAFVRLHEEGIIYRSTRLVNWsctlnsaisdievdkkeltgr 499
Cdd:cd00818 89 YVDEQE----EQFQRLGVWVDWENPYKTMDPEYMESVWWVFKQLHEKGLLYRGYKVVPW--------------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 500 tllsvpgykekvefgvlvsfaykvqgsdsdeevvvattrietmlgdvavavhpkdtryqhlkgknvihpflsrslPIVFd 579
Cdd:cd00818 144 ---------------------------------------------------------------------------PLIY- 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 580 efvdmdfgtgavkitpahdqndyevgqrhgleaisimdsrgalinvpppflglprfearKAVlvalkerglfrgiednpm 659
Cdd:cd00818 148 -----------------------------------------------------------RAT------------------ 150
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 660 vvplcnrskdvvepllrPQWYVRCGEMAQAASAAVTRgdLRILPEAHQRTWHAWMDNIREWCISRQLWWGHRIPAyfvtv 739
Cdd:cd00818 151 -----------------PQWFIRVTKIKDRLLEANDK--VNWIPEWVKNRFGNWLENRRDWCISRQRYWGTPIPV----- 206
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 740 sdpavppgedpdgryWVSgrneaearekaakefgVSPDKISLQQDEDVLDTWFSSGLFPLSILGWPNQSEDLSVFYPGTL 819
Cdd:cd00818 207 ---------------WYC----------------EDCGEVLVRRVPDVLDVWFDSGSMPYAQLHYPFENEDFEELFPADF 255
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530382523 820 LETGHDILFFWVARMVMLGLKLTGRLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVI--YG 880
Cdd:cd00818 256 ILEGSDQTRGWFYSLLLLSTALFGKAPYKNVIVHGFVLDEDGRKMSKSLGNYVDPQEVVdkYG 318
|
|
| Anticodon_1 |
pfam08264 |
Anticodon-binding domain of tRNA ligase; This domain is found mainly hydrophobic tRNA ... |
985-1133 |
7.37e-29 |
|
Anticodon-binding domain of tRNA ligase; This domain is found mainly hydrophobic tRNA synthetases. The domain binds to the anticodon of the tRNA ligase.
Pssm-ID: 400523 [Multi-domain] Cd Length: 141 Bit Score: 112.88 E-value: 7.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 985 DRWIRSRLTEAVRLSNQGFQAYDFPAVTTAQYSFWLYELCDVYLECLKPVLNGVDqvAAECARQTLYTCLDVGLRLLSPF 1064
Cdd:pfam08264 1 DRWILSRLNKLIKEVTEAYENYRFNTAAQALYEFFWNDLSDWYLELIKDRLYGEE--PDSRAQTTLYEVLETLLRLLAPF 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530382523 1065 MPFVTEELFQRLprrmpqappSLCVTPYPEPSECSwkDPEAEAALELALSITRAVRSLRADYNLTRIRP 1133
Cdd:pfam08264 79 MPFITEELWQKE---------SIHLAPWPEDAELE--EAELEEAFELRQEIVQAIRKLRSELKIKKSLP 136
|
|
| leuS_bact |
TIGR00396 |
leucyl-tRNA synthetase, eubacterial and mitochondrial family; The leucyl-tRNA synthetases ... |
301-1080 |
2.73e-28 |
|
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: 123.32 E-value: 2.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 301 YSPRYVEAAWYPWWEQQGFFKPEygrpnvSAANPRGVFMMCI-PPPnvTGSLHLGHALTNAIQDSLTRWHRMRGETTLWN 379
Cdd:TIGR00396 1 YNHIEIEEKWQQKWDENKTFKVT------DDSSKPKYYILSMfPYP--SGALHMGHVRNYTITDVLSRYYRMKGYNVLHP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 380 PGCDHAGI-ATQVVVEKKlwreqglsrhqlgreaflQEVWKWKEEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSAAVTE 458
Cdd:TIGR00396 73 IGWDAFGLpAENAAIKRG------------------IHPAKWTYENIANMKKQLQALGFSYDWDREIATCDPEYYKWTQW 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 459 AFVRLHEEGIIYRSTRLVNWSCTLNSAI-------------SDIEVDKKELTgRTLLSVPGYKEKV-------------- 511
Cdd:TIGR00396 135 IFLELFEKGLAYVKEADVNWCPNDGTVLaneqvdsdgrswrGDTPVEKKELK-QWFLKITAYAEELlndleeldhwpesv 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 512 ----------EFGVLVSFAYKvqgsDSDEEVVVATTRIETMLGDVAVAV---HP-------------------------K 553
Cdd:TIGR00396 214 kemqrnwigkSEGVEITFKIA----DHDEKITVFTTRPDTIFGVTYLALapeHPlvekaaennpkvaafikkilnktvaE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 554 DTRYQHLK-----GKNVIHPFLSRSLPIVFDEFVDMDFGTGAVKITPAHDQNDYEVGQRHGLEAISIMDS---------- 618
Cdd:TIGR00396 290 RTKATKEKkgvdtGIKAIHPLTGEKIPIWVANYVLMEYGTGAVMGVPAHDERDFEFAQKYGLPIKPVIDPaekdlsltaa 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 619 ---RGALINvPPPFLGLPRFEARKAVLVALKERGLfrgiednpmvvplcnrSKDVVEpllrpqwYvrcgemaqaasaavt 695
Cdd:TIGR00396 370 yteDGVLVN-SGEFNGLNSSEARNAIIDMLEKEGK----------------GKRKVN-------Y--------------- 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 696 rgdlrilpeahqrtwhawmdNIREWCISRQLWWGHRIPAYFVTVSDPAVPPGED-P-----DGRYWVSGRNEAEAREKAA 769
Cdd:TIGR00396 411 --------------------RLRDWGFSRQRYWGEPIPIIHCEDGGVVPVPEEDlPvilpeDVVYDGDGGSPLSRIPEWV 470
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 770 KEFGVSPDKISLQQdEDVLDTWFSSGLFPLSILGWPNQS-----EDLSVFYPGTLLETG--HDILF-----FWVARMVML 837
Cdd:TIGR00396 471 NVTCPSCGKPALRE-TDTMDTFAGSSWYYLRYLDPKNTDgpfdkEKAEYWLPVDLYIGGieHAILHllyarFFHKFLRDI 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 838 GLkLTGRLPFREVYLHAIV-----------------------RDAHGR--------KMSKSLGNVIDPLDViygislqgl 886
Cdd:TIGR00396 550 GY-VNTKEPFKKLINQGMVlgfyyppngkvpadvlterdekgKDKAGGelvyvgyeKMSKSKGNGIDPQEI--------- 619
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 887 hnqllnsnldpsevekakegqkadfpagIPECGTDALRFGLcayMSQG---RDINLDVNRILGYRHFCNKLWNatkFALR 963
Cdd:TIGR00396 620 ----------------------------VESYGADALRLFI---MFMGpiaASLEWNESGLEGARRFLDRVWN---LVYE 665
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 964 GLGKGFVPSPTSQPgghESLVDRWIRSRLTEAVRLSNQGFQ-AYDFPAVTTAQYSF----WLYELCDVYLECLKPVlngv 1038
Cdd:TIGR00396 666 ITGELDAASLTVTA---LEEAQKELRRDVHKFLKKVTEDLEkRESFNTAISAMMELlnklYKAKKEALMLEYLKGF---- 738
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 530382523 1039 dqvaaecarqtlytcldvgLRLLSPFMPFVTEELFQRLPRRM 1080
Cdd:TIGR00396 739 -------------------VTVLSPFAPHLAEELWEKLGSEP 761
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
297-880 |
8.88e-25 |
|
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: 112.07 E-value: 8.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 297 MPDSYSPRYVEAAWYPWWEQQGFFKPeygrPNVSAANPRGVFMMcIPPPnvTGSLHLGHALTNAIQDSLTRWHRMRGETT 376
Cdd:COG0495 1 MQERYNPKEIEKKWQKYWEENGTFKA----DEDSSKPKYYVLDM-FPYP--SGRLHMGHVRNYTIGDVVARYKRMQGYNV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 377 LwNP-GCD-------HAGIATQVvvekklwreqglsrHqlgrEAflqevwKWKEEKGDRIYHQLKKLGSSLDWDRACFTM 448
Cdd:COG0495 74 L-HPmGWDafglpaeNAAIKNGV--------------H----PA------EWTYENIANMRRQLKRLGLSYDWSREIATC 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 449 DP-------KLsaavteaFVRLHEEGIIYRSTRLVNWSCTLN------------SAISDIEVDKKELTG----------R 499
Cdd:COG0495 129 DPeyykwtqWI-------FLQLYEKGLAYRKEAPVNWCPVDQtvlaneqvidgrCWRCGAPVEKKELPQwflkitdyadE 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 500 tLLS----VPGYKEKV----------EFGVLVSFAYKvqgsDSDEEVVVATTRIETMLGD--VAVAV-HP------KDTR 556
Cdd:COG0495 202 -LLDdldkLDGWPEKVktmqrnwigrSEGAEVDFPVE----GSDEKITVFTTRPDTLFGAtfMVLAPeHPlvkelaTPEQ 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 557 YQHLK--------------------------GKNVIHPFLSRSLPI-VFDeFVDMDFGTGAVKITPAHDQNDYEVGQRHG 609
Cdd:COG0495 277 NAAVAafieeakkkseiertsetkektgvftGLYAINPLTGEKIPIwIAD-YVLMDYGTGAVMAVPAHDQRDFEFAKKYG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 610 L-----------EAISIMDS----RGALINvPPPFLGLPRFEARKAVLVALKERGLfrgiednpmvvplcnrskdvvepl 674
Cdd:COG0495 356 LpikqviapedgDDPDILEEaytgDGVLIN-SGEFDGLDSEEAKEAIIEWLEEKGL------------------------ 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 675 lrpqwyvrcGEmaqaasAAVT-RgdlrilpeahqrtwhawmdnIREWCISRQLWWGHRIPAYF------VTVSD------ 741
Cdd:COG0495 411 ---------GK------RKVNyR--------------------LRDWLISRQRYWGEPIPIIHcedcgvVPVPEdqlpve 455
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 742 -PAV----PPGEDPDGRY--WVS------GrneaeareKAAKefgvspdkislqQDEDVLDTWF-SSglfplsilgW--- 804
Cdd:COG0495 456 lPEDvdfdPTGGSPLARApeWVNvtcpkcG--------GPAR------------RETDTMDTFVdSS---------Wyyl 506
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 805 ----PNQSE--------------DLsvfYPGtlletG--HDIL------FFWvarMVM--LGLkLTGRLPFR-------- 848
Cdd:COG0495 507 rytdPHNDEapfdpeaanywlpvDQ---YIG-----GieHAILhllyarFFT---KVLrdLGL-VSFDEPFKrlltqgmv 574
|
730 740 750
....*....|....*....|....*....|....*
gi 530382523 849 -EVYLHAIVRDAHGrKMSKSLGNVIDPLDVI--YG 880
Cdd:COG0495 575 lEVGKDGVVIGGIE-KMSKSKGNVVDPDEIIekYG 608
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
351-1103 |
3.20e-21 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 100.71 E-value: 3.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 351 LHLGHALTNAIQDSLTRWHRMRGETTLWnPGCDHA------GIATQV----------------VVEKKLWReqglsrhql 408
Cdd:PRK12300 1 LHVGHGRTYTIGDVIARYKRMRGYNVLF-PMAFHVtgtpilGIAERIargdpetielykslygIPEEELEK--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 409 greafLQEVWKWKEEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSAAVTEAFVRLHEEGIIYRSTRLVNWSCTLNSAISD 488
Cdd:PRK12300 71 -----FKDPEYIVEYFSEEAKEDMKRIGYSIDWRREFTTTDPEYSKFIEWQFRKLKEKGLIVKGSHPVRYCPNDNNPVGD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 489 ieVDKKELTGrtllsvpgyKEKVEFgVLVSFAykvqgsDSDEEV-VVATTRIETMLGDVAVAVHPKDT------------ 555
Cdd:PRK12300 146 --HDLLDGEE---------PEIVEY-TLIKFE------ESEDLIlPAATLRPETIFGVTNLWVNPDATyvkaevdgekwi 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 556 ---------RYQH-------------LKGKNVIHPFLSRSLPIVFDEFVDMDFGTGAVKITPAHDQNDY----------- 602
Cdd:PRK12300 208 vskeaaeklSFQDrdveiieeikgseLIGKKVKNPVTGKEVPILPADFVDPDNGTGVVMSVPAHAPYDYvalrdlkknke 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 603 --------------EVGQRHGLEAISIMD---------------------SRGALINVPPPFLGLPRFEARKAVLVALKE 647
Cdd:PRK12300 288 lldviepiplieveGYGEFPAKEVVEKLGiksqedpeleeatkevyraefHKGVLKENTGEYAGKPVREAREKITKDLIE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 648 RGLFRGIED--NPMVVPLCNrSKDVVEpLLRPQWYVRCGEMAQAASA--AVTRgdLRILPEAHQRTWHAWMDNIREWCIS 723
Cdd:PRK12300 368 KGIADIMYEfsNRPVYCRCG-TECVVK-VVKDQWFIDYSDPEWKELAhkALDN--MEIIPEEYRKEFENTIDWLKDRACA 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 724 RQLWWGHRIP-----------------AYFvTVSdpavppgedpdgrywvsgrneaeareKAAKEFGVSPDKIslqqDED 786
Cdd:PRK12300 444 RRRGLGTRLPwdeewiieslsdstiymAYY-TIA--------------------------HKIREYGIKPEQL----TPE 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 787 VLDTWF-----------SSGLfPLSILgwPNQSEDLSVFYPGTLLETGHD-----ILFF------------WVARMVMLG 838
Cdd:PRK12300 493 FFDYVFlgkgdpeevskKTGI-PKEIL--EEMREEFLYWYPVDWRHSGKDlipnhLTFFifnhvaifpeekWPRGIVVNG 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 839 LKLtgrlpfREvylhaivrdahGRKMSKSLGNVIdPLdviygislqglhnqllnsnldpsevEKAKEgqkadfpagipEC 918
Cdd:PRK12300 570 FVL------LE-----------GKKMSKSKGNVI-PL-------------------------RKAIE-----------EY 595
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 919 GTDALRFGL--CAYMSQGRDINL-DVNRILgyRHFcNKLWNatkFALRGLGKGfvpsptsqPGGHESLVDRWIRSRLTEA 995
Cdd:PRK12300 596 GADVVRLYLtsSAELLQDADWREkEVESVR--RQL-ERFYE---LAKELIEIG--------GEEELRFIDKWLLSRLNRI 661
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 996 VRLSNQGFQAYDF-PAVTTAQYSfwLYELCDVYLEcLKPVLNgvdqvaaecaRQTLYTCLDVGLRLLSPFMPFVTEELFQ 1074
Cdd:PRK12300 662 IKETTEAMESFQTrDAVQEAFYE--LLNDLRWYLR-RVGEAN----------NKVLREVLEIWIRLLAPFTPHLAEELWH 728
|
890 900
....*....|....*....|....*....
gi 530382523 1075 RLPRrmpQAPPSLcvTPYPEPSEcSWKDP 1103
Cdd:PRK12300 729 KLGG---EGFVSL--EKWPEPDE-SKIDE 751
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
288-749 |
1.94e-20 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 97.97 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 288 GEKKDVSGPMPDSYSPRYVEAAWYPWWEQQGFFK-PEygrpNVSAANPRGVFMMCIPPPNVTGsLHLGHALTNAIQDSLT 366
Cdd:PLN02563 67 STTAKTTPAAKRAYPFHEIEPKWQRYWEENRTFRtPD----DVDTSKPKFYVLDMFPYPSGAG-LHVGHPEGYTATDILA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 367 RWHRMRGETTLWNPGCDHAGI-ATQVVVEKklwreqglSRHQlgREAFLQEVwkwkeekgDRIYHQLKKLGSSLDWDRAC 445
Cdd:PLN02563 142 RYKRMQGYNVLHPMGWDAFGLpAEQYAIET--------GTHP--KITTLKNI--------ARFRSQLKSLGFSYDWDREI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 446 FTMDPKLSAAVTEAFVRLHEEGIIYRSTRLVNWSCTLNSAISDIEVDK--KELTGRTLLSVP------------------ 505
Cdd:PLN02563 204 STTEPEYYKWTQWIFLQLLKRGLAYQAEVPVNWCPALGTVLANEEVVDglSERGGHPVIRKPmrqwmlkitayadrlled 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 506 --------GYKE------------KVEFGVLvsfayKVQGSDSDEEVVVATTRIETMLGDVAVAVHPKD----------- 554
Cdd:PLN02563 284 lddldwpeSIKEmqrnwigrsegaELDFSVL-----DGEGKERDEKITVYTTRPDTLFGATYLVVAPEHpllsslttaeq 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 555 -------------------TRYQHLK-----GKNVIHPFLSRSLPIVFDEFVDMDFGTGAVKITPAHDQNDYEVGQRHGL 610
Cdd:PLN02563 359 keaveeyvdaasrksdlerTELQKEKtgvftGSYAINPATGEAIPIWVADYVLGSYGTGAIMAVPAHDTRDFEFAQKFDL 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 611 EAISImdsrgalinVPPPFLGLPRFE---ARKAVLVALKERGL-FRGIEDNpmvvplcNRSKDVVEPLlrpqwyvrcgEM 686
Cdd:PLN02563 439 PIKWV---------VKPADGNEDDAEkayTGEGVIVNSSSSGLdINGLSSK-------EAAKKVIEWL----------EE 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530382523 687 AQAASAAVTRgdlrilpeahqrtwhawmdNIREWCISRQLWWGHRIPAYFVTVSDPAVPPGED 749
Cdd:PLN02563 493 TGNGKKKVNY-------------------KLRDWLFARQRYWGEPIPVVFLEDSGEPVPVPES 536
|
|
| Anticodon_Ia_Ile_ABEc |
cd07961 |
Anticodon-binding domain of archaeal, bacterial, and eukaryotic cytoplasmic isoleucyl tRNA ... |
948-1097 |
4.95e-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: 80.29 E-value: 4.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 948 RHFCNKLWNATKFAL--RGLgKGFVPSPTSQPGGHESLVDRWIRSRLTEAVRLSNQGFQAYDFPAVTTAQYSFWLyELCD 1025
Cdd:cd07961 11 RKVLLPLWNAYRFFVtyANL-DGFDPGKDDDAVASLNVLDRWILSRLNSLIKEVTEEMEAYDLYTAVRALLEFID-ELTN 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530382523 1026 VYL----ECLKPVLNGVDQVAAecaRQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRMPQAPPSLCVTPYPEPSE 1097
Cdd:cd07961 89 WYIrrnrKRFWGEEGDDDKLAA---YATLYEVLLTLSRLMAPFTPFITEEIYQNLRRELGDAPESVHLLDWPEVDE 161
|
|
| GST_C |
pfam00043 |
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ... |
107-198 |
5.90e-16 |
|
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: 74.24 E-value: 5.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 107 LIPAACGATLPALGLRS--SAQDPQAVLGALGRALSPLEEWLRLHTYLAGEAPTLADLAAVTALLLPFRYVLDPPaRRIW 184
Cdd:pfam00043 1 LMDLRMQIALLPYVPPEekKEPEVDEALEKVARVLSALEEVLKGQTYLVGDKLTLADIALAPALLWLYELDPACL-REKF 79
|
90
....*....|....
gi 530382523 185 NNVTRWFVTCVRQP 198
Cdd:pfam00043 80 PNLKAWFERVAARP 93
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
338-478 |
3.89e-13 |
|
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: 71.90 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 338 FMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAG-----IATQVVVEKKlwreqglsrhqlgrea 412
Cdd:cd00812 2 FYILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGlpaenAAIKIGRDPE---------------- 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530382523 413 flqevwKWKEEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSAAVTEAFVRLHEEGIIYRSTRLVNW 478
Cdd:cd00812 66 ------DWTEYNIKKMKEQLKRMGFSYDWRREFTTCDPEYYKFTQWLFLKLYEKGLAYKKEAPVNW 125
|
|
| Anticodon_Ia_Ile_BEm |
cd07960 |
Anticodon-binding domain of bacterial and eukaryotic mitochondrial isoleucyl tRNA synthetases; ... |
947-1103 |
1.14e-12 |
|
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: 67.55 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 947 YRhfcnKLWNATKFALRGLGkGFVPSPTSQPGGHESLVDRWIRSRLTEAVRLSNQGFQAYDFPAVTTAQYSFWLYELCDV 1026
Cdd:cd07960 13 YR----KIRNTFRFLLGNLN-DFDPAKDAVPYEELLELDRYALHRLNELIKEVREAYENYEFHKVYQALNNFCTVDLSAF 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530382523 1027 YLECLKPVL--NGVDQVAAECARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRMPQAPPSLcvTPYPEPSEcSWKDP 1103
Cdd:cd07960 88 YLDIIKDRLycDAKDSLERRSAQTVLYHILDALLKLLAPILPFTAEEVWEHLPGEKKEESVFL--EDWPELPE-EWKDE 163
|
|
| GstA |
COG0625 |
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; |
56-206 |
1.32e-11 |
|
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440390 [Multi-domain] Cd Length: 205 Bit Score: 65.30 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 56 RLPALEqgPGGLWVWGATAVAQLLwpAGLGG-----PGGSRAAVLVQQWVSYADTELIPAAcGATLPALGLRSSAQDPQA 130
Cdd:COG0625 52 KVPVLV--DDGLVLTESLAILEYL--AERYPeppllPADPAARARVRQWLAWADGDLHPAL-RNLLERLAPEKDPAAIAR 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530382523 131 VLGALGRALSPLEEWLRLHTYLAGEAPTLADLAAVTALLLPFRYVLDPPARRiwnNVTRWFVTCVRQPEFRAVLGE 206
Cdd:COG0625 127 ARAELARLLAVLEARLAGGPYLAGDRFSIADIALAPVLRRLDRLGLDLADYP---NLAAWLARLAARPAFQRALAA 199
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
800-1076 |
5.53e-11 |
|
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439913 [Multi-domain] Cd Length: 544 Bit Score: 66.68 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 800 SILGWP---NQSEDLSVFYPGTLLETGH----DILFF----WVArMVM-LGLKLTGRLPfrevylhaivrdAH------G 861
Cdd:COG0143 259 ATKGYAddrGLPEDFEKYWPAPDTELVHfigkDIIRFhaiiWPA-MLMaAGLPLPKKVF------------AHgfltveG 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 862 RKMSKSLGNVIDPLDVIygislqglhnqllnsnldpsevekakegqkADFPAgipecgtDALRFGLCAYMSQGRDINLD- 940
Cdd:COG0143 326 EKMSKSRGNVIDPDDLL------------------------------DRYGP-------DALRYYLLREVPFGQDGDFSw 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 941 ------------------VNRILGyrhFCNKLWNatkfalrglgkGFVPSPtsqpgGHESLVDRWIRSRLTEAVRLSNQG 1002
Cdd:COG0143 369 edfvarvnsdlandlgnlASRTLS---MIHKYFD-----------GKVPEP-----GELTEADEELLAEAEAALEEVAEA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 1003 FQAYDFPAVTTAqysfwLYELCDV---YLECLKP-VLngVDQVAAECARQTLYTCLDVgLR----LLSPFMPFVTEELFQ 1074
Cdd:COG0143 430 MEAFEFRKALEE-----IMALARAankYIDETAPwKL--AKDEDPERLATVLYTLLEA-LRilaiLLKPFLPETAEKILE 501
|
..
gi 530382523 1075 RL 1076
Cdd:COG0143 502 QL 503
|
|
| tRNA-synt_1_2 |
pfam13603 |
Leucyl-tRNA synthetase, Domain 2; This is a family of the conserved region of Leucine-tRNA ... |
514-641 |
3.28e-10 |
|
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: 60.64 E-value: 3.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 514 GVLVSFAYKvqgsDSDEEVVVATTRIETMLGD--VAVAV-HP-------KD-------TRYQHLK--------------- 561
Cdd:pfam13603 9 GAEITFPVE----GTDEKIEVFTTRPDTLMGVtfVALAPeHPlveklaeKNpevaafiEECKNTSeiertsetkekegvf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 562 -GKNVIHPFLSRSLPIVFDEFVDMDFGTGAVKITPAHDQNDYEVGQRHGL------------EAISIMDS----RGALIN 624
Cdd:pfam13603 85 tGLYAIHPITGEKIPIWIANFVLMEYGTGAVMAVPAHDQRDFEFAKKYNLpikpviqpedgdLDLDIMTEayteEGILVN 164
|
170
....*....|....*..
gi 530382523 625 vPPPFLGLPRFEARKAV 641
Cdd:pfam13603 165 -SGEFDGLDSEEAKEAI 180
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
799-881 |
4.76e-08 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 57.50 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 799 LSILGWPNQSEDLS-VFYPGTLLETGHDIL-F---FWVARMVMLGLKLtgrlpFREVYLHA-IVRDahGRKMSKSLGNVI 872
Cdd:PRK12267 236 ITALGYGSDDDELFkKFWPADVHLVGKDILrFhaiYWPIMLMALGLPL-----PKKVFAHGwWLMK--DGKMSKSKGNVV 308
|
90
....*....|.
gi 530382523 873 DPLDVI--YGI 881
Cdd:PRK12267 309 DPEELVdrYGL 319
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
779-1076 |
5.67e-08 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 56.81 E-value: 5.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 779 ISLQQDED-VLDTWFSSGLFPLSILGWPNQSEDLSV----FYPGTLLETGHDILFF----WVARMVMLGLKLTGRlpfre 849
Cdd:PRK11893 212 IPVPGDPKhVIYVWFDALTNYLTALGYPDDEELLAElfnkYWPADVHLIGKDILRFhavyWPAFLMAAGLPLPKR----- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 850 VYLHA-IVRDahGRKMSKSLGNVIDPLDVIYgislqglhnqllnsnldpsevekakegqkadfpagipECGTDALRFGLC 928
Cdd:PRK11893 287 VFAHGfLTLD--GEKMSKSLGNVIDPFDLVD-------------------------------------EYGVDAVRYFLL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 929 AYMSQGRDINLDVNRILGYR--HFCNKLWN---ATKFALRGLGKGFVPSPTSqpgghESLVDRWIRSRLTEAVRLSNQGF 1003
Cdd:PRK11893 328 REIPFGQDGDFSREAFINRInaDLANDLGNlaqRTLSMIAKNFDGKVPEPGA-----LTEADEALLEAAAALLERVRAAM 402
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530382523 1004 QAYDFpavTTAQYSFW-LYELCDVYLECLKP-VLNGVDQvaaECARQTLYTCLDvGLR----LLSPFMPFVTEELFQRL 1076
Cdd:PRK11893 403 DNLAF---DKALEAILaLVRAANKYIDEQAPwSLAKTDP---ERLATVLYTLLE-VLRgiavLLQPVMPELAAKILDQL 474
|
|
| Anticodon_Ia_like |
cd07375 |
Anticodon-binding domain of class Ia aminoacyl tRNA synthetases and similar domains; This ... |
942-1065 |
3.07e-07 |
|
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: 50.20 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 942 NRILGYRHFCNKLWNATKFALRGLGKGFVPSPTSQPGGheslVDRWIRSRLTEAVRLSNQGFQAYDFPAVTTAQYSFWLY 1021
Cdd:cd07375 2 ERLKQARAFLNRLYRLLSFFRKALGGTQPKWDNELLEE----ADRELLARLQEFIKRTTNALEALDPTTAVQELFKFTNE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 530382523 1022 ElcDVYLECLKPVLNgvDQVAAECARQTLYTCLDVGLRLLSPFM 1065
Cdd:cd07375 78 L--NWYLDELKPALQ--TEELREAVLAVLRAALVVLTKLLAPFT 117
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
345-470 |
4.85e-07 |
|
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: 53.30 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 345 PNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEkklwrEQGLSRHQLGRE--AFLQEVWKWke 422
Cdd:cd00814 9 PYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAE-----EEGVTPQELCDKyhEIFKDLFKW-- 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 530382523 423 ekgdriyhqlkkLGssLDWDRACFTMDPKLSAAVTEAFVRLHEEGIIY 470
Cdd:cd00814 82 ------------LN--ISFDYFIRTTSPRHKEIVQEFFKKLYENGYIY 115
|
|
| GST_C_family |
cd00299 |
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ... |
96-191 |
4.89e-07 |
|
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: 49.03 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 96 VQQWVSYADTELIPAACGATLPALGLRSSAQDPQ-AVLGALGRALSPLEEWLRLHTYLAGEAPTLADLAAVTALLLPFRY 174
Cdd:cd00299 1 VRALEDWADATLAPPLVRLLYLEKVPLPKDEAAVeAAREELPALLAALEQLLAGRPYLAGDQFSLADVALAPVLARLEAL 80
|
90
....*....|....*..
gi 530382523 175 VLDPPARRIWNNVTRWF 191
Cdd:cd00299 81 GPYYDLLDEYPRLKAWY 97
|
|
| Anticodon_Ia_Leu_AEc |
cd07959 |
Anticodon-binding domain of archaeal and eukaryotic cytoplasmic leucyl tRNA synthetases; This ... |
977-1076 |
5.68e-07 |
|
Anticodon-binding domain of archaeal and eukaryotic cytoplasmic leucyl tRNA synthetases; This domain is found in leucyl tRNA synthetases (LeuRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain. In contrast to other class Ia enzymes, the anticodon is not used as an identity element in LeuRS (with exceptions such as Saccharomyces cerevisiae and some other eukaryotes). No anticodon-binding site can be defined for this family, which includes archaeal and eukaryotic cytoplasmic members. LeuRS catalyzes the transfer of leucine to the 3'-end of its tRNA.
Pssm-ID: 153413 [Multi-domain] Cd Length: 117 Bit Score: 49.51 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 977 PGGHESLVDRWIRSRLTEAVRLSNQGFQAYDF-PAVTTAQYSFwlYELCDVYLEclkpvlngvdQVAAECARQTLYTCLD 1055
Cdd:cd07959 29 ELEELTFIDRWLLSRLNRLIKETTEAYENMQFrEALKEGLYEL--QNDLDWYRE----------RGGAGMNKDLLRRFIE 96
|
90 100
....*....|....*....|.
gi 530382523 1056 VGLRLLSPFMPFVTEELFQRL 1076
Cdd:cd07959 97 VWTRLLAPFAPHLAEEIWHEL 117
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
342-470 |
7.29e-07 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 53.35 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 342 IPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCD-HagiatQVVVEKKLwREQGLSRHQLGRE---AFlQEV 417
Cdd:PRK11893 7 TPIYYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFFLTGTDeH-----GQKIQRKA-EEAGISPQELADRnsaAF-KRL 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 530382523 418 WkwkeekgdriyhqlKKLGSSLDwdraCF--TMDPKLSAAVTEAFVRLHEEGIIY 470
Cdd:PRK11893 80 W--------------EALNISYD----DFirTTDPRHKEAVQEIFQRLLANGDIY 116
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
345-473 |
1.34e-06 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 52.29 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 345 PNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKklwreQGLSRHQLGreaflqevwkwkEEK 424
Cdd:pfam09334 8 PYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEK-----EGITPEELV------------DRY 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 530382523 425 GDRIYHQLKKLGSSLD-WDRacfTMDPKLSAAVTEAFVRLHEEGIIYRST 473
Cdd:pfam09334 71 HEIHREDFKKFNISFDdYGR---TTSERHHELVQEFFLKLYENGYIYEKE 117
|
|
| GST_C_AaRS_like |
cd10289 |
Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA ... |
93-191 |
3.35e-06 |
|
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: 46.15 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 93 AVLVQQWVSYADTELipaacgatlpaLGLRSSAQdpqavlgalgraLSPLEEWLRLHTYLAGEAPTLADLaAVTALLLPF 172
Cdd:cd10289 2 AAQVDQWLDLAGSLL-----------KGKELEAL------------LKSLNSYLASRTFLVGYSLTLADV-AVFSALYPS 57
|
90
....*....|....*....
gi 530382523 173 RYVLDPPARRIWNNVTRWF 191
Cdd:cd10289 58 GQKLSDKEKKKFPHVTRWF 76
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
555-880 |
4.44e-06 |
|
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: 50.32 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 555 TRYQHLKGKNVIHPFlsrslpiVFDEFvdmdfGTGAVKITPAHDQNDYEVGQRHGLEAISIMDSRGALINVPPPF-LGLP 633
Cdd:cd00812 30 ARYKRMQGYNVLFPM-------GFDAF-----GLPAENAAIKIGRDPEDWTEYNIKKMKEQLKRMGFSYDWRREFtTCDP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 634 RFEARKAVL-VALKERGLfrgIEDNPMVVPLCnRSKDvvepllrpQWYVRCGEMAQAASAAVTRGDLRILPEAHQRTWHA 712
Cdd:cd00812 98 EYYKFTQWLfLKLYEKGL---AYKKEAPVNWC-KLLD--------QWFLKYSETEWKEKLLKDLEKLDGWPEEVRAMQEN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 713 WMDnirewcISRQLWWGHRIPAYFV--TVSDPAVPPGedpdgRYWVSGRNEaearekaakefgvSPDKISLQQDedvldt 790
Cdd:cd00812 166 WIG------CSRQRYWGTPIPWTDTmeSLSDSTWYYA-----RYTDAHNLE-------------QPYEGDLEFD------ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 791 wfssglfplsilgwpnqSEDLSVFYPGTLLETGHD-----ILF--FWVArmVMLGLKLTGRLPFREVYLHAIVRdAHGRK 863
Cdd:cd00812 216 -----------------REEFEYWYPVDIYIGGKEhapnhLLYsrFNHK--ALFDEGLVTDEPPKGLIVQGMVL-LEGEK 275
|
330
....*....|....*....
gi 530382523 864 MSKSLGNVIDPLDVI--YG 880
Cdd:cd00812 276 MSKSKGNVVTPDEAIkkYG 294
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
347-429 |
3.25e-05 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 48.26 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 347 VTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCD-H----------AGIATQVVVE------KKLWREQGLS----- 404
Cdd:PRK12267 15 PNGKPHIGHAYTTIAADALARYKRLQGYDVFFLTGTDeHgqkiqqaaekAGKTPQEYVDeisagfKELWKKLDISydkfi 94
|
90 100 110
....*....|....*....|....*....|
gi 530382523 405 -----RHQLGREAFLQEVWkwkeEKGDrIY 429
Cdd:PRK12267 95 rttdeRHKKVVQKIFEKLY----EQGD-IY 119
|
|
| GST_C_AIMP3 |
cd10305 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ... |
95-201 |
1.06e-04 |
|
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: 42.66 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 95 LVQQWVSYADTELIPAACGATLPALglrssaqdpqavlgalgraLSPLEEWLRLHTYLAGEAPTLADlAAVTALLLPFRY 174
Cdd:cd10305 6 QVDQWLEYRVTQVAPASDKADAKSL-------------------LKELNSYLQDRTYLVGHKLTLAD-VVLYYGLHPIMK 65
|
90 100
....*....|....*....|....*..
gi 530382523 175 VLDPPARRIWNNVTRWFVTCVRQPEFR 201
Cdd:cd10305 66 DLSPQEKEQYLNVSRWFDHVQHLPGIR 92
|
|
| GST_C_7 |
cd03206 |
C-terminal, alpha helical domain of an unknown subfamily 7 of Glutathione S-transferases; ... |
96-184 |
1.68e-04 |
|
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: 41.83 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 96 VQQWVSYADTELIPAACGATLpaLGLRSSAQDPQAVLGALGRALSPLEEWLRLHTYLAGEAPTLADLAAvtalllpFRYV 175
Cdd:cd03206 1 VQRWLSFAAGEIAHGPAAARL--IHLFGAPLDPERARAISHRLLRLLDQHLAGRDWLAGDRPTIADVAC-------YPYI 71
|
90
....*....|....*....
gi 530382523 176 ---------LDP-PARRIW 184
Cdd:cd03206 72 alapeggvsLEPyPAIRAW 90
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
338-472 |
2.09e-04 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 45.48 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 338 FMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAG--IATQVVVEkklwreqglsrhqlGREAflq 415
Cdd:PLN02224 71 FVLTTPLYYVNAPPHMGSAYTTIAADSIARFQRLLGKKVIFITGTDEHGekIATSAAAN--------------GRNP--- 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 530382523 416 evwkwkEEKGDRIYHQLKKLGSSLD--WDRACFTMDPKLSAAVTEAFVRLHEEGIIYRS 472
Cdd:PLN02224 134 ------PEHCDIISQSYRTLWKDLDiaYDKFIRTTDPKHEAIVKEFYARVFANGDIYRA 186
|
|
| GST_C_Delta_Epsilon |
cd03177 |
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; ... |
121-198 |
3.50e-04 |
|
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: 41.36 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 121 LRSSAQDPQAVLGALGRALSPLEEWLRLHTYLAGEAPTLADLAAVTAL----LLPFryvldPPARriWNNVTRWFVTCVR 196
Cdd:cd03177 29 LFGGAEPPEEKLDKLEEALEFLETFLEGSDYVAGDQLTIADLSLVATVstleVVGF-----DLSK--YPNVAAWYERLKA 101
|
..
gi 530382523 197 QP 198
Cdd:cd03177 102 LP 103
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
784-878 |
6.28e-04 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 43.93 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382523 784 DEDVLDTWFSSGLFPLSILGWPNQSEDL----SVFYPGTLLETGHDILFF----WVARMVMLGLKLTgrlpfREVYLHAI 855
Cdd:PLN02224 285 DKQTIYVWFDALLGYISALTEDNKQQNLetavSFGWPASLHLIGKDILRFhavyWPAMLMSAGLELP-----KMVFGHGF 359
|
90 100
....*....|....*....|...
gi 530382523 856 VrDAHGRKMSKSLGNVIDPLDVI 878
Cdd:PLN02224 360 L-TKDGMKMGKSLGNTLEPFELV 381
|
|
| GST_C_5 |
cd03196 |
C-terminal, alpha helical domain of an unknown subfamily 5 of Glutathione S-transferases; ... |
139-203 |
6.45e-04 |
|
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: 40.60 E-value: 6.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530382523 139 LSPLEEWLRLHTYLAGEAPTLADLAavtalLLPF----------RYVLDPparriWNNVTRWFVTCVRQPEFRAV 203
Cdd:cd03196 50 LAELEARLSQHAYLFGDRPSLADYA-----IFPFvrqfahvdrdWFDASP-----YPNLRRWLNRFLQSPLFSKI 114
|
|
| Val_tRNA-synt_C |
pfam10458 |
Valyl tRNA synthetase tRNA binding arm; This domain is found at the C-terminus of Valyl tRNA ... |
1197-1259 |
8.47e-04 |
|
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: 38.79 E-value: 8.47e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530382523 1197 DPARELGKLQAKRVEAQRQAQRLRERRAASGYPVKVPLEVQEADEAKLQQTEAELRKVDEAIA 1259
Cdd:pfam10458 1 DVEKERARLEKELAKLQKEIERVQGKLANPGFVAKAPAEVVEEEKAKLAELEEQAEKLRERLS 63
|
|
| GST_C_GluProRS_N |
cd10309 |
Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional ... |
137-191 |
2.88e-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: 2.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 530382523 137 RALSPLEEWLRLHTYLAGEAPTLADLAAVTALllpFRYVLDPPARRIWNNVTRWF 191
Cdd:cd10309 24 SALSYLDKALSLRTYLVGNSLTLADFAVWAAL---RGNGEWLASKEKYVNVTRWF 75
|
|
| |
