|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
91-827 |
0e+00 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 830.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 91 ASKGRRVQPQWSPPA--GTEPCRLRLYNSLTRNKDVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRDYF 168
Cdd:PTZ00399 17 GQVSKSRLPEWKKPSkeGKYLTGLKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEDYF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 169 QYDVFYCMNITDIDDKIIRRARQNYLfeqyreqkppatqllkdvrdamkpfsvklsettdpdkrqmleriqnsvklatep 248
Cdd:PTZ00399 97 GYDVFYVMNITDIDDKIIKRAREEKL------------------------------------------------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 249 leqavrsslsgeevdskvqvlleeakdllsdwldstggsevtdnSIFSKLPKFWEEEFHKDMEALNVLPPDVLTRVSEYV 328
Cdd:PTZ00399 123 --------------------------------------------SIFLELARKWEKEFFEDMKALNVRPPDVITRVSEYV 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 329 PEIVNFVQKIVDNGYGYASNGSVYFDTAKFAASeKHSYGKLVPEAVGDQKALQEGEGDLSISAdrlSEKRSPNDFALWKA 408
Cdd:PTZ00399 159 PEIVDFIQKIIDNGFAYESNGSVYFDVEAFRKA-GHVYPKLEPESVADEDRIAEGEGALGKVS---GEKRSPNDFALWKA 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 409 SKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDCWVRYFLHTGHLTIAGC 488
Cdd:PTZ00399 235 SKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKGL 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 489 KMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSSNTMESALQYEKFMNEFFLNVKDILRAPVdiTGQFEKWEA 568
Cdd:PTZ00399 315 KMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSDESMDEAIEKDKVFFNFFANVKIKLRESE--LTSPQKWTQ 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 569 EEVELNKNFYGKKTAVHEALCDNIDTRTVMEEMRALVSQCNLYMAARKaerrRPNRALLENIAMYLTHMLKIFGAIEEes 648
Cdd:PTZ00399 393 HDFELNELFEETKSAVHAALLDNFDTPEALQALQKLISATNTYLNSGE----QPSAPLLRSVAQYVTKILSIFGLVEG-- 466
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 649 plGFPVGGPGTNlNLESTVMPYLQVLSEFREGVRKIAR--------EKKVLEVLQLSDALRDDILPELGVRFEDHEGLPT 720
Cdd:PTZ00399 467 --SDGLGSQGQN-STSENFKPLLEALLRFRDEVRDAAKaemklislDKKKKQLLQLCDKLRDEWLPNLGIRIEDKPDGPS 543
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 721 VVKLVDRDTLLKEKEGKKRAEEEKRRKKEEAARKKQEQEAAKLAKMKIPPSEMFLSEVNKYSKFDENGLPTHDTEGKELS 800
Cdd:PTZ00399 544 VWKLDDKEELQREKEEKEALKEQKRLRKLKKQEEKKKKELEKLEKAKIPPAEFFKRQEDKYSAFDETGLPTHDADGEEIS 623
|
730 740
....*....|....*....|....*..
gi 148747198 801 KGQAKKLKKLFEAQEKLYKEYLQMLQN 827
Cdd:PTZ00399 624 KKERKKLSKEYDKQAKLHEEYLAKGGK 650
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
112-715 |
1.34e-162 |
|
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439985 [Multi-domain] Cd Length: 465 Bit Score: 480.75 E-value: 1.34e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 112 LRLYNSLTRNKDVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRdYFQYDVFYCMNITDIDDKIIRRARQ 191
Cdd:COG0215 2 LKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLR-YLGYKVTYVRNITDVDDKIIKRAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 192 NylfeqyreqkppatqllkdvrdamkpfsvklsettdpdkrqmleriqnsvklatepleqavrsslsGEEVdskvqvlle 271
Cdd:COG0215 81 E------------------------------------------------------------------GESI--------- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 272 eakdllsdwldstggSEVTDnsifsklpkFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYASNGSV 351
Cdd:COG0215 86 ---------------WELAE---------RYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEADGDV 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 352 YFDTAKFaasekHSYGKL---VPEAvgdqkaLQEGEgdlsiSADRLSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWH 428
Cdd:COG0215 142 YFDVRSF-----PDYGKLsgrNLDD------LRAGA-----RVEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWH 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 429 IECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDcWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHS 508
Cdd:COG0215 206 IECSAMSTKYLGETFDIHGGGIDLIFPHHENEIAQSEAATGKP-FARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKKYD 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 509 ARQLRLAFLMHSWKDTLDYSSNTMESALQ-YEKFMNeFFLNVKDILRAPVDITGQFEKWEAEevelnknfygkktaVHEA 587
Cdd:COG0215 285 PEVLRFFLLSAHYRSPLDFSEEALEEAEKaLERLYN-ALRRLEEALGAADSSAEEIEELREE--------------FIAA 349
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 588 LCDNIDTRTVMEEMRALVSQCNLYMAARKaerrrpNRALLENIAMYLTHMLKIFGaIEEESPLGFpvGGPGTNLNLESTV 667
Cdd:COG0215 350 MDDDFNTPEALAVLFELVREINKALDEGE------DKAALAALAALLRALGGVLG-LLLLEPEAW--QGAAEDELLDALI 420
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 148747198 668 MPYLQvlsefregVRKIAREKKVLEvlqLSDALRDDILpELGVRFEDH 715
Cdd:COG0215 421 EALIE--------ERAEARKAKDFA---RADRIRDELA-ALGIVLEDT 456
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
125-540 |
3.66e-141 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 419.08 E-value: 3.66e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 125 FIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRdYFQYDVFYCMNITDIDDKIIRRARQNYLFEQyreqkpp 204
Cdd:pfam01406 2 FVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQ-ALGYDVQFVQNFTDIDDKIIKRARQEGESFR------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 205 atqllkdvrdamkpfsvklsettdpdkrqmleriqnsvklatepleqavrsslsgeevdskvqvlleeakdllsdwldst 284
Cdd:pfam01406 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 285 ggsevtdnsifsKLPKFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGY-ASNGSVYFDTAKFaasek 363
Cdd:pfam01406 74 ------------QLAARFIEAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYvSDNGDVYFDVSSF----- 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 364 HSYGKLVPEAVGDQKALQEGEGDlsisadrlSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASM 443
Cdd:pfam01406 137 PDYGKLSGQNLEQLEAGARGEVS--------EGKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQI 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 444 DIHGGGFDLRFPHHDNELAQSEAYFENDcWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKD 523
Cdd:pfam01406 209 DIHGGGIDLAFPHHENEIAQSEAAFDKQ-LANYWLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRS 287
|
410
....*....|....*..
gi 148747198 524 TLDYSsntmESALQYEK 540
Cdd:pfam01406 288 PLDFS----EELLEQAK 300
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
112-714 |
4.91e-140 |
|
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not from all species. The enzyme from one archaeal species, Archaeoglobus fulgidus, is found but the equivalent enzymes from some other Archaea, including Methanococcus jannaschii, are not found, although biochemical evidence suggests that tRNA(Cys) in these species are charged directly with Cys rather than through a misacylation and correction pathway as for tRNA(Gln). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273076 [Multi-domain] Cd Length: 464 Bit Score: 422.56 E-value: 4.91e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 112 LRLYNSLTRNKDVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRdYFQYDVFYCMNITDIDDKIIRRARQ 191
Cdd:TIGR00435 1 LKLYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLR-YLGYKVQYVQNITDIDDKIIKRARE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 192 NYLFEQyreqkppatqllkdvrdamkpfsvklsettdpdkrqmleriqnsvklatepleqavrsslsgeevdskvqvlle 271
Cdd:TIGR00435 80 NGESVY-------------------------------------------------------------------------- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 272 eakdllsdwldstggsEVTDNSIfsklpkfweEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYAS-NGS 350
Cdd:TIGR00435 86 ----------------EVSERFI---------EAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSdNGD 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 351 VYFDTAKFaasekHSYGKLvpeAVGDQKALQEGEGDLSISAdrlseKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIE 430
Cdd:TIGR00435 141 VYFDVSKF-----KDYGKL---SKQDLDQLEAGARVDVDEA-----KRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIE 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 431 CSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFeNDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSAR 510
Cdd:TIGR00435 208 CSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQSEAAF-GKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKNYDPE 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 511 QLRLAFLMHSWKDTLDYSsntmESALQYEKFMNEFFLNVKDILRAPVDITGQFEKWEAEEVelnKNFYgkkTAVHEALCD 590
Cdd:TIGR00435 287 ILRYFLLSVHYRSPLDFS----EELLEAAKNALERLYKALRVLDTSLAYSGNQSLNKFPDE---KEFE---ARFVEAMDD 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 591 NIDTR---TVMEEMralVSQCNLYMAarkaerrrpNRALLENIAMYLTHMLKIFGAIEEESPLGFPVGGPGTNLNLESTV 667
Cdd:TIGR00435 357 DLNTAnalAVLFEL---AKSINLTFV---------SKADAALLIEHLIFLESRLGLLLGLPSKPVQAGSNDDLGEIEALI 424
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 148747198 668 MPylqvlsefregvRKIAREKKvleVLQLSDALRDDiLPELGVRFED 714
Cdd:TIGR00435 425 EE------------RSIARKEK---DFAKADEIRDE-LAKKGIVLED 455
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
113-528 |
2.51e-110 |
|
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) 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.
Pssm-ID: 173899 [Multi-domain] Cd Length: 213 Bit Score: 336.09 E-value: 2.51e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 113 RLYNSLTRNKDVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRDYFqYDVFYCMNITDIDDKIIRRARQN 192
Cdd:cd00672 1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLG-YKVRYVQNITDIDDKIIKRAREE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 193 YLFeqyreqkppatqllkdvrdamkpfsvklsettdpdkrqmleriqnsvklatepleqavrsslsgeevdskvqvllee 272
Cdd:cd00672 80 GLS----------------------------------------------------------------------------- 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 273 akdllsdwldstggsevtdnsiFSKLPKFWEEEFHKDMEALNVLPPDVLTRVseyvpeivnfvqkivdngygyasngsvy 352
Cdd:cd00672 83 ----------------------WKEVADYYTKEFFEDMKALNVLPPDVVPRV---------------------------- 112
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 353 fdtakfaasekhsygklvpeavgdqkalqegegdlsisadrlsekrspndfalwkaskpgepswpcpwgkgrpgWHIECS 432
Cdd:cd00672 113 --------------------------------------------------------------------------WHIECS 118
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 433 AMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFeNDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQL 512
Cdd:cd00672 119 AMAMKYLGETFDIHGGGVDLIFPHHENEIAQSEAAT-GKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVL 197
|
410
....*....|....*.
gi 148747198 513 RLAFLMHSWKDTLDYS 528
Cdd:cd00672 198 RLALLSSHYRSPLDFS 213
|
|
| GST_C_CysRS_N |
cd10310 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Cysteinyl-tRNA synthetase ... |
4-76 |
6.14e-34 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of Cysteinyl-tRNA synthetase from higher eukaryotes; Glutathione S-transferase (GST) C-terminal domain family, Cysteinyl-tRNA synthetase (CysRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of CysRS 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 CysRS 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. CysRSs from prokaryotes and lower eukaryotes do not appear to contain this GST_C-like domain.
Pssm-ID: 198343 Cd Length: 73 Bit Score: 124.23 E-value: 6.14e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148747198 4 SSAEQAADYRSILSISDEAARVQALDQHLSTRSYIQGYSLSQADVDVFRQLSAPPADsRLFHVARWFRHIEAL 76
Cdd:cd10310 2 SSGQAAFDYGFILSISEEAARAEALNEYLSTRSYLQGFGPSQADVEVFRLLSRPPAD-RLVHVLRWYRHIEAL 73
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
91-827 |
0e+00 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 830.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 91 ASKGRRVQPQWSPPA--GTEPCRLRLYNSLTRNKDVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRDYF 168
Cdd:PTZ00399 17 GQVSKSRLPEWKKPSkeGKYLTGLKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEDYF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 169 QYDVFYCMNITDIDDKIIRRARQNYLfeqyreqkppatqllkdvrdamkpfsvklsettdpdkrqmleriqnsvklatep 248
Cdd:PTZ00399 97 GYDVFYVMNITDIDDKIIKRAREEKL------------------------------------------------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 249 leqavrsslsgeevdskvqvlleeakdllsdwldstggsevtdnSIFSKLPKFWEEEFHKDMEALNVLPPDVLTRVSEYV 328
Cdd:PTZ00399 123 --------------------------------------------SIFLELARKWEKEFFEDMKALNVRPPDVITRVSEYV 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 329 PEIVNFVQKIVDNGYGYASNGSVYFDTAKFAASeKHSYGKLVPEAVGDQKALQEGEGDLSISAdrlSEKRSPNDFALWKA 408
Cdd:PTZ00399 159 PEIVDFIQKIIDNGFAYESNGSVYFDVEAFRKA-GHVYPKLEPESVADEDRIAEGEGALGKVS---GEKRSPNDFALWKA 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 409 SKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDCWVRYFLHTGHLTIAGC 488
Cdd:PTZ00399 235 SKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKGL 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 489 KMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSSNTMESALQYEKFMNEFFLNVKDILRAPVdiTGQFEKWEA 568
Cdd:PTZ00399 315 KMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSDESMDEAIEKDKVFFNFFANVKIKLRESE--LTSPQKWTQ 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 569 EEVELNKNFYGKKTAVHEALCDNIDTRTVMEEMRALVSQCNLYMAARKaerrRPNRALLENIAMYLTHMLKIFGAIEEes 648
Cdd:PTZ00399 393 HDFELNELFEETKSAVHAALLDNFDTPEALQALQKLISATNTYLNSGE----QPSAPLLRSVAQYVTKILSIFGLVEG-- 466
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 649 plGFPVGGPGTNlNLESTVMPYLQVLSEFREGVRKIAR--------EKKVLEVLQLSDALRDDILPELGVRFEDHEGLPT 720
Cdd:PTZ00399 467 --SDGLGSQGQN-STSENFKPLLEALLRFRDEVRDAAKaemklislDKKKKQLLQLCDKLRDEWLPNLGIRIEDKPDGPS 543
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 721 VVKLVDRDTLLKEKEGKKRAEEEKRRKKEEAARKKQEQEAAKLAKMKIPPSEMFLSEVNKYSKFDENGLPTHDTEGKELS 800
Cdd:PTZ00399 544 VWKLDDKEELQREKEEKEALKEQKRLRKLKKQEEKKKKELEKLEKAKIPPAEFFKRQEDKYSAFDETGLPTHDADGEEIS 623
|
730 740
....*....|....*....|....*..
gi 148747198 801 KGQAKKLKKLFEAQEKLYKEYLQMLQN 827
Cdd:PTZ00399 624 KKERKKLSKEYDKQAKLHEEYLAKGGK 650
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
112-715 |
1.34e-162 |
|
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439985 [Multi-domain] Cd Length: 465 Bit Score: 480.75 E-value: 1.34e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 112 LRLYNSLTRNKDVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRdYFQYDVFYCMNITDIDDKIIRRARQ 191
Cdd:COG0215 2 LKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLR-YLGYKVTYVRNITDVDDKIIKRAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 192 NylfeqyreqkppatqllkdvrdamkpfsvklsettdpdkrqmleriqnsvklatepleqavrsslsGEEVdskvqvlle 271
Cdd:COG0215 81 E------------------------------------------------------------------GESI--------- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 272 eakdllsdwldstggSEVTDnsifsklpkFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYASNGSV 351
Cdd:COG0215 86 ---------------WELAE---------RYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEADGDV 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 352 YFDTAKFaasekHSYGKL---VPEAvgdqkaLQEGEgdlsiSADRLSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWH 428
Cdd:COG0215 142 YFDVRSF-----PDYGKLsgrNLDD------LRAGA-----RVEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWH 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 429 IECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDcWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHS 508
Cdd:COG0215 206 IECSAMSTKYLGETFDIHGGGIDLIFPHHENEIAQSEAATGKP-FARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKKYD 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 509 ARQLRLAFLMHSWKDTLDYSSNTMESALQ-YEKFMNeFFLNVKDILRAPVDITGQFEKWEAEevelnknfygkktaVHEA 587
Cdd:COG0215 285 PEVLRFFLLSAHYRSPLDFSEEALEEAEKaLERLYN-ALRRLEEALGAADSSAEEIEELREE--------------FIAA 349
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 588 LCDNIDTRTVMEEMRALVSQCNLYMAARKaerrrpNRALLENIAMYLTHMLKIFGaIEEESPLGFpvGGPGTNLNLESTV 667
Cdd:COG0215 350 MDDDFNTPEALAVLFELVREINKALDEGE------DKAALAALAALLRALGGVLG-LLLLEPEAW--QGAAEDELLDALI 420
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 148747198 668 MPYLQvlsefregVRKIAREKKVLEvlqLSDALRDDILpELGVRFEDH 715
Cdd:COG0215 421 EALIE--------ERAEARKAKDFA---RADRIRDELA-ALGIVLEDT 456
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
125-540 |
3.66e-141 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 419.08 E-value: 3.66e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 125 FIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRdYFQYDVFYCMNITDIDDKIIRRARQNYLFEQyreqkpp 204
Cdd:pfam01406 2 FVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQ-ALGYDVQFVQNFTDIDDKIIKRARQEGESFR------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 205 atqllkdvrdamkpfsvklsettdpdkrqmleriqnsvklatepleqavrsslsgeevdskvqvlleeakdllsdwldst 284
Cdd:pfam01406 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 285 ggsevtdnsifsKLPKFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGY-ASNGSVYFDTAKFaasek 363
Cdd:pfam01406 74 ------------QLAARFIEAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYvSDNGDVYFDVSSF----- 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 364 HSYGKLVPEAVGDQKALQEGEGDlsisadrlSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASM 443
Cdd:pfam01406 137 PDYGKLSGQNLEQLEAGARGEVS--------EGKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQI 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 444 DIHGGGFDLRFPHHDNELAQSEAYFENDcWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKD 523
Cdd:pfam01406 209 DIHGGGIDLAFPHHENEIAQSEAAFDKQ-LANYWLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRS 287
|
410
....*....|....*..
gi 148747198 524 TLDYSsntmESALQYEK 540
Cdd:pfam01406 288 PLDFS----EELLEQAK 300
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
112-714 |
4.91e-140 |
|
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not from all species. The enzyme from one archaeal species, Archaeoglobus fulgidus, is found but the equivalent enzymes from some other Archaea, including Methanococcus jannaschii, are not found, although biochemical evidence suggests that tRNA(Cys) in these species are charged directly with Cys rather than through a misacylation and correction pathway as for tRNA(Gln). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273076 [Multi-domain] Cd Length: 464 Bit Score: 422.56 E-value: 4.91e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 112 LRLYNSLTRNKDVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRdYFQYDVFYCMNITDIDDKIIRRARQ 191
Cdd:TIGR00435 1 LKLYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLR-YLGYKVQYVQNITDIDDKIIKRARE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 192 NYLFEQyreqkppatqllkdvrdamkpfsvklsettdpdkrqmleriqnsvklatepleqavrsslsgeevdskvqvlle 271
Cdd:TIGR00435 80 NGESVY-------------------------------------------------------------------------- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 272 eakdllsdwldstggsEVTDNSIfsklpkfweEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYAS-NGS 350
Cdd:TIGR00435 86 ----------------EVSERFI---------EAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSdNGD 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 351 VYFDTAKFaasekHSYGKLvpeAVGDQKALQEGEGDLSISAdrlseKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIE 430
Cdd:TIGR00435 141 VYFDVSKF-----KDYGKL---SKQDLDQLEAGARVDVDEA-----KRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIE 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 431 CSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFeNDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSAR 510
Cdd:TIGR00435 208 CSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQSEAAF-GKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKNYDPE 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 511 QLRLAFLMHSWKDTLDYSsntmESALQYEKFMNEFFLNVKDILRAPVDITGQFEKWEAEEVelnKNFYgkkTAVHEALCD 590
Cdd:TIGR00435 287 ILRYFLLSVHYRSPLDFS----EELLEAAKNALERLYKALRVLDTSLAYSGNQSLNKFPDE---KEFE---ARFVEAMDD 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 591 NIDTR---TVMEEMralVSQCNLYMAarkaerrrpNRALLENIAMYLTHMLKIFGAIEEESPLGFPVGGPGTNLNLESTV 667
Cdd:TIGR00435 357 DLNTAnalAVLFEL---AKSINLTFV---------SKADAALLIEHLIFLESRLGLLLGLPSKPVQAGSNDDLGEIEALI 424
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 148747198 668 MPylqvlsefregvRKIAREKKvleVLQLSDALRDDiLPELGVRFED 714
Cdd:TIGR00435 425 EE------------RSIARKEK---DFAKADEIRDE-LAKKGIVLED 455
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
113-528 |
2.51e-110 |
|
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) 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.
Pssm-ID: 173899 [Multi-domain] Cd Length: 213 Bit Score: 336.09 E-value: 2.51e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 113 RLYNSLTRNKDVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRDYFqYDVFYCMNITDIDDKIIRRARQN 192
Cdd:cd00672 1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLG-YKVRYVQNITDIDDKIIKRAREE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 193 YLFeqyreqkppatqllkdvrdamkpfsvklsettdpdkrqmleriqnsvklatepleqavrsslsgeevdskvqvllee 272
Cdd:cd00672 80 GLS----------------------------------------------------------------------------- 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 273 akdllsdwldstggsevtdnsiFSKLPKFWEEEFHKDMEALNVLPPDVLTRVseyvpeivnfvqkivdngygyasngsvy 352
Cdd:cd00672 83 ----------------------WKEVADYYTKEFFEDMKALNVLPPDVVPRV---------------------------- 112
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 353 fdtakfaasekhsygklvpeavgdqkalqegegdlsisadrlsekrspndfalwkaskpgepswpcpwgkgrpgWHIECS 432
Cdd:cd00672 113 --------------------------------------------------------------------------WHIECS 118
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 433 AMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFeNDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQL 512
Cdd:cd00672 119 AMAMKYLGETFDIHGGGVDLIFPHHENEIAQSEAAT-GKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVL 197
|
410
....*....|....*.
gi 148747198 513 RLAFLMHSWKDTLDYS 528
Cdd:cd00672 198 RLALLSSHYRSPLDFS 213
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
54-535 |
1.50e-90 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 296.46 E-value: 1.50e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 54 LSAPPADSRLfhvarwfRHIEALLGGPQGRDEPCRLQASKGRRVQPQWSPpaGTEpcrLRLYNSLTRNKDVFIPQDGKKV 133
Cdd:PLN02946 14 RLSSPPRSQL-------RIAFPLRPPKERQYRSCFFSASALASNGAPASR--GRE---LHLYNTMSRKKELFKPKVEGKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 134 TWYCCGPTVYDASHMGHARSYISFDILRRVLRdYFQYDVFYCMNITDIDDKIIRRARQnylfeqyreqkppatqLLKDvr 213
Cdd:PLN02946 82 GMYVCGVTAYDLSHIGHARVYVTFDVLYRYLK-HLGYEVRYVRNFTDVDDKIIARANE----------------LGED-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 214 damkPFSvklsettdpdkrqmleriqnsvklatepleqavrsslsgeevdskvqvlleeakdllsdwldstggsevtdns 293
Cdd:PLN02946 143 ----PIS------------------------------------------------------------------------- 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 294 ifskLPKFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYASNGSVYFDTAKFAasekhSYGKLVPEA 373
Cdd:PLN02946 146 ----LSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVDGDVYFSVDKFP-----EYGKLSGRK 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 374 VGDQKAlqeGEgdlSISADrlSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLR 453
Cdd:PLN02946 217 LEDNRA---GE---RVAVD--SRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLV 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 454 FPHHDNELAQSEAYFEnDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSSNTME 533
Cdd:PLN02946 289 FPHHENEIAQSCAACC-DSNISYWIHNGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDVQLE 367
|
..
gi 148747198 534 SA 535
Cdd:PLN02946 368 SA 369
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
114-535 |
5.48e-67 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 236.15 E-value: 5.48e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 114 LYNSLTRNKDVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRDyFQYDVFYCMNITDIDDKIIRRARQNy 193
Cdd:PRK14535 230 IYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRE-CGYPLTYVRNITDIDDKIIARAAEN- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 194 lfeqyreqkppatqllkdvrdamkpfsvklsettdpdkrqmleriqnsvklatepleqavrsslsGEEVdskvqvlleea 273
Cdd:PRK14535 308 -----------------------------------------------------------------GETI----------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 274 kdllsdwldstggsevtdnsifSKLPKFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGY-ASNGSVY 352
Cdd:PRK14535 312 ----------------------GELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYpAANGDVY 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 353 FDTAKFAAsekhsYGKLVPEAVGDQKALQEGEGDlsisadrlSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECS 432
Cdd:PRK14535 370 YAVREFAA-----YGQLSGKSLDDLRAGERVEVD--------GFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECS 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 433 AMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDC---------------WVRYFLHTGHLTIAGCKMSKSLKNF 497
Cdd:PRK14535 437 AMSENLFGDTFDIHGGGADLQFPHHENEIAQSVGATGHTCghhhaqthhgqsiasHVKYWLHNGFIRVDGEKMSKSLGNF 516
|
410 420 430
....*....|....*....|....*....|....*...
gi 148747198 498 ITIKDALKKHSARQLRLAFLMHSWKDTLDYSSNTMESA 535
Cdd:PRK14535 517 FTIREVLKQYDPEVVRFFILRAHYRSPLNYSDAHLDDA 554
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
101-537 |
7.59e-64 |
|
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this protein family are MshC, l-cysteine:1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase, an enzyme that uses ATP to ligate a Cys residue to a mycothiol precursor molecule, in the second to last step in mycothiol biosynthesis. This enzyme shows considerable homology to Cys--tRNA ligases, and many instances are misannotated as such. Mycothiol is found in Mycobacterium tuberculosis, Corynebacterium glutamicum, Streptomyces coelicolor, and various other members of the Actinobacteria. Mycothiol is an analog to glutathione. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
Pssm-ID: 132488 [Multi-domain] Cd Length: 411 Bit Score: 219.98 E-value: 7.59e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 101 WSPPA-----GTEPcRLRLYNSLTRN-KDVfipQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRDYfQYDVFY 174
Cdd:TIGR03447 3 WPAPAvpalpGTGP-PLRLFDTADGQvRPV---EPGPEAGMYVCGITPYDATHLGHAATYLTFDLVNRVWRDA-GHRVHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 175 CMNITDIDDKIIRRArqnylfeqyreqkppatqllkdVRDAMkpfsvklsettdpdkrqmleriqnsvklatepleqavr 254
Cdd:TIGR03447 78 VQNVTDVDDPLFERA----------------------ERDGV-------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 255 sslsgeevdskvqvlleeakdllsDWLDsTGGSEVtdnsifsklpkfweEEFHKDMEALNVLPPDVLTRVSEYVPEIVNF 334
Cdd:TIGR03447 98 ------------------------DWRE-LGTSQI--------------DLFREDMEALRVLPPRDYIGAVESIDEVVEM 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 335 VQKIVDNGYGY----ASNGSVYFDTAkfaASEKHSYGKLVPEAVGDQKALQEGeGDlsisADRLSeKRSPNDFALWKASK 410
Cdd:TIGR03447 139 VEKLLASGAAYivegPEYPDVYFSID---ATEQFGYESGYDRATMLELFAERG-GD----PDRPG-KRDPLDALLWRAAR 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 411 PGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDCWVRYFLHTGHLTIAGCKM 490
Cdd:TIGR03447 210 EGEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSDLIFPHHEFSAAHAEAATGVRRMARHYVHAGMIGLDGEKM 289
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 148747198 491 SKSLKNFITIKDaLKK--HSARQLRLAFLMHSWKDTLDYSSNTMESALQ 537
Cdd:TIGR03447 290 SKSLGNLVFVSK-LRAagVDPAAIRLGLLAGHYRQDRDWTDAVLAEAEA 337
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
130-537 |
1.05e-61 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 213.25 E-value: 1.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 130 GKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRDYfQYDVFYCMNITDIDDKIIRRARqnylfeqyreqkppatqll 209
Cdd:PRK12418 7 GGTATMYVCGITPYDATHLGHAATYLAFDLVNRVWRDA-GHDVHYVQNVTDVDDPLLERAA------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 210 kdvRDamkpfsvklsettdpdkrqmleriqnsvklatepleqavrsslsGEevdskvqvlleeakdllsDWLDsTGGSEV 289
Cdd:PRK12418 67 ---RD--------------------------------------------GV------------------DWRD-LAEREI 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 290 tdnsifsklpkfweEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGY----ASNGSVYFDTAkfAAsekhs 365
Cdd:PRK12418 81 --------------ALFREDMEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYvvddEEYPDVYFSVD--AT----- 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 366 ygklvpEAVGDQKALQEGEGdLSISADRLSE-----KRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLG 440
Cdd:PRK12418 140 ------PQFGYESGYDRATM-LELFAERGGDpdrpgKRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLG 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 441 ASMDIHGGGFDLRFPHHDNELAQSEAYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKdALKK--HSARQLRLAFLM 518
Cdd:PRK12418 213 SGFDIQGGGSDLIFPHHEFSAAHAEAATGERRFARHYVHAGMIGLDGEKMSKSRGNLVFVS-RLRAagVDPAAIRLALLA 291
|
410
....*....|....*....
gi 148747198 519 HSWKDTLDYSSNTMESALQ 537
Cdd:PRK12418 292 GHYRADREWTDAVLAEAEA 310
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
112-610 |
1.22e-59 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 210.93 E-value: 1.22e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 112 LRLYNSLTRNKDVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRdYFQYDVFYCMNITDIddkiirrarq 191
Cdd:PRK14536 3 LRLYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTLH-FLGYRVTHVMNITDV---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 192 NYLfeqyreqkppatqllkdvrdamkpfsvklseTTDPDkrqmleriqnsvklatepleqavrsslSGEevDSKVQVLLE 271
Cdd:PRK14536 72 GHL-------------------------------TDDAD---------------------------SGE--DKMVKSAQE 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 272 EAKDLLsdwldstggsevtdnsifsKLPKFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYASNGSV 351
Cdd:PRK14536 92 HGKSVL-------------------EIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCAGGNV 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 352 YFDTAKFAasekhSYGKLVPEAVGDqkaLQEGEgdlSISADrlSEKRSPNDFALWKASKPGEP---SWPCPWGKGRPGWH 428
Cdd:PRK14536 153 YFDIRTFP-----SYGSLASAAVED---LQAGA---RIEHD--TNKRNPHDFVLWFTRSKFENhalTWDSPWGRGYPGWH 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 429 IECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAyFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKK-H 507
Cdd:PRK14536 220 IECSAMSMKYLGEQCDIHIGGVDHIRVHHTNEIAQCEA-ATGKPWVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQEKgF 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 508 SARQLRLAFLMHSWKDTLDYSSNTMESALQYEKFMNEFFLNVKDILRAPVDIT-GQFEKWEAEEVELNKNFYGKK--TAV 584
Cdd:PRK14536 299 QPLDYRFFLLGGHYRSQLAFSWEALKTAKAARRSLVRRVARVVDAARATTGSVrGTLAECAAERVAESRASESELllTDF 378
|
490 500
....*....|....*....|....*.
gi 148747198 585 HEALCDNIDTRTVMEEMRALVSQCNL 610
Cdd:PRK14536 379 RAALEDDFSTPKALSELQKLVKDTSV 404
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
112-535 |
3.14e-43 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 163.87 E-value: 3.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 112 LRLYNslTRNKDVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRdYFQYDVFYCMNITDIDdkiirrarq 191
Cdd:PRK14534 3 LKLYN--TKTKDLSELKNFSDVKVYACGPTVYNYAHIGNFRTYIFEDLLIKSLR-LLKYNVNYAMNITDIG--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 192 nylfeqyreqkppatQLLKDVRDAmkpfsvklsettdPDKrqmleriqnSVKLATEpleqavrSSLSGEEVDskvqvlle 271
Cdd:PRK14534 71 ---------------HLTGDFDDG-------------EDK---------VVKAARE-------RGLTVYEIS-------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 272 eakdllsdwldstggsevtdnsifsklpKFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYASNGSV 351
Cdd:PRK14534 99 ----------------------------RFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTYFVNGNV 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 352 YFDTAKFaasekHSYGKLVPEAVGDQKALQEGEGDLSISadrlseKRSPNDFALWKAS---KPGEPSWPCPWGKGRPGWH 428
Cdd:PRK14534 151 YFDTSCF-----KSYGQMAGINLNDFKDMSVSRVEIDKS------KRNKSDFVLWFTNskfKDQEMKWDSPWGFGYPSWH 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 429 IECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFeNDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKH- 507
Cdd:PRK14534 220 LECAAMNLEYFKSTLDIHLGGVDHIGVHHINEIAIAECYL-NKKWCDMFVHGEFLIMEYEKMSKSNNNFITIKDLEDQGf 298
|
410 420
....*....|....*....|....*...
gi 148747198 508 SARQLRLAFLMHSWKDTLDYSSNTMESA 535
Cdd:PRK14534 299 SPLDFRYFCLTAHYRTQLKFTFNNLKAC 326
|
|
| GST_C_CysRS_N |
cd10310 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Cysteinyl-tRNA synthetase ... |
4-76 |
6.14e-34 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of Cysteinyl-tRNA synthetase from higher eukaryotes; Glutathione S-transferase (GST) C-terminal domain family, Cysteinyl-tRNA synthetase (CysRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of CysRS 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 CysRS 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. CysRSs from prokaryotes and lower eukaryotes do not appear to contain this GST_C-like domain.
Pssm-ID: 198343 Cd Length: 73 Bit Score: 124.23 E-value: 6.14e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148747198 4 SSAEQAADYRSILSISDEAARVQALDQHLSTRSYIQGYSLSQADVDVFRQLSAPPADsRLFHVARWFRHIEAL 76
Cdd:cd10310 2 SSGQAAFDYGFILSISEEAARAEALNEYLSTRSYLQGFGPSQADVEVFRLLSRPPAD-RLVHVLRWYRHIEAL 73
|
|
| GST_C_eEF1b_like |
cd10308 |
Glutathione S-transferase C-terminal-like, alpha helical domain of eukaryotic translation ... |
4-76 |
1.07e-22 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of eukaryotic translation Elongation Factor 1 beta; Glutathione S-transferase (GST) C-terminal domain family, eukaryotic translation Elongation Factor 1 beta (eEF1b) subfamily; eEF1b is a component 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. eEF1b contains a GST_C-like alpha helical domain at the N-terminal region and a C-terminal guanine nucleotide exchange domain. The GST_C-like domain likely functions as a protein-protein interaction domain, similar to the function of the GST_C-like domains of EF1Bgamma and various aminoacyl-tRNA synthetases (aaRSs) from higher eukaryotes.
Pssm-ID: 198341 Cd Length: 82 Bit Score: 92.49 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 4 SSAEQAADYRSILSISD--------EAARVQALDQHLSTRSYIQGYSLSQADVDVFRQLSAPPADSRLFHVARWFRHIEA 75
Cdd:cd10308 2 ANLATESKHKLLLGVSLdgsfadlkTDKGLEALNEYLADRSYISGYSPSQADVEVFDKLKKAPDATKFPHLARWYRHIAS 81
|
.
gi 148747198 76 L 76
Cdd:cd10308 82 F 82
|
|
| GST_C_AaRS_like |
cd10289 |
Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA ... |
14-76 |
1.07e-09 |
|
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: 55.78 E-value: 1.07e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148747198 14 SILSISDEAARVQALDQHLSTRSYIQGYSLSQADVDVFRQLSAPPADSR------LFHVARWFRHIEAL 76
Cdd:cd10289 14 SLLKGKELEALLKSLNSYLASRTFLVGYSLTLADVAVFSALYPSGQKLSdkekkkFPHVTRWFNHIQNL 82
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
138-201 |
1.11e-07 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 51.71 E-value: 1.11e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148747198 138 CGPTVYDASHMGHARSYISFDILRRVLRDyFQYDVFYCMNITDIDDKIIRRARQNYL-FEQYREQ 201
Cdd:cd00802 4 SGITPNGYLHIGHLRTIVTFDFLAQAYRK-LGYKVRCIALIDDAGGLIGDPANKKGEnAKAFVER 67
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
466-631 |
1.46e-07 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 55.26 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 466 AYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLaFLMHS---WKDtLDYSSNTMESAL-QYEKF 541
Cdd:PRK12300 554 AIFPEEKWPRGIVVNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRL-YLTSSaelLQD-ADWREKEVESVRrQLERF 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 542 MnEFFLNVKDIlrAPVDITGQFEKWeaeeveLNKNFYGKKTAVHEALcDNIDTRTVMEEmrALVsqcNLYMAARKAERR- 620
Cdd:PRK12300 632 Y-ELAKELIEI--GGEEELRFIDKW------LLSRLNRIIKETTEAM-ESFQTRDAVQE--AFY---ELLNDLRWYLRRv 696
|
170
....*....|..
gi 148747198 621 -RPNRALLENIA 631
Cdd:PRK12300 697 gEANNKVLREVL 708
|
|
| GST_C_GluRS_N |
cd10306 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Glutamyl-tRNA synthetase; ... |
28-76 |
1.75e-07 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of Glutamyl-tRNA synthetase; Glutathione S-transferase (GST) C-terminal domain family, Glutamyl-tRNA synthetase (GluRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of GluRS from lower eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. The GST_C-like domain of GluRS is involved in protein-protein interactions. This domain mediates the formation of the MetRS-Arc1p-GluRS ternary complex found in lower eukaryotes, which is considered an evolutionary intermediate between prokaryotic aaRS and the multi-aaRS complex found in higher eukaryotes. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.
Pssm-ID: 198339 [Multi-domain] Cd Length: 87 Bit Score: 49.66 E-value: 1.75e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 148747198 28 LDQHLSTRSYIQGYSLSQADVDVFRQL-SAPPADS-----RLFHVARWFRHIEAL 76
Cdd:cd10306 33 LDSHLTLRTFIVGYSLSLADIAVWGALrGNGVAGSliknkVYVNLSRWFSFLESL 87
|
|
| GST_C_AIMP3 |
cd10305 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ... |
4-84 |
2.69e-06 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 3; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein (AIMP) 3 subfamily; AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex that functions as a molecular hub to coordinate protein synthesis. There are three AIMPs, named AIMP1-3, which play diverse regulatory roles. AIMP3, also called p18 or eukaryotic translation elongation factor 1 epsilon-1 (EEF1E1), contains a C-terminal domain with similarity to the C-terminal alpha helical domain of GSTs. It specifically interacts with methionyl-tRNA synthetase (MetRS) and is translocated to the nucleus during DNA synthesis or in response to DNA damage and oncogenic stress. In the nucleus, it interacts with ATM and ATR, which are upstream kinase regulators of p53. It appears to work against DNA damage in cooperation with AIMP2, and similar to AIMP2, AIMP3 is also a haploinsufficient tumor suppressor. AIMP3 transgenic mice have shorter lifespans than wild-type mice and they show characteristics of progeria, suggesting that AIMP3 may also be involved in cellular and organismal aging.
Pssm-ID: 198338 [Multi-domain] Cd Length: 101 Bit Score: 46.51 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 4 SSAEQAADYRSILsisdeaarvQALDQHLSTRSYIQGYSLSQADVDVFRQLSAPPADS------RLFHVARWFRHIEALL 77
Cdd:cd10305 19 APASDKADAKSLL---------KELNSYLQDRTYLVGHKLTLADVVLYYGLHPIMKDLspqekeQYLNVSRWFDHVQHLP 89
|
....*..
gi 148747198 78 GGPQGRD 84
Cdd:cd10305 90 GIRQHLP 96
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
450-536 |
1.26e-05 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 48.91 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 450 FDLRFPHHD---NELAQS----EAYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRlaFLMHSWK 522
Cdd:PLN02959 672 FDLRVSGKDliqNHLTFAiynhTAIWAEEHWPRGFRCNGHLMLNSEKMSKSTGNFLTLRQAIEEFSADATR--FALADAG 749
|
90
....*....|....*..
gi 148747198 523 DTLD---YSSNTMESAL 536
Cdd:PLN02959 750 DGVDdanFVFETANAAI 766
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
474-520 |
2.20e-04 |
|
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: 44.06 E-value: 2.20e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 148747198 474 VRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHS 520
Cdd:cd00814 265 PTRIVAHGYLTVEGKKMSKSRGNVVDPDDLLERYGADALRYYLLRER 311
|
|
| GST_C_GluProRS_N |
cd10309 |
Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional ... |
26-76 |
4.29e-04 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional Glutamyl-Prolyl-tRNA synthetase; Glutathione S-transferase (GST) C-terminal domain family, bifunctional GluRS-Prolyl-tRNA synthetase (GluProRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of GluProRS from higher eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. The GST_C-like domain of GluProRS may be involved in protein-protein interactions, mediating the formation of the multi-aaRS complex in higher eukaryotes. The multi-aaRS complex acts as a molecular hub for protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.
Pssm-ID: 198342 [Multi-domain] Cd Length: 81 Bit Score: 39.61 E-value: 4.29e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 148747198 26 QALDQHLSTRSYIQGYSLSQADVDVFRQLSA----PPADSRLFHVARWFRHIEAL 76
Cdd:cd10309 27 SYLDKALSLRTYLVGNSLTLADFAVWAALRGngewLASKEKYVNVTRWFKFISSQ 81
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
480-520 |
8.05e-04 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 42.66 E-value: 8.05e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 148747198 480 TGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHS 520
Cdd:pfam09334 315 HGYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARNR 355
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
426-494 |
1.34e-03 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 39.77 E-value: 1.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747198 426 GWHIECSAMAGTLLGASMDIHGGGFDLRFpHHDNELAQSEAYfeNDCWVRYFLHTGHLTIA-GCKMSKSL 494
Cdd:cd00802 77 EYMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKA--GGPARPFGLTFGRVMGAdGTKMSKSK 143
|
|
| GST_C_ValRS_N |
cd10294 |
Glutathione S-transferase C-terminal-like, alpha helical domain of vertebrate Valyl-tRNA ... |
27-70 |
4.11e-03 |
|
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: 37.89 E-value: 4.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 148747198 27 ALDQHLSTRSYIQGYSLSQADVDV-------FRQLSAPPADSRLFHVARWF 70
Cdd:cd10294 51 VLDCYLKLRTYLVGEAITLADIAVacalllpFKYVLDPARRESLLNVTRWF 101
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| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
140-192 |
8.08e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 39.48 E-value: 8.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 148747198 140 PTVYDASHMGHARSYISFDILRRVLRdyfQ--YDVFYcmnITDIDD---KIIRRARQN 192
Cdd:PRK11893 10 YYPNGKPHIGHAYTTLAADVLARFKR---LrgYDVFF---LTGTDEhgqKIQRKAEEA 61
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