|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
91-787 |
0e+00 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 783.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 91 ASKGRRVQPQWSPPA--GTQPCRLHLYNSLTRNKEVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLKDYF 168
Cdd:PTZ00399 17 GQVSKSRLPEWKKPSkeGKYLTGLKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEDYF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 169 KFDVFYCMNITDIDDKIIKRARQNHLfeqyrekrpeaaqlledvqaalkpfsvklnettdpdkkqmleriqhavqlatep 248
Cdd:PTZ00399 97 GYDVFYVMNITDIDDKIIKRAREEKL------------------------------------------------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 249 lekavqsrltgeevnscvevlleeakdllsdwldstlgcdvtdnSIFSKLPKFWEGDFHRDMEALNVLPPDVLTRVSEYV 328
Cdd:PTZ00399 123 --------------------------------------------SIFLELARKWEKEFFEDMKALNVRPPDVITRVSEYV 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 329 PEIVNFVQKIVDNGYGYVSNGSVYFDTAKFASSeKHSYGKLVPEAVGDQKALQEGEGDLSISAdrlSEKRSPNDFALWKA 408
Cdd:PTZ00399 159 PEIVDFIQKIIDNGFAYESNGSVYFDVEAFRKA-GHVYPKLEPESVADEDRIAEGEGALGKVS---GEKRSPNDFALWKA 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 409 SKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDCWVRYFLHTGHLTIAGC 488
Cdd:PTZ00399 235 SKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKGL 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 489 KMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSSNTMESALQYEKFLNEFFLNVKDILRAPVdiTGQFEKWGE 568
Cdd:PTZ00399 315 KMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSDESMDEAIEKDKVFFNFFANVKIKLRESE--LTSPQKWTQ 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 569 EEAELNKNFYDKKTAIHKALCDNVDTRTVMEEMRALVSQCNLYMAArkavRKRPNQALLENIALYLTHMLKIFGAVEEDS 648
Cdd:PTZ00399 393 HDFELNELFEETKSAVHAALLDNFDTPEALQALQKLISATNTYLNS----GEQPSAPLLRSVAQYVTKILSIFGLVEGSD 468
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 649 SLGFPVGGpgtslSLEATVMPYLQVLSEFREGVRKIAR--------EQKVPEILQLSDALRDNILPELGVRFEDHEGLPT 720
Cdd:PTZ00399 469 GLGSQGQN-----STSENFKPLLEALLRFRDEVRDAAKaemklislDKKKKQLLQLCDKLRDEWLPNLGIRIEDKPDGPS 543
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 303304987 721 VVKLVDRNTLLKEREEKRRVEEEKRKKKEEAARRKQEQEAAKLAKMKIPPSEMFLSETDKYSKFDEN 787
Cdd:PTZ00399 544 VWKLDDKEELQREKEEKEALKEQKRLRKLKKQEEKKKKELEKLEKAKIPPAEFFKRQEDKYSAFDET 610
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
112-715 |
2.57e-160 |
|
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: 473.82 E-value: 2.57e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 112 LHLYNSLTRNKEVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLKdYFKFDVFYCMNITDIDDKIIKRARQ 191
Cdd:COG0215 2 LKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLR-YLGYKVTYVRNITDVDDKIIKRAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 192 NhlfeqyrekrpeaaqlledvqaalkpfsvklnettdpdkkqmleriqhavqlateplekavqsrltGEEVNscvevlle 271
Cdd:COG0215 81 E------------------------------------------------------------------GESIW-------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 272 eakdllsdwldstlgcDVTDnsifsklpkFWEGDFHRDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYVSNGSV 351
Cdd:COG0215 87 ----------------ELAE---------RYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEADGDV 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 352 YFDTAKFassekHSYGKL---VPEAvgdqkaLQEGEgdlsiSADRLSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWH 428
Cdd:COG0215 142 YFDVRSF-----PDYGKLsgrNLDD------LRAGA-----RVEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWH 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 429 IECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDcWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHS 508
Cdd:COG0215 206 IECSAMSTKYLGETFDIHGGGIDLIFPHHENEIAQSEAATGKP-FARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKKYD 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 509 ARQLRLAFLMHSWKDTLDYSSNTMESALQ-YEKfLNEFFLNVKDILRAPVDITGQFEKWgeeeaelnknfydkKTAIHKA 587
Cdd:COG0215 285 PEVLRFFLLSAHYRSPLDFSEEALEEAEKaLER-LYNALRRLEEALGAADSSAEEIEEL--------------REEFIAA 349
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 588 LCDNVDTRTVMEEMRALVSQCNlymaarKAVRKRPNQALLENIALYLTHMLKIFGAVEEDSSLgfpVGGPGTSLSLEATV 667
Cdd:COG0215 350 MDDDFNTPEALAVLFELVREIN------KALDEGEDKAALAALAALLRALGGVLGLLLLEPEA---WQGAAEDELLDALI 420
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 303304987 668 MPYLQvlsefregVRKIAREQKvpeILQLSDALRDNILpELGVRFEDH 715
Cdd:COG0215 421 EALIE--------ERAEARKAK---DFARADRIRDELA-ALGIVLEDT 456
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
112-714 |
5.85e-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: 421.79 E-value: 5.85e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 112 LHLYNSLTRNKEVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLKdYFKFDVFYCMNITDIDDKIIKRARQ 191
Cdd:TIGR00435 1 LKLYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLR-YLGYKVQYVQNITDIDDKIIKRARE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 192 NhlfeqyrekrpeaaqlledvqaalkpfsvklnettdpdkkqmleriqhavqlateplekavqsrltGEEVNSCVEVLLE 271
Cdd:TIGR00435 80 N------------------------------------------------------------------GESVYEVSERFIE 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 272 EakdllsdwldstlgcdvtdnsifsklpkfwegdFHRDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYVS-NGS 350
Cdd:TIGR00435 94 A---------------------------------YFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSdNGD 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 351 VYFDTAKFassekHSYGKLvpeAVGDQKALQEGEGDLSISAdrlseKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIE 430
Cdd:TIGR00435 141 VYFDVSKF-----KDYGKL---SKQDLDQLEAGARVDVDEA-----KRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIE 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 431 CSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFeNDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSAR 510
Cdd:TIGR00435 208 CSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQSEAAF-GKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKNYDPE 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 511 QLRLAFLMHSWKDTLDYSsntmESALQYEKFLNEFFLNVKDILRApvDITGQFEkWGEEEAELNKNFYDkktAIHKALCD 590
Cdd:TIGR00435 287 ILRYFLLSVHYRSPLDFS----EELLEAAKNALERLYKALRVLDT--SLAYSGN-QSLNKFPDEKEFEA---RFVEAMDD 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 591 NVDTR---TVMEEMralVSQCNLYMAarkavrkrpNQALLENIALYLTHMLKIFGAVEEDSSLGFPVGGPGTSLSLEATV 667
Cdd:TIGR00435 357 DLNTAnalAVLFEL---AKSINLTFV---------SKADAALLIEHLIFLESRLGLLLGLPSKPVQAGSNDDLGEIEALI 424
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 303304987 668 MPylqvlsefregvRKIAREQKVpeiLQLSDALRDNiLPELGVRFED 714
Cdd:TIGR00435 425 EE------------RSIARKEKD---FAKADEIRDE-LAKKGIVLED 455
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
125-540 |
1.36e-138 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 411.76 E-value: 1.36e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 125 FIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLKdYFKFDVFYCMNITDIDDKIIKRARQNHLFEQyrekrpe 204
Cdd:pfam01406 2 FVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQ-ALGYDVQFVQNFTDIDDKIIKRARQEGESFR------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 205 aaqlledvqaalkpfsvklnettdpdkkqmleriqhavqlateplekavqsrltgeevnscvevlleeakdllsdwldst 284
Cdd:pfam01406 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 285 lgcdvtdnsifsKLPKFWEGDFHRDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYVS-NGSVYFDTAKFassek 363
Cdd:pfam01406 74 ------------QLAARFIEAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSdNGDVYFDVSSF----- 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 364 HSYGKLVPEAVGDQKALQEGEGDlsisadrlSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASM 443
Cdd:pfam01406 137 PDYGKLSGQNLEQLEAGARGEVS--------EGKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQI 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 444 DIHGGGFDLRFPHHDNELAQSEAYFENDcWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKD 523
Cdd:pfam01406 209 DIHGGGIDLAFPHHENEIAQSEAAFDKQ-LANYWLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRS 287
|
410
....*....|....*..
gi 303304987 524 TLDYSsntmESALQYEK 540
Cdd:pfam01406 288 PLDFS----EELLEQAK 300
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
113-528 |
1.54e-109 |
|
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: 333.39 E-value: 1.54e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 113 HLYNSLTRNKEVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLKDYFkFDVFYCMNITDIDDKIIKRARQN 192
Cdd:cd00672 1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLG-YKVRYVQNITDIDDKIIKRAREE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 193 HLFeqyrekrpeaaqlledvqaalkpfsvklnettdpdkkqmleriqhavqlateplekavqsrltgeevnscvevllee 272
Cdd:cd00672 80 GLS----------------------------------------------------------------------------- 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 273 akdllsdwldstlgcdvtdnsiFSKLPKFWEGDFHRDMEALNVLPPDVLTRVseyvpeivnfvqkivdngygyvsngsvy 352
Cdd:cd00672 83 ----------------------WKEVADYYTKEFFEDMKALNVLPPDVVPRV---------------------------- 112
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 353 fdtakfassekhsygklvpeavgdqkalqegegdlsisadrlsekrspndfalwkaskpgepswpcpwgkgrpgWHIECS 432
Cdd:cd00672 113 --------------------------------------------------------------------------WHIECS 118
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 433 AMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFeNDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQL 512
Cdd:cd00672 119 AMAMKYLGETFDIHGGGVDLIFPHHENEIAQSEAAT-GKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVL 197
|
410
....*....|....*.
gi 303304987 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 ... |
3-76 |
1.32e-36 |
|
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: 131.94 E-value: 1.32e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 303304987 3 DSSGQQAPDYRSILSISDEAARAQALNEHLSTRSYVQGYSLSQADVDAFRQLSAPPADPqLFHVARWFRHIEAL 76
Cdd:cd10310 1 ASSGQAAFDYGFILSISEEAARAEALNEYLSTRSYLQGFGPSQADVEVFRLLSRPPADR-LVHVLRWYRHIEAL 73
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
91-787 |
0e+00 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 783.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 91 ASKGRRVQPQWSPPA--GTQPCRLHLYNSLTRNKEVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLKDYF 168
Cdd:PTZ00399 17 GQVSKSRLPEWKKPSkeGKYLTGLKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEDYF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 169 KFDVFYCMNITDIDDKIIKRARQNHLfeqyrekrpeaaqlledvqaalkpfsvklnettdpdkkqmleriqhavqlatep 248
Cdd:PTZ00399 97 GYDVFYVMNITDIDDKIIKRAREEKL------------------------------------------------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 249 lekavqsrltgeevnscvevlleeakdllsdwldstlgcdvtdnSIFSKLPKFWEGDFHRDMEALNVLPPDVLTRVSEYV 328
Cdd:PTZ00399 123 --------------------------------------------SIFLELARKWEKEFFEDMKALNVRPPDVITRVSEYV 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 329 PEIVNFVQKIVDNGYGYVSNGSVYFDTAKFASSeKHSYGKLVPEAVGDQKALQEGEGDLSISAdrlSEKRSPNDFALWKA 408
Cdd:PTZ00399 159 PEIVDFIQKIIDNGFAYESNGSVYFDVEAFRKA-GHVYPKLEPESVADEDRIAEGEGALGKVS---GEKRSPNDFALWKA 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 409 SKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDCWVRYFLHTGHLTIAGC 488
Cdd:PTZ00399 235 SKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKGL 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 489 KMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSSNTMESALQYEKFLNEFFLNVKDILRAPVdiTGQFEKWGE 568
Cdd:PTZ00399 315 KMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSDESMDEAIEKDKVFFNFFANVKIKLRESE--LTSPQKWTQ 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 569 EEAELNKNFYDKKTAIHKALCDNVDTRTVMEEMRALVSQCNLYMAArkavRKRPNQALLENIALYLTHMLKIFGAVEEDS 648
Cdd:PTZ00399 393 HDFELNELFEETKSAVHAALLDNFDTPEALQALQKLISATNTYLNS----GEQPSAPLLRSVAQYVTKILSIFGLVEGSD 468
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 649 SLGFPVGGpgtslSLEATVMPYLQVLSEFREGVRKIAR--------EQKVPEILQLSDALRDNILPELGVRFEDHEGLPT 720
Cdd:PTZ00399 469 GLGSQGQN-----STSENFKPLLEALLRFRDEVRDAAKaemklislDKKKKQLLQLCDKLRDEWLPNLGIRIEDKPDGPS 543
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 303304987 721 VVKLVDRNTLLKEREEKRRVEEEKRKKKEEAARRKQEQEAAKLAKMKIPPSEMFLSETDKYSKFDEN 787
Cdd:PTZ00399 544 VWKLDDKEELQREKEEKEALKEQKRLRKLKKQEEKKKKELEKLEKAKIPPAEFFKRQEDKYSAFDET 610
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
112-715 |
2.57e-160 |
|
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: 473.82 E-value: 2.57e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 112 LHLYNSLTRNKEVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLKdYFKFDVFYCMNITDIDDKIIKRARQ 191
Cdd:COG0215 2 LKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLR-YLGYKVTYVRNITDVDDKIIKRAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 192 NhlfeqyrekrpeaaqlledvqaalkpfsvklnettdpdkkqmleriqhavqlateplekavqsrltGEEVNscvevlle 271
Cdd:COG0215 81 E------------------------------------------------------------------GESIW-------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 272 eakdllsdwldstlgcDVTDnsifsklpkFWEGDFHRDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYVSNGSV 351
Cdd:COG0215 87 ----------------ELAE---------RYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEADGDV 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 352 YFDTAKFassekHSYGKL---VPEAvgdqkaLQEGEgdlsiSADRLSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWH 428
Cdd:COG0215 142 YFDVRSF-----PDYGKLsgrNLDD------LRAGA-----RVEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWH 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 429 IECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDcWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHS 508
Cdd:COG0215 206 IECSAMSTKYLGETFDIHGGGIDLIFPHHENEIAQSEAATGKP-FARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKKYD 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 509 ARQLRLAFLMHSWKDTLDYSSNTMESALQ-YEKfLNEFFLNVKDILRAPVDITGQFEKWgeeeaelnknfydkKTAIHKA 587
Cdd:COG0215 285 PEVLRFFLLSAHYRSPLDFSEEALEEAEKaLER-LYNALRRLEEALGAADSSAEEIEEL--------------REEFIAA 349
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 588 LCDNVDTRTVMEEMRALVSQCNlymaarKAVRKRPNQALLENIALYLTHMLKIFGAVEEDSSLgfpVGGPGTSLSLEATV 667
Cdd:COG0215 350 MDDDFNTPEALAVLFELVREIN------KALDEGEDKAALAALAALLRALGGVLGLLLLEPEA---WQGAAEDELLDALI 420
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 303304987 668 MPYLQvlsefregVRKIAREQKvpeILQLSDALRDNILpELGVRFEDH 715
Cdd:COG0215 421 EALIE--------ERAEARKAK---DFARADRIRDELA-ALGIVLEDT 456
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
112-714 |
5.85e-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: 421.79 E-value: 5.85e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 112 LHLYNSLTRNKEVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLKdYFKFDVFYCMNITDIDDKIIKRARQ 191
Cdd:TIGR00435 1 LKLYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLR-YLGYKVQYVQNITDIDDKIIKRARE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 192 NhlfeqyrekrpeaaqlledvqaalkpfsvklnettdpdkkqmleriqhavqlateplekavqsrltGEEVNSCVEVLLE 271
Cdd:TIGR00435 80 N------------------------------------------------------------------GESVYEVSERFIE 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 272 EakdllsdwldstlgcdvtdnsifsklpkfwegdFHRDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYVS-NGS 350
Cdd:TIGR00435 94 A---------------------------------YFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSdNGD 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 351 VYFDTAKFassekHSYGKLvpeAVGDQKALQEGEGDLSISAdrlseKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIE 430
Cdd:TIGR00435 141 VYFDVSKF-----KDYGKL---SKQDLDQLEAGARVDVDEA-----KRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIE 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 431 CSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFeNDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSAR 510
Cdd:TIGR00435 208 CSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQSEAAF-GKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKNYDPE 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 511 QLRLAFLMHSWKDTLDYSsntmESALQYEKFLNEFFLNVKDILRApvDITGQFEkWGEEEAELNKNFYDkktAIHKALCD 590
Cdd:TIGR00435 287 ILRYFLLSVHYRSPLDFS----EELLEAAKNALERLYKALRVLDT--SLAYSGN-QSLNKFPDEKEFEA---RFVEAMDD 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 591 NVDTR---TVMEEMralVSQCNLYMAarkavrkrpNQALLENIALYLTHMLKIFGAVEEDSSLGFPVGGPGTSLSLEATV 667
Cdd:TIGR00435 357 DLNTAnalAVLFEL---AKSINLTFV---------SKADAALLIEHLIFLESRLGLLLGLPSKPVQAGSNDDLGEIEALI 424
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 303304987 668 MPylqvlsefregvRKIAREQKVpeiLQLSDALRDNiLPELGVRFED 714
Cdd:TIGR00435 425 EE------------RSIARKEKD---FAKADEIRDE-LAKKGIVLED 455
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
125-540 |
1.36e-138 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 411.76 E-value: 1.36e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 125 FIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLKdYFKFDVFYCMNITDIDDKIIKRARQNHLFEQyrekrpe 204
Cdd:pfam01406 2 FVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQ-ALGYDVQFVQNFTDIDDKIIKRARQEGESFR------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 205 aaqlledvqaalkpfsvklnettdpdkkqmleriqhavqlateplekavqsrltgeevnscvevlleeakdllsdwldst 284
Cdd:pfam01406 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 285 lgcdvtdnsifsKLPKFWEGDFHRDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYVS-NGSVYFDTAKFassek 363
Cdd:pfam01406 74 ------------QLAARFIEAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSdNGDVYFDVSSF----- 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 364 HSYGKLVPEAVGDQKALQEGEGDlsisadrlSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASM 443
Cdd:pfam01406 137 PDYGKLSGQNLEQLEAGARGEVS--------EGKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQI 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 444 DIHGGGFDLRFPHHDNELAQSEAYFENDcWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKD 523
Cdd:pfam01406 209 DIHGGGIDLAFPHHENEIAQSEAAFDKQ-LANYWLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRS 287
|
410
....*....|....*..
gi 303304987 524 TLDYSsntmESALQYEK 540
Cdd:pfam01406 288 PLDFS----EELLEQAK 300
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
113-528 |
1.54e-109 |
|
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: 333.39 E-value: 1.54e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 113 HLYNSLTRNKEVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLKDYFkFDVFYCMNITDIDDKIIKRARQN 192
Cdd:cd00672 1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLG-YKVRYVQNITDIDDKIIKRAREE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 193 HLFeqyrekrpeaaqlledvqaalkpfsvklnettdpdkkqmleriqhavqlateplekavqsrltgeevnscvevllee 272
Cdd:cd00672 80 GLS----------------------------------------------------------------------------- 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 273 akdllsdwldstlgcdvtdnsiFSKLPKFWEGDFHRDMEALNVLPPDVLTRVseyvpeivnfvqkivdngygyvsngsvy 352
Cdd:cd00672 83 ----------------------WKEVADYYTKEFFEDMKALNVLPPDVVPRV---------------------------- 112
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 353 fdtakfassekhsygklvpeavgdqkalqegegdlsisadrlsekrspndfalwkaskpgepswpcpwgkgrpgWHIECS 432
Cdd:cd00672 113 --------------------------------------------------------------------------WHIECS 118
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 433 AMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFeNDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQL 512
Cdd:cd00672 119 AMAMKYLGETFDIHGGGVDLIFPHHENEIAQSEAAT-GKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVL 197
|
410
....*....|....*.
gi 303304987 513 RLAFLMHSWKDTLDYS 528
Cdd:cd00672 198 RLALLSSHYRSPLDFS 213
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
112-535 |
1.34e-91 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 298.77 E-value: 1.34e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 112 LHLYNSLTRNKEVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLKdYFKFDVFYCMNITDIDDKIIKRARQ 191
Cdd:PLN02946 60 LHLYNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYLK-HLGYEVRYVRNFTDVDDKIIARANE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 192 nhlfeqyrekrpeaaqLLEDvqaalkPFSvklnettdpdkkqmleriqhavqlateplekavqsrltgeevnscvevlle 271
Cdd:PLN02946 139 ----------------LGED------PIS--------------------------------------------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 272 eakdllsdwldstlgcdvtdnsifskLPKFWEGDFHRDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYVSNGSV 351
Cdd:PLN02946 146 --------------------------LSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVDGDV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 352 YFDTAKFASsekhsYGKLVPEAVGDQKAlqeGEgdlSISADrlSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIEC 431
Cdd:PLN02946 200 YFSVDKFPE-----YGKLSGRKLEDNRA---GE---RVAVD--SRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIEC 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 432 SAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFEnDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQ 511
Cdd:PLN02946 267 SAMSAAYLGHSFDIHGGGMDLVFPHHENEIAQSCAACC-DSNISYWIHNGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLA 345
|
410 420
....*....|....*....|....
gi 303304987 512 LRLAFLMHSWKDTLDYSSNTMESA 535
Cdd:PLN02946 346 LRLFLLGTHYRSPINYSDVQLESA 369
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
114-535 |
1.55e-65 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 231.91 E-value: 1.55e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 114 LYNSLTRNKEVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLKDyFKFDVFYCMNITDIDDKIIKRARQNh 193
Cdd:PRK14535 230 IYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRE-CGYPLTYVRNITDIDDKIIARAAEN- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 194 lfeqyrekrpeaaqlledvqaalkpfsvklnettdpdkkqmleriqhavqlateplekavqsrltGEEVNSCVEVLLEEa 273
Cdd:PRK14535 308 -----------------------------------------------------------------GETIGELTARFIQA- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 274 kdllsdwldstlgcdvtdnsifsklpkfwegdFHRDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGY-VSNGSVY 352
Cdd:PRK14535 322 --------------------------------MHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYpAANGDVY 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 353 FDTAKFASsekhsYGKLVPEAVGDQKALQEGEGDlsisadrlSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECS 432
Cdd:PRK14535 370 YAVREFAA-----YGQLSGKSLDDLRAGERVEVD--------GFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECS 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 433 AMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDC---------------WVRYFLHTGHLTIAGCKMSKSLKNF 497
Cdd:PRK14535 437 AMSENLFGDTFDIHGGGADLQFPHHENEIAQSVGATGHTCghhhaqthhgqsiasHVKYWLHNGFIRVDGEKMSKSLGNF 516
|
410 420 430
....*....|....*....|....*....|....*...
gi 303304987 498 ITIKDALKKHSARQLRLAFLMHSWKDTLDYSSNTMESA 535
Cdd:PRK14535 517 FTIREVLKQYDPEVVRFFILRAHYRSPLNYSDAHLDDA 554
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
130-537 |
1.83e-60 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 209.40 E-value: 1.83e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 130 GKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLKDYfKFDVFYCMNITDIDDKIIKRARQnhlfeqyrekrpeaaqll 209
Cdd:PRK12418 7 GGTATMYVCGITPYDATHLGHAATYLAFDLVNRVWRDA-GHDVHYVQNVTDVDDPLLERAAR------------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 210 edvqaalkpfsvklnettdpdkkqmleriqhavqlateplekavqsrlTGEevnscvevlleeakdllsDWLDstLGCDV 289
Cdd:PRK12418 68 ------------------------------------------------DGV------------------DWRD--LAERE 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 290 TDnsifskLpkfwegdFHRDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYV----SNGSVYFDTAkfassekhs 365
Cdd:PRK12418 80 IA------L-------FREDMEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYVvddeEYPDVYFSVD--------- 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 366 ygklVPEAVGDQKALQEGEGdLSISADRLSE-----KRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLG 440
Cdd:PRK12418 138 ----ATPQFGYESGYDRATM-LELFAERGGDpdrpgKRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLG 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 441 ASMDIHGGGFDLRFPHHDNELAQSEAYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKdALKK--HSARQLRLAFLM 518
Cdd:PRK12418 213 SGFDIQGGGSDLIFPHHEFSAAHAEAATGERRFARHYVHAGMIGLDGEKMSKSRGNLVFVS-RLRAagVDPAAIRLALLA 291
|
410
....*....|....*....
gi 303304987 519 HSWKDTLDYSSNTMESALQ 537
Cdd:PRK12418 292 GHYRADREWTDAVLAEAEA 310
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
101-537 |
1.86e-60 |
|
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: 210.35 E-value: 1.86e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 101 WSPPA-----GTQPcRLHLYNSLTRNKEVFIPqdGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLKDYfKFDVFYC 175
Cdd:TIGR03447 3 WPAPAvpalpGTGP-PLRLFDTADGQVRPVEP--GPEAGMYVCGITPYDATHLGHAATYLTFDLVNRVWRDA-GHRVHYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 176 MNITDIDDKIIKRArqnhlfeqyrekrpeaaqlledvqaalkpfsvklnettdpdkkqmlERiqhavqlateplekavqs 255
Cdd:TIGR03447 79 QNVTDVDDPLFERA----------------------------------------------ER------------------ 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 256 rlTGEevnscvevlleeakdllsDWLDstLGCDVTDNsifsklpkfwegdFHRDMEALNVLPPDVLTRVSEYVPEIVNFV 335
Cdd:TIGR03447 95 --DGV------------------DWRE--LGTSQIDL-------------FREDMEALRVLPPRDYIGAVESIDEVVEMV 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 336 QKIVDNGYGYV----SNGSVYFDTAkfaSSEKHSYGKLVPEAVGDQKALQEGeGDlsisADRLSeKRSPNDFALWKASKP 411
Cdd:TIGR03447 140 EKLLASGAAYIvegpEYPDVYFSID---ATEQFGYESGYDRATMLELFAERG-GD----PDRPG-KRDPLDALLWRAARE 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 412 GEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDCWVRYFLHTGHLTIAGCKMS 491
Cdd:TIGR03447 211 GEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSDLIFPHHEFSAAHAEAATGVRRMARHYVHAGMIGLDGEKMS 290
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 303304987 492 KSLKNFITIKDaLKK--HSARQLRLAFLMHSWKDTLDYSSNTMESALQ 537
Cdd:TIGR03447 291 KSLGNLVFVSK-LRAagVDPAAIRLGLLAGHYRQDRDWTDAVLAEAEA 337
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
112-649 |
3.56e-60 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 212.09 E-value: 3.56e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 112 LHLYNSLTRNKEVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLKdYFKFDVFYCMNITDIddkiikrarq 191
Cdd:PRK14536 3 LRLYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTLH-FLGYRVTHVMNITDV---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 192 NHLfeqyrekrpeaaqlledvqaalkpfsvklneTTDPDKKQmleriqhavqlatEPLEKAVQSRltGEEVnscvevlLE 271
Cdd:PRK14536 72 GHL-------------------------------TDDADSGE-------------DKMVKSAQEH--GKSV-------LE 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 272 EAKdllsdwldstlgcdvtdnsifsklpkFWEGDFHRDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYVSNGSV 351
Cdd:PRK14536 99 IAA--------------------------HYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCAGGNV 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 352 YFDTAKFASsekhsYGKLVPEAVGDqkaLQEGEgdlSISADrlSEKRSPNDFALWKASKPGEP---SWPCPWGKGRPGWH 428
Cdd:PRK14536 153 YFDIRTFPS-----YGSLASAAVED---LQAGA---RIEHD--TNKRNPHDFVLWFTRSKFENhalTWDSPWGRGYPGWH 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 429 IECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAyFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKK-H 507
Cdd:PRK14536 220 IECSAMSMKYLGEQCDIHIGGVDHIRVHHTNEIAQCEA-ATGKPWVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQEKgF 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 508 SARQLRLAFLMHSWKDTLDYSSNTMESALQYEKFLNEFFLNVKDILRAPVDITGQF------EKWGEEEAELNKNFYDKK 581
Cdd:PRK14536 299 QPLDYRFFLLGGHYRSQLAFSWEALKTAKAARRSLVRRVARVVDAARATTGSVRGTlaecaaERVAESRASESELLLTDF 378
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 303304987 582 TAihkALCDNVDTRTVMEEMRALVSQCNLYMAARKAVRKRPNQALLENIALYLTHMLKIFGAVEEDSS 649
Cdd:PRK14536 379 RA---ALEDDFSTPKALSELQKLVKDTSVPPSLCLSVLQAMDTVLGLGLIQEATASLSAQVPAGPSEE 443
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
112-579 |
4.26e-42 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 160.40 E-value: 4.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 112 LHLYNslTRNKEVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLKdYFKFDVFYCMNITDIddkiikrarq 191
Cdd:PRK14534 3 LKLYN--TKTKDLSELKNFSDVKVYACGPTVYNYAHIGNFRTYIFEDLLIKSLR-LLKYNVNYAMNITDI---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 192 NHLfeqyrekrpeaaqlledvqaalkpfsvklneTTDPDKKQmleriqhavqlatEPLEKAVQSR-LTGEEVNscvevll 270
Cdd:PRK14534 70 GHL-------------------------------TGDFDDGE-------------DKVVKAARERgLTVYEIS------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 271 eeakdllsdwldstlgcdvtdnsifsklpKFWEGDFHRDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYVSNGS 350
Cdd:PRK14534 99 -----------------------------RFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTYFVNGN 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 351 VYFDTAKFassekHSYGKLVPEAVGDQKALQEGEGDLSISadrlseKRSPNDFALWKAS---KPGEPSWPCPWGKGRPGW 427
Cdd:PRK14534 150 VYFDTSCF-----KSYGQMAGINLNDFKDMSVSRVEIDKS------KRNKSDFVLWFTNskfKDQEMKWDSPWGFGYPSW 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 428 HIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFeNDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKH 507
Cdd:PRK14534 219 HLECAAMNLEYFKSTLDIHLGGVDHIGVHHINEIAIAECYL-NKKWCDMFVHGEFLIMEYEKMSKSNNNFITIKDLEDQG 297
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 303304987 508 -SARQLRLAFLMHSWKDTLDYSSNTME-SALQYEKFLNE--FFLNVKDilraPVDITGQFEKWGEEEAELNKNFYD 579
Cdd:PRK14534 298 fSPLDFRYFCLTAHYRTQLKFTFNNLKaCKIARENMLNKltYFYSSLD----QFDLNLLNKDLENIEFSLEKEYYD 369
|
|
| GST_C_CysRS_N |
cd10310 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Cysteinyl-tRNA synthetase ... |
3-76 |
1.32e-36 |
|
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: 131.94 E-value: 1.32e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 303304987 3 DSSGQQAPDYRSILSISDEAARAQALNEHLSTRSYVQGYSLSQADVDAFRQLSAPPADPqLFHVARWFRHIEAL 76
Cdd:cd10310 1 ASSGQAAFDYGFILSISEEAARAEALNEYLSTRSYLQGFGPSQADVEVFRLLSRPPADR-LVHVLRWYRHIEAL 73
|
|
| GST_C_eEF1b_like |
cd10308 |
Glutathione S-transferase C-terminal-like, alpha helical domain of eukaryotic translation ... |
3-76 |
4.49e-25 |
|
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: 99.42 E-value: 4.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 3 DSSGQQAPDYRSILSISD--------EAARAQALNEHLSTRSYVQGYSLSQADVDAFRQLSAPPADPQLFHVARWFRHIE 74
Cdd:cd10308 1 KANLATESKHKLLLGVSLdgsfadlkTDKGLEALNEYLADRSYISGYSPSQADVEVFDKLKKAPDATKFPHLARWYRHIA 80
|
..
gi 303304987 75 AL 76
Cdd:cd10308 81 SF 82
|
|
| GST_C_AaRS_like |
cd10289 |
Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA ... |
14-76 |
4.01e-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: 53.86 E-value: 4.01e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 303304987 14 SILSISDEAARAQALNEHLSTRSYVQGYSLSQADVDAFRQLSAPPADPQ------LFHVARWFRHIEAL 76
Cdd:cd10289 14 SLLKGKELEALLKSLNSYLASRTFLVGYSLTLADVAVFSALYPSGQKLSdkekkkFPHVTRWFNHIQNL 82
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
466-601 |
5.38e-08 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 56.80 E-value: 5.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 466 AYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLaFLMHS---WKDtLDYSSNTMESAL-QYEKF 541
Cdd:PRK12300 554 AIFPEEKWPRGIVVNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRL-YLTSSaelLQD-ADWREKEVESVRrQLERF 631
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 542 LnEFFLNVKDIlrAPVDITGQFEKWgeEEAELNKNFydKKTaiHKALcDNVDTRTVMEEM 601
Cdd:PRK12300 632 Y-ELAKELIEI--GGEEELRFIDKW--LLSRLNRII--KET--TEAM-ESFQTRDAVQEA 681
|
|
| GST_C_GluRS_N |
cd10306 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Glutamyl-tRNA synthetase; ... |
16-76 |
4.54e-06 |
|
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: 45.42 E-value: 4.54e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 16 LSISDEAARAQALNE---HLSTRSYVQGYSLSQADV------DAFRQLSAPPADPQLFHVARWFRHIEAL 76
Cdd:cd10306 18 LVLKDFKALSQALEEldsHLTLRTFIVGYSLSLADIavwgalRGNGVAGSLIKNKVYVNLSRWFSFLESL 87
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
450-536 |
1.02e-05 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 49.30 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 450 FDLRFPHHD---NELAQS----EAYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRlaFLMHSWK 522
Cdd:PLN02959 672 FDLRVSGKDliqNHLTFAiynhTAIWAEEHWPRGFRCNGHLMLNSEKMSKSTGNFLTLRQAIEEFSADATR--FALADAG 749
|
90
....*....|....*..
gi 303304987 523 DTLD---YSSNTMESAL 536
Cdd:PLN02959 750 DGVDdanFVFETANAAI 766
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
138-200 |
1.10e-05 |
|
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: 45.93 E-value: 1.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 303304987 138 CGPTVYDASHMGHARSYISFDILRRVLKDyFKFDVFYCMNITDIDDKIIKRARQNHL-FEQYRE 200
Cdd:cd00802 4 SGITPNGYLHIGHLRTIVTFDFLAQAYRK-LGYKVRCIALIDDAGGLIGDPANKKGEnAKAFVE 66
|
|
| GST_C_AIMP3 |
cd10305 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ... |
28-79 |
2.66e-05 |
|
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: 43.82 E-value: 2.66e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 28 LNEHLSTRSYVQGYSLSQADV-------DAFRQLSapPAD-PQLFHVARWFRHIEALLGS 79
Cdd:cd10305 34 LNSYLQDRTYLVGHKLTLADVvlyyglhPIMKDLS--PQEkEQYLNVSRWFDHVQHLPGI 91
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
474-520 |
1.99e-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: 44.44 E-value: 1.99e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 303304987 474 VRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHS 520
Cdd:cd00814 265 PTRIVAHGYLTVEGKKMSKSRGNVVDPDDLLERYGADALRYYLLRER 311
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
480-520 |
7.79e-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: 7.79e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 303304987 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 |
1.30e-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: 1.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303304987 426 GWHIECSAMAGTLLGASMDIHGGGFDLRFpHHDNELAQSEAYfeNDCWVRYFLHTGHLTIA-GCKMSKSL 494
Cdd:cd00802 77 EYMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKA--GGPARPFGLTFGRVMGAdGTKMSKSK 143
|
|
| GST_C_GluProRS_N |
cd10309 |
Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional ... |
16-76 |
1.62e-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: 1.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 303304987 16 LSISDEAARA-QALNEHLSTRSYVQGYSLSQADVDAFRQL------SAPPADPQlfHVARWFRHIEAL 76
Cdd:cd10309 16 LSCDQDFSSAlSYLDKALSLRTYLVGNSLTLADFAVWAALrgngewLASKEKYV--NVTRWFKFISSQ 81
|
|
| |
