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Conserved domains on  [gi|1039778906|ref|XP_017177784|]
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cysteine--tRNA ligase, cytoplasmic isoform X3 [Mus musculus]

Protein Classification

cysteine--tRNA ligase; glutathione S-transferase C-terminal domain-containing protein( domain architecture ID 12969709)

cysteine--tRNA ligase catalyzes the attachment of cysteine to tRNA(Cys); glutathione S-transferase C-terminal domain-containing protein that also contains a class I SAM-dependent methyltransferase domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00399 super family cl36555
cysteinyl-tRNA-synthetase; Provisional
 91-690 0e+00

cysteinyl-tRNA-synthetase; Provisional


The actual alignment was detected with superfamily member PTZ00399:

Pssm-ID: 240402 [Multi-domain]  Cd Length: 651  Bit Score: 704.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906  91 ASKGRRVQPQWSPPA--GTEPCRLRLYNSLTRNKDVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRDYF 168
Cdd:PTZ00399   17 GQVSKSRLPEWKKPSkeGKYLTGLKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEDYF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 169 QYDVFYCMNITDIDDKIIRRARQNYLfeqyreqkppatqllkdvrdamkpfsvklsettdpdkrqmleriqnsvklatep 248
Cdd:PTZ00399   97 GYDVFYVMNITDIDDKIIKRAREEKL------------------------------------------------------ 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 249 leqavrsslsgeevdskvqvlleeakdllsdwldstggsevtdnSIFSKLPKFWEEEFHKDMEALNVLPPDVLTRVSEYV 328
Cdd:PTZ00399  123 --------------------------------------------SIFLELARKWEKEFFEDMKALNVRPPDVITRVSEYV 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 329 PEIVNFVQKIVDNGYGYASNGSVYFDTAKFAASeKHSYGKLVPEAVGDQKALQEGEGDLSISAdrlSEKRSPNDFALWKA 408
Cdd:PTZ00399  159 PEIVDFIQKIIDNGFAYESNGSVYFDVEAFRKA-GHVYPKLEPESVADEDRIAEGEGALGKVS---GEKRSPNDFALWKA 234

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 409 SKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDCWVRYFLHTGHLTIAGC 488
Cdd:PTZ00399  235 SKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKGL 314

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 489 KMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSSNTMESALQYEKFMNEFFLNVKDILRAPVdiTGQFEKWEA 568
Cdd:PTZ00399  315 KMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSDESMDEAIEKDKVFFNFFANVKIKLRESE--LTSPQKWTQ 392

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 569 EEVELNKNFYGKKTAVHEALCDNIDTRTVMEEMRALVSQCNLYMAARKaerrRPNRALLENIAMYLTHMLKIFGAIEEes 648
Cdd:PTZ00399  393 HDFELNELFEETKSAVHAALLDNFDTPEALQALQKLISATNTYLNSGE----QPSAPLLRSVAQYVTKILSIFGLVEG-- 466

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|..
gi 1039778906 649 plGFPVGGPGTNlNLESTVMPYLQVLSEFREGVRKIAREKKS 690
Cdd:PTZ00399  467 --SDGLGSQGQN-STSENFKPLLEALLRFRDEVRDAAKAEMK 505
GST_C_CysRS_N cd10310
Glutathione S-transferase C-terminal-like, alpha helical domain of Cysteinyl-tRNA synthetase ...
 4-76 1.31e-33

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: 123.08  E-value: 1.31e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039778906   4 SSAEQAADYRSILSISDEAARVQALDQHLSTRSYIQGYSLSQADVDVFRQLSAPPADsRLFHVARWFRHIEAL 76
Cdd:cd10310     2 SSGQAAFDYGFILSISEEAARAEALNEYLSTRSYLQGFGPSQADVEVFRLLSRPPAD-RLVHVLRWYRHIEAL 73
 
Name Accession Description Interval E-value
PTZ00399 PTZ00399
cysteinyl-tRNA-synthetase; Provisional
 91-690 0e+00

cysteinyl-tRNA-synthetase; Provisional


Pssm-ID: 240402 [Multi-domain]  Cd Length: 651  Bit Score: 704.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906  91 ASKGRRVQPQWSPPA--GTEPCRLRLYNSLTRNKDVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRDYF 168
Cdd:PTZ00399   17 GQVSKSRLPEWKKPSkeGKYLTGLKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEDYF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 169 QYDVFYCMNITDIDDKIIRRARQNYLfeqyreqkppatqllkdvrdamkpfsvklsettdpdkrqmleriqnsvklatep 248
Cdd:PTZ00399   97 GYDVFYVMNITDIDDKIIKRAREEKL------------------------------------------------------ 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 249 leqavrsslsgeevdskvqvlleeakdllsdwldstggsevtdnSIFSKLPKFWEEEFHKDMEALNVLPPDVLTRVSEYV 328
Cdd:PTZ00399  123 --------------------------------------------SIFLELARKWEKEFFEDMKALNVRPPDVITRVSEYV 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 329 PEIVNFVQKIVDNGYGYASNGSVYFDTAKFAASeKHSYGKLVPEAVGDQKALQEGEGDLSISAdrlSEKRSPNDFALWKA 408
Cdd:PTZ00399  159 PEIVDFIQKIIDNGFAYESNGSVYFDVEAFRKA-GHVYPKLEPESVADEDRIAEGEGALGKVS---GEKRSPNDFALWKA 234

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 409 SKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDCWVRYFLHTGHLTIAGC 488
Cdd:PTZ00399  235 SKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKGL 314

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 489 KMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSSNTMESALQYEKFMNEFFLNVKDILRAPVdiTGQFEKWEA 568
Cdd:PTZ00399  315 KMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSDESMDEAIEKDKVFFNFFANVKIKLRESE--LTSPQKWTQ 392

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 569 EEVELNKNFYGKKTAVHEALCDNIDTRTVMEEMRALVSQCNLYMAARKaerrRPNRALLENIAMYLTHMLKIFGAIEEes 648
Cdd:PTZ00399  393 HDFELNELFEETKSAVHAALLDNFDTPEALQALQKLISATNTYLNSGE----QPSAPLLRSVAQYVTKILSIFGLVEG-- 466

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|..
gi 1039778906 649 plGFPVGGPGTNlNLESTVMPYLQVLSEFREGVRKIAREKKS 690
Cdd:PTZ00399  467 --SDGLGSQGQN-STSENFKPLLEALLRFRDEVRDAAKAEMK 505
CysS COG0215
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ...
 112-689 5.77e-161

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: 471.51  E-value: 5.77e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 112 LRLYNSLTRNKDVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRdYFQYDVFYCMNITDIDDKIIRRARQ 191
Cdd:COG0215     2 LKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLR-YLGYKVTYVRNITDVDDKIIKRAAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 192 NylfeqyreqkppatqllkdvrdamkpfsvklsettdpdkrqmleriqnsvklatepleqavrsslsGEEVdskvqvlle 271
Cdd:COG0215    81 E------------------------------------------------------------------GESI--------- 85

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 272 eakdllsdwldstggSEVTDnsifsklpkFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYASNGSV 351
Cdd:COG0215    86 ---------------WELAE---------RYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEADGDV 141

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 352 YFDTAKFaasekHSYGKL---VPEAvgdqkaLQEGEgdlsiSADRLSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWH 428
Cdd:COG0215   142 YFDVRSF-----PDYGKLsgrNLDD------LRAGA-----RVEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWH 205

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 429 IECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDcWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHS 508
Cdd:COG0215   206 IECSAMSTKYLGETFDIHGGGIDLIFPHHENEIAQSEAATGKP-FARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKKYD 284

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 509 ARQLRLAFLMHSWKDTLDYSSNTMESALQ-YEKFMNeFFLNVKDILRAPVDITGQFEKWEAEevelnknfygkktaVHEA 587
Cdd:COG0215   285 PEVLRFFLLSAHYRSPLDFSEEALEEAEKaLERLYN-ALRRLEEALGAADSSAEEIEELREE--------------FIAA 349

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 588 LCDNIDTRTVMEEMRALVSQCNLYMAARKaerrrpNRALLENIAMYLTHMLKIFGaIEEESPLGFpvGGPGTNLNLESTV 667
Cdd:COG0215   350 MDDDFNTPEALAVLFELVREINKALDEGE------DKAALAALAALLRALGGVLG-LLLLEPEAW--QGAAEDELLDALI 420

                         570       580
                  ....*....|....*....|..
gi 1039778906 668 MPYLQvlsefregVRKIAREKK 689
Cdd:COG0215   421 EALIE--------ERAEARKAK 434
tRNA-synt_1e pfam01406
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ...
 125-540 5.85e-143

tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.


Pssm-ID: 396128 [Multi-domain]  Cd Length: 301  Bit Score: 419.47  E-value: 5.85e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 125 FIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRdYFQYDVFYCMNITDIDDKIIRRARQNYLFEQyreqkpp 204
Cdd:pfam01406   2 FVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQ-ALGYDVQFVQNFTDIDDKIIKRARQEGESFR------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 205 atqllkdvrdamkpfsvklsettdpdkrqmleriqnsvklatepleqavrsslsgeevdskvqvlleeakdllsdwldst 284
Cdd:pfam01406     --------------------------------------------------------------------------------

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 285 ggsevtdnsifsKLPKFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGY-ASNGSVYFDTAKFaasek 363
Cdd:pfam01406  74 ------------QLAARFIEAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYvSDNGDVYFDVSSF----- 136

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 364 HSYGKLVPEAVGDQKALQEGEGDlsisadrlSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASM 443
Cdd:pfam01406 137 PDYGKLSGQNLEQLEAGARGEVS--------EGKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQI 208

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 444 DIHGGGFDLRFPHHDNELAQSEAYFENDcWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKD 523
Cdd:pfam01406 209 DIHGGGIDLAFPHHENEIAQSEAAFDKQ-LANYWLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRS 287

                         410
                  ....*....|....*..
gi 1039778906 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 ...
 112-689 5.89e-139

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: 415.24  E-value: 5.89e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 112 LRLYNSLTRNKDVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRdYFQYDVFYCMNITDIDDKIIRRARQ 191
Cdd:TIGR00435   1 LKLYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLR-YLGYKVQYVQNITDIDDKIIKRARE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 192 NYLFEQyreqkppatqllkdvrdamkpfsvklsettdpdkrqmleriqnsvklatepleqavrsslsgeevdskvqvlle 271
Cdd:TIGR00435  80 NGESVY-------------------------------------------------------------------------- 85

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 272 eakdllsdwldstggsEVTDNSIfsklpkfweEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYAS-NGS 350
Cdd:TIGR00435  86 ----------------EVSERFI---------EAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSdNGD 140

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 351 VYFDTAKFaasekHSYGKLvpeAVGDQKALQEGEGDLSISAdrlseKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIE 430
Cdd:TIGR00435 141 VYFDVSKF-----KDYGKL---SKQDLDQLEAGARVDVDEA-----KRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIE 207

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 431 CSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFeNDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSAR 510
Cdd:TIGR00435 208 CSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQSEAAF-GKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKNYDPE 286

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 511 QLRLAFLMHSWKDTLDYSsntmESALQYEKFMNEFFLNVKDILRAPVDITGQFEKWEAEEVelnKNFYgkkTAVHEALCD 590
Cdd:TIGR00435 287 ILRYFLLSVHYRSPLDFS----EELLEAAKNALERLYKALRVLDTSLAYSGNQSLNKFPDE---KEFE---ARFVEAMDD 356

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 591 NIDTR---TVMEEMralVSQCNLYMAarkaerrrpNRALLENIAMYLTHMLKIFGAIEEESPLGFPVGGPGTNLNLESTV 667
Cdd:TIGR00435 357 DLNTAnalAVLFEL---AKSINLTFV---------SKADAALLIEHLIFLESRLGLLLGLPSKPVQAGSNDDLGEIEALI 424

                         570       580
                  ....*....|....*....|..
gi 1039778906 668 MPylqvlsefregvRKIAREKK 689
Cdd:TIGR00435 425 EE------------RSIARKEK 434
CysRS_core cd00672
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ...
 113-528 1.06e-111

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: 335.70  E-value: 1.06e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 113 RLYNSLTRNKDVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRDYFqYDVFYCMNITDIDDKIIRRARQN 192
Cdd:cd00672     1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLG-YKVRYVQNITDIDDKIIKRAREE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 193 YLFeqyreqkppatqllkdvrdamkpfsvklsettdpdkrqmleriqnsvklatepleqavrsslsgeevdskvqvllee 272
Cdd:cd00672    80 GLS----------------------------------------------------------------------------- 82

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 273 akdllsdwldstggsevtdnsiFSKLPKFWEEEFHKDMEALNVLPPDVLTRVseyvpeivnfvqkivdngygyasngsvy 352
Cdd:cd00672    83 ----------------------WKEVADYYTKEFFEDMKALNVLPPDVVPRV---------------------------- 112

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 353 fdtakfaasekhsygklvpeavgdqkalqegegdlsisadrlsekrspndfalwkaskpgepswpcpwgkgrpgWHIECS 432
Cdd:cd00672   113 --------------------------------------------------------------------------WHIECS 118

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 433 AMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFeNDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQL 512
Cdd:cd00672   119 AMAMKYLGETFDIHGGGVDLIFPHHENEIAQSEAAT-GKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVL 197

                         410
                  ....*....|....*.
gi 1039778906 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 1.31e-33

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: 123.08  E-value: 1.31e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039778906   4 SSAEQAADYRSILSISDEAARVQALDQHLSTRSYIQGYSLSQADVDVFRQLSAPPADsRLFHVARWFRHIEAL 76
Cdd:cd10310     2 SSGQAAFDYGFILSISEEAARAEALNEYLSTRSYLQGFGPSQADVEVFRLLSRPPAD-RLVHVLRWYRHIEAL 73
 
Name Accession Description Interval E-value
PTZ00399 PTZ00399
cysteinyl-tRNA-synthetase; Provisional
 91-690 0e+00

cysteinyl-tRNA-synthetase; Provisional


Pssm-ID: 240402 [Multi-domain]  Cd Length: 651  Bit Score: 704.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906  91 ASKGRRVQPQWSPPA--GTEPCRLRLYNSLTRNKDVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRDYF 168
Cdd:PTZ00399   17 GQVSKSRLPEWKKPSkeGKYLTGLKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEDYF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 169 QYDVFYCMNITDIDDKIIRRARQNYLfeqyreqkppatqllkdvrdamkpfsvklsettdpdkrqmleriqnsvklatep 248
Cdd:PTZ00399   97 GYDVFYVMNITDIDDKIIKRAREEKL------------------------------------------------------ 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 249 leqavrsslsgeevdskvqvlleeakdllsdwldstggsevtdnSIFSKLPKFWEEEFHKDMEALNVLPPDVLTRVSEYV 328
Cdd:PTZ00399  123 --------------------------------------------SIFLELARKWEKEFFEDMKALNVRPPDVITRVSEYV 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 329 PEIVNFVQKIVDNGYGYASNGSVYFDTAKFAASeKHSYGKLVPEAVGDQKALQEGEGDLSISAdrlSEKRSPNDFALWKA 408
Cdd:PTZ00399  159 PEIVDFIQKIIDNGFAYESNGSVYFDVEAFRKA-GHVYPKLEPESVADEDRIAEGEGALGKVS---GEKRSPNDFALWKA 234

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 409 SKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDCWVRYFLHTGHLTIAGC 488
Cdd:PTZ00399  235 SKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKGL 314

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 489 KMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSSNTMESALQYEKFMNEFFLNVKDILRAPVdiTGQFEKWEA 568
Cdd:PTZ00399  315 KMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSDESMDEAIEKDKVFFNFFANVKIKLRESE--LTSPQKWTQ 392

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 569 EEVELNKNFYGKKTAVHEALCDNIDTRTVMEEMRALVSQCNLYMAARKaerrRPNRALLENIAMYLTHMLKIFGAIEEes 648
Cdd:PTZ00399  393 HDFELNELFEETKSAVHAALLDNFDTPEALQALQKLISATNTYLNSGE----QPSAPLLRSVAQYVTKILSIFGLVEG-- 466

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|..
gi 1039778906 649 plGFPVGGPGTNlNLESTVMPYLQVLSEFREGVRKIAREKKS 690
Cdd:PTZ00399  467 --SDGLGSQGQN-STSENFKPLLEALLRFRDEVRDAAKAEMK 505
CysS COG0215
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ...
 112-689 5.77e-161

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: 471.51  E-value: 5.77e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 112 LRLYNSLTRNKDVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRdYFQYDVFYCMNITDIDDKIIRRARQ 191
Cdd:COG0215     2 LKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLR-YLGYKVTYVRNITDVDDKIIKRAAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 192 NylfeqyreqkppatqllkdvrdamkpfsvklsettdpdkrqmleriqnsvklatepleqavrsslsGEEVdskvqvlle 271
Cdd:COG0215    81 E------------------------------------------------------------------GESI--------- 85

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 272 eakdllsdwldstggSEVTDnsifsklpkFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYASNGSV 351
Cdd:COG0215    86 ---------------WELAE---------RYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEADGDV 141

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 352 YFDTAKFaasekHSYGKL---VPEAvgdqkaLQEGEgdlsiSADRLSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWH 428
Cdd:COG0215   142 YFDVRSF-----PDYGKLsgrNLDD------LRAGA-----RVEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWH 205

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 429 IECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDcWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHS 508
Cdd:COG0215   206 IECSAMSTKYLGETFDIHGGGIDLIFPHHENEIAQSEAATGKP-FARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKKYD 284

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 509 ARQLRLAFLMHSWKDTLDYSSNTMESALQ-YEKFMNeFFLNVKDILRAPVDITGQFEKWEAEevelnknfygkktaVHEA 587
Cdd:COG0215   285 PEVLRFFLLSAHYRSPLDFSEEALEEAEKaLERLYN-ALRRLEEALGAADSSAEEIEELREE--------------FIAA 349

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 588 LCDNIDTRTVMEEMRALVSQCNLYMAARKaerrrpNRALLENIAMYLTHMLKIFGaIEEESPLGFpvGGPGTNLNLESTV 667
Cdd:COG0215   350 MDDDFNTPEALAVLFELVREINKALDEGE------DKAALAALAALLRALGGVLG-LLLLEPEAW--QGAAEDELLDALI 420

                         570       580
                  ....*....|....*....|..
gi 1039778906 668 MPYLQvlsefregVRKIAREKK 689
Cdd:COG0215   421 EALIE--------ERAEARKAK 434
tRNA-synt_1e pfam01406
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ...
 125-540 5.85e-143

tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.


Pssm-ID: 396128 [Multi-domain]  Cd Length: 301  Bit Score: 419.47  E-value: 5.85e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 125 FIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRdYFQYDVFYCMNITDIDDKIIRRARQNYLFEQyreqkpp 204
Cdd:pfam01406   2 FVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQ-ALGYDVQFVQNFTDIDDKIIKRARQEGESFR------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 205 atqllkdvrdamkpfsvklsettdpdkrqmleriqnsvklatepleqavrsslsgeevdskvqvlleeakdllsdwldst 284
Cdd:pfam01406     --------------------------------------------------------------------------------

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 285 ggsevtdnsifsKLPKFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGY-ASNGSVYFDTAKFaasek 363
Cdd:pfam01406  74 ------------QLAARFIEAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYvSDNGDVYFDVSSF----- 136

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 364 HSYGKLVPEAVGDQKALQEGEGDlsisadrlSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASM 443
Cdd:pfam01406 137 PDYGKLSGQNLEQLEAGARGEVS--------EGKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQI 208

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 444 DIHGGGFDLRFPHHDNELAQSEAYFENDcWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKD 523
Cdd:pfam01406 209 DIHGGGIDLAFPHHENEIAQSEAAFDKQ-LANYWLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRS 287

                         410
                  ....*....|....*..
gi 1039778906 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 ...
 112-689 5.89e-139

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: 415.24  E-value: 5.89e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 112 LRLYNSLTRNKDVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRdYFQYDVFYCMNITDIDDKIIRRARQ 191
Cdd:TIGR00435   1 LKLYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLR-YLGYKVQYVQNITDIDDKIIKRARE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 192 NYLFEQyreqkppatqllkdvrdamkpfsvklsettdpdkrqmleriqnsvklatepleqavrsslsgeevdskvqvlle 271
Cdd:TIGR00435  80 NGESVY-------------------------------------------------------------------------- 85

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 272 eakdllsdwldstggsEVTDNSIfsklpkfweEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYAS-NGS 350
Cdd:TIGR00435  86 ----------------EVSERFI---------EAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSdNGD 140

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 351 VYFDTAKFaasekHSYGKLvpeAVGDQKALQEGEGDLSISAdrlseKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIE 430
Cdd:TIGR00435 141 VYFDVSKF-----KDYGKL---SKQDLDQLEAGARVDVDEA-----KRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIE 207

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 431 CSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFeNDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSAR 510
Cdd:TIGR00435 208 CSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQSEAAF-GKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKNYDPE 286

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 511 QLRLAFLMHSWKDTLDYSsntmESALQYEKFMNEFFLNVKDILRAPVDITGQFEKWEAEEVelnKNFYgkkTAVHEALCD 590
Cdd:TIGR00435 287 ILRYFLLSVHYRSPLDFS----EELLEAAKNALERLYKALRVLDTSLAYSGNQSLNKFPDE---KEFE---ARFVEAMDD 356

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 591 NIDTR---TVMEEMralVSQCNLYMAarkaerrrpNRALLENIAMYLTHMLKIFGAIEEESPLGFPVGGPGTNLNLESTV 667
Cdd:TIGR00435 357 DLNTAnalAVLFEL---AKSINLTFV---------SKADAALLIEHLIFLESRLGLLLGLPSKPVQAGSNDDLGEIEALI 424

                         570       580
                  ....*....|....*....|..
gi 1039778906 668 MPylqvlsefregvRKIAREKK 689
Cdd:TIGR00435 425 EE------------RSIARKEK 434
CysRS_core cd00672
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ...
 113-528 1.06e-111

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: 335.70  E-value: 1.06e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 113 RLYNSLTRNKDVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRDYFqYDVFYCMNITDIDDKIIRRARQN 192
Cdd:cd00672     1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLG-YKVRYVQNITDIDDKIIKRAREE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 193 YLFeqyreqkppatqllkdvrdamkpfsvklsettdpdkrqmleriqnsvklatepleqavrsslsgeevdskvqvllee 272
Cdd:cd00672    80 GLS----------------------------------------------------------------------------- 82

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 273 akdllsdwldstggsevtdnsiFSKLPKFWEEEFHKDMEALNVLPPDVLTRVseyvpeivnfvqkivdngygyasngsvy 352
Cdd:cd00672    83 ----------------------WKEVADYYTKEFFEDMKALNVLPPDVVPRV---------------------------- 112

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 353 fdtakfaasekhsygklvpeavgdqkalqegegdlsisadrlsekrspndfalwkaskpgepswpcpwgkgrpgWHIECS 432
Cdd:cd00672   113 --------------------------------------------------------------------------WHIECS 118

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 433 AMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFeNDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQL 512
Cdd:cd00672   119 AMAMKYLGETFDIHGGGVDLIFPHHENEIAQSEAAT-GKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVL 197

                         410
                  ....*....|....*.
gi 1039778906 513 RLAFLMHSWKDTLDYS 528
Cdd:cd00672   198 RLALLSSHYRSPLDFS 213
PLN02946 PLN02946
cysteine-tRNA ligase
 54-535 7.19e-92

cysteine-tRNA ligase


Pssm-ID: 178532 [Multi-domain]  Cd Length: 557  Bit Score: 296.46  E-value: 7.19e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906  54 LSAPPADSRLfhvarwfRHIEALLGGPQGRDEPCRLQASKGRRVQPQWSPpaGTEpcrLRLYNSLTRNKDVFIPQDGKKV 133
Cdd:PLN02946   14 RLSSPPRSQL-------RIAFPLRPPKERQYRSCFFSASALASNGAPASR--GRE---LHLYNTMSRKKELFKPKVEGKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 134 TWYCCGPTVYDASHMGHARSYISFDILRRVLRdYFQYDVFYCMNITDIDDKIIRRARQnylfeqyreqkppatqLLKDvr 213
Cdd:PLN02946   82 GMYVCGVTAYDLSHIGHARVYVTFDVLYRYLK-HLGYEVRYVRNFTDVDDKIIARANE----------------LGED-- 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 214 damkPFSvklsettdpdkrqmleriqnsvklatepleqavrsslsgeevdskvqvlleeakdllsdwldstggsevtdns 293
Cdd:PLN02946  143 ----PIS------------------------------------------------------------------------- 145

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 294 ifskLPKFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYASNGSVYFDTAKFAasekhSYGKLVPEA 373
Cdd:PLN02946  146 ----LSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVDGDVYFSVDKFP-----EYGKLSGRK 216

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 374 VGDQKAlqeGEgdlSISADrlSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLR 453
Cdd:PLN02946  217 LEDNRA---GE---RVAVD--SRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLV 288

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 454 FPHHDNELAQSEAYFEnDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSSNTME 533
Cdd:PLN02946  289 FPHHENEIAQSCAACC-DSNISYWIHNGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDVQLE 367


                  ..
gi 1039778906 534 SA 535
Cdd:PLN02946  368 SA 369
cysS PRK14535
cysteinyl-tRNA synthetase; Provisional
 114-535 3.48e-68

cysteinyl-tRNA synthetase; Provisional


Pssm-ID: 173001 [Multi-domain]  Cd Length: 699  Bit Score: 236.92  E-value: 3.48e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 114 LYNSLTRNKDVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRDyFQYDVFYCMNITDIDDKIIRRARQNy 193
Cdd:PRK14535  230 IYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRE-CGYPLTYVRNITDIDDKIIARAAEN- 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 194 lfeqyreqkppatqllkdvrdamkpfsvklsettdpdkrqmleriqnsvklatepleqavrsslsGEEVdskvqvlleea 273
Cdd:PRK14535  308 -----------------------------------------------------------------GETI----------- 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 274 kdllsdwldstggsevtdnsifSKLPKFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGY-ASNGSVY 352
Cdd:PRK14535  312 ----------------------GELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYpAANGDVY 369

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 353 FDTAKFAAsekhsYGKLVPEAVGDQKALQEGEGDlsisadrlSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECS 432
Cdd:PRK14535  370 YAVREFAA-----YGQLSGKSLDDLRAGERVEVD--------GFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECS 436

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 433 AMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDC---------------WVRYFLHTGHLTIAGCKMSKSLKNF 497
Cdd:PRK14535  437 AMSENLFGDTFDIHGGGADLQFPHHENEIAQSVGATGHTCghhhaqthhgqsiasHVKYWLHNGFIRVDGEKMSKSLGNF 516

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1039778906 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 4.02e-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: 218.44  E-value: 4.02e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 101 WSPPA-----GTEPcRLRLYNSLTRN-KDVfipQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRDYfQYDVFY 174
Cdd:TIGR03447   3 WPAPAvpalpGTGP-PLRLFDTADGQvRPV---EPGPEAGMYVCGITPYDATHLGHAATYLTFDLVNRVWRDA-GHRVHY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 175 CMNITDIDDKIIRRArqnylfeqyreqkppatqllkdVRDAMkpfsvklsettdpdkrqmleriqnsvklatepleqavr 254
Cdd:TIGR03447  78 VQNVTDVDDPLFERA----------------------ERDGV-------------------------------------- 97

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 255 sslsgeevdskvqvlleeakdllsDWLDsTGGSEVtdnsifsklpkfweEEFHKDMEALNVLPPDVLTRVSEYVPEIVNF 334
Cdd:TIGR03447  98 ------------------------DWRE-LGTSQI--------------DLFREDMEALRVLPPRDYIGAVESIDEVVEM 138

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 335 VQKIVDNGYGY----ASNGSVYFDTAkfaASEKHSYGKLVPEAVGDQKALQEGeGDlsisADRLSeKRSPNDFALWKASK 410
Cdd:TIGR03447 139 VEKLLASGAAYivegPEYPDVYFSID---ATEQFGYESGYDRATMLELFAERG-GD----PDRPG-KRDPLDALLWRAAR 209

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 411 PGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDCWVRYFLHTGHLTIAGCKM 490
Cdd:TIGR03447 210 EGEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSDLIFPHHEFSAAHAEAATGVRRMARHYVHAGMIGLDGEKM 289

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1039778906 491 SKSLKNFITIKDaLKK--HSARQLRLAFLMHSWKDTLDYSSNTMESALQ 537
Cdd:TIGR03447 290 SKSLGNLVFVSK-LRAagVDPAAIRLGLLAGHYRQDRDWTDAVLAEAEA 337
PRK12418 PRK12418
cysteinyl-tRNA synthetase; Provisional
 130-537 7.50e-62

cysteinyl-tRNA synthetase; Provisional


Pssm-ID: 183518 [Multi-domain]  Cd Length: 384  Bit Score: 211.33  E-value: 7.50e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 130 GKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRDYfQYDVFYCMNITDIDDKIIRRARqnylfeqyreqkppatqll 209
Cdd:PRK12418    7 GGTATMYVCGITPYDATHLGHAATYLAFDLVNRVWRDA-GHDVHYVQNVTDVDDPLLERAA------------------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 210 kdvRDamkpfsvklsettdpdkrqmleriqnsvklatepleqavrsslsGEevdskvqvlleeakdllsDWLDsTGGSEV 289
Cdd:PRK12418   67 ---RD--------------------------------------------GV------------------DWRD-LAEREI 80

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 290 tdnsifsklpkfweEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGY----ASNGSVYFDTAkfAAsekhs 365
Cdd:PRK12418   81 --------------ALFREDMEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYvvddEEYPDVYFSVD--AT----- 139

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 366 ygklvpEAVGDQKALQEGEGdLSISADRLSE-----KRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLG 440
Cdd:PRK12418  140 ------PQFGYESGYDRATM-LELFAERGGDpdrpgKRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLG 212

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 441 ASMDIHGGGFDLRFPHHDNELAQSEAYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKdALKK--HSARQLRLAFLM 518
Cdd:PRK12418  213 SGFDIQGGGSDLIFPHHEFSAAHAEAATGERRFARHYVHAGMIGLDGEKMSKSRGNLVFVS-RLRAagVDPAAIRLALLA 291

                         410
                  ....*....|....*....
gi 1039778906 519 HSWKDTLDYSSNTMESALQ 537
Cdd:PRK12418  292 GHYRADREWTDAVLAEAEA 310
cysS PRK14536
cysteinyl-tRNA synthetase; Provisional
 112-610 1.62e-60

cysteinyl-tRNA synthetase; Provisional


Pssm-ID: 184731 [Multi-domain]  Cd Length: 490  Bit Score: 210.93  E-value: 1.62e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 112 LRLYNSLTRNKDVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRdYFQYDVFYCMNITDIddkiirrarq 191
Cdd:PRK14536    3 LRLYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTLH-FLGYRVTHVMNITDV---------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 192 NYLfeqyreqkppatqllkdvrdamkpfsvklseTTDPDkrqmleriqnsvklatepleqavrsslSGEevDSKVQVLLE 271
Cdd:PRK14536   72 GHL-------------------------------TDDAD---------------------------SGE--DKMVKSAQE 91

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 272 EAKDLLsdwldstggsevtdnsifsKLPKFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYASNGSV 351
Cdd:PRK14536   92 HGKSVL-------------------EIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCAGGNV 152

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 352 YFDTAKFAasekhSYGKLVPEAVGDqkaLQEGEgdlSISADrlSEKRSPNDFALWKASKPGEP---SWPCPWGKGRPGWH 428
Cdd:PRK14536  153 YFDIRTFP-----SYGSLASAAVED---LQAGA---RIEHD--TNKRNPHDFVLWFTRSKFENhalTWDSPWGRGYPGWH 219

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 429 IECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAyFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKK-H 507
Cdd:PRK14536  220 IECSAMSMKYLGEQCDIHIGGVDHIRVHHTNEIAQCEA-ATGKPWVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQEKgF 298

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 508 SARQLRLAFLMHSWKDTLDYSSNTMESALQYEKFMNEFFLNVKDILRAPVDIT-GQFEKWEAEEVELNKNFYGKK--TAV 584
Cdd:PRK14536  299 QPLDYRFFLLGGHYRSQLAFSWEALKTAKAARRSLVRRVARVVDAARATTGSVrGTLAECAAERVAESRASESELllTDF 378

                         490       500
                  ....*....|....*....|....*.
gi 1039778906 585 HEALCDNIDTRTVMEEMRALVSQCNL 610
Cdd:PRK14536  379 RAALEDDFSTPKALSELQKLVKDTSV 404
cysS PRK14534
cysteinyl-tRNA synthetase; Provisional
 112-548 3.98e-44

cysteinyl-tRNA synthetase; Provisional


Pssm-ID: 173000 [Multi-domain]  Cd Length: 481  Bit Score: 165.41  E-value: 3.98e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 112 LRLYNslTRNKDVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRdYFQYDVFYCMNITDIDdkiirrarq 191
Cdd:PRK14534    3 LKLYN--TKTKDLSELKNFSDVKVYACGPTVYNYAHIGNFRTYIFEDLLIKSLR-LLKYNVNYAMNITDIG--------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 192 nylfeqyreqkppatQLLKDVRDAmkpfsvklsettdPDKrqmleriqnSVKLATEpleqavrSSLSGEEVDskvqvlle 271
Cdd:PRK14534   71 ---------------HLTGDFDDG-------------EDK---------VVKAARE-------RGLTVYEIS-------- 98

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 272 eakdllsdwldstggsevtdnsifsklpKFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYASNGSV 351
Cdd:PRK14534   99 ----------------------------RFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTYFVNGNV 150

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 352 YFDTAKFaasekHSYGKLVPEAVGDQKALQEGEGDLSISadrlseKRSPNDFALWKAS---KPGEPSWPCPWGKGRPGWH 428
Cdd:PRK14534  151 YFDTSCF-----KSYGQMAGINLNDFKDMSVSRVEIDKS------KRNKSDFVLWFTNskfKDQEMKWDSPWGFGYPSWH 219

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 429 IECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFeNDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKH- 507
Cdd:PRK14534  220 LECAAMNLEYFKSTLDIHLGGVDHIGVHHINEIAIAECYL-NKKWCDMFVHGEFLIMEYEKMSKSNNNFITIKDLEDQGf 298

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1039778906 508 SARQLRLAFLMHSWKDTLDYSSNTmesaLQYEKFMNEFFLN 548
Cdd:PRK14534  299 SPLDFRYFCLTAHYRTQLKFTFNN----LKACKIARENMLN 335
GST_C_CysRS_N cd10310
Glutathione S-transferase C-terminal-like, alpha helical domain of Cysteinyl-tRNA synthetase ...
 4-76 1.31e-33

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: 123.08  E-value: 1.31e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039778906   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 1.44e-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: 92.10  E-value: 1.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906   4 SSAEQAADYRSILSISD--------EAARVQALDQHLSTRSYIQGYSLSQADVDVFRQLSAPPADSRLFHVARWFRHIEA 75
Cdd:cd10308     2 ANLATESKHKLLLGVSLdgsfadlkTDKGLEALNEYLADRSYISGYSPSQADVEVFDKLKKAPDATKFPHLARWYRHIAS 81


                  .
gi 1039778906  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 9.19e-10

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: 55.40  E-value: 9.19e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039778906  14 SILSISDEAARVQALDQHLSTRSYIQGYSLSQADVDVFRQLSAPPADSR------LFHVARWFRHIEAL 76
Cdd:cd10289    14 SLLKGKELEALLKSLNSYLASRTFLVGYSLTLADVAVFSALYPSGQKLSdkekkkFPHVTRWFNHIQNL 82
leuS PRK12300
leucyl-tRNA synthetase; Reviewed
 466-631 7.74e-08

leucyl-tRNA synthetase; Reviewed


Pssm-ID: 237049 [Multi-domain]  Cd Length: 897  Bit Score: 55.64  E-value: 7.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 466 AYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLaFLMHS---WKDtLDYSSNTMESAL-QYEKF 541
Cdd:PRK12300  554 AIFPEEKWPRGIVVNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRL-YLTSSaelLQD-ADWREKEVESVRrQLERF 631

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 542 MnEFFLNVKDIlrAPVDITGQFEKWeaeeveLNKNFYGKKTAVHEALcDNIDTRTVMEEmrALVsqcNLYMAARKAERR- 620
Cdd:PRK12300  632 Y-ELAKELIEI--GGEEELRFIDKW------LLSRLNRIIKETTEAM-ESFQTRDAVQE--AFY---ELLNDLRWYLRRv 696

                         170
                  ....*....|..
gi 1039778906 621 -RPNRALLENIA 631
Cdd:PRK12300  697 gEANNKVLREVL 708
class_I_aaRS_core cd00802
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ...
 138-201 1.02e-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: 1.02e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039778906 138 CGPTVYDASHMGHARSYISFDILRRVLRDyFQYDVFYCMNITDIDDKIIRRARQNYL-FEQYREQ 201
Cdd:cd00802     4 SGITPNGYLHIGHLRTIVTFDFLAQAYRK-LGYKVRCIALIDDAGGLIGDPANKKGEnAKAFVER 67
GST_C_GluRS_N cd10306
Glutathione S-transferase C-terminal-like, alpha helical domain of Glutamyl-tRNA synthetase; ...
 28-76 1.62e-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: 49.27  E-value: 1.62e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039778906  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 1.78e-06

Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 3; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein (AIMP) 3 subfamily; AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex that functions as a molecular hub to coordinate protein synthesis. There are three AIMPs, named AIMP1-3, which play diverse regulatory roles. AIMP3, also called p18 or eukaryotic translation elongation factor 1 epsilon-1 (EEF1E1), contains a C-terminal domain with similarity to the C-terminal alpha helical domain of GSTs. It specifically interacts with methionyl-tRNA synthetase (MetRS) and is translocated to the nucleus during DNA synthesis or in response to DNA damage and oncogenic stress. In the nucleus, it interacts with ATM and ATR, which are upstream kinase regulators of p53. It appears to work against DNA damage in cooperation with AIMP2, and similar to AIMP2, AIMP3 is also a haploinsufficient tumor suppressor. AIMP3 transgenic mice have shorter lifespans than wild-type mice and they show characteristics of progeria, suggesting that AIMP3 may also be involved in cellular and organismal aging.


Pssm-ID: 198338 [Multi-domain]  Cd Length: 101  Bit Score: 46.90  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906   4 SSAEQAADYRSILsisdeaarvQALDQHLSTRSYIQGYSLSQADVDVFRQLSAPPADS------RLFHVARWFRHIEALL 77
Cdd:cd10305    19 APASDKADAKSLL---------KELNSYLQDRTYLVGHKLTLADVVLYYGLHPIMKDLspqekeQYLNVSRWFDHVQHLP 89


                  ....*..
gi 1039778906  78 GGPQGRD 84
Cdd:cd10305    90 GIRQHLP 96
PLN02959 PLN02959
aminoacyl-tRNA ligase
 450-536 7.96e-06

aminoacyl-tRNA ligase


Pssm-ID: 215518 [Multi-domain]  Cd Length: 1084  Bit Score: 49.30  E-value: 7.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906  450 FDLRFPHHD---NELAQS----EAYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRlaFLMHSWK 522
Cdd:PLN02959   672 FDLRVSGKDliqNHLTFAiynhTAIWAEEHWPRGFRCNGHLMLNSEKMSKSTGNFLTLRQAIEEFSADATR--FALADAG 749

                           90
                   ....*....|....*..
gi 1039778906  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 1.90e-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: 1.90e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1039778906 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 4.31e-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: 4.31e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039778906  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 6.34e-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: 6.34e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1039778906 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 1.23e-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: 1.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778906 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 2.91e-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: 38.28  E-value: 2.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039778906  27 ALDQHLSTRSYIQGYSLSQADVDV-------FRQLSAPPADSRLFHVARWF 70
Cdd:cd10294    51 VLDCYLKLRTYLVGEAITLADIAVacalllpFKYVLDPARRESLLNVTRWF 101
PRK11893 PRK11893
methionyl-tRNA synthetase; Reviewed
 140-192 6.55e-03

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237012 [Multi-domain]  Cd Length: 511  Bit Score: 39.48  E-value: 6.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039778906 140 PTVYDASHMGHARSYISFDILRRVLRdyfQ--YDVFYcmnITDIDD---KIIRRARQN 192
Cdd:PRK11893   10 YYPNGKPHIGHAYTTLAADVLARFKR---LrgYDVFF---LTGTDEhgqKIQRKAEEA 61
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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