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Conserved domains on  [gi|1859345866|ref|WP_175078544|]
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MULTISPECIES: cysteine--tRNA ligase [Pseudoalteromonas]

Protein Classification

cysteine--tRNA ligase( domain architecture ID 11415459)

cysteine--tRNA ligase catalyzes the attachment of cysteine to tRNA(Cys)

CATH:  1.20.120.640|3.40.50.620
EC:  6.1.1.16
Gene Ontology:  GO:0004817|GO:0008270|GO:0005524|GO:0006423
PubMed:  1864365|8274143|1852601|2053131|10447505|10704480|12458790
SCOP:  4003807

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CysS COG0215
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ...
 1-459 0e+00

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: 843.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866   1 MVQIYNTLTRQKEQFKPLVDGKIDMYVCGITIYDYCHIGHARTFVGFDVIVRYLRHIGYDLKYVRNITDVDDKIIKRANE 80
Cdd:COG0215     1 TLKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYLGYKVTYVRNITDVDDKIIKRAAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  81 NGESINDLTTRMTKAMHEDFDSLNMLRPDVEPTVTNHMDEIIAMVERLIAKGHAYVAaDGDVLFDVSTFEQYGALSQQDL 160
Cdd:COG0215    81 EGESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEA-DGDVYFDVRSFPDYGKLSGRNL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 161 TMLQAGSRVEVAQDKQDPLDFVLWKKAKPEEPSWSSPWGEGRPGWHIECSAMSSKHLGEHFDIHGGGSDLQFPHHENEIA 240
Cdd:COG0215   160 DDLRAGARVEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 241 QSCCANNGKYVNTWIHTGMVQVNKEKMSKSLNNFFTVRDVLKEYDAESVRYFLISGHYRSQLNYSQENLEQARSSLERIY 320
Cdd:COG0215   240 QSEAATGKPFARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKALERLY 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 321 TALRGVTPI-----ECDLASNEYVAKFRKAMDDDFNTPEALPVLFELAKELNRVKDS--DTEQAGKLAYVLRSVAEVLGV 393
Cdd:COG0215   320 NALRRLEEAlgaadSSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKALDEgeDKAALAALAALLRALGGVLGL 399

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1859345866 394 AQQDPEAFLQGGQADDEVAHIEALIAKRNEARASKDWAAADEARDALNALGVVLEDSAGKTTWRKA 459
Cdd:COG0215   400 LLLEPEAWQGAAEDELLDALIEALIEERAEARKAKDFARADRIRDELAALGIVLEDTPDGTTWRRK 465
 
Name Accession Description Interval E-value
CysS COG0215
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ...
 1-459 0e+00

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: 843.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866   1 MVQIYNTLTRQKEQFKPLVDGKIDMYVCGITIYDYCHIGHARTFVGFDVIVRYLRHIGYDLKYVRNITDVDDKIIKRANE 80
Cdd:COG0215     1 TLKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYLGYKVTYVRNITDVDDKIIKRAAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  81 NGESINDLTTRMTKAMHEDFDSLNMLRPDVEPTVTNHMDEIIAMVERLIAKGHAYVAaDGDVLFDVSTFEQYGALSQQDL 160
Cdd:COG0215    81 EGESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEA-DGDVYFDVRSFPDYGKLSGRNL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 161 TMLQAGSRVEVAQDKQDPLDFVLWKKAKPEEPSWSSPWGEGRPGWHIECSAMSSKHLGEHFDIHGGGSDLQFPHHENEIA 240
Cdd:COG0215   160 DDLRAGARVEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 241 QSCCANNGKYVNTWIHTGMVQVNKEKMSKSLNNFFTVRDVLKEYDAESVRYFLISGHYRSQLNYSQENLEQARSSLERIY 320
Cdd:COG0215   240 QSEAATGKPFARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKALERLY 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 321 TALRGVTPI-----ECDLASNEYVAKFRKAMDDDFNTPEALPVLFELAKELNRVKDS--DTEQAGKLAYVLRSVAEVLGV 393
Cdd:COG0215   320 NALRRLEEAlgaadSSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKALDEgeDKAALAALAALLRALGGVLGL 399

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1859345866 394 AQQDPEAFLQGGQADDEVAHIEALIAKRNEARASKDWAAADEARDALNALGVVLEDSAGKTTWRKA 459
Cdd:COG0215   400 LLLEPEAWQGAAEDELLDALIEALIEERAEARKAKDFARADRIRDELAALGIVLEDTPDGTTWRRK 465
cysS TIGR00435
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ...
 4-458 0e+00

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: 656.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866   4 IYNTLTRQKEQFKPLVDGKIDMYVCGITIYDYCHIGHARTFVGFDVIVRYLRHIGYDLKYVRNITDVDDKIIKRANENGE 83
Cdd:TIGR00435   3 LYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLRYLGYKVQYVQNITDIDDKIIKRARENGE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  84 SINDLTTRMTKAMHEDFDSLNMLRPDVEPTVTNHMDEIIAMVERLIAKGHAYVAADGDVLFDVSTFEQYGALSQQDLTML 163
Cdd:TIGR00435  83 SVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVYFDVSKFKDYGKLSKQDLDQL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 164 QAGSRVEVAQDKQDPLDFVLWKKAKPEEPSWSSPWGEGRPGWHIECSAMSSKHLGEHFDIHGGGSDLQFPHHENEIAQSC 243
Cdd:TIGR00435 163 EAGARVDVDEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQSE 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 244 CANNGKYVNTWIHTGMVQVNKEKMSKSLNNFFTVRDVLKEYDAESVRYFLISGHYRSQLNYSQENLEQARSSLERIYTAL 323
Cdd:TIGR00435 243 AAFGKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKNALERLYKAL 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 324 RGVtpiECDLAS------------NEYVAKFRKAMDDDFNTPEALPVLFELAKELNrVKDSDTEQAGKLAYVLRSVAEVL 391
Cdd:TIGR00435 323 RVL---DTSLAYsgnqslnkfpdeKEFEARFVEAMDDDLNTANALAVLFELAKSIN-LTFVSKADAALLIEHLIFLESRL 398

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1859345866 392 GVAQQDPEAFLQGGqADDEVAHIEALIAKRNEARASKDWAAADEARDALNALGVVLEDSAGKTTWRK 458
Cdd:TIGR00435 399 GLLLGLPSKPVQAG-SNDDLGEIEALIEERSIARKEKDFAKADEIRDELAKKGIVLEDTPQGTTWRR 464
cysS PRK14535
cysteinyl-tRNA synthetase; Provisional
 1-459 0e+00

cysteinyl-tRNA synthetase; Provisional


Pssm-ID: 173001 [Multi-domain]  Cd Length: 699  Bit Score: 532.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866   1 MVQIYNTLTRQKEQFKPLVDGKIDMYVCGITIYDYCHIGHARTFVGFDVIVRYLRHIGYDLKYVRNITDVDDKIIKRANE 80
Cdd:PRK14535  227 MTTIYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAE 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  81 NGESINDLTTRMTKAMHEDFDSLNMLRPDVEPTVTNHMDEIIAMVERLIAKGHAYVAADGDVLFDVSTFEQYGALSQQDL 160
Cdd:PRK14535  307 NGETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVYYAVREFAAYGQLSGKSL 386

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 161 TMLQAGSRVEVAQDKQDPLDFVLWKKAKPEEPSWSSPWGEGRPGWHIECSAMSSKHLGEHFDIHGGGSDLQFPHHENEIA 240
Cdd:PRK14535  387 DDLRAGERVEVDGFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIA 466

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 241 QSCCANN----------------GKYVNTWIHTGMVQVNKEKMSKSLNNFFTVRDVLKEYDAESVRYFLISGHYRSQLNY 304
Cdd:PRK14535  467 QSVGATGhtcghhhaqthhgqsiASHVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNY 546

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 305 SQENLEQARSSLERIYTALRGVTPIECDL--ASNEYVAKFRKAMDDDFNTPEALPVLFELAKELNRVKDSdteqagKLAY 382
Cdd:PRK14535  547 SDAHLDDAKGALTRLYTTLKNTPAAEFMLseNVNDYTRRFYAAMNDDFGTVEAVAVLFELAGEVNKTNDA------QLAG 620

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1859345866 383 VLRSVAEVLGVAQQDPEAFLQGGQADDEVAH--IEALIAKRNEARASKDWAAADEARDALNALGVVLEDSAGKTTWRKA 459
Cdd:PRK14535  621 CLKALGGIIGLLQRDPTEFLQGGAASDGLSNeeIEDLIARRKQARADKNWAESDRIRDLLNEHKIILEDNAGGTTWRRG 699
tRNA-synt_1e pfam01406
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ...
 14-314 0e+00

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


Pssm-ID: 396128 [Multi-domain]  Cd Length: 301  Bit Score: 514.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  14 QFKPLVDGKIDMYVCGITIYDYCHIGHARTFVGFDVIVRYLRHIGYDLKYVRNITDVDDKIIKRANENGESINDLTTRMT 93
Cdd:pfam01406   1 FFVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  94 KAMHEDFDSLNMLRPDVEPTVTNHMDEIIAMVERLIAKGHAYVAADGDVLFDVSTFEQYGALSQQDLTMLQAGSRVEVAQ 173
Cdd:pfam01406  81 EAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVYFDVSSFPDYGKLSGQNLEQLEAGARGEVSE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 174 DKQDPLDFVLWKKAKPEEPSWSSPWGEGRPGWHIECSAMSSKHLGEHFDIHGGGSDLQFPHHENEIAQSCCANNGKYVNT 253
Cdd:pfam01406 161 GKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFDKQLANY 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1859345866 254 WIHTGMVQVNKEKMSKSLNNFFTVRDVLKEYDAESVRYFLISGHYRSQLNYSQENLEQARS 314
Cdd:pfam01406 241 WLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAKS 301
CysRS_core cd00672
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ...
 3-305 3.27e-123

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: 357.27  E-value: 3.27e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866   3 QIYNTLTRQKEQFKPLVDGKIDMYVCGITIYDYCHIGHARTFVGFDVIVRYLRHIGYDLKYVRNITDVDDKIIKRANENG 82
Cdd:cd00672     1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLGYKVRYVQNITDIDDKIIKRAREEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  83 ESINDLTTRMTKAMHEDFDSLNMLRPDVEPTVtnhmdeiiamverliakghayvaadgdvlfdvstfeqygalsqqdltm 162
Cdd:cd00672    81 LSWKEVADYYTKEFFEDMKALNVLPPDVVPRV------------------------------------------------ 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 163 lqagsrvevaqdkqdpldfvlwkkakpeepswsspwgegrpgWHIECSAMSSKHLGEHFDIHGGGSDLQFPHHENEIAQS 242
Cdd:cd00672   113 ------------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQS 150

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1859345866 243 CCANNGKYVNTWIHTGMVQVNKEKMSKSLNNFFTVRDVLKEYDAESVRYFLISGHYRSQLNYS 305
Cdd:cd00672   151 EAATGKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
DALR_2 smart00840
This DALR domain is found in cysteinyl-tRNA-synthetases;
341-393 1.27e-18

This DALR domain is found in cysteinyl-tRNA-synthetases;


Pssm-ID: 214848 [Multi-domain]  Cd Length: 56  Bit Score: 79.15  E-value: 1.27e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1859345866  341 KFRKAMDDDFNTPEALPVLFELAKELNR--VKDSDTEQAGKLAYVLRSVAEVLGV 393
Cdd:smart00840   1 RFEEAMDDDFNTPEALAVLFELAREINRlaLKATDAEELAALAALLRALGGVLGL 55
 
Name Accession Description Interval E-value
CysS COG0215
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ...
 1-459 0e+00

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: 843.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866   1 MVQIYNTLTRQKEQFKPLVDGKIDMYVCGITIYDYCHIGHARTFVGFDVIVRYLRHIGYDLKYVRNITDVDDKIIKRANE 80
Cdd:COG0215     1 TLKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYLGYKVTYVRNITDVDDKIIKRAAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  81 NGESINDLTTRMTKAMHEDFDSLNMLRPDVEPTVTNHMDEIIAMVERLIAKGHAYVAaDGDVLFDVSTFEQYGALSQQDL 160
Cdd:COG0215    81 EGESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEA-DGDVYFDVRSFPDYGKLSGRNL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 161 TMLQAGSRVEVAQDKQDPLDFVLWKKAKPEEPSWSSPWGEGRPGWHIECSAMSSKHLGEHFDIHGGGSDLQFPHHENEIA 240
Cdd:COG0215   160 DDLRAGARVEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 241 QSCCANNGKYVNTWIHTGMVQVNKEKMSKSLNNFFTVRDVLKEYDAESVRYFLISGHYRSQLNYSQENLEQARSSLERIY 320
Cdd:COG0215   240 QSEAATGKPFARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKALERLY 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 321 TALRGVTPI-----ECDLASNEYVAKFRKAMDDDFNTPEALPVLFELAKELNRVKDS--DTEQAGKLAYVLRSVAEVLGV 393
Cdd:COG0215   320 NALRRLEEAlgaadSSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKALDEgeDKAALAALAALLRALGGVLGL 399

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1859345866 394 AQQDPEAFLQGGQADDEVAHIEALIAKRNEARASKDWAAADEARDALNALGVVLEDSAGKTTWRKA 459
Cdd:COG0215   400 LLLEPEAWQGAAEDELLDALIEALIEERAEARKAKDFARADRIRDELAALGIVLEDTPDGTTWRRK 465
cysS TIGR00435
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ...
 4-458 0e+00

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: 656.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866   4 IYNTLTRQKEQFKPLVDGKIDMYVCGITIYDYCHIGHARTFVGFDVIVRYLRHIGYDLKYVRNITDVDDKIIKRANENGE 83
Cdd:TIGR00435   3 LYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLRYLGYKVQYVQNITDIDDKIIKRARENGE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  84 SINDLTTRMTKAMHEDFDSLNMLRPDVEPTVTNHMDEIIAMVERLIAKGHAYVAADGDVLFDVSTFEQYGALSQQDLTML 163
Cdd:TIGR00435  83 SVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVYFDVSKFKDYGKLSKQDLDQL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 164 QAGSRVEVAQDKQDPLDFVLWKKAKPEEPSWSSPWGEGRPGWHIECSAMSSKHLGEHFDIHGGGSDLQFPHHENEIAQSC 243
Cdd:TIGR00435 163 EAGARVDVDEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQSE 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 244 CANNGKYVNTWIHTGMVQVNKEKMSKSLNNFFTVRDVLKEYDAESVRYFLISGHYRSQLNYSQENLEQARSSLERIYTAL 323
Cdd:TIGR00435 243 AAFGKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKNALERLYKAL 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 324 RGVtpiECDLAS------------NEYVAKFRKAMDDDFNTPEALPVLFELAKELNrVKDSDTEQAGKLAYVLRSVAEVL 391
Cdd:TIGR00435 323 RVL---DTSLAYsgnqslnkfpdeKEFEARFVEAMDDDLNTANALAVLFELAKSIN-LTFVSKADAALLIEHLIFLESRL 398

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1859345866 392 GVAQQDPEAFLQGGqADDEVAHIEALIAKRNEARASKDWAAADEARDALNALGVVLEDSAGKTTWRK 458
Cdd:TIGR00435 399 GLLLGLPSKPVQAG-SNDDLGEIEALIEERSIARKEKDFAKADEIRDELAKKGIVLEDTPQGTTWRR 464
cysS PRK14535
cysteinyl-tRNA synthetase; Provisional
 1-459 0e+00

cysteinyl-tRNA synthetase; Provisional


Pssm-ID: 173001 [Multi-domain]  Cd Length: 699  Bit Score: 532.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866   1 MVQIYNTLTRQKEQFKPLVDGKIDMYVCGITIYDYCHIGHARTFVGFDVIVRYLRHIGYDLKYVRNITDVDDKIIKRANE 80
Cdd:PRK14535  227 MTTIYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAE 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  81 NGESINDLTTRMTKAMHEDFDSLNMLRPDVEPTVTNHMDEIIAMVERLIAKGHAYVAADGDVLFDVSTFEQYGALSQQDL 160
Cdd:PRK14535  307 NGETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVYYAVREFAAYGQLSGKSL 386

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 161 TMLQAGSRVEVAQDKQDPLDFVLWKKAKPEEPSWSSPWGEGRPGWHIECSAMSSKHLGEHFDIHGGGSDLQFPHHENEIA 240
Cdd:PRK14535  387 DDLRAGERVEVDGFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIA 466

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 241 QSCCANN----------------GKYVNTWIHTGMVQVNKEKMSKSLNNFFTVRDVLKEYDAESVRYFLISGHYRSQLNY 304
Cdd:PRK14535  467 QSVGATGhtcghhhaqthhgqsiASHVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNY 546

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 305 SQENLEQARSSLERIYTALRGVTPIECDL--ASNEYVAKFRKAMDDDFNTPEALPVLFELAKELNRVKDSdteqagKLAY 382
Cdd:PRK14535  547 SDAHLDDAKGALTRLYTTLKNTPAAEFMLseNVNDYTRRFYAAMNDDFGTVEAVAVLFELAGEVNKTNDA------QLAG 620

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1859345866 383 VLRSVAEVLGVAQQDPEAFLQGGQADDEVAH--IEALIAKRNEARASKDWAAADEARDALNALGVVLEDSAGKTTWRKA 459
Cdd:PRK14535  621 CLKALGGIIGLLQRDPTEFLQGGAASDGLSNeeIEDLIARRKQARADKNWAESDRIRDLLNEHKIILEDNAGGTTWRRG 699
tRNA-synt_1e pfam01406
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ...
 14-314 0e+00

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


Pssm-ID: 396128 [Multi-domain]  Cd Length: 301  Bit Score: 514.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  14 QFKPLVDGKIDMYVCGITIYDYCHIGHARTFVGFDVIVRYLRHIGYDLKYVRNITDVDDKIIKRANENGESINDLTTRMT 93
Cdd:pfam01406   1 FFVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  94 KAMHEDFDSLNMLRPDVEPTVTNHMDEIIAMVERLIAKGHAYVAADGDVLFDVSTFEQYGALSQQDLTMLQAGSRVEVAQ 173
Cdd:pfam01406  81 EAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVYFDVSSFPDYGKLSGQNLEQLEAGARGEVSE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 174 DKQDPLDFVLWKKAKPEEPSWSSPWGEGRPGWHIECSAMSSKHLGEHFDIHGGGSDLQFPHHENEIAQSCCANNGKYVNT 253
Cdd:pfam01406 161 GKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFDKQLANY 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1859345866 254 WIHTGMVQVNKEKMSKSLNNFFTVRDVLKEYDAESVRYFLISGHYRSQLNYSQENLEQARS 314
Cdd:pfam01406 241 WLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAKS 301
PLN02946 PLN02946
cysteine-tRNA ligase
 4-459 3.05e-161

cysteine-tRNA ligase


Pssm-ID: 178532 [Multi-domain]  Cd Length: 557  Bit Score: 467.10  E-value: 3.05e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866   4 IYNTLTRQKEQFKPLVDGKIDMYVCGITIYDYCHIGHARTFVGFDVIVRYLRHIGYDLKYVRNITDVDDKIIKRANENGE 83
Cdd:PLN02946   62 LYNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYLKHLGYEVRYVRNFTDVDDKIIARANELGE 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  84 SINDLTTRMTKAMHEDFDSLNMLRPDVEPTVTNHMDEIIAMVERLIAKGHAYvAADGDVLFDVSTFEQYGALSQQDLTML 163
Cdd:PLN02946  142 DPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAY-RVDGDVYFSVDKFPEYGKLSGRKLEDN 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 164 QAGSRVEVAQDKQDPLDFVLWKKAKPEEPSWSSPWGEGRPGWHIECSAMSSKHLGEHFDIHGGGSDLQFPHHENEIAQSC 243
Cdd:PLN02946  221 RAGERVAVDSRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLVFPHHENEIAQSC 300

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 244 CANNGKYVNTWIHTGMVQVNKEKMSKSLNNFFTVRDVLKEYDAESVRYFLISGHYRSQLNYSQENLEQARSSLERIYTAL 323
Cdd:PLN02946  301 AACCDSNISYWIHNGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDVQLESASERIFYIYQTL 380

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 324 R---------------GVTPIECDLASNEYVAKFRKAMDDDFNTPEALPVLFELAKELN--------RVKDSDTEQAGKL 380
Cdd:PLN02946  381 HdceeslqqhdstfekDSVPPDTLNCINKFHDEFVTSMSDDLHTPVALAALSEPLKTINdllhtrkgKKQEKRLESLAAL 460

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 381 AYVLRSVAEVLG--------VAQQDPEAFLQGGQADDEvaHIEALIAKRNEARASKDWAAADEARDALNALGVVLEDSAG 452
Cdd:PLN02946  461 EKKIRDVLSVLGlmptsyseALQQLREKALRRAKLTEE--QVLQKIEERTVARKNKEYEKSDAIRKDLAAVGIALMDSPD 538


                  ....*..
gi 1859345866 453 KTTWRKA 459
Cdd:PLN02946  539 GTTWRPA 545
cysS PRK14536
cysteinyl-tRNA synthetase; Provisional
 2-458 3.59e-138

cysteinyl-tRNA synthetase; Provisional


Pssm-ID: 184731 [Multi-domain]  Cd Length: 490  Bit Score: 405.84  E-value: 3.59e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866   2 VQIYNTLTRQKEQFKPLVDGKIDMYVCGITIYDYCHIGHARTFVGFDVIVRYLRHIGYDLKYVRNITDV----------D 71
Cdd:PRK14536    3 LRLYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTLHFLGYRVTHVMNITDVghltddadsgE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  72 DKIIKRANENGESINDLTTRMTKAMHEDFDSLNMLRPDVEPTVTNHMDEIIAMVERLIAKGHAYVAAdGDVLFDVSTFEQ 151
Cdd:PRK14536   83 DKMVKSAQEHGKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCAG-GNVYFDIRTFPS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 152 YGALSQQDLTMLQAGSRVEVAQDKQDPLDFVLW-KKAKPEEPS--WSSPWGEGRPGWHIECSAMSSKHLGEHFDIHGGGS 228
Cdd:PRK14536  162 YGSLASAAVEDLQAGARIEHDTNKRNPHDFVLWfTRSKFENHAltWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIGGV 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 229 DLQFPHHENEIAQSCCANNGKYVNTWIHTGMVQVNKEKMSKSLNNFFTVRDVL-KEYDAESVRYFLISGHYRSQLNYSQE 307
Cdd:PRK14536  242 DHIRVHHTNEIAQCEAATGKPWVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQeKGFQPLDYRFFLLGGHYRSQLAFSWE 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 308 NLEQARSSLE-------RIYTALRGVTPI------EC---------DLASNEYVAKFRKAMDDDFNTPEALPVLFELake 365
Cdd:PRK14536  322 ALKTAKAARRslvrrvaRVVDAARATTGSvrgtlaECaaervaesrASESELLLTDFRAALEDDFSTPKALSELQKL--- 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 366 lnrVKDSDTEQAGKLAyVLRSVAEVLGVAQ-QDPEAFLQG-GQADDEVAHIEALIAKRNEARASKDWAAADEARDALNAL 443
Cdd:PRK14536  399 ---VKDTSVPPSLCLS-VLQAMDTVLGLGLiQEATASLSAqVPAGPSEEEIGQLIEARAHARQTKDFPLADEIRDKLKAE 474

                         490
                  ....*....|....*
gi 1859345866 444 GVVLEDSAGKTTWRK 458
Cdd:PRK14536  475 GIELEDTHLGTIWKR 489
PTZ00399 PTZ00399
cysteinyl-tRNA-synthetase; Provisional
 4-456 1.19e-136

cysteinyl-tRNA-synthetase; Provisional


Pssm-ID: 240402 [Multi-domain]  Cd Length: 651  Bit Score: 407.49  E-value: 1.19e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866   4 IYNTLTRQKEQFKPLVDGKIDMYVCGITIYDYCHIGHARTFVGFDVIVRYLR-HIGYDLKYVRNITDVDDKIIKRANENG 82
Cdd:PTZ00399   42 VNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEdYFGYDVFYVMNITDIDDKIIKRAREEK 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  83 -ESINDLTTRMTKAMHEDFDSLNMLRPDVEPTVTNHMDEIIAMVERLIAKGHAYVAaDGDVLFDVSTFEQ----YGALSQ 157
Cdd:PTZ00399  122 lSIFLELARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYES-NGSVYFDVEAFRKaghvYPKLEP 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 158 Q----DLTMLQA-GSRVEVAQDKQDPLDFVLWKKAKPEEPSWSSPWGEGRPGWHIECSAMSSKHLGEHFDIHGGGSDLQF 232
Cdd:PTZ00399  201 EsvadEDRIAEGeGALGKVSGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDLKF 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 233 PHHENEIAQS-CCANNGKYVNTWIHTGMVQVNKEKMSKSLNNFFTVRDVLKEYDAESVRY-FLISgHYRSQLNYSQENLE 310
Cdd:PTZ00399  281 PHHDNELAQSeAYFDKHQWVNYFLHSGHLHIKGLKMSKSLKNFITIRQALSKYTARQIRLlFLLH-KWDKPMNYSDESMD 359

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 311 QARsSLERIYTA--------LRGV---TPIECDLASNEYVAKFRKAMD-------DDFNTPEALPVLFELAKELNRV--- 369
Cdd:PTZ00399  360 EAI-EKDKVFFNffanvkikLRESeltSPQKWTQHDFELNELFEETKSavhaallDNFDTPEALQALQKLISATNTYlns 438

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 370 -KDSDTEQAGKLAYVLRSVAEVLGVAQQDPEAFLQGGQADDEVAH--IEALIAKR----NEARASKDWA----------- 431
Cdd:PTZ00399  439 gEQPSAPLLRSVAQYVTKILSIFGLVEGSDGLGSQGQNSTSENFKplLEALLRFRdevrDAAKAEMKLIsldkkkkqllq 518

                         490       500
                  ....*....|....*....|....*..
gi 1859345866 432 AADEARD-ALNALGVVLED-SAGKTTW 456
Cdd:PTZ00399  519 LCDKLRDeWLPNLGIRIEDkPDGPSVW 545
CysRS_core cd00672
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ...
 3-305 3.27e-123

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: 357.27  E-value: 3.27e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866   3 QIYNTLTRQKEQFKPLVDGKIDMYVCGITIYDYCHIGHARTFVGFDVIVRYLRHIGYDLKYVRNITDVDDKIIKRANENG 82
Cdd:cd00672     1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLGYKVRYVQNITDIDDKIIKRAREEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  83 ESINDLTTRMTKAMHEDFDSLNMLRPDVEPTVtnhmdeiiamverliakghayvaadgdvlfdvstfeqygalsqqdltm 162
Cdd:cd00672    81 LSWKEVADYYTKEFFEDMKALNVLPPDVVPRV------------------------------------------------ 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 163 lqagsrvevaqdkqdpldfvlwkkakpeepswsspwgegrpgWHIECSAMSSKHLGEHFDIHGGGSDLQFPHHENEIAQS 242
Cdd:cd00672   113 ------------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQS 150

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1859345866 243 CCANNGKYVNTWIHTGMVQVNKEKMSKSLNNFFTVRDVLKEYDAESVRYFLISGHYRSQLNYS 305
Cdd:cd00672   151 EAATGKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
PRK12418 PRK12418
cysteinyl-tRNA synthetase; Provisional
 25-394 7.61e-105

cysteinyl-tRNA synthetase; Provisional


Pssm-ID: 183518 [Multi-domain]  Cd Length: 384  Bit Score: 316.87  E-value: 7.61e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  25 MYVCGITIYDYCHIGHARTFVGFDVIVRYLRHIGYDLKYVRNITDVDDKIIKRANENGESINDLTTRMTKAMHEDFDSLN 104
Cdd:PRK12418   12 MYVCGITPYDATHLGHAATYLAFDLVNRVWRDAGHDVHYVQNVTDVDDPLLERAARDGVDWRDLAEREIALFREDMEALR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 105 MLRPDVEPTVTNHMDEIIAMVERLIAKGHAYVAAD---GDVLFDVSTFEQYGALSQQDL-TMLQ-----------AGsrv 169
Cdd:PRK12418   92 VLPPRDYVGAVESIPEVVELVEKLLASGAAYVVDDeeyPDVYFSVDATPQFGYESGYDRaTMLElfaerggdpdrPG--- 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 170 evaqdKQDPLDFVLWKKAKPEEPSWSSPWGEGRPGWHIECSAMSSKHLGEHFDIHGGGSDLQFPHHENEIAQSCCANNG- 248
Cdd:PRK12418  169 -----KRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAHAEAATGEr 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 249 KYVNTWIHTGMVQVNKEKMSKSLNNFFTVRDVLKE-YDAESVRYFLISGHYRSQLNYSQENLEQARSSLERIYTALRGVT 327
Cdd:PRK12418  244 RFARHYVHAGMIGLDGEKMSKSRGNLVFVSRLRAAgVDPAAIRLALLAGHYRADREWTDAVLAEAEARLARWRAAAALPA 323

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1859345866 328 PIECDlasnEYVAKFRKAMDDDFNTPEALPVLFELAkELNRVKDSDTEQAGKLayVLRSVAEVLGVA 394
Cdd:PRK12418  324 GPDAA----DVVARVRAALADDLDTPGALAAVDGWA-TDALEGGGDDAAAPAL--VATAVDALLGVA 383
mycothiol_MshC TIGR03447
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ...
 2-394 1.04e-103

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: 314.74  E-value: 1.04e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866   2 VQIYNTLTRQkeqFKPL-VDGKIDMYVCGITIYDYCHIGHARTFVGFDVIVRYLRHIGYDLKYVRNITDVDDKIIKRANE 80
Cdd:TIGR03447  18 LRLFDTADGQ---VRPVePGPEAGMYVCGITPYDATHLGHAATYLTFDLVNRVWRDAGHRVHYVQNVTDVDDPLFERAER 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  81 NGESINDLTTRMTKAMHEDFDSLNMLRPDVEPTVTNHMDEIIAMVERLIAKGHAYV---AADGDVLFDVSTFEQYGALSQ 157
Cdd:TIGR03447  95 DGVDWRELGTSQIDLFREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYIvegPEYPDVYFSIDATEQFGYESG 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 158 QD-LTMLQAGSrvEVAQD-----KQDPLDFVLWKKAKPEEPSWSSPWGEGRPGWHIECSAMSSKHLGEHFDIHGGGSDLQ 231
Cdd:TIGR03447 175 YDrATMLELFA--ERGGDpdrpgKRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSDLI 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 232 FPHHENEIAQSCCANNG-KYVNTWIHTGMVQVNKEKMSKSLNNFFTVRDVLKE-YDAESVRYFLISGHYRSQLNYSQENL 309
Cdd:TIGR03447 253 FPHHEFSAAHAEAATGVrRMARHYVHAGMIGLDGEKMSKSLGNLVFVSKLRAAgVDPAAIRLGLLAGHYRQDRDWTDAVL 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 310 EQARSSLERIYTALrGVTPIEcdlASNEYVAKFRKAMDDDFNTPEALPVLFELAKELNRVKDSDTEQAGKLAyvlRSVAE 389
Cdd:TIGR03447 333 AEAEARLARWRAAL-ALPDAP---DATDLIARLRQHLANDLDTPAALAAVDGWAADALSYGGSDTEAPALVA---TAVDA 405


                  ....*
gi 1859345866 390 VLGVA 394
Cdd:TIGR03447 406 LLGVR 410
Anticodon_Ia_Cys cd07963
Anticodon-binding domain of cysteinyl tRNA synthetases; This domain is found in cysteinyl tRNA ...
 306-458 1.72e-79

Anticodon-binding domain of cysteinyl tRNA synthetases; This domain is found in cysteinyl tRNA synthetases (CysRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. CysRS catalyzes the transfer of cysteine to the 3'-end of its tRNA.


Pssm-ID: 153417 [Multi-domain]  Cd Length: 156  Bit Score: 243.62  E-value: 1.72e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 306 QENLEQARSSLERIYTALRGVTPIECDLA-SNEYVAKFRKAMDDDFNTPEALPVLFELAKELNRVKDSDTEQAGKLAYVL 384
Cdd:cd07963     1 DDNLEDARAALERLYTALRGVPPTTVDIDwGEPFAERFIAAMDDDFNTPEALAVLFELAREINRLKKEDIEKAAALAALL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1859345866 385 RSVAEVLGVAQQDPEAFLQGGQ--ADDEVAHIEALIAKRNEARASKDWAAADEARDALNALGVVLEDSAGKTTWRK 458
Cdd:cd07963    81 KALGGVLGLLQQDPEAFLQGGTgeGGLSVAEIEALIAQRNQARKAKDWAEADRIRDELAAQGIILEDSPEGTTWRR 156
cysS PRK14534
cysteinyl-tRNA synthetase; Provisional
 1-450 2.36e-76

cysteinyl-tRNA synthetase; Provisional


Pssm-ID: 173000 [Multi-domain]  Cd Length: 481  Bit Score: 246.69  E-value: 2.36e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866   1 MVQIYNTLTRQKEQFKPLVDGKIdmYVCGITIYDYCHIGHARTFVGFDVIVRYLRHIGYDLKYVRNITDV---------- 70
Cdd:PRK14534    2 LLKLYNTKTKDLSELKNFSDVKV--YACGPTVYNYAHIGNFRTYIFEDLLIKSLRLLKYNVNYAMNITDIghltgdfddg 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  71 DDKIIKRANENGESINDLTTRMTKAMHEDFDSLNMLRPDVEPTVTNHMDEIIAMVERLIAKGHAYVAaDGDVLFDVSTFE 150
Cdd:PRK14534   80 EDKVVKAARERGLTVYEISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTYFV-NGNVYFDTSCFK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 151 QYGALSQQDLTMLQ--AGSRVEVAQDKQDPLDFVLW---KKAKPEEPSWSSPWGEGRPGWHIECSAMSSKHLGEHFDIHG 225
Cdd:PRK14534  159 SYGQMAGINLNDFKdmSVSRVEIDKSKRNKSDFVLWftnSKFKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKSTLDIHL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 226 GGSDLQFPHHENEIAQSCCANNGKYVNTWIHTGMVQVNKEKMSKSLNNFFTVRDVLKE-YDAESVRYFLISGHYRSQLNY 304
Cdd:PRK14534  239 GGVDHIGVHHINEIAIAECYLNKKWCDMFVHGEFLIMEYEKMSKSNNNFITIKDLEDQgFSPLDFRYFCLTAHYRTQLKF 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 305 SQENLEQARSSLERIYTAL----RGVTPIECDLAS-----------NEYVAKFRKAMDDDFNTPEALPVLFELakelnrV 369
Cdd:PRK14534  319 TFNNLKACKIARENMLNKLtyfySSLDQFDLNLLNkdleniefsleKEYYDSFLEKIAFDLNIPQGLALLWDI------I 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 370 KDSDTEQAGKLAYVLRsVAEVLGVAQQdpEAFLQGGQADDEVA--HIEALIAKRNEARASKDWAAADEARDALNALGVVL 447
Cdd:PRK14534  393 KDDNLSFLSKLRLAFK-FDEVLSLGLR--EEILREIENHRIVIddNMKSLIEERRLAKCEKDFKRADEIREYFASKGFVL 469


                  ...
gi 1859345866 448 EDS 450
Cdd:PRK14534  470 IDT 472
DALR_2 pfam09190
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases.
 341-402 1.06e-25

DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases.


Pssm-ID: 462711 [Multi-domain]  Cd Length: 63  Bit Score: 99.20  E-value: 1.06e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1859345866 341 KFRKAMDDDFNTPEALPVLFELAKELNR-VKDSDTEQAGKLAYVLRSVAEVLGVAQQDPEAFL 402
Cdd:pfam09190   1 KFIEAMDDDFNTPEALAVLFELAKEINRaLKTNDAEAAAALAALLRELGDVLGLLQQDPEAFL 63
class_I_aaRS_core cd00802
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ...
 25-271 1.15e-23

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: 96.39  E-value: 1.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  25 MYVCGITIYDYCHIGHARTFVGFDVIVRYLRHIGYDLKYVRNITDVDDKIIKRANENGESINdlttrmtkamhedfdsln 104
Cdd:cd00802     1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAK------------------ 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 105 mlrpdveptvtnhmdeiiAMVERLIAKGHayvaadgdvlfdvstfEQYgalsqqdltmlqagsrvevaqdkqdpldfvlw 184
Cdd:cd00802    63 ------------------AFVERWIERIK----------------EDV-------------------------------- 76

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 185 kkakpeepswsspwgegrpGWHIECSAMSSKHLGEHFDIHGGGSDLQFpHHENEIAQSCCAnNGKYVNTWIHTGMVQV-N 263
Cdd:cd00802    77 -------------------EYMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKA-GGPARPFGLTFGRVMGaD 135


                  ....*...
gi 1859345866 264 KEKMSKSL 271
Cdd:cd00802   136 GTKMSKSK 143
DALR_2 smart00840
This DALR domain is found in cysteinyl-tRNA-synthetases;
341-393 1.27e-18

This DALR domain is found in cysteinyl-tRNA-synthetases;


Pssm-ID: 214848 [Multi-domain]  Cd Length: 56  Bit Score: 79.15  E-value: 1.27e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1859345866  341 KFRKAMDDDFNTPEALPVLFELAKELNR--VKDSDTEQAGKLAYVLRSVAEVLGV 393
Cdd:smart00840   1 RFEEAMDDDFNTPEALAVLFELAREINRlaLKATDAEELAALAALLRALGGVLGL 55
Anticodon_Ia_Cys_like cd07955
Anticodon-binding domain of cysteinyl tRNA synthetases and domain found in MshC; This domain ...
 307-393 4.39e-14

Anticodon-binding domain of cysteinyl tRNA synthetases and domain found in MshC; This domain is found in cysteinyl tRNA synthetases (CysRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. CysRS catalyzes the transfer of cysteine to the 3'-end of its tRNA. The family also includes a domain of MshC, the rate-determining enzyme in the mycothiol biosynthetic pathway, which is specific to actinomycetes. The anticodon-binding site of CysRS lies C-terminal to this model's footprint and is not shared by MshC.


Pssm-ID: 153409 [Multi-domain]  Cd Length: 81  Bit Score: 67.46  E-value: 4.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 307 ENLEQARSSLERIYTALRGVTPIECDlasnEYVAKFRKAMDDDFNTPEALPVLFELAKElnrVKDSDTEQAGKLAYVLRS 386
Cdd:cd07955     2 EVLADAEARLARWRSAVALPDGPDAE----ALVARLREALADDLDTPKALAALDAWARE---ALSRGGTDPDAPALVRTA 74


                  ....*..
gi 1859345866 387 VAEVLGV 393
Cdd:cd07955    75 VDALLGV 81
Ile_Leu_Val_MetRS_core cd00668
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ...
 37-296 4.55e-14

catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases. These class I enzymes are all monomers. However, in some species, MetRS functions as a homodimer, as a result of an additional C-terminal domain. These enzymes aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. Enzymes in this subfamily share an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. MetRS has a significantly shorter insertion, which lacks the editing function.


Pssm-ID: 185674 [Multi-domain]  Cd Length: 312  Bit Score: 72.84  E-value: 4.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  37 HIGHARTFVGFDVIVRYLRHIGYDLKY--------------VRNITDVDDKIIKRANENGESINdLTTRMTKAMHEDFDS 102
Cdd:cd00668    16 HLGHALTHIIADFIARYKRMRGYEVPFlpgwdthglpielkAERKGGRKKKTIWIEEFREDPKE-FVEEMSGEHKEDFRR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 103 LNmLRPDVEPTVTNHMDEIIAMVER---------LIAKGHAYVAADGDVLFDVSTFEQYGALSQQDLTMLQAGSRVEVAQ 173
Cdd:cd00668    95 LG-ISYDWSDEYITTEPEYSKAVELifsrlyekgLIYRGTHPVRITEQWFFDMPKFKEKLLKALRRGKIVPEHVKNRMEA 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 174 DKQDPLDFVLWKKAkpeepswssPWGEGRPGWHIEC---------SAMSSKHLGEHF------DIHGGGSDLQFPHHENE 238
Cdd:cd00668   174 WLESLLDWAISRQR---------YWGTPLPEDVFDVwfdsgigplGSLGYPEEKEWFkdsypaDWHLIGKDILRGWANFW 244

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 239 IAQSCCAN-NGKYVNTWIHtGMVQVNK-EKMSKSLNNFFTVRDVLKEYDAESVRYFLISG 296
Cdd:cd00668   245 ITMLVALFgEIPPKNLLVH-GFVLDEGgQKMSKSKGNVIDPSDVVEKYGADALRYYLTSL 303
PRK11893 PRK11893
methionyl-tRNA synthetase; Reviewed
 37-391 2.33e-13

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237012 [Multi-domain]  Cd Length: 511  Bit Score: 71.84  E-value: 2.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  37 HIGHARTFVGFDVIVRYLRHIGYDlkyVRNITDVDD---KIIKRANENGESINDLTTRMTKAMHEDFDSLNmLRPD--VE 111
Cdd:PRK11893   17 HIGHAYTTLAADVLARFKRLRGYD---VFFLTGTDEhgqKIQRKAEEAGISPQELADRNSAAFKRLWEALN-ISYDdfIR 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 112 PTVTNHMDEIIAMVERLIAKGHAYVAA------DGDVLF----DVSTFEQYGALSQQDLTMLQAGS---RVEVAQDK--- 175
Cdd:PRK11893   93 TTDPRHKEAVQEIFQRLLANGDIYLGKyegwycVRCEEFytesELIEDGYRCPPTGAPVEWVEEESyffRLSKYQDKlle 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 176 --QDPLDFVLWKKAKPEEPSWSSP-------------WGEGRPGwhiecsamSSKH------------------------ 216
Cdd:PRK11893  173 lyEANPDFIQPASRRNEVISFVKSglkdlsisrtnfdWGIPVPG--------DPKHviyvwfdaltnyltalgypddeel 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 217 LGEHF------DIHGGGSDLQFPHheneiaqscC--------ANNGK-----YVNTWIHtgmvqVNKEKMSKSLNNFFTV 277
Cdd:PRK11893  245 LAELFnkywpaDVHLIGKDILRFH---------AvywpaflmAAGLPlpkrvFAHGFLT-----LDGEKMSKSLGNVIDP 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 278 RDVLKEYDAESVRYFLIS----------------GHYRSQLNYSQENLEQARSSLERIYTALRGVTPIECDLA------- 334
Cdd:PRK11893  311 FDLVDEYGVDAVRYFLLReipfgqdgdfsreafiNRINADLANDLGNLAQRTLSMIAKNFDGKVPEPGALTEAdeallea 390

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1859345866 335 SNEYVAKFRKAMDD-DFNtpEALPVLFELAKELNR---------VKDSDTEqagKLAYVLRSVAEVL 391
Cdd:PRK11893  391 AAALLERVRAAMDNlAFD--KALEAILALVRAANKyideqapwsLAKTDPE---RLATVLYTLLEVL 452
MetG COG0143
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ...
 37-391 5.10e-12

Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439913 [Multi-domain]  Cd Length: 544  Bit Score: 67.83  E-value: 5.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  37 HIGHARTFVGFDVIVRYLRHIGYDLKYVrniTDVDD---KIIKRANENGESINDLTTRMTKAMHEDFDSLNM-----LRP 108
Cdd:COG0143    17 HIGHLYTYIPADILARYQRLRGHDVLFV---TGTDEhgtKIELAAEKEGITPQELVDRIHAEFKELFEKLGIsfdnfIRT 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 109 DvEPtvtNHMDEIIAMVERLIAKGHAYVAADgDVLFDVS--TF----------------EQYGAL-----SQQDLTMLQA 165
Cdd:COG0143    94 T-SP---EHKELVQEIFQRLYDNGDIYKGEY-EGWYCPEceRFlpdryvegtcpkcgaeDAYGDQcencgATLEPTELIN 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 166 ------GSRVEVAQDK---------QDPL-DFVlwkKAKPE-EP-------SW------------SSPWG---EGRPG-- 204
Cdd:COG0143   169 prsaisGAPPELREEEhyffrlskyQDRLlEWI---EENPDiQPevrnevlSWlkeglqdlsisrDFDWGipvPGDPGkv 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 205 ---WhIEcsA----MSSkhLGEHFDIHGGGSDLQ--FPhheneiaqsccANNGKYV------NTWIHT------------ 257
Cdd:COG0143   246 fyvW-FD--AligyISA--TKGYADDRGLPEDFEkyWP-----------APDTELVhfigkdIIRFHAiiwpamlmaagl 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 258 ---------GMVQVNKEKMSKSLNNFFTVRDVLKEYDAESVRYFLIS-GHYRSQLNYSQENLEQ-------------ARS 314
Cdd:COG0143   310 plpkkvfahGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLReVPFGQDGDFSWEDFVArvnsdlandlgnlASR 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 315 SLERIYTALRGVTP--IECDLASNEYVAKFRKAMD------DDFNTPEALPVLFELAKELNR----------VKDSDTEQ 376
Cdd:COG0143   390 TLSMIHKYFDGKVPepGELTEADEELLAEAEAALEevaeamEAFEFRKALEEIMALARAANKyidetapwklAKDEDPER 469

                         490
                  ....*....|....*....
gi 1859345866 377 AGK----LAYVLRSVAEVL 391
Cdd:COG0143   470 LATvlytLLEALRILAILL 488
leuS PRK12300
leucyl-tRNA synthetase; Reviewed
 258-390 5.75e-12

leucyl-tRNA synthetase; Reviewed


Pssm-ID: 237049 [Multi-domain]  Cd Length: 897  Bit Score: 67.97  E-value: 5.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 258 GMVQVNKEKMSKSLNNFFTVRDVLKEYDAESVRYFL-ISGHYRSQLNYSQENLEQARSSLERIYTALRGVTPIECD---- 332
Cdd:PRK12300  569 GFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLtSSAELLQDADWREKEVESVRRQLERFYELAKELIEIGGEeelr 648

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 333 -----LAS--NEYVAKFRKAMdDDFNTPEAL-PVLFELAKELN----RVKDSDTeqagklaYVLRSVAEV 390
Cdd:PRK12300  649 fidkwLLSrlNRIIKETTEAM-ESFQTRDAVqEAFYELLNDLRwylrRVGEANN-------KVLREVLEI 710
tRNA-synt_1g pfam09334
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
 37-295 1.18e-07

tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.


Pssm-ID: 401322 [Multi-domain]  Cd Length: 387  Bit Score: 53.45  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  37 HIGHARTFVGFDVIVRYLRHIGYDlkyVRNITDVDD---KIIKRANENGESINDLTTRMTKAMHEDFDSLNMLRPDVEPT 113
Cdd:pfam09334  15 HLGHLYSYIPADIFARYLRLRGYD---VLFVCGTDEhgtPIELKAEKEGITPEELVDRYHEIHREDFKKFNISFDDYGRT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 114 VT-NHMDEIIAMVERLIAKGHAYVAADgDVLFDVSTfEQYgaLSQQDLTM--------LQAGSRVEVAQDKQDPLDFVLW 184
Cdd:pfam09334  92 TSeRHHELVQEFFLKLYENGYIYEKEI-EQFYCPSD-ERF--LPDRYVEGtcphcgseDARGDQCENCGRHLEPTELINP 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 185 K----KAKPE---EPSWSSP----------W-GEGRPGWHIECSAMSSKHLGEHF-------DIHGGgsdLQFPHHENEI 239
Cdd:pfam09334 168 KcvicGTTPEvkeTEHYFFDlskfqdklreWiEENNPEWPENVKNMVLEWLKEGLkdraisrDLDWG---IPVPGAEGKV 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 240 -------------AQSCCANNGKYVNTW---------IH-------------------------------TGMVQVNKEK 266
Cdd:pfam09334 245 fyvwldapigyisATKELSGNEEKWKEWwpndpdtelVHfigkdiiyfhtifwpamllgagyrlpttvfaHGYLTYEGGK 324

                         330       340
                  ....*....|....*....|....*....
gi 1859345866 267 MSKSLNNFFTVRDVLKEYDAESVRYFLIS 295
Cdd:pfam09334 325 MSKSRGNVVWPSEALDRFPPDALRYYLAR 353
LeuRS_core cd00812
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ...
 255-295 2.67e-07

catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.


Pssm-ID: 173906 [Multi-domain]  Cd Length: 314  Bit Score: 52.25  E-value: 2.67e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1859345866 255 IHTGMVQVNKEKMSKSLNNFFTVRDVLKEYDAESVRYFLIS 295
Cdd:cd00812   264 IVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLYILF 304
MetRS_core cd00814
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ...
 37-295 8.15e-07

catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function.


Pssm-ID: 173907 [Multi-domain]  Cd Length: 319  Bit Score: 50.61  E-value: 8.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  37 HIGHARTFVGFDVIVRYLRHIGYDLKYVrniTDVDD---KIIKRANENGESINDLTTRMTKAMHEDFDSLNM-----LRP 108
Cdd:cd00814    16 HLGHLYGTVLADVFARYQRLRGYDVLFV---TGTDEhgtKIEQKAEEEGVTPQELCDKYHEIFKDLFKWLNIsfdyfIRT 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 109 DVEptvtNHMDEIIAMVERLIAKGH--------AYVAADGDVL----------FDVSTFEQY--------GALSQQD--- 159
Cdd:cd00814    93 TSP----RHKEIVQEFFKKLYENGYiyegeyegLYCVSCERFLpewreeehyfFRLSKFQDRllewleknPDFIWPEnar 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 160 ---LTMLQAG------SR------VEVAQDKQ-------D-PLDFV----LWKKAKPEEPSWSSPWGEgrpgwhiecsam 212
Cdd:cd00814   169 nevLSWLKEGlkdlsiTRdlfdwgIPVPLDPGkviyvwfDaLIGYIsatgYYNEEWGNSWWWKDGWPE------------ 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 213 sskhlgehfDIHGGGSDLqFPHHeneiaqscC--------ANNGKYVNTWIHTGMVQVNKEKMSKSLNNFFTVRDVLKEY 284
Cdd:cd00814   237 ---------LVHFIGKDI-IRFH--------AiywpamllGAGLPLPTRIVAHGYLTVEGKKMSKSRGNVVDPDDLLERY 298

                         330
                  ....*....|.
gi 1859345866 285 DAESVRYFLIS 295
Cdd:cd00814   299 GADALRYYLLR 309
valS TIGR00422
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ...
 257-391 1.54e-06

valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase and is particularly closely related to the isoleucyl tRNA synthetase. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273070 [Multi-domain]  Cd Length: 861  Bit Score: 50.83  E-value: 1.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 257 TGMVQ-VNKEKMSKSLNNFFTVRDVLKEYDAESVRYFLISGHYRSQ-LNYSQENLEQARSSLERIYTALRGV-------- 326
Cdd:TIGR00422 515 HGLVRdEQGRKMSKSLGNVIDPLDVIEKYGADALRFTLASLVTPGDdINFDWKRVESARNFLNKLWNASRFVlmnlsddl 594

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 327 ---------TPIECDLAS--NEYVAKFRKAMDD-DFNTPEALPVLF----------ELAKELNRVKDSDTEQAGK--LAY 382
Cdd:TIGR00422 595 elsggeeklSLADRWILSklNRTIKEVRKALDKyRFAEAAKALYEFiwndfcdwyiELVKYRLYNGNEAEKKAARdtLYY 674


                  ....*....
gi 1859345866 383 VLRSVAEVL 391
Cdd:TIGR00422 675 VLDKALRLL 683
metG TIGR00398
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ...
 26-393 2.24e-06

methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model appears to recognize the methionyl-tRNA synthetase of every species, including eukaryotic cytosolic and mitochondrial forms. The UPGMA difference tree calculated after search and alignment according to this model shows an unusual deep split between two families of MetG. One family contains forms from the Archaea, yeast cytosol, spirochetes, and E. coli, among others. The other family includes forms from yeast mitochondrion, Synechocystis sp., Bacillus subtilis, the Mycoplasmas, Aquifex aeolicus, and Helicobacter pylori. The E. coli enzyme is homodimeric, although monomeric forms can be prepared that are fully active. Activity of this enzyme in bacteria includes aminoacylation of fMet-tRNA with Met; subsequent formylation of the Met to fMet is catalyzed by a separate enzyme. Note that the protein from Aquifex aeolicus is split into an alpha (large) and beta (small) subunit; this model does not include the C-terminal region corresponding to the beta chain. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273058 [Multi-domain]  Cd Length: 530  Bit Score: 50.07  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  26 YVCGITiydycHIGHARTFVGFDVIVRYLRHIGYDlkyVRNITDVDD---KIIKRANENGESINDLTTRMTKAMHEDFDS 102
Cdd:TIGR00398   9 YANGKP-----HLGHAYTTILADVYARYKRLRGYE---VLFVCGTDEhgtKIELKAEQEGLTPKELVDKYHEEFKDDWKW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 103 LNMLRPDVEPTVT-NHMDEIIAMVERLIAKGH--------AYVAADGDVLFDvsTFEQYGALSQQDLTMLqaGSRVEVAQ 173
Cdd:TIGR00398  81 LNISFDRFIRTTDeEHKEIVQKIFQKLKENGYiyekeikqLYCPECEMFLPD--RYVEGTCPKCGSEDAR--GDHCEVCG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 174 DKQDPLDFVLWK----KAKPEE----------PSWSSP---WGEGRPgwhiECSAMSS--KHLGEHFdIHGGGSDL---- 230
Cdd:TIGR00398 157 RHLEPTELINPRckicGAKPELrdsehyffrlSAFEKEleeWIRKNP----ESGSPASnvKNKAQNW-LKGGLKDLaitr 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 231 -------QFPHHENE------------IAQSCCANNG--KYVNTW--------IH------------------------- 256
Cdd:TIGR00398 232 dlvywgiPVPNDPNKvvyvwfdaligyISSLGILSGDteDWKKWWnndedaelIHfigkdivrfhtiywpamlmglglpl 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 257 ------TGMVQVNKEKMSKSLNNFFTVRDVLKEYDAESVRYFLISGHYRSQ-LNYSQENLEQARSS---------LER-- 318
Cdd:TIGR00398 312 ptqvfsHGYLTVEGGKMSKSLGNVVDPSDLLARFGADILRYYLLKERPLGKdGDFSWEDFVERVNAdlanklgnlLNRtl 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 319 --IYTALRGVTPI--ECDLASNEYVAKFRKAMD------DDFNTPEALPVLFELAKELNR--------VKDSDTEQAGKL 380
Cdd:TIGR00398 392 gfIKKYFNGVLPSedITDEEDKKLLKLINEALEqideaiESFEFRKALREIMKLADRGNKyidenkpwELFKQSPRLKEL 471

                         490
                  ....*....|...
gi 1859345866 381 AYVLRSVAEVLGV 393
Cdd:TIGR00398 472 LAVCSMLIRVLSI 484
metG PRK00133
methionyl-tRNA synthetase; Reviewed
 257-436 2.64e-06

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 49.76  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 257 TGMVQVNKEKMSKSLNNFFTVRDVLKEYDAESVRYFLIS--GHYRSQLNYSQENLeQARS--------------SLERIY 320
Cdd:PRK00133  320 HGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAAklPETIDDLDFNWEDF-QQRVnselvgkvvnfasrTAGFIN 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 321 TALRGVTPieCDLASNEYVAKFRKAMD------DDFNTPEALPVLFELAKELNR---------VKDSDTEQAGK------ 379
Cdd:PRK00133  399 KRFDGKLP--DALADPELLEEFEAAAEkiaeayEAREFRKALREIMALADFANKyvddnepwkLAKQDGERLQAvcsvgl 476

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 380 -----LAYVLRSV--------AEVLGVAQ---QDPEAFLQGGQADD--------EVAHIEALIAKRNEARASKDWAAADE 435
Cdd:PRK00133  477 nlfraLAIYLKPVlpelaeraEAFLNLEEltwDDAQQPLAGHPINKfkilftriEDKQIEALIEASKEAAAAKAAAAAAA 556


                  .
gi 1859345866 436 A 436
Cdd:PRK00133  557 A 557
IleS COG0060
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ...
 266-324 3.12e-06

Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439830 [Multi-domain]  Cd Length: 931  Bit Score: 49.69  E-value: 3.12e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1859345866 266 KMSKSLNNFFTVRDVLKEYDAESVRYFLISGHYRSQLNYSQENLEQARSSLERIYTALR 324
Cdd:COG0060   603 KMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEILKEVRDVYRRLRNTYR 661
lysK PRK00750
lysyl-tRNA synthetase; Reviewed
 263-294 1.98e-04

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 234829 [Multi-domain]  Cd Length: 510  Bit Score: 43.65  E-value: 1.98e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1859345866 263 NKEKMSKSLNNFFTVRDVLKEYDAESVRYFLI 294
Cdd:PRK00750  277 KGEKISKSKGNVITIEDWLEYAPPESLRLFMF 308
PLN02959 PLN02959
aminoacyl-tRNA ligase
 258-293 2.11e-04

aminoacyl-tRNA ligase


Pssm-ID: 215518 [Multi-domain]  Cd Length: 1084  Bit Score: 43.90  E-value: 2.11e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1859345866  258 GMVQVNKEKMSKSLNNFFTVRDVLKEYDAESVRYFL 293
Cdd:PLN02959   710 GHLMLNSEKMSKSTGNFLTLRQAIEEFSADATRFAL 745
argS PRK01611
arginyl-tRNA synthetase; Reviewed
 37-149 2.24e-04

arginyl-tRNA synthetase; Reviewed


Pssm-ID: 234964 [Multi-domain]  Cd Length: 507  Bit Score: 43.61  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  37 HIGHAR-TFVGfDVIVRYLRHIGYDLkYVRNItdVDD-------------KIIKRANEngesindlttRMTKAMHEDFDS 102
Cdd:PRK01611  127 HVGHLRsAVIG-DALARILEFAGYDV-TREYY--VNDagtqigmliasleLLWRKAVD----------ISLDEIKEDLDR 192

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1859345866 103 LNmlrpdVEPTVTNHMDEII------AMVERLIAKGHAYVAADGDVLFDVSTF 149
Cdd:PRK01611  193 LG-----VHFDVWFSESELYyngkvdEVVEDLKEKGLLYVESDGALWVRLTEF 240
Anticodon_Ia_like cd07375
Anticodon-binding domain of class Ia aminoacyl tRNA synthetases and similar domains; This ...
 307-391 2.92e-04

Anticodon-binding domain of class Ia aminoacyl tRNA synthetases and similar domains; This domain is found in a variety of class Ia aminoacyl tRNA synthetases, C-terminal to the catalytic core domain. It recognizes and specifically binds to the anticodon of the tRNA. Aminoacyl tRNA synthetases catalyze the transfer of cognate amino acids to the 3'-end of their tRNAs by specifically recognizing cognate from non-cognate amino acids. Members include valyl-, leucyl-, isoleucyl-, cysteinyl-, arginyl-, and methionyl-tRNA synthethases. This superfamily also includes a domain from MshC, an enzyme in the mycothiol biosynthetic pathway.


Pssm-ID: 153408 [Multi-domain]  Cd Length: 117  Bit Score: 40.57  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866 307 ENLEQARSSLERIYTALRGV----------------TPIECDLAS--NEYVAKFRKAMDDdFNTPEALPVLFELAKELNR 368
Cdd:cd07375     2 ERLKQARAFLNRLYRLLSFFrkalggtqpkwdnellEEADRELLArlQEFIKRTTNALEA-LDPTTAVQELFKFTNELNW 80

                          90       100
                  ....*....|....*....|....*....
gi 1859345866 369 VKDSD------TEQAGKLAYVLRSVAEVL 391
Cdd:cd07375    81 YLDELkpalqtEELREAVLAVLRAALVVL 109
metG PRK00133
methionyl-tRNA synthetase; Reviewed
 36-104 5.11e-04

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 42.45  E-value: 5.11e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1859345866  36 CHIGHARTFVGFDVIVRYLRHIGYDLKYVRNitdvDDK----IIKRANENGESINDLTTRMTKAMHEDFDSLN 104
Cdd:PRK00133   17 IHLGHLVEYIQADIWVRYQRMRGHEVLFVCA----DDAhgtpIMLKAEKEGITPEELIARYHAEHKRDFAGFG 85
PRK12267 PRK12267
methionyl-tRNA synthetase; Reviewed
 30-84 7.80e-04

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237028 [Multi-domain]  Cd Length: 648  Bit Score: 42.09  E-value: 7.80e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1859345866  30 IT--IY---DYCHIGHARTFVGFDVIVRYLRHIGYDLKYVrniTDVD---DKIIKRANENGES 84
Cdd:PRK12267    8 ITtpIYypnGKPHIGHAYTTIAADALARYKRLQGYDVFFL---TGTDehgQKIQQAAEKAGKT 67
tRNA-synt_1c pfam00749
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ...
 35-137 7.91e-04

tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).


Pssm-ID: 395606 [Multi-domain]  Cd Length: 314  Bit Score: 41.54  E-value: 7.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859345866  35 YCHIGHARTfvgfdVIVRYL--RHIGYDLkYVRnitdVDDKIIKRANENGEsindlttrmtKAMHEDFDSLNmLRPDVEP 112
Cdd:pfam00749  13 YLHIGHAKA-----ALFNYLyaKNHNGKF-ILR----FEDTDPERETPEFE----------ESILEDLKWLG-IKWDYGP 71

                          90       100
                  ....*....|....*....|....*.
gi 1859345866 113 T-VTNHMDEIIAMVERLIAKGHAYVA 137
Cdd:pfam00749  72 YyQSDRFDIYYKYAEELIKKGKAYVC 97
LysRS_core_class_I cd00674
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) ...
 263-295 8.28e-04

catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) 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. The class I LysRS is found only in archaea and some bacteria and has evolved separately from class II LysRS, as the two do not share structural or sequence similarity.


Pssm-ID: 173900 [Multi-domain]  Cd Length: 353  Bit Score: 41.54  E-value: 8.28e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1859345866 263 NKEKMSKSLNNFFTVRDVLKEYDAESVRYFLIS 295
Cdd:cd00674   272 GGGKMSSSKGNVITPSDWLEVAPPEVLRYLYAR 304
leuS PRK12300
leucyl-tRNA synthetase; Reviewed
 37-60 8.58e-04

leucyl-tRNA synthetase; Reviewed


Pssm-ID: 237049 [Multi-domain]  Cd Length: 897  Bit Score: 41.78  E-value: 8.58e-04
                          10        20
                  ....*....|....*....|....
gi 1859345866  37 HIGHARTFVGFDVIVRYLRHIGYD 60
Cdd:PRK12300    2 HVGHGRTYTIGDVIARYKRMRGYN 25
LysS COG1384
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ...
 263-293 2.09e-03

Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA synthetase, class I is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 440994 [Multi-domain]  Cd Length: 525  Bit Score: 40.56  E-value: 2.09e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1859345866 263 NKEKMSKSLNNFFTVRDVLKEYDAESVRYFL 293
Cdd:COG1384   284 NGEKISKSKGNGLTVEEWLEYAEPESLRYFM 314
ValRS_core cd00817
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ...
 265-297 3.55e-03

catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) catalytic core domain. This enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. ValRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.


Pssm-ID: 185677 [Multi-domain]  Cd Length: 382  Bit Score: 39.54  E-value: 3.55e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1859345866 265 EKMSKSLNNFFTVRDVLKEYDAESVRYFLISGH 297
Cdd:cd00817   342 RKMSKSLGNVIDPLDVIDGYGADALRFTLASAA 374
tRNA-synt_1 pfam00133
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ...
 266-305 5.20e-03

tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.


Pssm-ID: 459685 [Multi-domain]  Cd Length: 602  Bit Score: 39.32  E-value: 5.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1859345866 266 KMSKSLNNFFTVRDVLKEYDAESVRYFLISGHYRSQLNYS 305
Cdd:pfam00133 563 KMSKSLGNVIDPLDVIDKYGADALRLWLANSDYGRDINLS 602
 
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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