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Conserved domains on  [gi|1162405973|gb|OPX20677|]
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MAG: cysteine--tRNA ligase [Desulfobacca sp. 4484_104]

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 ...
 1-489 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: 820.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973   1 MRVYNTLGKRKEEFSPQTPGRVGIYACGVTVYDDCHIGHARSAVVFDVIVRYLRYRGLQVTWVRNFTDVDDKIINRARQE 80
Cdd:COG0215     2 LKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYLGYKVTYVRNITDVDDKIIKRAAEE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  81 NTTCQAIAEKYINAFQTDMAALGVARADIEPRATEHIKEIIDLIAALEAKGFAYQRGGDVYFPVARFPGYGKLSGRSLED 160
Cdd:COG0215    82 GESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEADGDVYFDVRSFPDYGKLSGRNLDD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 161 MQAGARVEVDVQKDNPLDFVLWKASKPGEPVWDSPWGPGRPGWHIECSAMCMRYLGTTIDIHGGGQDLIFPHHENEIAQS 240
Cdd:COG0215   162 LRAGARVEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIAQS 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 241 EAATGQPFVRYWLHNGLVTINQEKMSKSLGNFFTVREVLARFHPEVVRFFLIHSHYRSPLDFSDAALAEAETALLRLYTP 320
Cdd:COG0215   242 EAATGKPFARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKALERLYNA 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 321 LARIKELSGNPELAPAAAPDsacsalsveeqerllsLPARFEAAMDDDFNTAQALGHLFEAARLLNRVLEHSPTDS---A 397
Cdd:COG0215   322 LRRLEEALGAADSSAEEIEE----------------LREEFIAAMDDDFNTPEALAVLFELVREINKALDEGEDKAalaA 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 398 ILDLVRRLGEImitlghpLNLLQAEPSEmvrhlRQKTEDLKISPEEIDRLIEARRQARHQKDWARADAIRSQLTESGILL 477
Cdd:COG0215   386 LAALLRALGGV-------LGLLLLEPEA-----WQGAAEDELLDALIEALIEERAEARKAKDFARADRIRDELAALGIVL 453

                         490
                  ....*....|..
gi 1162405973 478 EDTPQGTVWRVK 489
Cdd:COG0215   454 EDTPDGTTWRRK 465
 
Name Accession Description Interval E-value
CysS COG0215
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ...
 1-489 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: 820.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973   1 MRVYNTLGKRKEEFSPQTPGRVGIYACGVTVYDDCHIGHARSAVVFDVIVRYLRYRGLQVTWVRNFTDVDDKIINRARQE 80
Cdd:COG0215     2 LKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYLGYKVTYVRNITDVDDKIIKRAAEE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  81 NTTCQAIAEKYINAFQTDMAALGVARADIEPRATEHIKEIIDLIAALEAKGFAYQRGGDVYFPVARFPGYGKLSGRSLED 160
Cdd:COG0215    82 GESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEADGDVYFDVRSFPDYGKLSGRNLDD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 161 MQAGARVEVDVQKDNPLDFVLWKASKPGEPVWDSPWGPGRPGWHIECSAMCMRYLGTTIDIHGGGQDLIFPHHENEIAQS 240
Cdd:COG0215   162 LRAGARVEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIAQS 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 241 EAATGQPFVRYWLHNGLVTINQEKMSKSLGNFFTVREVLARFHPEVVRFFLIHSHYRSPLDFSDAALAEAETALLRLYTP 320
Cdd:COG0215   242 EAATGKPFARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKALERLYNA 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 321 LARIKELSGNPELAPAAAPDsacsalsveeqerllsLPARFEAAMDDDFNTAQALGHLFEAARLLNRVLEHSPTDS---A 397
Cdd:COG0215   322 LRRLEEALGAADSSAEEIEE----------------LREEFIAAMDDDFNTPEALAVLFELVREINKALDEGEDKAalaA 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 398 ILDLVRRLGEImitlghpLNLLQAEPSEmvrhlRQKTEDLKISPEEIDRLIEARRQARHQKDWARADAIRSQLTESGILL 477
Cdd:COG0215   386 LAALLRALGGV-------LGLLLLEPEA-----WQGAAEDELLDALIEALIEERAEARKAKDFARADRIRDELAALGIVL 453

                         490
                  ....*....|..
gi 1162405973 478 EDTPQGTVWRVK 489
Cdd:COG0215   454 EDTPDGTTWRRK 465
cysS TIGR00435
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ...
 1-488 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: 614.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973   1 MRVYNTLGKRKEEFSPQTPGRVGIYACGVTVYDDCHIGHARSAVVFDVIVRYLRYRGLQVTWVRNFTDVDDKIINRARQE 80
Cdd:TIGR00435   1 LKLYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLRYLGYKVQYVQNITDIDDKIIKRAREN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  81 NTTCQAIAEKYINAFQTDMAALGVARADIEPRATEHIKEIIDLIAALEAKGFAYQRG-GDVYFPVARFPGYGKLSGRSLE 159
Cdd:TIGR00435  81 GESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDnGDVYFDVSKFKDYGKLSKQDLD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 160 DMQAGARVEVDVQKDNPLDFVLWKASKPGEPVWDSPWGPGRPGWHIECSAMCMRYLGTTIDIHGGGQDLIFPHHENEIAQ 239
Cdd:TIGR00435 161 QLEAGARVDVDEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 240 SEAATGQPFVRYWLHNGLVTINQEKMSKSLGNFFTVREVLARFHPEVVRFFLIHSHYRSPLDFSDAALAEAETALLRLYT 319
Cdd:TIGR00435 241 SEAAFGKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKNALERLYK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 320 PLARIKElsgnpelapAAAPDSACSALSVEEQERLLslpARFEAAMDDDFNTAQALGHLFEAARLLNrvleHSPTDSAIL 399
Cdd:TIGR00435 321 ALRVLDT---------SLAYSGNQSLNKFPDEKEFE---ARFVEAMDDDLNTANALAVLFELAKSIN----LTFVSKADA 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 400 DLVRrlgEIMITLGHPLNLLQAEPSEMVRhlrqktEDLKISPEEIDRLIEARRQARHQKDWARADAIRSQLTESGILLED 479
Cdd:TIGR00435 385 ALLI---EHLIFLESRLGLLLGLPSKPVQ------AGSNDDLGEIEALIEERSIARKEKDFAKADEIRDELAKKGIVLED 455


                  ....*....
gi 1162405973 480 TPQGTVWRV 488
Cdd:TIGR00435 456 TPQGTTWRR 464
tRNA-synt_1e pfam01406
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ...
 13-304 4.89e-179

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


Pssm-ID: 396128 [Multi-domain]  Cd Length: 301  Bit Score: 503.82  E-value: 4.89e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  13 EFSPQTPGRVGIYACGVTVYDDCHIGHARSAVVFDVIVRYLRYRGLQVTWVRNFTDVDDKIINRARQENTTCQAIAEKYI 92
Cdd:pfam01406   1 FFVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  93 NAFQTDMAALGVARADIEPRATEHIKEIIDLIAALEAKGFAYQRG-GDVYFPVARFPGYGKLSGRSLEDMQAGARVEVDV 171
Cdd:pfam01406  81 EAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDnGDVYFDVSSFPDYGKLSGQNLEQLEAGARGEVSE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 172 QKDNPLDFVLWKASKPGEPVWDSPWGPGRPGWHIECSAMCMRYLGTTIDIHGGGQDLIFPHHENEIAQSEAATGQPFVRY 251
Cdd:pfam01406 161 GKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFDKQLANY 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1162405973 252 WLHNGLVTINQEKMSKSLGNFFTVREVLARFHPEVVRFFLIHSHYRSPLDFSD 304
Cdd:pfam01406 241 WLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSE 293
PLN02946 PLN02946
cysteine-tRNA ligase
 1-487 5.31e-171

cysteine-tRNA ligase


Pssm-ID: 178532 [Multi-domain]  Cd Length: 557  Bit Score: 493.29  E-value: 5.31e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973   1 MRVYNTLGKRKEEFSPQTPGRVGIYACGVTVYDDCHIGHARSAVVFDVIVRYLRYRGLQVTWVRNFTDVDDKIINRARQE 80
Cdd:PLN02946   60 LHLYNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYLKHLGYEVRYVRNFTDVDDKIIARANEL 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  81 NTTCQAIAEKYINAFQTDMAALGVARADIEPRATEHIKEIIDLIAALEAKGFAYQRGGDVYFPVARFPGYGKLSGRSLED 160
Cdd:PLN02946  140 GEDPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVDGDVYFSVDKFPEYGKLSGRKLED 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 161 MQAGARVEVDVQKDNPLDFVLWKASKPGEPVWDSPWGPGRPGWHIECSAMCMRYLGTTIDIHGGGQDLIFPHHENEIAQS 240
Cdd:PLN02946  220 NRAGERVAVDSRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLVFPHHENEIAQS 299

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 241 EAATGQPFVRYWLHNGLVTINQEKMSKSLGNFFTVREVLARFHPEVVRFFLIHSHYRSPLDFSDAALAEAETALLRLYTP 320
Cdd:PLN02946  300 CAACCDSNISYWIHNGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDVQLESASERIFYIYQT 379

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 321 LARIKELSGNPELAPAAAPdsacsaLSVEEQERLLSLPARFEAAMDDDFNTAQALGHLFEAARLLNRVLEHSPTDSAILD 400
Cdd:PLN02946  380 LHDCEESLQQHDSTFEKDS------VPPDTLNCINKFHDEFVTSMSDDLHTPVALAALSEPLKTINDLLHTRKGKKQEKR 453

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 401 L--VRRLGEIMITLGHPLNLLQAEPSEMVRHLRQKT-EDLKISPEEIDRLIEARRQARHQKDWARADAIRSQLTESGILL 477
Cdd:PLN02946  454 LesLAALEKKIRDVLSVLGLMPTSYSEALQQLREKAlRRAKLTEEQVLQKIEERTVARKNKEYEKSDAIRKDLAAVGIAL 533

                         490
                  ....*....|
gi 1162405973 478 EDTPQGTVWR 487
Cdd:PLN02946  534 MDSPDGTTWR 543
CysRS_core cd00672
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ...
 2-303 5.78e-129

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: 373.07  E-value: 5.78e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973   2 RVYNTLGKRKEEFSPQTPGRVGIYACGVTVYDDCHIGHARSAVVFDVIVRYLRYRGLQVTWVRNFTDVDDKIINRARQEN 81
Cdd:cd00672     1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLGYKVRYVQNITDIDDKIIKRAREEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  82 TTCQAIAEKYINAFQTDMAALGVARADIEPRAtehikeiidliaaleakgfayqrggdvyfpvarfpgygklsgrsledm 161
Cdd:cd00672    81 LSWKEVADYYTKEFFEDMKALNVLPPDVVPRV------------------------------------------------ 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 162 qagarvevdvqkdnpldfvlwkaskpgepvwdspwgpgrpgWHIECSAMCMRYLGTTIDIHGGGQDLIFPHHENEIAQSE 241
Cdd:cd00672   113 -----------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQSE 151

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1162405973 242 AATGQPFVRYWLHNGLVTINQEKMSKSLGNFFTVREVLARFHPEVVRFFLIHSHYRSPLDFS 303
Cdd:cd00672   152 AATGKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
DALR_2 smart00840
This DALR domain is found in cysteinyl-tRNA-synthetases;
360-409 1.74e-14

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


Pssm-ID: 214848 [Multi-domain]  Cd Length: 56  Bit Score: 67.59  E-value: 1.74e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1162405973  360 RFEAAMDDDFNTAQALGHLFEAARLLNRvLEHSPTDS----AILDLVRRLGEIM 409
Cdd:smart00840   1 RFEEAMDDDFNTPEALAVLFELAREINR-LALKATDAeelaALAALLRALGGVL 53
 
Name Accession Description Interval E-value
CysS COG0215
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ...
 1-489 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: 820.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973   1 MRVYNTLGKRKEEFSPQTPGRVGIYACGVTVYDDCHIGHARSAVVFDVIVRYLRYRGLQVTWVRNFTDVDDKIINRARQE 80
Cdd:COG0215     2 LKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYLGYKVTYVRNITDVDDKIIKRAAEE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  81 NTTCQAIAEKYINAFQTDMAALGVARADIEPRATEHIKEIIDLIAALEAKGFAYQRGGDVYFPVARFPGYGKLSGRSLED 160
Cdd:COG0215    82 GESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEADGDVYFDVRSFPDYGKLSGRNLDD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 161 MQAGARVEVDVQKDNPLDFVLWKASKPGEPVWDSPWGPGRPGWHIECSAMCMRYLGTTIDIHGGGQDLIFPHHENEIAQS 240
Cdd:COG0215   162 LRAGARVEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIAQS 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 241 EAATGQPFVRYWLHNGLVTINQEKMSKSLGNFFTVREVLARFHPEVVRFFLIHSHYRSPLDFSDAALAEAETALLRLYTP 320
Cdd:COG0215   242 EAATGKPFARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKALERLYNA 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 321 LARIKELSGNPELAPAAAPDsacsalsveeqerllsLPARFEAAMDDDFNTAQALGHLFEAARLLNRVLEHSPTDS---A 397
Cdd:COG0215   322 LRRLEEALGAADSSAEEIEE----------------LREEFIAAMDDDFNTPEALAVLFELVREINKALDEGEDKAalaA 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 398 ILDLVRRLGEImitlghpLNLLQAEPSEmvrhlRQKTEDLKISPEEIDRLIEARRQARHQKDWARADAIRSQLTESGILL 477
Cdd:COG0215   386 LAALLRALGGV-------LGLLLLEPEA-----WQGAAEDELLDALIEALIEERAEARKAKDFARADRIRDELAALGIVL 453

                         490
                  ....*....|..
gi 1162405973 478 EDTPQGTVWRVK 489
Cdd:COG0215   454 EDTPDGTTWRRK 465
cysS TIGR00435
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ...
 1-488 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: 614.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973   1 MRVYNTLGKRKEEFSPQTPGRVGIYACGVTVYDDCHIGHARSAVVFDVIVRYLRYRGLQVTWVRNFTDVDDKIINRARQE 80
Cdd:TIGR00435   1 LKLYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLRYLGYKVQYVQNITDIDDKIIKRAREN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  81 NTTCQAIAEKYINAFQTDMAALGVARADIEPRATEHIKEIIDLIAALEAKGFAYQRG-GDVYFPVARFPGYGKLSGRSLE 159
Cdd:TIGR00435  81 GESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDnGDVYFDVSKFKDYGKLSKQDLD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 160 DMQAGARVEVDVQKDNPLDFVLWKASKPGEPVWDSPWGPGRPGWHIECSAMCMRYLGTTIDIHGGGQDLIFPHHENEIAQ 239
Cdd:TIGR00435 161 QLEAGARVDVDEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 240 SEAATGQPFVRYWLHNGLVTINQEKMSKSLGNFFTVREVLARFHPEVVRFFLIHSHYRSPLDFSDAALAEAETALLRLYT 319
Cdd:TIGR00435 241 SEAAFGKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKNALERLYK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 320 PLARIKElsgnpelapAAAPDSACSALSVEEQERLLslpARFEAAMDDDFNTAQALGHLFEAARLLNrvleHSPTDSAIL 399
Cdd:TIGR00435 321 ALRVLDT---------SLAYSGNQSLNKFPDEKEFE---ARFVEAMDDDLNTANALAVLFELAKSIN----LTFVSKADA 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 400 DLVRrlgEIMITLGHPLNLLQAEPSEMVRhlrqktEDLKISPEEIDRLIEARRQARHQKDWARADAIRSQLTESGILLED 479
Cdd:TIGR00435 385 ALLI---EHLIFLESRLGLLLGLPSKPVQ------AGSNDDLGEIEALIEERSIARKEKDFAKADEIRDELAKKGIVLED 455


                  ....*....
gi 1162405973 480 TPQGTVWRV 488
Cdd:TIGR00435 456 TPQGTTWRR 464
tRNA-synt_1e pfam01406
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ...
 13-304 4.89e-179

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


Pssm-ID: 396128 [Multi-domain]  Cd Length: 301  Bit Score: 503.82  E-value: 4.89e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  13 EFSPQTPGRVGIYACGVTVYDDCHIGHARSAVVFDVIVRYLRYRGLQVTWVRNFTDVDDKIINRARQENTTCQAIAEKYI 92
Cdd:pfam01406   1 FFVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  93 NAFQTDMAALGVARADIEPRATEHIKEIIDLIAALEAKGFAYQRG-GDVYFPVARFPGYGKLSGRSLEDMQAGARVEVDV 171
Cdd:pfam01406  81 EAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDnGDVYFDVSSFPDYGKLSGQNLEQLEAGARGEVSE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 172 QKDNPLDFVLWKASKPGEPVWDSPWGPGRPGWHIECSAMCMRYLGTTIDIHGGGQDLIFPHHENEIAQSEAATGQPFVRY 251
Cdd:pfam01406 161 GKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFDKQLANY 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1162405973 252 WLHNGLVTINQEKMSKSLGNFFTVREVLARFHPEVVRFFLIHSHYRSPLDFSD 304
Cdd:pfam01406 241 WLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSE 293
PLN02946 PLN02946
cysteine-tRNA ligase
 1-487 5.31e-171

cysteine-tRNA ligase


Pssm-ID: 178532 [Multi-domain]  Cd Length: 557  Bit Score: 493.29  E-value: 5.31e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973   1 MRVYNTLGKRKEEFSPQTPGRVGIYACGVTVYDDCHIGHARSAVVFDVIVRYLRYRGLQVTWVRNFTDVDDKIINRARQE 80
Cdd:PLN02946   60 LHLYNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYLKHLGYEVRYVRNFTDVDDKIIARANEL 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  81 NTTCQAIAEKYINAFQTDMAALGVARADIEPRATEHIKEIIDLIAALEAKGFAYQRGGDVYFPVARFPGYGKLSGRSLED 160
Cdd:PLN02946  140 GEDPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVDGDVYFSVDKFPEYGKLSGRKLED 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 161 MQAGARVEVDVQKDNPLDFVLWKASKPGEPVWDSPWGPGRPGWHIECSAMCMRYLGTTIDIHGGGQDLIFPHHENEIAQS 240
Cdd:PLN02946  220 NRAGERVAVDSRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLVFPHHENEIAQS 299

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 241 EAATGQPFVRYWLHNGLVTINQEKMSKSLGNFFTVREVLARFHPEVVRFFLIHSHYRSPLDFSDAALAEAETALLRLYTP 320
Cdd:PLN02946  300 CAACCDSNISYWIHNGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDVQLESASERIFYIYQT 379

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 321 LARIKELSGNPELAPAAAPdsacsaLSVEEQERLLSLPARFEAAMDDDFNTAQALGHLFEAARLLNRVLEHSPTDSAILD 400
Cdd:PLN02946  380 LHDCEESLQQHDSTFEKDS------VPPDTLNCINKFHDEFVTSMSDDLHTPVALAALSEPLKTINDLLHTRKGKKQEKR 453

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 401 L--VRRLGEIMITLGHPLNLLQAEPSEMVRHLRQKT-EDLKISPEEIDRLIEARRQARHQKDWARADAIRSQLTESGILL 477
Cdd:PLN02946  454 LesLAALEKKIRDVLSVLGLMPTSYSEALQQLREKAlRRAKLTEEQVLQKIEERTVARKNKEYEKSDAIRKDLAAVGIAL 533

                         490
                  ....*....|
gi 1162405973 478 EDTPQGTVWR 487
Cdd:PLN02946  534 MDSPDGTTWR 543
cysS PRK14535
cysteinyl-tRNA synthetase; Provisional
 3-487 2.79e-155

cysteinyl-tRNA synthetase; Provisional


Pssm-ID: 173001 [Multi-domain]  Cd Length: 699  Bit Score: 458.03  E-value: 2.79e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973   3 VYNTLGKRKEEFSPQTPGRVGIYACGVTVYDDCHIGHARSAVVFDVIVRYLRYRGLQVTWVRNFTDVDDKIINRARQENT 82
Cdd:PRK14535  230 IYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAENGE 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  83 TCQAIAEKYINAFQTDMAALGVARADIEPRATEHIKEIIDLIAALEAKGFAYQRG-GDVYFPVARFPGYGKLSGRSLEDM 161
Cdd:PRK14535  310 TIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAAnGDVYYAVREFAAYGQLSGKSLDDL 389

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 162 QAGARVEVDVQKDNPLDFVLWKASKPGEPVWDSPWGPGRPGWHIECSAMCMRYLGTTIDIHGGGQDLIFPHHENEIAQSE 241
Cdd:PRK14535  390 RAGERVEVDGFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIAQSV 469

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 242 AATGQ----------------PFVRYWLHNGLVTINQEKMSKSLGNFFTVREVLARFHPEVVRFFLIHSHYRSPLDFSDA 305
Cdd:PRK14535  470 GATGHtcghhhaqthhgqsiaSHVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNYSDA 549

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 306 ALAEAETALLRLYTPLARikelsgnpelAPAAAPDSAcsalsveeqERLLSLPARFEAAMDDDFNTAQALGHLFEAARLL 385
Cdd:PRK14535  550 HLDDAKGALTRLYTTLKN----------TPAAEFMLS---------ENVNDYTRRFYAAMNDDFGTVEAVAVLFELAGEV 610

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 386 NRVlehspTDSAILDLVRRLGEImitlghpLNLLQAEPSEMvrhLRQKTEDLKISPEEIDRLIEARRQARHQKDWARADA 465
Cdd:PRK14535  611 NKT-----NDAQLAGCLKALGGI-------IGLLQRDPTEF---LQGGAASDGLSNEEIEDLIARRKQARADKNWAESDR 675

                         490       500
                  ....*....|....*....|..
gi 1162405973 466 IRSQLTESGILLEDTPQGTVWR 487
Cdd:PRK14535  676 IRDLLNEHKIILEDNAGGTTWR 697
cysS PRK14536
cysteinyl-tRNA synthetase; Provisional
 1-487 3.66e-142

cysteinyl-tRNA synthetase; Provisional


Pssm-ID: 184731 [Multi-domain]  Cd Length: 490  Bit Score: 417.40  E-value: 3.66e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973   1 MRVYNTLGKRKEEFSPQTPGRVGIYACGVTVYDDCHIGHARSAVVFDVIVRYLRYRGLQVTWVRNFTDV----------D 70
Cdd:PRK14536    3 LRLYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTLHFLGYRVTHVMNITDVghltddadsgE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  71 DKIINRARQENTTCQAIAEKYINAFQTDMAALGVARADIEPRATEHIKEIIDLIAALEAKGFAYQRGGDVYFPVARFPGY 150
Cdd:PRK14536   83 DKMVKSAQEHGKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCAGGNVYFDIRTFPSY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 151 GKLSGRSLEDMQAGARVEVDVQKDNPLDFVLWKASKPGEP---VWDSPWGPGRPGWHIECSAMCMRYLGTTIDIHGGGQD 227
Cdd:PRK14536  163 GSLASAAVEDLQAGARIEHDTNKRNPHDFVLWFTRSKFENhalTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIGGVD 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 228 LIFPHHENEIAQSEAATGQPFVRYWLHNGLVTINQEKMSKSLGNFFTVREVLAR-FHPEVVRFFLIHSHYRSPLDFSDAA 306
Cdd:PRK14536  243 HIRVHHTNEIAQCEAATGKPWVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQEKgFQPLDYRFFLLGGHYRSQLAFSWEA 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 307 LAEAETALLRLYTPLARIKE-LSGNPELAPAAAPDSACSALSVEEQERLLSLPARFEAAMDDDFNTAQALGHLfeaaRLL 385
Cdd:PRK14536  323 LKTAKAARRSLVRRVARVVDaARATTGSVRGTLAECAAERVAESRASESELLLTDFRAALEDDFSTPKALSEL----QKL 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 386 NRVLEHSPTD--SAILDLVRRLGeimitlghpLNLLQaEPSemvrHLRQKTEDLKISPEEIDRLIEARRQARHQKDWARA 463
Cdd:PRK14536  399 VKDTSVPPSLclSVLQAMDTVLG---------LGLIQ-EAT----ASLSAQVPAGPSEEEIGQLIEARAHARQTKDFPLA 464

                         490       500
                  ....*....|....*....|....
gi 1162405973 464 DAIRSQLTESGILLEDTPQGTVWR 487
Cdd:PRK14536  465 DEIRDKLKAEGIELEDTHLGTIWK 488
PTZ00399 PTZ00399
cysteinyl-tRNA-synthetase; Provisional
 2-490 1.00e-132

cysteinyl-tRNA-synthetase; Provisional


Pssm-ID: 240402 [Multi-domain]  Cd Length: 651  Bit Score: 398.63  E-value: 1.00e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973   2 RVYNTLGKRKEEFSPQTPGRVGIYACGVTVYDDCHIGHARSAVVFDVIVRYLR-YRGLQVTWVRNFTDVDDKIINRARQE 80
Cdd:PTZ00399   41 KVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEdYFGYDVFYVMNITDIDDKIIKRAREE 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  81 NTTC-QAIAEKYINAFQTDMAALGVARADIEPRATEHIKEIIDLIAALEAKGFAYQRGGDVYFPVARFPG----YGKLSG 155
Cdd:PTZ00399  121 KLSIfLELARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYESNGSVYFDVEAFRKaghvYPKLEP 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 156 RSLEDMQA-----GARVEVDVQKDNPLDFVLWKASKPGEPVWDSPWGPGRPGWHIECSAMCMRYLGTTIDIHGGGQDLIF 230
Cdd:PTZ00399  201 ESVADEDRiaegeGALGKVSGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDLKF 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 231 PHHENEIAQSEAATGQP-FVRYWLHNGLVTINQEKMSKSLGNFFTVREVLARFHPEVVRF-FLIHsHYRSPLDFSDAALA 308
Cdd:PTZ00399  281 PHHDNELAQSEAYFDKHqWVNYFLHSGHLHIKGLKMSKSLKNFITIRQALSKYTARQIRLlFLLH-KWDKPMNYSDESMD 359

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 309 EAETALLRLYTPLARIKELSGNPELAPAAAPDSACSALSveeqERLLSLPARFEAAMDDDFNTAQALGHLFEAARLLNRV 388
Cdd:PTZ00399  360 EAIEKDKVFFNFFANVKIKLRESELTSPQKWTQHDFELN----ELFEETKSAVHAALLDNFDTPEALQALQKLISATNTY 435

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 389 LEHSPTDSAilDLVRRLGE----IMITLGhpLNllqaEPSEMVRHLRQKTEDlkispEEIDRLIEA----RRQARhqkDW 460
Cdd:PTZ00399  436 LNSGEQPSA--PLLRSVAQyvtkILSIFG--LV----EGSDGLGSQGQNSTS-----ENFKPLLEAllrfRDEVR---DA 499

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 1162405973 461 ARA------------------DAIRSQ-LTESGILLEDTPQG-TVWRVKS 490
Cdd:PTZ00399  500 AKAemklisldkkkkqllqlcDKLRDEwLPNLGIRIEDKPDGpSVWKLDD 549
CysRS_core cd00672
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ...
 2-303 5.78e-129

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: 373.07  E-value: 5.78e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973   2 RVYNTLGKRKEEFSPQTPGRVGIYACGVTVYDDCHIGHARSAVVFDVIVRYLRYRGLQVTWVRNFTDVDDKIINRARQEN 81
Cdd:cd00672     1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLGYKVRYVQNITDIDDKIIKRAREEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  82 TTCQAIAEKYINAFQTDMAALGVARADIEPRAtehikeiidliaaleakgfayqrggdvyfpvarfpgygklsgrsledm 161
Cdd:cd00672    81 LSWKEVADYYTKEFFEDMKALNVLPPDVVPRV------------------------------------------------ 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 162 qagarvevdvqkdnpldfvlwkaskpgepvwdspwgpgrpgWHIECSAMCMRYLGTTIDIHGGGQDLIFPHHENEIAQSE 241
Cdd:cd00672   113 -----------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQSE 151

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1162405973 242 AATGQPFVRYWLHNGLVTINQEKMSKSLGNFFTVREVLARFHPEVVRFFLIHSHYRSPLDFS 303
Cdd:cd00672   152 AATGKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
PRK12418 PRK12418
cysteinyl-tRNA synthetase; Provisional
 16-404 3.82e-94

cysteinyl-tRNA synthetase; Provisional


Pssm-ID: 183518 [Multi-domain]  Cd Length: 384  Bit Score: 290.29  E-value: 3.82e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  16 PQTPG-RVGIYACGVTVYDDCHIGHARSAVVFDVIVRYLRYRGLQVTWVRNFTDVDDKIINRARQENTTCQAIAEKYINA 94
Cdd:PRK12418    3 PVAPGgTATMYVCGITPYDATHLGHAATYLAFDLVNRVWRDAGHDVHYVQNVTDVDDPLLERAARDGVDWRDLAEREIAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  95 FQTDMAALGVaradIEPR----ATEHIKEIIDLIAALEAKGFAYQ----RGGDVYFPVARFPGYGKLSGRSLEDM----- 161
Cdd:PRK12418   83 FREDMEALRV----LPPRdyvgAVESIPEVVELVEKLLASGAAYVvddeEYPDVYFSVDATPQFGYESGYDRATMlelfa 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 162 -------QAGarvevdvqKDNPLDFVLWKASKPGEPVWDSPWGPGRPGWHIECSAMCMRYLGTTIDIHGGGQDLIFPHHE 234
Cdd:PRK12418  159 erggdpdRPG--------KRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHE 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 235 NEIAQSEAATGQ-PFVRYWLHNGLVTINQEKMSKSLGNF-FTVREVLARFHPEVVRFFLIHSHYRSPLDFSDAALAEAET 312
Cdd:PRK12418  231 FSAAHAEAATGErRFARHYVHAGMIGLDGEKMSKSRGNLvFVSRLRAAGVDPAAIRLALLAGHYRADREWTDAVLAEAEA 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 313 AllrlytpLARIKELSGNPELAPAAApdsacsalsveeqerllsLPARFEAAMDDDFNTAQALGHLFEAARllnRVLEHS 392
Cdd:PRK12418  311 R-------LARWRAAAALPAGPDAAD------------------VVARVRAALADDLDTPGALAAVDGWAT---DALEGG 362

                         410
                  ....*....|..
gi 1162405973 393 PTDSAILDLVRR 404
Cdd:PRK12418  363 GDDAAAPALVAT 374
mycothiol_MshC TIGR03447
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ...
 1-404 2.25e-88

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: 276.61  E-value: 2.25e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973   1 MRVYNTLGKRKEEFSPqtPGRVGIYACGVTVYDDCHIGHARSAVVFDVIVRYLRYRGLQVTWVRNFTDVDDKIINRARQE 80
Cdd:TIGR03447  18 LRLFDTADGQVRPVEP--GPEAGMYVCGITPYDATHLGHAATYLTFDLVNRVWRDAGHRVHYVQNVTDVDDPLFERAERD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  81 NTTCQAIAEKYINAFQTDMAALGVaradIEPR----ATEHIKEIIDLIAALEAKGFAYQ----RGGDVYFPVARFPGYGK 152
Cdd:TIGR03447  96 GVDWRELGTSQIDLFREDMEALRV----LPPRdyigAVESIDEVVEMVEKLLASGAAYIvegpEYPDVYFSIDATEQFGY 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 153 LSGRSLEDM-----QAGARVEvDVQKDNPLDFVLWKASKPGEPVWDSPWGPGRPGWHIECSAMCMRYLGTTIDIHGGGQD 227
Cdd:TIGR03447 172 ESGYDRATMlelfaERGGDPD-RPGKRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSD 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 228 LIFPHHENEIAQSEAATG-QPFVRYWLHNGLVTINQEKMSKSLGNFFTVREVLARFH-PEVVRFFLIHSHYRSPLDFSDA 305
Cdd:TIGR03447 251 LIFPHHEFSAAHAEAATGvRRMARHYVHAGMIGLDGEKMSKSLGNLVFVSKLRAAGVdPAAIRLGLLAGHYRQDRDWTDA 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 306 AlaeaetallrLYTPLARIKELSgnpelapaaapdsacSALSVEEQERLLSLPARFEAAMDDDFNTAQALGHLFEAArll 385
Cdd:TIGR03447 331 V----------LAEAEARLARWR---------------AALALPDAPDATDLIARLRQHLANDLDTPAALAAVDGWA--- 382

                         410
                  ....*....|....*....
gi 1162405973 386 NRVLEHSPTDSAILDLVRR 404
Cdd:TIGR03447 383 ADALSYGGSDTEAPALVAT 401
cysS PRK14534
cysteinyl-tRNA synthetase; Provisional
 1-484 4.45e-77

cysteinyl-tRNA synthetase; Provisional


Pssm-ID: 173000 [Multi-domain]  Cd Length: 481  Bit Score: 249.38  E-value: 4.45e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973   1 MRVYNTlgkRKEEFSPQTP-GRVGIYACGVTVYDDCHIGHARSAVVFDVIVRYLRYRGLQVTWVRNFTDV---------- 69
Cdd:PRK14534    3 LKLYNT---KTKDLSELKNfSDVKVYACGPTVYNYAHIGNFRTYIFEDLLIKSLRLLKYNVNYAMNITDIghltgdfddg 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  70 DDKIINRARQENTTCQAIAEKYINAFQTDMAALGVARADIEPRATEHIKEIIDLIAALEAKGFAYQRGGDVYFPVARFPG 149
Cdd:PRK14534   80 EDKVVKAARERGLTVYEISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTYFVNGNVYFDTSCFKS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 150 YGKLSGRSLEDMQ--AGARVEVDVQKDNPLDFVLWKAS---KPGEPVWDSPWGPGRPGWHIECSAMCMRYLGTTIDIHGG 224
Cdd:PRK14534  160 YGQMAGINLNDFKdmSVSRVEIDKSKRNKSDFVLWFTNskfKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKSTLDIHLG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 225 GQDLIFPHHENEIAQSEAATGQPFVRYWLHNGLVTINQEKMSKSLGNFFTVREVLAR-FHPEVVRFFLIHSHYRSPLDFS 303
Cdd:PRK14534  240 GVDHIGVHHINEIAIAECYLNKKWCDMFVHGEFLIMEYEKMSKSNNNFITIKDLEDQgFSPLDFRYFCLTAHYRTQLKFT 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 304 DAALAEAETALLRLYTPLARIKELSGNPELAPAAAPDSACSalSVEEQERLLSlparFEAAMDDDFNTAQALGHLFEAAR 383
Cdd:PRK14534  320 FNNLKACKIARENMLNKLTYFYSSLDQFDLNLLNKDLENIE--FSLEKEYYDS----FLEKIAFDLNIPQGLALLWDIIK 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 384 llnrvlEHSPTDSAILDLVRRLGEIMitlghPLNLLQAEPSEMVRHlrqkteDLKISpEEIDRLIEARRQARHQKDWARA 463
Cdd:PRK14534  394 ------DDNLSFLSKLRLAFKFDEVL-----SLGLREEILREIENH------RIVID-DNMKSLIEERRLAKCEKDFKRA 455

                         490       500
                  ....*....|....*....|.
gi 1162405973 464 DAIRSQLTESGILLEDTPQGT 484
Cdd:PRK14534  456 DEIREYFASKGFVLIDTEEGT 476
Anticodon_Ia_Cys cd07963
Anticodon-binding domain of cysteinyl tRNA synthetases; This domain is found in cysteinyl tRNA ...
 359-487 3.24e-39

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: 139.23  E-value: 3.24e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 359 ARFEAAMDDDFNTAQALGHLFEAARLLNRV----LEHSPTDSAILdlvRRLGEImitlghpLNLLQAEPSEMvrhLRQKT 434
Cdd:cd07963    36 ERFIAAMDDDFNTPEALAVLFELAREINRLkkedIEKAAALAALL---KALGGV-------LGLLQQDPEAF---LQGGT 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1162405973 435 EDLKISPEEIDRLIEARRQARHQKDWARADAIRSQLTESGILLEDTPQGTVWR 487
Cdd:cd07963   103 GEGGLSVAEIEALIAQRNQARKAKDWAEADRIRDELAAQGIILEDSPEGTTWR 155
Ile_Leu_Val_MetRS_core cd00668
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ...
 36-292 4.79e-18

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: 84.78  E-value: 4.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  36 HIGHARSAVVFDVIVRYLRYRGLQVTWVRNfTD---------------VDDKIINRARQeNTTCQAIAEKYINAFQTDMA 100
Cdd:cd00668    16 HLGHALTHIIADFIARYKRMRGYEVPFLPG-WDthglpielkaerkggRKKKTIWIEEF-REDPKEFVEEMSGEHKEDFR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 101 ALGVARADIEPRAT---EHIKEIIDLIAALEAKGFAYQRggdvYFPVARFPGY----GKLSGRSLEDMQAGARVEVDVQK 173
Cdd:cd00668    94 RLGISYDWSDEYITtepEYSKAVELIFSRLYEKGLIYRG----THPVRITEQWffdmPKFKEKLLKALRRGKIVPEHVKN 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 174 ------DNPLDfvlWKASKPgepvwdSPWGPGRPGWHIE----CSAMCMRYLG-----------TTIDIHGGGQDLIFPH 232
Cdd:cd00668   170 rmeawlESLLD---WAISRQ------RYWGTPLPEDVFDvwfdSGIGPLGSLGypeekewfkdsYPADWHLIGKDILRGW 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162405973 233 HENEIAQSEAATGQPFVRYWLHNGLVTINQ-EKMSKSLGNFFTVREVLARFHPEVVRFFLI 292
Cdd:cd00668   241 ANFWITMLVALFGEIPPKNLLVHGFVLDEGgQKMSKSKGNVIDPSDVVEKYGADALRYYLT 301
DALR_2 pfam09190
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases.
 360-425 2.32e-17

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


Pssm-ID: 462711 [Multi-domain]  Cd Length: 63  Bit Score: 76.09  E-value: 2.32e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1162405973 360 RFEAAMDDDFNTAQALGHLFEAARLLNRVLEHSPTDSAIldlvrRLGEIMITLGHPLNLLQAEPSE 425
Cdd:pfam09190   1 KFIEAMDDDFNTPEALAVLFELAKEINRALKTNDAEAAA-----ALAALLRELGDVLGLLQQDPEA 61
MetRS_core cd00814
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ...
 36-292 3.08e-16

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: 79.50  E-value: 3.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  36 HIGHARSAVVFDVIVRYLRYRGLQVTWVrnfTDVDD---KIINRARQENTTCQAIAEKYINAFQTDMAALGVArADIEPR 112
Cdd:cd00814    16 HLGHLYGTVLADVFARYQRLRGYDVLFV---TGTDEhgtKIEQKAEEEGVTPQELCDKYHEIFKDLFKWLNIS-FDYFIR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 113 ATE--HIKEIIDLIAALEAKGFAYQRGGDVYFPVA----------------RFPGYGK-----LSGRSLEDMQAGARVEV 169
Cdd:cd00814    92 TTSprHKEIVQEFFKKLYENGYIYEGEYEGLYCVScerflpewreeehyffRLSKFQDrllewLEKNPDFIWPENARNEV 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 170 -----------DVQKDNPldfvLWKASKPGEP-----VW-DSPWG-----------PGRPGWHIEcsamcmrylGTTIDI 221
Cdd:cd00814   172 lswlkeglkdlSITRDLF----DWGIPVPLDPgkviyVWfDALIGyisatgyyneeWGNSWWWKD---------GWPELV 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1162405973 222 HGGGQDlIFPHHeneiAQ----SEAATGQPFVRYWLHNGLVTINQEKMSKSLGNFFTVREVLARFHPEVVRFFLI 292
Cdd:cd00814   239 HFIGKD-IIRFH----AIywpaMLLGAGLPLPTRIVAHGYLTVEGKKMSKSRGNVVDPDDLLERYGADALRYYLL 308
DALR_2 smart00840
This DALR domain is found in cysteinyl-tRNA-synthetases;
360-409 1.74e-14

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


Pssm-ID: 214848 [Multi-domain]  Cd Length: 56  Bit Score: 67.59  E-value: 1.74e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1162405973  360 RFEAAMDDDFNTAQALGHLFEAARLLNRvLEHSPTDS----AILDLVRRLGEIM 409
Cdd:smart00840   1 RFEEAMDDDFNTPEALAVLFELAREINR-LALKATDAeelaALAALLRALGGVL 53
class_I_aaRS_core cd00802
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ...
 24-269 3.16e-14

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: 69.82  E-value: 3.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  24 IYACGVTVYDDCHIGHARSAVVFDVIVRYLRYRGLQVTWVRNFTDVDDKIInRARQENTTC-QAIAEKYInafqtdmaal 102
Cdd:cd00802     1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIG-DPANKKGENaKAFVERWI---------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 103 gvaradiepratehikeiidliaaleakgfayqrggdvyfpvarfpgygklsgrsledmqagARVEVDVqkdnpldfvlw 182
Cdd:cd00802    70 --------------------------------------------------------------ERIKEDV----------- 76

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 183 kaskpgepvwdspwgpgrpGWHIECSAMCMRYLGTTIDIHGGGQDLIFpHHENEIAQSEAATGqPFVRYWLHNGLVTI-N 261
Cdd:cd00802    77 -------------------EYMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKAGG-PARPFGLTFGRVMGaD 135


                  ....*...
gi 1162405973 262 QEKMSKSL 269
Cdd:cd00802   136 GTKMSKSK 143
LeuRS_core cd00812
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ...
 36-294 3.62e-12

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: 67.27  E-value: 3.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  36 HIGHARSAVVFDVIVRYLRYRGLQVTWVRNFTDVDDKIINRARQENTTCQAIAEKYINAFQTDMAALG--------VARA 107
Cdd:cd00812    16 HVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWTEYNIKKMKEQLKRMGfsydwrreFTTC 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 108 DIE-PRATEHikeiidLIAALEAKGFAYQRGGDV--------YFPVARFPGYGKLSGRSLEDMQAGARVEVDVQKdNPLD 178
Cdd:cd00812    96 DPEyYKFTQW------LFLKLYEKGLAYKKEAPVnwcklldqWFLKYSETEWKEKLLKDLEKLDGWPEEVRAMQE-NWIG 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 179 FV---LWkaskpGEPV-W--------DSPWGPGR--------PGWHIECSAMCMRYLG-TTIDIHGGGQDLIFPH----- 232
Cdd:cd00812   169 CSrqrYW-----GTPIpWtdtmeslsDSTWYYARytdahnleQPYEGDLEFDREEFEYwYPVDIYIGGKEHAPNHllysr 243

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1162405973 233 -HENEIAQSEAATGQPFVRYwLHNGLVTINQEKMSKSLGNFFTVREVLARFHPEVVRFFLIHS 294
Cdd:cd00812   244 fNHKALFDEGLVTDEPPKGL-IVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLYILFA 305
MetG COG0143
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ...
 33-387 4.65e-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: 68.22  E-value: 4.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  33 DDCHIGHARSAVVFDVIVRYLRYRGLQVTWVrnfTDVDD---KIINRARQENTTCQAIAEKYINAFQTDMAALGVA---- 105
Cdd:COG0143    14 GPPHIGHLYTYIPADILARYQRLRGHDVLFV---TGTDEhgtKIELAAEKEGITPQELVDRIHAEFKELFEKLGISfdnf 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 106 -RADiEPratEHIKEIIDLIAALEAKGFAY--------------------------------QRG------GDVYFPVAR 146
Cdd:COG0143    91 iRTT-SP---EHKELVQEIFQRLYDNGDIYkgeyegwycpecerflpdryvegtcpkcgaedAYGdqcencGATLEPTEL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 147 FPGYGKLSGRSLE--------------------------DMQAGARVEVdvqkdnpLDFVlwkasKPGEPVW----DSPW 196
Cdd:COG0143   167 INPRSAISGAPPElreeehyffrlskyqdrllewieenpDIQPEVRNEV-------LSWL-----KEGLQDLsisrDFDW 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 197 G---PGRPG-----W---HIEcsamcmrYLGTTI---DIHGGGQDL--IFPHHENEIAQseaatgqpF-----VR----Y 251
Cdd:COG0143   235 GipvPGDPGkvfyvWfdaLIG-------YISATKgyaDDRGLPEDFekYWPAPDTELVH--------FigkdiIRfhaiI 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 252 W---LH------------NGLVTINQEKMSKSLGNFFTVREVLARFHPEVVRFFLI-HSHYRSPLDFSdaalaeaetaLL 315
Cdd:COG0143   300 WpamLMaaglplpkkvfaHGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLrEVPFGQDGDFS----------WE 369

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 316 RLytpLARI-KELSGN--------------------PELAPAAAPDSacsalsvEEQERLLSLPARFEAAMdDDFNTAQA 374
Cdd:COG0143   370 DF---VARVnSDLANDlgnlasrtlsmihkyfdgkvPEPGELTEADE-------ELLAEAEAALEEVAEAM-EAFEFRKA 438

                         490
                  ....*....|...
gi 1162405973 375 LGHLFEAARLLNR 387
Cdd:COG0143   439 LEEIMALARAANK 451
tRNA-synt_1g pfam09334
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
 25-303 7.19e-11

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


Pssm-ID: 401322 [Multi-domain]  Cd Length: 387  Bit Score: 63.85  E-value: 7.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  25 YACGVTvyddcHIGHARSAVVFDVIVRYLRYRGLQVTWVrnfTDVDD---KIINRARQENTTCQAIAEKYINAFQTDMAA 101
Cdd:pfam09334   9 YANGPP-----HLGHLYSYIPADIFARYLRLRGYDVLFV---CGTDEhgtPIELKAEKEGITPEELVDRYHEIHREDFKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 102 LGVARaDIEPRATE--HIKEIIDLIAALEAKGFAYQRGGDVYFPVA--RFpgygkLSGRSLE--------DMQAGARVEV 169
Cdd:pfam09334  81 FNISF-DDYGRTTSerHHELVQEFFLKLYENGYIYEKEIEQFYCPSdeRF-----LPDRYVEgtcphcgsEDARGDQCEN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 170 DVQKDNPLDFVLWKA----SKP-------------------------GEPVW-----------------------DSPWG 197
Cdd:pfam09334 155 CGRHLEPTELINPKCvicgTTPevketehyffdlskfqdklrewieeNNPEWpenvknmvlewlkeglkdraisrDLDWG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 198 ---PGRPG-----WhieCSAMcMRYLGTTID--------------------IHGGGQDlIFPHHENEIAQSEAATGQPFV 249
Cdd:pfam09334 235 ipvPGAEGkvfyvW---LDAP-IGYISATKElsgneekwkewwpndpdtelVHFIGKD-IIYFHTIFWPAMLLGAGYRLP 309

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1162405973 250 RYWLHNGLVTINQEKMSKSLGNFFTVREVLARFHPEVVRFFLI-HSHYRSPLDFS 303
Cdd:pfam09334 310 TTVFAHGYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLArNRPETKDTDFS 364
PRK11893 PRK11893
methionyl-tRNA synthetase; Reviewed
 30-293 2.66e-09

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237012 [Multi-domain]  Cd Length: 511  Bit Score: 59.51  E-value: 2.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  30 TVYDDCHIGHARSAVVFDVIVRYLRYRGLQVTWVrnfTDVDD---KIINRARQENTTCQAIAEKYINAFQTDMAALgvar 106
Cdd:PRK11893   11 YPNGKPHIGHAYTTLAADVLARFKRLRGYDVFFL---TGTDEhgqKIQRKAEEAGISPQELADRNSAAFKRLWEAL---- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 107 aDIEP----RATE--HIKEIIDLIAALEAKGFAYQRG--------------------GDVYFPVA--------------R 146
Cdd:PRK11893   84 -NISYddfiRTTDprHKEAVQEIFQRLLANGDIYLGKyegwycvrceefyteselieDGYRCPPTgapvewveeesyffR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 147 FPGYGKLSGRSLEDMQ-----AGARVEVDVQKDNPL-DFVLWKAS-KPGEPVwdsPWGPGRP---------------GWH 204
Cdd:PRK11893  163 LSKYQDKLLELYEANPdfiqpASRRNEVISFVKSGLkDLSISRTNfDWGIPV---PGDPKHViyvwfdaltnyltalGYP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 205 IECSAMCMRYLGT-TIDIHGGGQDLIFPHHENEIAQSEAAtGQPFVRYWLHNGLVTINQEKMSKSLGNFFTVREVLARFH 283
Cdd:PRK11893  240 DDEELLAELFNKYwPADVHLIGKDILRFHAVYWPAFLMAA-GLPLPKRVFAHGFLTLDGEKMSKSLGNVIDPFDLVDEYG 318

                         330
                  ....*....|
gi 1162405973 284 PEVVRFFLIH 293
Cdd:PRK11893  319 VDAVRYFLLR 328
leuS PRK12300
leucyl-tRNA synthetase; Reviewed
 255-333 4.28e-09

leucyl-tRNA synthetase; Reviewed


Pssm-ID: 237049 [Multi-domain]  Cd Length: 897  Bit Score: 59.11  E-value: 4.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 255 NGLVTINQEKMSKSLGNFFTVREVLARFHPEVVRFFLIHS-HYRSPLDFSDAALAEAETALLRLYTPLARIKELSGNPEL 333
Cdd:PRK12300  568 NGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLTSSaELLQDADWREKEVESVRRQLERFYELAKELIEIGGEEEL 647
metG PRK00133
methionyl-tRNA synthetase; Reviewed
 255-303 1.18e-06

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 50.92  E-value: 1.18e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1162405973 255 NGLVTINQEKMSKSLGNFFTVREVLARFHPEVVRFFL--IHSHYRSPLDFS 303
Cdd:PRK00133  320 HGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLaaKLPETIDDLDFN 370
LysS COG1384
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ...
 257-304 4.05e-06

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: 49.42  E-value: 4.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1162405973 257 LVTINQ-EKMSKSLGNFFTVREVLARFHPEVVRFFLihshYRSP-----LDFSD 304
Cdd:COG1384   279 LFLDENgEKISKSKGNGLTVEEWLEYAEPESLRYFM----FRKPkkakdLDFDV 328
metG PRK00133
methionyl-tRNA synthetase; Reviewed
 25-105 8.20e-06

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 48.22  E-value: 8.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  25 YACGvtvydDCHIGHARSAVVFDVIVRYLRYRGLQVTWVRNftdvDDK----IINRARQENTTCQAIAEKYINAFQTDMA 100
Cdd:PRK00133   12 YANG-----PIHLGHLVEYIQADIWVRYQRMRGHEVLFVCA----DDAhgtpIMLKAEKEGITPEELIARYHAEHKRDFA 82


                  ....*
gi 1162405973 101 ALGVA 105
Cdd:PRK00133   83 GFGIS 87
lysK PRK00750
lysyl-tRNA synthetase; Reviewed
 257-292 2.25e-05

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 234829 [Multi-domain]  Cd Length: 510  Bit Score: 46.73  E-value: 2.25e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1162405973 257 LVTINQ-EKMSKSLGNFFTVREVLARFHPEVVRFFLI 292
Cdd:PRK00750  272 LFLDKKgEKISKSKGNVITIEDWLEYAPPESLRLFMF 308
LysRS_core_class_I cd00674
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) ...
 261-292 6.62e-05

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: 45.01  E-value: 6.62e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1162405973 261 NQEKMSKSLGNFFTVREVLARFHPEVVRFFLI 292
Cdd:cd00674   272 GGGKMSSSKGNVITPSDWLEVAPPEVLRYLYA 303
argS PRK01611
arginyl-tRNA synthetase; Reviewed
 36-303 1.06e-04

arginyl-tRNA synthetase; Reviewed


Pssm-ID: 234964 [Multi-domain]  Cd Length: 507  Bit Score: 44.76  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  36 HIGHARSAVVFDVIVRYLRYRGLQVTwvRNFtdvddkIINRA-RQEN---TTCQAIAEKYIN----AFQTDMAALGVA-- 105
Cdd:PRK01611  127 HVGHLRSAVIGDALARILEFAGYDVT--REY------YVNDAgTQIGmliASLELLWRKAVDisldEIKEDLDRLGVHfd 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 106 RADIEPRATEHiKEIIDLIAALEAKGFAYQR-GGDVYFpvaRFPGYGKLsgrsledmqaGARVevdVQKDN--PLDFV-- 180
Cdd:PRK01611  199 VWFSESELYYN-GKVDEVVEDLKEKGLLYVEsDGALWV---RLTEFGDD----------KDRV---LIKSDgtYTYFTrd 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 181 ----LWKASKpgepvwdspwgpgrpgwhiecsamcmryLGTTIDIHGGGQDLIFphheneiAQSEAAT-----GQPFVRY 251
Cdd:PRK01611  262 iayhLYKFER----------------------------FDRVIYVVGADHHGHF-------KRLKAALkalgyDPDALEV 306

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1162405973 252 WLHN--GLVTINQE-KMSKSLGNFFTVREVLA----RFHPEV-------------VRFFLIHSHYRSPLDFS 303
Cdd:PRK01611  307 LLHQmvGLVRGGEGvKMSTRAGNVVTLDDLLDeavgRARELIeekeiaeavgidaVRYFDLSRSRDKDLDFD 378
PLN02959 PLN02959
aminoacyl-tRNA ligase
 255-291 1.63e-04

aminoacyl-tRNA ligase


Pssm-ID: 215518 [Multi-domain]  Cd Length: 1084  Bit Score: 44.29  E-value: 1.63e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1162405973  255 NGLVTINQEKMSKSLGNFFTVREVLARFHPEVVRFFL 291
Cdd:PLN02959   709 NGHLMLNSEKMSKSTGNFLTLRQAIEEFSADATRFAL 745
IleS COG0060
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ...
 264-304 1.88e-04

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: 44.30  E-value: 1.88e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1162405973 264 KMSKSLGNFFTVREVLARFHPEVVRFFLIHSHYRSPLDFSD 304
Cdd:COG0060   603 KMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSD 643
ArgRS_core cd00671
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ...
 36-158 2.09e-04

catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) 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. There are at least three subgroups of ArgRS. One type contains both characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The second subtype lacks the KMSKS motif; however, it has a lysine N-terminal to the HIGH motif, which serves as the functional counterpart to the second lysine of the KMSKS motif. A third group, which is found primarily in archaea and a few bacteria, lacks both the KMSKS motif and the HIGH loop lysine.


Pssm-ID: 185675 [Multi-domain]  Cd Length: 212  Bit Score: 42.55  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  36 HIGHARSAVVFDVIVRYLRYRGLQVTwVRNFtdVDDkiinRARQENTT------CQAIAEKYINAFQTDMAALGVARaDI 109
Cdd:cd00671    16 HVGHLRNAIIGDSLARILEFLGYDVT-REYY--IND----WGRQIGLLilslekWRKLVEESIKADLETYGRLDVRF-DV 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1162405973 110 EPRATEHIKEIIDLIAALEAKGFAYQRGGDVYFpvaRFPGYGKLSGRSL 158
Cdd:cd00671    88 WFGESSYLGLMGKVVELLEELGLLYEEDGALWL---DLTEFGDDKDRVL 133
tRNA-synt_1f pfam01921
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from ...
 263-291 3.92e-04

tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from prokaryotes.


Pssm-ID: 396483  Cd Length: 357  Bit Score: 42.63  E-value: 3.92e-04
                          10        20
                  ....*....|....*....|....*....
gi 1162405973 263 EKMSKSLGNFFTVREVLARFHPEVVRFFL 291
Cdd:pfam01921 278 GKMSSSKGNVITPEDWLEYAPPESLRFLM 306
Anticodon_Ia_Cys_like cd07955
Anticodon-binding domain of cysteinyl tRNA synthetases and domain found in MshC; This domain ...
 344-404 6.68e-04

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: 38.57  E-value: 6.68e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162405973 344 SALSVEEQERLLSLPARFEAAMDDDFNTAQALGHLFEAARllnRVLEHSPTDSAILDLVRR 404
Cdd:cd07955    16 SAVALPDGPDAEALVARLREALADDLDTPKALAALDAWAR---EALSRGGTDPDAPALVRT 73
ValRS_core cd00817
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ...
 225-292 2.29e-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: 40.31  E-value: 2.29e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 225 GQDLIFPHHENEIAQSEAATGQ-PFVRYWLHnGLVTINQ-EKMSKSLGNFFTVREVLARFHPEVVRFFLI 292
Cdd:cd00817   303 GHDIIFFWVARMIMRGLKLTGKlPFKEVYLH-GLVRDEDgRKMSKSLGNVIDPLDVIDGYGADALRFTLA 371
valS TIGR00422
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ...
 202-295 2.82e-03

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: 40.43  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973 202 GWHIECSAMCMRYLGTTIDIhggGQDLIFPHHENEIAQSEAATGQ-PFVRYWLHnGLVTINQ-EKMSKSLGNFFTVREVL 279
Cdd:TIGR00422 465 GWPDETKDLKKFYPTDLLVT---GYDIIFFWVARMIFRSLALTGQvPFKEVYIH-GLVRDEQgRKMSKSLGNVIDPLDVI 540

                          90
                  ....*....|....*.
gi 1162405973 280 ARFHPEVVRFFLIHSH 295
Cdd:TIGR00422 541 EKYGADALRFTLASLV 556
IleRS_core cd00818
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ...
 36-144 6.28e-03

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


Pssm-ID: 173909 [Multi-domain]  Cd Length: 338  Bit Score: 38.75  E-value: 6.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  36 HIGHARSAVVFDVIVRYLRYRGLQVT----W----------------VRNFTDVDDKIINRARQEnttCQAIAEKYINAF 95
Cdd:cd00818    17 HYGHALNKILKDIINRYKTMQGYYVPrrpgWdchglpielkvekelgISGKKDIEKMGIAEFNAK---CREFALRYVDEQ 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1162405973  96 QTDMAALGVaRADIE-PRAT---EHIKEIIDLIAALEAKGFAYQRGGDVYFPV 144
Cdd:cd00818    94 EEQFQRLGV-WVDWEnPYKTmdpEYMESVWWVFKQLHEKGLLYRGYKVVPWPL 145
ArgS COG0018
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ...
 36-156 7.92e-03

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


Pssm-ID: 439789 [Multi-domain]  Cd Length: 574  Bit Score: 38.59  E-value: 7.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  36 HIGHARSAVVFDVIVRYLRYRGLQVT------------------WVR------------------------NFTDVDDKI 73
Cdd:COG0018   132 HVGHLRGAVIGDALARILEAAGYDVTrenyindagtqigklalsLERygeeeiepeskpdgylgdlyvkfhKEYEEDPEL 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405973  74 INRARQENTTCQAIAEKYI-----------NAFQTDMAALGVARADI--EpRATEHIKEIIDLIAALEAKGFAYQRGGDV 140
Cdd:COG0018   212 EDIARELLAKLEPGDEEALelwkkavdwslEEIKEDLKRLGVEFDVWfsE-SSLYDSGAVEEVVEELKEKGLLYESDGAL 290

                         170
                  ....*....|....*.
gi 1162405973 141 YFpvaRFPGYGKLSGR 156
Cdd:COG0018   291 WV---RLTEFGDDKDR 303
 
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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