|
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
|
|
|