|
Name |
Accession |
Description |
Interval |
E-value |
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
1-469 |
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: 800.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 1 MIKIYNTLTRKKEEFIPIQKGHVGMYVCGPTVYNYIHIGNARSTIAFDTIRRYFEYRGYKVDFVSNFTDVDDKIIRTANE 80
Cdd:COG0215 1 TLKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYLGYKVTYVRNITDVDDKIIKRAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 81 LGITAPEVADRFIRAFEEDTKALNVEPATLHPRVMDHMPDILAFIQVLVEKGYAYESSGDVYYRTRKFENYGKLSDQSID 160
Cdd:COG0215 81 EGESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEADGDVYFDVRSFPDYGKLSGRNLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 161 ELEVGAsqrTGEEQQQKEDPLDFALWKQAKPGEISWDSPWGKGRPGWHIECSVMATKHLGETIDIHGGGQDLEFPHHENE 240
Cdd:COG0215 161 DLRAGA---RVEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 241 IAQSEAKTGKKFANYWMHNGYVTIgeDDEKMSKSLGNFITVHEMIKNVDPQVLRFFMATTQYRRPIRYSETTMKEAATNL 320
Cdd:COG0215 238 IAQSEAATGKPFARYWMHNGFLTV--NGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKAL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 321 QRLKNTFDNLKfrqetasENLADDADKIALLENLEQRFIEEMDDDFNAANGITVVYELAKWLNTYLDQPKvSAAVLAQGE 400
Cdd:COG0215 316 ERLYNALRRLE-------EALGAADSSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKALDEGE-DKAALAALA 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488251564 401 ALFSQWLSIFGILF---------TAEELLDEEIEQLIEERNQARSNRDFARSDEIRDLLKEKGILLEDTPQGTRWRRE 469
Cdd:COG0215 388 ALLRALGGVLGLLLlepeawqgaAEDELLDALIEALIEERAEARKAKDFARADRIRDELAALGIVLEDTPDGTTWRRK 465
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
2-468 |
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: 612.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 2 IKIYNTLTRKKEEFIPIQKGHVGMYVCGPTVYNYIHIGNARSTIAFDTIRRYFEYRGYKVDFVSNFTDVDDKIIRTANEL 81
Cdd:TIGR00435 1 LKLYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLRYLGYKVQYVQNITDIDDKIIKRAREN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 82 GITAPEVADRFIRAFEEDTKALNVEPATLHPRVMDHMPDILAFIQVLVEKGYAYESS-GDVYYRTRKFENYGKLSDQSID 160
Cdd:TIGR00435 81 GESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDnGDVYFDVSKFKDYGKLSKQDLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 161 ELEVGAsqrTGEEQQQKEDPLDFALWKQAKPGEISWDSPWGKGRPGWHIECSVMATKHLGETIDIHGGGQDLEFPHHENE 240
Cdd:TIGR00435 161 QLEAGA---RVDVDEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 241 IAQSEAKTGKKFANYWMHNGYVTIgeDDEKMSKSLGNFITVHEMIKNVDPQVLRFFMATTQYRRPIRYSETTMKEAATNL 320
Cdd:TIGR00435 238 IAQSEAAFGKQLAKYWMHNGFLMI--DNEKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKNAL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 321 QRLKNTFDNLKFRQETASENladDADKIALLENLEQRFIEEMDDDFNAANGITVVYELAKWLNTYLDQPKVSAAVLAQGE 400
Cdd:TIGR00435 316 ERLYKALRVLDTSLAYSGNQ---SLNKFPDEKEFEARFVEAMDDDLNTANALAVLFELAKSINLTFVSKADAALLIEHLI 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488251564 401 ALFSQWLSIFGILFTAEELL----DEEIEQLIEERNQARSNRDFARSDEIRDLLKEKGILLEDTPQGTRWRR 468
Cdd:TIGR00435 393 FLESRLGLLLGLPSKPVQAGsnddLGEIEALIEERSIARKEKDFAKADEIRDELAKKGIVLEDTPQGTTWRR 464
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
14-316 |
2.62e-176 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 496.12 E-value: 2.62e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 14 EFIPIQKGHVGMYVCGPTVYNYIHIGNARSTIAFDTIRRYFEYRGYKVDFVSNFTDVDDKIIRTANELGITAPEVADRFI 93
Cdd:pfam01406 1 FFVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 94 RAFEEDTKALNVEPATLHPRVMDHMPDILAFIQVLVEKGYAYESS-GDVYYRTRKFENYGKLSDQSIDELEVGAsqrTGE 172
Cdd:pfam01406 81 EAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDnGDVYFDVSSFPDYGKLSGQNLEQLEAGA---RGE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 173 EQQQKEDPLDFALWKQAKPGEISWDSPWGKGRPGWHIECSVMATKHLGETIDIHGGGQDLEFPHHENEIAQSEAKTGKKF 252
Cdd:pfam01406 158 VSEGKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFDKQL 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488251564 253 ANYWMHNGYVTIgeDDEKMSKSLGNFITVHEMIKNVDPQVLRFFMATTQYRRPIRYSETTMKEA 316
Cdd:pfam01406 238 ANYWLHNGHVMI--DGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQA 299
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
4-467 |
1.69e-143 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 422.42 E-value: 1.69e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 4 IYNTLTRKKEEFIPIQKGHVGMYVCGPTVYNYIHIGNARSTIAFDTIRRYFEYRGYKVDFVSNFTDVDDKIIRTANELGI 83
Cdd:PLN02946 62 LYNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYLKHLGYEVRYVRNFTDVDDKIIARANELGE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 84 TAPEVADRFIRAFEEDTKALNVEPATLHPRVMDHMPDILAFIQVLVEKGYAYESSGDVYYRTRKFENYGKLSDQSIDEle 163
Cdd:PLN02946 142 DPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVDGDVYFSVDKFPEYGKLSGRKLED-- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 164 vgasQRTGEE---QQQKEDPLDFALWKQAKPGEISWDSPWGKGRPGWHIECSVMATKHLGETIDIHGGGQDLEFPHHENE 240
Cdd:PLN02946 220 ----NRAGERvavDSRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLVFPHHENE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 241 IAQSEAKTGKKFANYWMHNGYVTIgeDDEKMSKSLGNFITVHEMIKNVDPQVLRFFMATTQYRRPIRYSETTMKEAATNL 320
Cdd:PLN02946 296 IAQSCAACCDSNISYWIHNGFVTV--DSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDVQLESASERI 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 321 QRLKNTF---DNLKFRQETASENLADDADKIALLENLEQRFIEEMDDDFNAANGITVVYELAKWLNTYLDQPKVSAAV-- 395
Cdd:PLN02946 374 FYIYQTLhdcEESLQQHDSTFEKDSVPPDTLNCINKFHDEFVTSMSDDLHTPVALAALSEPLKTINDLLHTRKGKKQEkr 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 396 ---LAQGEALFSQWLSIFGILFTA---------------EELLDEEIEQLIEERNQARSNRDFARSDEIRDLLKEKGILL 457
Cdd:PLN02946 454 lesLAALEKKIRDVLSVLGLMPTSysealqqlrekalrrAKLTEEQVLQKIEERTVARKNKEYEKSDAIRKDLAAVGIAL 533
|
490
....*....|
gi 488251564 458 EDTPQGTRWR 467
Cdd:PLN02946 534 MDSPDGTTWR 543
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
2-464 |
4.89e-138 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 411.35 E-value: 4.89e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 2 IKIYNTLTRKKEEFIPIQKGHVGMYVCGPTVYNYIHIGNARSTIAFDTIRRYFE-YRGYKVDFVSNFTDVDDKIIRTANE 80
Cdd:PTZ00399 40 LKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEdYFGYDVFYVMNITDIDDKIIKRARE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 81 LGI-TAPEVADRFIRAFEEDTKALNVEPATLHPRVMDHMPDILAFIQVLVEKGYAYESSGDVYYRTRKF----ENYGKLS 155
Cdd:PTZ00399 120 EKLsIFLELARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYESNGSVYFDVEAFrkagHVYPKLE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 156 DQSI-DELEVGASQRT-GEEQQQKEDPLDFALWKQAKPGEISWDSPWGKGRPGWHIECSVMATKHLGETIDIHGGGQDLE 233
Cdd:PTZ00399 200 PESVaDEDRIAEGEGAlGKVSGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDLK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 234 FPHHENEIAQSEAKTGKK-FANYWMHNGYVTIgeDDEKMSKSLGNFITVHEMIKNVDPQVLRFFMATTQYRRPIRYSETT 312
Cdd:PTZ00399 280 FPHHDNELAQSEAYFDKHqWVNYFLHSGHLHI--KGLKMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSDES 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 313 MKEAATNLQRLKNTFDNLK--FRQETASENLADDADKIAL---LENLEQRFIEEMDDDFNAANGITVVYELAKWLNTYLD 387
Cdd:PTZ00399 358 MDEAIEKDKVFFNFFANVKikLRESELTSPQKWTQHDFELnelFEETKSAVHAALLDNFDTPEALQALQKLISATNTYLN 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 388 QPK-VSAAVLAQGEALFSQWLSIFGIL-------FTAEELLDEEIEQLIEERNQARSN-RDFARS--------------- 443
Cdd:PTZ00399 438 SGEqPSAPLLRSVAQYVTKILSIFGLVegsdglgSQGQNSTSENFKPLLEALLRFRDEvRDAAKAemklisldkkkkqll 517
|
490 500
....*....|....*....|....*
gi 488251564 444 ---DEIRD-LLKEKGILLEDTPQGT 464
Cdd:PTZ00399 518 qlcDKLRDeWLPNLGIRIEDKPDGP 542
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
1-468 |
9.06e-132 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 396.78 E-value: 9.06e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 1 MIKIYNTLTRKKEEFIPIQKGHVGMYVCGPTVYNYIHIGNARSTIAFDTIRRYFEYRGYKVDFVSNFTDVDDKIIRTANE 80
Cdd:PRK14535 227 MTTIYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 81 LGITAPEVADRFIRAFEEDTKALNVEPATLHPRVMDHMPDILAFIQVLVEKGYAYESS-GDVYYRTRKFENYGKLSDQSI 159
Cdd:PRK14535 307 NGETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAAnGDVYYAVREFAAYGQLSGKSL 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 160 DELEVGasQRTgEEQQQKEDPLDFALWKQAKPGEISWDSPWGKGRPGWHIECSVMATKHLGETIDIHGGGQDLEFPHHEN 239
Cdd:PRK14535 387 DDLRAG--ERV-EVDGFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHEN 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 240 EIAQSEAKTG----------------KKFANYWMHNGYVTIgeDDEKMSKSLGNFITVHEMIKNVDPQVLRFFMATTQYR 303
Cdd:PRK14535 464 EIAQSVGATGhtcghhhaqthhgqsiASHVKYWLHNGFIRV--DGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYR 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 304 RPIRYSETTMKEAATNLQRLKNTFDNLKFRQETASENLADdadkiallenLEQRFIEEMDDDFNAANGITVVYELAKWLN 383
Cdd:PRK14535 542 SPLNYSDAHLDDAKGALTRLYTTLKNTPAAEFMLSENVND----------YTRRFYAAMNDDFGTVEAVAVLFELAGEVN 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 384 TYLDqpkvsaavlAQGEALFSQWLSIFGIL-----------FTAEELLDEEIEQLIEERNQARSNRDFARSDEIRDLLKE 452
Cdd:PRK14535 612 KTND---------AQLAGCLKALGGIIGLLqrdpteflqggAASDGLSNEEIEDLIARRKQARADKNWAESDRIRDLLNE 682
|
490
....*....|....*.
gi 488251564 453 KGILLEDTPQGTRWRR 468
Cdd:PRK14535 683 HKIILEDNAGGTTWRR 698
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
2-468 |
1.72e-129 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 384.27 E-value: 1.72e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 2 IKIYNTLTRKKEEFIPIQKGHVGMYVCGPTVYNYIHIGNARSTIAFDTIRRYFEYRGYKVDFVSNFTDV----------D 71
Cdd:PRK14536 3 LRLYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTLHFLGYRVTHVMNITDVghltddadsgE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 72 DKIIRTANELGITAPEVADRFIRAFEEDTKALNVEPATLHPRVMDHMPDILAFIQVLVEKGYAYESSGDVYYRTRKFENY 151
Cdd:PRK14536 83 DKMVKSAQEHGKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCAGGNVYFDIRTFPSY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 152 GKLSDQSIDELEVGASQrtgEEQQQKEDPLDFALWKQAKPGE---ISWDSPWGKGRPGWHIECSVMATKHLGETIDIHGG 228
Cdd:PRK14536 163 GSLASAAVEDLQAGARI---EHDTNKRNPHDFVLWFTRSKFEnhaLTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 229 GQDLEFPHHENEIAQSEAKTGKKFANYWMHNGYVTIGEDdeKMSKSLGNFITVHEMI-KNVDPQVLRFFMATTQYRRPIR 307
Cdd:PRK14536 240 GVDHIRVHHTNEIAQCEAATGKPWVRYWLHHEFLLMNKG--KMSKSAGQFLTLSSLQeKGFQPLDYRFFLLGGHYRSQLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 308 YSETTMKEAATNLQRLKN----TFDNLKFRQETASENLADDA------DKIALLENLEQRFIEEMDDDFNAANGITVVYE 377
Cdd:PRK14536 318 FSWEALKTAKAARRSLVRrvarVVDAARATTGSVRGTLAECAaervaeSRASESELLLTDFRAALEDDFSTPKALSELQK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 378 LAKWLNTyldQPKVSAAVLAQGEalfsqwlSIFGILFTAE-----------ELLDEEIEQLIEERNQARSNRDFARSDEI 446
Cdd:PRK14536 398 LVKDTSV---PPSLCLSVLQAMD-------TVLGLGLIQEataslsaqvpaGPSEEEIGQLIEARAHARQTKDFPLADEI 467
|
490 500
....*....|....*....|..
gi 488251564 447 RDLLKEKGILLEDTPQGTRWRR 468
Cdd:PRK14536 468 RDKLKAEGIELEDTHLGTIWKR 489
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
3-309 |
4.37e-122 |
|
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: 354.58 E-value: 4.37e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 3 KIYNTLTRKKEEFIPIQKGHVGMYVCGPTVYNYIHIGNARSTIAFDTIRRYFEYRGYKVDFVSNFTDVDDKIIRTANELG 82
Cdd:cd00672 1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLGYKVRYVQNITDIDDKIIKRAREEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 83 ITAPEVADRFIRAFEEDTKALNVEPATLHPRVmdhmpdilafiqvlvekgyayessgdvyyrtrkfenygklsdqsidel 162
Cdd:cd00672 81 LSWKEVADYYTKEFFEDMKALNVLPPDVVPRV------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 163 evgasqrtgeeqqqkedpldfalwkqakpgeiswdspwgkgrpgWHIECSVMATKHLGETIDIHGGGQDLEFPHHENEIA 242
Cdd:cd00672 113 --------------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIA 148
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488251564 243 QSEAKTGKKFANYWMHNGYVTIgeDDEKMSKSLGNFITVHEMIKNVDPQVLRFFMATTQYRRPIRYS 309
Cdd:cd00672 149 QSEAATGKPFARYWLHTGHLTI--DGEKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
2-375 |
6.18e-86 |
|
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: 269.67 E-value: 6.18e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 2 IKIYNTLTRKKEEFIPiqKGHVGMYVCGPTVYNYIHIGNARSTIAFDTIRRYFEYRGYKVDFVSNFTDVDDKIIRTANEL 81
Cdd:TIGR03447 18 LRLFDTADGQVRPVEP--GPEAGMYVCGITPYDATHLGHAATYLTFDLVNRVWRDAGHRVHYVQNVTDVDDPLFERAERD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 82 GITAPEVADRFIRAFEEDTKALNVEPATLHPRVMDHMPDILAFIQVLVEKGYAYE----SSGDVYYRTRKFENYGKLSDQ 157
Cdd:TIGR03447 96 GVDWRELGTSQIDLFREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYIvegpEYPDVYFSIDATEQFGYESGY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 158 SIDELEVGASQRTGE-EQQQKEDPLDFALWKQAKPGEISWDSPWGKGRPGWHIECSVMATKHLGETIDIHGGGQDLEFPH 236
Cdd:TIGR03447 176 DRATMLELFAERGGDpDRPGKRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSDLIFPH 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 237 HENEIAQSEAKTG-KKFANYWMHNGyvTIGEDDEKMSKSLGNFITVHEMIK-NVDPQVLRFFMATTQYRRPIRYSETTMK 314
Cdd:TIGR03447 256 HEFSAAHAEAATGvRRMARHYVHAG--MIGLDGEKMSKSLGNLVFVSKLRAaGVDPAAIRLGLLAGHYRQDRDWTDAVLA 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488251564 315 EAATNLQRlkntfdnlkFRQETASENLADDADKIAllenleqRFIEEMDDDFNAANGITVV 375
Cdd:TIGR03447 334 EAEARLAR---------WRAALALPDAPDATDLIA-------RLRQHLANDLDTPAALAAV 378
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
23-375 |
5.73e-83 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 261.02 E-value: 5.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 23 VGMYVCGPTVYNYIHIGNARSTIAFDTIRRYFEYRGYKVDFVSNFTDVDDKIIRTANELGITAPEVADRFIRAFEEDTKA 102
Cdd:PRK12418 10 ATMYVCGITPYDATHLGHAATYLAFDLVNRVWRDAGHDVHYVQNVTDVDDPLLERAARDGVDWRDLAEREIALFREDMEA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 103 LNVEPATLHPRVMDHMPDILAFIQVLVEKGYAYE----SSGDVYYRTRKFENYGKLSDQSIDELEVGASQRTGE-EQQQK 177
Cdd:PRK12418 90 LRVLPPRDYVGAVESIPEVVELVEKLLASGAAYVvddeEYPDVYFSVDATPQFGYESGYDRATMLELFAERGGDpDRPGK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 178 EDPLDFALWKQAKPGEISWDSPWGKGRPGWHIECSVMATKHLGETIDIHGGGQDLEFPHHENEIAQSEAKTG-KKFANYW 256
Cdd:PRK12418 170 RDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAHAEAATGeRRFARHY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 257 MHNGyvTIGEDDEKMSKSLGNFITVHEMIKN-VDPQVLRFFMATTQYRRPIRYSETTMKEAATNLQRlkntfdnlkFRQE 335
Cdd:PRK12418 250 VHAG--MIGLDGEKMSKSRGNLVFVSRLRAAgVDPAAIRLALLAGHYRADREWTDAVLAEAEARLAR---------WRAA 318
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 488251564 336 TASENLADDADKIAllenleqRFIEEMDDDFNAANGITVV 375
Cdd:PRK12418 319 AALPAGPDAADVVA-------RVRAALADDLDTPGALAAV 351
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
1-468 |
1.06e-79 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 255.55 E-value: 1.06e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 1 MIKIYNTLTRKKEEFIPIQKghVGMYVCGPTVYNYIHIGNARSTIAFDTIRRYFEYRGYKVDFVSNFTDV---------- 70
Cdd:PRK14534 2 LLKLYNTKTKDLSELKNFSD--VKVYACGPTVYNYAHIGNFRTYIFEDLLIKSLRLLKYNVNYAMNITDIghltgdfddg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 71 DDKIIRTANELGITAPEVADRFIRAFEEDTKALNVepatLHP-RVM---DHMPDILAFIQVLVEKGYAYESSGDVYYRTR 146
Cdd:PRK14534 80 EDKVVKAARERGLTVYEISRFFTEAFFDDCKKLNI----VYPdKVLvasEYIPIMIEVVKVLEENGFTYFVNGNVYFDTS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 147 KFENYGKLSDQSIDELEVGASQRTgEEQQQKEDPLDFALW---KQAKPGEISWDSPWGKGRPGWHIECSVMATKHLGETI 223
Cdd:PRK14534 156 CFKSYGQMAGINLNDFKDMSVSRV-EIDKSKRNKSDFVLWftnSKFKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKSTL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 224 DIHGGGQDLEFPHHENEIAQSEAKTGKKFANYWMHNGYVTIgeDDEKMSKSLGNFITVHEM-IKNVDPQVLRFFMATTQY 302
Cdd:PRK14534 235 DIHLGGVDHIGVHHINEIAIAECYLNKKWCDMFVHGEFLIM--EYEKMSKSNNNFITIKDLeDQGFSPLDFRYFCLTAHY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 303 RRPIRYSETTMKeaATNLQRlKNTFDNLKFRQETASE----NLADDADKIALLENLE--QRFIEEMDDDFNAANGITVVY 376
Cdd:PRK14534 313 RTQLKFTFNNLK--ACKIAR-ENMLNKLTYFYSSLDQfdlnLLNKDLENIEFSLEKEyyDSFLEKIAFDLNIPQGLALLW 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 377 ELAKWLNTYLdqpkVSAAVLAqgeALFSQWLSIF---GILFTAEE---LLDEEIEQLIEERNQARSNRDFARSDEIRDLL 450
Cdd:PRK14534 390 DIIKDDNLSF----LSKLRLA---FKFDEVLSLGlreEILREIENhriVIDDNMKSLIEERRLAKCEKDFKRADEIREYF 462
|
490
....*....|....*...
gi 488251564 451 KEKGILLEDTPQGTRWRR 468
Cdd:PRK14534 463 ASKGFVLIDTEEGTKVKR 480
|
|
| Anticodon_Ia_Cys |
cd07963 |
Anticodon-binding domain of cysteinyl tRNA synthetases; This domain is found in cysteinyl tRNA ... |
313-468 |
1.02e-34 |
|
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: 126.91 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 313 MKEAATNLQRLKntfdnlkfrqeTASENLADDADKIALLENLEQRFIEEMDDDFNAANGITVVYELAKWLNTYLDQPKVS 392
Cdd:cd07963 4 LEDARAALERLY-----------TALRGVPPTTVDIDWGEPFAERFIAAMDDDFNTPEALAVLFELAREINRLKKEDIEK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 393 AAVLAqgeALFSQWLSIFGILF-TAEELL----------DEEIEQLIEERNQARSNRDFARSDEIRDLLKEKGILLEDTP 461
Cdd:cd07963 73 AAALA---ALLKALGGVLGLLQqDPEAFLqggtgegglsVAEIEALIAQRNQARKAKDWAEADRIRDELAAQGIILEDSP 149
|
....*..
gi 488251564 462 QGTRWRR 468
Cdd:cd07963 150 EGTTWRR 156
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
25-275 |
2.39e-18 |
|
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: 81.37 E-value: 2.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 25 MYVCGPTVYNYIHIGNARSTIAFDTIRRYFEYRGYKVDFVSNFTDVDDKIIRTANELGITAPEVADRFIRAFEEDtkaln 104
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKED----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 105 vepatlhprvmdhmpdilafiqvlvekgyayessgdvyyrtrkfenygklsdqsidelevgasqrtgeeqqqkedpldfa 184
Cdd:cd00802 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 185 lwkqakpgeisWDspwgkgrpgWHIECSVMATKHLGETIDIHGGGQDLEFpHHENEIAQSEAKTGKKfANYWMHNGYVTi 264
Cdd:cd00802 76 -----------VE---------YMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKAGGPA-RPFGLTFGRVM- 132
|
250
....*....|.
gi 488251564 265 GEDDEKMSKSL 275
Cdd:cd00802 133 GADGTKMSKSK 143
|
|
| DALR_2 |
pfam09190 |
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases. |
357-420 |
1.04e-16 |
|
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases.
Pssm-ID: 462711 [Multi-domain] Cd Length: 63 Bit Score: 74.16 E-value: 1.04e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488251564 357 RFIEEMDDDFNAANGITVVYELAKWLNTYLDQpkVSAAVLAQGEALFSQWLSIFGILF-TAEELL 420
Cdd:pfam09190 1 KFIEAMDDDFNTPEALAVLFELAKEINRALKT--NDAEAAAALAALLRELGDVLGLLQqDPEAFL 63
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
30-300 |
9.72e-16 |
|
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: 77.84 E-value: 9.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 30 PTVYNYIHIGNARSTIAFDTIRRYFEYRGYKVDFVSNFTDVDDKIIRTANELGITAP-------------EVADRFIRAF 96
Cdd:cd00668 9 PYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGGRKKktiwieefredpkEFVEEMSGEH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 97 EEDTKALNV------EPATLHPRVMDHMpdILAFIQvLVEKGYAYESsgdvYYRTRKFENY----GKLSDQSIDELEVGA 166
Cdd:cd00668 89 KEDFRRLGIsydwsdEYITTEPEYSKAV--ELIFSR-LYEKGLIYRG----THPVRITEQWffdmPKFKEKLLKALRRGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 167 ---SQRTGEEQQQKEDPLDFAlwkqakpgeISWDSPWGKGRPGWHIEC-------SVMATKHLGETI--------DIHGG 228
Cdd:cd00668 162 ivpEHVKNRMEAWLESLLDWA---------ISRQRYWGTPLPEDVFDVwfdsgigPLGSLGYPEEKEwfkdsypaDWHLI 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488251564 229 GQDLEFPHHENEIAQSEAKTGK-KFANYWMHnGYVTiGEDDEKMSKSLGNFITVHEMIKNVDPQVLRFFMATT 300
Cdd:cd00668 233 GKDILRGWANFWITMLVALFGEiPPKNLLVH-GFVL-DEGGQKMSKSKGNVIDPSDVVEKYGADALRYYLTSL 303
|
|
| DALR_2 |
smart00840 |
This DALR domain is found in cysteinyl-tRNA-synthetases; |
357-413 |
2.38e-14 |
|
This DALR domain is found in cysteinyl-tRNA-synthetases;
Pssm-ID: 214848 [Multi-domain] Cd Length: 56 Bit Score: 67.21 E-value: 2.38e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 488251564 357 RFIEEMDDDFNAANGITVVYELAKWLNTyLDQPKVSAAVLAQGEALFSQWLSIFGIL 413
Cdd:smart00840 1 RFEEAMDDDFNTPEALAVLFELAREINR-LALKATDAEELAALAALLRALGGVLGLL 56
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
37-461 |
1.67e-12 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 69.14 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 37 HIGNARSTIAFDTIRRYFEYRGYKVDFVsnfTDVDD---KIIRTANELGITAPEVADRFIRAFEEDTKALNVEP----AT 109
Cdd:PRK11893 17 HIGHAYTTLAADVLARFKRLRGYDVFFL---TGTDEhgqKIQRKAEEAGISPQELADRNSAAFKRLWEALNISYddfiRT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 110 LHPRvmdHMPDILAFIQVLVEKGYAYESSGDVYYRTRKFENYGKlSDQSIDELEVGASQRTGEeqQQKEDPLDFALWK-Q 188
Cdd:PRK11893 94 TDPR---HKEAVQEIFQRLLANGDIYLGKYEGWYCVRCEEFYTE-SELIEDGYRCPPTGAPVE--WVEEESYFFRLSKyQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 189 AKPGEISWDSPW---GKGRpgwhiecsvmatkhLGETID-IHGGGQDL-----------EFPHHEN-------------- 239
Cdd:PRK11893 168 DKLLELYEANPDfiqPASR--------------RNEVISfVKSGLKDLsisrtnfdwgiPVPGDPKhviyvwfdaltnyl 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 240 ---EIAQSEAKTGKKFANYW-----------------------MH-----------NGYVTIgeDDEKMSKSLGNFITVH 282
Cdd:PRK11893 234 talGYPDDEELLAELFNKYWpadvhligkdilrfhavywpaflMAaglplpkrvfaHGFLTL--DGEKMSKSLGNVIDPF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 283 EMIKNVDPQVLR-FFMATTQYRRPIRYSETTMKEAATNLqrLKNTFDNL---------KFRQETASENLADDADKIALLE 352
Cdd:PRK11893 312 DLVDEYGVDAVRyFLLREIPFGQDGDFSREAFINRINAD--LANDLGNLaqrtlsmiaKNFDGKVPEPGALTEADEALLE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 353 NLEQ---RFIEEMDD-DFNAAngITVVYELAKWLNTYLDQP------KVSAAVLAQGEALFSQWLSIFGILF------TA 416
Cdd:PRK11893 390 AAAAlleRVRAAMDNlAFDKA--LEAILALVRAANKYIDEQapwslaKTDPERLATVLYTLLEVLRGIAVLLqpvmpeLA 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 488251564 417 EELLDeeieQLIEERNQARSNRDFArsdeiRDLLKEKGILLEDTP 461
Cdd:PRK11893 468 AKILD----QLGVEEDENRDFAALS-----WGRLAPGTTLPKPEP 503
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
26-388 |
4.48e-12 |
|
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439913 [Multi-domain] Cd Length: 544 Bit Score: 67.83 E-value: 4.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 26 YVCGPtvynyIHIGNARSTIAFDTIRRYFEYRGYKVDFVSNftdvDD----KIIRTANELGITAPEVADRFIRAFEEDTK 101
Cdd:COG0143 11 YANGP-----PHIGHLYTYIPADILARYQRLRGHDVLFVTG----TDehgtKIELAAEKEGITPQELVDRIHAEFKELFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 102 ALNV---------EPAtlHPRVMDHmpdilaFIQVLVEKGYAYESSGDVYYRTRK----FENY--GK-----LSDQSIDE 161
Cdd:COG0143 82 KLGIsfdnfirttSPE--HKELVQE------IFQRLYDNGDIYKGEYEGWYCPECerflPDRYveGTcpkcgAEDAYGDQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 162 LEVGASQRTGEEQQQKEDPLD-------------FALWK---------QAKP-------GE-ISW------------DSP 199
Cdd:COG0143 154 CENCGATLEPTELINPRSAISgappelreeehyfFRLSKyqdrllewiEENPdiqpevrNEvLSWlkeglqdlsisrDFD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 200 WGKGRPGW--HiecsVM------------ATKHLGETIdihggGQDLEF----PHHENEIAQSeakTGK---KF-ANYW- 256
Cdd:COG0143 234 WGIPVPGDpgK----VFyvwfdaligyisATKGYADDR-----GLPEDFekywPAPDTELVHF---IGKdiiRFhAIIWp 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 257 ---MH-----------NGYVTIgeDDEKMSKSLGNFITVHEMIKNVDPQVLR-FFMATTQYRRPIRYSETTMKeaatnlQ 321
Cdd:COG0143 302 amlMAaglplpkkvfaHGFLTV--EGEKMSKSRGNVIDPDDLLDRYGPDALRyYLLREVPFGQDGDFSWEDFV------A 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 322 R----LKNTFDNL---------KFRQ---ETASENLADDADKIALLENLEQRFIEEMDD-DFNAAngITVVYELAKWLNT 384
Cdd:COG0143 374 RvnsdLANDLGNLasrtlsmihKYFDgkvPEPGELTEADEELLAEAEAALEEVAEAMEAfEFRKA--LEEIMALARAANK 451
|
....
gi 488251564 385 YLDQ 388
Cdd:COG0143 452 YIDE 455
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
259-369 |
4.03e-11 |
|
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: 65.49 E-value: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 259 NGYVtIGEDDEKMSKSLGNFITVHEMIKNVDPQVLRFFMATTQYRRPIRYSETTMKEAATNLQRLKNTF-------DNLK 331
Cdd:COG0060 593 HGFV-LDEDGRKMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEILKEVRDVYRRLRNTYrfllanlDDFD 671
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 488251564 332 FRQETASENLADDADK--IALLENLEQRFIEEMDD-DFNAA 369
Cdd:COG0060 672 PAEDAVPYEDLPELDRwiLSRLNELIKEVTEAYDNyDFHRA 712
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
26-298 |
6.50e-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: 6.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 26 YVCGPtvynyIHIGNARSTIAFDTIRRYFEYRGYKVDFVSNftdvDD----KIIRTANELGITAPEVADRFIRAFEEDTK 101
Cdd:pfam09334 9 YANGP-----PHLGHLYSYIPADIFARYLRLRGYDVLFVCG----TDehgtPIELKAEKEGITPEELVDRYHEIHREDFK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 102 ALNVE-PATLHPRVMDHMPDILAFIQVLVEKGYAYESSGDVYYRTRKFENygkLSDQSID--ELEVGASQRTG---EEQQ 175
Cdd:pfam09334 80 KFNISfDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERF---LPDRYVEgtCPHCGSEDARGdqcENCG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 176 QKEDPLDFALWKQAkpgeISWDSPW----------------------GKGRPGWHIECSVMATKHLGE-------TIDIH 226
Cdd:pfam09334 157 RHLEPTELINPKCV----ICGTTPEvketehyffdlskfqdklrewiEENNPEWPENVKNMVLEWLKEglkdraiSRDLD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 227 GGgqdLEFPHHENE------------IAQSE--AKTGKKFANYWM------------------H---------------- 258
Cdd:pfam09334 233 WG---IPVPGAEGKvfyvwldapigyISATKelSGNEEKWKEWWPndpdtelvhfigkdiiyfHtifwpamllgagyrlp 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 488251564 259 -----NGYVTIgeDDEKMSKSLGNFITVHEMIKNVDPQVLRFFMA 298
Cdd:pfam09334 310 ttvfaHGYLTY--EGGKMSKSRGNVVWPSEALDRFPPDALRYYLA 352
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
26-299 |
1.01e-08 |
|
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: 56.77 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 26 YVCGPtvynyIHIGNARSTIAFDTIRRYFEYRGYKVDFVSNftdvDD----KIIRTANELGITAPEVADRFIRAFEEDTK 101
Cdd:cd00814 10 YVNGV-----PHLGHLYGTVLADVFARYQRLRGYDVLFVTG----TDehgtKIEQKAEEEGVTPQELCDKYHEIFKDLFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 102 ALNVE--------PATLHPRVMDhmpdilaFIQVLVEKGYAYESSGDVYYRT---------RKFENY----GKLSDQSID 160
Cdd:cd00814 81 WLNISfdyfirttSPRHKEIVQE-------FFKKLYENGYIYEGEYEGLYCVscerflpewREEEHYffrlSKFQDRLLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 161 ELE-----VGASQRTGEEQQQKEDPLdfalwkqaKPGEISWDSP-WG-------------------------------KG 203
Cdd:cd00814 154 WLEknpdfIWPENARNEVLSWLKEGL--------KDLSITRDLFdWGipvpldpgkviyvwfdaligyisatgyyneeWG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 204 RPGWHIEcsvmatkhlGETIDIHGGGQDLeFPHHeneiAQ----SEAKTGKKFANYWMHNGYVTIgeDDEKMSKSLGNFI 279
Cdd:cd00814 226 NSWWWKD---------GWPELVHFIGKDI-IRFH----AIywpaMLLGAGLPLPTRIVAHGYLTV--EGKKMSKSRGNVV 289
|
330 340
....*....|....*....|
gi 488251564 280 TVHEMIKNVDPQVLRFFMAT 299
Cdd:cd00814 290 DPDDLLERYGADALRYYLLR 309
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
35-300 |
1.79e-07 |
|
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173906 [Multi-domain] Cd Length: 314 Bit Score: 52.64 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 35 YIHIGNARSTIAFDTIRRYFEYRGYKVDFVSNFTDVDDKIIRTANELGITAPEVADRFIRAFEEDTKALNV------EPA 108
Cdd:cd00812 14 ALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWTEYNIKKMKEQLKRMGFsydwrrEFT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 109 TLHPRVMDhmpdilaFIQ----VLVEKGYAYESSGDVyyrtrkfeNYGKLSDQSIDELEVGAsqrTGEEQQQKEDPLDFa 184
Cdd:cd00812 94 TCDPEYYK-------FTQwlflKLYEKGLAYKKEAPV--------NWCKLLDQWFLKYSETE---WKEKLLKDLEKLDG- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 185 lwkqakpgeisWDSPWGKGRPGWhIECSvmATKHLGETIDIhgggQDL--EF------------PHHENEIAQSEAKTGK 250
Cdd:cd00812 155 -----------WPEEVRAMQENW-IGCS--RQRYWGTPIPW----TDTmeSLsdstwyyarytdAHNLEQPYEGDLEFDR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 251 KFANYWM-----------------------------------------HNGYVTIGedDEKMSKSLGNFITVHEMIKNVD 289
Cdd:cd00812 217 EEFEYWYpvdiyiggkehapnhllysrfnhkalfdeglvtdeppkgliVQGMVLLE--GEKMSKSKGNVVTPDEAIKKYG 294
|
330
....*....|.
gi 488251564 290 PQVLRFFMATT 300
Cdd:cd00812 295 ADAARLYILFA 305
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
37-135 |
3.62e-07 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 52.50 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 37 HIGNARSTIAFDTIRRYFEYRGYKVDFVsnfTDVD---DKIIRTANELGITAPEVADRFIRAFEEDTKALNVEP----AT 109
Cdd:PRK12267 20 HIGHAYTTIAADALARYKRLQGYDVFFL---TGTDehgQKIQQAAEKAGKTPQEYVDEISAGFKELWKKLDISYdkfiRT 96
|
90 100
....*....|....*....|....*.
gi 488251564 110 LHPRvmdHMPDILAFIQVLVEKGYAY 135
Cdd:PRK12267 97 TDER---HKKVVQKIFEKLYEQGDIY 119
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
241-377 |
5.04e-07 |
|
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: 52.37 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 241 IAQSEAKTGKK-FANYWMHnGYVTiGEDDEKMSKSLGNFITVHEMIKNVDPQVLRFFMAT-TQYRRPIRYSETTMKEAAT 318
Cdd:TIGR00422 497 IFRSLALTGQVpFKEVYIH-GLVR-DEQGRKMSKSLGNVIDPLDVIEKYGADALRFTLASlVTPGDDINFDWKRVESARN 574
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488251564 319 NLQRLKNTFD----NLKFRQETAS-ENLADDADKIAL--LENLEQRFIEEMDD-DFNAANGItvVYE 377
Cdd:TIGR00422 575 FLNKLWNASRfvlmNLSDDLELSGgEEKLSLADRWILskLNRTIKEVRKALDKyRFAEAAKA--LYE 639
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
259-387 |
6.57e-07 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 51.69 E-value: 6.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 259 NGYVTIgeDDEKMSKSLGNFITVHEMIKNVDPQVLRFFMATtqyrrpiRYSEtTMKEAATNL----QR----LKNTFDN- 329
Cdd:PRK00133 320 HGFLTV--EGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAA-------KLPE-TIDDLDFNWedfqQRvnseLVGKVVNf 389
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488251564 330 ----LKFRQETASENLADDADKIALLENLEQRF--IEEMDDDFNAANGITVVYELAKWLNTYLD 387
Cdd:PRK00133 390 asrtAGFINKRFDGKLPDALADPELLEEFEAAAekIAEAYEAREFRKALREIMALADFANKYVD 453
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
241-369 |
4.80e-06 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 49.04 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 241 IAQSEAKTGKK-FANYWMhNGYVtIGEDDEKMSKSLGNFITVHEMIKN--VDpqVLRFFMATTqyrRP---IRYSETTMK 314
Cdd:PRK13208 505 ILRAYLLTGKLpWKNIMI-SGMV-LDPDGKKMSKSKGNVVTPEELLEKygAD--AVRYWAASA---RLgsdTPFDEKQVK 577
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488251564 315 EAATNLQRLKNTF---DNLKFRQETASENLADDADK--IALLENLEQRFIEEMDD-DFNAA 369
Cdd:PRK13208 578 IGRRLLTKLWNASrfvLHFSADPEPDKAEVLEPLDRwiLAKLAKVVEKATEALENyDFAKA 638
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
259-343 |
5.31e-06 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 49.10 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 259 NGYVTIGedDEKMSKSLGNFITVHEMIKNVDPQVLRFFMATT-QYRRPIRYSETTMKEAATNLQRLKNTFDNLKFRQETA 337
Cdd:PRK12300 568 NGFVLLE--GKKMSKSKGNVIPLRKAIEEYGADVVRLYLTSSaELLQDADWREKEVESVRRQLERFYELAKELIEIGGEE 645
|
....*.
gi 488251564 338 SENLAD 343
Cdd:PRK12300 646 ELRFID 651
|
|
| LysRS_core_class_I |
cd00674 |
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) ... |
24-339 |
8.14e-06 |
|
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: 47.70 E-value: 8.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 24 GMYVC--GPTVYNYIHIGNARSTIAFDTIRRYFEYRGYKVDFVSNFTDVD--DKIIRT-----ANELG-----ITAPE-- 87
Cdd:cd00674 19 EKYVVasGISPSGHIHIGNFREVITADLVARALRDLGFEVRLIYSWDDYDrlRKVPPNvpesyEQYIGmplssVPDPFgc 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 88 ---VADRFIRAFEEDTKALNVEPATLHP--------------RVMDHMPDILAfiqVLVEkgyayessgdvyYRTRKF-- 148
Cdd:cd00674 99 cesYAEHFERPFEESLEKLGIEVEFISQsqmyksglydenilIALEKRDEIMA---ILNE------------YRGRELqe 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 149 ---------ENYGKLSDQsIDELEVGASQRTGEEQQQKEDPLDFALWKqakpGEISWDSPWGkgrpgwhiecsvMATKHL 219
Cdd:cd00674 164 twypfmpycEKCGKDTTT-VEAYDAKAGTVTYKCECGHEETVDIRTGR----GKLTWRVDWP------------MRWAIL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 220 GetIDIHGGGQDlefpHHENeiaQSEAKTGKKFANYwMHNG-------YVTIG-EDDEKMSKSLGNFITVHEMIKNVDPQ 291
Cdd:cd00674 227 G--VDFEPFGKD----HASA---GGSYDTGKEIARE-IFGGeppvpvmYEFIGlKGGGKMSSSKGNVITPSDWLEVAPPE 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 488251564 292 VLRFFMAttQYRRPIRYSETTMKeaatnLQRLKNTFDNLK---FRQETASE 339
Cdd:cd00674 297 VLRYLYA--RRKNPEKHIGFDLD-----ILRLYDEYDRLErkyYGVEDAAE 340
|
|
| tRNA-synt_1f |
pfam01921 |
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from ... |
13-307 |
1.58e-05 |
|
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from prokaryotes.
Pssm-ID: 396483 Cd Length: 357 Bit Score: 46.87 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 13 EEFIPIQKGHVGMYVC--GPTVYNYIHIGNARSTIAFDTIRRYFEYRGYKVDFVSNFTDVD---------DKIIRTANEL 81
Cdd:pfam01921 9 EKLLKERKKRGGEYLVasGISPSGLPHIGNFREVLRTDAVRRALRKRGFEVRLIAFSDDMDglrkvpdnvPNSEMLEKYL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 82 G-----ITAPE-----VADRFIRAFEEDTKALNVEPATLHPR--------------VMDHMPDILAfiqVLVEkgyayes 137
Cdd:pfam01921 89 GkpltrIPDPFgchesYAEHFNAPFREFLDRFGIEYEFISATelyksglydeaikiALENRDEIME---ILNP------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 138 sgdvyYRTRK-FENY----------GKlsdqsIDELEVgasqrtgeEQQQKEDPLDFALWKQAKPGEISWDSPWGKgrPG 206
Cdd:pfam01921 159 -----YRGEErQETYspylpicpkcGR-----VLTTPV--------VEYDEGGTIRYRCDECGHEGEVDIRGGNGK--LQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 207 WHIECSvMATKHLGetIDIHGGGQDlefpHHEneiAQSEAKTGKKFANYWMHNG------YVTIG-EDDEKMSKSLGNFI 279
Cdd:pfam01921 219 WKVDWA-MRWAALG--VDFEPFGKD----HAA---PGGSYDTSSRIADEIFGGEppegfpYELILlKGGGKMSSSKGNVI 288
|
330 340
....*....|....*....|....*...
gi 488251564 280 TVHEMIKNVDPQVLRFFMATTQYRRPIR 307
Cdd:pfam01921 289 TPEDWLEYAPPESLRFLMFRTKPKKAKD 316
|
|
| lysK |
PRK00750 |
lysyl-tRNA synthetase; Reviewed |
269-419 |
1.98e-05 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234829 [Multi-domain] Cd Length: 510 Bit Score: 47.11 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 269 EKMSKSLGNFITVHEMIKNVDPQVLRFFMattqYRRPiryseTTMKE-AATNLQRLKNTFDNLK---FRQETASE----- 339
Cdd:PRK00750 279 EKISKSKGNVITIEDWLEYAPPESLRLFM----FARP-----KPAKRlDFDVIPKLVDEYDRFErkyFGQEEKKEeeela 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 340 --------------------NLADdadkIALLENLEQ--RFIEEMDDDFNAANgITVVYELAK----WLNTYlDQPKVSA 393
Cdd:PRK00750 350 npvyhihngnplpvpfrlllNLAQ----IANAEDKEVlwGFLKRYAPGATPET-HPRLDRLVEyainWYRDF-VAPEKKY 423
|
170 180 190
....*....|....*....|....*....|
gi 488251564 394 AVL--AQGEAL--FSQWLSIFGILFTAEEL 419
Cdd:PRK00750 424 RAPteKERAALedLDDALRELADGADAEEI 453
|
|
| LysS |
COG1384 |
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
269-305 |
5.96e-05 |
|
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: 45.57 E-value: 5.96e-05
10 20 30
....*....|....*....|....*....|....*..
gi 488251564 269 EKMSKSLGNFITVHEMIKNVDPQVLRFFMattqYRRP 305
Cdd:COG1384 286 EKISKSKGNGLTVEEWLEYAEPESLRYFM----FRKP 318
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
37-388 |
1.20e-04 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 44.70 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 37 HIGNARSTIAFDTIRRYFEYRGYKVDFVSNFTDVDDKIIRTANELGITAPEVADRFIRAFEEDTKALNVEPATLhPRVMD 116
Cdd:PLN02224 85 HMGSAYTTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEHCDIISQSYRTLWKDLDIAYDKF-IRTTD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 117 hmPDILAFIQVLVEKGYAyesSGDVyYRTRKFENYGKLSDQSIDELEVGASQRTGEEQQ----QKEDPLDFALWKQAKPG 192
Cdd:PLN02224 164 --PKHEAIVKEFYARVFA---NGDI-YRADYEGLYCVNCEEYKDEKELLENNCCPVHQMpcvaRKEDNYFFALSKYQKPL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 193 E------------------------------------ISWDSP-----------WGKGRPGW-------HIECSVMATKH 218
Cdd:PLN02224 238 EdilaqnprfvqpsyrlnevqswiksglrdfsisralVDWGIPvpdddkqtiyvWFDALLGYisaltedNKQQNLETAVS 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 219 LGETIDIHGGGQDLeFPHHENEIAQSEAKTGKKFANYWMHNGYVTigEDDEKMSKSLGNFITVHEMIKNVDPQVLR-FFM 297
Cdd:PLN02224 318 FGWPASLHLIGKDI-LRFHAVYWPAMLMSAGLELPKMVFGHGFLT--KDGMKMGKSLGNTLEPFELVQKFGPDAVRyFFL 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 298 ATTQYRRPIRYSETTMKEAATnlQRLKNTFDNLKFR-----QETASENLADD----ADKIALLENLEqRFIEEMD---DD 365
Cdd:PLN02224 395 REVEFGNDGDYSEDRFIKIVN--AHLANTIGNLLNRtlgllKKNCESTLVEDstvaAEGVPLKDTVE-KLVEKAQtnyEN 471
|
410 420
....*....|....*....|...
gi 488251564 366 FNAANGITVVYELAKWLNTYLDQ 388
Cdd:PLN02224 472 LSLSSACEAVLEIGNAGNTYMDQ 494
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
36-300 |
6.49e-04 |
|
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: 41.83 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 36 IHIGNARSTIAFDTIRRYFEYRGYKVDFVSNFtD-----VDDKIIRtanELGITAP----------------EVADRFIR 94
Cdd:cd00818 16 PHYGHALNKILKDIINRYKTMQGYYVPRRPGW-DchglpIELKVEK---ELGISGKkdiekmgiaefnakcrEFALRYVD 91
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 95 AFEEDTKALNVEPATLHP-RVMD--HMPDILAFIQVLVEKGYAYESSGDVY----YRTRK--FENYGKLSDQSIDELE-- 163
Cdd:cd00818 92 EQEEQFQRLGVWVDWENPyKTMDpeYMESVWWVFKQLHEKGLLYRGYKVVPwpliYRATPqwFIRVTKIKDRLLEANDkv 171
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 164 --VGASQRTGeeqqqkedpldFALW-KQAKPGEISWDSPWGKGRPGWHIE-CSVMATKHLGETIDI-------HGGGQDL 232
Cdd:cd00818 172 nwIPEWVKNR-----------FGNWlENRRDWCISRQRYWGTPIPVWYCEdCGEVLVRRVPDVLDVwfdsgsmPYAQLHY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 233 EFPHHENE----------------------IAQSEAKTGK-KFANYWMHnGYVtIGEDDEKMSKSLGNFITVHEMIKNVD 289
Cdd:cd00818 241 PFENEDFEelfpadfilegsdqtrgwfyslLLLSTALFGKaPYKNVIVH-GFV-LDEDGRKMSKSLGNYVDPQEVVDKYG 318
|
330
....*....|.
gi 488251564 290 PQVLRFFMATT 300
Cdd:cd00818 319 ADALRLWVASS 329
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|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
241-309 |
1.94e-03 |
|
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.
Pssm-ID: 459685 [Multi-domain] Cd Length: 602 Bit Score: 40.86 E-value: 1.94e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488251564 241 IAQSEAKTGKK-FANYWMHnGYVTiGEDDEKMSKSLGNFITVHEMIKNVDPQVLRFFMATTQYRRPIRYS 309
Cdd:pfam00133 535 IMLSTALTGSVpFKNVLVH-GLVR-DEQGRKMSKSLGNVIDPLDVIDKYGADALRLWLANSDYGRDINLS 602
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
257-299 |
2.27e-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: 2.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 488251564 257 MHNGYVtIGEDDEKMSKSLGNFITVHEMIKNVDPQVLRFFMAT 299
Cdd:cd00817 331 YLHGLV-RDEDGRKMSKSLGNVIDPLDVIDGYGADALRFTLAS 372
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