|
Name |
Accession |
Description |
Interval |
E-value |
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
2-465 |
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: 806.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 2 TITLYNTLTRQKETFVPLEEGKVKMYVCGPTVYNYIHIGNARPAIVYDTVRNYLEYKGYDVQYVSNFTDVDDKLIKAANE 81
Cdd:COG0215 1 TLKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYLGYKVTYVRNITDVDDKIIKRAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 82 LGEDVPTISERFIKAYFEDVGALGCRKADLHPRVMENMDAIIEFVDQLVKKGYAYESEGDVYFKTRAFEGYGKLSQQSID 161
Cdd:COG0215 81 EGESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEADGDVYFDVRSFPDYGKLSGRNLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 162 ELRSGARIRVGEKKEDALDFALWKAAKEGEISWDSPWGKGRPGWHIECSAMVKKYLGDQIDIHAGGQDLTFPHHENEIAQ 241
Cdd:COG0215 161 DLRAGARVEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 242 SEALTGKTFAKYWLHNGYINIDNEKMSKSLGNFVLVHDIIKQHDPQLLRFFMLSVHYRHPINYSEELLENTKSAFSRLKT 321
Cdd:COG0215 241 SEAATGKPFARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKALERLYN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 322 AYSNLQHRLNSSTNLTEDddqwlekVEEHRKAFEEEMDDDFNTANAISVLFDLAKHANYYLQKDHTADhVITAFIEMFDR 401
Cdd:COG0215 321 ALRRLEEALGAADSSAEE-------IEELREEFIAAMDDDFNTPEALAVLFELVREINKALDEGEDKA-ALAALAALLRA 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1238238996 402 IVSVLGF---------SLGEQELLDQEIEDLIEKRNEARRNRDFALSDQIRDQLKSMNIILEDTAQGTRWKRG 465
Cdd:COG0215 393 LGGVLGLlllepeawqGAAEDELLDALIEALIEERAEARKAKDFARADRIRDELAALGIVLEDTPDGTTWRRK 465
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
3-464 |
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: 741.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 3 ITLYNTLTRQKETFVPLEEGKVKMYVCGPTVYNYIHIGNARPAIVYDTVRNYLEYKGYDVQYVSNFTDVDDKLIKAANEL 82
Cdd:TIGR00435 1 LKLYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLRYLGYKVQYVQNITDIDDKIIKRAREN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 83 GEDVPTISERFIKAYFEDVGALGCRKADLHPRVMENMDAIIEFVDQLVKKGYAYESE-GDVYFKTRAFEGYGKLSQQSID 161
Cdd:TIGR00435 81 GESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDnGDVYFDVSKFKDYGKLSKQDLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 162 ELRSGARIRVGEKKEDALDFALWKAAKEGEISWDSPWGKGRPGWHIECSAMVKKYLGDQIDIHAGGQDLTFPHHENEIAQ 241
Cdd:TIGR00435 161 QLEAGARVDVDEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 242 SEALTGKTFAKYWLHNGYINIDNEKMSKSLGNFVLVHDIIKQHDPQLLRFFMLSVHYRHPINYSEELLENTKSAFSRLKT 321
Cdd:TIGR00435 241 SEAAFGKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKNALERLYK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 322 AYSNLQHRLNSSTNLTEDDdqwLEKVEEHRKAFEEEMDDDFNTANAISVLFDLAKHANYYLQKDHTADHVITAFIEMFDR 401
Cdd:TIGR00435 321 ALRVLDTSLAYSGNQSLNK---FPDEKEFEARFVEAMDDDLNTANALAVLFELAKSINLTFVSKADAALLIEHLIFLESR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238238996 402 IVSVLGFSLG-EQELLD---QEIEDLIEKRNEARRNRDFALSDQIRDQLKSMNIILEDTAQGTRWKR 464
Cdd:TIGR00435 398 LGLLLGLPSKpVQAGSNddlGEIEALIEERSIARKEKDFAKADEIRDELAKKGIVLEDTPQGTTWRR 464
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
15-314 |
0e+00 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 554.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 15 TFVPLEEGKVKMYVCGPTVYNYIHIGNARPAIVYDTVRNYLEYKGYDVQYVSNFTDVDDKLIKAANELGEDVPTISERFI 94
Cdd:pfam01406 1 FFVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 95 KAYFEDVGALGCRKADLHPRVMENMDAIIEFVDQLVKKGYAYESE-GDVYFKTRAFEGYGKLSQQSIDELRSGARIRVGE 173
Cdd:pfam01406 81 EAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDnGDVYFDVSSFPDYGKLSGQNLEQLEAGARGEVSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 174 KKEDALDFALWKAAKEGEISWDSPWGKGRPGWHIECSAMVKKYLGDQIDIHAGGQDLTFPHHENEIAQSEALTGKTFAKY 253
Cdd:pfam01406 161 GKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFDKQLANY 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1238238996 254 WLHNGYINIDNEKMSKSLGNFVLVHDIIKQHDPQLLRFFMLSVHYRHPINYSEELLENTKS 314
Cdd:pfam01406 241 WLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAKS 301
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
5-463 |
1.21e-151 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 442.83 E-value: 1.21e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 5 LYNTLTRQKETFVPLEEGKVKMYVCGPTVYNYIHIGNARPAIVYDTVRNYLEYKGYDVQYVSNFTDVDDKLIKAANELGE 84
Cdd:PLN02946 62 LYNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYLKHLGYEVRYVRNFTDVDDKIIARANELGE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 85 DVPTISERFIKAYFEDVGALGCRKADLHPRVMENMDAIIEFVDQLVKKGYAYESEGDVYFKTRAFEGYGKLSQQSIDELR 164
Cdd:PLN02946 142 DPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVDGDVYFSVDKFPEYGKLSGRKLEDNR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 165 SGARIRVGEKKEDALDFALWKAAKEGEISWDSPWGKGRPGWHIECSAMVKKYLGDQIDIHAGGQDLTFPHHENEIAQSEA 244
Cdd:PLN02946 222 AGERVAVDSRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLVFPHHENEIAQSCA 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 245 LTGKTFAKYWLHNGYINIDNEKMSKSLGNFVLVHDIIKQHDPQLLRFFMLSVHYRHPINYSEELLEntkSAFSRLKTAYS 324
Cdd:PLN02946 302 ACCDSNISYWIHNGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDVQLE---SASERIFYIYQ 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 325 NL--------QHRLNSSTNLTEDDDqwLEKVEEHRKAFEEEMDDDFNTANAISVLFDLAKHANYYL-----QKDHTADHV 391
Cdd:PLN02946 379 TLhdceeslqQHDSTFEKDSVPPDT--LNCINKFHDEFVTSMSDDLHTPVALAALSEPLKTINDLLhtrkgKKQEKRLES 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 392 ITAFIEMFDRIVSVLGF---------------SLGEQELLDQEIEDLIEKRNEARRNRDFALSDQIRDQLKSMNIILEDT 456
Cdd:PLN02946 457 LAALEKKIRDVLSVLGLmptsysealqqlrekALRRAKLTEEQVLQKIEERTVARKNKEYEKSDAIRKDLAAVGIALMDS 536
|
....*..
gi 1238238996 457 AQGTRWK 463
Cdd:PLN02946 537 PDGTTWR 543
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
4-465 |
5.41e-145 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 430.68 E-value: 5.41e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 4 TLYNTLTRQKETFVPLEEGKVKMYVCGPTVYNYIHIGNARPAIVYDTVRNYLEYKGYDVQYVSNFTDVDDKLIKAANELG 83
Cdd:PRK14535 229 TIYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAENG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 84 EDVPTISERFIKAYFEDVGALGCRKADLHPRVMENMDAIIEFVDQLVKKGYAY-ESEGDVYFKTRAFEGYGKLSQQSIDE 162
Cdd:PRK14535 309 ETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYpAANGDVYYAVREFAAYGQLSGKSLDD 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 163 LRSGARIRVGEKKEDALDFALWKAAKEGEISWDSPWGKGRPGWHIECSAMVKKYLGDQIDIHAGGQDLTFPHHENEIAQS 242
Cdd:PRK14535 389 LRAGERVEVDGFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIAQS 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 243 EALTGKT----------------FAKYWLHNGYINIDNEKMSKSLGNFVLVHDIIKQHDPQLLRFFMLSVHYRHPINYSE 306
Cdd:PRK14535 469 VGATGHTcghhhaqthhgqsiasHVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNYSD 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 307 ELLENTKSAFSRLktaYSNLQHRLNSSTNLTEDddqwlekVEEHRKAFEEEMDDDFNTANAISVLFDLAKHANyylqkdH 386
Cdd:PRK14535 549 AHLDDAKGALTRL---YTTLKNTPAAEFMLSEN-------VNDYTRRFYAAMNDDFGTVEAVAVLFELAGEVN------K 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 387 TADHVITAFIEMFDRIVSVLGFSLGE--------QELLDQEIEDLIEKRNEARRNRDFALSDQIRDQLKSMNIILEDTAQ 458
Cdd:PRK14535 613 TNDAQLAGCLKALGGIIGLLQRDPTEflqggaasDGLSNEEIEDLIARRKQARADKNWAESDRIRDLLNEHKIILEDNAG 692
|
....*..
gi 1238238996 459 GTRWKRG 465
Cdd:PRK14535 693 GTTWRRG 699
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
1-464 |
1.19e-137 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 404.69 E-value: 1.19e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 1 MTITLYNTLTRQKETFVPLEEGKVKMYVCGPTVYNYIHIGNARPAIVYDTVRNYLEYKGYDVQYVSNFTDV--------- 71
Cdd:PRK14536 1 MALRLYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTLHFLGYRVTHVMNITDVghltddads 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 72 -DDKLIKAANELGEDVPTISERFIKAYFEDVGALGCRKADLHPRVMENMDAIIEFVDQLVKKGYAYESEGDVYFKTRAFE 150
Cdd:PRK14536 81 gEDKMVKSAQEHGKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCAGGNVYFDIRTFP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 151 GYGKLSQQSIDELRSGARIRVGEKKEDALDFALWKAAKEGE---ISWDSPWGKGRPGWHIECSAMVKKYLGDQIDIHAGG 227
Cdd:PRK14536 161 SYGSLASAAVEDLQAGARIEHDTNKRNPHDFVLWFTRSKFEnhaLTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 228 QDLTFPHHENEIAQSEALTGKTFAKYWLHNGYINIDNEKMSKSLGNFVLVHDII-KQHDPQLLRFFMLSVHYRHPINYSE 306
Cdd:PRK14536 241 VDHIRVHHTNEIAQCEAATGKPWVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQeKGFQPLDYRFFLLGGHYRSQLAFSW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 307 ELLENTKSAFSRLKTAYSNLQHRLNSSTNLT--EDDDQWLEKVEEHRKA--------FEEEMDDDFNTANAISVLFDLAK 376
Cdd:PRK14536 321 EALKTAKAARRSLVRRVARVVDAARATTGSVrgTLAECAAERVAESRASesellltdFRAALEDDFSTPKALSELQKLVK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 377 hanyylQKDHTADHVITAFIEMfDRivsVLGFSL-----------GEQELLDQEIEDLIEKRNEARRNRDFALSDQIRDQ 445
Cdd:PRK14536 401 ------DTSVPPSLCLSVLQAM-DT---VLGLGLiqeataslsaqVPAGPSEEEIGQLIEARAHARQTKDFPLADEIRDK 470
|
490
....*....|....*....
gi 1238238996 446 LKSMNIILEDTAQGTRWKR 464
Cdd:PRK14536 471 LKAEGIELEDTHLGTIWKR 489
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
1-466 |
2.22e-133 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 399.40 E-value: 2.22e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 1 MTITLYNTLTRQKETFVPLEEGKVKMYVCGPTVYNYIHIGNARPAIVYDTVRNYLE-YKGYDVQYVSNFTDVDDKLIKAA 79
Cdd:PTZ00399 38 TGLKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEdYFGYDVFYVMNITDIDDKIIKRA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 80 NELGEDVPT-ISERFIKAYFEDVGALGCRKADLHPRVMENMDAIIEFVDQLVKKGYAYESEGDVYFKTRAFEG----YGK 154
Cdd:PTZ00399 118 REEKLSIFLeLARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYESNGSVYFDVEAFRKaghvYPK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 155 LSQQSI-DELR----SGARIRVGEKKEDALDFALWKAAKEGEISWDSPWGKGRPGWHIECSAMVKKYLGDQIDIHAGGQD 229
Cdd:PTZ00399 198 LEPESVaDEDRiaegEGALGKVSGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGID 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 230 LTFPHHENEIAQSEALTGKT-FAKYWLHNGYINIDNEKMSKSLGNFVLVHDIIKQHDPQLLRFFMLSVHYRHPINYSEEL 308
Cdd:PTZ00399 278 LKFPHHDNELAQSEAYFDKHqWVNYFLHSGHLHIKGLKMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSDES 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 309 LENTKSA-------FSRLKTAYSNLQhrLNSSTNLTEDDDQWLEKVEEHRKAFEEEMDDDFNTANAISVLFDLAKHANYY 381
Cdd:PTZ00399 358 MDEAIEKdkvffnfFANVKIKLRESE--LTSPQKWTQHDFELNELFEETKSAVHAALLDNFDTPEALQALQKLISATNTY 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 382 LQKDHTADH-VITAFIEMFDRIVSVLGF---SLGEQELLDQEIEDLI------------EKRNEARRNRD---------- 435
Cdd:PTZ00399 436 LNSGEQPSApLLRSVAQYVTKILSIFGLvegSDGLGSQGQNSTSENFkplleallrfrdEVRDAAKAEMKlisldkkkkq 515
|
490 500 510
....*....|....*....|....*....|....
gi 1238238996 436 -FALSDQIRDQ-LKSMNIILEDTAQGTR-WKRGE 466
Cdd:PTZ00399 516 lLQLCDKLRDEwLPNLGIRIEDKPDGPSvWKLDD 549
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
4-305 |
5.77e-125 |
|
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: 361.90 E-value: 5.77e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 4 TLYNTLTRQKETFVPLEEGKVKMYVCGPTVYNYIHIGNARPAIVYDTVRNYLEYKGYDVQYVSNFTDVDDKLIKAANELG 83
Cdd:cd00672 1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLGYKVRYVQNITDIDDKIIKRAREEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 84 EDVPTISERFIKAYFEDVGALGCRKADLHPRVmenmdaiiefvdqlvkkgyayesegdvyfktrafegygklsqqsidel 163
Cdd:cd00672 81 LSWKEVADYYTKEFFEDMKALNVLPPDVVPRV------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 164 rsgarirvgekkedaldfalwkaakegeiswdspwgkgrpgWHIECSAMVKKYLGDQIDIHAGGQDLTFPHHENEIAQSE 243
Cdd:cd00672 113 -----------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQSE 151
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238238996 244 ALTGKTFAKYWLHNGYINIDNEKMSKSLGNFVLVHDIIKQHDPQLLRFFMLSVHYRHPINYS 305
Cdd:cd00672 152 AATGKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
5-397 |
4.87e-89 |
|
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: 277.38 E-value: 4.87e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 5 LYNTLTRQketFVPLEEG-KVKMYVCGPTVYNYIHIGNARPAIVYDTVRNYLEYKGYDVQYVSNFTDVDDKLIKAANELG 83
Cdd:TIGR03447 20 LFDTADGQ---VRPVEPGpEAGMYVCGITPYDATHLGHAATYLTFDLVNRVWRDAGHRVHYVQNVTDVDDPLFERAERDG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 84 EDVPTISERFIKAYFEDVGALgcrkADLHPR----VMENMDAIIEFVDQLVKKGYAYESEG----DVYFKTRAFEGYGKL 155
Cdd:TIGR03447 97 VDWRELGTSQIDLFREDMEAL----RVLPPRdyigAVESIDEVVEMVEKLLASGAAYIVEGpeypDVYFSIDATEQFGYE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 156 SQ---QSIDEL---RSGARIRVGekKEDALDFALWKAAKEGEISWDSPWGKGRPGWHIECSAMVKKYLGDQIDIHAGGQD 229
Cdd:TIGR03447 173 SGydrATMLELfaeRGGDPDRPG--KRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 230 LTFPHHENEIAQSEALTG-KTFAKYWLHNGYINIDNEKMSKSLGNFVLVHDIIKQ-HDPQLLRFFMLSVHYRHPINYSEE 307
Cdd:TIGR03447 251 LIFPHHEFSAAHAEAATGvRRMARHYVHAGMIGLDGEKMSKSLGNLVFVSKLRAAgVDPAAIRLGLLAGHYRQDRDWTDA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 308 LLENTKSAFSRLKTAYSnlqhrlnsstnlTEDDDQWLEKVEEHRkafeEEMDDDFNTANAISVLFDLAKHANYYLQKDHT 387
Cdd:TIGR03447 331 VLAEAEARLARWRAALA------------LPDAPDATDLIARLR----QHLANDLDTPAALAAVDGWAADALSYGGSDTE 394
|
410
....*....|
gi 1238238996 388 ADHVITAFIE 397
Cdd:TIGR03447 395 APALVATAVD 404
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
17-371 |
5.31e-86 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 268.72 E-value: 5.31e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 17 VPLEEG-KVKMYVCGPTVYNYIHIGNARPAIVYDTVRNYLEYKGYDVQYVSNFTDVDDKLIKAANELGEDVPTISERFIK 95
Cdd:PRK12418 2 RPVAPGgTATMYVCGITPYDATHLGHAATYLAFDLVNRVWRDAGHDVHYVQNVTDVDDPLLERAARDGVDWRDLAEREIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 96 AYFEDVGALgcrkADLHPR----VMENMDAIIEFVDQLVKKGYAYESEG----DVYFKTRAFEGYGKLSQQSIDEL---- 163
Cdd:PRK12418 82 LFREDMEAL----RVLPPRdyvgAVESIPEVVELVEKLLASGAAYVVDDeeypDVYFSVDATPQFGYESGYDRATMlelf 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 164 --RSGARIRVGekKEDALDFALWKAAKEGEISWDSPWGKGRPGWHIECSAMVKKYLGDQIDIHAGGQDLTFPHHENEIAQ 241
Cdd:PRK12418 158 aeRGGDPDRPG--KRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 242 SEALTGKT-FAKYWLHNGYINIDNEKMSKSLGNFVLVHDIIKQ-HDPQLLRFFMLSVHYRHPINYSEELLENTKSAFSRL 319
Cdd:PRK12418 236 AEAATGERrFARHYVHAGMIGLDGEKMSKSRGNLVFVSRLRAAgVDPAAIRLALLAGHYRADREWTDAVLAEAEARLARW 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1238238996 320 KTAysnlqhrlnSSTNLTEDDDQWLEKVEEHrkafeeeMDDDFNTANAISVL 371
Cdd:PRK12418 316 RAA---------AALPAGPDAADVVARVRAA-------LADDLDTPGALAAV 351
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
1-465 |
1.34e-82 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 262.87 E-value: 1.34e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 1 MTITLYNTLTRQKETFVPLEEgkVKMYVCGPTVYNYIHIGNARPAIVYDTVRNYLEYKGYDVQYVSNFTDV--------- 71
Cdd:PRK14534 1 MLLKLYNTKTKDLSELKNFSD--VKVYACGPTVYNYAHIGNFRTYIFEDLLIKSLRLLKYNVNYAMNITDIghltgdfdd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 72 -DDKLIKAANELGEDVPTISERFIKAYFEDvgalgCRKAD-LHP-RVM---ENMDAIIEFVDQLVKKGYAYESEGDVYFK 145
Cdd:PRK14534 79 gEDKVVKAARERGLTVYEISRFFTEAFFDD-----CKKLNiVYPdKVLvasEYIPIMIEVVKVLEENGFTYFVNGNVYFD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 146 TRAFEGYGKLSQQSIDELR--SGARIRVGEKKEDALDFALW---KAAKEGEISWDSPWGKGRPGWHIECSAMVKKYLGDQ 220
Cdd:PRK14534 154 TSCFKSYGQMAGINLNDFKdmSVSRVEIDKSKRNKSDFVLWftnSKFKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKST 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 221 IDIHAGGQDLTFPHHENEIAQSEALTGKTFAKYWLHNGYINIDNEKMSKSLGNFVLVHDIIKQH-DPQLLRFFMLSVHYR 299
Cdd:PRK14534 234 LDIHLGGVDHIGVHHINEIAIAECYLNKKWCDMFVHGEFLIMEYEKMSKSNNNFITIKDLEDQGfSPLDFRYFCLTAHYR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 300 HPINYSEELLENTKSA----FSRLKTAYSNLQHrlnSSTNLTEDDDQWLEKVEEHR--KAFEEEMDDDFNTANAISVLFD 373
Cdd:PRK14534 314 TQLKFTFNNLKACKIArenmLNKLTYFYSSLDQ---FDLNLLNKDLENIEFSLEKEyyDSFLEKIAFDLNIPQGLALLWD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 374 LAKHANY-YLQKdhtadhVITAFIemFDRIVS------VLGFSLGEQELLDQEIEDLIEKRNEARRNRDFALSDQIRDQL 446
Cdd:PRK14534 391 IIKDDNLsFLSK------LRLAFK--FDEVLSlglreeILREIENHRIVIDDNMKSLIEERRLAKCEKDFKRADEIREYF 462
|
490
....*....|....*....
gi 1238238996 447 KSMNIILEDTAQGTRWKRG 465
Cdd:PRK14534 463 ASKGFVLIDTEEGTKVKRG 481
|
|
| Anticodon_Ia_Cys |
cd07963 |
Anticodon-binding domain of cysteinyl tRNA synthetases; This domain is found in cysteinyl tRNA ... |
306-464 |
1.12e-36 |
|
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: 132.30 E-value: 1.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 306 EELLENTKSAFSRLKTAysnLQHrlnssTNLTEDDDQWlekVEEHRKAFEEEMDDDFNTANAISVLFDLAKHANYYLQKD 385
Cdd:cd07963 1 DDNLEDARAALERLYTA---LRG-----VPPTTVDIDW---GEPFAERFIAAMDDDFNTPEALAVLFELAREINRLKKED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 386 HTADHVITAFIEmfdRIVSVLGF-----------SLGEQELLDQEIEDLIEKRNEARRNRDFALSDQIRDQLKSMNIILE 454
Cdd:cd07963 70 IEKAAALAALLK---ALGGVLGLlqqdpeaflqgGTGEGGLSVAEIEALIAQRNQARKAKDWAEADRIRDELAAQGIILE 146
|
170
....*....|
gi 1238238996 455 DTAQGTRWKR 464
Cdd:cd07963 147 DSPEGTTWRR 156
|
|
| DALR_2 |
smart00840 |
This DALR domain is found in cysteinyl-tRNA-synthetases; |
353-408 |
1.46e-15 |
|
This DALR domain is found in cysteinyl-tRNA-synthetases;
Pssm-ID: 214848 [Multi-domain] Cd Length: 56 Bit Score: 70.67 E-value: 1.46e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1238238996 353 AFEEEMDDDFNTANAISVLFDLAKHANYYLQKDhTADHVITAFIEMFDRIVSVLGF 408
Cdd:smart00840 1 RFEEAMDDDFNTPEALAVLFELAREINRLALKA-TDAEELAALAALLRALGGVLGL 55
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
26-271 |
2.00e-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: 70.20 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 26 MYVCGPTVYNYIHIGNARPAIVYDTVRNYLEYKGYDVQYVSNFTDVDDKLIKAANELGEDVPTISERFIKAYFEDVgalg 105
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKEDV---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 106 crkadlhprvmenmdaiiefvdqlvkkgyayesegdvyfktrafegygklsqqsidelrsgarirvgekkedaldfalwk 185
Cdd:cd00802 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 186 aakegeiswdspwgkgrpGWHIECSAMVKKYLGDQIDIHAGGQDLTFpHHENEIAQSEALTGKTFAkYWLHNGYINI-DN 264
Cdd:cd00802 77 ------------------EYMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKAGGPARP-FGLTFGRVMGaDG 136
|
....*..
gi 1238238996 265 EKMSKSL 271
Cdd:cd00802 137 TKMSKSK 143
|
|
| DALR_2 |
pfam09190 |
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases. |
353-414 |
2.11e-14 |
|
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases.
Pssm-ID: 462711 [Multi-domain] Cd Length: 63 Bit Score: 67.61 E-value: 2.11e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238238996 353 AFEEEMDDDFNTANAISVLFDLAKHANyyLQKDHTADHVITAFIEMFDRIVSVLGFSLGEQE 414
Cdd:pfam09190 1 KFIEAMDDDFNTPEALAVLFELAKEIN--RALKTNDAEAAAALAALLRELGDVLGLLQQDPE 60
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
257-406 |
8.75e-14 |
|
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: 73.22 E-value: 8.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 257 NGYINIDNEKMSKSLGNFVLVHDIIKQHDPQLLRFFMLS-VHYRHPINYSEELLENTKSA---------FSR-LKTAYSN 325
Cdd:COG0143 318 HGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLReVPFGQDGDFSWEDFVARVNSdlandlgnlASRtLSMIHKY 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 326 LQHRLNSSTNLTEDDDQWLEKVEEHRKAFEEEMdDDFNTANAISVLFDLAKHANYYLQ--------KDHT---ADHVITA 394
Cdd:COG0143 398 FDGKVPEPGELTEADEELLAEAEAALEEVAEAM-EAFEFRKALEEIMALARAANKYIDetapwklaKDEDperLATVLYT 476
|
170
....*....|..
gi 1238238996 395 FIEMFdRIVSVL 406
Cdd:COG0143 477 LLEAL-RILAIL 487
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
31-295 |
4.20e-12 |
|
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: 67.06 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 31 PTVYNYIHIGNARPAIVYDTVRNYLEYKGYDVQYVSNfTD--------------VDDKLIKAANELGEDVPTISERFIKA 96
Cdd:cd00668 9 PYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPG-WDthglpielkaerkgGRKKKTIWIEEFREDPKEFVEEMSGE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 97 YFEDVGALGCR--KADLHPRVMENMDAIIEFV-DQLVKKGYAYESEGDVYFKTRAFEGYGKLSQQSIDELRSGA------ 167
Cdd:cd00668 88 HKEDFRRLGISydWSDEYITTEPEYSKAVELIfSRLYEKGLIYRGTHPVRITEQWFFDMPKFKEKLLKALRRGKivpehv 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 168 RIRVGEKKEDALDFAlwkaakegeISWDSPWGKGRPGWHIEC-------SAMVKKYLGDQI--------DIHAGGQDLTF 232
Cdd:cd00668 168 KNRMEAWLESLLDWA---------ISRQRYWGTPLPEDVFDVwfdsgigPLGSLGYPEEKEwfkdsypaDWHLIGKDILR 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238238996 233 PHHENEIAQSEALTGKTFAKYWLHNGYINI-DNEKMSKSLGNFVLVHDIIKQHDPQLLRFFMLS 295
Cdd:cd00668 239 GWANFWITMLVALFGEIPPKNLLVHGFVLDeGGQKMSKSKGNVIDPSDVVEKYGADALRYYLTS 302
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
220-383 |
7.03e-12 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 67.21 E-value: 7.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 220 QIDIHAGGQDLTFPHHENEIAQSEALTGKTFAKYwLHNGYINIDNEKMSKSLGNFVLVHDIIKQHDPQLLRFFMLS-VHY 298
Cdd:PRK11893 254 PADVHLIGKDILRFHAVYWPAFLMAAGLPLPKRV-FAHGFLTLDGEKMSKSLGNVIDPFDLVDEYGVDAVRYFLLReIPF 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 299 RHPINYSEELLENTKSA---------FSR-LKTAYSNLQHRLNSSTNLTEDDDQWLEKVEEHRKAFEEEMdDDFNTANAI 368
Cdd:PRK11893 333 GQDGDFSREAFINRINAdlandlgnlAQRtLSMIAKNFDGKVPEPGALTEADEALLEAAAALLERVRAAM-DNLAFDKAL 411
|
170
....*....|....*
gi 1238238996 369 SVLFDLAKHANYYLQ 383
Cdd:PRK11893 412 EAILALVRAANKYID 426
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
266-365 |
1.34e-09 |
|
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: 60.48 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 266 KMSKSLGNFVLVHDIIKQHDPQLLRFFMLSVHYRHPINYSEELLENTKSAFSRLKTAYS----NLqHRLNSSTNLTEDD- 340
Cdd:COG0060 603 KMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEILKEVRDVYRRLRNTYRfllaNL-DDFDPAEDAVPYEd 681
|
90 100 110
....*....|....*....|....*....|.
gi 1238238996 341 ----DQW-LEKVEEHRKAFEEEMDD-DFNTA 365
Cdd:COG0060 682 lpelDRWiLSRLNELIKEVTEAYDNyDFHRA 712
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
257-383 |
3.44e-09 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 59.01 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 257 NGYINIDNEKMSKSLGNFVLVHDIIKQHDPQLLRFFMLSvhyrhpiNYSEELLEN--TKSAF-----SRLKTAYSNLQHR 329
Cdd:PRK00133 320 HGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAA-------KLPETIDDLdfNWEDFqqrvnSELVGKVVNFASR 392
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238238996 330 LNSSTN--------LTEDDDQWLEKVEEHRKAFEEEMdDDFNTANAISVLFDLAKHANYYLQ 383
Cdd:PRK00133 393 TAGFINkrfdgklpDALADPELLEEFEAAAEKIAEAY-EAREFRKALREIMALADFANKYVD 453
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
258-406 |
1.01e-07 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 54.42 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 258 GYINIDNEKMSKSLGNFVLVHDIIKQHDPQLLRFFML-SVHYRHPINYSEEllentksAF-----SRLKTAYSNLQHR-- 329
Cdd:PRK12267 291 GWWLMKDGKMSKSKGNVVDPEELVDRYGLDALRYYLLrEVPFGSDGDFSPE-------ALverinSDLANDLGNLLNRtv 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 330 ----------LNSSTNLTEDDDQWLEKVEEHRKAFEEEMdDDFNTANAISVLFDLAKHANYY--------LQKDHT---- 387
Cdd:PRK12267 364 aminkyfdgeIPAPGNVTEFDEELIALAEETLKNYEELM-EELQFSRALEEVWKLISRANKYidetapwvLAKDEGkker 442
|
170
....*....|....*....
gi 1238238996 388 ADHVITAFIEMFdRIVSVL 406
Cdd:PRK12267 443 LATVMYHLAESL-RKVAVL 460
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
221-295 |
1.53e-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: 53.02 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 221 IDIHAGGQDLTFPH------HENEIAQSEALTGKTFAKYwLHNGYINIDNEKMSKSLGNFVLVHDIIKQHDPQLLRFFML 294
Cdd:cd00812 225 VDIYIGGKEHAPNHllysrfNHKALFDEGLVTDEPPKGL-IVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLYIL 303
|
.
gi 1238238996 295 S 295
Cdd:cd00812 304 F 304
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
257-382 |
3.85e-07 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 52.56 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 257 NGYINIDNEKMSKSLGNFVLVHDIIKQHDPQLLRFF-MLSVHYRHPINYSEELLENTKSAFSRLKtaysNLQHRLNSSTN 335
Cdd:PRK12300 568 NGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYlTSSAELLQDADWREKEVESVRRQLERFY----ELAKELIEIGG 643
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1238238996 336 LTEDD--DQWLE-KVEEHRKAFEEEMdDDFNTANAI-SVLFDLAKHANYYL 382
Cdd:PRK12300 644 EEELRfiDKWLLsRLNRIIKETTEAM-ESFQTRDAVqEAFYELLNDLRWYL 693
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
257-295 |
9.61e-07 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 50.75 E-value: 9.61e-07
10 20 30
....*....|....*....|....*....|....*....
gi 1238238996 257 NGYINIDNEKMSKSLGNFVLVHDIIKQHDPQLLRFFMLS 295
Cdd:pfam09334 315 HGYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLAR 353
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
257-295 |
1.23e-06 |
|
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function.
Pssm-ID: 173907 [Multi-domain] Cd Length: 319 Bit Score: 50.22 E-value: 1.23e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1238238996 257 NGYINIDNEKMSKSLGNFVLVHDIIKQHDPQLLRFFMLS 295
Cdd:cd00814 271 HGYLTVEGKKMSKSRGNVVDPDDLLERYGADALRYYLLR 309
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
37-296 |
4.21e-06 |
|
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: 48.77 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 37 IHIGNARPAIVYDTVRNYLEYKGYDVQYVSNF--------TDVDDKLIKAANELGEDVPT---------ISERFIKAYFE 99
Cdd:cd00818 16 PHYGHALNKILKDIINRYKTMQGYYVPRRPGWdchglpieLKVEKELGISGKKDIEKMGIaefnakcreFALRYVDEQEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 100 DVGALGcRKADL-HP-RVMEN--MDAIIEFVDQLVKKGYAYESEGDVYFKT--RA----FEGYGKLSQQSIDELRS---- 165
Cdd:cd00818 96 QFQRLG-VWVDWeNPyKTMDPeyMESVWWVFKQLHEKGLLYRGYKVVPWPLiyRAtpqwFIRVTKIKDRLLEANDKvnwi 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 166 --GARIRVGEKKEDALDFAlwkaakegeISWDSPWGKGRPGWHIE-CSAMVKKYLGDQIDI-------HAGGQDLTFPHH 235
Cdd:cd00818 175 peWVKNRFGNWLENRRDWC---------ISRQRYWGTPIPVWYCEdCGEVLVRRVPDVLDVwfdsgsmPYAQLHYPFENE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 236 ENE----------------------IAQSEALTGKTFAKYWLHNGYINI-DNEKMSKSLGNFVLVHDIIKQHDPQLLRFF 292
Cdd:cd00818 246 DFEelfpadfilegsdqtrgwfyslLLLSTALFGKAPYKNVIVHGFVLDeDGRKMSKSLGNYVDPQEVVDKYGADALRLW 325
|
....
gi 1238238996 293 MLSV 296
Cdd:cd00818 326 VASS 329
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
222-305 |
1.87e-04 |
|
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: 43.94 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 222 DIHAGGQDLTFPHHENEIAQSEALTGKTFAKYWLHNGYI-NIDNEKMSKSLGNFVLVHDIIKQHDPQLLRFFMLSVHYRH 300
Cdd:pfam00133 518 DMLLEGSDQTRGWFYRMIMLSTALTGSVPFKNVLVHGLVrDEQGRKMSKSLGNVIDPLDVIDKYGADALRLWLANSDYGR 597
|
....*
gi 1238238996 301 PINYS 305
Cdd:pfam00133 598 DINLS 602
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
239-383 |
2.38e-04 |
|
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: 43.89 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 239 IAQSEALTGKTFAKYWLHNGYI-NIDNEKMSKSLGNFVLVHDIIKQHDPQLLRFFMLSVHYR-HPINYSEELLENTKSAF 316
Cdd:TIGR00422 497 IFRSLALTGQVPFKEVYIHGLVrDEQGRKMSKSLGNVIDPLDVIEKYGADALRFTLASLVTPgDDINFDWKRVESARNFL 576
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238238996 317 SRLKTA-YSNLQH-----RLNSSTNLTEDDDQW-LEKVEEHRKAFEEEMDD-DFNTANAISVLFDLAKHANYYLQ 383
Cdd:TIGR00422 577 NKLWNAsRFVLMNlsddlELSGGEEKLSLADRWiLSKLNRTIKEVRKALDKyRFAEAAKALYEFIWNDFCDWYIE 651
|
|
| Anticodon_Ia_Met |
cd07957 |
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA ... |
334-406 |
4.62e-04 |
|
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA synthetases (MetRS), 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 (CAU). MetRS catalyzes the transfer of methionine to the 3'-end of its tRNA.
Pssm-ID: 153411 [Multi-domain] Cd Length: 129 Bit Score: 40.17 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 334 TNLTEDDDQWLEKVEEHRKAFEEEMdDDFNTANAISVLFDLAKHANYYLQ--------KDHT---ADHVITAFIEMFdRI 402
Cdd:cd07957 32 GGLTEEDEELLEEAEELLEEVAEAM-EELEFRKALEEIMELARAANKYIDetapwklaKEEDperLATVLYVLLELL-RI 109
|
....
gi 1238238996 403 VSVL 406
Cdd:cd07957 110 LAIL 113
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
37-149 |
8.88e-04 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 41.68 E-value: 8.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 37 IHIGNARPAIVYDTVRNYLEYKGYDVQ---YVsNftdvD-----DKLIKAANELGEDVPTISERFIKayfEDVGALGCR- 107
Cdd:PRK01611 126 LHVGHLRSAVIGDALARILEFAGYDVTreyYV-N----DagtqiGMLIASLELLWRKAVDISLDEIK---EDLDRLGVHf 197
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1238238996 108 -KADLHPRVMENmDAIIEFVDQLVKKGYAY-ESEGDVYFKTRAF 149
Cdd:PRK01611 198 dVWFSESELYYN-GKVDEVVEDLKEKGLLYvESDGALWVRLTEF 240
|
|
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
37-151 |
2.72e-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: 40.13 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 37 IHIGNARPAIVYDTVRNYLEYKGYDVQ---YVsNftdvD-----DKLIKAANELGEDVPTISE-----------RFIKAY 97
Cdd:COG0018 131 LHVGHLRGAVIGDALARILEAAGYDVTrenYI-N----DagtqiGKLALSLERYGEEEIEPESkpdgylgdlyvKFHKEY 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 98 FEDVGALGCRKA---DLHP--------------RVMENMDAI-----IEF------------------VDQLVKKGYAYE 137
Cdd:COG0018 206 EEDPELEDIAREllaKLEPgdeealelwkkavdWSLEEIKEDlkrlgVEFdvwfsesslydsgaveevVEELKEKGLLYE 285
|
170
....*....|....
gi 1238238996 138 SEGDVYFKTRAFEG 151
Cdd:COG0018 286 SDGALWVRLTEFGD 299
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
257-291 |
3.58e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 40.05 E-value: 3.58e-03
10 20 30
....*....|....*....|....*....|....*
gi 1238238996 257 NGYINIDNEKMSKSLGNFVLVHDIIKQHDPQLLRF 291
Cdd:PLN02959 709 NGHLMLNSEKMSKSTGNFLTLRQAIEEFSADATRF 743
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
171-337 |
9.14e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 38.77 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 171 VGEKKEDALDFALWKAAKEGEISWDSP----------WGKGRPGWHIECSAMVKKYLgdQIDIHAGGQDLTFPHHENEIA 240
Cdd:PLN02943 479 VARSAEEALEKAREKYGKDVEIYQDPDvldtwfssalWPFSTLGWPDVSAEDFKKFY--PTTVLETGHDILFFWVARMVM 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238996 241 QSEALTGKT-FAKYWLHNGYINIDNEKMSKSLGNFVLVHDIIKQHDPQLLRFFMLSVHYRHPINYSEELLENTKSAFSRL 319
Cdd:PLN02943 557 MGIEFTGTVpFSYVYLHGLIRDSQGRKMSKTLGNVIDPLDTIKEFGTDALRFTLALGTAGQDLNLSTERLTSNKAFTNKL 636
|
170
....*....|....*...
gi 1238238996 320 KTAYSNLQHRLNSSTNLT 337
Cdd:PLN02943 637 WNAGKFVLQNLPSQSDTS 654
|
|
| |
