|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
1-450 |
3.20e-149 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 439.46 E-value: 3.20e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 1 MVMGITDVDDKIIKRANEMNISPAS-LASLYEEDFKQDMAALKVLPPTVYLRVTENIPQIISFIEGIIARGNAYStAKGN 79
Cdd:PTZ00399 102 YVMNITDIDDKIIKRAREEKLSIFLeLARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYE-SNGS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 80 VYFDLKS-RGDK--YGKLVgvvPGPV--------GEPA----DSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIEC 144
Cdd:PTZ00399 181 VYFDVEAfRKAGhvYPKLE---PESVadedriaeGEGAlgkvSGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIEC 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 145 SAIASMVFGSQLDIHSGGIDLAFPHHENEIAQCEVFHQCEQWGNYFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKTFSP 224
Cdd:PTZ00399 258 SAMASNILGDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKG--LKMSKSLKNFITIRQALSKYTA 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 225 DVFRFFCLRSSYRSAIDYSDSAMLQAQQLLLGLGSFLEDARAYMKgQLACGSVR-----EAMLWERLSSTKRAVKAALAD 299
Cdd:PTZ00399 336 RQIRLLFLLHKWDKPMNYSDESMDEAIEKDKVFFNFFANVKIKLR-ESELTSPQkwtqhDFELNELFEETKSAVHAALLD 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 300 DFDTPRVVDAILGLAhhgnGQLRASLKEPEGPRSPAVFgAIISYFEQFFETVGISLANQQYVSGD--GSEATLHGVVDEL 377
Cdd:PTZ00399 415 NFDTPEALQALQKLI----SATNTYLNSGEQPSAPLLR-SVAQYVTKILSIFGLVEGSDGLGSQGqnSTSENFKPLLEAL 489
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578825266 378 VRFRQKVRQFALA-MPEATGDARRQQllerqpLLEACDTLRR-GLTAHGINIKDRSSTTSTWELLD----QRTKDQKSA 450
Cdd:PTZ00399 490 LRFRDEVRDAAKAeMKLISLDKKKKQ------LLQLCDKLRDeWLPNLGIRIEDKPDGPSVWKLDDkeelQREKEEKEA 562
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
2-439 |
5.80e-142 |
|
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: 414.11 E-value: 5.80e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 2 VMGITDVDDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPTVYLRVTENIPQIISFIEGIIARGNAYsTAKGNVY 81
Cdd:COG0215 64 VRNITDVDDKIIKRAAEEGESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAY-EADGDVY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 82 FDLKSRGDkYGKLVGVVP-----GPVGEPaDSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQL 156
Cdd:COG0215 143 FDVRSFPD-YGKLSGRNLddlraGARVEV-DEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETF 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 157 DIHSGGIDLAFPHHENEIAQCEVFHqCEQWGNYFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSY 236
Cdd:COG0215 221 DIHGGGIDLIFPHHENEIAQSEAAT-GKPFARYWMHNGFLTVNG--EKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHY 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 237 RSAIDYSDSAmlqaqqlllglgsfLEDAR--------AYMKGQLACGSVREAMlwERLSSTKRAVKAALADDFDTPRVVD 308
Cdd:COG0215 298 RSPLDFSEEA--------------LEEAEkalerlynALRRLEEALGAADSSA--EEIEELREEFIAAMDDDFNTPEALA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 309 AILGLAHHGNgqlraslKEPEGPRSPAVFGAIISYFEQFFETVGISLANQQYVSGDGSEATLHGVVDELVRFRQKVRQ-- 386
Cdd:COG0215 362 VLFELVREIN-------KALDEGEDKAALAALAALLRALGGVLGLLLLEPEAWQGAAEDELLDALIEALIEERAEARKak 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 578825266 387 -FALAmpeatgdarrqqllerqplleacDTLRRGLTAHGINIKDRSSTTsTWEL 439
Cdd:COG0215 435 dFARA-----------------------DRIRDELAALGIVLEDTPDGT-TWRR 464
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
2-247 |
1.77e-112 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 333.18 E-value: 1.77e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 2 VMGITDVDDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPTVYLRVTENIPQIISFIEGIIARGNAYSTAKGNVY 81
Cdd:pfam01406 51 VQNFTDIDDKIIKRARQEGESFRQLAARFIEAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 82 FDlKSRGDKYGKLVGVVPGPV----GEPADSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLD 157
Cdd:pfam01406 131 FD-VSSFPDYGKLSGQNLEQLeagaRGEVSEGKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQID 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 158 IHSGGIDLAFPHHENEIAQCEVFHQcEQWGNYFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYR 237
Cdd:pfam01406 210 IHGGGIDLAFPHHENEIAQSEAAFD-KQLANYWLHNGHVMIDG--EKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYR 286
|
250
....*....|
gi 578825266 238 SAIDYSDSAM 247
Cdd:pfam01406 287 SPLDFSEELL 296
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
2-411 |
8.01e-108 |
|
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: 327.03 E-value: 8.01e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 2 VMGITDVDDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPTVYLRVTENIPQIISFIEGIIARGNAYSTAKGNVY 81
Cdd:TIGR00435 63 VQNITDIDDKIIKRARENGESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 82 FDLkSRGDKYGKLVG-----VVPGPVGEPaDSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQL 156
Cdd:TIGR00435 143 FDV-SKFKDYGKLSKqdldqLEAGARVDV-DEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 157 DIHSGGIDLAFPHHENEIAQCEVFHQcEQWGNYFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSY 236
Cdd:TIGR00435 221 DIHGGGVDLIFPHHENEIAQSEAAFG-KQLAKYWMHNGFLMIDN--EKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHY 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 237 RSAIDYSDSAMLQAQQLLLGLGSFLEDAR---AYMKGQLACGSVREAMLwerlsstKRAVKAALADDFDTPRVVDAILGL 313
Cdd:TIGR00435 298 RSPLDFSEELLEAAKNALERLYKALRVLDtslAYSGNQSLNKFPDEKEF-------EARFVEAMDDDLNTANALAVLFEL 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 314 AHHGNGQlraslkepegPRSPAVFGAIISYFEQFFETVGIslanqqyVSGDGSEATLHGVVDELVRFRQKVRQFALAMPE 393
Cdd:TIGR00435 371 AKSINLT----------FVSKADAALLIEHLIFLESRLGL-------LLGLPSKPVQAGSNDDLGEIEALIEERSIARKE 433
|
410 420
....*....|....*....|.
gi 578825266 394 ---ATGDARRQQLLERQPLLE 411
Cdd:TIGR00435 434 kdfAKADEIRDELAKKGIVLE 454
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
1-243 |
4.60e-78 |
|
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: 241.71 E-value: 4.60e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 1 MVMGITDVDDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPTVYLRVtenipqiisfiegiiargnaystakgnv 80
Cdd:cd00672 61 YVQNITDIDDKIIKRAREEGLSWKEVADYYTKEFFEDMKALNVLPPDVVPRV---------------------------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 81 yfdlksrgdkygklvgvvpgpvgepadsdkrhasdfalwkaakpqevfwaspwgpgrpgWHIECSAIASMVFGSQLDIHS 160
Cdd:cd00672 113 -----------------------------------------------------------WHIECSAMAMKYLGETFDIHG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 161 GGIDLAFPHHENEIAQCEVFHQcEQWGNYFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAI 240
Cdd:cd00672 134 GGVDLIFPHHENEIAQSEAATG-KPFARYWLHTGHLTIDG--EKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPL 210
|
...
gi 578825266 241 DYS 243
Cdd:cd00672 211 DFS 213
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
1-450 |
3.20e-149 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 439.46 E-value: 3.20e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 1 MVMGITDVDDKIIKRANEMNISPAS-LASLYEEDFKQDMAALKVLPPTVYLRVTENIPQIISFIEGIIARGNAYStAKGN 79
Cdd:PTZ00399 102 YVMNITDIDDKIIKRAREEKLSIFLeLARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYE-SNGS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 80 VYFDLKS-RGDK--YGKLVgvvPGPV--------GEPA----DSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIEC 144
Cdd:PTZ00399 181 VYFDVEAfRKAGhvYPKLE---PESVadedriaeGEGAlgkvSGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIEC 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 145 SAIASMVFGSQLDIHSGGIDLAFPHHENEIAQCEVFHQCEQWGNYFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKTFSP 224
Cdd:PTZ00399 258 SAMASNILGDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKG--LKMSKSLKNFITIRQALSKYTA 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 225 DVFRFFCLRSSYRSAIDYSDSAMLQAQQLLLGLGSFLEDARAYMKgQLACGSVR-----EAMLWERLSSTKRAVKAALAD 299
Cdd:PTZ00399 336 RQIRLLFLLHKWDKPMNYSDESMDEAIEKDKVFFNFFANVKIKLR-ESELTSPQkwtqhDFELNELFEETKSAVHAALLD 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 300 DFDTPRVVDAILGLAhhgnGQLRASLKEPEGPRSPAVFgAIISYFEQFFETVGISLANQQYVSGD--GSEATLHGVVDEL 377
Cdd:PTZ00399 415 NFDTPEALQALQKLI----SATNTYLNSGEQPSAPLLR-SVAQYVTKILSIFGLVEGSDGLGSQGqnSTSENFKPLLEAL 489
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578825266 378 VRFRQKVRQFALA-MPEATGDARRQQllerqpLLEACDTLRR-GLTAHGINIKDRSSTTSTWELLD----QRTKDQKSA 450
Cdd:PTZ00399 490 LRFRDEVRDAAKAeMKLISLDKKKKQ------LLQLCDKLRDeWLPNLGIRIEDKPDGPSVWKLDDkeelQREKEEKEA 562
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
2-439 |
5.80e-142 |
|
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: 414.11 E-value: 5.80e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 2 VMGITDVDDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPTVYLRVTENIPQIISFIEGIIARGNAYsTAKGNVY 81
Cdd:COG0215 64 VRNITDVDDKIIKRAAEEGESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAY-EADGDVY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 82 FDLKSRGDkYGKLVGVVP-----GPVGEPaDSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQL 156
Cdd:COG0215 143 FDVRSFPD-YGKLSGRNLddlraGARVEV-DEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETF 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 157 DIHSGGIDLAFPHHENEIAQCEVFHqCEQWGNYFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSY 236
Cdd:COG0215 221 DIHGGGIDLIFPHHENEIAQSEAAT-GKPFARYWMHNGFLTVNG--EKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHY 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 237 RSAIDYSDSAmlqaqqlllglgsfLEDAR--------AYMKGQLACGSVREAMlwERLSSTKRAVKAALADDFDTPRVVD 308
Cdd:COG0215 298 RSPLDFSEEA--------------LEEAEkalerlynALRRLEEALGAADSSA--EEIEELREEFIAAMDDDFNTPEALA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 309 AILGLAHHGNgqlraslKEPEGPRSPAVFGAIISYFEQFFETVGISLANQQYVSGDGSEATLHGVVDELVRFRQKVRQ-- 386
Cdd:COG0215 362 VLFELVREIN-------KALDEGEDKAALAALAALLRALGGVLGLLLLEPEAWQGAAEDELLDALIEALIEERAEARKak 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 578825266 387 -FALAmpeatgdarrqqllerqplleacDTLRRGLTAHGINIKDRSSTTsTWEL 439
Cdd:COG0215 435 dFARA-----------------------DRIRDELAALGIVLEDTPDGT-TWRR 464
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
2-247 |
1.77e-112 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 333.18 E-value: 1.77e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 2 VMGITDVDDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPTVYLRVTENIPQIISFIEGIIARGNAYSTAKGNVY 81
Cdd:pfam01406 51 VQNFTDIDDKIIKRARQEGESFRQLAARFIEAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 82 FDlKSRGDKYGKLVGVVPGPV----GEPADSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLD 157
Cdd:pfam01406 131 FD-VSSFPDYGKLSGQNLEQLeagaRGEVSEGKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQID 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 158 IHSGGIDLAFPHHENEIAQCEVFHQcEQWGNYFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYR 237
Cdd:pfam01406 210 IHGGGIDLAFPHHENEIAQSEAAFD-KQLANYWLHNGHVMIDG--EKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYR 286
|
250
....*....|
gi 578825266 238 SAIDYSDSAM 247
Cdd:pfam01406 287 SPLDFSEELL 296
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
2-411 |
8.01e-108 |
|
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: 327.03 E-value: 8.01e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 2 VMGITDVDDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPTVYLRVTENIPQIISFIEGIIARGNAYSTAKGNVY 81
Cdd:TIGR00435 63 VQNITDIDDKIIKRARENGESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 82 FDLkSRGDKYGKLVG-----VVPGPVGEPaDSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQL 156
Cdd:TIGR00435 143 FDV-SKFKDYGKLSKqdldqLEAGARVDV-DEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 157 DIHSGGIDLAFPHHENEIAQCEVFHQcEQWGNYFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSY 236
Cdd:TIGR00435 221 DIHGGGVDLIFPHHENEIAQSEAAFG-KQLAKYWMHNGFLMIDN--EKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHY 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 237 RSAIDYSDSAMLQAQQLLLGLGSFLEDAR---AYMKGQLACGSVREAMLwerlsstKRAVKAALADDFDTPRVVDAILGL 313
Cdd:TIGR00435 298 RSPLDFSEELLEAAKNALERLYKALRVLDtslAYSGNQSLNKFPDEKEF-------EARFVEAMDDDLNTANALAVLFEL 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 314 AHHGNGQlraslkepegPRSPAVFGAIISYFEQFFETVGIslanqqyVSGDGSEATLHGVVDELVRFRQKVRQFALAMPE 393
Cdd:TIGR00435 371 AKSINLT----------FVSKADAALLIEHLIFLESRLGL-------LLGLPSKPVQAGSNDDLGEIEALIEERSIARKE 433
|
410 420
....*....|....*....|.
gi 578825266 394 ---ATGDARRQQLLERQPLLE 411
Cdd:TIGR00435 434 kdfAKADEIRDELAKKGIVLE 454
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
1-243 |
4.60e-78 |
|
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: 241.71 E-value: 4.60e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 1 MVMGITDVDDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPTVYLRVtenipqiisfiegiiargnaystakgnv 80
Cdd:cd00672 61 YVQNITDIDDKIIKRAREEGLSWKEVADYYTKEFFEDMKALNVLPPDVVPRV---------------------------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 81 yfdlksrgdkygklvgvvpgpvgepadsdkrhasdfalwkaakpqevfwaspwgpgrpgWHIECSAIASMVFGSQLDIHS 160
Cdd:cd00672 113 -----------------------------------------------------------WHIECSAMAMKYLGETFDIHG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 161 GGIDLAFPHHENEIAQCEVFHQcEQWGNYFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAI 240
Cdd:cd00672 134 GGVDLIFPHHENEIAQSEAATG-KPFARYWLHTGHLTIDG--EKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPL 210
|
...
gi 578825266 241 DYS 243
Cdd:cd00672 211 DFS 213
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
2-244 |
6.84e-78 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 252.55 E-value: 6.84e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 2 VMGITDVDDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPTVYLRVTENIPQIISFIEGIIARGNAYSTaKGNVY 81
Cdd:PLN02946 122 VRNFTDVDDKIIARANELGEDPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRV-DGDVY 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 82 FDLKsRGDKYGKLVG--VVPGPVGE--PADSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLD 157
Cdd:PLN02946 201 FSVD-KFPEYGKLSGrkLEDNRAGErvAVDSRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFD 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 158 IHSGGIDLAFPHHENEIAQ----CevfhqCEQWGNYFLHSGHLHAkgKEEKMSKSLKNYITIKDFLKTFSPDVFRFFCLR 233
Cdd:PLN02946 280 IHGGGMDLVFPHHENEIAQscaaC-----CDSNISYWIHNGFVTV--DSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLG 352
|
250
....*....|.
gi 578825266 234 SSYRSAIDYSD 244
Cdd:PLN02946 353 THYRSPINYSD 363
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
2-326 |
1.27e-68 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 231.14 E-value: 1.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 2 VMGITDVDDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPTVYLRVTENIPQIISFIEGIIARGNAYSTAKGNVY 81
Cdd:PRK14535 290 VRNITDIDDKIIARAAENGETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVY 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 82 FDLKSRGdKYGKLVGVVPGPV--GEPADSD--KRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLD 157
Cdd:PRK14535 370 YAVREFA-AYGQLSGKSLDDLraGERVEVDgfKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFD 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 158 IHSGGIDLAFPHHENEIAQ--------CEVFHQCEQWGN-------YFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKTF 222
Cdd:PRK14535 449 IHGGGADLQFPHHENEIAQsvgatghtCGHHHAQTHHGQsiashvkYWLHNGFIRVDG--EKMSKSLGNFFTIREVLKQY 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 223 SPDVFRFFCLRSSYRSAIDYSDSAMLQAQQLLLGLGSFLEDARAymkgqlacgsvREAMLWERLSSTKRAVKAALADDFD 302
Cdd:PRK14535 527 DPEVVRFFILRAHYRSPLNYSDAHLDDAKGALTRLYTTLKNTPA-----------AEFMLSENVNDYTRRFYAAMNDDFG 595
|
330 340
....*....|....*....|....*...
gi 578825266 303 TPRVVDAILGLAHHGN----GQLRASLK 326
Cdd:PRK14535 596 TVEAVAVLFELAGEVNktndAQLAGCLK 623
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
2-438 |
1.76e-59 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 202.46 E-value: 1.76e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 2 VMGITDV----------DDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPTVYLRVTENIPQIISFIEGIIARGN 71
Cdd:PRK14536 65 VMNITDVghltddadsgEDKMVKSAQEHGKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGH 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 72 AYsTAKGNVYFDLKSRGDkYGKLVGVVPGPVGEPA----DSDKRHASDFALW---KAAKPQEVFWASPWGPGRPGWHIEC 144
Cdd:PRK14536 145 TY-CAGGNVYFDIRTFPS-YGSLASAAVEDLQAGAriehDTNKRNPHDFVLWftrSKFENHALTWDSPWGRGYPGWHIEC 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 145 SAIASMVFGSQLDIHSGGIDLAFPHHENEIAQCEVFhQCEQWGNYFLHSGHL-HAKGkeeKMSKSLKNYITIKDFL-KTF 222
Cdd:PRK14536 223 SAMSMKYLGEQCDIHIGGVDHIRVHHTNEIAQCEAA-TGKPWVRYWLHHEFLlMNKG---KMSKSAGQFLTLSSLQeKGF 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 223 SPDVFRFFCLRSSYRSAIDYSDSAMLQAQQLLLGLGSFLedARAYMKGQLACGSVREAM--LWERLSSTKRAVK------ 294
Cdd:PRK14536 299 QPLDYRFFLLGGHYRSQLAFSWEALKTAKAARRSLVRRV--ARVVDAARATTGSVRGTLaeCAAERVAESRASEselllt 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 295 ---AALADDFDTPRVVDAILGLahhgngqlrasLKEPEGPRspavfGAIISYFEQFFETVGISL--ANQQYVSGDGSEAT 369
Cdd:PRK14536 377 dfrAALEDDFSTPKALSELQKL-----------VKDTSVPP-----SLCLSVLQAMDTVLGLGLiqEATASLSAQVPAGP 440
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578825266 370 LHGVVDELVRFRQKVRQ---FALAmpeatgdarrqqllerqplleacDTLRRGLTAHGINIKDRSSTTsTWE 438
Cdd:PRK14536 441 SEEEIGQLIEARAHARQtkdFPLA-----------------------DEIRDKLKAEGIELEDTHLGT-IWK 488
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
2-332 |
3.08e-54 |
|
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: 186.47 E-value: 3.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 2 VMGITDVDDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPTVYLRVTENIPQIISFIEGIIARGNAY---STAKG 78
Cdd:TIGR03447 78 VQNVTDVDDPLFERAERDGVDWRELGTSQIDLFREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYiveGPEYP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 79 NVYFDLKSrGDKYGKLVGVVPGPV--------GEPADSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASM 150
Cdd:TIGR03447 158 DVYFSIDA-TEQFGYESGYDRATMlelfaergGDPDRPGKRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALN 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 151 VFGSQLDIHSGGIDLAFPHHENEIAQCEVFHQCEQWGNYFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKT-FSPDVFRF 229
Cdd:TIGR03447 237 RLGAGFDIQGGGSDLIFPHHEFSAAHAEAATGVRRMARHYVHAGMIGLDG--EKMSKSLGNLVFVSKLRAAgVDPAAIRL 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 230 FCLRSSYRSAIDYSDSAMLQAqqlllglgsflEDARAYMKGQLACGSVREAmlwerlSSTKRAVKAALADDFDTPRVVDA 309
Cdd:TIGR03447 315 GLLAGHYRQDRDWTDAVLAEA-----------EARLARWRAALALPDAPDA------TDLIARLRQHLANDLDTPAALAA 377
|
330 340
....*....|....*....|...
gi 578825266 310 ILGLAhhgNGQLRASLKEPEGPR 332
Cdd:TIGR03447 378 VDGWA---ADALSYGGSDTEAPA 397
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
2-310 |
8.62e-54 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 184.36 E-value: 8.62e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 2 VMGITDVDDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPTVYLRVTENIPQIISFIEGIIARGNAY---STAKG 78
Cdd:PRK12418 51 VQNVTDVDDPLLERAARDGVDWRDLAEREIALFREDMEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYvvdDEEYP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 79 NVYFDLkSRGDKYGKLVGVVPGPV--------GEPADSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASM 150
Cdd:PRK12418 131 DVYFSV-DATPQFGYESGYDRATMlelfaergGDPDRPGKRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALN 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 151 VFGSQLDIHSGGIDLAFPHHENEIAQCEVFHQCEQWGNYFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKT-FSPDVFRF 229
Cdd:PRK12418 210 RLGSGFDIQGGGSDLIFPHHEFSAAHAEAATGERRFARHYVHAGMIGLDG--EKMSKSRGNLVFVSRLRAAgVDPAAIRL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 230 FCLRSSYRSAIDYSDSAmlqaqqlllglgsfLEDARAYM---KGQLACGSVREAMlwerlsSTKRAVKAALADDFDTPRV 306
Cdd:PRK12418 288 ALLAGHYRADREWTDAV--------------LAEAEARLarwRAAAALPAGPDAA------DVVARVRAALADDLDTPGA 347
|
....
gi 578825266 307 VDAI 310
Cdd:PRK12418 348 LAAV 351
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
3-243 |
9.77e-45 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 162.71 E-value: 9.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 3 MGITDV----------DDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPTVYLRVTENIPQIISFIEGIIARGNA 72
Cdd:PRK14534 64 MNITDIghltgdfddgEDKVVKAARERGLTVYEISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 73 YsTAKGNVYFDLkSRGDKYGKLVGVVPGPVGEPA------DSDKRHASDFALW---KAAKPQEVFWASPWGPGRPGWHIE 143
Cdd:PRK14534 144 Y-FVNGNVYFDT-SCFKSYGQMAGINLNDFKDMSvsrveiDKSKRNKSDFVLWftnSKFKDQEMKWDSPWGFGYPSWHLE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 144 CSAIASMVFGSQLDIHSGGIDLAFPHHENEIAQCEVFHQcEQWGNYFLHSGHLHAkgKEEKMSKSLKNYITIKDF-LKTF 222
Cdd:PRK14534 222 CAAMNLEYFKSTLDIHLGGVDHIGVHHINEIAIAECYLN-KKWCDMFVHGEFLIM--EYEKMSKSNNNFITIKDLeDQGF 298
|
250 260
....*....|....*....|.
gi 578825266 223 SPDVFRFFCLRSSYRSAIDYS 243
Cdd:PRK14534 299 SPLDFRYFCLTAHYRTQLKFT 319
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
193-235 |
5.64e-07 |
|
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function.
Pssm-ID: 173907 [Multi-domain] Cd Length: 319 Bit Score: 50.99 E-value: 5.64e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 578825266 193 SGHLHAKGKeeKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSS 235
Cdd:cd00814 271 HGYLTVEGK--KMSKSRGNVVDPDDLLERYGADALRYYLLRER 311
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
156-235 |
9.71e-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: 50.32 E-value: 9.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578825266 156 LDIHSGGIDLA--------FPHHeneiaqceVFHQCEQWGNY----FLHSGHLHAKGkeEKMSKSLKNYITIKDFLKTFS 223
Cdd:cd00812 225 VDIYIGGKEHApnhllysrFNHK--------ALFDEGLVTDEppkgLIVQGMVLLEG--EKMSKSKGNVVTPDEAIKKYG 294
|
90
....*....|..
gi 578825266 224 PDVFRFFCLRSS 235
Cdd:cd00812 295 ADAARLYILFAA 306
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
193-233 |
1.70e-06 |
|
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: 50.11 E-value: 1.70e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 578825266 193 SGHLHAKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLR 233
Cdd:COG0143 318 HGFLTVEG--EKMSKSRGNVIDPDDLLDRYGPDALRYYLLR 356
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
193-245 |
3.72e-05 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 45.74 E-value: 3.72e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 578825266 193 SGHLHAKGKeeKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSA-IDYSDS 245
Cdd:pfam09334 315 HGYLTYEGG--KMSKSRGNVVWPSEALDRFPPDALRYYLARNRPETKdTDFSWE 366
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
194-244 |
1.54e-04 |
|
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439830 [Multi-domain] Cd Length: 931 Bit Score: 44.30 E-value: 1.54e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 578825266 194 GH-LHAKGKeeKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYSD 244
Cdd:COG0060 594 GFvLDEDGR--KMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSD 643
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
187-233 |
2.47e-04 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 43.33 E-value: 2.47e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 578825266 187 GNYFLhsghlhaKGKEEKMSKSLKNYITIKDFLKTFSPDVFRFFCLR 233
Cdd:PRK11893 289 AHGFL-------TLDGEKMSKSLGNVIDPFDLVDEYGVDAVRYFLLR 328
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
188-243 |
3.52e-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: 42.78 E-value: 3.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 578825266 188 NYFLHSGHLHAKGKeeKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYS 243
Cdd:pfam00133 549 NVLVHGLVRDEQGR--KMSKSLGNVIDPLDVIDKYGADALRLWLANSDYGRDINLS 602
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
203-230 |
4.08e-04 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 42.93 E-value: 4.08e-04
10 20
....*....|....*....|....*...
gi 578825266 203 EKMSKSLKNYITIKDFLKTFSPDVFRFF 230
Cdd:PRK12300 576 KKMSKSKGNVIPLRKAIEEYGADVVRLY 603
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
184-231 |
1.41e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 41.21 E-value: 1.41e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 578825266 184 EQWGNYFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFC 231
Cdd:PLN02959 700 EHWPRGFRCNGHLMLNS--EKMSKSTGNFLTLRQAIEEFSADATRFAL 745
|
|
| LysS |
COG1384 |
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
203-243 |
2.63e-03 |
|
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA synthetase, class I is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440994 [Multi-domain] Cd Length: 525 Bit Score: 40.18 E-value: 2.63e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 578825266 203 EKMSKSLKNYITIKDFLKTFSPDVFRFFCLRsSYRSAIDYS 243
Cdd:COG1384 286 EKISKSKGNGLTVEEWLEYAEPESLRYFMFR-KPKKAKDLD 325
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
203-230 |
3.14e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 40.14 E-value: 3.14e-03
10 20
....*....|....*....|....*....
gi 578825266 203 EKMSKSlKNY-ITIKDFLKTFSPDVFRFF 230
Cdd:PRK00133 328 AKMSKS-RGTfIWARTYLDHLDPDYLRYY 355
|
|
| tRNA-synt_1f |
pfam01921 |
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from ... |
201-241 |
3.66e-03 |
|
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from prokaryotes.
Pssm-ID: 396483 Cd Length: 357 Bit Score: 39.55 E-value: 3.66e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 578825266 201 KEEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAID 241
Cdd:pfam01921 276 GGGKMSSSKGNVITPEDWLEYAPPESLRFLMFRTKPKKAKD 316
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
195-234 |
8.56e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 38.63 E-value: 8.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 578825266 195 HLHAKG----KEEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRS 234
Cdd:PRK12267 286 KVFAHGwwlmKDGKMSKSKGNVVDPEELVDRYGLDALRYYLLRE 329
|
|
|