|
Name |
Accession |
Description |
Interval |
E-value |
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
2-462 |
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: 705.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 2 ELRLYDTLTRDKRPFTPIDPANVRMYVCGPTVYDFAHIGNARPVIVFDVLFRLLRHLYgeAHVKYVRNITDVDDKINDRA 81
Cdd:COG0215 1 TLKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYLG--YKVTYVRNITDVDDKIIKRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 82 ARDypglplNEAIRKVTEQTERQFHDDVDALGCLRPTVEPRATEHIGEMRSIIEKLVAGGFAYVEQDHVLFSPSAMnaan 161
Cdd:COG0215 79 AEE------GESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEADGDVYFDVRSF---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 162 gvlPRYGSLANRSLDEMIAGARVDVAPYKRDATDFVLWKPSKPGEPSWPSPAGiatPGRPGWHIECSAMSWKHLGETFDI 241
Cdd:COG0215 149 ---PDYGKLSGRNLDDLRAGARVEVDEEKRDPLDFALWKAAKPGEPSWDSPWG---RGRPGWHIECSAMSTKYLGETFDI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 242 HGGGIDLVFPHHENEVAQSCCAFHtERMAQTWMHNGFLQVEGEKMSKSLGNFITIRELLATnkfggrsWDGATLRLAMLK 321
Cdd:COG0215 223 HGGGIDLIFPHHENEIAQSEAATG-KPFARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKK-------YDPEVLRFFLLS 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 322 THYRQPIDWTVDALHEAEKAILDWSDFAKDATPVR-------------CDEVIAALTDDLNTPKMIAELHALRRAG---- 384
Cdd:COG0215 295 AHYRSPLDFSEEALEEAEKALERLYNALRRLEEALgaadssaeeieelREEFIAAMDDDFNTPEALAVLFELVREInkal 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 385 -----------KADELRGAMQLLGINP-------VVRAPVDLDATAKSLIEARTAARANKDWKESDRIRDELAAMGVVLK 446
Cdd:COG0215 375 degedkaalaaLAALLRALGGVLGLLLlepeawqGAAEDELLDALIEALIEERAEARKAKDFARADRIRDELAALGIVLE 454
|
490
....*....|....*.
gi 499470912 447 DGKdaDGksvTTWELA 462
Cdd:COG0215 455 DTP--DG---TTWRRK 465
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
3-460 |
3.47e-163 |
|
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: 468.79 E-value: 3.47e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 3 LRLYDTLTRDKRPFTPIDPANVRMYVCGPTVYDFAHIGNARPVIVFDVLFRLLRHLYGEahVKYVRNITDVDDKINDRAa 82
Cdd:TIGR00435 1 LKLYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLRYLGYK--VQYVQNITDIDDKIIKRA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 83 rdypgLPLNEAIRKVTEQTERQFHDDVDALGCLRPTVEPRATEHIGEMRSIIEKLVAGGFAYV-EQDHVLFSPSAmnaan 161
Cdd:TIGR00435 78 -----RENGESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVsDNGDVYFDVSK----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 162 gvLPRYGSLANRSLDEMIAGARVDVAPYKRDATDFVLWKPSKPGEPSWPSPAGIatpGRPGWHIECSAMSWKHLGETFDI 241
Cdd:TIGR00435 148 --FKDYGKLSKQDLDQLEAGARVDVDEAKRNKLDFVLWKSSKEGEPKWDSPWGK---GRPGWHIECSAMNDKYLGDQIDI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 242 HGGGIDLVFPHHENEVAQSCCAFHTErMAQTWMHNGFLQVEGEKMSKSLGNFITIRELLatNKFggrswDGATLRLAMLK 321
Cdd:TIGR00435 223 HGGGVDLIFPHHENEIAQSEAAFGKQ-LAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVL--KNY-----DPEILRYFLLS 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 322 THYRQPIDWTVDALHEAEKAI-------------LDWSD-FAKDATPVR---CDEVIAALTDDLNTPKMIAELHAL---- 380
Cdd:TIGR00435 295 VHYRSPLDFSEELLEAAKNALerlykalrvldtsLAYSGnQSLNKFPDEkefEARFVEAMDDDLNTANALAVLFELaksi 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 381 --------RRAGKADELRGAMQLLGI------NPVVRAPVDLDATAKSLIEARTAARANKDWKESDRIRDELAAMGVVLK 446
Cdd:TIGR00435 375 nltfvskaDAALLIEHLIFLESRLGLllglpsKPVQAGSNDDLGEIEALIEERSIARKEKDFAKADEIRDELAKKGIVLE 454
|
490
....*....|....
gi 499470912 447 DGKDAdgksvTTWE 460
Cdd:TIGR00435 455 DTPQG-----TTWR 463
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
15-340 |
5.73e-142 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 408.68 E-value: 5.73e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 15 PFTPIDPANVRMYVCGPTVYDFAHIGNARPVIVFDVLFRLLRHLYGEahVKYVRNITDVDDKINDRAARDYpglplnEAI 94
Cdd:pfam01406 1 FFVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQALGYD--VQFVQNFTDIDDKIIKRARQEG------ESF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 95 RKVTEQTERQFHDDVDALGCLRPTVEPRATEHIGEMRSIIEKLVAGGFAYV-EQDHVLFSPSAmnaangvLPRYGSLANR 173
Cdd:pfam01406 73 RQLAARFIEAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVsDNGDVYFDVSS-------FPDYGKLSGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 174 SLDEMIAGARVDVAPYKRDATDFVLWKPSKPGEPSWPSPAGiatPGRPGWHIECSAMSWKHLGETFDIHGGGIDLVFPHH 253
Cdd:pfam01406 146 NLEQLEAGARGEVSEGKRDPLDFALWKASKEGEPSWDSPWG---KGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHH 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 254 ENEVAQSCCAFHTErMAQTWMHNGFLQVEGEKMSKSLGNFITIRELLATnkfggrsWDGATLRLAMLKTHYRQPIDWTVD 333
Cdd:pfam01406 223 ENEIAQSEAAFDKQ-LANYWLHNGHVMIDGEKMSKSLGNFFTIRDVLKR-------YDPEILRYFLLSVHYRSPLDFSEE 294
|
....*..
gi 499470912 334 ALHEAEK 340
Cdd:pfam01406 295 LLEQAKS 301
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
2-462 |
2.91e-129 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 385.44 E-value: 2.91e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 2 ELRLYDTLTRDKRPFTPIDPANVRMYVCGPTVYDFAHIGNARPVIVFDVLFRLLRHLygEAHVKYVRNITDVDDKINDRA 81
Cdd:PLN02946 59 ELHLYNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYLKHL--GYEVRYVRNFTDVDDKIIARA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 82 ARdypglpLNEAIRKVTEQTERQFHDDVDALGCLRPTVEPRATEHIGEMRSIIEKLVAGGFAYVEQDHVLFSPSAmnaan 161
Cdd:PLN02946 137 NE------LGEDPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVDGDVYFSVDK----- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 162 gvLPRYGSLANRSLDEMIAGARVDVAPYKRDATDFVLWKPSKPGEPSWPSPAGiatPGRPGWHIECSAMSWKHLGETFDI 241
Cdd:PLN02946 206 --FPEYGKLSGRKLEDNRAGERVAVDSRKKNPADFALWKAAKEGEPFWDSPWG---PGRPGWHIECSAMSAAYLGHSFDI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 242 HGGGIDLVFPHHENEVAQSCCAFHTERMAQtWMHNGFLQVEGEKMSKSLGNFITIRELLATnkfggrsWDGATLRLAMLK 321
Cdd:PLN02946 281 HGGGMDLVFPHHENEIAQSCAACCDSNISY-WIHNGFVTVDSEKMSKSLGNFFTIRQVIDL-------YHPLALRLFLLG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 322 THYRQPIDWTV--------------DALHEAEKAI-LDWSDFAKDATPVRC--------DEVIAALTDDLNTP------- 371
Cdd:PLN02946 353 THYRSPINYSDvqlesaserifyiyQTLHDCEESLqQHDSTFEKDSVPPDTlncinkfhDEFVTSMSDDLHTPvalaals 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 372 ---KMIAELHALRRAGKADE-----------LRGAMQLLGINPVVRAPVDLDATAKSL-------------IEARTAARA 424
Cdd:PLN02946 433 eplKTINDLLHTRKGKKQEKrleslaalekkIRDVLSVLGLMPTSYSEALQQLREKALrraklteeqvlqkIEERTVARK 512
|
490 500 510
....*....|....*....|....*....|....*...
gi 499470912 425 NKDWKESDRIRDELAAMGVVLKDGKDAdgksvTTWELA 462
Cdd:PLN02946 513 NKEYEKSDAIRKDLAAVGIALMDSPDG-----TTWRPA 545
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
4-331 |
2.15e-108 |
|
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: 319.52 E-value: 2.15e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 4 RLYDTLTRDKRPFTPIDPANVRMYVCGPTVYDFAHIGNARPVIVFDVLFRLLRHL-YGeahVKYVRNITDVDDKINDRAA 82
Cdd:cd00672 1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLgYK---VRYVQNITDIDDKIIKRAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 83 RDypglplNEAIRKVTEQTERQFHDDVDALGCLRPTVEPRAtehigemrsiieklvaggfayveqdhvlfspsamnaang 162
Cdd:cd00672 78 EE------GLSWKEVADYYTKEFFEDMKALNVLPPDVVPRV--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 163 vlprygslanrsldemiagarvdvapykrdatdfvlwkpskpgepswpspagiatpgrpgWHIECSAMSWKHLGETFDIH 242
Cdd:cd00672 113 ------------------------------------------------------------WHIECSAMAMKYLGETFDIH 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 243 GGGIDLVFPHHENEVAQSCCAFHtERMAQTWMHNGFLQVEGEKMSKSLGNFITIRELLATnkfggrsWDGATLRLAMLKT 322
Cdd:cd00672 133 GGGVDLIFPHHENEIAQSEAATG-KPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKK-------YDPEVLRLALLSS 204
|
....*....
gi 499470912 323 HYRQPIDWT 331
Cdd:cd00672 205 HYRSPLDFS 213
|
|
| DALR_2 |
smart00840 |
This DALR domain is found in cysteinyl-tRNA-synthetases; |
359-398 |
2.36e-03 |
|
This DALR domain is found in cysteinyl-tRNA-synthetases;
Pssm-ID: 214848 [Multi-domain] Cd Length: 56 Bit Score: 36.01 E-value: 2.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 499470912 359 EVIAALTDDLNTPKMIAELHALRRAGK---------------ADELRGAMQLLGI 398
Cdd:smart00840 1 RFEEAMDDDFNTPEALAVLFELAREINrlalkatdaeelaalAALLRALGGVLGL 55
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
2-462 |
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: 705.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 2 ELRLYDTLTRDKRPFTPIDPANVRMYVCGPTVYDFAHIGNARPVIVFDVLFRLLRHLYgeAHVKYVRNITDVDDKINDRA 81
Cdd:COG0215 1 TLKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYLG--YKVTYVRNITDVDDKIIKRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 82 ARDypglplNEAIRKVTEQTERQFHDDVDALGCLRPTVEPRATEHIGEMRSIIEKLVAGGFAYVEQDHVLFSPSAMnaan 161
Cdd:COG0215 79 AEE------GESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEADGDVYFDVRSF---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 162 gvlPRYGSLANRSLDEMIAGARVDVAPYKRDATDFVLWKPSKPGEPSWPSPAGiatPGRPGWHIECSAMSWKHLGETFDI 241
Cdd:COG0215 149 ---PDYGKLSGRNLDDLRAGARVEVDEEKRDPLDFALWKAAKPGEPSWDSPWG---RGRPGWHIECSAMSTKYLGETFDI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 242 HGGGIDLVFPHHENEVAQSCCAFHtERMAQTWMHNGFLQVEGEKMSKSLGNFITIRELLATnkfggrsWDGATLRLAMLK 321
Cdd:COG0215 223 HGGGIDLIFPHHENEIAQSEAATG-KPFARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKK-------YDPEVLRFFLLS 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 322 THYRQPIDWTVDALHEAEKAILDWSDFAKDATPVR-------------CDEVIAALTDDLNTPKMIAELHALRRAG---- 384
Cdd:COG0215 295 AHYRSPLDFSEEALEEAEKALERLYNALRRLEEALgaadssaeeieelREEFIAAMDDDFNTPEALAVLFELVREInkal 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 385 -----------KADELRGAMQLLGINP-------VVRAPVDLDATAKSLIEARTAARANKDWKESDRIRDELAAMGVVLK 446
Cdd:COG0215 375 degedkaalaaLAALLRALGGVLGLLLlepeawqGAAEDELLDALIEALIEERAEARKAKDFARADRIRDELAALGIVLE 454
|
490
....*....|....*.
gi 499470912 447 DGKdaDGksvTTWELA 462
Cdd:COG0215 455 DTP--DG---TTWRRK 465
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
3-460 |
3.47e-163 |
|
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: 468.79 E-value: 3.47e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 3 LRLYDTLTRDKRPFTPIDPANVRMYVCGPTVYDFAHIGNARPVIVFDVLFRLLRHLYGEahVKYVRNITDVDDKINDRAa 82
Cdd:TIGR00435 1 LKLYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLRYLGYK--VQYVQNITDIDDKIIKRA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 83 rdypgLPLNEAIRKVTEQTERQFHDDVDALGCLRPTVEPRATEHIGEMRSIIEKLVAGGFAYV-EQDHVLFSPSAmnaan 161
Cdd:TIGR00435 78 -----RENGESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVsDNGDVYFDVSK----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 162 gvLPRYGSLANRSLDEMIAGARVDVAPYKRDATDFVLWKPSKPGEPSWPSPAGIatpGRPGWHIECSAMSWKHLGETFDI 241
Cdd:TIGR00435 148 --FKDYGKLSKQDLDQLEAGARVDVDEAKRNKLDFVLWKSSKEGEPKWDSPWGK---GRPGWHIECSAMNDKYLGDQIDI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 242 HGGGIDLVFPHHENEVAQSCCAFHTErMAQTWMHNGFLQVEGEKMSKSLGNFITIRELLatNKFggrswDGATLRLAMLK 321
Cdd:TIGR00435 223 HGGGVDLIFPHHENEIAQSEAAFGKQ-LAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVL--KNY-----DPEILRYFLLS 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 322 THYRQPIDWTVDALHEAEKAI-------------LDWSD-FAKDATPVR---CDEVIAALTDDLNTPKMIAELHAL---- 380
Cdd:TIGR00435 295 VHYRSPLDFSEELLEAAKNALerlykalrvldtsLAYSGnQSLNKFPDEkefEARFVEAMDDDLNTANALAVLFELaksi 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 381 --------RRAGKADELRGAMQLLGI------NPVVRAPVDLDATAKSLIEARTAARANKDWKESDRIRDELAAMGVVLK 446
Cdd:TIGR00435 375 nltfvskaDAALLIEHLIFLESRLGLllglpsKPVQAGSNDDLGEIEALIEERSIARKEKDFAKADEIRDELAKKGIVLE 454
|
490
....*....|....
gi 499470912 447 DGKDAdgksvTTWE 460
Cdd:TIGR00435 455 DTPQG-----TTWR 463
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
15-340 |
5.73e-142 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 408.68 E-value: 5.73e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 15 PFTPIDPANVRMYVCGPTVYDFAHIGNARPVIVFDVLFRLLRHLYGEahVKYVRNITDVDDKINDRAARDYpglplnEAI 94
Cdd:pfam01406 1 FFVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQALGYD--VQFVQNFTDIDDKIIKRARQEG------ESF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 95 RKVTEQTERQFHDDVDALGCLRPTVEPRATEHIGEMRSIIEKLVAGGFAYV-EQDHVLFSPSAmnaangvLPRYGSLANR 173
Cdd:pfam01406 73 RQLAARFIEAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVsDNGDVYFDVSS-------FPDYGKLSGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 174 SLDEMIAGARVDVAPYKRDATDFVLWKPSKPGEPSWPSPAGiatPGRPGWHIECSAMSWKHLGETFDIHGGGIDLVFPHH 253
Cdd:pfam01406 146 NLEQLEAGARGEVSEGKRDPLDFALWKASKEGEPSWDSPWG---KGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHH 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 254 ENEVAQSCCAFHTErMAQTWMHNGFLQVEGEKMSKSLGNFITIRELLATnkfggrsWDGATLRLAMLKTHYRQPIDWTVD 333
Cdd:pfam01406 223 ENEIAQSEAAFDKQ-LANYWLHNGHVMIDGEKMSKSLGNFFTIRDVLKR-------YDPEILRYFLLSVHYRSPLDFSEE 294
|
....*..
gi 499470912 334 ALHEAEK 340
Cdd:pfam01406 295 LLEQAKS 301
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
2-462 |
2.91e-129 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 385.44 E-value: 2.91e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 2 ELRLYDTLTRDKRPFTPIDPANVRMYVCGPTVYDFAHIGNARPVIVFDVLFRLLRHLygEAHVKYVRNITDVDDKINDRA 81
Cdd:PLN02946 59 ELHLYNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYLKHL--GYEVRYVRNFTDVDDKIIARA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 82 ARdypglpLNEAIRKVTEQTERQFHDDVDALGCLRPTVEPRATEHIGEMRSIIEKLVAGGFAYVEQDHVLFSPSAmnaan 161
Cdd:PLN02946 137 NE------LGEDPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVDGDVYFSVDK----- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 162 gvLPRYGSLANRSLDEMIAGARVDVAPYKRDATDFVLWKPSKPGEPSWPSPAGiatPGRPGWHIECSAMSWKHLGETFDI 241
Cdd:PLN02946 206 --FPEYGKLSGRKLEDNRAGERVAVDSRKKNPADFALWKAAKEGEPFWDSPWG---PGRPGWHIECSAMSAAYLGHSFDI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 242 HGGGIDLVFPHHENEVAQSCCAFHTERMAQtWMHNGFLQVEGEKMSKSLGNFITIRELLATnkfggrsWDGATLRLAMLK 321
Cdd:PLN02946 281 HGGGMDLVFPHHENEIAQSCAACCDSNISY-WIHNGFVTVDSEKMSKSLGNFFTIRQVIDL-------YHPLALRLFLLG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 322 THYRQPIDWTV--------------DALHEAEKAI-LDWSDFAKDATPVRC--------DEVIAALTDDLNTP------- 371
Cdd:PLN02946 353 THYRSPINYSDvqlesaserifyiyQTLHDCEESLqQHDSTFEKDSVPPDTlncinkfhDEFVTSMSDDLHTPvalaals 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 372 ---KMIAELHALRRAGKADE-----------LRGAMQLLGINPVVRAPVDLDATAKSL-------------IEARTAARA 424
Cdd:PLN02946 433 eplKTINDLLHTRKGKKQEKrleslaalekkIRDVLSVLGLMPTSYSEALQQLREKALrraklteeqvlqkIEERTVARK 512
|
490 500 510
....*....|....*....|....*....|....*...
gi 499470912 425 NKDWKESDRIRDELAAMGVVLKDGKDAdgksvTTWELA 462
Cdd:PLN02946 513 NKEYEKSDAIRKDLAAVGIALMDSPDG-----TTWRPA 545
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
5-459 |
1.64e-117 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 359.80 E-value: 1.64e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 5 LYDTLTRDKRPFTPIDPANVRMYVCGPTVYDFAHIGNARPVIVFDVLFRLLRHLygEAHVKYVRNITDVDDKINDRAARD 84
Cdd:PRK14535 230 IYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLREC--GYPLTYVRNITDIDDKIIARAAEN 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 85 ypglplNEAIRKVTEQTERQFHDDVDALGCLRPTVEPRATEHIGEMRSIIEKLVAGGFAYVEQDHVLFSPSAMNAAngvl 164
Cdd:PRK14535 308 ------GETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVYYAVREFAA---- 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 165 prYGSLANRSLDEMIAGARVDVAPYKRDATDFVLWKPSKPGEPSWPSPAGiatPGRPGWHIECSAMSWKHLGETFDIHGG 244
Cdd:PRK14535 378 --YGQLSGKSLDDLRAGERVEVDGFKRDPLDFVLWKAAKAGEPAWESPWG---NGRPGWHIECSAMSENLFGDTFDIHGG 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 245 GIDLVFPHHENEVAQSCCAF-HT--ERMAQT------------WMHNGFLQVEGEKMSKSLGNFITIRELLatnkfggRS 309
Cdd:PRK14535 453 GADLQFPHHENEIAQSVGATgHTcgHHHAQThhgqsiashvkyWLHNGFIRVDGEKMSKSLGNFFTIREVL-------KQ 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 310 WDGATLRLAMLKTHYRQPIDWTVDALHEAEKAILDWSDFAKDATPVRCD----------EVIAALTDDLNTPKMIAELHA 379
Cdd:PRK14535 526 YDPEVVRFFILRAHYRSPLNYSDAHLDDAKGALTRLYTTLKNTPAAEFMlsenvndytrRFYAAMNDDFGTVEAVAVLFE 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 380 LrrAGKAD-----ELRGAMQLLG--INPVVRAPVDL-----------DATAKSLIEARTAARANKDWKESDRIRDELAAM 441
Cdd:PRK14535 606 L--AGEVNktndaQLAGCLKALGgiIGLLQRDPTEFlqggaasdglsNEEIEDLIARRKQARADKNWAESDRIRDLLNEH 683
|
490
....*....|....*...
gi 499470912 442 GVVLKDgkDADGksvTTW 459
Cdd:PRK14535 684 KIILED--NAGG---TTW 696
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
1-461 |
2.96e-110 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 339.70 E-value: 2.96e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 1 MELRLYDTLTRDKRPFTPIDPANVRMYVCGPTVYDFAHIGNARPVIVFDVLFRLLRHLYGeAHVKYVRNITDVDDKINDR 80
Cdd:PTZ00399 38 TGLKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEDYFG-YDVFYVMNITDIDDKIIKR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 81 AardypglpLNEAIRKVTEQT---ERQFHDDVDALGCLRPTVEPRATEHIGEMRSIIEKLVAGGFAYVEQDHVLFSPSAM 157
Cdd:PTZ00399 117 A--------REEKLSIFLELArkwEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYESNGSVYFDVEAF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 158 NAANGVLPRYGSLANRSLDEMI--AGARVDVAPYKRDATDFVLWKPSKPGEPSWPSPAGiatPGRPGWHIECSAMSWKHL 235
Cdd:PTZ00399 189 RKAGHVYPKLEPESVADEDRIAegEGALGKVSGEKRSPNDFALWKASKPGEPSWDSPWG---KGRPGWHIECSAMASNIL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 236 GETFDIHGGGIDLVFPHHENEVAQSCCAFHTERMAQTWMHNGFLQVEGEKMSKSLGNFITIRELLatNKFGGRswdgaTL 315
Cdd:PTZ00399 266 GDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKGLKMSKSLKNFITIRQAL--SKYTAR-----QI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 316 RLAMLKTHYRQPIDWTVDALHEA---EKAILDW---------------------SDFAKDATPVRCDEVI-AALTDDLNT 370
Cdd:PTZ00399 339 RLLFLLHKWDKPMNYSDESMDEAiekDKVFFNFfanvkiklreseltspqkwtqHDFELNELFEETKSAVhAALLDNFDT 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 371 PKMIAELHALRRAG----------KADELRGAMQ-------LLGINP-----VVRAPVDLDATAKSLIEA--------RT 420
Cdd:PTZ00399 419 PEALQALQKLISATntylnsgeqpSAPLLRSVAQyvtkilsIFGLVEgsdglGSQGQNSTSENFKPLLEAllrfrdevRD 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 499470912 421 AARANKDW-----------KESDRIRDE-LAAMGVVLKDGKDadgkSVTTWEL 461
Cdd:PTZ00399 499 AAKAEMKLisldkkkkqllQLCDKLRDEwLPNLGIRIEDKPD----GPSVWKL 547
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
4-331 |
2.15e-108 |
|
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: 319.52 E-value: 2.15e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 4 RLYDTLTRDKRPFTPIDPANVRMYVCGPTVYDFAHIGNARPVIVFDVLFRLLRHL-YGeahVKYVRNITDVDDKINDRAA 82
Cdd:cd00672 1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLgYK---VRYVQNITDIDDKIIKRAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 83 RDypglplNEAIRKVTEQTERQFHDDVDALGCLRPTVEPRAtehigemrsiieklvaggfayveqdhvlfspsamnaang 162
Cdd:cd00672 78 EE------GLSWKEVADYYTKEFFEDMKALNVLPPDVVPRV--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 163 vlprygslanrsldemiagarvdvapykrdatdfvlwkpskpgepswpspagiatpgrpgWHIECSAMSWKHLGETFDIH 242
Cdd:cd00672 113 ------------------------------------------------------------WHIECSAMAMKYLGETFDIH 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 243 GGGIDLVFPHHENEVAQSCCAFHtERMAQTWMHNGFLQVEGEKMSKSLGNFITIRELLATnkfggrsWDGATLRLAMLKT 322
Cdd:cd00672 133 GGGVDLIFPHHENEIAQSEAATG-KPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKK-------YDPEVLRLALLSS 204
|
....*....
gi 499470912 323 HYRQPIDWT 331
Cdd:cd00672 205 HYRSPLDFS 213
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
1-447 |
1.50e-100 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 309.54 E-value: 1.50e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 1 MELRLYDTLTRDKRPFTPIDPANVRMYVCGPTVYDFAHIGNARPVIVFDVLFRLLRHLygEAHVKYVRNITDV------- 73
Cdd:PRK14536 1 MALRLYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTLHFL--GYRVTHVMNITDVghltdda 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 74 ---DDKInDRAARDYpglplNEAIRKVTEQTERQFHDDVDALGCLRPTVEPRATEHIGEMRSIIEKLVAGGFAYVEQDHV 150
Cdd:PRK14536 79 dsgEDKM-VKSAQEH-----GKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCAGGNV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 151 LFSPSAmnaangvLPRYGSLANRSLDEMIAGARVDVAPYKRDATDFVLWKPSKPGEP---SWPSPAGiatPGRPGWHIEC 227
Cdd:PRK14536 153 YFDIRT-------FPSYGSLASAAVEDLQAGARIEHDTNKRNPHDFVLWFTRSKFENhalTWDSPWG---RGYPGWHIEC 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 228 SAMSWKHLGETFDIHGGGIDLVFPHHENEVAQsCCAFHTERMAQTWMHNGFLQVEGEKMSKSLGNFITIRELLatnkfgG 307
Cdd:PRK14536 223 SAMSMKYLGEQCDIHIGGVDHIRVHHTNEIAQ-CEAATGKPWVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQ------E 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 308 RSWDGATLRLAMLKTHYRQPIDWTVDALHEAEKA-------ILDWSDFAKDATPV------RC----------------- 357
Cdd:PRK14536 296 KGFQPLDYRFFLLGGHYRSQLAFSWEALKTAKAArrslvrrVARVVDAARATTGSvrgtlaECaaervaesraseselll 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 358 DEVIAALTDDLNTPKMIAELHALRRAG------KADELRGAMQLLGINPVVRAPVDLDATAKS---------LIEARTAA 422
Cdd:PRK14536 376 TDFRAALEDDFSTPKALSELQKLVKDTsvppslCLSVLQAMDTVLGLGLIQEATASLSAQVPAgpseeeigqLIEARAHA 455
|
490 500
....*....|....*....|....*
gi 499470912 423 RANKDWKESDRIRDELAAMGVVLKD 447
Cdd:PRK14536 456 RQTKDFPLADEIRDKLKAEGIELED 480
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
3-377 |
2.61e-87 |
|
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: 272.75 E-value: 2.61e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 3 LRLYDTLTRDKRPFTPidPANVRMYVCGPTVYDFAHIGNARPVIVFDVLFRLLRHlyGEAHVKYVRNITDVDDKINDRAA 82
Cdd:TIGR03447 18 LRLFDTADGQVRPVEP--GPEAGMYVCGITPYDATHLGHAATYLTFDLVNRVWRD--AGHRVHYVQNVTDVDDPLFERAE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 83 RDypglplNEAIRKVTEQTERQFHDDVDALGCLRPTVEPRATEHIGEMRSIIEKLVAGGFAY-VEQDH---VLFSPSAmn 158
Cdd:TIGR03447 94 RD------GVDWRELGTSQIDLFREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYiVEGPEypdVYFSIDA-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 159 aangvLPRYGSLANRSLDEMIA-----GARVDvAPYKRDATDFVLWKPSKPGEPSWPSPAGiatPGRPGWHIECSAMSWK 233
Cdd:TIGR03447 166 -----TEQFGYESGYDRATMLElfaerGGDPD-RPGKRDPLDALLWRAAREGEPSWDSPFG---RGRPGWHIECSAIALN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 234 HLGETFDIHGGGIDLVFPHHENEVAQSCCAFHTERMAQTWMHNGFLQVEGEKMSKSLGNFITIRELLATNKfggrswDGA 313
Cdd:TIGR03447 237 RLGAGFDIQGGGSDLIFPHHEFSAAHAEAATGVRRMARHYVHAGMIGLDGEKMSKSLGNLVFVSKLRAAGV------DPA 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499470912 314 TLRLAMLKTHYRQPIDWTVDALHEAEKAILDWSDF-----AKDATPVrCDEVIAALTDDLNTPKMIAEL 377
Cdd:TIGR03447 311 AIRLGLLAGHYRQDRDWTDAVLAEAEARLARWRAAlalpdAPDATDL-IARLRQHLANDLDTPAALAAV 378
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
14-377 |
9.96e-85 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 265.26 E-value: 9.96e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 14 RPFTPIDPAnvRMYVCGPTVYDFAHIGNARPVIVFDVLFRLLR---HlygeaHVKYVRNITDVDDKINDRAARDypGLPL 90
Cdd:PRK12418 2 RPVAPGGTA--TMYVCGITPYDATHLGHAATYLAFDLVNRVWRdagH-----DVHYVQNVTDVDDPLLERAARD--GVDW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 91 NEAirkVTEQTERqFHDDVDALGCLRPTVEPRATEHIGEMRSIIEKLVAGGFAYVEQDH----VLFSPSAmnaangvLPR 166
Cdd:PRK12418 73 RDL---AEREIAL-FREDMEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYVVDDEeypdVYFSVDA-------TPQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 167 YGSLANRSLDEMIA-----GARVDvAPYKRDATDFVLWKPSKPGEPSWPSPAGiatPGRPGWHIECSAMSWKHLGETFDI 241
Cdd:PRK12418 142 FGYESGYDRATMLElfaerGGDPD-RPGKRDPLDALLWRAARPGEPSWPSPFG---PGRPGWHIECSAIALNRLGSGFDI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 242 HGGGIDLVFPHHENEVAQSCCAFHTERMAQTWMHNGFLQVEGEKMSKSLGNFITIRELLAtnkfggRSWDGATLRLAMLK 321
Cdd:PRK12418 218 QGGGSDLIFPHHEFSAAHAEAATGERRFARHYVHAGMIGLDGEKMSKSRGNLVFVSRLRA------AGVDPAAIRLALLA 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 322 THYRQPIDWTVDALHEAEKAILDWSDFAKDATPVRCDEVIA----ALTDDLNTPKMIAEL 377
Cdd:PRK12418 292 GHYRADREWTDAVLAEAEARLARWRAAAALPAGPDAADVVArvraALADDLDTPGALAAV 351
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
1-450 |
1.76e-65 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 218.18 E-value: 1.76e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 1 MELRLYDTLTRDKRPFTPIDpaNVRMYVCGPTVYDFAHIGNARPVIVFDVLFRLLRHLygEAHVKYVRNITDV------- 73
Cdd:PRK14534 1 MLLKLYNTKTKDLSELKNFS--DVKVYACGPTVYNYAHIGNFRTYIFEDLLIKSLRLL--KYNVNYAMNITDIghltgdf 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 74 ---DDKINdRAARDyPGLPLNEAIRKVTEQterqFHDDVDALGCLRPTVEPRATEHIGEMRSIIEKLVAGGFAYVEQDHV 150
Cdd:PRK14534 77 ddgEDKVV-KAARE-RGLTVYEISRFFTEA----FFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTYFVNGNV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 151 LFSPSAMNAangvlprYGSLANRSLDEM--IAGARVDVAPYKRDATDFVLWKPS---KPGEPSWPSPAGIatpGRPGWHI 225
Cdd:PRK14534 151 YFDTSCFKS-------YGQMAGINLNDFkdMSVSRVEIDKSKRNKSDFVLWFTNskfKDQEMKWDSPWGF---GYPSWHL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 226 ECSAMSWKHLGETFDIHGGGIDLVFPHHENEVAQSCCaFHTERMAQTWMHNGFLQVEGEKMSKSLGNFITIRELLATNkf 305
Cdd:PRK14534 221 ECAAMNLEYFKSTLDIHLGGVDHIGVHHINEIAIAEC-YLNKKWCDMFVHGEFLIMEYEKMSKSNNNFITIKDLEDQG-- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 306 ggrsWDGATLRLAMLKTHYRQPIDWTVDALHEA----EKAILDWSDFAKDATPVRC-------------------DEVIA 362
Cdd:PRK14534 298 ----FSPLDFRYFCLTAHYRTQLKFTFNNLKACkiarENMLNKLTYFYSSLDQFDLnllnkdleniefslekeyyDSFLE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 363 ALTDDLNTPKMIA------------ELHALRRAGKADELRGAMQLLGI-NPVVRAPVDLDATAKSLIEARTAARANKDWK 429
Cdd:PRK14534 374 KIAFDLNIPQGLAllwdiikddnlsFLSKLRLAFKFDEVLSLGLREEIlREIENHRIVIDDNMKSLIEERRLAKCEKDFK 453
|
490 500
....*....|....*....|.
gi 499470912 430 ESDRIRDELAAMGVVLKDGKD 450
Cdd:PRK14534 454 RADEIREYFASKGFVLIDTEE 474
|
|
| Anticodon_Ia_Cys |
cd07963 |
Anticodon-binding domain of cysteinyl tRNA synthetases; This domain is found in cysteinyl tRNA ... |
361-459 |
5.19e-19 |
|
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: 83.77 E-value: 5.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 361 IAALTDDLNTPKMIAEL----HALRRAGKADELRGAM---------QLLGI---NP------VVRAPVDLDATAKSLIEA 418
Cdd:cd07963 39 IAAMDDDFNTPEALAVLfelaREINRLKKEDIEKAAAlaallkalgGVLGLlqqDPeaflqgGTGEGGLSVAEIEALIAQ 118
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 499470912 419 RTAARANKDWKESDRIRDELAAMGVVLKDGkdADGksvTTW 459
Cdd:cd07963 119 RNQARKAKDWAEADRIRDELAAQGIILEDS--PEG---TTW 154
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
26-110 |
2.07e-08 |
|
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: 52.87 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 26 MYVCGPTVYDFAHIGNARPVIVFDVLFRLLRHLYGEahVKYVRNITDVDDKINDRAardypGLPLNEAIRKVtEQTERQF 105
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYK--VRCIALIDDAGGLIGDPA-----NKKGENAKAFV-ERWIERI 72
|
....*
gi 499470912 106 HDDVD 110
Cdd:cd00802 73 KEDVE 77
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
276-359 |
2.36e-07 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 53.33 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 276 NGFLQVEGEKMSKSLGNFITIREllATNKFGGrswDgaTLRLAMLKT-HYRQPIDWTVDALHEAEKAILDWSDFAKDATP 354
Cdd:PRK12300 568 NGFVLLEGKKMSKSKGNVIPLRK--AIEEYGA---D--VVRLYLTSSaELLQDADWREKEVESVRRQLERFYELAKELIE 640
|
....*
gi 499470912 355 VRCDE 359
Cdd:PRK12300 641 IGGEE 645
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
276-306 |
1.30e-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: 50.88 E-value: 1.30e-06
10 20 30
....*....|....*....|....*....|.
gi 499470912 276 NGFLQVEGEKMSKSLGNFITIRELLatNKFG 306
Cdd:COG0143 318 HGFLTVEGEKMSKSRGNVIDPDDLL--DRYG 346
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
239-320 |
5.39e-06 |
|
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: 48.01 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 239 FDIHGGGIDLV--------FPHHenevaqsccAFHTERMAQT-W----MHNGFLQVEGEKMSKSLGNFITIREllATNKF 305
Cdd:cd00812 225 VDIYIGGKEHApnhllysrFNHK---------ALFDEGLVTDePpkglIVQGMVLLEGEKMSKSKGNVVTPDE--AIKKY 293
|
90
....*....|....*
gi 499470912 306 GGrswDgaTLRLAML 320
Cdd:cd00812 294 GA---D--AARLYIL 303
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
228-330 |
7.94e-05 |
|
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: 44.33 E-value: 7.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 228 SAMSWKHLGETF------DIHGGGIDLVFPHhENEVAQSCCAFHTERMAQTWMHNGFLQVE-GEKMSKSLGNFITIRELL 300
Cdd:cd00668 210 GSLGYPEEKEWFkdsypaDWHLIGKDILRGW-ANFWITMLVALFGEIPPKNLLVHGFVLDEgGQKMSKSKGNVIDPSDVV 288
|
90 100 110
....*....|....*....|....*....|.
gi 499470912 301 atNKFGGRSwdgatLRL-AMLKTHYRQPIDW 330
Cdd:cd00668 289 --EKYGADA-----LRYyLTSLAPYGDDIRL 312
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
276-306 |
2.42e-04 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 43.33 E-value: 2.42e-04
10 20 30
....*....|....*....|....*....|.
gi 499470912 276 NGFLQVEGEKMSKSLGNFITIRELLAtnKFG 306
Cdd:PRK11893 290 HGFLTLDGEKMSKSLGNVIDPFDLVD--EYG 318
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
276-300 |
5.50e-04 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 42.45 E-value: 5.50e-04
10 20
....*....|....*....|....*
gi 499470912 276 NGFLQVEGEKMSKSLGNFITIRELL 300
Cdd:PRK00133 320 HGFLTVEGAKMSKSRGTFIWARTYL 344
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
276-298 |
7.56e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 41.98 E-value: 7.56e-04
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
276-300 |
8.67e-04 |
|
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: 41.36 E-value: 8.67e-04
10 20
....*....|....*....|....*
gi 499470912 276 NGFLQVEGEKMSKSLGNFITIRELL 300
Cdd:cd00814 271 HGYLTVEGKKMSKSRGNVVDPDDLL 295
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
276-302 |
1.44e-03 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 40.74 E-value: 1.44e-03
10 20
....*....|....*....|....*..
gi 499470912 276 NGFLQVEGEKMSKSLGNFITIRELLAT 302
Cdd:pfam09334 315 HGYLTYEGGKMSKSRGNVVWPSEALDR 341
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
275-406 |
1.92e-03 |
|
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440261 [Multi-domain] Cd Length: 826 Bit Score: 40.80 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 275 HNGFLQVEGEKMSKSLGNFITIRELLAtnKFggrswdGA-TLRLAML-KTHYRQPIDWT---VDALH------------E 337
Cdd:COG0495 579 KDGVVIGGIEKMSKSKGNVVDPDEIIE--KY------GAdTLRLFEMfAGPPERDLEWSdsgVEGAYrflnrvwrlvvdE 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470912 338 AEKAILDWSDFAKDATPVRCD--EVIAALTDDL-----NTpkMIAELH----ALRRAGKADELRGAMQLLGINPVVR--A 404
Cdd:COG0495 651 AEALKLDVADLSEADKELRRAlhKTIKKVTEDIerlrfNT--AIAALMelvnALYKAKDSGEADRAVLREALETLVLllA 728
|
..
gi 499470912 405 PV 406
Cdd:COG0495 729 PF 730
|
|
| DALR_2 |
smart00840 |
This DALR domain is found in cysteinyl-tRNA-synthetases; |
359-398 |
2.36e-03 |
|
This DALR domain is found in cysteinyl-tRNA-synthetases;
Pssm-ID: 214848 [Multi-domain] Cd Length: 56 Bit Score: 36.01 E-value: 2.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 499470912 359 EVIAALTDDLNTPKMIAELHALRRAGK---------------ADELRGAMQLLGI 398
Cdd:smart00840 1 RFEEAMDDDFNTPEALAVLFELAREINrlalkatdaeelaalAALLRALGGVLGL 55
|
|
| DALR_2 |
pfam09190 |
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases. |
359-398 |
3.78e-03 |
|
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases.
Pssm-ID: 462711 [Multi-domain] Cd Length: 63 Bit Score: 35.64 E-value: 3.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 499470912 359 EVIAALTDDLNTPKMIAELH----ALRRAGK----------ADELRGAMQLLGI 398
Cdd:pfam09190 1 KFIEAMDDDFNTPEALAVLFelakEINRALKtndaeaaaalAALLRELGDVLGL 54
|
|
| |
