|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
118-647 |
0e+00 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 685.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 118 SIFSKLPKFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYASNGSVYFDTAKFAASeKHSYGKLVPE 197
Cdd:PTZ00399 123 SIFLELARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYESNGSVYFDVEAFRKA-GHVYPKLEPE 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 198 AVGDQKALQEGEGDLSISAdrlSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDL 277
Cdd:PTZ00399 202 SVADEDRIAEGEGALGKVS---GEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 278 RFPHHDNELAQSEAYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSSNTM 357
Cdd:PTZ00399 279 KFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKGLKMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSDESM 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 358 ESALQYEKFMNEFFLNVKDILRAPVdiTGQFEKWEAEEVELNKNFYGKKTAVHEALCDNIDTRTVMEEMRALVSQCNLYM 437
Cdd:PTZ00399 359 DEAIEKDKVFFNFFANVKIKLRESE--LTSPQKWTQHDFELNELFEETKSAVHAALLDNFDTPEALQALQKLISATNTYL 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 438 AARKaerrRPNRALLENIAMYLTHMLKIFGAIEEesplGFPVGGPGTNlNLESTVMPYLQVLSEFREGVRKIAR------ 511
Cdd:PTZ00399 437 NSGE----QPSAPLLRSVAQYVTKILSIFGLVEG----SDGLGSQGQN-STSENFKPLLEALLRFRDEVRDAAKaemkli 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 512 --EKKVLEVLQLSDALRDDILPELGVRFEDHEGLPTVVKLVDRDTLLKEKEGKKRAEEEKRRKKEEAARKKQEQEAAKLA 589
Cdd:PTZ00399 508 slDKKKKQLLQLCDKLRDEWLPNLGIRIEDKPDGPSVWKLDDKEELQREKEEKEALKEQKRLRKLKKQEEKKKKELEKLE 587
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720422850 590 KMKIPPSEMFLSEVNKYSKFDENGLPTHDTEGKELSKGQAKKLKKLFEAQEKLYKEYL 647
Cdd:PTZ00399 588 KAKIPPAEFFKRQEDKYSAFDETGLPTHDADGEEISKKERKKLSKEYDKQAKLHEEYL 645
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
1-540 |
7.11e-123 |
|
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: 372.51 E-value: 7.11e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 1 MNITDIDDKIIRRARQNylfeqyreqkppatqllkdvrdamkpfsvklsettdpdkrqmleriqnsvklatepleqavrs 80
Cdd:COG0215 65 RNITDVDDKIIKRAAEE--------------------------------------------------------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 81 slsGEEVdskvqvlleeakdllsdwldstggSEVTDnsifsklpkFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFV 160
Cdd:COG0215 82 ---GESI------------------------WELAE---------RYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELI 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 161 QKIVDNGYGYASNGSVYFDTAKFaasekHSYGKL---VPEAvgdqkaLQEGEgdlsiSADRLSEKRSPNDFALWKASKPG 237
Cdd:COG0215 126 ERLIEKGHAYEADGDVYFDVRSF-----PDYGKLsgrNLDD------LRAGA-----RVEVDEEKRDPLDFALWKAAKPG 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 238 EPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDcWVRYFLHTGHLTIAGCKMSK 317
Cdd:COG0215 190 EPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIAQSEAATGKP-FARYWMHNGFLTVNGEKMSK 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 318 SLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSSNTMESALQ-YEKFMNeFFLNVKDILRAPVDITGQFEKWEAEev 396
Cdd:COG0215 269 SLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKaLERLYN-ALRRLEEALGAADSSAEEIEELREE-- 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 397 elnknfygkktaVHEALCDNIDTRTVMEEMRALVSQCNLYMAARKaerrrpNRALLENIAMYLTHMLKIFGaIEEESPLG 476
Cdd:COG0215 346 ------------FIAAMDDDFNTPEALAVLFELVREINKALDEGE------DKAALAALAALLRALGGVLG-LLLLEPEA 406
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720422850 477 FpvGGPGTNLNLESTVMPYLQvlsefregVRKIAREKKVLEvlqLSDALRDDILpELGVRFEDH 540
Cdd:COG0215 407 W--QGAAEDELLDALIEALIE--------ERAEARKAKDFA---RADRIRDELA-ALGIVLEDT 456
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
120-365 |
2.43e-110 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 334.34 E-value: 2.43e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 120 FSKLPKFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGY-ASNGSVYFDTAKFaasekHSYGKLVPEA 198
Cdd:pfam01406 72 FRQLAARFIEAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYvSDNGDVYFDVSSF-----PDYGKLSGQN 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 199 VGDQKALQEGEGDlsisadrlSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLR 278
Cdd:pfam01406 147 LEQLEAGARGEVS--------EGKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 279 FPHHDNELAQSEAYFENDcWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSsntmE 358
Cdd:pfam01406 219 FPHHENEIAQSEAAFDKQ-LANYWLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFS----E 293
|
....*..
gi 1720422850 359 SALQYEK 365
Cdd:pfam01406 294 ELLEQAK 300
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
120-539 |
5.76e-100 |
|
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: 313.55 E-value: 5.76e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 120 FSKLPKFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYAS-NGSVYFDTAKFaasekHSYGKLvpeA 198
Cdd:TIGR00435 84 VYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSdNGDVYFDVSKF-----KDYGKL---S 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 199 VGDQKALQEGEGDLSISAdrlseKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLR 278
Cdd:TIGR00435 156 KQDLDQLEAGARVDVDEA-----KRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 279 FPHHDNELAQSEAYFeNDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSsntmE 358
Cdd:TIGR00435 231 FPHHENEIAQSEAAF-GKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFS----E 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 359 SALQYEKFMNEFFLNVKDILRAPVDITGQFEKWEAEEVelnKNFYgkkTAVHEALCDNIDTRTVMEEMRALVSQCNLYMA 438
Cdd:TIGR00435 306 ELLEAAKNALERLYKALRVLDTSLAYSGNQSLNKFPDE---KEFE---ARFVEAMDDDLNTANALAVLFELAKSINLTFV 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 439 arkaerrrpNRALLENIAMYLTHMLKIFGAIEEESPLGFPVGGPGTNLNLESTVMPylqvlsefregvRKIAREKKvleV 518
Cdd:TIGR00435 380 ---------SKADAALLIEHLIFLESRLGLLLGLPSKPVQAGSNDDLGEIEALIEE------------RSIARKEK---D 435
|
410 420
....*....|....*....|.
gi 1720422850 519 LQLSDALRDDiLPELGVRFED 539
Cdd:TIGR00435 436 FAKADEIRDE-LAKKGIVLED 455
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
116-353 |
1.30e-65 |
|
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: 214.75 E-value: 1.30e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 116 DNSIFSKLPKFWEEEFHKDMEALNVLPPDVLTRVseyvpeivnfvqkivdngygyasngsvyfdtakfaasekhsygklv 195
Cdd:cd00672 79 EGLSWKEVADYYTKEFFEDMKALNVLPPDVVPRV---------------------------------------------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 196 peavgdqkalqegegdlsisadrlsekrspndfalwkaskpgepswpcpwgkgrpgWHIECSAMAGTLLGASMDIHGGGF 275
Cdd:cd00672 113 --------------------------------------------------------WHIECSAMAMKYLGETFDIHGGGV 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720422850 276 DLRFPHHDNELAQSEAYFeNDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYS 353
Cdd:cd00672 137 DLIFPHHENEIAQSEAAT-GKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
118-647 |
0e+00 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 685.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 118 SIFSKLPKFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYASNGSVYFDTAKFAASeKHSYGKLVPE 197
Cdd:PTZ00399 123 SIFLELARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYESNGSVYFDVEAFRKA-GHVYPKLEPE 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 198 AVGDQKALQEGEGDLSISAdrlSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDL 277
Cdd:PTZ00399 202 SVADEDRIAEGEGALGKVS---GEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 278 RFPHHDNELAQSEAYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSSNTM 357
Cdd:PTZ00399 279 KFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKGLKMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSDESM 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 358 ESALQYEKFMNEFFLNVKDILRAPVdiTGQFEKWEAEEVELNKNFYGKKTAVHEALCDNIDTRTVMEEMRALVSQCNLYM 437
Cdd:PTZ00399 359 DEAIEKDKVFFNFFANVKIKLRESE--LTSPQKWTQHDFELNELFEETKSAVHAALLDNFDTPEALQALQKLISATNTYL 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 438 AARKaerrRPNRALLENIAMYLTHMLKIFGAIEEesplGFPVGGPGTNlNLESTVMPYLQVLSEFREGVRKIAR------ 511
Cdd:PTZ00399 437 NSGE----QPSAPLLRSVAQYVTKILSIFGLVEG----SDGLGSQGQN-STSENFKPLLEALLRFRDEVRDAAKaemkli 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 512 --EKKVLEVLQLSDALRDDILPELGVRFEDHEGLPTVVKLVDRDTLLKEKEGKKRAEEEKRRKKEEAARKKQEQEAAKLA 589
Cdd:PTZ00399 508 slDKKKKQLLQLCDKLRDEWLPNLGIRIEDKPDGPSVWKLDDKEELQREKEEKEALKEQKRLRKLKKQEEKKKKELEKLE 587
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720422850 590 KMKIPPSEMFLSEVNKYSKFDENGLPTHDTEGKELSKGQAKKLKKLFEAQEKLYKEYL 647
Cdd:PTZ00399 588 KAKIPPAEFFKRQEDKYSAFDETGLPTHDADGEEISKKERKKLSKEYDKQAKLHEEYL 645
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
1-540 |
7.11e-123 |
|
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: 372.51 E-value: 7.11e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 1 MNITDIDDKIIRRARQNylfeqyreqkppatqllkdvrdamkpfsvklsettdpdkrqmleriqnsvklatepleqavrs 80
Cdd:COG0215 65 RNITDVDDKIIKRAAEE--------------------------------------------------------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 81 slsGEEVdskvqvlleeakdllsdwldstggSEVTDnsifsklpkFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFV 160
Cdd:COG0215 82 ---GESI------------------------WELAE---------RYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELI 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 161 QKIVDNGYGYASNGSVYFDTAKFaasekHSYGKL---VPEAvgdqkaLQEGEgdlsiSADRLSEKRSPNDFALWKASKPG 237
Cdd:COG0215 126 ERLIEKGHAYEADGDVYFDVRSF-----PDYGKLsgrNLDD------LRAGA-----RVEVDEEKRDPLDFALWKAAKPG 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 238 EPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDcWVRYFLHTGHLTIAGCKMSK 317
Cdd:COG0215 190 EPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIAQSEAATGKP-FARYWMHNGFLTVNGEKMSK 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 318 SLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSSNTMESALQ-YEKFMNeFFLNVKDILRAPVDITGQFEKWEAEev 396
Cdd:COG0215 269 SLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKaLERLYN-ALRRLEEALGAADSSAEEIEELREE-- 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 397 elnknfygkktaVHEALCDNIDTRTVMEEMRALVSQCNLYMAARKaerrrpNRALLENIAMYLTHMLKIFGaIEEESPLG 476
Cdd:COG0215 346 ------------FIAAMDDDFNTPEALAVLFELVREINKALDEGE------DKAALAALAALLRALGGVLG-LLLLEPEA 406
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720422850 477 FpvGGPGTNLNLESTVMPYLQvlsefregVRKIAREKKVLEvlqLSDALRDDILpELGVRFEDH 540
Cdd:COG0215 407 W--QGAAEDELLDALIEALIE--------ERAEARKAKDFA---RADRIRDELA-ALGIVLEDT 456
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
120-365 |
2.43e-110 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 334.34 E-value: 2.43e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 120 FSKLPKFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGY-ASNGSVYFDTAKFaasekHSYGKLVPEA 198
Cdd:pfam01406 72 FRQLAARFIEAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYvSDNGDVYFDVSSF-----PDYGKLSGQN 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 199 VGDQKALQEGEGDlsisadrlSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLR 278
Cdd:pfam01406 147 LEQLEAGARGEVS--------EGKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 279 FPHHDNELAQSEAYFENDcWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSsntmE 358
Cdd:pfam01406 219 FPHHENEIAQSEAAFDKQ-LANYWLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFS----E 293
|
....*..
gi 1720422850 359 SALQYEK 365
Cdd:pfam01406 294 ELLEQAK 300
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
120-539 |
5.76e-100 |
|
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: 313.55 E-value: 5.76e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 120 FSKLPKFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYAS-NGSVYFDTAKFaasekHSYGKLvpeA 198
Cdd:TIGR00435 84 VYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSdNGDVYFDVSKF-----KDYGKL---S 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 199 VGDQKALQEGEGDLSISAdrlseKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLR 278
Cdd:TIGR00435 156 KQDLDQLEAGARVDVDEA-----KRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 279 FPHHDNELAQSEAYFeNDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSsntmE 358
Cdd:TIGR00435 231 FPHHENEIAQSEAAF-GKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFS----E 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 359 SALQYEKFMNEFFLNVKDILRAPVDITGQFEKWEAEEVelnKNFYgkkTAVHEALCDNIDTRTVMEEMRALVSQCNLYMA 438
Cdd:TIGR00435 306 ELLEAAKNALERLYKALRVLDTSLAYSGNQSLNKFPDE---KEFE---ARFVEAMDDDLNTANALAVLFELAKSINLTFV 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 439 arkaerrrpNRALLENIAMYLTHMLKIFGAIEEESPLGFPVGGPGTNLNLESTVMPylqvlsefregvRKIAREKKvleV 518
Cdd:TIGR00435 380 ---------SKADAALLIEHLIFLESRLGLLLGLPSKPVQAGSNDDLGEIEALIEE------------RSIARKEK---D 435
|
410 420
....*....|....*....|.
gi 1720422850 519 LQLSDALRDDiLPELGVRFED 539
Cdd:TIGR00435 436 FAKADEIRDE-LAKKGIVLED 455
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
123-360 |
1.25e-69 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 236.37 E-value: 1.25e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 123 LPKFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYASNGSVYFDTAKFAasekhSYGKLVPEAVGDQ 202
Cdd:PLN02946 146 LSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVDGDVYFSVDKFP-----EYGKLSGRKLEDN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 203 KAlqeGEgdlSISADrlSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHH 282
Cdd:PLN02946 221 RA---GE---RVAVD--SRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLVFPHH 292
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720422850 283 DNELAQSEAYFEnDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSSNTMESA 360
Cdd:PLN02946 293 ENEIAQSCAACC-DSNISYWIHNGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDVQLESA 369
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
116-353 |
1.30e-65 |
|
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: 214.75 E-value: 1.30e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 116 DNSIFSKLPKFWEEEFHKDMEALNVLPPDVLTRVseyvpeivnfvqkivdngygyasngsvyfdtakfaasekhsygklv 195
Cdd:cd00672 79 EGLSWKEVADYYTKEFFEDMKALNVLPPDVVPRV---------------------------------------------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 196 peavgdqkalqegegdlsisadrlsekrspndfalwkaskpgepswpcpwgkgrpgWHIECSAMAGTLLGASMDIHGGGF 275
Cdd:cd00672 113 --------------------------------------------------------WHIECSAMAMKYLGETFDIHGGGV 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720422850 276 DLRFPHHDNELAQSEAYFeNDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYS 353
Cdd:cd00672 137 DLIFPHHENEIAQSEAAT-GKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
102-360 |
5.06e-54 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 196.86 E-value: 5.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 102 LSDWLDSTGGSEVTDNSIFSKLPKFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGY-ASNGSVYFDT 180
Cdd:PRK14535 293 ITDIDDKIIARAAENGETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYpAANGDVYYAV 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 181 AKFAAsekhsYGKLVPEAVGDQKALQEGEGDlsisadrlSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMA 260
Cdd:PRK14535 373 REFAA-----YGQLSGKSLDDLRAGERVEVD--------GFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMS 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 261 GTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDC---------------WVRYFLHTGHLTIAGCKMSKSLKNFITI 325
Cdd:PRK14535 440 ENLFGDTFDIHGGGADLQFPHHENEIAQSVGATGHTCghhhaqthhgqsiasHVKYWLHNGFIRVDGEKMSKSLGNFFTI 519
|
250 260 270
....*....|....*....|....*....|....*
gi 1720422850 326 KDALKKHSARQLRLAFLMHSWKDTLDYSSNTMESA 360
Cdd:PRK14535 520 REVLKQYDPEVVRFFILRAHYRSPLNYSDAHLDDA 554
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
131-362 |
1.24e-50 |
|
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: 181.08 E-value: 1.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 131 FHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGY----ASNGSVYFDTAkfaASEKHSYGKLVPEAVGDQKALQ 206
Cdd:TIGR03447 110 FREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYivegPEYPDVYFSID---ATEQFGYESGYDRATMLELFAE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 207 EGeGDlsisADRLSeKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNEL 286
Cdd:TIGR03447 187 RG-GD----PDRPG-KRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSDLIFPHHEFSA 260
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720422850 287 AQSEAYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDaLKK--HSARQLRLAFLMHSWKDTLDYSSNTMESALQ 362
Cdd:TIGR03447 261 AHAEAATGVRRMARHYVHAGMIGLDGEKMSKSLGNLVFVSK-LRAagVDPAAIRLGLLAGHYRQDRDWTDAVLAEAEA 337
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
131-362 |
2.86e-49 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 176.66 E-value: 2.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 131 FHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGY----ASNGSVYFDTAkfAAsekhsygklvpEAVGDQKALQ 206
Cdd:PRK12418 83 FREDMEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYvvddEEYPDVYFSVD--AT-----------PQFGYESGYD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 207 EGEGdLSISADRLSE-----KRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPH 281
Cdd:PRK12418 150 RATM-LELFAERGGDpdrpgKRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPH 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 282 HDNELAQSEAYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKdALKK--HSARQLRLAFLMHSWKDTLDYSSNTMES 359
Cdd:PRK12418 229 HEFSAAHAEAATGERRFARHYVHAGMIGLDGEKMSKSRGNLVFVS-RLRAagVDPAAIRLALLAGHYRADREWTDAVLAE 307
|
...
gi 1720422850 360 ALQ 362
Cdd:PRK12418 308 AEA 310
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
122-435 |
1.14e-44 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 166.63 E-value: 1.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 122 KLPKFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYASNGSVYFDTAKFAasekhSYGKLVPEAVGD 201
Cdd:PRK14536 98 EIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCAGGNVYFDIRTFP-----SYGSLASAAVED 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 202 qkaLQEGEgdlSISADrlSEKRSPNDFALWKASKPGEP---SWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLR 278
Cdd:PRK14536 173 ---LQAGA---RIEHD--TNKRNPHDFVLWFTRSKFENhalTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIGGVDHI 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 279 FPHHDNELAQSEAyFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKK-HSARQLRLAFLMHSWKDTLDYSSNTM 357
Cdd:PRK14536 245 RVHHTNEIAQCEA-ATGKPWVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQEKgFQPLDYRFFLLGGHYRSQLAFSWEAL 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 358 ESALQYEKFMNEFFLNVKDILRAPVDIT-GQFEKWEAEEVELNKNFYGKK--TAVHEALCDNIDTRTVMEEMRALVSQCN 434
Cdd:PRK14536 324 KTAKAARRSLVRRVARVVDAARATTGSVrGTLAECAAERVAESRASESELllTDFRAALEDDFSTPKALSELQKLVKDTS 403
|
.
gi 1720422850 435 L 435
Cdd:PRK14536 404 V 404
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
122-327 |
2.01e-35 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 139.99 E-value: 2.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 122 KLPKFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYASNGSVYFDTAKFaasekHSYGKLVPEAVGD 201
Cdd:PRK14534 96 EISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTYFVNGNVYFDTSCF-----KSYGQMAGINLND 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 202 QKALQEGEGDLSISadrlseKRSPNDFALWKAS---KPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLR 278
Cdd:PRK14534 171 FKDMSVSRVEIDKS------KRNKSDFVLWFTNskfKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKSTLDIHLGGVDHI 244
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720422850 279 FPHHDNELAQSEAYFeNDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKD 327
Cdd:PRK14534 245 GVHHINEIAIAECYL-NKKWCDMFVHGEFLIMEYEKMSKSNNNFITIKD 292
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
291-456 |
2.48e-07 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 54.10 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 291 AYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLaFLMHS---WKDtLDYSSNTMESAL-QYEKF 366
Cdd:PRK12300 554 AIFPEEKWPRGIVVNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRL-YLTSSaelLQD-ADWREKEVESVRrQLERF 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 367 MnEFFLNVKDIlrAPVDITGQFEKWeaeeveLNKNFYGKKTAVHEALcDNIDTRTVMEEmrALVsqcNLYMAARKAERR- 445
Cdd:PRK12300 632 Y-ELAKELIEI--GGEEELRFIDKW------LLSRLNRIIKETTEAM-ESFQTRDAVQE--AFY---ELLNDLRWYLRRv 696
|
170
....*....|..
gi 1720422850 446 -RPNRALLENIA 456
Cdd:PRK12300 697 gEANNKVLREVL 708
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
275-361 |
1.24e-05 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 48.53 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 275 FDLRFPHHD---NELAQS----EAYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRlaFLMHSWK 347
Cdd:PLN02959 672 FDLRVSGKDliqNHLTFAiynhTAIWAEEHWPRGFRCNGHLMLNSEKMSKSTGNFLTLRQAIEEFSADATR--FALADAG 749
|
90
....*....|....*..
gi 1720422850 348 DTLD---YSSNTMESAL 361
Cdd:PLN02959 750 DGVDdanFVFETANAAI 766
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
299-345 |
1.64e-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: 44.06 E-value: 1.64e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1720422850 299 VRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHS 345
Cdd:cd00814 265 PTRIVAHGYLTVEGKKMSKSRGNVVDPDDLLERYGADALRYYLLRER 311
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
305-345 |
5.98e-04 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 42.66 E-value: 5.98e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1720422850 305 TGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHS 345
Cdd:pfam09334 315 HGYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARNR 355
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
251-319 |
1.03e-03 |
|
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: 39.77 E-value: 1.03e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422850 251 GWHIECSAMAGTLLGASMDIHGGGFDLRFpHHDNELAQSEAYfeNDCWVRYFLHTGHLTIA-GCKMSKSL 319
Cdd:cd00802 77 EYMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKA--GGPARPFGLTFGRVMGAdGTKMSKSK 143
|
|
| |
