|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
45-522 |
0e+00 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 600.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 45 YASNGSVYFDTAKFAASeKHSYGKLVPEAVGDQKALQEGEGDLSISAdrlSEKRSPNDFALWKASKPGEPSWPCPWGKGR 124
Cdd:PTZ00399 175 YESNGSVYFDVEAFRKA-GHVYPKLEPESVADEDRIAEGEGALGKVS---GEKRSPNDFALWKASKPGEPSWDSPWGKGR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 125 PGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDAL 204
Cdd:PTZ00399 251 PGWHIECSAMASNILGDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKGLKMSKSLKNFITIRQAL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 205 KKHSARQLRLAFLMHSWKDTLDYSSNTMESALQYEKFMNEFFLNVKDILRAPVdiTGQFEKWEAEEVELNKNFYGKKTAV 284
Cdd:PTZ00399 331 SKYTARQIRLLFLLHKWDKPMNYSDESMDEAIEKDKVFFNFFANVKIKLRESE--LTSPQKWTQHDFELNELFEETKSAV 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 285 HEALCDNIDTRTVMEEMRALVSQCNLYMAARKaerrRPNRALLENIAMYLTHMLKIFGAIEEesplGFPVGGPGTNlNLE 364
Cdd:PTZ00399 409 HAALLDNFDTPEALQALQKLISATNTYLNSGE----QPSAPLLRSVAQYVTKILSIFGLVEG----SDGLGSQGQN-STS 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 365 STVMPYLQVLSEFREGVRKIAR--------EKKVLEVLQLSDALRDDILPELGVRFEDHEGLPTVVKLVDRDTLLKEKEG 436
Cdd:PTZ00399 480 ENFKPLLEALLRFRDEVRDAAKaemklislDKKKKQLLQLCDKLRDEWLPNLGIRIEDKPDGPSVWKLDDKEELQREKEE 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 437 KKRAEEEKRRKKEEAARKKQEQEAAKLAKMKIPPSEMFLSEVNKYSKFDENGLPTHDTEGKELSKGQAKKLKKLFEAQEK 516
Cdd:PTZ00399 560 KEALKEQKRLRKLKKQEEKKKKELEKLEKAKIPPAEFFKRQEDKYSAFDETGLPTHDADGEEISKKERKKLSKEYDKQAK 639
|
....*.
gi 1907181709 517 LYKEYL 522
Cdd:PTZ00399 640 LHEEYL 645
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
45-415 |
2.06e-98 |
|
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: 305.49 E-value: 2.06e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 45 YASNGSVYFDTAKFaasekHSYGKL---VPEAvgdqkaLQEGEgdlsiSADRLSEKRSPNDFALWKASKPGEPSWPCPWG 121
Cdd:COG0215 135 YEADGDVYFDVRSF-----PDYGKLsgrNLDD------LRAGA-----RVEVDEEKRDPLDFALWKAAKPGEPSWDSPWG 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 122 KGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDcWVRYFLHTGHLTIAGCKMSKSLKNFITIK 201
Cdd:COG0215 199 RGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIAQSEAATGKP-FARYWMHNGFLTVNGEKMSKSLGNFFTVR 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 202 DALKKHSARQLRLAFLMHSWKDTLDYSSNTMESALQ-YEKFMNeFFLNVKDILRAPVDITGQFEKWEAEevelnknfygk 280
Cdd:COG0215 278 DLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKaLERLYN-ALRRLEEALGAADSSAEEIEELREE----------- 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 281 ktaVHEALCDNIDTRTVMEEMRALVSQCNLYMAARKaerrrpNRALLENIAMYLTHMLKIFGaIEEESPLGFpvGGPGTN 360
Cdd:COG0215 346 ---FIAAMDDDFNTPEALAVLFELVREINKALDEGE------DKAALAALAALLRALGGVLG-LLLLEPEAW--QGAAED 413
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907181709 361 LNLESTVMPYLQvlsefregVRKIAREKKVLEvlqLSDALRDDILpELGVRFEDH 415
Cdd:COG0215 414 ELLDALIEALIE--------ERAEARKAKDFA---RADRIRDELA-ALGIVLEDT 456
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
46-240 |
5.56e-84 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 262.69 E-value: 5.56e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 46 ASNGSVYFDTAKFaasekHSYGKLVPEAVGDQKALQEGEGDlsisadrlSEKRSPNDFALWKASKPGEPSWPCPWGKGRP 125
Cdd:pfam01406 124 SDNGDVYFDVSSF-----PDYGKLSGQNLEQLEAGARGEVS--------EGKRDPLDFALWKASKEGEPSWDSPWGKGRP 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 126 GWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDcWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALK 205
Cdd:pfam01406 191 GWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFDKQ-LANYWLHNGHVMIDGEKMSKSLGNFFTIRDVLK 269
|
170 180 190
....*....|....*....|....*....|....*
gi 1907181709 206 KHSARQLRLAFLMHSWKDTLDYSsntmESALQYEK 240
Cdd:pfam01406 270 RYDPEILRYFLLSVHYRSPLDFS----EELLEQAK 300
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
46-414 |
1.80e-80 |
|
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: 258.85 E-value: 1.80e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 46 ASNGSVYFDTAKFaasekHSYGKLvpeAVGDQKALQEGEGDLSISAdrlseKRSPNDFALWKASKPGEPSWPCPWGKGRP 125
Cdd:TIGR00435 136 SDNGDVYFDVSKF-----KDYGKL---SKQDLDQLEAGARVDVDEA-----KRNKLDFVLWKSSKEGEPKWDSPWGKGRP 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 126 GWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFeNDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALK 205
Cdd:TIGR00435 203 GWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQSEAAF-GKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 206 KHSARQLRLAFLMHSWKDTLDYSsntmESALQYEKFMNEFFLNVKDILRAPVDITGQFEKWEAEEVelnKNFYgkkTAVH 285
Cdd:TIGR00435 282 NYDPEILRYFLLSVHYRSPLDFS----EELLEAAKNALERLYKALRVLDTSLAYSGNQSLNKFPDE---KEFE---ARFV 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 286 EALCDNIDTR---TVMEEMralVSQCNLYMAarkaerrrpNRALLENIAMYLTHMLKIFGAIEEESPLGFPVGGPGTNLN 362
Cdd:TIGR00435 352 EAMDDDLNTAnalAVLFEL---AKSINLTFV---------SKADAALLIEHLIFLESRLGLLLGLPSKPVQAGSNDDLGE 419
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1907181709 363 LESTVMPylqvlsefregvRKIAREKKvleVLQLSDALRDDiLPELGVRFED 414
Cdd:TIGR00435 420 IEALIEE------------RSIARKEK---DFAKADEIRDE-LAKKGIVLED 455
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
127-228 |
2.91e-64 |
|
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: 208.20 E-value: 2.91e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 127 WHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFeNDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKK 206
Cdd:cd00672 113 WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQSEAAT-GKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKK 191
|
90 100
....*....|....*....|..
gi 1907181709 207 HSARQLRLAFLMHSWKDTLDYS 228
Cdd:cd00672 192 YDPEVLRLALLSSHYRSPLDFS 213
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
45-522 |
0e+00 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 600.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 45 YASNGSVYFDTAKFAASeKHSYGKLVPEAVGDQKALQEGEGDLSISAdrlSEKRSPNDFALWKASKPGEPSWPCPWGKGR 124
Cdd:PTZ00399 175 YESNGSVYFDVEAFRKA-GHVYPKLEPESVADEDRIAEGEGALGKVS---GEKRSPNDFALWKASKPGEPSWDSPWGKGR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 125 PGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDAL 204
Cdd:PTZ00399 251 PGWHIECSAMASNILGDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKGLKMSKSLKNFITIRQAL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 205 KKHSARQLRLAFLMHSWKDTLDYSSNTMESALQYEKFMNEFFLNVKDILRAPVdiTGQFEKWEAEEVELNKNFYGKKTAV 284
Cdd:PTZ00399 331 SKYTARQIRLLFLLHKWDKPMNYSDESMDEAIEKDKVFFNFFANVKIKLRESE--LTSPQKWTQHDFELNELFEETKSAV 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 285 HEALCDNIDTRTVMEEMRALVSQCNLYMAARKaerrRPNRALLENIAMYLTHMLKIFGAIEEesplGFPVGGPGTNlNLE 364
Cdd:PTZ00399 409 HAALLDNFDTPEALQALQKLISATNTYLNSGE----QPSAPLLRSVAQYVTKILSIFGLVEG----SDGLGSQGQN-STS 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 365 STVMPYLQVLSEFREGVRKIAR--------EKKVLEVLQLSDALRDDILPELGVRFEDHEGLPTVVKLVDRDTLLKEKEG 436
Cdd:PTZ00399 480 ENFKPLLEALLRFRDEVRDAAKaemklislDKKKKQLLQLCDKLRDEWLPNLGIRIEDKPDGPSVWKLDDKEELQREKEE 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 437 KKRAEEEKRRKKEEAARKKQEQEAAKLAKMKIPPSEMFLSEVNKYSKFDENGLPTHDTEGKELSKGQAKKLKKLFEAQEK 516
Cdd:PTZ00399 560 KEALKEQKRLRKLKKQEEKKKKELEKLEKAKIPPAEFFKRQEDKYSAFDETGLPTHDADGEEISKKERKKLSKEYDKQAK 639
|
....*.
gi 1907181709 517 LYKEYL 522
Cdd:PTZ00399 640 LHEEYL 645
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
45-415 |
2.06e-98 |
|
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: 305.49 E-value: 2.06e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 45 YASNGSVYFDTAKFaasekHSYGKL---VPEAvgdqkaLQEGEgdlsiSADRLSEKRSPNDFALWKASKPGEPSWPCPWG 121
Cdd:COG0215 135 YEADGDVYFDVRSF-----PDYGKLsgrNLDD------LRAGA-----RVEVDEEKRDPLDFALWKAAKPGEPSWDSPWG 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 122 KGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDcWVRYFLHTGHLTIAGCKMSKSLKNFITIK 201
Cdd:COG0215 199 RGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIAQSEAATGKP-FARYWMHNGFLTVNGEKMSKSLGNFFTVR 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 202 DALKKHSARQLRLAFLMHSWKDTLDYSSNTMESALQ-YEKFMNeFFLNVKDILRAPVDITGQFEKWEAEevelnknfygk 280
Cdd:COG0215 278 DLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKaLERLYN-ALRRLEEALGAADSSAEEIEELREE----------- 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 281 ktaVHEALCDNIDTRTVMEEMRALVSQCNLYMAARKaerrrpNRALLENIAMYLTHMLKIFGaIEEESPLGFpvGGPGTN 360
Cdd:COG0215 346 ---FIAAMDDDFNTPEALAVLFELVREINKALDEGE------DKAALAALAALLRALGGVLG-LLLLEPEAW--QGAAED 413
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907181709 361 LNLESTVMPYLQvlsefregVRKIAREKKVLEvlqLSDALRDDILpELGVRFEDH 415
Cdd:COG0215 414 ELLDALIEALIE--------ERAEARKAKDFA---RADRIRDELA-ALGIVLEDT 456
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
46-240 |
5.56e-84 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 262.69 E-value: 5.56e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 46 ASNGSVYFDTAKFaasekHSYGKLVPEAVGDQKALQEGEGDlsisadrlSEKRSPNDFALWKASKPGEPSWPCPWGKGRP 125
Cdd:pfam01406 124 SDNGDVYFDVSSF-----PDYGKLSGQNLEQLEAGARGEVS--------EGKRDPLDFALWKASKEGEPSWDSPWGKGRP 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 126 GWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDcWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALK 205
Cdd:pfam01406 191 GWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFDKQ-LANYWLHNGHVMIDGEKMSKSLGNFFTIRDVLK 269
|
170 180 190
....*....|....*....|....*....|....*
gi 1907181709 206 KHSARQLRLAFLMHSWKDTLDYSsntmESALQYEK 240
Cdd:pfam01406 270 RYDPEILRYFLLSVHYRSPLDFS----EELLEQAK 300
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
46-414 |
1.80e-80 |
|
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: 258.85 E-value: 1.80e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 46 ASNGSVYFDTAKFaasekHSYGKLvpeAVGDQKALQEGEGDLSISAdrlseKRSPNDFALWKASKPGEPSWPCPWGKGRP 125
Cdd:TIGR00435 136 SDNGDVYFDVSKF-----KDYGKL---SKQDLDQLEAGARVDVDEA-----KRNKLDFVLWKSSKEGEPKWDSPWGKGRP 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 126 GWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFeNDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALK 205
Cdd:TIGR00435 203 GWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQSEAAF-GKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 206 KHSARQLRLAFLMHSWKDTLDYSsntmESALQYEKFMNEFFLNVKDILRAPVDITGQFEKWEAEEVelnKNFYgkkTAVH 285
Cdd:TIGR00435 282 NYDPEILRYFLLSVHYRSPLDFS----EELLEAAKNALERLYKALRVLDTSLAYSGNQSLNKFPDE---KEFE---ARFV 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 286 EALCDNIDTR---TVMEEMralVSQCNLYMAarkaerrrpNRALLENIAMYLTHMLKIFGAIEEESPLGFPVGGPGTNLN 362
Cdd:TIGR00435 352 EAMDDDLNTAnalAVLFEL---AKSINLTFV---------SKADAALLIEHLIFLESRLGLLLGLPSKPVQAGSNDDLGE 419
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1907181709 363 LESTVMPylqvlsefregvRKIAREKKvleVLQLSDALRDDiLPELGVRFED 414
Cdd:TIGR00435 420 IEALIEE------------RSIARKEK---DFAKADEIRDE-LAKKGIVLED 455
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
127-228 |
2.91e-64 |
|
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: 208.20 E-value: 2.91e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 127 WHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFeNDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKK 206
Cdd:cd00672 113 WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQSEAAT-GKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKK 191
|
90 100
....*....|....*....|..
gi 1907181709 207 HSARQLRLAFLMHSWKDTLDYS 228
Cdd:cd00672 192 YDPEVLRLALLSSHYRSPLDFS 213
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
44-235 |
3.17e-51 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 183.59 E-value: 3.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 44 SYASNGSVYFDTAKFAasekhSYGKLVPEAVGDQKAlqeGEgdlSISADrlSEKRSPNDFALWKASKPGEPSWPCPWGKG 123
Cdd:PLN02946 192 AYRVDGDVYFSVDKFP-----EYGKLSGRKLEDNRA---GE---RVAVD--SRKKNPADFALWKAAKEGEPFWDSPWGPG 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 124 RPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFEnDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDA 203
Cdd:PLN02946 259 RPGWHIECSAMSAAYLGHSFDIHGGGMDLVFPHHENEIAQSCAACC-DSNISYWIHNGFVTVDSEKMSKSLGNFFTIRQV 337
|
170 180 190
....*....|....*....|....*....|..
gi 1907181709 204 LKKHSARQLRLAFLMHSWKDTLDYSSNTMESA 235
Cdd:PLN02946 338 IDLYHPLALRLFLLGTHYRSPINYSDVQLESA 369
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
46-235 |
5.53e-45 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 168.74 E-value: 5.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 46 ASNGSVYFDTAKFAAsekhsYGKLVPEAVGDQKALQEGEGDlsisadrlSEKRSPNDFALWKASKPGEPSWPCPWGKGRP 125
Cdd:PRK14535 363 AANGDVYYAVREFAA-----YGQLSGKSLDDLRAGERVEVD--------GFKRDPLDFVLWKAAKAGEPAWESPWGNGRP 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 126 GWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDC---------------WVRYFLHTGHLTIAGCKM 190
Cdd:PRK14535 430 GWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIAQSVGATGHTCghhhaqthhgqsiasHVKYWLHNGFIRVDGEKM 509
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907181709 191 SKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSSNTMESA 235
Cdd:PRK14535 510 SKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNYSDAHLDDA 554
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
97-237 |
3.31e-37 |
|
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: 142.17 E-value: 3.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 97 KRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDCWVRY 176
Cdd:TIGR03447 196 KRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSDLIFPHHEFSAAHAEAATGVRRMARH 275
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907181709 177 FLHTGHLTIAGCKMSKSLKNFITIKDaLKK--HSARQLRLAFLMHSWKDTLDYSSNTMESALQ 237
Cdd:TIGR03447 276 YVHAGMIGLDGEKMSKSLGNLVFVSK-LRAagVDPAAIRLGLLAGHYRQDRDWTDAVLAEAEA 337
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
97-237 |
7.22e-36 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 137.75 E-value: 7.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 97 KRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDCWVRY 176
Cdd:PRK12418 169 KRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAHAEAATGERRFARH 248
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907181709 177 FLHTGHLTIAGCKMSKSLKNFITIKdALKK--HSARQLRLAFLMHSWKDTLDYSSNTMESALQ 237
Cdd:PRK12418 249 YVHAGMIGLDGEKMSKSRGNLVFVS-RLRAagVDPAAIRLALLAGHYRADREWTDAVLAEAEA 310
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
44-310 |
5.77e-35 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 137.36 E-value: 5.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 44 SYASNGSVYFDTAKFAasekhSYGKLVPEAVGDqkaLQEGEgdlSISADrlSEKRSPNDFALWKASKPGEP---SWPCPW 120
Cdd:PRK14536 145 TYCAGGNVYFDIRTFP-----SYGSLASAAVED---LQAGA---RIEHD--TNKRNPHDFVLWFTRSKFENhalTWDSPW 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 121 GKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAyFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITI 200
Cdd:PRK14536 212 GRGYPGWHIECSAMSMKYLGEQCDIHIGGVDHIRVHHTNEIAQCEA-ATGKPWVRYWLHHEFLLMNKGKMSKSAGQFLTL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 201 KDALKK-HSARQLRLAFLMHSWKDTLDYSSNTMESALQYEKFMNEFFLNVKDILRAPVDIT-GQFEKWEAEEVELNKNFY 278
Cdd:PRK14536 291 SSLQEKgFQPLDYRFFLLGGHYRSQLAFSWEALKTAKAARRSLVRRVARVVDAARATTGSVrGTLAECAAERVAESRASE 370
|
250 260 270
....*....|....*....|....*....|....
gi 1907181709 279 GKK--TAVHEALCDNIDTRTVMEEMRALVSQCNL 310
Cdd:PRK14536 371 SELllTDFRAALEDDFSTPKALSELQKLVKDTSV 404
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
44-235 |
6.00e-26 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 110.71 E-value: 6.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 44 SYASNGSVYFDTAKFaasekHSYGKLVPEAVGDQKALQEGEGDLSISadrlseKRSPNDFALWKAS---KPGEPSWPCPW 120
Cdd:PRK14534 143 TYFVNGNVYFDTSCF-----KSYGQMAGINLNDFKDMSVSRVEIDKS------KRNKSDFVLWFTNskfKDQEMKWDSPW 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 121 GKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFeNDCWVRYFLHTGHLTIAGCKMSKSLKNFITI 200
Cdd:PRK14534 212 GFGYPSWHLECAAMNLEYFKSTLDIHLGGVDHIGVHHINEIAIAECYL-NKKWCDMFVHGEFLIMEYEKMSKSNNNFITI 290
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907181709 201 KDALKKH-SARQLRLAFLMHSWKDTLDYSSNTMESA 235
Cdd:PRK14534 291 KDLEDQGfSPLDFRYFCLTAHYRTQLKFTFNNLKAC 326
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
166-331 |
6.59e-08 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 55.64 E-value: 6.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 166 AYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLaFLMHS---WKDtLDYSSNTMESAL-QYEKF 241
Cdd:PRK12300 554 AIFPEEKWPRGIVVNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRL-YLTSSaelLQD-ADWREKEVESVRrQLERF 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 242 MnEFFLNVKDIlrAPVDITGQFEKWeaeeveLNKNFYGKKTAVHEALcDNIDTRTVMEEmrALVsqcNLYMAARKAERR- 320
Cdd:PRK12300 632 Y-ELAKELIEI--GGEEELRFIDKW------LLSRLNRIIKETTEAM-ESFQTRDAVQE--AFY---ELLNDLRWYLRRv 696
|
170
....*....|..
gi 1907181709 321 -RPNRALLENIA 331
Cdd:PRK12300 697 gEANNKVLREVL 708
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
150-236 |
9.59e-06 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 48.53 E-value: 9.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 150 FDLRFPHHD---NELAQS----EAYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRlaFLMHSWK 222
Cdd:PLN02959 672 FDLRVSGKDliqNHLTFAiynhTAIWAEEHWPRGFRCNGHLMLNSEKMSKSTGNFLTLRQAIEEFSADATR--FALADAG 749
|
90
....*....|....*..
gi 1907181709 223 DTLD---YSSNTMESAL 236
Cdd:PLN02959 750 DGVDdanFVFETANAAI 766
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
174-220 |
1.10e-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: 44.44 E-value: 1.10e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1907181709 174 VRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHS 220
Cdd:cd00814 265 PTRIVAHGYLTVEGKKMSKSRGNVVDPDDLLERYGADALRYYLLRER 311
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
180-220 |
4.50e-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: 4.50e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1907181709 180 TGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHS 220
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 ... |
126-194 |
8.07e-04 |
|
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: 8.07e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181709 126 GWHIECSAMAGTLLGASMDIHGGGFDLRFpHHDNELAQSEAYfeNDCWVRYFLHTGHLTIA-GCKMSKSL 194
Cdd:cd00802 77 EYMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKA--GGPARPFGLTFGRVMGAdGTKMSKSK 143
|
|
| |
