|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
29-412 |
0e+00 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 784.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 29 VRPVTPGPTATMYVCGITPYDATHLGHAATYLTFDLVHRLWLDAGHTVHYVQNVTDVDDPLFERADRDGIDWRDLGDRET 108
Cdd:PRK12418 1 VRPVAPGGTATMYVCGITPYDATHLGHAATYLAFDLVNRVWRDAGHDVHYVQNVTDVDDPLLERAARDGVDWRDLAEREI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 109 QLFREDMTALRVLPPHDYVAATETISEVVELVEKMLASGAAYVVDDAQYPDVYYRADATTQFGYESGYDRETMLRLFGER 188
Cdd:PRK12418 81 ALFREDMEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYVVDDEEYPDVYFSVDATPQFGYESGYDRATMLELFAER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 189 GGDPDRPGKSDELDALLWRAERPGEPSWPSPFGAGRPGWHVECSAIALTRIGSGLDIQGGGSDLIFPHHEFSAAHAESVT 268
Cdd:PRK12418 161 GGDPDRPGKRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAHAEAAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 269 GERRFARHYVHAGMIGWDGHKMSKSRGNLVLVSRLRAQGVDPSAVRLGLFAGHYRSDRFWSDAVLDEANARLKQWRTATA 348
Cdd:PRK12418 241 GERRFARHYVHAGMIGLDGEKMSKSRGNLVFVSRLRAAGVDPAAIRLALLAGHYRADREWTDAVLAEAEARLARWRAAAA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039668908 349 LPAGPDATDVVARVRQYLADDLDTPKALAALDGWCTDALAYGGHDAAAPRQVAATVDALLGVEL 412
Cdd:PRK12418 321 LPAGPDAADVVARVRAALADDLDTPGALAAVDGWATDALEGGGDDAAAPALVATAVDALLGVAL 384
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
2-412 |
0e+00 |
|
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: 769.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 2 QSWSAPSIPVLEGRGPQLRLYDSADRQVRPVTPGPTATMYVCGITPYDATHLGHAATYLTFDLVHRLWLDAGHTVHYVQN 81
Cdd:TIGR03447 1 QSWPAPAVPALPGTGPPLRLFDTADGQVRPVEPGPEAGMYVCGITPYDATHLGHAATYLTFDLVNRVWRDAGHRVHYVQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 82 VTDVDDPLFERADRDGIDWRDLGDRETQLFREDMTALRVLPPHDYVAATETISEVVELVEKMLASGAAYVVDDAQYPDVY 161
Cdd:TIGR03447 81 VTDVDDPLFERAERDGVDWRELGTSQIDLFREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYIVEGPEYPDVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 162 YRADATTQFGYESGYDRETMLRLFGERGGDPDRPGKSDELDALLWRAERPGEPSWPSPFGAGRPGWHVECSAIALTRIGS 241
Cdd:TIGR03447 161 FSIDATEQFGYESGYDRATMLELFAERGGDPDRPGKRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNRLGA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 242 GLDIQGGGSDLIFPHHEFSAAHAESVTGERRFARHYVHAGMIGWDGHKMSKSRGNLVLVSRLRAQGVDPSAVRLGLFAGH 321
Cdd:TIGR03447 241 GFDIQGGGSDLIFPHHEFSAAHAEAATGVRRMARHYVHAGMIGLDGEKMSKSLGNLVFVSKLRAAGVDPAAIRLGLLAGH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 322 YRSDRFWSDAVLDEANARLKQWRTATALPAGPDATDVVARVRQYLADDLDTPKALAALDGWCTDALAYGGHDAAAPRQVA 401
Cdd:TIGR03447 321 YRQDRDWTDAVLAEAEARLARWRAALALPDAPDATDLIARLRQHLANDLDTPAALAAVDGWAADALSYGGSDTEAPALVA 400
|
410
....*....|.
gi 1039668908 402 ATVDALLGVEL 412
Cdd:TIGR03447 401 TAVDALLGVRL 411
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
19-410 |
1.46e-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: 365.58 E-value: 1.46e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 19 LRLYDSADRQVR---PVTPGpTATMYVCGITPYDATHLGHAATYLTFDLVHRlWLDA-GHTVHYVQNVTDVDDPLFERAD 94
Cdd:COG0215 2 LKLYNTLTRKKEefvPLEPG-KVRMYVCGPTVYDYAHIGHARTFVVFDVLRR-YLRYlGYKVTYVRNITDVDDKIIKRAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 95 RDGIDWRDLGDRETQLFREDMTALRVLPPHDYVAATETISEVVELVEKMLASGAAYVVDDaqypDVYYRADATTQFGYES 174
Cdd:COG0215 80 EEGESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEADG----DVYFDVRSFPDYGKLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 175 GYDRETMLRlfGERGgDPDrPGKSDELDALLWRAERPGEPSWPSPFGAGRPGWHVECSAIALTRIGSGLDIQGGGSDLIF 254
Cdd:COG0215 156 GRNLDDLRA--GARV-EVD-EEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 255 PHHEFSAAHAESVTGErRFARHYVHAGMIGWDGHKMSKSRGNLVLVSRLRAQgVDPSAVRLGLFAGHYRS--DrfWSDAV 332
Cdd:COG0215 232 PHHENEIAQSEAATGK-PFARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKK-YDPEVLRFFLLSAHYRSplD--FSEEA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 333 LDEANARLKQWRTA---------TALPAGPDATDVVARVRQYLADDLDTPKALAALDGWCTDALAY--GGHDAAAPRQVA 401
Cdd:COG0215 308 LEEAEKALERLYNAlrrleealgAADSSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKAldEGEDKAALAALA 387
|
....*....
gi 1039668908 402 ATVDALLGV 410
Cdd:COG0215 388 ALLRALGGV 396
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
28-324 |
6.70e-100 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 299.67 E-value: 6.70e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 28 QVRPVTPGpTATMYVCGITPYDATHLGHAATYLTFDLVHRLWLDAGHTVHYVQNVTDVDDPLFERADRDGIDWRDLGDRE 107
Cdd:pfam01406 1 FFVPLHQG-KVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 108 TQLFREDMTALRVLPPHDYVAATETISEVVELVEKMLASGAAYVVDDAqypDVYYRADATTQFGYESGYDRETmlRLFGE 187
Cdd:pfam01406 80 IEAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNG---DVYFDVSSFPDYGKLSGQNLEQ--LEAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 188 RGgdPDRPGKSDELDALLWRAERPGEPSWPSPFGAGRPGWHVECSAIALTRIGSGLDIQGGGSDLIFPHHEFSAAHAESV 267
Cdd:pfam01406 155 RG--EVSEGKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAA 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039668908 268 TGeRRFARHYVHAGMIGWDGHKMSKSRGNLVLVsRLRAQGVDPSAVRLGLFAGHYRS 324
Cdd:pfam01406 233 FD-KQLANYWLHNGHVMIDGEKMSKSLGNFFTI-RDVLKRYDPEILRYFLLSVHYRS 287
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
20-329 |
7.63e-93 |
|
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: 278.31 E-value: 7.63e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 20 RLYDSADRQVRPVTP--GPTATMYVCGITPYDATHLGHAATYLTFDLVHRLWLDAGHTVHYVQNVTDVDDPLFERADRDG 97
Cdd:cd00672 1 RLYNTLTRQKEEFVPlnPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLGYKVRYVQNITDIDDKIIKRAREEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 98 IDWRDLGDRETQLFREDMTALRVLPphdyvaatetisevvelvekmlasgaayvvddaqyPDVYYRAdattqfgyesgyd 177
Cdd:cd00672 81 LSWKEVADYYTKEFFEDMKALNVLP-----------------------------------PDVVPRV------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 178 retmlrlfgerggdpdrpgksdeldallwraerpgepswpspfgagrpgWHVECSAIALTRIGSGLDIQGGGSDLIFPHH 257
Cdd:cd00672 113 -------------------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHH 143
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039668908 258 EFSAAHAESVTGErRFARHYVHAGMIGWDGHKMSKSRGNLVLVSRLrAQGVDPSAVRLGLFAGHYRSDRFWS 329
Cdd:cd00672 144 ENEIAQSEAATGK-PFARYWLHTGHLTIDGEKMSKSLGNFITVRDA-LKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
29-412 |
0e+00 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 784.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 29 VRPVTPGPTATMYVCGITPYDATHLGHAATYLTFDLVHRLWLDAGHTVHYVQNVTDVDDPLFERADRDGIDWRDLGDRET 108
Cdd:PRK12418 1 VRPVAPGGTATMYVCGITPYDATHLGHAATYLAFDLVNRVWRDAGHDVHYVQNVTDVDDPLLERAARDGVDWRDLAEREI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 109 QLFREDMTALRVLPPHDYVAATETISEVVELVEKMLASGAAYVVDDAQYPDVYYRADATTQFGYESGYDRETMLRLFGER 188
Cdd:PRK12418 81 ALFREDMEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYVVDDEEYPDVYFSVDATPQFGYESGYDRATMLELFAER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 189 GGDPDRPGKSDELDALLWRAERPGEPSWPSPFGAGRPGWHVECSAIALTRIGSGLDIQGGGSDLIFPHHEFSAAHAESVT 268
Cdd:PRK12418 161 GGDPDRPGKRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAHAEAAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 269 GERRFARHYVHAGMIGWDGHKMSKSRGNLVLVSRLRAQGVDPSAVRLGLFAGHYRSDRFWSDAVLDEANARLKQWRTATA 348
Cdd:PRK12418 241 GERRFARHYVHAGMIGLDGEKMSKSRGNLVFVSRLRAAGVDPAAIRLALLAGHYRADREWTDAVLAEAEARLARWRAAAA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039668908 349 LPAGPDATDVVARVRQYLADDLDTPKALAALDGWCTDALAYGGHDAAAPRQVAATVDALLGVEL 412
Cdd:PRK12418 321 LPAGPDAADVVARVRAALADDLDTPGALAAVDGWATDALEGGGDDAAAPALVATAVDALLGVAL 384
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
2-412 |
0e+00 |
|
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: 769.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 2 QSWSAPSIPVLEGRGPQLRLYDSADRQVRPVTPGPTATMYVCGITPYDATHLGHAATYLTFDLVHRLWLDAGHTVHYVQN 81
Cdd:TIGR03447 1 QSWPAPAVPALPGTGPPLRLFDTADGQVRPVEPGPEAGMYVCGITPYDATHLGHAATYLTFDLVNRVWRDAGHRVHYVQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 82 VTDVDDPLFERADRDGIDWRDLGDRETQLFREDMTALRVLPPHDYVAATETISEVVELVEKMLASGAAYVVDDAQYPDVY 161
Cdd:TIGR03447 81 VTDVDDPLFERAERDGVDWRELGTSQIDLFREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYIVEGPEYPDVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 162 YRADATTQFGYESGYDRETMLRLFGERGGDPDRPGKSDELDALLWRAERPGEPSWPSPFGAGRPGWHVECSAIALTRIGS 241
Cdd:TIGR03447 161 FSIDATEQFGYESGYDRATMLELFAERGGDPDRPGKRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNRLGA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 242 GLDIQGGGSDLIFPHHEFSAAHAESVTGERRFARHYVHAGMIGWDGHKMSKSRGNLVLVSRLRAQGVDPSAVRLGLFAGH 321
Cdd:TIGR03447 241 GFDIQGGGSDLIFPHHEFSAAHAEAATGVRRMARHYVHAGMIGLDGEKMSKSLGNLVFVSKLRAAGVDPAAIRLGLLAGH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 322 YRSDRFWSDAVLDEANARLKQWRTATALPAGPDATDVVARVRQYLADDLDTPKALAALDGWCTDALAYGGHDAAAPRQVA 401
Cdd:TIGR03447 321 YRQDRDWTDAVLAEAEARLARWRAALALPDAPDATDLIARLRQHLANDLDTPAALAAVDGWAADALSYGGSDTEAPALVA 400
|
410
....*....|.
gi 1039668908 402 ATVDALLGVEL 412
Cdd:TIGR03447 401 TAVDALLGVRL 411
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
19-410 |
1.46e-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: 365.58 E-value: 1.46e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 19 LRLYDSADRQVR---PVTPGpTATMYVCGITPYDATHLGHAATYLTFDLVHRlWLDA-GHTVHYVQNVTDVDDPLFERAD 94
Cdd:COG0215 2 LKLYNTLTRKKEefvPLEPG-KVRMYVCGPTVYDYAHIGHARTFVVFDVLRR-YLRYlGYKVTYVRNITDVDDKIIKRAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 95 RDGIDWRDLGDRETQLFREDMTALRVLPPHDYVAATETISEVVELVEKMLASGAAYVVDDaqypDVYYRADATTQFGYES 174
Cdd:COG0215 80 EEGESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEADG----DVYFDVRSFPDYGKLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 175 GYDRETMLRlfGERGgDPDrPGKSDELDALLWRAERPGEPSWPSPFGAGRPGWHVECSAIALTRIGSGLDIQGGGSDLIF 254
Cdd:COG0215 156 GRNLDDLRA--GARV-EVD-EEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 255 PHHEFSAAHAESVTGErRFARHYVHAGMIGWDGHKMSKSRGNLVLVSRLRAQgVDPSAVRLGLFAGHYRS--DrfWSDAV 332
Cdd:COG0215 232 PHHENEIAQSEAATGK-PFARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKK-YDPEVLRFFLLSAHYRSplD--FSEEA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 333 LDEANARLKQWRTA---------TALPAGPDATDVVARVRQYLADDLDTPKALAALDGWCTDALAY--GGHDAAAPRQVA 401
Cdd:COG0215 308 LEEAEKALERLYNAlrrleealgAADSSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKAldEGEDKAALAALA 387
|
....*....
gi 1039668908 402 ATVDALLGV 410
Cdd:COG0215 388 ALLRALGGV 396
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
19-379 |
5.38e-101 |
|
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: 308.16 E-value: 5.38e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 19 LRLYDSADRQVRPVTP--GPTATMYVCGITPYDATHLGHAATYLTFDLVHRLWLDAGHTVHYVQNVTDVDDPLFERADRD 96
Cdd:TIGR00435 1 LKLYNTLTRQKEEFEPlvQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLRYLGYKVQYVQNITDIDDKIIKRAREN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 97 GIDWRDLGDRETQLFREDMTALRVLPPHDYVAATETISEVVELVEKMLASGAAYVVDDAqypDVYYRADATTQFGYESGY 176
Cdd:TIGR00435 81 GESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNG---DVYFDVSKFKDYGKLSKQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 177 DRETMLRlfgERGGDPDRpGKSDELDALLWRAERPGEPSWPSPFGAGRPGWHVECSAIALTRIGSGLDIQGGGSDLIFPH 256
Cdd:TIGR00435 158 DLDQLEA---GARVDVDE-AKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 257 HEFSAAHAESVTGeRRFARHYVHAGMIGWDGHKMSKSRGNLVLVSRLrAQGVDPSAVRLGLFAGHYRSDRFWSDAVLDEA 336
Cdd:TIGR00435 234 HENEIAQSEAAFG-KQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDV-LKNYDPEILRYFLLSVHYRSPLDFSEELLEAA 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039668908 337 NARLKQWRTA------TALPAG-------PDATDVVARVRQYLADDLDTPKALAAL 379
Cdd:TIGR00435 312 KNALERLYKAlrvldtSLAYSGnqslnkfPDEKEFEARFVEAMDDDLNTANALAVL 367
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
28-324 |
6.70e-100 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 299.67 E-value: 6.70e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 28 QVRPVTPGpTATMYVCGITPYDATHLGHAATYLTFDLVHRLWLDAGHTVHYVQNVTDVDDPLFERADRDGIDWRDLGDRE 107
Cdd:pfam01406 1 FFVPLHQG-KVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 108 TQLFREDMTALRVLPPHDYVAATETISEVVELVEKMLASGAAYVVDDAqypDVYYRADATTQFGYESGYDRETmlRLFGE 187
Cdd:pfam01406 80 IEAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNG---DVYFDVSSFPDYGKLSGQNLEQ--LEAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 188 RGgdPDRPGKSDELDALLWRAERPGEPSWPSPFGAGRPGWHVECSAIALTRIGSGLDIQGGGSDLIFPHHEFSAAHAESV 267
Cdd:pfam01406 155 RG--EVSEGKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAA 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039668908 268 TGeRRFARHYVHAGMIGWDGHKMSKSRGNLVLVsRLRAQGVDPSAVRLGLFAGHYRS 324
Cdd:pfam01406 233 FD-KQLANYWLHNGHVMIDGEKMSKSLGNFFTI-RDVLKRYDPEILRYFLLSVHYRS 287
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
20-329 |
7.63e-93 |
|
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: 278.31 E-value: 7.63e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 20 RLYDSADRQVRPVTP--GPTATMYVCGITPYDATHLGHAATYLTFDLVHRLWLDAGHTVHYVQNVTDVDDPLFERADRDG 97
Cdd:cd00672 1 RLYNTLTRQKEEFVPlnPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLGYKVRYVQNITDIDDKIIKRAREEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 98 IDWRDLGDRETQLFREDMTALRVLPphdyvaatetisevvelvekmlasgaayvvddaqyPDVYYRAdattqfgyesgyd 177
Cdd:cd00672 81 LSWKEVADYYTKEFFEDMKALNVLP-----------------------------------PDVVPRV------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 178 retmlrlfgerggdpdrpgksdeldallwraerpgepswpspfgagrpgWHVECSAIALTRIGSGLDIQGGGSDLIFPHH 257
Cdd:cd00672 113 -------------------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHH 143
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039668908 258 EFSAAHAESVTGErRFARHYVHAGMIGWDGHKMSKSRGNLVLVSRLrAQGVDPSAVRLGLFAGHYRSDRFWS 329
Cdd:cd00672 144 ENEIAQSEAATGK-PFARYWLHTGHLTIDGEKMSKSLGNFITVRDA-LKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
14-379 |
6.46e-77 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 248.69 E-value: 6.46e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 14 GRGPQLRLYDSADRQ---VRPVTPGPTAtMYVCGITPYDATHLGHAATYLTFDLVHRLWLDAGHTVHYVQNVTDVDDPLF 90
Cdd:PLN02946 55 SRGRELHLYNTMSRKkelFKPKVEGKVG-MYVCGVTAYDLSHIGHARVYVTFDVLYRYLKHLGYEVRYVRNFTDVDDKII 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 91 ERADRDGIDWRDLGDRETQLFREDMTALRVLPPHDYVAATETISEVVELVEKMLASGAAYVVDDaqypDVYYRADATTQF 170
Cdd:PLN02946 134 ARANELGEDPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVDG----DVYFSVDKFPEY 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 171 GYESGydRETMLRLFGERGGDPDRpgKSDELDALLWRAERPGEPSWPSPFGAGRPGWHVECSAIALTRIGSGLDIQGGGS 250
Cdd:PLN02946 210 GKLSG--RKLEDNRAGERVAVDSR--KKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGM 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 251 DLIFPHHEFSAAHAESVTGERRFArHYVHAGMIGWDGHKMSKSRGNLVLVsRLRAQGVDPSAVRLGLFAGHYRSDRFWSD 330
Cdd:PLN02946 286 DLVFPHHENEIAQSCAACCDSNIS-YWIHNGFVTVDSEKMSKSLGNFFTI-RQVIDLYHPLALRLFLLGTHYRSPINYSD 363
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039668908 331 AVLDEANARL---------------KQWRTATALPAGPDATDVVARVRQ----YLADDLDTPKALAAL 379
Cdd:PLN02946 364 VQLESASERIfyiyqtlhdceeslqQHDSTFEKDSVPPDTLNCINKFHDefvtSMSDDLHTPVALAAL 431
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
9-381 |
1.00e-69 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 231.84 E-value: 1.00e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 9 IPVLEGRGPQ-LRLYDSADRQVRPVTP--GPTATMYVCGITPYDATHLGHAATYLTFDLVHRLWLDA-GHTVHYVQNVTD 84
Cdd:PTZ00399 29 KPSKEGKYLTgLKVNNSLTGGKVEFVPqnGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEDYfGYDVFYVMNITD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 85 VDDPLFERADRDGID-WRDLGDRETQLFREDMTALRVLPPHDYVAATETISEVVELVEKMLASGAAYVVDDAQYPDVY-Y 162
Cdd:PTZ00399 109 IDDKIIKRAREEKLSiFLELARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYESNGSVYFDVEaF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 163 RADATTqfgY-----ESGYDRETMLRLFGERGGDPDRpgKSDELDALLWRAERPGEPSWPSPFGAGRPGWHVECSAIALT 237
Cdd:PTZ00399 189 RKAGHV---YpklepESVADEDRIAEGEGALGKVSGE--KRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 238 RIGSGLDIQGGGSDLIFPHHEFSAAHAESVTGERRFARHYVHAGMIGWDGHKMSKSRGNLV----LVSRLraqgvDPSAV 313
Cdd:PTZ00399 264 ILGDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKGLKMSKSLKNFItirqALSKY-----TARQI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 314 RLgLFAGH-YRSDRFWSDAVLDEA--------------NARLKQwrTATALPAGPDATDV---------VARVRQYLADD 369
Cdd:PTZ00399 339 RL-LFLLHkWDKPMNYSDESMDEAiekdkvffnffanvKIKLRE--SELTSPQKWTQHDFelnelfeetKSAVHAALLDN 415
|
410
....*....|..
gi 1039668908 370 LDTPKALAALDG 381
Cdd:PTZ00399 416 FDTPEALQALQK 427
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
17-379 |
1.80e-69 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 232.30 E-value: 1.80e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 17 PQLRLYDSADRQVRPVTP--GPTATMYVCGITPYDATHLGHAATYLTFDLVHRLWLDAGHTVHYVQNVTDVDDPLFERAD 94
Cdd:PRK14535 226 PMTTIYNTLTRQKEPFAPidPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 95 RDGIDWRDLGDRETQLFREDMTALRVLPPHDYVAATETISEVVELVEKMLASGAAYvvdDAQYPDVYYRADATTQFGYES 174
Cdd:PRK14535 306 ENGETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAY---PAANGDVYYAVREFAAYGQLS 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 175 GYDRETMLRlfGERggdPDRPG-KSDELDALLWRAERPGEPSWPSPFGAGRPGWHVECSAIALTRIGSGLDIQGGGSDLI 253
Cdd:PRK14535 383 GKSLDDLRA--GER---VEVDGfKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQ 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 254 FPHHEFSAAHAESVTGER---------------RFARHYVHAGMIGWDGHKMSKSRGNLVLVSRLRAQgVDPSAVRLGLF 318
Cdd:PRK14535 458 FPHHENEIAQSVGATGHTcghhhaqthhgqsiaSHVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQ-YDPEVVRFFIL 536
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039668908 319 AGHYRSDRFWSDAVLDEANARLKQWRTA--TALPAGPDAT----DVVARVRQYLADDLDTPKALAAL 379
Cdd:PRK14535 537 RAHYRSPLNYSDAHLDDAKGALTRLYTTlkNTPAAEFMLSenvnDYTRRFYAAMNDDFGTVEAVAVL 603
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
19-379 |
2.06e-45 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 163.55 E-value: 2.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 19 LRLYDSADRQV---RPVTPGpTATMYVCGITPYDATHLGHAATYLTFDLVHRLWLDAGHTVHYVQNVTDV---------- 85
Cdd:PRK14536 3 LRLYNTLGRQQeefQPIEHG-HVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTLHFLGYRVTHVMNITDVghltddadsg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 86 DDPLFERADRDGIDWRDLGDRETQLFREDMTALRVLPPHDYVAATETISEVVELVEKMLASGAAYVVDDaqypDVYYRAD 165
Cdd:PRK14536 82 EDKMVKSAQEHGKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCAGG----NVYFDIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 166 ATTQFGYESGYDRETMLRlfGERGgDPDRpGKSDELDALLWRAERPGEP---SWPSPFGAGRPGWHVECSAIALTRIGSG 242
Cdd:PRK14536 158 TFPSYGSLASAAVEDLQA--GARI-EHDT-NKRNPHDFVLWFTRSKFENhalTWDSPWGRGYPGWHIECSAMSMKYLGEQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 243 LDIQGGGSDLIFPHHEFSAAHAESVTGeRRFARHYVHAGMIGWDGHKMSKSRGNLVLVSRLRAQGVDPSAVRLGLFAGHY 322
Cdd:PRK14536 234 CDIHIGGVDHIRVHHTNEIAQCEAATG-KPWVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQEKGFQPLDYRFFLLGGHY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 323 RSDRFWSDAVLDEANARLKQ--------------------------WRTATALPAGPDATDVVARVRQYLADDLDTPKAL 376
Cdd:PRK14536 313 RSQLAFSWEALKTAKAARRSlvrrvarvvdaarattgsvrgtlaecAAERVAESRASESELLLTDFRAALEDDFSTPKAL 392
|
...
gi 1039668908 377 AAL 379
Cdd:PRK14536 393 SEL 395
|
|
| Anticodon_Ia_Cys_like |
cd07955 |
Anticodon-binding domain of cysteinyl tRNA synthetases and domain found in MshC; This domain ... |
330-410 |
1.49e-33 |
|
Anticodon-binding domain of cysteinyl tRNA synthetases and domain found in MshC; 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. The family also includes a domain of MshC, the rate-determining enzyme in the mycothiol biosynthetic pathway, which is specific to actinomycetes. The anticodon-binding site of CysRS lies C-terminal to this model's footprint and is not shared by MshC.
Pssm-ID: 153409 [Multi-domain] Cd Length: 81 Bit Score: 120.24 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 330 DAVLDEANARLKQWRTATALPAGPDATDVVARVRQYLADDLDTPKALAALDGWCTDALAYGGHDAAAPRQVAATVDALLG 409
Cdd:cd07955 1 DEVLADAEARLARWRSAVALPDGPDAEALVARLREALADDLDTPKALAALDAWAREALSRGGTDPDAPALVRTAVDALLG 80
|
.
gi 1039668908 410 V 410
Cdd:cd07955 81 V 81
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
19-324 |
3.41e-32 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 126.89 E-value: 3.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 19 LRLYDSADRQVRPVTPGPTATMYVCGITPYDATHLGHAATYLTFDLVHRLWLDAGHTVHYVQNVTDV----------DDP 88
Cdd:PRK14534 3 LKLYNTKTKDLSELKNFSDVKVYACGPTVYNYAHIGNFRTYIFEDLLIKSLRLLKYNVNYAMNITDIghltgdfddgEDK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 89 LFERADRDGIDWRDLGDRETQLFREDMTALRVLPPHDYVAATETISEVVELVEKMLASGAAYVVDDaqypDVYYRADATT 168
Cdd:PRK14534 83 VVKAARERGLTVYEISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTYFVNG----NVYFDTSCFK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 169 QFGYESGYDRETMLRLFGERGgDPDrPGKSDELDALLWRAE---RPGEPSWPSPFGAGRPGWHVECSAIALTRIGSGLDI 245
Cdd:PRK14534 159 SYGQMAGINLNDFKDMSVSRV-EID-KSKRNKSDFVLWFTNskfKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKSTLDI 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039668908 246 QGGGSDLIFPHHEFSAAHAESVTGeRRFARHYVHAGMIGWDGHKMSKSRGNLVLVSRLRAQGVDPSAVRLGLFAGHYRS 324
Cdd:PRK14534 237 HLGGVDHIGVHHINEIAIAECYLN-KKWCDMFVHGEFLIMEYEKMSKSNNNFITIKDLEDQGFSPLDFRYFCLTAHYRT 314
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
40-114 |
3.36e-07 |
|
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: 49.40 E-value: 3.36e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039668908 40 MYVCGITPYDATHLGHAATYLTFDLVHRLWLDAGHTVHYVQNVTDVDDPLFERADRDGIDWRDLGDRETQLFRED 114
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKED 75
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
226-293 |
5.27e-05 |
|
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: 42.85 E-value: 5.27e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039668908 226 GWHVECSAIALTRIGSGLDIQGGGSDLIFpHHEFSAAHAESVTGERRfaRHYVHAGMI-GWDGHKMSKS 293
Cdd:cd00802 77 EYMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKAGGPAR--PFGLTFGRVmGADGTKMSKS 142
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
249-328 |
2.01e-04 |
|
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: 43.18 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 249 GSDLIFPHHEFSAAHAESVTGERRFARHYVHAGMIGWDGHKMSKSRGNLVLVSR-LRAQGVDpsAVRLGLFAG-HYRSDR 326
Cdd:cd00668 233 GKDILRGWANFWITMLVALFGEIPPKNLLVHGFVLDEGGQKMSKSKGNVIDPSDvVEKYGAD--ALRYYLTSLaPYGDDI 310
|
..
gi 1039668908 327 FW 328
Cdd:cd00668 311 RL 312
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
249-327 |
5.76e-04 |
|
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) catalytic core domain. This 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. ValRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 185677 [Multi-domain] Cd Length: 382 Bit Score: 41.85 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 249 GSDLIFphheFSAAH----AESVTGERRFARHYVHAGMIGWDGHKMSKSRGNLV-LVSRLRAQGVDpsAVRLGLFAGHYR 323
Cdd:cd00817 303 GHDIIF----FWVARmimrGLKLTGKLPFKEVYLHGLVRDEDGRKMSKSLGNVIdPLDVIDGYGAD--ALRFTLASAATQ 376
|
....
gi 1039668908 324 SDRF 327
Cdd:cd00817 377 GRDI 380
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
249-321 |
6.51e-04 |
|
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase and is particularly closely related to the isoleucyl tRNA synthetase. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273070 [Multi-domain] Cd Length: 861 Bit Score: 41.97 E-value: 6.51e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039668908 249 GSDLIFphheFSAAH----AESVTGERRFARHYVHaGMI-GWDGHKMSKSRGNLVL-VSRLRAQGVDpsAVRLGLFAGH 321
Cdd:TIGR00422 485 GYDIIF----FWVARmifrSLALTGQVPFKEVYIH-GLVrDEQGRKMSKSLGNVIDpLDVIEKYGAD--ALRFTLASLV 556
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
243-328 |
2.66e-03 |
|
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: 39.54 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 243 LDIQGGGSDLIFPHHEFS-----AAHAESVTGERRFARhYVHAGMIGWDGHKMSKSRGNLVLVSRLRAQ-GVDpsAVRLG 316
Cdd:cd00812 225 VDIYIGGKEHAPNHLLYSrfnhkALFDEGLVTDEPPKG-LIVQGMVLLEGEKMSKSKGNVVTPDEAIKKyGAD--AARLY 301
|
90
....*....|...
gi 1039668908 317 L-FAGHYRSDRFW 328
Cdd:cd00812 302 IlFAAPPDADFDW 314
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
275-340 |
6.35e-03 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 39.02 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668908 275 RHYVHAG-------MI-GW----DGHKMSKSRGNLvlvsrlraqgVDPSAVrlglfAGHYRSD--RFWSdavldeANARL 340
Cdd:PRK13208 507 RAYLLTGklpwkniMIsGMvldpDGKKMSKSKGNV----------VTPEEL-----LEKYGADavRYWA------ASARL 565
|
|
| |
