|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
8-430 |
8.11e-138 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 409.42 E-value: 8.11e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 8 LASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYStATGSVYFDLHA-RGDK--YGKLVNTVPSAT 84
Cdd:PTZ00399 128 LARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYE-SNGSVYFDVEAfRKAGhvYPKLEPESVADE 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 85 AEPGD---------SDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENE 155
Cdd:PTZ00399 207 DRIAEgegalgkvsGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDLKFPHHDNE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 156 IAQSEVFHQCQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHL 235
Cdd:PTZ00399 287 LAQSEAYFDKHQWVNYFLHSGHLHIKG--LKMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSDESMDEAIEK 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 236 LLGLASFVEDARAYVKGQLTCGPVEEDV----LWERLTSTKKAVKAALANDFDTPRAVNTILDLVHHANRQLRAVSKeas 311
Cdd:PTZ00399 365 DKVFFNFFANVKIKLRESELTSPQKWTQhdfeLNELFEETKSAVHAALLDNFDTPEALQALQKLISATNTYLNSGEQ--- 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 312 gPRSPTVFgAIISYVEQFFETVGISLANRQC-VSGDSSTV-TLRCVVDELVRFRLKVRQYAldtpgAAGEARKRQLQERQ 389
Cdd:PTZ00399 442 -PSAPLLR-SVAQYVTKILSIFGLVEGSDGLgSQGQNSTSeNFKPLLEALLRFRDEVRDAA-----KAEMKLISLDKKKK 514
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1907191153 390 PLLEACDTLR-QDLVTHGINVKDRGSAASTWELLDP----RTRHQK 430
Cdd:PTZ00399 515 QLLQLCDKLRdEWLPNLGIRIEDKPDGPSVWKLDDKeelqREKEEK 560
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
2-421 |
8.27e-133 |
|
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: 390.23 E-value: 8.27e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 2 NVTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYsTATGSVYFDLhARGDKYGKLVNTVP 81
Cdd:COG0215 82 GESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAY-EADGDVYFDV-RSFPDYGKLSGRNL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 82 -----SATAEPgDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEI 156
Cdd:COG0215 160 ddlraGARVEV-DEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEI 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 157 AQSEVFHqCQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHLL 236
Cdd:COG0215 239 AQSEAAT-GKPFARYWMHNGFLTVNG--EKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKAL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 237 LGLASFVEDARAYVKgqltcgpvEEDVLWERLTSTKKAVKAALANDFDTPRAVNTILDLVHHANRQLravskeaSGPRSP 316
Cdd:COG0215 316 ERLYNALRRLEEALG--------AADSSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKAL-------DEGEDK 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 317 TVFGAIISYVEQFFETVGISLANRQCVSGDSSTVtlrcVVDELVRFRLKVRQyaldtpgaagEARKRQLQERqplleAcD 396
Cdd:COG0215 381 AALAALAALLRALGGVLGLLLLEPEAWQGAAEDE----LLDALIEALIEERA----------EARKAKDFAR-----A-D 440
|
410 420
....*....|....*....|....*
gi 1907191153 397 TLRQDLVTHGINVKDrGSAASTWEL 421
Cdd:COG0215 441 RIRDELAALGIVLED-TPDGTTWRR 464
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
8-233 |
2.55e-103 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 308.91 E-value: 2.55e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 8 LASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYFDLHArGDKYGKL----VNTVPSA 83
Cdd:pfam01406 75 LAARFIEAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVYFDVSS-FPDYGKLsgqnLEQLEAG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 84 TAEPGDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFH 163
Cdd:pfam01406 154 ARGEVSEGKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAF 233
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 164 QcQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAK 233
Cdd:pfam01406 234 D-KQLANYWLHNGHVMIDG--EKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAK 300
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
2-300 |
4.66e-102 |
|
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: 311.62 E-value: 4.66e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 2 NVTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYFDLHARgDKYGKLVNTVP 81
Cdd:TIGR00435 81 GESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVYFDVSKF-KDYGKLSKQDL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 82 S-----ATAEPgDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEI 156
Cdd:TIGR00435 160 DqleagARVDV-DEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEI 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 157 AQSEVFHQcQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAK--- 233
Cdd:TIGR00435 239 AQSEAAFG-KQLAKYWMHNGFLMIDN--EKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKnal 315
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907191153 234 -HLLLGLASFVEDArAYVKGQ-LTCGPVEEDVlwerltstKKAVKAALANDFDTPRAVNTILDLVHHAN 300
Cdd:TIGR00435 316 eRLYKALRVLDTSL-AYSGNQsLNKFPDEKEF--------EARFVEAMDDDLNTANALAVLFELAKSIN 375
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
1-225 |
1.22e-61 |
|
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: 198.96 E-value: 1.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 1 MNVTPASLASLFEEEFKQDMAALKVLPPTVYLRVtenipqiiafiegiiahghaystatgsvyfdlhargdkygklvntv 80
Cdd:cd00672 79 EGLSWKEVADYYTKEFFEDMKALNVLPPDVVPRV---------------------------------------------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 81 psataepgdsdkrhssdfalwkaakpqevfwaspwgdgrpgWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSE 160
Cdd:cd00672 113 -----------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQSE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907191153 161 VFHQCqQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYS 225
Cdd:cd00672 152 AATGK-PFARYWLHTGHLTIDG--EKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
8-430 |
8.11e-138 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 409.42 E-value: 8.11e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 8 LASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYStATGSVYFDLHA-RGDK--YGKLVNTVPSAT 84
Cdd:PTZ00399 128 LARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYE-SNGSVYFDVEAfRKAGhvYPKLEPESVADE 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 85 AEPGD---------SDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENE 155
Cdd:PTZ00399 207 DRIAEgegalgkvsGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDLKFPHHDNE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 156 IAQSEVFHQCQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHL 235
Cdd:PTZ00399 287 LAQSEAYFDKHQWVNYFLHSGHLHIKG--LKMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSDESMDEAIEK 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 236 LLGLASFVEDARAYVKGQLTCGPVEEDV----LWERLTSTKKAVKAALANDFDTPRAVNTILDLVHHANRQLRAVSKeas 311
Cdd:PTZ00399 365 DKVFFNFFANVKIKLRESELTSPQKWTQhdfeLNELFEETKSAVHAALLDNFDTPEALQALQKLISATNTYLNSGEQ--- 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 312 gPRSPTVFgAIISYVEQFFETVGISLANRQC-VSGDSSTV-TLRCVVDELVRFRLKVRQYAldtpgAAGEARKRQLQERQ 389
Cdd:PTZ00399 442 -PSAPLLR-SVAQYVTKILSIFGLVEGSDGLgSQGQNSTSeNFKPLLEALLRFRDEVRDAA-----KAEMKLISLDKKKK 514
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1907191153 390 PLLEACDTLR-QDLVTHGINVKDRGSAASTWELLDP----RTRHQK 430
Cdd:PTZ00399 515 QLLQLCDKLRdEWLPNLGIRIEDKPDGPSVWKLDDKeelqREKEEK 560
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
2-421 |
8.27e-133 |
|
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: 390.23 E-value: 8.27e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 2 NVTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYsTATGSVYFDLhARGDKYGKLVNTVP 81
Cdd:COG0215 82 GESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAY-EADGDVYFDV-RSFPDYGKLSGRNL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 82 -----SATAEPgDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEI 156
Cdd:COG0215 160 ddlraGARVEV-DEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEI 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 157 AQSEVFHqCQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHLL 236
Cdd:COG0215 239 AQSEAAT-GKPFARYWMHNGFLTVNG--EKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKAL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 237 LGLASFVEDARAYVKgqltcgpvEEDVLWERLTSTKKAVKAALANDFDTPRAVNTILDLVHHANRQLravskeaSGPRSP 316
Cdd:COG0215 316 ERLYNALRRLEEALG--------AADSSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKAL-------DEGEDK 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 317 TVFGAIISYVEQFFETVGISLANRQCVSGDSSTVtlrcVVDELVRFRLKVRQyaldtpgaagEARKRQLQERqplleAcD 396
Cdd:COG0215 381 AALAALAALLRALGGVLGLLLLEPEAWQGAAEDE----LLDALIEALIEERA----------EARKAKDFAR-----A-D 440
|
410 420
....*....|....*....|....*
gi 1907191153 397 TLRQDLVTHGINVKDrGSAASTWEL 421
Cdd:COG0215 441 RIRDELAALGIVLED-TPDGTTWRR 464
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
8-233 |
2.55e-103 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 308.91 E-value: 2.55e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 8 LASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYFDLHArGDKYGKL----VNTVPSA 83
Cdd:pfam01406 75 LAARFIEAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVYFDVSS-FPDYGKLsgqnLEQLEAG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 84 TAEPGDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFH 163
Cdd:pfam01406 154 ARGEVSEGKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAF 233
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 164 QcQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAK 233
Cdd:pfam01406 234 D-KQLANYWLHNGHVMIDG--EKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAK 300
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
2-300 |
4.66e-102 |
|
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: 311.62 E-value: 4.66e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 2 NVTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYFDLHARgDKYGKLVNTVP 81
Cdd:TIGR00435 81 GESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVYFDVSKF-KDYGKLSKQDL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 82 S-----ATAEPgDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEI 156
Cdd:TIGR00435 160 DqleagARVDV-DEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEI 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 157 AQSEVFHQcQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAK--- 233
Cdd:TIGR00435 239 AQSEAAFG-KQLAKYWMHNGFLMIDN--EKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKnal 315
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907191153 234 -HLLLGLASFVEDArAYVKGQ-LTCGPVEEDVlwerltstKKAVKAALANDFDTPRAVNTILDLVHHAN 300
Cdd:TIGR00435 316 eRLYKALRVLDTSL-AYSGNQsLNKFPDEKEF--------EARFVEAMDDDLNTANALAVLFELAKSIN 375
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
5-232 |
5.33e-67 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 223.27 E-value: 5.33e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 5 PASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTAtGSVYFDLHaRGDKYGKLV------N 78
Cdd:PLN02946 143 PISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVD-GDVYFSVD-KFPEYGKLSgrkledN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 79 TVPSATAEpgDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQ 158
Cdd:PLN02946 221 RAGERVAV--DSRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLVFPHHENEIAQ 298
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907191153 159 SEVfHQCQQWGNYFLHSGHLHVKgtEEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEA 232
Cdd:PLN02946 299 SCA-ACCDSNISYWIHNGFVTVD--SEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDVQLESA 369
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
4-319 |
4.14e-66 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 224.21 E-value: 4.14e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 4 TPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYF---DLHARGDKYGKLVNTV 80
Cdd:PRK14535 310 TIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVYYavrEFAAYGQLSGKSLDDL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 81 PSATAEPGDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQS- 159
Cdd:PRK14535 390 RAGERVEVDGFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIAQSv 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 160 -EVFHQCQQWG-------------NYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYS 225
Cdd:PRK14535 470 gATGHTCGHHHaqthhgqsiashvKYWLHNGFIRVDG--EKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNYS 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 226 DSTLVEAKHLLLGLASFVEDArayvkgqltcgPVEEDVLWERLTSTKKAVKAALANDFDTPRAVNTILDLVHHANR---- 301
Cdd:PRK14535 548 DAHLDDAKGALTRLYTTLKNT-----------PAAEFMLSENVNDYTRRFYAAMNDDFGTVEAVAVLFELAGEVNKtnda 616
|
330 340
....*....|....*....|...
gi 1907191153 302 QLRAVSKEASG-----PRSPTVF 319
Cdd:PRK14535 617 QLAGCLKALGGiigllQRDPTEF 639
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
1-225 |
1.22e-61 |
|
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: 198.96 E-value: 1.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 1 MNVTPASLASLFEEEFKQDMAALKVLPPTVYLRVtenipqiiafiegiiahghaystatgsvyfdlhargdkygklvntv 80
Cdd:cd00672 79 EGLSWKEVADYYTKEFFEDMKALNVLPPDVVPRV---------------------------------------------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 81 psataepgdsdkrhssdfalwkaakpqevfwaspwgdgrpgWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSE 160
Cdd:cd00672 113 -----------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQSE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907191153 161 VFHQCqQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYS 225
Cdd:cd00672 152 AATGK-PFARYWLHTGHLTIDG--EKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
16-292 |
1.27e-53 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 183.59 E-value: 1.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 16 FKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAY---STATGSVYFDLHARGDkYGKLVNTVPSATAE------ 86
Cdd:PRK12418 83 FREDMEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYvvdDEEYPDVYFSVDATPQ-FGYESGYDRATMLElfaerg 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 87 --PGDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHQ 164
Cdd:PRK12418 162 gdPDRPGKRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAHAEAATG 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 165 CQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKT-FSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHLLlglasfv 243
Cdd:PRK12418 242 ERRFARHYVHAGMIGLDG--EKMSKSRGNLVFVSRLRAAgVDPAAIRLALLAGHYRADREWTDAVLAEAEARL------- 312
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1907191153 244 EDARAYVKgqLTCGPVEEDVLwerltstkKAVKAALANDFDTPRAVNTI 292
Cdd:PRK12418 313 ARWRAAAA--LPAGPDAADVV--------ARVRAALADDLDTPGALAAV 351
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
16-288 |
2.70e-51 |
|
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: 177.99 E-value: 2.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 16 FKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAY---STATGSVYFDLHArGDKYGKLVN----TVPSATAE-- 86
Cdd:TIGR03447 110 FREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYiveGPEYPDVYFSIDA-TEQFGYESGydraTMLELFAErg 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 87 --PGDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHQ 164
Cdd:TIGR03447 189 gdPDRPGKRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSDLIFPHHEFSAAHAEAATG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 165 CQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKT-FSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHLLlglasfv 243
Cdd:TIGR03447 269 VRRMARHYVHAGMIGLDG--EKMSKSLGNLVFVSKLRAAgVDPAAIRLGLLAGHYRQDRDWTDAVLAEAEARL------- 339
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907191153 244 edARAYVKGQLTCGPVEEDVLwerltstkKAVKAALANDFDTPRA 288
Cdd:TIGR03447 340 --ARWRAALALPDAPDATDLI--------ARLRQHLANDLDTPAA 374
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
8-296 |
8.59e-50 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 175.88 E-value: 8.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 8 LASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYsTATGSVYFDLHARGDkYGKLVNT----VPSA 83
Cdd:PRK14536 99 IAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTY-CAGGNVYFDIRTFPS-YGSLASAavedLQAG 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 84 TAEPGDSDKRHSSDFALW---KAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSE 160
Cdd:PRK14536 177 ARIEHDTNKRNPHDFVLWftrSKFENHALTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIGGVDHIRVHHTNEIAQCE 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 161 VFhQCQQWGNYFLHSGHLHVKgtEEKMSKSLKNYITIKDFL-KTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAK----HL 235
Cdd:PRK14536 257 AA-TGKPWVRYWLHHEFLLMN--KGKMSKSAGQFLTLSSLQeKGFQPLDYRFFLLGGHYRSQLAFSWEALKTAKaarrSL 333
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907191153 236 LLGLASFVEDARAY---VKGQLTcgpveeDVLWERLTSTKKA--------VKAALANDFDTPRAVNTILDLV 296
Cdd:PRK14536 334 VRRVARVVDAARATtgsVRGTLA------ECAAERVAESRASesellltdFRAALEDDFSTPKALSELQKLV 399
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
3-233 |
2.59e-40 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 150.00 E-value: 2.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 3 VTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYsTATGSVYFDLhARGDKYGKL----VN 78
Cdd:PRK14534 92 LTVYEISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTY-FVNGNVYFDT-SCFKSYGQMaginLN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 79 TVPSATAEPGDSD--KRHSSDFALW---KAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHE 153
Cdd:PRK14534 170 DFKDMSVSRVEIDksKRNKSDFVLWftnSKFKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKSTLDIHLGGVDHIGVHHI 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 154 NEIAQSEVFHQcQQWGNYFLHSGHLHVKgtEEKMSKSLKNYITIKDF-LKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEA 232
Cdd:PRK14534 250 NEIAIAECYLN-KKWCDMFVHGEFLIME--YEKMSKSNNNFITIKDLeDQGFSPLDFRYFCLTAHYRTQLKFTFNNLKAC 326
|
.
gi 1907191153 233 K 233
Cdd:PRK14534 327 K 327
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
175-301 |
5.19e-09 |
|
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439913 [Multi-domain] Cd Length: 544 Bit Score: 58.20 E-value: 5.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 175 SGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSA-IEYSDSTLVE-------AK--HLLLGLASFVE 244
Cdd:COG0143 318 HGFLTVEG--EKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVPFGQdGDFSWEDFVArvnsdlaNDlgNLASRTLSMIH 395
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 245 darAYVKGQLTCGPVEEDV---LWERLTSTKKAVKAALANdFDTPRAVNTILDLVHHANR 301
Cdd:COG0143 396 ---KYFDGKVPEPGELTEAdeeLLAEAEAALEEVAEAMEA-FEFRKALEEIMALARAANK 451
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
138-212 |
4.59e-07 |
|
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173906 [Multi-domain] Cd Length: 314 Bit Score: 51.48 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 138 LDIHTGGIDLAFPH-----------HENEIAQSEVFHQcqqwgnyFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSP 206
Cdd:cd00812 225 VDIYIGGKEHAPNHllysrfnhkalFDEGLVTDEPPKG-------LIVQGMVLLEG--EKMSKSKGNVVTPDEAIKKYGA 295
|
....*.
gi 1907191153 207 DVFRLF 212
Cdd:cd00812 296 DAARLY 301
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
186-296 |
1.67e-06 |
|
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439830 [Multi-domain] Cd Length: 931 Bit Score: 50.46 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 186 KMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVE-AKHL---------LLG-LASFVEDARAYVKGQL 254
Cdd:COG0060 603 KMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEILKEvRDVYrrlrntyrfLLAnLDDFDPAEDAVPYEDL 682
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1907191153 255 TcgpvEED--VLwERLTSTKKAVKAALaNDFDTPRAVNTILDLV 296
Cdd:COG0060 683 P----ELDrwIL-SRLNELIKEVTEAY-DNYDFHRAYRALHNFC 720
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
175-227 |
2.19e-06 |
|
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: 49.07 E-value: 2.19e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907191153 175 SGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLrtnyRSAIEYSDS 227
Cdd:cd00814 271 HGYLTVEG--KKMSKSRGNVVDPDDLLERYGADALRYYLL----RERPEGKDS 317
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
175-301 |
5.97e-05 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 45.53 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 175 SGHLHVKGteEKMSKSlKNY-ITIKDFLKTFSPDVFRlFCLRTNYRSAIEYSD-----------STLVeAKhllLG-LAS 241
Cdd:PRK00133 320 HGFLTVEG--AKMSKS-RGTfIWARTYLDHLDPDYLR-YYLAAKLPETIDDLDfnwedfqqrvnSELV-GK---VVnFAS 391
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907191153 242 ----FVEDaraYVKGQLTCGPVEEDvLWERLTSTKKAVKAALaNDFDTPRAVNTILDLVHHANR 301
Cdd:PRK00133 392 rtagFINK---RFDGKLPDALADPE-LLEEFEAAAEKIAEAY-EAREFRKALREIMALADFANK 450
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
175-231 |
1.17e-04 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 44.20 E-value: 1.17e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907191153 175 SGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLR-TNYRSAIEYSDSTLVE 231
Cdd:pfam09334 315 HGYLTYEG--GKMSKSRGNVVWPSEALDRFPPDALRYYLARnRPETKDTDFSWEDFVE 370
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
121-191 |
1.32e-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: 42.08 E-value: 1.32e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907191153 121 GWHIECSTMASEVFGSHLDIHTGGIDLAFpHHENEIAQSEVFHqcQQWGNYFLHSGHLHVKGTeEKMSKSL 191
Cdd:cd00802 77 EYMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKAG--GPARPFGLTFGRVMGADG-TKMSKSK 143
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
171-216 |
1.56e-04 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 43.72 E-value: 1.56e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1907191153 171 YFLHsGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRT 216
Cdd:PRK11893 287 VFAH-GFLTLDG--EKMSKSLGNVIDPFDLVDEYGVDAVRYFLLRE 329
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
185-212 |
2.80e-04 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 43.32 E-value: 2.80e-04
10 20
....*....|....*....|....*...
gi 1907191153 185 EKMSKSLKNYITIKDFLKTFSPDVFRLF 212
Cdd:PRK12300 576 KKMSKSKGNVIPLRKAIEEYGADVVRLY 603
|
|
| DALR_2 |
pfam09190 |
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases. |
274-310 |
1.85e-03 |
|
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases.
Pssm-ID: 462711 [Multi-domain] Cd Length: 63 Bit Score: 36.41 E-value: 1.85e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1907191153 274 AVKAALANDFDTPRAVNTILDLVHHANRQLRAVSKEA 310
Cdd:pfam09190 1 KFIEAMDDDFNTPEALAVLFELAKEINRALKTNDAEA 37
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
186-225 |
2.36e-03 |
|
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.
Pssm-ID: 459685 [Multi-domain] Cd Length: 602 Bit Score: 40.09 E-value: 2.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1907191153 186 KMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYS 225
Cdd:pfam00133 563 KMSKSLGNVIDPLDVIDKYGADALRLWLANSDYGRDINLS 602
|
|
| tRNA-synt_1f |
pfam01921 |
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from ... |
185-223 |
5.16e-03 |
|
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from prokaryotes.
Pssm-ID: 396483 Cd Length: 357 Bit Score: 38.78 E-value: 5.16e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1907191153 185 EKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIE 223
Cdd:pfam01921 278 GKMSSSKGNVITPEDWLEYAPPESLRFLMFRTKPKKAKD 316
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
168-214 |
5.19e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 39.28 E-value: 5.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1907191153 168 WGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRlFCL 214
Cdd:PLN02959 702 WPRGFRCNGHLMLNS--EKMSKSTGNFLTLRQAIEEFSADATR-FAL 745
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
185-219 |
5.60e-03 |
|
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases (IleRS) 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. IleRS 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: 173909 [Multi-domain] Cd Length: 338 Bit Score: 38.75 E-value: 5.60e-03
10 20 30
....*....|....*....|....*....|....*
gi 1907191153 185 EKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYR 219
Cdd:cd00818 298 RKMSKSLGNYVDPQEVVDKYGADALRLWVASSDVY 332
|
|
| |
