|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
27-315 |
2.08e-156 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 452.95 E-value: 2.08e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 27 WQRPQGQD---TGVQVHNSLTGRKEPLIVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILTRVFGCNVVMAMSI 103
Cdd:PTZ00399 27 WKKPSKEGkylTGLKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEDYFGYDVFYVMNI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 104 TDVDDKIIKRANEMNVTPAS-LASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYStATGSVYFDL 182
Cdd:PTZ00399 107 TDIDDKIIKRAREEKLSIFLeLARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYE-SNGSVYFDV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 183 HA-RGDK--YGKLVNTVPSATAEPGD---------SDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVF 250
Cdd:PTZ00399 186 EAfRKAGhvYPKLEPESVADEDRIAEgegalgkvsGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNIL 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26334827 251 GSHLDIHTGGIDLAFPHHENEIAQSEVFHQCQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKD 315
Cdd:PTZ00399 266 GDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKG--LKMSKSLKNFITIRQ 328
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
38-315 |
1.61e-142 |
|
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: 411.03 E-value: 1.61e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 38 QVHNSLTGRKEPLIVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILTRVfGCNVVMAMSITDVDDKIIKRANEM 117
Cdd:COG0215 3 KLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYL-GYKVTYVRNITDVDDKIIKRAAEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 118 NVTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYsTATGSVYFDLhARGDKYGKLVNTVP 197
Cdd:COG0215 82 GESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAY-EADGDVYFDV-RSFPDYGKLSGRNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 198 -----SATAEPgDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEI 272
Cdd:COG0215 160 ddlraGARVEV-DEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEI 238
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 26334827 273 AQSEVFHqCQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKD 315
Cdd:COG0215 239 AQSEAAT-GKPFARYWMHNGFLTVNG--EKMSKSLGNFFTVRD 278
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
58-315 |
3.74e-126 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 363.23 E-value: 3.74e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 58 VSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEEFKQDMA 137
Cdd:pfam01406 10 VTMYVCGPTVYDYSHIGHARSAVAFDVLRRYL-QALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFIEAYTKDMD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 138 ALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYFDLHArGDKYGKL----VNTVPSATAEPGDSDKRHSSD 213
Cdd:pfam01406 89 ALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVYFDVSS-FPDYGKLsgqnLEQLEAGARGEVSEGKRDPLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 214 FALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHQcQQWGNYFLHSGH 293
Cdd:pfam01406 168 FALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFD-KQLANYWLHNGH 246
|
250 260
....*....|....*....|..
gi 26334827 294 LHVKGteEKMSKSLKNYITIKD 315
Cdd:pfam01406 247 VMIDG--EKMSKSLGNFFTIRD 266
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
39-315 |
6.81e-123 |
|
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: 360.93 E-value: 6.81e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 39 VHNSLTGRKEPLIVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMN 118
Cdd:TIGR00435 3 LYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYL-RYLGYKVQYVQNITDIDDKIIKRARENG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 119 VTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYFDLHARgDKYGKLVNTVPS 198
Cdd:TIGR00435 82 ESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVYFDVSKF-KDYGKLSKQDLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 199 -----ATAEPgDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIA 273
Cdd:TIGR00435 161 qleagARVDV-DEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 26334827 274 QSEVFHQcQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKD 315
Cdd:TIGR00435 240 QSEAAFG-KQLAKYWMHNGFLMIDN--EKMSKSLGNFFTVRD 278
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
38-315 |
3.70e-96 |
|
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: 283.70 E-value: 3.70e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 38 QVHNSLTGRKEPLIVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEM 117
Cdd:cd00672 1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYL-EDLGYKVRYVQNITDIDDKIIKRAREE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 118 NVTPASLASLFEEEFKQDMAALKVLPPTVYLRVtenipqiiafiegiiahghaystatgsvyfdlhargdkygklvntvp 197
Cdd:cd00672 80 GLSWKEVADYYTKEFFEDMKALNVLPPDVVPRV----------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 198 sataepgdsdkrhssdfalwkaakpqevfwaspwgdgrpgWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEV 277
Cdd:cd00672 113 ----------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQSEA 152
|
250 260 270
....*....|....*....|....*....|....*...
gi 26334827 278 FHQCqQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKD 315
Cdd:cd00672 153 ATGK-PFARYWLHTGHLTIDG--EKMSKSLGNFITVRD 187
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
27-315 |
2.08e-156 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 452.95 E-value: 2.08e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 27 WQRPQGQD---TGVQVHNSLTGRKEPLIVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILTRVFGCNVVMAMSI 103
Cdd:PTZ00399 27 WKKPSKEGkylTGLKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEDYFGYDVFYVMNI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 104 TDVDDKIIKRANEMNVTPAS-LASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYStATGSVYFDL 182
Cdd:PTZ00399 107 TDIDDKIIKRAREEKLSIFLeLARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYE-SNGSVYFDV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 183 HA-RGDK--YGKLVNTVPSATAEPGD---------SDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVF 250
Cdd:PTZ00399 186 EAfRKAGhvYPKLEPESVADEDRIAEgegalgkvsGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNIL 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26334827 251 GSHLDIHTGGIDLAFPHHENEIAQSEVFHQCQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKD 315
Cdd:PTZ00399 266 GDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKG--LKMSKSLKNFITIRQ 328
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
38-315 |
1.61e-142 |
|
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: 411.03 E-value: 1.61e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 38 QVHNSLTGRKEPLIVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILTRVfGCNVVMAMSITDVDDKIIKRANEM 117
Cdd:COG0215 3 KLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYL-GYKVTYVRNITDVDDKIIKRAAEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 118 NVTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYsTATGSVYFDLhARGDKYGKLVNTVP 197
Cdd:COG0215 82 GESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAY-EADGDVYFDV-RSFPDYGKLSGRNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 198 -----SATAEPgDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEI 272
Cdd:COG0215 160 ddlraGARVEV-DEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEI 238
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 26334827 273 AQSEVFHqCQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKD 315
Cdd:COG0215 239 AQSEAAT-GKPFARYWMHNGFLTVNG--EKMSKSLGNFFTVRD 278
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
58-315 |
3.74e-126 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 363.23 E-value: 3.74e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 58 VSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEEFKQDMA 137
Cdd:pfam01406 10 VTMYVCGPTVYDYSHIGHARSAVAFDVLRRYL-QALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFIEAYTKDMD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 138 ALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYFDLHArGDKYGKL----VNTVPSATAEPGDSDKRHSSD 213
Cdd:pfam01406 89 ALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVYFDVSS-FPDYGKLsgqnLEQLEAGARGEVSEGKRDPLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 214 FALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHQcQQWGNYFLHSGH 293
Cdd:pfam01406 168 FALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFD-KQLANYWLHNGH 246
|
250 260
....*....|....*....|..
gi 26334827 294 LHVKGteEKMSKSLKNYITIKD 315
Cdd:pfam01406 247 VMIDG--EKMSKSLGNFFTIRD 266
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
39-315 |
6.81e-123 |
|
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: 360.93 E-value: 6.81e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 39 VHNSLTGRKEPLIVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMN 118
Cdd:TIGR00435 3 LYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYL-RYLGYKVQYVQNITDIDDKIIKRARENG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 119 VTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYFDLHARgDKYGKLVNTVPS 198
Cdd:TIGR00435 82 ESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVYFDVSKF-KDYGKLSKQDLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 199 -----ATAEPgDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIA 273
Cdd:TIGR00435 161 qleagARVDV-DEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 26334827 274 QSEVFHQcQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKD 315
Cdd:TIGR00435 240 QSEAAFG-KQLAKYWMHNGFLMIDN--EKMSKSLGNFFTVRD 278
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
38-315 |
3.70e-96 |
|
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: 283.70 E-value: 3.70e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 38 QVHNSLTGRKEPLIVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEM 117
Cdd:cd00672 1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYL-EDLGYKVRYVQNITDIDDKIIKRAREE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 118 NVTPASLASLFEEEFKQDMAALKVLPPTVYLRVtenipqiiafiegiiahghaystatgsvyfdlhargdkygklvntvp 197
Cdd:cd00672 80 GLSWKEVADYYTKEFFEDMKALNVLPPDVVPRV----------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 198 sataepgdsdkrhssdfalwkaakpqevfwaspwgdgrpgWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEV 277
Cdd:cd00672 113 ----------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQSEA 152
|
250 260 270
....*....|....*....|....*....|....*...
gi 26334827 278 FHQCqQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKD 315
Cdd:cd00672 153 ATGK-PFARYWLHTGHLTIDG--EKMSKSLGNFITVRD 187
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
30-314 |
2.39e-84 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 265.26 E-value: 2.39e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 30 PQGQDTGVQVHNSLTGRKEPLIVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDK 109
Cdd:PLN02946 53 PASRGRELHLYNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYL-KHLGYEVRYVRNFTDVDDK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 110 IIKRANEMNVTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTAtGSVYFDLHaRGDKY 189
Cdd:PLN02946 132 IIARANELGEDPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVD-GDVYFSVD-KFPEY 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 190 GKLV------NTVPSATAEpgDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDL 263
Cdd:PLN02946 210 GKLSgrkledNRAGERVAV--DSRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDL 287
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 26334827 264 AFPHHENEIAQSEVfHQCQQWGNYFLHSGHLHVKgtEEKMSKSLKNYITIK 314
Cdd:PLN02946 288 VFPHHENEIAQSCA-ACCDSNISYWIHNGFVTVD--SEKMSKSLGNFFTIR 335
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
39-315 |
4.87e-73 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 238.85 E-value: 4.87e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 39 VHNSLTGRKEPLIVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMN 118
Cdd:PRK14535 230 IYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWL-RECGYPLTYVRNITDIDDKIIARAAENG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 119 VTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYF---DLHARGDKYGKLVNT 195
Cdd:PRK14535 309 ETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVYYavrEFAAYGQLSGKSLDD 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 196 VPSATAEPGDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQS 275
Cdd:PRK14535 389 LRAGERVEVDGFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIAQS 468
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 26334827 276 --EVFHQCQQWG-------------NYFLHSGHLHVKGteEKMSKSLKNYITIKD 315
Cdd:PRK14535 469 vgATGHTCGHHHaqthhgqsiashvKYWLHNGFIRVDG--EKMSKSLGNFFTIRE 521
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
26-334 |
3.49e-68 |
|
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: 219.21 E-value: 3.49e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 26 SWQRPQ-----GQDTGVQVHNSLTGRKEPliVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMA 100
Cdd:TIGR03447 2 SWPAPAvpalpGTGPPLRLFDTADGQVRP--VEPGPEAGMYVCGITPYDATHLGHAATYLTFDLVNRVW-RDAGHRVHYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 101 MSITDVDDKIIKRANEMNVTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAY---STATGS 177
Cdd:TIGR03447 79 QNVTDVDDPLFERAERDGVDWRELGTSQIDLFREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYiveGPEYPD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 178 VYFDLHArGDKYGKLVNTVPSATAE--------PGDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEV 249
Cdd:TIGR03447 159 VYFSIDA-TEQFGYESGYDRATMLElfaerggdPDRPGKRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 250 FGSHLDIHTGGIDLAFPHHENEIAQSEVFHQCQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIkdsAGLQAVGAEPPGL 329
Cdd:TIGR03447 238 LGAGFDIQGGGSDLIFPHHEFSAAHAEAATGVRRMARHYVHAGMIGLDG--EKMSKSLGNLVFV---SKLRAAGVDPAAI 312
|
....*
gi 26334827 330 LFALL 334
Cdd:TIGR03447 313 RLGLL 317
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
52-334 |
4.19e-66 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 212.87 E-value: 4.19e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 52 VARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEE 131
Cdd:PRK12418 4 VAPGGTATMYVCGITPYDATHLGHAATYLAFDLVNRVW-RDAGHDVHYVQNVTDVDDPLLERAARDGVDWRDLAEREIAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 132 FKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAY---STATGSVYFDLHARGDkYGKLVNTVPSATAE------ 202
Cdd:PRK12418 83 FREDMEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYvvdDEEYPDVYFSVDATPQ-FGYESGYDRATMLElfaerg 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 203 --PGDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHQ 280
Cdd:PRK12418 162 gdPDRPGKRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAHAEAATG 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 26334827 281 CQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIkdsAGLQAVGAEPPGLLFALL 334
Cdd:PRK12418 242 ERRFARHYVHAGMIGLDG--EKMSKSRGNLVFV---SRLRAAGVDPAAIRLALL 290
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
37-334 |
9.01e-63 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 207.08 E-value: 9.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 37 VQVHNSLTGRKEPLIVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDV---------- 106
Cdd:PRK14536 3 LRLYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTL-HFLGYRVTHVMNITDVghltddadsg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 107 DDKIIKRANEMNVTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYsTATGSVYFDLHARG 186
Cdd:PRK14536 82 EDKMVKSAQEHGKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTY-CAGGNVYFDIRTFP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 187 DkYGKLVNT----VPSATAEPGDSDKRHSSDFALW---KAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTG 259
Cdd:PRK14536 161 S-YGSLASAavedLQAGARIEHDTNKRNPHDFVLWftrSKFENHALTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIG 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26334827 260 GIDLAFPHHENEIAQSEVFhQCQQWGNYFLHSGHLHVKgtEEKMSKSLKNYITIKDsagLQAVGAEPPGLLFALL 334
Cdd:PRK14536 240 GVDHIRVHHTNEIAQCEAA-TGKPWVRYWLHHEFLLMN--KGKMSKSAGQFLTLSS---LQEKGFQPLDYRFFLL 308
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
52-315 |
3.70e-52 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 178.89 E-value: 3.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 52 VARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDV----------DDKIIKRANEMNVTP 121
Cdd:PRK14534 16 LKNFSDVKVYACGPTVYNYAHIGNFRTYIFEDLLIKSL-RLLKYNVNYAMNITDIghltgdfddgEDKVVKAARERGLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 122 ASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYsTATGSVYFDLhARGDKYGKL----VNTVP 197
Cdd:PRK14534 95 YEISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTY-FVNGNVYFDT-SCFKSYGQMaginLNDFK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 198 SATAEPGDSD--KRHSSDFALW---KAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEI 272
Cdd:PRK14534 173 DMSVSRVEIDksKRNKSDFVLWftnSKFKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKSTLDIHLGGVDHIGVHHINEI 252
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 26334827 273 AQSEVFHQcQQWGNYFLHSGHLHVKgtEEKMSKSLKNYITIKD 315
Cdd:PRK14534 253 AIAECYLN-KKWCDMFVHGEFLIME--YEKMSKSNNNFITIKD 292
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
65-141 |
5.41e-06 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 47.95 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334827 65 PTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMamsITDVDD---KIIKRANEMNVTPASLASLFEEEFKQDMAALKV 141
Cdd:PRK11893 10 YYPNGKPHIGHAYTTLAADVLARFK-RLRGYDVFF---LTGTDEhgqKIQRKAEEAGISPQELADRNSAAFKRLWEALNI 85
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
61-135 |
1.05e-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: 41.70 E-value: 1.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26334827 61 YSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEEFKQD 135
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAY-RKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKED 75
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
237-307 |
2.77e-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: 40.54 E-value: 2.77e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26334827 237 GWHIECSTMASEVFGSHLDIHTGGIDLAFpHHENEIAQSEVFHqcQQWGNYFLHSGHLHVKGTeEKMSKSL 307
Cdd:cd00802 77 EYMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKAG--GPARPFGLTFGRVMGADG-TKMSKSK 143
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
72-141 |
5.08e-03 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 38.43 E-value: 5.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26334827 72 HLGHACSYVRFDIIRRILtRVFGCNVVMamsITDVDD---KIIKRANEMNVTPASLASLFEEEFKQDMAALKV 141
Cdd:pfam09334 15 HLGHLYSYIPADIFARYL-RLRGYDVLF---VCGTDEhgtPIELKAEKEGITPEELVDRYHEIHREDFKKFNI 83
|
|
|