|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
2-301 |
1.19e-71 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 233.00 E-value: 1.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 2 VFGSQLDIHSGGIDLAFPHHENEIAQCEVFHQCEQWGNYFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFF 81
Cdd:PTZ00399 264 ILGDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKG--LKMSKSLKNFITIRQALSKYTARQIRLL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 82 CLRSSYRSAIDYSDSAMLQAQQLLLGLGSFLEDARAYMKgQLACGSVR-----EAMLWERLSSTKRAVKAALADDFDTPR 156
Cdd:PTZ00399 342 FLLHKWDKPMNYSDESMDEAIEKDKVFFNFFANVKIKLR-ESELTSPQkwtqhDFELNELFEETKSAVHAALLDNFDTPE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 157 VVDAILGLAhhgnGQLRASLKEPEGPRSPAVFgAIISYFEQFFETVGISLANQQYVSGD--GSEATLHGVVDELVRFRQK 234
Cdd:PTZ00399 421 ALQALQKLI----SATNTYLNSGEQPSAPLLR-SVAQYVTKILSIFGLVEGSDGLGSQGqnSTSENFKPLLEALLRFRDE 495
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1206271390 235 VRQFALA-MPEATGDARRQQllerqpLLEACDTLRR-GLTAHGINIKDRSSTTSTWELLD----QRTKDQKSA 301
Cdd:PTZ00399 496 VRDAAKAeMKLISLDKKKKQ------LLQLCDKLRDeWLPNLGIRIEDKPDGPSVWKLDDkeelQREKEEKEA 562
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
3-290 |
1.67e-59 |
|
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: 196.86 E-value: 1.67e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 3 FGSQLDIHSGGIDLAFPHHENEIAQCEVFHqCEQWGNYFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFC 82
Cdd:COG0215 216 LGETFDIHGGGIDLIFPHHENEIAQSEAAT-GKPFARYWMHNGFLTVNG--EKMSKSLGNFFTVRDLLKKYDPEVLRFFL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 83 LRSSYRSAIDYSDSAmlqaqqlllglgsfLEDAR--------AYMKGQLACGSVREAMlwERLSSTKRAVKAALADDFDT 154
Cdd:COG0215 293 LSAHYRSPLDFSEEA--------------LEEAEkalerlynALRRLEEALGAADSSA--EEIEELREEFIAAMDDDFNT 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 155 PRVVDAILGLAHHGNgqlraslKEPEGPRSPAVFGAIISYFEQFFETVGISLANQQYVSGDGSEATLHGVVDELVRFRQK 234
Cdd:COG0215 357 PEALAVLFELVREIN-------KALDEGEDKAALAALAALLRALGGVLGLLLLEPEAWQGAAEDELLDALIEALIEERAE 429
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1206271390 235 VRQ---FALAmpeatgdarrqqllerqplleacDTLRRGLTAHGINIKDRSSTTsTWEL 290
Cdd:COG0215 430 ARKakdFARA-----------------------DRIRDELAALGIVLEDTPDGT-TWRR 464
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
1-94 |
6.18e-51 |
|
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: 166.99 E-value: 6.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 1 MVFGSQLDIHSGGIDLAFPHHENEIAQCEVFHQcEQWGNYFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKTFSPDVFRF 80
Cdd:cd00672 123 KYLGETFDIHGGGVDLIFPHHENEIAQSEAATG-KPFARYWLHTGHLTIDG--EKMSKSLGNFITVRDALKKYDPEVLRL 199
|
90
....*....|....
gi 1206271390 81 FCLRSSYRSAIDYS 94
Cdd:cd00672 200 ALLSSHYRSPLDFS 213
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
3-262 |
1.79e-43 |
|
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: 154.46 E-value: 1.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 3 FGSQLDIHSGGIDLAFPHHENEIAQCEVFHQcEQWGNYFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFC 82
Cdd:TIGR00435 216 LGDQIDIHGGGVDLIFPHHENEIAQSEAAFG-KQLAKYWMHNGFLMIDN--EKMSKSLGNFFTVRDVLKNYDPEILRYFL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 83 LRSSYRSAIDYSDSAMLQAQQLLLGLGSFLEDAR---AYMKGQLACGSVREAMLwerlsstKRAVKAALADDFDTPRVVD 159
Cdd:TIGR00435 293 LSVHYRSPLDFSEELLEAAKNALERLYKALRVLDtslAYSGNQSLNKFPDEKEF-------EARFVEAMDDDLNTANALA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 160 AILGLAHHGNGQlraslkepegPRSPAVFGAIISYFEQFFETVGIslanqqyVSGDGSEATLHGVVDELVRFRQKVRQFA 239
Cdd:TIGR00435 366 VLFELAKSINLT----------FVSKADAALLIEHLIFLESRLGL-------LLGLPSKPVQAGSNDDLGEIEALIEERS 428
|
250 260
....*....|....*....|....*.
gi 1206271390 240 LAMPE---ATGDARRQQLLERQPLLE 262
Cdd:TIGR00435 429 IARKEkdfAKADEIRDELAKKGIVLE 454
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
3-98 |
1.10e-40 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 143.28 E-value: 1.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 3 FGSQLDIHSGGIDLAFPHHENEIAQCEVFHQcEQWGNYFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFC 82
Cdd:pfam01406 204 LGDQIDIHGGGIDLAFPHHENEIAQSEAAFD-KQLANYWLHNGHVMIDG--EKMSKSLGNFFTIRDVLKRYDPEILRYFL 280
|
90
....*....|....*.
gi 1206271390 83 LRSSYRSAIDYSDSAM 98
Cdd:pfam01406 281 LSVHYRSPLDFSEELL 296
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
2-301 |
1.19e-71 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 233.00 E-value: 1.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 2 VFGSQLDIHSGGIDLAFPHHENEIAQCEVFHQCEQWGNYFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFF 81
Cdd:PTZ00399 264 ILGDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKG--LKMSKSLKNFITIRQALSKYTARQIRLL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 82 CLRSSYRSAIDYSDSAMLQAQQLLLGLGSFLEDARAYMKgQLACGSVR-----EAMLWERLSSTKRAVKAALADDFDTPR 156
Cdd:PTZ00399 342 FLLHKWDKPMNYSDESMDEAIEKDKVFFNFFANVKIKLR-ESELTSPQkwtqhDFELNELFEETKSAVHAALLDNFDTPE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 157 VVDAILGLAhhgnGQLRASLKEPEGPRSPAVFgAIISYFEQFFETVGISLANQQYVSGD--GSEATLHGVVDELVRFRQK 234
Cdd:PTZ00399 421 ALQALQKLI----SATNTYLNSGEQPSAPLLR-SVAQYVTKILSIFGLVEGSDGLGSQGqnSTSENFKPLLEALLRFRDE 495
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1206271390 235 VRQFALA-MPEATGDARRQQllerqpLLEACDTLRR-GLTAHGINIKDRSSTTSTWELLD----QRTKDQKSA 301
Cdd:PTZ00399 496 VRDAAKAeMKLISLDKKKKQ------LLQLCDKLRDeWLPNLGIRIEDKPDGPSVWKLDDkeelQREKEEKEA 562
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
3-290 |
1.67e-59 |
|
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: 196.86 E-value: 1.67e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 3 FGSQLDIHSGGIDLAFPHHENEIAQCEVFHqCEQWGNYFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFC 82
Cdd:COG0215 216 LGETFDIHGGGIDLIFPHHENEIAQSEAAT-GKPFARYWMHNGFLTVNG--EKMSKSLGNFFTVRDLLKKYDPEVLRFFL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 83 LRSSYRSAIDYSDSAmlqaqqlllglgsfLEDAR--------AYMKGQLACGSVREAMlwERLSSTKRAVKAALADDFDT 154
Cdd:COG0215 293 LSAHYRSPLDFSEEA--------------LEEAEkalerlynALRRLEEALGAADSSA--EEIEELREEFIAAMDDDFNT 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 155 PRVVDAILGLAHHGNgqlraslKEPEGPRSPAVFGAIISYFEQFFETVGISLANQQYVSGDGSEATLHGVVDELVRFRQK 234
Cdd:COG0215 357 PEALAVLFELVREIN-------KALDEGEDKAALAALAALLRALGGVLGLLLLEPEAWQGAAEDELLDALIEALIEERAE 429
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1206271390 235 VRQ---FALAmpeatgdarrqqllerqplleacDTLRRGLTAHGINIKDRSSTTsTWEL 290
Cdd:COG0215 430 ARKakdFARA-----------------------DRIRDELAALGIVLEDTPDGT-TWRR 464
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
1-94 |
6.18e-51 |
|
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: 166.99 E-value: 6.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 1 MVFGSQLDIHSGGIDLAFPHHENEIAQCEVFHQcEQWGNYFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKTFSPDVFRF 80
Cdd:cd00672 123 KYLGETFDIHGGGVDLIFPHHENEIAQSEAATG-KPFARYWLHTGHLTIDG--EKMSKSLGNFITVRDALKKYDPEVLRL 199
|
90
....*....|....
gi 1206271390 81 FCLRSSYRSAIDYS 94
Cdd:cd00672 200 ALLSSHYRSPLDFS 213
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
3-262 |
1.79e-43 |
|
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: 154.46 E-value: 1.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 3 FGSQLDIHSGGIDLAFPHHENEIAQCEVFHQcEQWGNYFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFC 82
Cdd:TIGR00435 216 LGDQIDIHGGGVDLIFPHHENEIAQSEAAFG-KQLAKYWMHNGFLMIDN--EKMSKSLGNFFTVRDVLKNYDPEILRYFL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 83 LRSSYRSAIDYSDSAMLQAQQLLLGLGSFLEDAR---AYMKGQLACGSVREAMLwerlsstKRAVKAALADDFDTPRVVD 159
Cdd:TIGR00435 293 LSVHYRSPLDFSEELLEAAKNALERLYKALRVLDtslAYSGNQSLNKFPDEKEF-------EARFVEAMDDDLNTANALA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 160 AILGLAHHGNGQlraslkepegPRSPAVFGAIISYFEQFFETVGIslanqqyVSGDGSEATLHGVVDELVRFRQKVRQFA 239
Cdd:TIGR00435 366 VLFELAKSINLT----------FVSKADAALLIEHLIFLESRLGL-------LLGLPSKPVQAGSNDDLGEIEALIEERS 428
|
250 260
....*....|....*....|....*.
gi 1206271390 240 LAMPE---ATGDARRQQLLERQPLLE 262
Cdd:TIGR00435 429 IARKEkdfAKADEIRDELAKKGIVLE 454
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
3-98 |
1.10e-40 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 143.28 E-value: 1.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 3 FGSQLDIHSGGIDLAFPHHENEIAQCEVFHQcEQWGNYFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFC 82
Cdd:pfam01406 204 LGDQIDIHGGGIDLAFPHHENEIAQSEAAFD-KQLANYWLHNGHVMIDG--EKMSKSLGNFFTIRDVLKRYDPEILRYFL 280
|
90
....*....|....*.
gi 1206271390 83 LRSSYRSAIDYSDSAM 98
Cdd:pfam01406 281 LSVHYRSPLDFSEELL 296
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
2-177 |
2.47e-26 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 108.65 E-value: 2.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 2 VFGSQLDIHSGGIDLAFPHHENEIAQ--------CEVFHQCEQWGN-------YFLHSGHLHAKGkeEKMSKSLKNYITI 66
Cdd:PRK14535 442 LFGDTFDIHGGGADLQFPHHENEIAQsvgatghtCGHHHAQTHHGQsiashvkYWLHNGFIRVDG--EKMSKSLGNFFTI 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 67 KDFLKTFSPDVFRFFCLRSSYRSAIDYSDSAMLQAQQLLLGLGSFLEDARAymkgqlacgsvREAMLWERLSSTKRAVKA 146
Cdd:PRK14535 520 REVLKQYDPEVVRFFILRAHYRSPLNYSDAHLDDAKGALTRLYTTLKNTPA-----------AEFMLSENVNDYTRRFYA 588
|
170 180 190
....*....|....*....|....*....|....*
gi 1206271390 147 ALADDFDTPRVVDAILGLAHHGN----GQLRASLK 177
Cdd:PRK14535 589 AMNDDFGTVEAVAVLFELAGEVNktndAQLAGCLK 623
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
4-289 |
3.29e-21 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 93.45 E-value: 3.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 4 GSQLDIHSGGIDLAFPHHENEIAQCEVFhQCEQWGNYFLHSGHL-HAKGkeeKMSKSLKNYITIKDFL-KTFSPDVFRFF 81
Cdd:PRK14536 231 GEQCDIHIGGVDHIRVHHTNEIAQCEAA-TGKPWVRYWLHHEFLlMNKG---KMSKSAGQFLTLSSLQeKGFQPLDYRFF 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 82 CLRSSYRSAIDYSDSAMLQAQQLLLGLGSFLedARAYMKGQLACGSVREAM--LWERLSSTKRAVK---------AALAD 150
Cdd:PRK14536 307 LLGGHYRSQLAFSWEALKTAKAARRSLVRRV--ARVVDAARATTGSVRGTLaeCAAERVAESRASEsellltdfrAALED 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 151 DFDTPRVVDAILGLahhgngqlrasLKEPEGPRspavfGAIISYFEQFFETVGISL--ANQQYVSGDGSEATLHGVVDEL 228
Cdd:PRK14536 385 DFSTPKALSELQKL-----------VKDTSVPP-----SLCLSVLQAMDTVLGLGLiqEATASLSAQVPAGPSEEEIGQL 448
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1206271390 229 VRFRQKVRQ---FALAmpeatgdarrqqllerqplleacDTLRRGLTAHGINIKDRSSTTsTWE 289
Cdd:PRK14536 449 IEARAHARQtkdFPLA-----------------------DEIRDKLKAEGIELEDTHLGT-IWK 488
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
3-95 |
1.59e-20 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 91.53 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 3 FGSQLDIHSGGIDLAFPHHENEIAQ----CevfhqCEQWGNYFLHSGHLHAKgkEEKMSKSLKNYITIKDFLKTFSPDVF 78
Cdd:PLN02946 274 LGHSFDIHGGGMDLVFPHHENEIAQscaaC-----CDSNISYWIHNGFVTVD--SEKMSKSLGNFFTIRQVIDLYHPLAL 346
|
90
....*....|....*..
gi 1206271390 79 RFFCLRSSYRSAIDYSD 95
Cdd:PLN02946 347 RLFLLGTHYRSPINYSD 363
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
3-94 |
7.57e-16 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 77.58 E-value: 7.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 3 FGSQLDIHSGGIDLAFPHHENEIAQCEVFHQcEQWGNYFLHSGHLHAkgKEEKMSKSLKNYITIKDF-LKTFSPDVFRFF 81
Cdd:PRK14534 230 FKSTLDIHLGGVDHIGVHHINEIAIAECYLN-KKWCDMFVHGEFLIM--EYEKMSKSNNNFITIKDLeDQGFSPLDFRYF 306
|
90
....*....|...
gi 1206271390 82 CLRSSYRSAIDYS 94
Cdd:PRK14534 307 CLTAHYRTQLKFT 319
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
4-161 |
1.33e-11 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 64.57 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 4 GSQLDIHSGGIDLAFPHHENEIAQCEVFHQCEQWGNYFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKT-FSPDVFRFFC 82
Cdd:PRK12418 212 GSGFDIQGGGSDLIFPHHEFSAAHAEAATGERRFARHYVHAGMIGLDG--EKMSKSRGNLVFVSRLRAAgVDPAAIRLAL 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 83 LRSSYRSAIDYSDSAmlqaqqlllglgsfLEDARAYM---KGQLACGSVREAMlwerlsSTKRAVKAALADDFDTPRVVD 159
Cdd:PRK12418 290 LAGHYRADREWTDAV--------------LAEAEARLarwRAAAALPAGPDAA------DVVARVRAALADDLDTPGALA 349
|
..
gi 1206271390 160 AI 161
Cdd:PRK12418 350 AV 351
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
44-86 |
2.59e-07 |
|
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: 50.99 E-value: 2.59e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1206271390 44 SGHLHAKGKeeKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSS 86
Cdd:cd00814 271 HGYLTVEGK--KMSKSRGNVVDPDDLLERYGADALRYYLLRER 311
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
7-86 |
3.00e-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: 51.09 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271390 7 LDIHSGGIDLA--------FPHHeneiaqceVFHQCEQWGNY----FLHSGHLHAKGkeEKMSKSLKNYITIKDFLKTFS 74
Cdd:cd00812 225 VDIYIGGKEHApnhllysrFNHK--------ALFDEGLVTDEppkgLIVQGMVLLEG--EKMSKSKGNVVTPDEAIKKYG 294
|
90
....*....|..
gi 1206271390 75 PDVFRFFCLRSS 86
Cdd:cd00812 295 ADAARLYILFAA 306
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
44-84 |
5.91e-07 |
|
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: 50.50 E-value: 5.91e-07
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1206271390 44 SGHLHAKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLR 84
Cdd:COG0143 318 HGFLTVEG--EKMSKSRGNVIDPDDLLDRYGPDALRYYLLR 356
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
44-96 |
1.81e-05 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 45.74 E-value: 1.81e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1206271390 44 SGHLHAKGKeeKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSA-IDYSDS 96
Cdd:pfam09334 315 HGYLTYEGG--KMSKSRGNVVWPSEALDRFPPDALRYYLARNRPETKdTDFSWE 366
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
45-95 |
5.56e-05 |
|
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: 44.69 E-value: 5.56e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1206271390 45 GH-LHAKGKeeKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYSD 95
Cdd:COG0060 594 GFvLDEDGR--KMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSD 643
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
38-84 |
1.11e-04 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 43.33 E-value: 1.11e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1206271390 38 GNYFLhsghlhaKGKEEKMSKSLKNYITIKDFLKTFSPDVFRFFCLR 84
Cdd:PRK11893 289 AHGFL-------TLDGEKMSKSLGNVIDPFDLVDEYGVDAVRYFLLR 328
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
39-94 |
1.54e-04 |
|
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: 43.17 E-value: 1.54e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1206271390 39 NYFLHSGHLHAKGKeeKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYS 94
Cdd:pfam00133 549 NVLVHGLVRDEQGR--KMSKSLGNVIDPLDVIDKYGADALRLWLANSDYGRDINLS 602
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
54-81 |
1.91e-04 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 42.93 E-value: 1.91e-04
10 20
....*....|....*....|....*...
gi 1206271390 54 EKMSKSLKNYITIKDFLKTFSPDVFRFF 81
Cdd:PRK12300 576 KKMSKSKGNVIPLRKAIEEYGADVVRLY 603
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
35-82 |
7.02e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 41.21 E-value: 7.02e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1206271390 35 EQWGNYFLHSGHLHAKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFC 82
Cdd:PLN02959 700 EHWPRGFRCNGHLMLNS--EKMSKSTGNFLTLRQAIEEFSADATRFAL 745
|
|
| LysS |
COG1384 |
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
54-94 |
1.09e-03 |
|
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA synthetase, class I is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440994 [Multi-domain] Cd Length: 525 Bit Score: 40.56 E-value: 1.09e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1206271390 54 EKMSKSLKNYITIKDFLKTFSPDVFRFFCLRsSYRSAIDYS 94
Cdd:COG1384 286 EKISKSKGNGLTVEEWLEYAEPESLRYFMFR-KPKKAKDLD 325
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
54-81 |
1.37e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 40.14 E-value: 1.37e-03
10 20
....*....|....*....|....*....
gi 1206271390 54 EKMSKSlKNY-ITIKDFLKTFSPDVFRFF 81
Cdd:PRK00133 328 AKMSKS-RGTfIWARTYLDHLDPDYLRYY 355
|
|
| tRNA-synt_1f |
pfam01921 |
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from ... |
50-92 |
1.58e-03 |
|
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from prokaryotes.
Pssm-ID: 396483 Cd Length: 357 Bit Score: 39.55 E-value: 1.58e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1206271390 50 KGKEeKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAID 92
Cdd:pfam01921 275 KGGG-KMSSSKGNVITPEDWLEYAPPESLRFLMFRTKPKKAKD 316
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
46-85 |
4.46e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 38.63 E-value: 4.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1206271390 46 HLHAKG----KEEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRS 85
Cdd:PRK12267 286 KVFAHGwwlmKDGKMSKSKGNVVDPEELVDRYGLDALRYYLLRE 329
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
47-88 |
6.80e-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: 37.60 E-value: 6.80e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1206271390 47 LHAKGKeeKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYR 88
Cdd:cd00818 293 LDEDGR--KMSKSLGNYVDPQEVVDKYGADALRLWVASSDVY 332
|
|
| LysRS_core_class_I |
cd00674 |
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) ... |
51-85 |
7.87e-03 |
|
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) 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. The class I LysRS is found only in archaea and some bacteria and has evolved separately from class II LysRS, as the two do not share structural or sequence similarity.
Pssm-ID: 173900 [Multi-domain] Cd Length: 353 Bit Score: 37.30 E-value: 7.87e-03
10 20 30
....*....|....*....|....*....|....*
gi 1206271390 51 GKEEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRS 85
Cdd:cd00674 271 KGGGKMSSSKGNVITPSDWLEVAPPEVLRYLYARR 305
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