|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
11-583 |
0e+00 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 754.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 11 NKNKIILFRLYTTTINSSNNGSTIREWKKPSLENSYDTGIMVKNSLFKnGNVPFLisncsEKNQRPISWYTCGPTVYSSS 90
Cdd:PTZ00399 1 FKNNIIFLALAGLNGTGQVSKSRLPEWKKPSKEGKYLTGLKVNNSLTG-GKVEFV-----PQNGRQVRWYTCGPTVYDSS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 91 HIGHARNYMTVDIIQRILINYFRFNIIHVMGLTDIDDKIINKSKQELI-SASELSKKFEQEFFEDLKSLNIKPPMFTTRV 169
Cdd:PTZ00399 75 HLGHARTYVTFDIIRRILEDYFGYDVFYVMNITDIDDKIIKRAREEKLsIFLELARKWEKEFFEDMKALNVRPPDVITRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 170 SEHIDEIIKYIEKIKENQLTYESTKSVIFDVNKFGID--RYCSLRAanQQIKSDDTLLE---------KDKKSSQDFVLW 238
Cdd:PTZ00399 155 SEYVPEIVDFIQKIIDNGFAYESNGSVYFDVEAFRKAghVYPKLEP--ESVADEDRIAEgegalgkvsGEKRSPNDFALW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 239 KAYNEnididgtGNPvCWDSPFGKGRPGWHIECSAMIDSIFKDHLDVHSGGVDLEFPHHQNEIAQCEGHSHSHgsgdaes 318
Cdd:PTZ00399 233 KASKP-------GEP-SWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDLKFPHHDNELAQSEAYFDKH------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 319 tQWANYFFHIGHLILNNEKMSKSLGNVITIRDFLSRYSANSLRWICLIHKYNDPLSFSDETLQLCISKEIKFLNWFKIVR 398
Cdd:PTZ00399 298 -QWVNYFLHSGHLHIKGLKMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSDESMDEAIEKDKVFFNFFANVK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 399 SKLKleQTSVNKVKKTFNHSIELLNQLSETKYLIEKDLKDDFNTPSVIKRLELLMKQTNESMNS---IDTDLLFNVQDYV 475
Cdd:PTZ00399 377 IKLR--ESELTSPQKWTQHDFELNELFEETKSAVHAALLDNFDTPEALQALQKLISATNTYLNSgeqPSAPLLRSVAQYV 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 476 ESILNIFGLEVNS---EISDHNKTDESNQFLLEKLLDFRSDVKNLAKN---EKSLDQIKSKIYQITDQLRSDCQSEISLR 549
Cdd:PTZ00399 455 TKILSIFGLVEGSdglGSQGQNSTSENFKPLLEALLRFRDEVRDAAKAemkLISLDKKKKQLLQLCDKLRDEWLPNLGIR 534
|
570 580 590
....*....|....*....|....*....|....
gi 66818080 550 VSDIPDkgtnKPYTVDWLDKNHIQLLNIKKQSKK 583
Cdd:PTZ00399 535 IEDKPD----GPSVWKLDDKEELQREKEEKEALK 564
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
80-527 |
1.50e-126 |
|
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: 379.83 E-value: 1.50e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 80 YTCGPTVYSSSHIGHARNYMTVDIIQRILInYFRFNIIHVMGLTDIDDKIINKSKQELISASELSKKFEQEFFEDLKSLN 159
Cdd:COG0215 26 YVCGPTVYDYAHIGHARTFVVFDVLRRYLR-YLGYKVTYVRNITDVDDKIIKRAAEEGESIWELAERYIAAFHEDMDALG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 160 IKPPMFTTRVSEHIDEIIKYIEKIKENQLTYESTKSVIFDVNKFgiDRYCSLraANQQIksDDTL------LEKDKKSSQ 233
Cdd:COG0215 105 VLPPDIEPRATEHIPEMIELIERLIEKGHAYEADGDVYFDVRSF--PDYGKL--SGRNL--DDLRagarveVDEEKRDPL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 234 DFVLWKAYNEnididgtGNPvCWDSPFGKGRPGWHIECSAMIDSIFKDHLDVHSGGVDLEFPHHQNEIAQCEGHSHshgs 313
Cdd:COG0215 179 DFALWKAAKP-------GEP-SWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIAQSEAATG---- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 314 gdaesTQWANYFFHIGHLILNNEKMSKSLGNVITIRDFLSRYSANSLRWICLIHKYNDPLSFSDETLQlciskeikflnw 393
Cdd:COG0215 247 -----KPFARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALE------------ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 394 fkivRSKLKLE--QTSVNKVKKTFNHSIELLNQLSETKYLIEKDLKDDFNTPSVIKRLELLMKQTNESMNS-IDTDLLFN 470
Cdd:COG0215 310 ----EAEKALErlYNALRRLEEALGAADSSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKALDEgEDKAALAA 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66818080 471 VQDYVESILNIFGL-----EVNSEISDHNKTDEsnqfLLEKLLDFRSDVKNlAKN-EKSlDQI 527
Cdd:COG0215 386 LAALLRALGGVLGLlllepEAWQGAAEDELLDA----LIEALIEERAEARK-AKDfARA-DRI 442
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
77-530 |
4.13e-117 |
|
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: 355.54 E-value: 4.13e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 77 ISWYTCGPTVYSSSHIGHARNYMTVDIIQRILiNYFRFNIIHVMGLTDIDDKIINKSKQELISASELSKKFEQEFFEDLK 156
Cdd:TIGR00435 22 VKMYVCGPTVYDYCHIGHARTAIVFDVLRRYL-RYLGYKVQYVQNITDIDDKIIKRARENGESVYEVSERFIEAYFEDMK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 157 SLNIKPPMFTTRVSEHIDEIIKYIEKIKENQLTYESTK-SVIFDVNKFgiDRYCSLraANQQIKSDDT----LLEKDKKS 231
Cdd:TIGR00435 101 ALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNgDVYFDVSKF--KDYGKL--SKQDLDQLEAgarvDVDEAKRN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 232 SQDFVLWKAYnenididgTGNPVCWDSPFGKGRPGWHIECSAMIDSIFKDHLDVHSGGVDLEFPHHQNEIAQCEGhshsh 311
Cdd:TIGR00435 177 KLDFVLWKSS--------KEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQSEA----- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 312 gsgdAESTQWANYFFHIGHLILNNEKMSKSLGNVITIRDFLSRYSANSLRWICLIHKYNDPLSFSDETLQLciskeikfl 391
Cdd:TIGR00435 244 ----AFGKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEA--------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 392 nwfkiVRSKLKLEQTSVNKVKKTFNHS--IELLNQLSETKYL--IEKDLKDDFNTPSVIKRLELLMKQTN-ESMNSIDTD 466
Cdd:TIGR00435 311 -----AKNALERLYKALRVLDTSLAYSgnQSLNKFPDEKEFEarFVEAMDDDLNTANALAVLFELAKSINlTFVSKADAA 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66818080 467 LLFNVQDYVESILNI-FGLEVNSEISDHNKTDESNQFLLEKLLDFRSDvKNLAKNEKSLDQIKSK 530
Cdd:TIGR00435 386 LLIEHLIFLESRLGLlLGLPSKPVQAGSNDDLGEIEALIEERSIARKE-KDFAKADEIRDELAKK 449
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
74-381 |
1.71e-116 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 347.82 E-value: 1.71e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 74 QRPISWYTCGPTVYSSSHIGHARNYMTVDIIQRILiNYFRFNIIHVMGLTDIDDKIINKSKQELISASELSKKFEQEFFE 153
Cdd:pfam01406 7 QGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYL-QALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFIEAYTK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 154 DLKSLNIKPPMFTTRVSEHIDEIIKYIEKIKENQLTYESTK-SVIFDVNKFgiDRYCSLRAAN----QQIKSDDtlLEKD 228
Cdd:pfam01406 86 DMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNgDVYFDVSSF--PDYGKLSGQNleqlEAGARGE--VSEG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 229 KKSSQDFVLWKAYNEnididgtGNPVcWDSPFGKGRPGWHIECSAMIDSIFKDHLDVHSGGVDLEFPHHQNEIAQCEGhs 308
Cdd:pfam01406 162 KRDPLDFALWKASKE-------GEPS-WDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEA-- 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66818080 309 hshgsgdAESTQWANYFFHIGHLILNNEKMSKSLGNVITIRDFLSRYSANSLRWICLIHKYNDPLSFSDETLQ 381
Cdd:pfam01406 232 -------AFDKQLANYWLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLE 297
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
73-376 |
1.20e-84 |
|
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: 262.52 E-value: 1.20e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 73 NQRPISWYTCGPTVYSSSHIGHARNYMTVDIIQRILINYFrFNIIHVMGLTDIDDKIINKSKQELISASELSKKFEQEFF 152
Cdd:cd00672 17 NPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLG-YKVRYVQNITDIDDKIIKRAREEGLSWKEVADYYTKEFF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 153 EDLKSLNIKPPMFTTRVsehideiikyiekikenqltyestksvifdvnkfgidrycslraanqqiksddtllekdkkss 232
Cdd:cd00672 96 EDMKALNVLPPDVVPRV--------------------------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 233 qdfvlwkaynenididgtgnpvcwdspfgkgrpgWHIECSAMIDSIFKDHLDVHSGGVDLEFPHHQNEIAQCEGHSHShg 312
Cdd:cd00672 113 ----------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQSEAATGK-- 156
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66818080 313 sgdaestQWANYFFHIGHLILNNEKMSKSLGNVITIRDFLSRYSANSLRWICLIHKYNDPLSFS 376
Cdd:cd00672 157 -------PFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
80-561 |
8.11e-76 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 251.00 E-value: 8.11e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 80 YTCGPTVYSSSHIGHARNYMTVDIIQRILiNYFRFNIIHVMGLTDIDDKIINKSKQELISASELSKKFEQEFFEDLKSLN 159
Cdd:PLN02946 84 YVCGVTAYDLSHIGHARVYVTFDVLYRYL-KHLGYEVRYVRNFTDVDDKIIARANELGEDPISLSRRYCEEFLSDMAYLH 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 160 IKPPMFTTRVSEHIDEIIKYIEKIKENQLTYESTKSVIFDVNKFGIDRYCSLRAANQQIKSDDTLLEKDKKSSQDFVLWK 239
Cdd:PLN02946 163 CLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVDGDVYFSVDKFPEYGKLSGRKLEDNRAGERVAVDSRKKNPADFALWK 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 240 AYNEnididgtGNPVcWDSPFGKGRPGWHIECSAMIDSIFKDHLDVHSGGVDLEFPHHQNEIAQceghshshgSGDAEST 319
Cdd:PLN02946 243 AAKE-------GEPF-WDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLVFPHHENEIAQ---------SCAACCD 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 320 QWANYFFHIGHLILNNEKMSKSLGNVITIRDFLSRYSANSLRWICLIHKYNDPLSFSDEtlQLCISKEIKFLNWFKIVRS 399
Cdd:PLN02946 306 SNISYWIHNGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDV--QLESASERIFYIYQTLHDC 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 400 KLKLEQTSVNKVKKTF-NHSIELLNQLSETkylIEKDLKDDFNTPSVIKRLELLMKQTNESMNS-------IDTDLLFNV 471
Cdd:PLN02946 384 EESLQQHDSTFEKDSVpPDTLNCINKFHDE---FVTSMSDDLHTPVALAALSEPLKTINDLLHTrkgkkqeKRLESLAAL 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 472 QDYVESILNIFGLEVNSeisdhnkTDESNQFLLEKLLDfRSDVKN---LAKNEKSLDQIKSKIYQITDQLRSDCqSEISL 548
Cdd:PLN02946 461 EKKIRDVLSVLGLMPTS-------YSEALQQLREKALR-RAKLTEeqvLQKIEERTVARKNKEYEKSDAIRKDL-AAVGI 531
|
490
....*....|...
gi 66818080 549 RVSDIPDKGTNKP 561
Cdd:PLN02946 532 ALMDSPDGTTWRP 544
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
80-531 |
6.85e-72 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 238.67 E-value: 6.85e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 80 YTCGPTVYSSSHIGHARNYMTVDIIQRILiNYFRFNIIHVMGLTDI----------DDKIINKSKQELISASELSKKFEQ 149
Cdd:PRK14536 27 YGCGPTVYNYAHIGNLRTYVFQDTLRRTL-HFLGYRVTHVMNITDVghltddadsgEDKMVKSAQEHGKSVLEIAAHYTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 150 EFFEDLKSLNIKPPMFTTRVSEHIDEIIKYIEKIKENQLTYESTKSVIFDVNKFgiDRYCSLRAANQQIKSDDTLLEKD- 228
Cdd:PRK14536 106 AFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCAGGNVYFDIRTF--PSYGSLASAAVEDLQAGARIEHDt 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 229 -KKSSQDFVLW--KAYNENididgtgNPVCWDSPFGKGRPGWHIECSAMIDSIFKDHLDVHSGGVDLEFPHHQNEIAQCE 305
Cdd:PRK14536 184 nKRNPHDFVLWftRSKFEN-------HALTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIGGVDHIRVHHTNEIAQCE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 306 GhshshgsgdAESTQWANYFFHIGHLILNNEKMSKSLGNVITIRDFLSR-YSANSLRWICLIHKYNDPLSFSDETLQLCI 384
Cdd:PRK14536 257 A---------ATGKPWVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQEKgFQPLDYRFFLLGGHYRSQLAFSWEALKTAK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 385 SKEIKFLNWFKIVRSKLKLEQTSV-NKVKKTFNHSIELLNQLSETKYL--IEKDLKDDFNTPSVIKRLELLMKQTnesmn 461
Cdd:PRK14536 328 AARRSLVRRVARVVDAARATTGSVrGTLAECAAERVAESRASESELLLtdFRAALEDDFSTPKALSELQKLVKDT----- 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 462 SIDTDLLFNVQDYVESILNIFGLEVNSEISDHNKTDESNQFLLEKLLDFRSDVKnLAKNEKSLDQIKSKI 531
Cdd:PRK14536 403 SVPPSLCLSVLQAMDTVLGLGLIQEATASLSAQVPAGPSEEEIGQLIEARAHAR-QTKDFPLADEIRDKL 471
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
77-380 |
4.38e-55 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 198.02 E-value: 4.38e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 77 ISWYTCGPTVYSSSHIGHARNYMTVDIIQRILiNYFRFNIIHVMGLTDIDDKIINKSKQELISASELSKKFEQEFFEDLK 156
Cdd:PRK14535 249 VRMYVCGMTVYDYCHLGHARVMVVFDMIARWL-RECGYPLTYVRNITDIDDKIIARAAENGETIGELTARFIQAMHEDAD 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 157 SLNIKPPMFTTRVSEHIDEIIKYIEKIKENQLTYESTK-SVIFDVNKFGIDRYCSLRAANQQIKSDDTLLEKDKKSSQDF 235
Cdd:PRK14535 328 ALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANgDVYYAVREFAAYGQLSGKSLDDLRAGERVEVDGFKRDPLDF 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 236 VLWKAYNenididgTGNPVcWDSPFGKGRPGWHIECSAMIDSIFKDHLDVHSGGVDLEFPHHQNEIAQCE-------GHS 308
Cdd:PRK14535 408 VLWKAAK-------AGEPA-WESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIAQSVgatghtcGHH 479
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66818080 309 HSHGSGDAESTQWANYFFHIGHLILNNEKMSKSLGNVITIRDFLSRYSANSLRWICLIHKYNDPLSFSDETL 380
Cdd:PRK14535 480 HAQTHHGQSIASHVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNYSDAHL 551
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
72-420 |
1.72e-49 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 178.51 E-value: 1.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 72 KNQRPISWYTCGPTVYSSSHIGHARNYMTVDIIQRILiNYFRFNIIHVMGLTDI----------DDKIINKSKQELISAS 141
Cdd:PRK14534 17 KNFSDVKVYACGPTVYNYAHIGNFRTYIFEDLLIKSL-RLLKYNVNYAMNITDIghltgdfddgEDKVVKAARERGLTVY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 142 ELSKKFEQEFFEDLKSLNIKPPMFTTRVSEHIDEIIKYIEKIKENQLTYESTKSVIFDVNKFgiDRYCSLRAANQQIKSD 221
Cdd:PRK14534 96 EISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTYFVNGNVYFDTSCF--KSYGQMAGINLNDFKD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 222 DTL----LEKDKKSSQDFVLWKAYNENIDidgtgNPVCWDSPFGKGRPGWHIECSAMIDSIFKDHLDVHSGGVDLEFPHH 297
Cdd:PRK14534 174 MSVsrveIDKSKRNKSDFVLWFTNSKFKD-----QEMKWDSPWGFGYPSWHLECAAMNLEYFKSTLDIHLGGVDHIGVHH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 298 QNEIAQCEGHSHShgsgdaestQWANYFFHIGHLILNNEKMSKSLGNVITIRDFLSR-YSANSLRWICLIHKYNDPLSFS 376
Cdd:PRK14534 249 INEIAIAECYLNK---------KWCDMFVHGEFLIMEYEKMSKSNNNFITIKDLEDQgFSPLDFRYFCLTAHYRTQLKFT 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 66818080 377 DETLQLCISKEIKFLNWFKIVRSKL-KLEQTSVNKVKKTFNHSIE 420
Cdd:PRK14534 320 FNNLKACKIARENMLNKLTYFYSSLdQFDLNLLNKDLENIEFSLE 364
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
74-381 |
5.53e-47 |
|
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: 169.91 E-value: 5.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 74 QRPISWYTCGPTVYSSSHIGHARNYMTVDIIQRILINYFRfNIIHVMGLTDIDDKIINKSKQELISASELSKKFEQEFFE 153
Cdd:TIGR03447 34 GPEAGMYVCGITPYDATHLGHAATYLTFDLVNRVWRDAGH-RVHYVQNVTDVDDPLFERAERDGVDWRELGTSQIDLFRE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 154 DLKSLNIKPPMFTTRVSEHIDEIIKYIEKIKENQLTYE----STKSVIFDVN---KFG-IDRYcslraanqqikSDDTLL 225
Cdd:TIGR03447 113 DMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYIvegpEYPDVYFSIDateQFGyESGY-----------DRATML 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 226 E-----------KDKKSSQDFVLWKAYNEnididgtGNPvCWDSPFGKGRPGWHIECSAMIDSIFKDHLDVHSGGVDLEF 294
Cdd:TIGR03447 182 ElfaerggdpdrPGKRDPLDALLWRAARE-------GEP-SWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSDLIF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 295 PHHQneiaqceghshsHGSGDAEST----QWANYFFHIGHLILNNEKMSKSLGNVItirdFLSRYSA-----NSLRWICL 365
Cdd:TIGR03447 254 PHHE------------FSAAHAEAAtgvrRMARHYVHAGMIGLDGEKMSKSLGNLV----FVSKLRAagvdpAAIRLGLL 317
|
330
....*....|....*.
gi 66818080 366 IHKYNDPLSFSDETLQ 381
Cdd:TIGR03447 318 AGHYRQDRDWTDAVLA 333
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
80-380 |
2.04e-42 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 156.63 E-value: 2.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 80 YTCGPTVYSSSHIGHARNYMTVDIIQRIL------INYfrfniihVMGLTDIDDKIINKSKQELISASELSKKFEQEFFE 153
Cdd:PRK12418 13 YVCGITPYDATHLGHAATYLAFDLVNRVWrdaghdVHY-------VQNVTDVDDPLLERAARDGVDWRDLAEREIALFRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 154 DLKSLNIKPPMFTTRVSEHIDEIIKYIEKIKENQLTYE----STKSVIFDVN---KFG-IDRYcslraanqqikSDDTLL 225
Cdd:PRK12418 86 DMEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYVvddeEYPDVYFSVDatpQFGyESGY-----------DRATML 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 226 E-----------KDKKSSQDFVLWKAYNEnididgtGNPvCWDSPFGKGRPGWHIECSAMIDSIFKDHLDVHSGGVDLEF 294
Cdd:PRK12418 155 ElfaerggdpdrPGKRDPLDALLWRAARP-------GEP-SWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 295 PHHQneiaqcegHSHSHGSGDAESTQWANYFFHIGHLILNNEKMSKSLGNVItirdFLSRYSAN-----SLRWICLIHKY 369
Cdd:PRK12418 227 PHHE--------FSAAHAEAATGERRFARHYVHAGMIGLDGEKMSKSRGNLV----FVSRLRAAgvdpaAIRLALLAGHY 294
|
330
....*....|.
gi 66818080 370 NDPLSFSDETL 380
Cdd:PRK12418 295 RADREWTDAVL 305
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
81-362 |
1.54e-10 |
|
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases. These class I enzymes are all monomers. However, in some species, MetRS functions as a homodimer, as a result of an additional C-terminal domain. These enzymes aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. Enzymes in this subfamily share an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. MetRS has a significantly shorter insertion, which lacks the editing function.
Pssm-ID: 185674 [Multi-domain] Cd Length: 312 Bit Score: 62.44 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 81 TCG-PTVYSSSHIGHARNYMTVDIIQRilinYFR---FNIIHVMGlTDI---------DDKIINKSKQELISAS-----E 142
Cdd:cd00668 5 TTPpPYANGSLHLGHALTHIIADFIAR----YKRmrgYEVPFLPG-WDThglpielkaERKGGRKKKTIWIEEFredpkE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 143 LSKKFEQEFFEDLKSLNI----KPPMFTTRvSEHIDEIIKYIEKIKENQLTYESTKSVI------FDVNKFGIDrycsLR 212
Cdd:cd00668 80 FVEEMSGEHKEDFRRLGIsydwSDEYITTE-PEYSKAVELIFSRLYEKGLIYRGTHPVRiteqwfFDMPKFKEK----LL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 213 AANQQIKsddtllekdkkssqdFVLWKAYNENIDIdgTGNPVCW----DSPFGKGRPGWHIE----CSAMIDSIFK---D 281
Cdd:cd00668 155 KALRRGK---------------IVPEHVKNRMEAW--LESLLDWaisrQRYWGTPLPEDVFDvwfdSGIGPLGSLGypeE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 282 H--------LDVHSGGVDLEFPHHqneiaqceghSHSHGSGDAESTQWANYFFHIGHLILNNE--KMSKSLGNVITIRDF 351
Cdd:cd00668 218 KewfkdsypADWHLIGKDILRGWA----------NFWITMLVALFGEIPPKNLLVHGFVLDEGgqKMSKSKGNVIDPSDV 287
|
330
....*....|.
gi 66818080 352 LSRYSANSLRW 362
Cdd:cd00668 288 VEKYGADALRY 298
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
329-387 |
4.45e-08 |
|
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: 55.89 E-value: 4.45e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66818080 329 GHLILNNEKMSKSLGNVITIRDFLSRYSANSLRWiCLIHK--YNDPLSFSDETLQLCISKE 387
Cdd:COG0143 319 GFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRY-YLLREvpFGQDGDFSWEDFVARVNSD 378
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
317-399 |
6.11e-08 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 55.85 E-value: 6.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 317 ESTQWANYFFHIGHLILNNEKMSKSLGNVITIRDFLSRYSANSLRWIC------LihkynDPLSFSDETLQLCISKEIKF 390
Cdd:PLN02959 698 AEEHWPRGFRCNGHLMLNSEKMSKSTGNFLTLRQAIEEFSADATRFALadagdgV-----DDANFVFETANAAILRLTKE 772
|
....*....
gi 66818080 391 LNWFKIVRS 399
Cdd:PLN02959 773 IAWMEEVLA 781
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
329-475 |
3.77e-07 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 53.33 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 329 GHLILNNEKMSKSLGNVITIRDFLSRYSANSLRWIclihkyndpLSFSDETLQLciskeikfLNWfkivRSKLkleqtsV 408
Cdd:PRK12300 569 GFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLY---------LTSSAELLQD--------ADW----REKE------V 621
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66818080 409 NKVKKTFNHSIELLNQLSETKYLIEKDLKDDFntpsVIKRLELLMKQTNESMNSIDT-----DLLFNVQDYV 475
Cdd:PRK12300 622 ESVRRQLERFYELAKELIEIGGEEELRFIDKW----LLSRLNRIIKETTEAMESFQTrdavqEAFYELLNDL 689
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
81-388 |
4.29e-07 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 52.29 E-value: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 81 TCG-PTVYSSSHIGHARNYMTVDIIQRilinYFRFNIIHVMGLTDIDD---KIINKSKQELISASELSKKFEQEFFEDLK 156
Cdd:pfam09334 4 TTAlPYANGPPHLGHLYSYIPADIFAR----YLRLRGYDVLFVCGTDEhgtPIELKAEKEGITPEELVDRYHEIHREDFK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 157 SLNIKPPMFTTRVSE-HIDEIIKYIEKIKENQLTYESTKSVIFDV--NKFGIDRY--------CSLRAA-----NQQIKS 220
Cdd:pfam09334 80 KFNISFDDYGRTTSErHHELVQEFFLKLYENGYIYEKEIEQFYCPsdERFLPDRYvegtcphcGSEDARgdqceNCGRHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 221 DDTLLEKDKKSSQDFVLWKAYNENI--DIDGTGNPV-CWdspFGKGRPGWHIECSAMIDSIFKDHL-------DVHSGgv 290
Cdd:pfam09334 160 EPTELINPKCVICGTTPEVKETEHYffDLSKFQDKLrEW---IEENNPEWPENVKNMVLEWLKEGLkdraisrDLDWG-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 291 dLEFPHHQNE------------IAqceghSHSHGSGDAESTQ--WAN-------YF-------FHI-------------- 328
Cdd:pfam09334 235 -IPVPGAEGKvfyvwldapigyIS-----ATKELSGNEEKWKewWPNdpdtelvHFigkdiiyFHTifwpamllgagyrl 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66818080 329 -------GHLILNNEKMSKSLGNVITIRDFLSRYSANSLRWICLihkYNDPLS----FSDETLQLCISKEI 388
Cdd:pfam09334 309 pttvfahGYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLA---RNRPETkdtdFSWEDFVERVNSEL 376
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
91-362 |
8.39e-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: 8.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 91 HIGHARNYMTVDIIQRilinYFR---FNIIHVMGLTDIDDKIINKSKQELISASELSKKFEQEFFEDLKSLNIK---PPM 164
Cdd:cd00812 16 HVGHVRTYTIGDIIAR----YKRmqgYNVLFPMGFDAFGLPAENAAIKIGRDPEDWTEYNIKKMKEQLKRMGFSydwRRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 165 FTTrvseHIDEIIKYIEKI----KENQLTYESTKSVIFDVN------KFGIDRYcslraANQQIKSDDTLLEKDKKSSQD 234
Cdd:cd00812 92 FTT----CDPEYYKFTQWLflklYEKGLAYKKEAPVNWCKLldqwflKYSETEW-----KEKLLKDLEKLDGWPEEVRAM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 235 FVLWkaynenIDID---GTGNPVCWDspfgkgrpgWHIE---CSAM-----IDSIFKDH------------------LDV 285
Cdd:cd00812 163 QENW------IGCSrqrYWGTPIPWT---------DTMEslsDSTWyyaryTDAHNLEQpyegdlefdreefeywypVDI 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66818080 286 HSGGVDlefpHHQNEIAQCEGHSHSHGSGDAESTQWANYFFHIGHLILNNEKMSKSLGNVITIRDFLSRYSANSLRW 362
Cdd:cd00812 228 YIGGKE----HAPNHLLYSRFNHKALFDEGLVTDEPPKGLIVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARL 300
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
329-362 |
5.82e-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: 48.68 E-value: 5.82e-06
10 20 30
....*....|....*....|....*....|....
gi 66818080 329 GHLILNNEKMSKSLGNVITIRDFLSRYSANSLRW 362
Cdd:cd00814 272 GYLTVEGKKMSKSRGNVVDPDDLLERYGADALRY 305
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
80-185 |
8.31e-06 |
|
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: 45.93 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 80 YTCGPTVYSSSHIGHARNYMTVDIIQRILiNYFRFNIIHVMGLTDIDDKIINKSKQELISASELSKKFEQEFFEDLK--- 156
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAY-RKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKEDVEymf 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 66818080 157 -------SLNIKPPMFTTRVSEHIDEIIKYIEKIKE 185
Cdd:cd00802 81 lqaadflLLYETECDIHLGGSDQLGHIELGLELLKK 116
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
337-381 |
9.42e-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: 48.54 E-value: 9.42e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 66818080 337 KMSKSLGNVITIRDFLSRYSANSLRWICLIHKYNDPLSFSDETLQ 381
Cdd:COG0060 603 KMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEILK 647
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
322-365 |
6.81e-05 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 45.64 E-value: 6.81e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 66818080 322 ANYFfhighLILNNEKMSKSLGNVITIRDFLSRYSANSLRWICL 365
Cdd:PRK11893 289 AHGF-----LTLDGEKMSKSLGNVIDPFDLVDEYGVDAVRYFLL 327
|
|
| LysRS_core_class_I |
cd00674 |
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) ... |
325-368 |
3.47e-04 |
|
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: 43.08 E-value: 3.47e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 66818080 325 FFHIGhlilNNEKMSKSLGNVITIRDFLSRYSANSLRWICLIHK 368
Cdd:cd00674 267 FIGLK----GGGKMSSSKGNVITPSDWLEVAPPEVLRYLYARRK 306
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
91-190 |
4.08e-04 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 42.69 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66818080 91 HIGHARNymtvdiiqrILINYF---RFNIIHVMgltDIDDKIINKSKQElisaselskkFEQEFFEDLKSLNIKPPMFTT 167
Cdd:pfam00749 15 HIGHAKA---------ALFNYLyakNHNGKFIL---RFEDTDPERETPE----------FEESILEDLKWLGIKWDYGPY 72
|
90 100
....*....|....*....|...
gi 66818080 168 RVSEHIDEIIKYIEKIKENQLTY 190
Cdd:pfam00749 73 YQSDRFDIYYKYAEELIKKGKAY 95
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
334-365 |
4.83e-04 |
|
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) catalytic core domain. This enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. ValRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 185677 [Multi-domain] Cd Length: 382 Bit Score: 42.62 E-value: 4.83e-04
10 20 30
....*....|....*....|....*....|...
gi 66818080 334 NNEKMSKSLGNVITIRDFLSRYSANSLR-WICL 365
Cdd:cd00817 340 DGRKMSKSLGNVIDPLDVIDGYGADALRfTLAS 372
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
329-361 |
5.72e-04 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 42.87 E-value: 5.72e-04
10 20 30
....*....|....*....|....*....|...
gi 66818080 329 GHLILNNEKMSKSLGNVITIRDFLSRYSANSLR 361
Cdd:PRK12267 291 GWWLMKDGKMSKSKGNVVDPEELVDRYGLDALR 323
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
336-362 |
8.30e-04 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 42.49 E-value: 8.30e-04
10 20
....*....|....*....|....*..
gi 66818080 336 EKMSKSLGNVITIRDFLSRYSANSLRW 362
Cdd:PRK13208 532 KKMSKSKGNVVTPEELLEKYGADAVRY 558
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
329-362 |
8.76e-04 |
|
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440261 [Multi-domain] Cd Length: 826 Bit Score: 42.35 E-value: 8.76e-04
10 20 30
....*....|....*....|....*....|....
gi 66818080 329 GHLILNNEKMSKSLGNVITIRDFLSRYSANSLRW 362
Cdd:COG0495 581 GVVIGGIEKMSKSKGNVVDPDEIIEKYGADTLRL 614
|
|
| LysS |
COG1384 |
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
334-363 |
8.81e-04 |
|
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: 42.10 E-value: 8.81e-04
10 20 30
....*....|....*....|....*....|
gi 66818080 334 NNEKMSKSLGNVITIRDFLSRYSANSLRWI 363
Cdd:COG1384 284 NGEKISKSKGNGLTVEEWLEYAEPESLRYF 313
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
334-376 |
1.42e-03 |
|
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase and is particularly closely related to the isoleucyl tRNA synthetase. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273070 [Multi-domain] Cd Length: 861 Bit Score: 41.58 E-value: 1.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 66818080 334 NNEKMSKSLGNVITIRDFLSRYSANSLR-WICLIHKYNDPLSFS 376
Cdd:TIGR00422 522 QGRKMSKSLGNVIDPLDVIEKYGADALRfTLASLVTPGDDINFD 565
|
|
| tRNA-synt_1f |
pfam01921 |
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from ... |
336-376 |
1.80e-03 |
|
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from prokaryotes.
Pssm-ID: 396483 Cd Length: 357 Bit Score: 40.71 E-value: 1.80e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 66818080 336 EKMSKSLGNVITIRDFLSRYSANSLRWICLIHKYNDPLSFS 376
Cdd:pfam01921 278 GKMSSSKGNVITPEDWLEYAPPESLRFLMFRTKPKKAKDLD 318
|
|
| lysK |
PRK00750 |
lysyl-tRNA synthetase; Reviewed |
323-382 |
1.99e-03 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234829 [Multi-domain] Cd Length: 510 Bit Score: 40.95 E-value: 1.99e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66818080 323 NY-FFHIGhlilNNEKMSKSLGNVITIRDFLSRYSANSLR-WICLIHKYNDPLSFS------DETLQL 382
Cdd:PRK00750 269 VYeLFLDK----KGEKISKSKGNVITIEDWLEYAPPESLRlFMFARPKPAKRLDFDvipklvDEYDRF 332
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
329-361 |
3.48e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 40.14 E-value: 3.48e-03
10 20 30
....*....|....*....|....*....|...
gi 66818080 329 GHLILNNEKMSKSLGNVITIRDFLSRYSANSLR 361
Cdd:PRK00133 321 GFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLR 353
|
|
| |
