|
Name |
Accession |
Description |
Interval |
E-value |
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
7-479 |
0e+00 |
|
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: 657.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 7 NSLTHKMEEFHPLVEGKVKMYTCGPTVYGTPHIGNYRTFFMADILRRYFEFKGFEVFHVMNITDIDDKTIRDSAKEGLTL 86
Cdd:COG0215 6 NTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYLGYKVTYVRNITDVDDKIIKRAAEEGESI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 87 KEFTEKYTKIFFKGIDWLHIKRAHIYPRATDHIQDMINWIQKLVNKGFAYVTEDGVYFAIQKFDKYGQLVNLKLGKQKVG 166
Cdd:COG0215 86 WELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEADGDVYFDVRSFPDYGKLSGRNLDDLRAG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 167 ERAKADEYdKEHVQDFALWKKSTEEEikrgIYYESPWGKGRPGWHIECSVMSMKYLGETFDIHTGAVDLKFPHHTNEIAQ 246
Cdd:COG0215 166 ARVEVDEE-KRDPLDFALWKAAKPGE----PSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 247 AEAITGKPFVHYWIHGEFLSIKEEKMSKSLGNVTTLHQLMSSFEPDTIRYLYLSTRYDALLVFSEDKLISAKNSVEKLRN 326
Cdd:COG0215 241 SEAATGKPFARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKALERLYN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 327 TLENVLAVLreptiaspfsEQEEALLTKAHALKNEFEQVMDNNFDTPKGLKIIHELAKSLNKYLEGDINPGVLQEAFTIY 406
Cdd:COG0215 321 ALRRLEEAL----------GAADSSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKALDEGEDKAALAALAALL 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491309305 407 KTLLGTFGLFEKLSLKDAALQGDKLTDELLNFLIEIRNAARKRKDFETSDMIRDRLAKLDVILEDTPKGTVWK 479
Cdd:COG0215 391 RALGGVLGLLLLEPEAWQGAAEDELLDALIEALIEERAEARKAKDFARADRIRDELAALGIVLEDTPDGTTWR 463
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
7-479 |
1.70e-165 |
|
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: 475.33 E-value: 1.70e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 7 NSLTHKMEEFHPLVEGKVKMYTCGPTVYGTPHIGNYRTFFMADILRRYFEFKGFEVFHVMNITDIDDKTIRDSAKEGLTL 86
Cdd:TIGR00435 5 NTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLRYLGYKVQYVQNITDIDDKIIKRARENGESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 87 KEFTEKYTKIFFKGIDWLHIKRAHIYPRATDHIQDMINWIQKLVNKGFAYVTEDG-VYFAIQKFDKYGQLVNLKLGKQKV 165
Cdd:TIGR00435 85 YEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGdVYFDVSKFKDYGKLSKQDLDQLEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 166 GERAKADEyDKEHVQDFALWKKSTEEEIKrgiyYESPWGKGRPGWHIECSVMSMKYLGETFDIHTGAVDLKFPHHTNEIA 245
Cdd:TIGR00435 165 GARVDVDE-AKRNKLDFVLWKSSKEGEPK----WDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 246 QAEAITGKPFVHYWIHGEFLSIKEEKMSKSLGNVTTLHQLMSSFEPDTIRYLYLSTRYDALLVFSEDKLISAKNSVEKLR 325
Cdd:TIGR00435 240 QSEAAFGKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKNALERLY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 326 NTLENVLavlrepTIASPFSEQEEALLTKAHALKNEFEQVMDNNFDTPKGLKIIHELAKSLNKYLEGDINPGVLQEAFti 405
Cdd:TIGR00435 320 KALRVLD------TSLAYSGNQSLNKFPDEKEFEARFVEAMDDDLNTANALAVLFELAKSINLTFVSKADAALLIEHL-- 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1491309305 406 yKTLLGTFGLFEKLSLKDAALQGDKLTDELLNfLIEIRNAARKRKDFETSDMIRDRLAKLDVILEDTPKGTVWK 479
Cdd:TIGR00435 392 -IFLESRLGLLLGLPSKPVQAGSNDDLGEIEA-LIEERSIARKEKDFAKADEIRDELAKKGIVLEDTPQGTTWR 463
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
1-479 |
3.72e-136 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 401.61 E-value: 3.72e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 1 MAIIVRNSLTHKMEEFHPLVEGKVKMYTCGPTVYGTPHIGNYRTFFMADILRRYFEFKGFEVFHVMNITDI--------- 71
Cdd:PRK14536 1 MALRLYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTLHFLGYRVTHVMNITDVghltddads 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 72 -DDKTIRDSAKEGLTLKEFTEKYTKIFFKGIDWLHIKRAHIYPRATDHIQDMINWIQKLVNKGFAYVTEDGVYFAIQKFD 150
Cdd:PRK14536 81 gEDKMVKSAQEHGKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCAGGNVYFDIRTFP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 151 KYGQLVNLKLGKQKVGERAKADEyDKEHVQDFALWKKSTEEEiKRGIYYESPWGKGRPGWHIECSVMSMKYLGETFDIHT 230
Cdd:PRK14536 161 SYGSLASAAVEDLQAGARIEHDT-NKRNPHDFVLWFTRSKFE-NHALTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 231 GAVDLKFPHHTNEIAQAEAITGKPFVHYWIHGEFLSIKEEKMSKSLGNVTTLHQLMS-SFEPDTIRYLYLSTRYDALLVF 309
Cdd:PRK14536 239 GGVDHIRVHHTNEIAQCEAATGKPWVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQEkGFQPLDYRFFLLGGHYRSQLAF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 310 SEDKLISAKNSVEKLRNTLENVLAVLREPT--------------IASPFSEQEEALLTKahalkneFEQVMDNNFDTPKG 375
Cdd:PRK14536 319 SWEALKTAKAARRSLVRRVARVVDAARATTgsvrgtlaecaaerVAESRASESELLLTD-------FRAALEDDFSTPKA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 376 LKIIHELAKslnkylEGDINPGVLQEAFTIYKTLLGtFGLFEKLSLKDAALQGDKLTDELLNFLIEIRNAARKRKDFETS 455
Cdd:PRK14536 392 LSELQKLVK------DTSVPPSLCLSVLQAMDTVLG-LGLIQEATASLSAQVPAGPSEEEIGQLIEARAHARQTKDFPLA 464
|
490 500
....*....|....*....|....
gi 1491309305 456 DMIRDRLAKLDVILEDTPKGTVWK 479
Cdd:PRK14536 465 DEIRDKLKAEGIELEDTHLGTIWK 488
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
3-479 |
2.75e-128 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 386.69 E-value: 2.75e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 3 IIVRNSLTHKMEEFHPLVEGKVKMYTCGPTVYGTPHIGNYRTFFMADILRR----YFefkGFEVFHVMNITDIDDKTIRD 78
Cdd:PTZ00399 40 LKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRiledYF---GYDVFYVMNITDIDDKIIKR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 79 SAKEGLTLK-EFTEKYTKIFFKGIDWLHIKRAHIYPRATDHIQDMINWIQKLVNKGFAYVTEDGVYFAIQKFDKYGQlVN 157
Cdd:PTZ00399 117 AREEKLSIFlELARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYESNGSVYFDVEAFRKAGH-VY 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 158 LKLGKQKVGERAKADE---------YDKEHVQDFALWKKSTEEEIKrgiyYESPWGKGRPGWHIECSVMSMKYLGETFDI 228
Cdd:PTZ00399 196 PKLEPESVADEDRIAEgegalgkvsGEKRSPNDFALWKASKPGEPS----WDSPWGKGRPGWHIECSAMASNILGDPIDI 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 229 HTGAVDLKFPHHTNEIAQAEAITGKP-FVHYWIHGEFLSIKEEKMSKSLGNVTTLHQLMSSFEPDTIRYLYLSTRYDALL 307
Cdd:PTZ00399 272 HSGGIDLKFPHHDNELAQSEAYFDKHqWVNYFLHSGHLHIKGLKMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPM 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 308 VFSEDKLISAKNSVEKLRNTLENVLAVLREPTIASP--FSEQEEALLTKAHALKNEFEQVMDNNFDTPKGLKIIHELAKS 385
Cdd:PTZ00399 352 NYSDESMDEAIEKDKVFFNFFANVKIKLRESELTSPqkWTQHDFELNELFEETKSAVHAALLDNFDTPEALQALQKLISA 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 386 LNKYLEGDINP--GVLQEAFTIYKTLLGTFGLFEKLSLKDAALQGDK------LTDELLNFLIEIRNAARKRKD------ 451
Cdd:PTZ00399 432 TNTYLNSGEQPsaPLLRSVAQYVTKILSIFGLVEGSDGLGSQGQNSTsenfkpLLEALLRFRDEVRDAAKAEMKlisldk 511
|
490 500 510
....*....|....*....|....*....|....*
gi 1491309305 452 -----FETSDMIRD-RLAKLDVILEDTPKG-TVWK 479
Cdd:PTZ00399 512 kkkqlLQLCDKLRDeWLPNLGIRIEDKPDGpSVWK 546
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
15-319 |
4.66e-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: 368.62 E-value: 4.66e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 15 EFHPLVEGKVKMYTCGPTVYGTPHIGNYRTFFMADILRRYFEFKGFEVFHVMNITDIDDKTIRDSAKEGLTLKEFTEKYT 94
Cdd:pfam01406 1 FFVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 95 KIFFKGIDWLHIKRAHIYPRATDHIQDMINWIQKLVNKGFAYVTEDG-VYFAIQKFDKYGQLVNLKLGKQKVGERAKADE 173
Cdd:pfam01406 81 EAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGdVYFDVSSFPDYGKLSGQNLEQLEAGARGEVSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 174 yDKEHVQDFALWKKSTEEEIKrgiyYESPWGKGRPGWHIECSVMSMKYLGETFDIHTGAVDLKFPHHTNEIAQAEAITGK 253
Cdd:pfam01406 161 -GKRDPLDFALWKASKEGEPS----WDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFDK 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1491309305 254 PFVHYWIHGEFLSIKEEKMSKSLGNVTTLHQLMSSFEPDTIRYLYLSTRYDALLVFSEDKLISAKN 319
Cdd:pfam01406 236 QLANYWLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAKS 301
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
7-479 |
1.37e-115 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 351.16 E-value: 1.37e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 7 NSLTHKMEEFHPLVEGKVKMYTCGPTVYGTPHIGNYRTFFMADILRRYFEFKGFEVFHVMNITDIDDKTIRDSAKEGLTL 86
Cdd:PLN02946 64 NTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYLKHLGYEVRYVRNFTDVDDKIIARANELGEDP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 87 KEFTEKYTKIFFKGIDWLHIKRAHIYPRATDHIQDMINWIQKLVNKGFAYVTEDGVYFAIQKFDKYGQLVNLKLGKQKVG 166
Cdd:PLN02946 144 ISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVDGDVYFSVDKFPEYGKLSGRKLEDNRAG 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 167 ERAKADEyDKEHVQDFALWKKSTEEEIkrgiYYESPWGKGRPGWHIECSVMSMKYLGETFDIHTGAVDLKFPHHTNEIAQ 246
Cdd:PLN02946 224 ERVAVDS-RKKNPADFALWKAAKEGEP----FWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLVFPHHENEIAQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 247 AEAITGKPFVHYWIHGEFLSIKEEKMSKSLGNVTTLHQLMSSFEPDTIRYLYLSTRYDALLVFSEDKLISAKNSVEKLRN 326
Cdd:PLN02946 299 SCAACCDSNISYWIHNGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDVQLESASERIFYIYQ 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 327 TLENVLAVLREPTIASPFSEQEEALLTKAHALKNEFEQVMDNNFDTPKGLKIIHELAKSLNKYL---EGDINPGVLQEAF 403
Cdd:PLN02946 379 TLHDCEESLQQHDSTFEKDSVPPDTLNCINKFHDEFVTSMSDDLHTPVALAALSEPLKTINDLLhtrKGKKQEKRLESLA 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 404 TIYKTL---LGTFGLF-----EKL-SLKDAALQGDKLTDELLNFLIEIRNAARKRKDFETSDMIRDRLAKLDVILEDTPK 474
Cdd:PLN02946 459 ALEKKIrdvLSVLGLMptsysEALqQLREKALRRAKLTEEQVLQKIEERTVARKNKEYEKSDAIRKDLAAVGIALMDSPD 538
|
....*
gi 1491309305 475 GTVWK 479
Cdd:PLN02946 539 GTTWR 543
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
7-310 |
1.07e-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: 290.25 E-value: 1.07e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 7 NSLTHKMEEFHPLVEGKVKMYTCGPTVYGTPHIGNYRTFFMADILRRYFEFKGFEVFHVMNITDIDDKTIRDSAKEGLTL 86
Cdd:cd00672 4 NTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLGYKVRYVQNITDIDDKIIKRAREEGLSW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 87 KEFTEKYTKIFFKGIDWLHIKRAHIYPRAtdhiqdminwiqklvnkgfayvtedgvyfaiqkfdkygqlvnlklgkqkvg 166
Cdd:cd00672 84 KEVADYYTKEFFEDMKALNVLPPDVVPRV--------------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 167 erakadeydkehvqdfalwkksteeeikrgiyyespwgkgrpgWHIECSVMSMKYLGETFDIHTGAVDLKFPHHTNEIAQ 246
Cdd:cd00672 113 -------------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQ 149
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1491309305 247 AEAITGKPFVHYWIHGEFLSIKEEKMSKSLGNVTTLHQLMSSFEPDTIRYLYLSTRYDALLVFS 310
Cdd:cd00672 150 SEAATGKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
5-479 |
4.11e-94 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 299.71 E-value: 4.11e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 5 VRNSLTHKMEEFHPLVEGKVKMYTCGPTVYGTPHIGNYRTFFMADILRRYFEFKGFEVFHVMNITDIDDKTIRDSAKEGL 84
Cdd:PRK14535 230 IYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAENGE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 85 TLKEFTEKYTKIFFKGIDWLHIKRAHIYPRATDHIQDMINWIQKLVNKGFAYVTEDG-VYFAIQKFDKYGQLVNLKLGKQ 163
Cdd:PRK14535 310 TIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGdVYYAVREFAAYGQLSGKSLDDL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 164 KVGERAKADEYDKEHVqDFALWKKSTEEEIKrgiyYESPWGKGRPGWHIECSVMSMKYLGETFDIHTGAVDLKFPHHTNE 243
Cdd:PRK14535 390 RAGERVEVDGFKRDPL-DFVLWKAAKAGEPA----WESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENE 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 244 IAQAEAITGK----------------PFVHYWIHGEFLSIKEEKMSKSLGNVTTLHQLMSSFEPDTIRYLYLSTRYDALL 307
Cdd:PRK14535 465 IAQSVGATGHtcghhhaqthhgqsiaSHVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPL 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 308 VFSEDKLISAKNSVEKLRNTLENVLAVLREPTIAspfseqeealltkAHALKNEFEQVMDNNFDTPKGLKIIHELAKSLN 387
Cdd:PRK14535 545 NYSDAHLDDAKGALTRLYTTLKNTPAAEFMLSEN-------------VNDYTRRFYAAMNDDFGTVEAVAVLFELAGEVN 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 388 KYLEGDInPGVLqeaftiyKTLLGTFGLFEK--LSLKDAALQGDKLTDELLNFLIEIRNAARKRKDFETSDMIRDRLAKL 465
Cdd:PRK14535 612 KTNDAQL-AGCL-------KALGGIIGLLQRdpTEFLQGGAASDGLSNEEIEDLIARRKQARADKNWAESDRIRDLLNEH 683
|
490
....*....|....
gi 1491309305 466 DVILEDTPKGTVWK 479
Cdd:PRK14535 684 KIILEDNAGGTTWR 697
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
24-476 |
9.32e-74 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 240.52 E-value: 9.32e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 24 VKMYTCGPTVYGTPHIGNYRTFFMADILRRYFEFKGFEVFHVMNITDI----------DDKTIRDSAKEGLTLKEFTEKY 93
Cdd:PRK14534 22 VKVYACGPTVYNYAHIGNFRTYIFEDLLIKSLRLLKYNVNYAMNITDIghltgdfddgEDKVVKAARERGLTVYEISRFF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 94 TKIFFKGIDWLHIKRAHIYPRATDHIQDMINWIQKLVNKGFAYVTEDGVYFAIQKFDKYGQL--VNLKLGKQKVGERAKA 171
Cdd:PRK14534 102 TEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTYFVNGNVYFDTSCFKSYGQMagINLNDFKDMSVSRVEI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 172 DEYdKEHVQDFALW---KKSTEEEIKrgiyYESPWGKGRPGWHIECSVMSMKYLGETFDIHTGAVDLKFPHHTNEIAQAE 248
Cdd:PRK14534 182 DKS-KRNKSDFVLWftnSKFKDQEMK----WDSPWGFGYPSWHLECAAMNLEYFKSTLDIHLGGVDHIGVHHINEIAIAE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 249 AITGKPFVHYWIHGEFLSIKEEKMSKSLGNVTTLHQLMS-SFEPDTIRYLYLSTRYDALLVFSEDKLISAKNSVEKLRNT 327
Cdd:PRK14534 257 CYLNKKWCDMFVHGEFLIMEYEKMSKSNNNFITIKDLEDqGFSPLDFRYFCLTAHYRTQLKFTFNNLKACKIARENMLNK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 328 LENVLAVLREPTIASPFSEQEEALLTKAHALKNEFEQVMDNNFDTPKGLKIIHELAKSLNkylegdinpgvlqeaFTIYK 407
Cdd:PRK14534 337 LTYFYSSLDQFDLNLLNKDLENIEFSLEKEYYDSFLEKIAFDLNIPQGLALLWDIIKDDN---------------LSFLS 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491309305 408 TLLGTFGLFEKLS--LKDAALQ----GDKLTDELLNFLIEIRNAARKRKDFETSDMIRDRLAKLDVILEDTPKGT 476
Cdd:PRK14534 402 KLRLAFKFDEVLSlgLREEILReienHRIVIDDNMKSLIEERRLAKCEKDFKRADEIREYFASKGFVLIDTEEGT 476
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
24-411 |
8.77e-54 |
|
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: 186.08 E-value: 8.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 24 VKMYTCGPTVYGTPHIGNYRTFFMADILRRYFEFKGFEVFHVMNITDIDDKTIRDSAKEGLTLKEFTEKYTKIFFKGIDW 103
Cdd:TIGR03447 37 AGMYVCGITPYDATHLGHAATYLTFDLVNRVWRDAGHRVHYVQNVTDVDDPLFERAERDGVDWRELGTSQIDLFREDMEA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 104 LHIKRAHIYPRATDHIQDMINWIQKLVNKGFAYVTEDG----VYFAIQKFDKYGQLVNL--KLGKQKVGERA-KADEYDK 176
Cdd:TIGR03447 117 LRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYIVEGPeypdVYFSIDATEQFGYESGYdrATMLELFAERGgDPDRPGK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 177 EHVQDFALWKKSTEEEIKrgiyYESPWGKGRPGWHIECSVMSMKYLGETFDIHTGAVDLKFPHHTNEIAQAEAITG-KPF 255
Cdd:TIGR03447 197 RDPLDALLWRAAREGEPS----WDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSDLIFPHHEFSAAHAEAATGvRRM 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 256 VHYWIHGEFLSIKEEKMSKSLGNVTTLHQLMSS-FEPDTIRYLYLSTRYDALLVFSEDKLISAKNSveklrntlenvLAV 334
Cdd:TIGR03447 273 ARHYVHAGMIGLDGEKMSKSLGNLVFVSKLRAAgVDPAAIRLGLLAGHYRQDRDWTDAVLAEAEAR-----------LAR 341
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1491309305 335 LREPTIASPFSEqeealltkAHALKNEFEQVMDNNFDTPKGLKIIHELAKSLNKYLEGDIN-PGVLQEAFtiyKTLLG 411
Cdd:TIGR03447 342 WRAALALPDAPD--------ATDLIARLRQHLANDLDTPAALAAVDGWAADALSYGGSDTEaPALVATAV---DALLG 408
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
22-314 |
6.58e-49 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 172.04 E-value: 6.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 22 GKVKMYTCGPTVYGTPHIGNYRTFFMADILRRYFEFKGFEVFHVMNITDIDDKTIRDSAKEGLTLKEFTEKYTKIFFKGI 101
Cdd:PRK12418 8 GTATMYVCGITPYDATHLGHAATYLAFDLVNRVWRDAGHDVHYVQNVTDVDDPLLERAARDGVDWRDLAEREIALFREDM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 102 DWLHIKRAHIYPRATDHIQDMINWIQKLVNKGFAYVTEDG----VYFAIQKFDKYGQLVN------LKLGKQKVG--ERA 169
Cdd:PRK12418 88 EALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYVVDDEeypdVYFSVDATPQFGYESGydratmLELFAERGGdpDRP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 170 kadeyDKEHVQDFALWKKSTEEEIKrgiyYESPWGKGRPGWHIECSVMSMKYLGETFDIHTGAVDLKFPHHTNEIAQAEA 249
Cdd:PRK12418 168 -----GKRDPLDALLWRAARPGEPS----WPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAHAEA 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1491309305 250 ITG-KPFVHYWIHGEFLSIKEEKMSKSLGNVTTLHQLMSS-FEPDTIRYLYLSTRY-------DALLVFSEDKL 314
Cdd:PRK12418 239 ATGeRRFARHYVHAGMIGLDGEKMSKSRGNLVFVSRLRAAgVDPAAIRLALLAGHYradrewtDAVLAEAEARL 312
|
|
| Anticodon_Ia_Cys |
cd07963 |
Anticodon-binding domain of cysteinyl tRNA synthetases; This domain is found in cysteinyl tRNA ... |
311-478 |
6.84e-25 |
|
Anticodon-binding domain of cysteinyl tRNA synthetases; This domain is found in cysteinyl tRNA synthetases (CysRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. CysRS catalyzes the transfer of cysteine to the 3'-end of its tRNA.
Pssm-ID: 153417 [Multi-domain] Cd Length: 156 Bit Score: 100.33 E-value: 6.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 311 EDKLISAKNSVEKLRNTLENVLAVLREPTIASPFSEQeealltkahalkneFEQVMDNNFDTPKGLKIIHELAKSLNKYL 390
Cdd:cd07963 1 DDNLEDARAALERLYTALRGVPPTTVDIDWGEPFAER--------------FIAAMDDDFNTPEALAVLFELAREINRLK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 391 EGDINPGVlQEAFTIyKTLLGTFGLFEKLSlkDAALQGD----KLTDELLNFLIEIRNAARKRKDFETSDMIRDRLAKLD 466
Cdd:cd07963 67 KEDIEKAA-ALAALL-KALGGVLGLLQQDP--EAFLQGGtgegGLSVAEIEALIAQRNQARKAKDWAEADRIRDELAAQG 142
|
170
....*....|..
gi 1491309305 467 VILEDTPKGTVW 478
Cdd:cd07963 143 IILEDSPEGTTW 154
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
26-151 |
1.28e-15 |
|
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: 73.67 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 26 MYTCGPTVYGTPHIGNYRTFFMADILRRYFEFKGFEVFHVMNITDIDDKTIRDSAKEGLTLKEFTEKYTKIFFKGIDWL- 104
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKEDVEYMf 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491309305 105 ---------HIKRAHIYPRATDHIQDMINWIQKLVNKGFAYVTEDGVYFAIQKFDK 151
Cdd:cd00802 81 lqaadflllYETECDIHLGGSDQLGHIELGLELLKKAGGPARPFGLTFGRVMGADG 136
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
28-301 |
7.28e-14 |
|
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: 72.45 E-value: 7.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 28 TCG-PTVYGTPHIGNYRTFFMADILRRYFEFKGFEVFHVMNiTD--------------IDDKTIRDSAKEGLTLKEFTEK 92
Cdd:cd00668 5 TTPpPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPG-WDthglpielkaerkgGRKKKTIWIEEFREDPKEFVEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 93 YTKIF---FKGI----DWlhiKRAHI--YPRATDHIQdminWI-QKLVNKGFAYVTEDGVYFAIQKFDKYGQLvnlklgK 162
Cdd:cd00668 84 MSGEHkedFRRLgisyDW---SDEYIttEPEYSKAVE----LIfSRLYEKGLIYRGTHPVRITEQWFFDMPKF------K 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 163 QKVGERAKADEYDKEHVQD-FALWKKSTEE-EIKRGIYyespWGKGRPGWHIEC-------SVMSMKYLGETF------- 226
Cdd:cd00668 151 EKLLKALRRGKIVPEHVKNrMEAWLESLLDwAISRQRY----WGTPLPEDVFDVwfdsgigPLGSLGYPEEKEwfkdsyp 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1491309305 227 -DIHTGAVDLKFPHHTNEIAQAEAITGK-PFVHYWIHGEFLSIKEEKMSKSLGNVTTLHQLMSSFEPDTIRYLYLST 301
Cdd:cd00668 227 aDWHLIGKDILRGWANFWITMLVALFGEiPPKNLLVHGFVLDEGGQKMSKSKGNVIDPSDVVEKYGADALRYYLTSL 303
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
255-391 |
4.50e-12 |
|
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: 68.22 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 255 FVHywihgEFLSIKEEKMSKSLGNVTTLHQLMSSFEPDTIRYLYLSTR-YDALLVFSEDKLISAKNS--VEKLRNTLENV 331
Cdd:COG0143 316 FAH-----GFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVpFGQDGDFSWEDFVARVNSdlANDLGNLASRT 390
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1491309305 332 LA--------VLREPtiaSPFSEQEEALLTKAHALKNEFEQVMDnNFDTPKGLKIIHELAKSLNKYLE 391
Cdd:COG0143 391 LSmihkyfdgKVPEP---GELTEADEELLAEAEAALEEVAEAME-AFEFRKALEEIMALARAANKYID 454
|
|
| DALR_2 |
smart00840 |
This DALR domain is found in cysteinyl-tRNA-synthetases; |
361-416 |
3.58e-11 |
|
This DALR domain is found in cysteinyl-tRNA-synthetases;
Pssm-ID: 214848 [Multi-domain] Cd Length: 56 Bit Score: 58.35 E-value: 3.58e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491309305 361 EFEQVMDNNFDTPKGLKIIHELAKSLNKYLEGDINPGVLQEAFTIYKTLLGTFGLF 416
Cdd:smart00840 1 RFEEAMDDDFNTPEALAVLFELAREINRLALKATDAEELAALAALLRALGGVLGLL 56
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
255-390 |
4.99e-11 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 64.90 E-value: 4.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 255 FVHYWIHgeflsIKEEKMSKSLGNVTTLHQLMSSFEPDTIRYLYLST-RYDALLVFSEDKLISAKNSVekLRNTLENVL- 332
Cdd:PRK11893 288 FAHGFLT-----LDGEKMSKSLGNVIDPFDLVDEYGVDAVRYFLLREiPFGQDGDFSREAFINRINAD--LANDLGNLAq 360
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 333 -----------AVLREPTIaspFSEQEEALLTKAHALKNEFEQVMDN-NFDtpKGLKIIHELAKSLNKYL 390
Cdd:PRK11893 361 rtlsmiaknfdGKVPEPGA---LTEADEALLEAAAALLERVRAAMDNlAFD--KALEAILALVRAANKYI 425
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
28-332 |
3.00e-10 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 61.92 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 28 TCG-PTVYGTPHIGNYRTFFMADILRRYFEFKGFEVFHVMNiTDIDDKTIRDSA-KEGLTLKEFTEKYTKIFFKGIDWLH 105
Cdd:pfam09334 4 TTAlPYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCG-TDEHGTPIELKAeKEGITPEELVDRYHEIHREDFKKFN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 106 IKRAHiYPRATD--HIQDMINWIQKLVNKGFAYVTEDGVYF--AIQKF--DKY--GQLVNLKlgkqkvGERAKADEYDK- 176
Cdd:pfam09334 83 ISFDD-YGRTTSerHHELVQEFFLKLYENGYIYEKEIEQFYcpSDERFlpDRYveGTCPHCG------SEDARGDQCENc 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 177 -EHVQDF-------ALWKKSTEEEIKRGIYYESP--------W-GKGRPGWHIECSVMSMKYLGE-------TFDIHTGa 232
Cdd:pfam09334 156 gRHLEPTelinpkcVICGTTPEVKETEHYFFDLSkfqdklreWiEENNPEWPENVKNMVLEWLKEglkdraiSRDLDWG- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 233 vdLKFPHHTNE------------IAQAEAITGKP--FVHYW--------IH----------------------------- 261
Cdd:pfam09334 235 --IPVPGAEGKvfyvwldapigyISATKELSGNEekWKEWWpndpdtelVHfigkdiiyfhtifwpamllgagyrlpttv 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491309305 262 --GEFLSIKEEKMSKSLGNVTTLHQLMSSFEPDTIRYlYLStrydALLVFSEDKLISAKNSVEKLRNTLENVL 332
Cdd:pfam09334 313 faHGYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRY-YLA----RNRPETKDTDFSWEDFVERVNSELADDL 380
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
28-302 |
1.54e-09 |
|
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: 59.08 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 28 TCG-PTVYGTPHIGNYRTFFMADILRRYFEFKGFEVFHVMNiTD-----IDDKTIrdsaKEGLTLKEFTEKYTKIFFKGI 101
Cdd:cd00814 5 TTAlPYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTG-TDehgtkIEQKAE----EEGVTPQELCDKYHEIFKDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 102 DWLHIKRAHiYPRATD--HIQDMINWIQKLVNKGF--------AYVTEDGVYFAIQK-----FdkygqlvnLKLGKQKvg 166
Cdd:cd00814 80 KWLNISFDY-FIRTTSprHKEIVQEFFKKLYENGYiyegeyegLYCVSCERFLPEWReeehyF--------FRLSKFQ-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 167 erakadEYDKEHVQD--FALW----KKSTEEEIKRGIY------YESPWG------------------------KGRPGW 210
Cdd:cd00814 149 ------DRLLEWLEKnpDFIWpenaRNEVLSWLKEGLKdlsitrDLFDWGipvpldpgkviyvwfdaligyisaTGYYNE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 211 HIECSVMSMKYLGETF-----DIhtgavdlkFPHHT-----NEIAQAEAITGKPFVHywihgEFLSIKEEKMSKSLGNVT 280
Cdd:cd00814 223 EWGNSWWWKDGWPELVhfigkDI--------IRFHAiywpaMLLGAGLPLPTRIVAH-----GYLTVEGKKMSKSRGNVV 289
|
330 340
....*....|....*....|..
gi 1491309305 281 TLHQLMSSFEPDTIRYLYLSTR 302
Cdd:cd00814 290 DPDDLLERYGADALRYYLLRER 311
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
255-389 |
1.48e-08 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 57.12 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 255 FVHYWihgefLSIKEEKMSKSLGNVTTLHQLMSSFEPDTIRYlylstrydALL---------VFSEDKLISAKNSveKLR 325
Cdd:PRK12267 288 FAHGW-----WLMKDGKMSKSKGNVVDPEELVDRYGLDALRY--------YLLrevpfgsdgDFSPEALVERINS--DLA 352
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1491309305 326 NTLENVL------------AVLREPTIASPFseqEEALLTKAHALKNEFEQVMDnNFDTPKGLKIIHELAKSLNKY 389
Cdd:PRK12267 353 NDLGNLLnrtvaminkyfdGEIPAPGNVTEF---DEELIALAEETLKNYEELME-ELQFSRALEEVWKLISRANKY 424
|
|
| DALR_2 |
pfam09190 |
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases. |
361-418 |
1.25e-07 |
|
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases.
Pssm-ID: 462711 [Multi-domain] Cd Length: 63 Bit Score: 48.35 E-value: 1.25e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1491309305 361 EFEQVMDNNFDTPKGLKIIHELAKSLNKYLEGDiNPGVLQEAFTIYKTLLGTFGLFEK 418
Cdd:pfam09190 1 KFIEAMDDDFNTPEALAVLFELAKEINRALKTN-DAEAAAALAALLRELGDVLGLLQQ 57
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
35-299 |
2.43e-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: 52.25 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 35 GTPHIGNYRTFFMADILRRYFEFKGFEVFHVMN-------ITDIDDKTIRDSAKeglTLKEFTEKYTKIFFKG---IDWl 104
Cdd:cd00812 13 GALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGfdafglpAENAAIKIGRDPED---WTEYNIKKMKEQLKRMgfsYDW- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 105 HIKRAHIYPRATDHIQdminWI-QKLVNKGFAYVTEDGVYFAI---QKFDKYGQlvnlKLGKQKVGERAKADEYDKEHV- 179
Cdd:cd00812 89 RREFTTCDPEYYKFTQ----WLfLKLYEKGLAYKKEAPVNWCKlldQWFLKYSE----TEWKEKLLKDLEKLDGWPEEVr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 180 QDFALWKksteeEIKRGIYyespWGKGRP-GWHIECSVMSMKY--------------------LGETF------DIHTGA 232
Cdd:cd00812 161 AMQENWI-----GCSRQRY----WGTPIPwTDTMESLSDSTWYyarytdahnleqpyegdlefDREEFeywypvDIYIGG 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491309305 233 VDLKFPH------HTNEIAQAEAITGKPFVHYWIHGeFLSIKEEKMSKSLGNVTTLHQLMSSFEPDTIRyLYL 299
Cdd:cd00812 232 KEHAPNHllysrfNHKALFDEGLVTDEPPKGLIVQG-MVLLEGEKMSKSKGNVVTPDEAIKKYGADAAR-LYI 302
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
244-326 |
3.54e-06 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 49.81 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 244 IAQAEAITG-KPFVHYWIHGEFLSIKEEKMSKSLGNVTTLHQLMSSFEPDTIRYLYLSTR--YDAllVFSEDKLISAKNS 320
Cdd:PRK13208 505 ILRAYLLTGkLPWKNIMISGMVLDPDGKKMSKSKGNVVTPEELLEKYGADAVRYWAASARlgSDT--PFDEKQVKIGRRL 582
|
....*.
gi 1491309305 321 VEKLRN 326
Cdd:PRK13208 583 LTKLWN 588
|
|
| LysRS_core_class_I |
cd00674 |
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) ... |
25-302 |
7.81e-06 |
|
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: 48.09 E-value: 7.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 25 KMYTC--GPTVYGTPHIGNYRTFFMADILRRYFEFKGFEVFHVMNITDIDD-----KTIRDSAKE--GLTL--------- 86
Cdd:cd00674 19 EKYVVasGISPSGHIHIGNFREVITADLVARALRDLGFEVRLIYSWDDYDRlrkvpPNVPESYEQyiGMPLssvpdpfgc 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 87 -KEFTEKYTKIFFKGIDWLHIKRAHIYprATDHIQDminwiqklvnkgfayvtedGVY-----FAIQKFDKYGQLVNLKL 160
Cdd:cd00674 99 cESYAEHFERPFEESLEKLGIEVEFIS--QSQMYKS-------------------GLYdenilIALEKRDEIMAILNEYR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 161 GKQK---------VGERAKADEYDKEHVqDFALWKKSTEEEIKRGIYYESPWGKGRPGWHIECSvMSMKYLGETFDihTG 231
Cdd:cd00674 158 GRELqetwypfmpYCEKCGKDTTTVEAY-DAKAGTVTYKCECGHEETVDIRTGRGKLTWRVDWP-MRWAILGVDFE--PF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 232 AVDlkfpHHTN--------EIAqaEAITGKPFVHYWIHgEFLSIK-EEKMSKSLGNVTTLHQLMSSFEPDTIRYLYLSTR 302
Cdd:cd00674 234 GKD----HASAggsydtgkEIA--REIFGGEPPVPVMY-EFIGLKgGGKMSSSKGNVITPSDWLEVAPPEVLRYLYARRK 306
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
261-391 |
1.27e-04 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 44.70 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 261 HGeFLSIKEEKMSKSLGNVTTLHQLMSSFEPDTIRYLYL-STRYDALLVFSEDKLISAKNSveKLRNTLENVL------- 332
Cdd:PLN02224 357 HG-FLTKDGMKMGKSLGNTLEPFELVQKFGPDAVRYFFLrEVEFGNDGDYSEDRFIKIVNA--HLANTIGNLLnrtlgll 433
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1491309305 333 ------AVLREPTIAS---PFSEQEEALLTKAhalKNEFEqvmdnNFDTPKGLKIIHELAKSLNKYLE 391
Cdd:PLN02224 434 kkncesTLVEDSTVAAegvPLKDTVEKLVEKA---QTNYE-----NLSLSSACEAVLEIGNAGNTYMD 493
|
|
| tRNA-synt_1f |
pfam01921 |
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from ... |
30-302 |
1.52e-04 |
|
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from prokaryotes.
Pssm-ID: 396483 Cd Length: 357 Bit Score: 43.79 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 30 GPTVYGTPHIGNYRTFFMADILRRYFEFKGFEVFHVMNITDIDD-KTIRDSAKEGLTLKEFTEK-YTKI----------- 96
Cdd:pfam01921 27 GISPSGLPHIGNFREVLRTDAVRRALRKRGFEVRLIAFSDDMDGlRKVPDNVPNSEMLEKYLGKpLTRIpdpfgchesya 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 97 ------FFKGIDWLHIKRAHIypRATDhiqdminwiqkLVNKGfayVTEDGVYFAIQKFDKYGQLVNLKLGKQK------ 164
Cdd:pfam01921 107 ehfnapFREFLDRFGIEYEFI--SATE-----------LYKSG---LYDEAIKIALENRDEIMEILNPYRGEERqetysp 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 165 ---VGER------AKADEYDKEHVQDFALWKKSTEEEIKrgiyYESPWGKgrPGWHIECSvMSMKYLGETF-----DIHT 230
Cdd:pfam01921 171 ylpICPKcgrvltTPVVEYDEGGTIRYRCDECGHEGEVD----IRGGNGK--LQWKVDWA-MRWAALGVDFepfgkDHAA 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491309305 231 --GAVDLkfphhTNEIAQaEAITGKPFVHYWIhgEFLSIKE-EKMSKSLGNVTTLHQLMSSFEPDTIRYLYLSTR 302
Cdd:pfam01921 244 pgGSYDT-----SSRIAD-EIFGGEPPEGFPY--ELILLKGgGKMSSSKGNVITPEDWLEYAPPESLRFLMFRTK 310
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
271-381 |
2.19e-04 |
|
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: 43.92 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 271 KMSKSLGNVTTLHQLMSSFEPDTIRYLYLSTRYDALLVFSEDKLisaKNSVE---KLRNTLENVLAVL---REPTIASPF 344
Cdd:COG0060 603 KMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEIL---KEVRDvyrRLRNTYRFLLANLddfDPAEDAVPY 679
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1491309305 345 SEQEEA---LLTKAHALKNEFEQVMDnNFDTPKGLKIIHE 381
Cdd:COG0060 680 EDLPELdrwILSRLNELIKEVTEAYD-NYDFHRAYRALHN 718
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
264-413 |
5.37e-04 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 42.55 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 264 FLSIKEEKMSKSLGNVTTLHQLMSSFEPDTIR-YLYLSTRYDALLVFSEDKLISAKNSVEKLRNTLENVLAVLREPTIAS 342
Cdd:PRK12300 570 FVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRlYLTSSAELLQDADWREKEVESVRRQLERFYELAKELIEIGGEEELRF 649
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1491309305 343 PfseqEEALLTKAHALKNEFEQVMDnNFDTPKGLKIIH-ELAKSLNKYLE--GDINPGVLQEAFTIYKTLLGTF 413
Cdd:PRK12300 650 I----DKWLLSRLNRIIKETTEAME-SFQTRDAVQEAFyELLNDLRWYLRrvGEANNKVLREVLEIWIRLLAPF 718
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
28-106 |
1.66e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 40.91 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 28 TCG-PTVYGTPHIGNYRTFFMADILRRYFEFKGFEVFHV----MNITDIddkTIRdSAKEGLTLKEFTEKYTKIFFKGID 102
Cdd:PRK00133 7 TCAlPYANGPIHLGHLVEYIQADIWVRYQRMRGHEVLFVcaddAHGTPI---MLK-AEKEGITPEELIARYHAEHKRDFA 82
|
....
gi 1491309305 103 WLHI 106
Cdd:PRK00133 83 GFGI 86
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
249-368 |
1.99e-03 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 40.91 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 249 AITGK-PFVHYWIHGEFLSIKEEKMSKSLGNVTTLHQLM-----SSFEP----DTIRYLYLSTRYdallvfSEDKLISAK 318
Cdd:PLN02843 588 ATKGKaPYKSVLTHGFVLDEKGFKMSKSLGNVVDPRLVIeggknQKQEPaygaDVLRLWVASVDY------TGDVLIGPQ 661
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491309305 319 ------NSVEKLRNTLENVLAVLR--EPTIASPFSEQ---EEALLTKAHALKNEFEQVMDN 368
Cdd:PLN02843 662 ilkqmsDIYRKLRGTLRYLLGNLHdwKPDNAVPYEDLpsiDKYALFQLENVVNEIEESYDN 722
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
255-390 |
3.67e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 39.75 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 255 FVHywihgEFLSIKEEKMSKSLGNVTTLHQLMSSFEPDTIRYlYLSTRY-----DalLVFSEDKLISAKNSveKLRNTLE 329
Cdd:PRK00133 318 FAH-----GFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRY-YLAAKLpetidD--LDFNWEDFQQRVNS--ELVGKVV 387
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491309305 330 NvlavlreptIAS--------------PFSEQEEALLTKAHALKNEFEQVMDnNFDTPKGLKIIHELAKSLNKYL 390
Cdd:PRK00133 388 N---------FASrtagfinkrfdgklPDALADPELLEEFEAAAEKIAEAYE-AREFRKALREIMALADFANKYV 452
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
244-372 |
4.92e-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: 39.66 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 244 IAQAEAITGK-PFVHYWIHGEFLSIKEEKMSKSLGNVTTLHQLMSSFEPDTIRYL---YLSTRYDalLVFSEDKLISAKN 319
Cdd:TIGR00422 497 IFRSLALTGQvPFKEVYIHGLVRDEQGRKMSKSLGNVIDPLDVIEKYGADALRFTlasLVTPGDD--INFDWKRVESARN 574
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1491309305 320 SVEKLRNTLENVLAVLREPTIAS----PFSEQEEALLTKAHALKNEFEQVMDN-NFDT 372
Cdd:TIGR00422 575 FLNKLWNASRFVLMNLSDDLELSggeeKLSLADRWILSKLNRTIKEVRKALDKyRFAE 632
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
251-394 |
9.76e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 38.77 E-value: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 251 TGK-PFVHYWIHGEFLSIKEEKMSKSLGNVTTLHQLMSSFEPDTIRYLYLSTRYDALLVFSEDKLISAKNSVEKLRNTLE 329
Cdd:PLN02943 562 TGTvPFSYVYLHGLIRDSQGRKMSKTLGNVIDPLDTIKEFGTDALRFTLALGTAGQDLNLSTERLTSNKAFTNKLWNAGK 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491309305 330 NVLAVLREPTIASPfseqeealltkahalkneFEQVMDNNFDTPKGL-----------KIIHEL----AKSLNKYLEGDI 394
Cdd:PLN02943 642 FVLQNLPSQSDTSA------------------WEHILACKFDKEESLlslplpecwvvSKLHELidsvTTSYDKYFFGDV 703
|
|
| |
