|
Name |
Accession |
Description |
Interval |
E-value |
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
7-497 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 914.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 7 EELNDQQIVRREKMAALAEQGIDPFGKRFDRTTNSGELKEKYSDKTKEDLQELQATAIIAGRLMTKRGKGKVGFAHLQDR 86
Cdd:PRK00484 1 EELNEQIAVRREKLAELREQGIDPYPNKFERTHTAAELRAKYDDKEKEELEELEIEVSVAGRVMLKRVMGKASFATLQDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 87 QGQIQIYVRKDSVGDDNYDIFKKADLGDFIGVEGDIMCTDMGELSIKATKLTHLSKSLRPLPEKFHGLTDIETIYRKRHL 166
Cdd:PRK00484 81 SGRIQLYVSKDDVGEEALEAFKKLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLPDKFHGLTDVETRYRQRYV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 167 DLISNRSSFERFITRSKMISEIRRYLDGLGFLEVETPVLHNEAGGAAARPFITHHNAQDIDMVLRIAPELHLKRLIVGGM 246
Cdd:PRK00484 161 DLIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLIVGGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 247 ERVYEIGRIFRNEGMDATHNPEFTSIEVYEAYADYLDMMTLTEGIIQHAAKAVKGEGPIDYQGTEIKLHEPFRRVHMVDA 326
Cdd:PRK00484 241 ERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTYQGTEIDFGPPFKRLTMVDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 327 IKEVTGIDFWpEMTFEEATALANEKHVPVEKHFTsVGHIINAFFEAFVEDTLIQPTFVYGHPVEVSPLAKKNPEDSRFTD 406
Cdd:PRK00484 321 IKEYTGVDFD-DMTDEEARALAKELGIEVEKSWG-LGKLINELFEEFVEPKLIQPTFITDYPVEISPLAKRHREDPGLTE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 407 RFELFIMTKEYANAFTELNDPIDQLSRFKAQAAAKELGDDEATGIDYDFVEALEYGMPPTGGLGIGIDRLCMLLTNTTTI 486
Cdd:PRK00484 399 RFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSI 478
|
490
....*....|.
gi 501964611 487 RDVLLFPTMKP 497
Cdd:PRK00484 479 RDVILFPLMRP 489
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
1-497 |
0e+00 |
|
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA synthetase (class II) is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440803 [Multi-domain] Cd Length: 495 Bit Score: 888.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 1 MSNQhiEELNDQQIVRREKMAALAEQGIDPFGKRFDRTTNSGELKEKYSDKTKEDlqELQATAIIAGRLMTKRGKGKVGF 80
Cdd:COG1190 1 MSEE--EDLNEQIRVRREKLEELREAGIDPYPNKFPRTHTAAEIREKYDELEAEE--ETGDEVSVAGRIMAKRDMGKASF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 81 AHLQDRQGQIQIYVRKDSVGDDNYDIFKKADLGDFIGVEGDIMCTDMGELSIKATKLTHLSKSLRPLPEKFHGLTDIETI 160
Cdd:COG1190 77 ADLQDGSGRIQLYLRRDELGEEAYELFKLLDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDPETR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 161 YRKRHLDLISNRSSFERFITRSKMISEIRRYLDGLGFLEVETPVLHNEAGGAAARPFITHHNAQDIDMVLRIAPELHLKR 240
Cdd:COG1190 157 YRQRYVDLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 241 LIVGGMERVYEIGRIFRNEGMDATHNPEFTSIEVYEAYADYLDMMTLTEGIIQHAAKAVKGEGPIDYQGTEIKLHEPFRR 320
Cdd:COG1190 237 LIVGGFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTYQGQEIDLSPPWRR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 321 VHMVDAIKEVTGIDFWPEMTFEEATALANEKHVPVEKHFTsVGHIINAFFEAFVEDTLIQPTFVYGHPVEVSPLAKKNPE 400
Cdd:COG1190 317 ITMVEAIKEATGIDVTPLTDDEELRALAKELGIEVDPGWG-RGKLIDELFEELVEPKLIQPTFVTDYPVEVSPLAKRHRD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 401 DSRFTDRFELFIMTKEYANAFTELNDPIDQLSRFKAQAAAKELGDDEATGIDYDFVEALEYGMPPTGGLGIGIDRLCMLL 480
Cdd:COG1190 396 DPGLTERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGIDRLVMLL 475
|
490
....*....|....*..
gi 501964611 481 TNTTTIRDVLLFPTMKP 497
Cdd:COG1190 476 TDSPSIRDVILFPLMRP 492
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
8-497 |
0e+00 |
|
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the lysyl-tRNA synthetases that are class II amino-acyl tRNA synthetases. It includes all eukaryotic and most bacterial examples of the enzyme, but not archaeal or spirochete forms. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273107 [Multi-domain] Cd Length: 493 Bit Score: 702.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 8 ELNDQQIVRREKMAALAEQGIDPFGKRFDRTTNSGELKEKYSDKTKEDLQELQATAIIAGRLMTKRGKGKVGFAHLQDRQ 87
Cdd:TIGR00499 1 ELNDQAQQRLEKLNRLRQTGNNPYLHKFERTHSAQEFQEKYADLSNEELKEKELKVSIAGRIKAIRSMGKATFITLQDES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 88 GQIQIYVRKDSVGDDNYDIFKK-ADLGDFIGVEGDIMCTDMGELSIKATKLTHLSKSLRPLPEKFHGLTDIETIYRKRHL 166
Cdd:TIGR00499 81 GQIQLYVNKNKLPEDFYEFDEYlLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQETRYRQRYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 167 DLISNRSSFERFITRSKMISEIRRYLDGLGFLEVETPVLHNEAGGAAARPFITHHNAQDIDMVLRIAPELHLKRLIVGGM 246
Cdd:TIGR00499 161 DLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKRLIVGGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 247 ERVYEIGRIFRNEGMDATHNPEFTSIEVYEAYADYLDMMTLTEGIIQHAAKAVKGEGPIDYQGTEIKLHEPFRRVHMVDA 326
Cdd:TIGR00499 241 EKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINYNDLEIDLKPPWKRITMVDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 327 IKEVTGIDFWPEMTFEEATALANEKHVPVEKHFTSVGHIINAFFEAFVEDTLIQPTFVYGHPVEVSPLAKKNPEDSRFTD 406
Cdd:TIGR00499 321 LEMVTGIDFDILKDDETAKALAKEHGIEVAEDSLTLGHILNKFFEQFLEHTLIQPTFITHYPAEISPLAKRDPSNPEFTE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 407 RFELFIMTKEYANAFTELNDPIDQLSRFKAQAAAKELGDDEATGIDYDFVEALEYGMPPTGGLGIGIDRLCMLLTNTTTI 486
Cdd:TIGR00499 401 RFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGIGIDRLVMLLTDAPSI 480
|
490
....*....|.
gi 501964611 487 RDVLLFPTMKP 497
Cdd:TIGR00499 481 RDVLLFPQLRP 491
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
7-497 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 646.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 7 EELNDQQI--VRREKMAALAEQGIDPFGKRFDRTTNSGELKEKYSDKtkEDLQELQATAI-IAGRLMTKRGKGKVGFAHL 83
Cdd:PLN02502 54 ETMDPTQYraNRLKKVEALRAKGVEPYPYKFDVTHTAPELQEKYGSL--ENGEELEDVSVsVAGRIMAKRAFGKLAFYDL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 84 QDRQGQIQIYVRKDSVGDDNyDIFKK----ADLGDFIGVEGDIMCTDMGELSIKATKLTHLSKSLRPLPEKFHGLTDIET 159
Cdd:PLN02502 132 RDDGGKIQLYADKKRLDLDE-EEFEKlhslVDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLPDKYHGLTDQET 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 160 IYRKRHLDLISNRSSFERFITRSKMISEIRRYLDGLGFLEVETPVLHNEAGGAAARPFITHHNAQDIDMVLRIAPELHLK 239
Cdd:PLN02502 211 RYRQRYLDLIANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRIATELHLK 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 240 RLIVGGMERVYEIGRIFRNEGMDATHNPEFTSIEVYEAYADYLDMMTLTEGIIQHAAKAVKGEGPIDYQGTEIKLHEPFR 319
Cdd:PLN02502 291 RLVVGGFERVYEIGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYHGIEIDFTPPFR 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 320 RVHMVDAIKEVTGIDFWPEMTFEEATAL---ANEKHVPVEKHFTSVGHIINAFFEAFVEDTLIQPTFVYGHPVEVSPLAK 396
Cdd:PLN02502 371 RISMISLVEEATGIDFPADLKSDEANAYliaACEKFDVKCPPPQTTGRLLNELFEEFLEETLVQPTFVLDHPVEMSPLAK 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 397 KNPEDSRFTDRFELFIMTKEYANAFTELNDPIDQLSRFKAQAAAKELGDDEATGIDYDFVEALEYGMPPTGGLGIGIDRL 476
Cdd:PLN02502 451 PHRSKPGLTERFELFINGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRL 530
|
490 500
....*....|....*....|.
gi 501964611 477 CMLLTNTTTIRDVLLFPTMKP 497
Cdd:PLN02502 531 VMLLTDSASIRDVIAFPAMKP 551
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
171-497 |
0e+00 |
|
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a lysine to the 3' OH group of ribose of the appropriate tRNA. Its assignment to class II aaRS is based upon its structure and the presence of three characteristic sequence motifs in the core domain. It is found in eukaryotes as well as some prokaryotes and archaea. However, LysRS belongs to class I aaRS's in some prokaryotes and archaea. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.
Pssm-ID: 238398 [Multi-domain] Cd Length: 329 Bit Score: 547.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 171 NRSSFERFITRSKMISEIRRYLDGLGFLEVETPVLHNEAGGAAARPFITHHNAQDIDMVLRIAPELHLKRLIVGGMERVY 250
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 251 EIGRIFRNEGMDATHNPEFTSIEVYEAYADYLDMMTLTEGIIQHAAKAVKGEGPIDYQGTEIKLHEPFRRVHMVDAIKEV 330
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEYGGKELDFTPPFKRVTMVDALKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 331 TGIDFWP---EMTFEEATALANEKHVPVEKHFTSvGHIINAFFEAFVEDTLIQPTFVYGHPVEVSPLAKKNPEDSRFTDR 407
Cdd:cd00775 161 TGIDFPEldlEQPEELAKLLAKLIKEKIEKPRTL-GKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRHRSNPGLTER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 408 FELFIMTKEYANAFTELNDPIDQLSRFKAQAAAKELGDDEATGIDYDFVEALEYGMPPTGGLGIGIDRLCMLLTNTTTIR 487
Cdd:cd00775 240 FELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTDSNSIR 319
|
330
....*....|
gi 501964611 488 DVLLFPTMKP 497
Cdd:cd00775 320 DVILFPAMRP 329
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
9-497 |
4.15e-165 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 495.64 E-value: 4.15e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 9 LNDQQIVRREKMAALAEQGIDPFGKRFDRTTNSGELKEKYSDktkedlqelqATAIIAGRLMTKRGKGKVGFAHLQDRQG 88
Cdd:PRK02983 610 LPEQVRVRLAKLEALRAAGVDPYPVGVPPTHTVAEALDAPTG----------EEVSVSGRVLRIRDYGGVLFADLRDWSG 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 89 QIQIYVRKDSVGDDNYDIFKKA-DLGDFIGVEGDIMCTDMGELSIKATKLTHLSKSLRPLPEKFHGLTDIETIYRKRHLD 167
Cdd:PRK02983 680 ELQVLLDASRLEQGSLADFRAAvDLGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLD 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 168 LISNRSSFERFITRSKMISEIRRYLDGLGFLEVETPVLHNEAGGAAARPFITHHNAQDIDMVLRIAPELHLKRLIVGGME 247
Cdd:PRK02983 760 LAVNPEARDLLRARSAVVRAVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVE 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 248 RVYEIGRIFRNEGMDATHNPEFTSIEVYEAYADYLDMMTLTEGIIQHAAKAVKGEGPI-----DYQGTEIKLHEPFRRVH 322
Cdd:PRK02983 840 RVFELGRNFRNEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGAPVVmrpdgDGVLEPVDISGPWPVVT 919
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 323 MVDAIKEVTGIDFWPEMTFEEATALANEKHVPVEKHFTSvGHIINAFFEAFVEDTLIQPTFVYGHPVEVSPLAKKNPEDS 402
Cdd:PRK02983 920 VHDAVSEALGEEIDPDTPLAELRKLCDAAGIPYRTDWDA-GAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPHRSDP 998
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 403 RFTDRFELFIMTKEYANAFTELNDPIDQLSRFKAQ---AAAkelGDDEATGIDYDFVEALEYGMPPTGGLGIGIDRLCML 479
Cdd:PRK02983 999 GLAERWDLVAWGVELGTAYSELTDPVEQRRRLTEQsllAAG---GDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVML 1075
|
490
....*....|....*...
gi 501964611 480 LTNtTTIRDVLLFPTMKP 497
Cdd:PRK02983 1076 LTG-RSIRETLPFPLVKP 1092
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
8-497 |
1.32e-160 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 465.31 E-value: 1.32e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 8 ELNDQQIVRREKMAALAEQGIdPFGKRFDRTTNSGELKEKYSDKTKEDLQELQATAIIAGRLMTKRGKGKVGFAHLQDRQ 87
Cdd:PRK12445 14 DFNDELRNRREKLAALRQQGV-AFPNDFRRDHTSDQLHEEFDAKDNQELESLNIEVSVAGRMMTRRIMGKASFVTLQDVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 88 GQIQIYVRKDSVGDDNY-DIFKKADLGDFIGVEGDIMCTDMGELSIKATKLTHLSKSLRPLPEKFHGLTDIETIYRKRHL 166
Cdd:PRK12445 93 GRIQLYVARDSLPEGVYnDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEVRYRQRYL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 167 DLISNRSSFERFITRSKMISEIRRYLDGLGFLEVETPVLHNEAGGAAARPFITHHNAQDIDMVLRIAPELHLKRLIVGGM 246
Cdd:PRK12445 173 DLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 247 ERVYEIGRIFRNEGMDATHNPEFTSIEVYEAYADYLDMMTLTEGIIQHAAKAVKGEGPIDYQGTEIKLHEPFRRVHMVDA 326
Cdd:PRK12445 253 ERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDFGKPFEKLTMREA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 327 IKEvtgidFWPEM------TFEEATALANEKHVPVEKHFtSVGHIINAFFEAFVEDTLIQPTFVYGHPVEVSPLAKKNPE 400
Cdd:PRK12445 333 IKK-----YRPETdmadldNFDAAKALAESIGITVEKSW-GLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 401 DSRFTDRFELFIMTKEYANAFTELNDPIDQLSRFKAQAAAKELGDDEATGIDYDFVEALEYGMPPTGGLGIGIDRLCMLL 480
Cdd:PRK12445 407 NPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLF 486
|
490
....*....|....*..
gi 501964611 481 TNTTTIRDVLLFPTMKP 497
Cdd:PRK12445 487 TNSHTIRDVILFPAMRP 503
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
10-497 |
2.73e-122 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 369.72 E-value: 2.73e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 10 NDQQIVRREKmaalaEQGIDPFGKRFDRTTNSGELKEKYSDKTKEdlQELQATAI-IAGRLMTKRGKG-KVGFAHLQDRQ 87
Cdd:PTZ00417 88 NRSKFIQEQK-----AKGINPYPHKFERTITVPEFVEKYQDLASG--EHLEDTILnVTGRIMRVSASGqKLRFFDLVGDG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 88 GQIQI---YVRKDSVGDDNYDIFKKADLGDFIGVEGDIMCTDMGELSIKATKLTHLSKSLRPLPEKFhGLTDIETIYRKR 164
Cdd:PTZ00417 161 AKIQVlanFAFHDHTKSNFAECYDKIRRGDIVGIVGFPGKSKKGELSIFPKETIILSPCLHMLPMKY-GLKDTEIRYRQR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 165 HLDLISNRSSFERFITRSKMISEIRRYLDGLGFLEVETPVLHNEAGGAAARPFITHHNAQDIDMVLRIAPELHLKRLIVG 244
Cdd:PTZ00417 240 YLDLMINESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHNDLDLDLYLRIATELPLKMLIVG 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 245 GMERVYEIGRIFRNEGMDATHNPEFTSIEVYEAYADYLDMMTLTE----GIIQHAAKAVK----GEGPiDYQGTEIKLHE 316
Cdd:PTZ00417 320 GIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEdffsQLVMHLFGTYKilynKDGP-EKDPIEIDFTP 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 317 PFRRVHMVDAIKEVTGID----FWPEMTFEEATALANEKHVPVEKHFTSvGHIINAFFEAFVEDTLI-QPTFVYGHPVEV 391
Cdd:PTZ00417 399 PYPKVSIVEELEKLTNTKleqpFDSPETINKMINLIKENKIEMPNPPTA-AKLLDQLASHFIENKYPnKPFFIIEHPQIM 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 392 SPLAKKNPEDSRFTDRFELFIMTKEYANAFTELNDPIDQLSRFKAQAAAKELGDDEATGIDYDFVEALEYGMPPTGGLGI 471
Cdd:PTZ00417 478 SPLAKYHRSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPTGGLGL 557
|
490 500
....*....|....*....|....*.
gi 501964611 472 GIDRLCMLLTNTTTIRDVLLFPTMKP 497
Cdd:PTZ00417 558 GIDRITMFLTNKNCIKDVILFPTMRP 583
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
35-496 |
2.49e-121 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 369.75 E-value: 2.49e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 35 FDRTTNSGELKEKYSDKTKEDlQELQATAIIAGRLMTKRGKGKVGFAHLQDRQGQIQIYVRkdsVGDDnydiFKKADL-- 112
Cdd:PTZ00385 83 FRGITPISEVRERYGYLASGD-RAAQATVRVAGRVTSVRDIGKIIFVTIRSNGNELQVVGQ---VGEH----FTREDLkk 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 113 -------GDFIGVEGdIMC-TDMGELSIKATKLTHLS------KSLRPLPEKFHGLTDIETIYRKRHLDLISNRSSFERF 178
Cdd:PTZ00385 155 lkvslrvGDIIGADG-VPCrMQRGELSVAASRMLILSpyvctdQVVCPNLRGFTVLQDNDVKYRYRFTDMMTNPCVIETI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 179 ITRSKMISEIRRYLDGLGFLEVETPVLHNEAGGAAARPFITHHNAQDIDMVLRIAPELHLKRLIVGGMERVYEIGRIFRN 258
Cdd:PTZ00385 234 KKRHVMLQALRDYFNERNFVEVETPVLHTVASGANAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRN 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 259 EGMDATHNPEFTSIEVYEAYADYLDMMTLTEGIIQHAAKAVKGEGPIDYQ-------GTEIKLHEPFRRVHMVDAIKEVT 331
Cdd:PTZ00385 314 EDADRSHNPEFTSCEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTVVQIYpenahgnPVTVDLGKPFRRVSVYDEIQRMS 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 332 GIDFWPE--------MTFEEATALANEKHVPVEKhftSVGHIINAFFEAFVEDTLIQPTFVYGHPVEVSPLAKKNPEDSR 403
Cdd:PTZ00385 394 GVEFPPPnelntpkgIAYMSVVMLRYNIPLPPVR---TAAKMFEKLIDFFITDRVVEPTFVMDHPLFMSPLAKEQVSRPG 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 404 FTDRFELFIMTKEYANAFTELNDPIDQLSRFKAQAAAKELGDDEATGIDYDFVEALEYGMPPTGGLGIGIDRLCMLLTNT 483
Cdd:PTZ00385 471 LAERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNS 550
|
490
....*....|...
gi 501964611 484 TTIRDVLLFPTMK 496
Cdd:PTZ00385 551 SNIRDGIIFPLLR 563
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
156-496 |
4.82e-115 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 341.85 E-value: 4.82e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 156 DIETIYRKRHLDLiSNRSSFERFITRSKMISEIRRYLDGLGFLEVETPVLHNEAGGAAARPFITHHNAQDIDMVLRIAPE 235
Cdd:pfam00152 1 DEETRLKYRYLDL-RRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 236 LHLKRLIVGGMERVYEIGRIFRNEGMDATHNPEFTSIEVYEAYADYLDMMTLTEGIIQHAAKAVKGEGPIDYQGTEIKLH 315
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 316 EPFRRVHMVDAIKEVTGIDF--WPEMTFEEATALANEKHVPVEKHftsvghiinaffeafvedtliQPTFVYGHPVEVSP 393
Cdd:pfam00152 160 KPFPRITYAEAIEKLNGKDVeeLGYGSDKPDLRFLLELVIDKNKF---------------------NPLWVTDFPAEHHP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 394 LAKKNPED-SRFTDRFELFIMTKEYANAFTELNDPIDQLSRFKAQAAAKElgddEATGIDYDFVEALEYGMPPTGGLGIG 472
Cdd:pfam00152 219 FTMPKDEDdPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPE----EAEEKFGFYLDALKYGAPPHGGLGIG 294
|
330 340
....*....|....*....|....
gi 501964611 473 IDRLCMLLTNTTTIRDVLLFPTMK 496
Cdd:pfam00152 295 LDRLVMLLTGLESIREVIAFPKTR 318
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
178-497 |
5.23e-95 |
|
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of class II aminoacyl-tRNA synthetases of the subgroup containing aspartyl, lysyl, and asparaginyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. Nearly all class II tRNA synthetases are dimers and enzymes in this subgroup are homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238358 [Multi-domain] Cd Length: 269 Bit Score: 288.61 E-value: 5.23e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 178 FITRSKMISEIRRYLDGLGFLEVETPVLHNEAGGAAARPFITHHNAQDIDMVLRIAPELHLKRLIVGGMERVYEIGRIFR 257
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 258 NEGMDATHNPEFTSIEVYEAYADYLDMMTLTEGIIQHAAKAVKGEGPIDYQGTEIKLHEPFRRVHMVDAIKEvtgidfwp 337
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGFELEDFGLPFPRLTYREALER-------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 338 emtfeeatalanekhvpvekhftsvghiinaffeafvedtLIQPTFVYGHPVE-VSPLAKKNPEDSRFTDRFELFIMTKE 416
Cdd:cd00669 153 ----------------------------------------YGQPLFLTDYPAEmHSPLASPHDVNPEIADAFDLFINGVE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 417 YANAFTELNDPIDQLSRFKAQAAAKELGDDEatgiDYDFVEALEYGMPPTGGLGIGIDRLCMLLTNTTTIRDVLLFPTMK 496
Cdd:cd00669 193 VGNGSSRLHDPDIQAEVFQEQGINKEAGMEY----FEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMR 268
|
.
gi 501964611 497 P 497
Cdd:cd00669 269 R 269
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
174-490 |
6.49e-70 |
|
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441870 [Multi-domain] Cd Length: 309 Bit Score: 225.37 E-value: 6.49e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 174 SFERFITRSKMISEIRRYLDGLGFLEVETPVLhNEAGGAAA--RPFIT---HHNAQDIDMVLRIAPELHLKRLIVGGMER 248
Cdd:COG2269 2 SREALRARARLLAAIRAFFAERGVLEVETPAL-SVAPGTDPhlDSFATefiGPDGGGRPLYLHTSPEFAMKRLLAAGSGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 249 VYEIGRIFRNEGMDATHNPEFTSIEVYEAYADYLDMMTLTEGIIQHAAKAVKgegpidyqgteiklHEPFRRVHMVDAIK 328
Cdd:COG2269 81 IYQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAAG--------------FAPAERLSYQEAFL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 329 EVTGIDFWpEMTFEEATALANEKHVPVEKHFTSVGhIINAFFEAFVEDTLIQ--PTFVYGHPVEVSPLAKKNPEDSRFTD 406
Cdd:COG2269 147 RYLGIDPL-TADLDELAAAAAAAGLRVADDDDRDD-LLDLLLSERVEPQLGRdrPTFLYDYPASQAALARISPDDPRVAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 407 RFELFIMTKEYANAFTELNDPIDQLSRFKAQAAAKELGDDEATGIDYDFVEALEYGMPPTGGLGIGIDRLCMLLTNTTTI 486
Cdd:COG2269 225 RFELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAERI 304
|
....
gi 501964611 487 RDVL 490
Cdd:COG2269 305 DDVL 308
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
191-490 |
1.38e-59 |
|
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous to the C-terminal region of lysyl-tRNA synthetase (LysS). Multiple sequence alignment of these proteins with the homologous regions of collected LysS proteins shows that these proteins form a distinct set rather than just similar truncations of LysS. The protein is termed GenX after its designation in E. coli. Interestingly, genX often is located near a homolog of lysine-2,3-aminomutase. Its function is unknown. [Unknown function, General]
Pssm-ID: 273090 [Multi-domain] Cd Length: 290 Bit Score: 197.77 E-value: 1.38e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 191 YLDGLGFLEVETPVLHNeAGGAAA--RPFITH---HNAQDIDMVLRIAPELHLKRLIVGGMERVYEIGRIFRNEGMDATH 265
Cdd:TIGR00462 1 FFAERGVLEVETPLLSP-APVTDPhlDAFATEfvgPDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 266 NPEFTSIEVYEAYADYLDMMTLTEGIIQHAAKavkgegpidyqgteiKLHEPFRRVHMVDAIKEVTGIDFwPEMTFEEAT 345
Cdd:TIGR00462 80 NPEFTMLEWYRPGFDYHDLMDEVEALLQELLG---------------DPFAPAERLSYQEAFLRYAGIDP-LTASLAELQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 346 ALANEKHV--PVEKHFTSVghiinaFFEAFVEdtLIQP-------TFVYGHPVEVSPLAKKNPEDSRFTDRFELFIMTKE 416
Cdd:TIGR00462 144 AAAAAHGIraSEEDDRDDL------LDLLFSE--KVEPhlgfgrpTFLYDYPASQAALARISPDDPRVAERFELYIKGLE 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501964611 417 YANAFTELNDPIDQLSRFKAQAAAKELGDDEATGIDYDFVEALEYGMPPTGGLGIGIDRLCMLLTNTTTIRDVL 490
Cdd:TIGR00462 216 LANGFHELTDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVL 289
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
174-489 |
1.99e-53 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 182.44 E-value: 1.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 174 SFERFITRSKMISEIRRYLDGLGFLEVETPVL--------HNEaggaaarPFITH----HNAQDIDMVLRIAPELHLKRL 241
Cdd:PRK09350 1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILsqatvtdiHLV-------PFETRfvgpGASQGKTLWLMTSPEYHMKRL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 242 IVGGMERVYEIGRIFRNEGMDATHNPEFTSIEVYEAYADYLDMMTLTEGIIQHAAKAVKGEgPIDYQgteiklhepfrrv 321
Cdd:PRK09350 74 LAAGSGPIFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCEPAE-SLSYQ------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 322 hmvDAIKEVTGIDFWPEMTfEEATALAnekhvpvEKHftsvgHIINAFFEAFVEDTLIQ---------------PTFVYG 386
Cdd:PRK09350 140 ---QAFLRYLGIDPLSADK-TQLREVA-------AKL-----GLSNIADEEEDRDTLLQllftfgvepnigkekPTFVYH 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 387 HPVEVSPLAKKNPEDSRFTDRFELFIMTKEYANAFTELNDPIDQLSRFK---AQAAAKELGDDEatgIDYDFVEALEYGM 463
Cdd:PRK09350 204 FPASQAALAKISTEDHRVAERFEVYFKGIELANGFHELTDAREQRQRFEqdnRKRAARGLPQQP---IDENLIAALEAGL 280
|
330 340
....*....|....*....|....*.
gi 501964611 464 PPTGGLGIGIDRLCMLLTNTTTIRDV 489
Cdd:PRK09350 281 PDCSGVALGVDRLIMLALGAESISEV 306
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
65-168 |
7.55e-51 |
|
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These enzymes are homodimeric class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Included in this group are E. coli LysS and LysU. These two isoforms of LysRS are encoded by distinct genes which are differently regulated. Eukaryotes contain 2 sets of aaRSs, both of which encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Saccharomyces cerevisiae cytoplasmic and mitochondrial LysRSs have been shown to participate in the mitochondrial import of the only nuclear-encoded tRNA of S. cerevisiae (tRNAlysCUU). The gene for human LysRS encodes both the cytoplasmic and the mitochondrial isoforms of LysRS. In addition to their housekeeping role, human lysRS may function as a signaling molecule that activates immune cells and tomato LysRS may participate in a root-specific process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging.
Pssm-ID: 239817 [Multi-domain] Cd Length: 108 Bit Score: 168.42 E-value: 7.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 65 IAGRLMTKRGKGKVGFAHLQDRQGQIQIYVRKDSVGDDNYDIFKKA-DLGDFIGVEGDIMCTDMGELSIKATKLTHLSKS 143
Cdd:cd04322 4 VAGRIMSKRGSGKLSFADLQDESGKIQVYVNKDDLGEEEFEDFKKLlDLGDIIGVTGTPFKTKTGELSIFVKEFTLLSKS 83
|
90 100
....*....|....*....|....*
gi 501964611 144 LRPLPEKFHGLTDIETIYRKRHLDL 168
Cdd:cd04322 84 LRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
37-493 |
2.03e-42 |
|
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl/asparaginyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439788 [Multi-domain] Cd Length: 430 Bit Score: 155.98 E-value: 2.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 37 RTTNSGELKEKYSDKTkedlqelqatAIIAGRLMTKRGKGKVGFAHLQDRQGQIQIYVRKDSVgdDNYDIFKKADLGDFI 116
Cdd:COG0017 1 KRTYIKDLLPEHVGQE----------VTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKL--ENFEEAKKLTTESSV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 117 GVEGDIMCTDM--GELSIKATKLTHLSKSLRPLP--EKFHGLtdiETIYRKRHLDLISNRSSfERFITRSKMISEIRRYL 192
Cdd:COG0017 69 EVTGTVVESPRapQGVELQAEEIEVLGEADEPYPlqPKRHSL---EFLLDNRHLRLRTNRFG-AIFRIRSELARAIREFF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 193 DGLGFLEVETPVLHNEAG-GAAA--------RP-FIThhnaQdidmvlriAPELHlKRLIVGGMERVYEIGRIFRNEGMD 262
Cdd:COG0017 145 QERGFVEVHTPIITASATeGGGElfpvdyfgKEaYLT----Q--------SGQLY-KEALAMALEKVYTFGPTFRAEKSN 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 263 AT-HNPEFTSIEVYEAYADYLDMMTLTEGIIQHAAKAVKgegpiDYQGTEIKLHEpfrrvHMVDAIKEVTGIDFwPEMTF 341
Cdd:COG0017 212 TRrHLAEFWMIEPEMAFADLEDVMDLAEEMLKYIIKYVL-----ENCPEELEFLG-----RDVERLEKVPESPF-PRITY 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 342 EEATALANEKHVPVE-------KHFTSVGHIinaFFEAFVedtliqptFVYGHPVEVSPL-AKKNPEDSRFTDRFELfiM 413
Cdd:COG0017 281 TEAIEILKKSGEKVEwgddlgtEHERYLGEE---FFKKPV--------FVTDYPKEIKAFyMKPNPDDPKTVAAFDL--L 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 414 TKEYAnaftEL------NDPIDQLsrfkaQAAAKELGDDEAtgiDYDF-VEALEYGMPPTGGLGIGIDRLCMLLTNTTTI 486
Cdd:COG0017 348 APGIG----EIiggsqrEHRYDVL-----VERIKEKGLDPE---DYEWyLDLRRYGSVPHAGFGLGLERLVMWLTGLENI 415
|
....*..
gi 501964611 487 RDVLLFP 493
Cdd:COG0017 416 REVIPFP 422
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
62-493 |
7.41e-42 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 154.58 E-value: 7.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 62 TAIIAGRLMTKRGKGKVGFAHLQDRQGQIQIYVRKDSVgDDNYDIFKKADLGDFIGVEGDIMCTDM--GELSIKATKLTH 139
Cdd:PRK05159 18 EVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVD-EELFETIKKLKRESVVSVTGTVKANPKapGGVEVIPEEIEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 140 LSKSLRPLPEKFHG--LTDIETIYRKRHLDLISNRSSfERFITRSKMISEIRRYLDGLGFLEVETPVLHNEA--GGAAAR 215
Cdd:PRK05159 97 LNKAEEPLPLDISGkvLAELDTRLDNRFLDLRRPRVR-AIFKIRSEVLRAFREFLYENGFTEIFTPKIVASGteGGAELF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 216 PfITHHN-----AQdidmvlriAPELHlKRLIVG-GMERVYEIGRIFRNEGMDAT-HNPEFTSIEVYEAYAD-YLDMMTL 287
Cdd:PRK05159 176 P-IDYFEkeaylAQ--------SPQLY-KQMMVGaGFERVFEIGPVFRAEEHNTSrHLNEYTSIDVEMGFIDdHEDVMDL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 288 TEGIIQHAAKAVKGEGPIDYQGTEIKLHEPfrrvhmvdaIKEVtgidfwPEMTFEEATALANEK--HVPVEKHFTSVG-H 364
Cdd:PRK05159 246 LENLLRYMYEDVAENCEKELELLGIELPVP---------ETPI------PRITYDEAIEILKSKgnEISWGDDLDTEGeR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 365 IINAFFEafvEDTLIQPTFVYGHPVEVSPL-AKKNPEDSRFTDRFELFIMTKEYANAFTELNDPIDQLSRFKAQAAAKEl 443
Cdd:PRK05159 311 LLGEYVK---EEYGSDFYFITDYPSEKRPFyTMPDEDDPEISKSFDLLFRGLEITSGGQRIHRYDMLVESIKEKGLNPE- 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 501964611 444 gddeatgiDYDF-VEALEYGMPPTGGLGIGIDRLCMLLTNTTTIRDVLLFP 493
Cdd:PRK05159 387 --------SFEFyLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
64-493 |
2.21e-36 |
|
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, aspS_arch, represents aspartyl-tRNA synthetases from the eukaryotic cytosol and from the Archaea. In some species, this enzyme aminoacylates tRNA for both Asp and Asn; Asp-tRNA(asn) is subsequently transamidated to Asn-tRNA(asn). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273087 [Multi-domain] Cd Length: 428 Bit Score: 139.57 E-value: 2.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 64 IIAGRLMTKRGKGKVGFAHLQDRQGQIQIYVRKDSVGDDNYDIFKKADLGDFIGVEGDIMCTD--MGELSIKATKLTHLS 141
Cdd:TIGR00458 16 TFMGWVHEIRDLGGLIFVLLRDREGLIQITAPAKKVSKNLFKWAKKLNLESVVAVRGIVKIKEkaPGGFEIIPTKIEVIN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 142 KSLRPLP----EKFHGltDIETIYRKRHLDLISNRSSfERFITRSKMISEIRRYLDGLGFLEVETPVLHNEA--GGAAAR 215
Cdd:TIGR00458 96 EAKEPLPldptEKVPA--ELDTRLDYRFLDLRRPTVQ-AIFRIRSGVLESVREFLAEEGFIEVHTPKLVASAteGGTELF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 216 PfITHHNAQdidMVLRIAPELHLKRLIVGGMERVYEIGRIFRNEGMDAT-HNPEFTSIEVYEAYADYLDMMTLTEGIIQH 294
Cdd:TIGR00458 173 P-ITYFERE---AFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHrHLNEATSIDIEMAFEDHHDVMDILEELVVR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 295 AAKAVKGEGPIDYQGTEIKLHEPFRRvhmvdaikevtgidfWPEMTFEEATALANEKHVPVekhftSVGHIINAFFEAFV 374
Cdd:TIGR00458 249 VFEDVPERCAHQLETLEFKLEKPEGK---------------FVRLTYDEAIEMANAKGVEI-----GWGEDLSTEAEKAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 375 EDTLIQPTFVYGHPVEVSPLAKKNPEDS-RFTDRFELFIMTKEYANAFTELNDPIDQLSRFKAQAAAKElgddeatGIDY 453
Cdd:TIGR00458 309 GEEMDGLYFITDWPTEIRPFYTMPDEDNpEISKSFDLMYRDLEISSGAQRIHLHDLLVERIKAKGLNPE-------GFKD 381
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 501964611 454 dFVEALEYGMPPTGGLGIGIDRLCMLLTNTTTIRDVLLFP 493
Cdd:TIGR00458 382 -YLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFP 420
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
178-493 |
3.64e-34 |
|
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. AspRS is a homodimer, which attaches a specific amino acid to the 3' OH group of ribose of the appropriate tRNA. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. AspRS in this family differ from those found in the AsxRS family by a GAD insert in the core domain.
Pssm-ID: 238400 [Multi-domain] Cd Length: 280 Bit Score: 130.00 E-value: 3.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 178 FITRSKMISEIRRYLDGLGFLEVETPVLhNEAGGAAARPFI----THHN---AqdidmvLRIAPELHLKRLIVGGMERVY 250
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPIL-TKSTPEGARDFLvpsrLHPGkfyA------LPQSPQLFKQLLMVSGFDRYF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 251 EIGRIFRNEGMDATHNPEFTSIEVYEAYADYLDMMTLTEGIIQHAAKAVKGegpidyqgteIKLHEPFRRVHMVDAIKEV 330
Cdd:cd00777 74 QIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG----------VELTTPFPRMTYAEAMERY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 331 tGIDF-----WPEMTFEEAtalanekhvpvEKHFTSVGHIinafFEAFVEDTLiqptfvyghpvevsPLAKKNPEDSRfT 405
Cdd:cd00777 144 -GFKFlwivdFPLFEWDEE-----------EGRLVSAHHP----FTAPKEEDL--------------DLLEKDPEDAR-A 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 406 DRFELFIMTKEYANAFTELNDPIDQLSRFKAqaaakeLGDDEATgiDYD----FVEALEYGMPPTGGLGIGIDRLCMLLT 481
Cdd:cd00777 193 QAYDLVLNGVELGGGSIRIHDPDIQEKVFEI------LGLSEEE--AEEkfgfLLEAFKYGAPPHGGIALGLDRLVMLLT 264
|
330
....*....|..
gi 501964611 482 NTTTIRDVLLFP 493
Cdd:cd00777 265 GSESIRDVIAFP 276
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
156-493 |
4.01e-32 |
|
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs in the core domain. This family includes AsnRS as well as a subgroup of AspRS. AsnRS and AspRS are homodimers, which attach either asparagine or aspartate to the 3'OH group of ribose of the appropriate tRNA. While archaea lack asnRS, they possess a non-discriminating aspRS, which can mischarge Asp-tRNA with Asn. Subsequently, a tRNA-dependent aspartate amidotransferase converts the bound aspartate to asparagine. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.
Pssm-ID: 238399 [Multi-domain] Cd Length: 322 Bit Score: 125.37 E-value: 4.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 156 DIETIYRKRHLDLISNRSSfERFITRSKMISEIRRYLDGLGFLEVETPVLHNEA--GGAAARPFithhNAQDIDMVLRIA 233
Cdd:cd00776 3 NLETLLDNRHLDLRTPKVQ-AIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDteGGAELFKV----SYFGKPAYLAQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 234 PELHLKRLIvGGMERVYEIGRIFRNEGMDAT-HNPEFTSIEVYEAYA-DYLDMMTLTEGIIQHAAKAVKgegpiDYQGTE 311
Cdd:cd00776 78 PQLYKEMLI-AALERVYEIGPVFRAEKSNTRrHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVL-----ERCAKE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 312 IKLHEPFRRVHMVDAIKevtgidfWPEMTFEEATALANEKHVPVEKHFtsvGHIINAFFEAFVEDTLIQ-PTFVYGHPVE 390
Cdd:cd00776 152 LELVNQLNRELLKPLEP-------FPRITYDEAIELLREKGVEEEVKW---GEDLSTEHERLLGEIVKGdPVFVTDYPKE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 391 VSPL-AKKNPEDSRFTDRFELFImtkeyaNAFTEL-------NDPiDQLsrfkaQAAAKELGDDEAtgiDYDF-VEALEY 461
Cdd:cd00776 222 IKPFyMKPDDDNPETVESFDLLM------PGVGEIvggsqriHDY-DEL-----EERIKEHGLDPE---SFEWyLDLRKY 286
|
330 340 350
....*....|....*....|....*....|..
gi 501964611 462 GMPPTGGLGIGIDRLCMLLTNTTTIRDVLLFP 493
Cdd:cd00776 287 GMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
37-493 |
1.49e-30 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 125.18 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 37 RTTNSGELKEKYSDKTkedlqelqatAIIAGRLMTKRGKGKVGFAHLQDRQGQIQIYVRKDSvgddnyDIFKKAD-LG-- 113
Cdd:PRK00476 4 RTHYCGELRESHVGQT----------VTLCGWVHRRRDHGGLIFIDLRDREGIVQVVFDPDA------EAFEVAEsLRse 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 114 DFIGVEGDI-----------MCTdmGELSIKATKLTHLSKS--LrPLPEKFHGLTDIETIYRKRHLDLISNRSsFERFIT 180
Cdd:PRK00476 68 YVIQVTGTVrarpegtvnpnLPT--GEIEVLASELEVLNKSktL-PFPIDDEEDVSEELRLKYRYLDLRRPEM-QKNLKL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 181 RSKMISEIRRYLDGLGFLEVETPVLhneagGAA----ARPFI----THHN-----AQdidmvlriAPELhLKRLI-VGGM 246
Cdd:PRK00476 144 RSKVTSAIRNFLDDNGFLEIETPIL-----TKStpegARDYLvpsrVHPGkfyalPQ--------SPQL-FKQLLmVAGF 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 247 ERVYEIGRIFRNEGMDATHNPEFTSIEVYEAYADYLDMMTLTEGIIQHAAKAVKGegpidyqgteIKLHEPFRRVHMVDA 326
Cdd:PRK00476 210 DRYYQIARCFRDEDLRADRQPEFTQIDIEMSFVTQEDVMALMEGLIRHVFKEVLG----------VDLPTPFPRMTYAEA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 327 ----------------IKEVTgiDFWPEMTFEE-ATALANEKHV------------------------------------ 353
Cdd:PRK00476 280 mrrygsdkpdlrfgleLVDVT--DLFKDSGFKVfAGAANDGGRVkairvpggaaqlsrkqideltefakiygakglayik 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 354 --------PVEKHFTsvghiiNAFFEAFVEDTLIQPT----FVYGHPVEVS----------------------------- 392
Cdd:PRK00476 358 vnedglkgPIAKFLS------EEELAALLERTGAKDGdlifFGADKAKVVNdalgalrlklgkelglidedkfaflwvvd 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 393 -PLAKKNPEDSRFTDRFELFIMTKEYANAFTELNDPIDQLS--------------------RFKAQAAAKE---LGDDEA 448
Cdd:PRK00476 432 fPMFEYDEEEGRWVAAHHPFTMPKDEDLDELETTDPGKARAyaydlvlngyelgggsirihRPEIQEKVFEilgISEEEA 511
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 501964611 449 T---GIdydFVEALEYGMPPTGGLGIGIDRLCMLLTNTTTIRDVLLFP 493
Cdd:PRK00476 512 EekfGF---LLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
37-493 |
3.31e-27 |
|
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439943 [Multi-domain] Cd Length: 589 Bit Score: 115.10 E-value: 3.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 37 RTTNSGELKEKYSDKTkedlqelqatAIIAGRLMTKRGKGKVGFAHLQDRQGQIQIYVRKDsvgdDNYDIFKKAD-LG-- 113
Cdd:COG0173 3 RTHYCGELRESDVGQE----------VTLSGWVHRRRDHGGLIFIDLRDRYGITQVVFDPD----DSAEAFEKAEkLRse 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 114 DFIGVEGDI-----------MCTdmGELSIKATKLTHLSKSlRPLPEKFHGLTDI--ETIYRKRHLDLisnRSS--FERF 178
Cdd:COG0173 69 YVIAVTGKVrarpegtvnpkLPT--GEIEVLASELEILNKA-KTPPFQIDDDTDVseELRLKYRYLDL---RRPemQKNL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 179 ITRSKMISEIRRYLDGLGFLEVETPVLhneagGAA----ARPFI----THHN-----AQdidmvlriAPELhLKRLI-VG 244
Cdd:COG0173 143 ILRHKVTKAIRNYLDENGFLEIETPIL-----TKStpegARDYLvpsrVHPGkfyalPQ--------SPQL-FKQLLmVS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 245 GMERVYEIGRIFRNEGMDATHNPEFTSIEVYEAYADYLDMMTLTEGIIQHAAKAVKGegpidyqgteIKLHEPFRR---- 320
Cdd:COG0173 209 GFDRYFQIARCFRDEDLRADRQPEFTQLDIEMSFVDQEDVFELMEGLIRHLFKEVLG----------VELPTPFPRmtya 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 321 ----------------VHMVDAIKEVTGIDF-----------------------WPEMTFEEATALA------------- 348
Cdd:COG0173 279 eamerygsdkpdlrfgLELVDVTDIFKDSGFkvfagaaenggrvkainvpggasLSRKQIDELTEFAkqygakglayikv 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 349 NEKHV--PVEKHFTsvGHIINAFFEAF---VEDTLIqptFVYGHPVEVSP--------LAKK----NPEDSRF---TDrF 408
Cdd:COG0173 359 NEDGLksPIAKFLS--EEELAAILERLgakPGDLIF---FVADKPKVVNKalgalrlkLGKElgliDEDEFAFlwvVD-F 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 409 ELFimtkEYA----------NAFTELNDP-IDQLSRFKAQAAAK---------ELG-------DDE-------ATGIDYD 454
Cdd:COG0173 433 PLF----EYDeeegrwvamhHPFTMPKDEdLDLLETDPGKVRAKaydlvlngyELGggsirihDPElqekvfeLLGISEE 508
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 501964611 455 --------FVEALEYGMPPTGGLGIGIDRLCMLLTNTTTIRDVLLFP 493
Cdd:COG0173 509 eaeekfgfLLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
73-493 |
8.02e-24 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 105.26 E-value: 8.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 73 RGKGKVGFAHLQDRQGQIQIYVRKDSVgDDNYDIFKKADLGDFIGVEGDI-----------MCTdmGELSIKATKLTHLS 141
Cdd:PLN02903 85 RDMGGLTFLDVRDHTGIVQVVTLPDEF-PEAHRTANRLRNEYVVAVEGTVrsrpqespnkkMKT--GSVEVVAESVDILN 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 142 KSLRPLPEKFHGLTDI------ETIYRKRHLDLisNRSSFERFIT-RSKMISEIRRYL-DGLGFLEVETPVLhNEAGGAA 213
Cdd:PLN02903 162 VVTKSLPFLVTTADEQkdsikeEVRLRYRVLDL--RRPQMNANLRlRHRVVKLIRRYLeDVHGFVEIETPIL-SRSTPEG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 214 ARPFITHHNAQDIDM-VLRIAPELHLKRLIVGGMERVYEIGRIFRNEGMDATHNPEFTSIEVYEAYADYLDMMTLTEGII 292
Cdd:PLN02903 239 ARDYLVPSRVQPGTFyALPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDMELAFTPLEDMLKLNEDLI 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 293 QHAAKAVKGegpidyqgteIKLHEPFRRVHMVDAI----------------KEVTgiDFWPEMTFEE-ATALANEKHVPV 355
Cdd:PLN02903 319 RQVFKEIKG----------VQLPNPFPRLTYAEAMskygsdkpdlryglelVDVS--DVFAESSFKVfAGALESGGVVKA 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 356 ------EKHFTSV----GHIIN----------AFFEAFVEDTLIQPTFVYGhpvEVSPLAKKN----------------- 398
Cdd:PLN02903 387 icvpdgKKISNNTalkkGDIYNeaiksgakglAFLKVLDDGELEGIKALVE---SLSPEQAEQllaacgagpgdlilfaa 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 399 -PEDS--RFTDRFELFI-----MTKEYANAFTELND-PI----DQLSRFKA-----QAAAKELGDD--EATGIDYDFV-- 456
Cdd:PLN02903 464 gPTSSvnKTLDRLRQFIaktldLIDPSRHSILWVTDfPMfewnEDEQRLEAlhhpfTAPNPEDMGDlsSARALAYDMVyn 543
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501964611 457 ---------------------------------------EALEYGMPPTGGLGIGIDRLCMLLTNTTTIRDVLLFP 493
Cdd:PLN02903 544 gveigggslriyrrdvqqkvleaiglspeeaeskfgyllEALDMGAPPHGGIAYGLDRLVMLLAGAKSIRDVIAFP 619
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
12-493 |
3.16e-23 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 102.76 E-value: 3.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 12 QQIVRREKMAALAEQGIDPFGKR--FDRTTNSGELKEKYSDKTKEDLqeLQATAIIAGRLMTKRGKGKVGFAHLQDRQGQ 89
Cdd:PTZ00401 30 EEKARAAEKAALVEKYKDVFGAApmVQSTTYKSRTFIPVAVLSKPEL--VDKTVLIRARVSTTRKKGKMAFMVLRDGSDS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 90 IQIYVrkdSVGDDnydifKKADLGDFIG----------------VEGDIMCTDMGELSIKATKLTHLSKSLRPLP----- 148
Cdd:PTZ00401 108 VQAMA---AVEGD-----VPKEMIDFIGqiptesivdveatvckVEQPITSTSHSDIELKVKKIHTVTESLRTLPftled 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 149 ----EKFHGL-TDIETIYRKRHLDLISNRSSfERFITRSKMISEIRRYLDGLGFLEVETPVLHNEAGGAAARPF-ITHHN 222
Cdd:PTZ00401 180 asrkESDEGAkVNFDTRLNSRWMDLRTPASG-AIFRLQSRVCQYFRQFLIDSDFCEIHSPKIINAPSEGGANVFkLEYFN 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 223 AqdiDMVLRIAPELHLKRLIVGGMERVYEIGRIFRNEGMDA-THNPEFTSIEVY----EAYADYLDMM-TLTEGIIQHAA 296
Cdd:PTZ00401 259 R---FAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNThRHLTEFVGLDVEmrinEHYYEVLDLAeSLFNYIFERLA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 297 ------KAVKGEGPID---YQGTEIKLHEpfrrvHMVDAIKE-VTGIDFWP-----------EMTFEEATALAN----EK 351
Cdd:PTZ00401 336 thtkelKAVCQQYPFEplvWKLTPERMKE-----LGVGVISEgVEPTDKYQarvhnmdsrmlRINYMHCIELLNtvleEK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 352 HVPVEKHFTSVGHIINAFF-EAFVEDTLIQPTFvyghPVEVSPL-AKKNPEDSRFTDRFELFIMTKEYANAFTELNDPID 429
Cdd:PTZ00401 411 MAPTDDINTTNEKLLGKLVkERYGTDFFISDRF----PSSARPFyTMECKDDERFTNSYDMFIRGEEISSGAQRIHDPDL 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501964611 430 QLSRfkaqaaAKELGDDEATGIDYdfVEALEYGMPPTGGLGIGIDRLCMLLTNTTTIRDVLLFP 493
Cdd:PTZ00401 487 LLAR------AKMLNVDLTPIKEY--VDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFP 542
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
2-493 |
5.40e-21 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 95.93 E-value: 5.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 2 SNQHIEELNDQQIVRRE--KMAALAEQGIDPFGKRFDRTTNSGE---LKEKYSDKTKEDLQELQA--------------- 61
Cdd:PLN02850 1 SSQEAVEESGEKISKKAakKAAAKAEKLRREATAKAAAASLEDEddpLASNYGDVPLEELQSKVTgrewtdvsdlgeela 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 62 --TAIIAGRLMTKRGKGKVGFAHLQDRQGQIQ--IYVRKDSVGDDNYDIFKKADLGDFIGVEGDIM--------CTDMGE 129
Cdd:PLN02850 81 gsEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQcvVFVSEVTVSKGMVKYAKQLSRESVVDVEGVVSvpkkpvkgTTQQVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 130 LSIkaTKLTHLSKSLRPLP-----------EKFHGLTDIETIYR--------KRHLDLisnRSSFERFITR--SKMISEI 188
Cdd:PLN02850 161 IQV--RKIYCVSKALATLPfnvedaarsesEIEKALQTGEQLVRvgqdtrlnNRVLDL---RTPANQAIFRiqSQVCNLF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 189 RRYLDGLGFLEVETPVLHNEA--GGAAArpFITHHNAQDidMVLRIAPELHLKRLIVGGMERVYEIGRIFRNEGmDATHN 266
Cdd:PLN02850 236 REFLLSKGFVEIHTPKLIAGAseGGSAV--FRLDYKGQP--ACLAQSPQLHKQMAICGDFRRVFEIGPVFRAED-SFTHR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 267 P--EFTSI----EVYEAYADYLDMM-----TLTEGIIQHAAK---AVKGEGPIDyqgtEIKLHEPFRRVHMVDAI---KE 329
Cdd:PLN02850 311 HlcEFTGLdlemEIKEHYSEVLDVVdelfvAIFDGLNERCKKeleAIREQYPFE----PLKYLPKTLRLTFAEGIqmlKE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 330 V-TGIDFWPEMTFEEATALANekhVPVEKHFTSvghiinaFFeafvedtliqptFVYGHPVEVSPL-AKKNPEDSRFTDR 407
Cdd:PLN02850 387 AgVEVDPLGDLNTESERKLGQ---LVKEKYGTD-------FY------------ILHRYPLAVRPFyTMPCPDDPKYSNS 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 408 FELFIMTKEYANAFTELNDPiDQLSRfkaqaAAKELGDDEATGIDYdfVEALEYGMPPTGGLGIGIDRLCMLLTNTTTIR 487
Cdd:PLN02850 445 FDVFIRGEEIISGAQRVHDP-ELLEK-----RAEECGIDVKTISTY--IDSFRYGAPPHGGFGVGLERVVMLFCGLNNIR 516
|
....*.
gi 501964611 488 DVLLFP 493
Cdd:PLN02850 517 KTSLFP 522
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
64-493 |
1.00e-18 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 89.28 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 64 IIAGRLMTKRGKGKVGFAHLQDRQGQIQIYVRKDSVGDDNYDIFKKADLGDFIGVEGDIM---------CTDMGELSIKA 134
Cdd:PRK12820 22 CLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAAPADVYELAASLRAEFCVALQGEVQkrleetenpHIETGDIEVFV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 135 TKLTHLSKSLR---PLPEKF-----------HGLTDIETIYRkrHLDLisNRSSFER-FITRSKMISEIRRYLDGLGFLE 199
Cdd:PRK12820 102 RELSILAASEAlpfAISDKAmtagagsagadAVNEDLRLQYR--YLDI--RRPAMQDhLAKRHRIIKCARDFLDSRGFLE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 200 VETPVLhNEAGGAAARPFITHHNAQDIDM-VLRIAPELHLKRLIVGGMERVYEIGRIFRNEGMDATHNPEFTSIEVYEAY 278
Cdd:PRK12820 178 IETPIL-TKSTPEGARDYLVPSRIHPKEFyALPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFTQLDIEASF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 279 ADYLDMMTLTEGIIQHAAkAVKGegpidyqgteIKLHEPFRRVHMVDAIkEVTGIDfWPEMTFE----EAT--------- 345
Cdd:PRK12820 257 IDEEFIFELIEELTARMF-AIGG----------IALPRPFPRMPYAEAM-DTTGSD-RPDLRFDlkfaDATdifentryg 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 346 ---------------------------ALANEKHVPVEKHFTSVG-------------HIINAF-----------FEAFV 374
Cdd:PRK12820 324 ifkqilqrggrikginikgqseklsknVLQNEYAKEIAPSFGAKGmtwmraeaggldsNIVQFFsadekealkrrFHAED 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 375 EDTLIQ---------------------------PTFVYgHPVEVSPLAKKNPEDSR--------FT--DR---------- 407
Cdd:PRK12820 404 GDVIIMiadascaivlsalgqlrlhladrlgliPEGVF-HPLWITDFPLFEATDDGgvtsshhpFTapDRedfdpgdiee 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 408 --------FELFIMTKEYANAFTELNDPIDQLSRFKAQAAAKELGDDEaTGIdydFVEALEYGMPPTGGLGIGIDRLCML 479
Cdd:PRK12820 483 lldlrsraYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDIEDK-FGF---FLRAFDFAAPPHGGIALGLDRVVSM 558
|
570
....*....|....
gi 501964611 480 LTNTTTIRDVLLFP 493
Cdd:PRK12820 559 ILQTPSIREVIAFP 572
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
180-296 |
1.08e-16 |
|
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 78.70 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 180 TRSKMISEIRRYLDGLGFLEVETPVLHNEAGGAAAR----PFITHHNAQDIDMVLRIAPELHLKRLIVG----GMERVYE 251
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGhepkDLLPVGAENEEDLYLRPTLEPGLVRLFVShirkLPLRLAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 501964611 252 IGRIFRNEG--MDATHNPEFTSIEVYEAYADYLD------MMTLTEGIIQHAA 296
Cdd:cd00768 81 IGPAFRNEGgrRGLRRVREFTQLEGEVFGEDGEEasefeeLIELTEELLRALG 133
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
65-142 |
3.56e-15 |
|
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. Class 2b aaRSs include the homodimeric aspartyl-, asparaginyl-, and lysyl-tRNA synthetases (AspRS, AsnRS, and LysRS). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Included in this group are archeal and archeal-like AspRSs which are non-discriminating and can charge both tRNAAsp and tRNAAsn. E. coli cells have two isoforms of LysRSs (LysS and LysU) encoded by two distinct genes, which are differentially regulated. The cytoplasmic and the mitochondrial isoforms of human LysRS are encoded by a single gene. Yeast cytoplasmic and mitochondrial LysRSs participate in mitochondrial import of cytoplasmic tRNAlysCUU. In addition to their housekeeping role, human LysRS may function as a signaling molecule that activates immune cells. Tomato LysRS may participate in a process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging. AsnRS is immunodominant antigen of the filarial nematode Brugia malayai and is of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.
Pssm-ID: 239766 [Multi-domain] Cd Length: 85 Bit Score: 70.67 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 65 IAGRLMTKRGKGKVGFAHLQDRQGQIQIYVRKDSVGDDnYDIFKKADLGDFIGVEG-----DIMCTDMGELSIKATKLTH 139
Cdd:cd04100 4 LAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELGEF-FEEAEKLRTESVVGVTGtvvkrPEGNLATGEIELQAEELEV 82
|
...
gi 501964611 140 LSK 142
Cdd:cd04100 83 LSK 85
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
65-140 |
1.98e-13 |
|
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic acids. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See pfam00152). Aminoacyl-tRNA synthetases catalyze the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a hetero-trimeric complex, that contains a subunit in this family. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain.
Pssm-ID: 460164 [Multi-domain] Cd Length: 75 Bit Score: 65.33 E-value: 1.98e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501964611 65 IAGRLMTK-RGKGKVGFAHLQDRQGQIQIYVRKdsvgDDNYDIFKKADLGDFIGVEGDIMCTDMGELSIKATKLTHL 140
Cdd:pfam01336 3 VAGRVTSIrRSGGKLLFLTLRDGTGSIQVVVFK----EEAEKLAKKLKEGDVVRVTGKVKKRKGGELELVVEEIELL 75
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
181-493 |
4.29e-12 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 67.35 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 181 RSKMISEIRRYLDGLGFLEVETPVL--------HNEAGGAAARPFIthhNAQDIDMVLRIAPELHlKRLIVGGMERVYEI 252
Cdd:PRK06462 33 QSSILRYTREFLDGRGFVEVLPPIIspstdplmGLGSDLPVKQISI---DFYGVEYYLADSMILH-KQLALRMLGKIFYL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 253 GRIFRNEGMDA---THNPEFTSIEVYEAYADYLDMMTLTEGIIQHAAKAVKGEGP--IDYQGTEI-KLHEPFRRvhmvda 326
Cdd:PRK06462 109 SPNFRLEPVDKdtgRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEdeLEFFGRDLpHLKRPFKR------ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 327 ikevtgidfwpeMTFEEATALANE--KHVPVEKHFTSVGhiinaffEAFVEDTLIQPTFVYGHPVEVSPLAKKnpEDSRF 404
Cdd:PRK06462 183 ------------ITHKEAVEILNEegCRGIDLEELGSEG-------EKSLSEHFEEPFWIIDIPKGSREFYDR--EDPER 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 405 TDRFELFIMTkeYANAFTEL-------NDPIDQLSRFkaqaaaKELGDDEAtgiDYD-FVEALEYGMPPTGGLGIGIDRL 476
Cdd:PRK06462 242 PGVLRNYDLL--LPEGYGEAvsggereYEYEEIVERI------REHGVDPE---KYKwYLEMAKEGPLPSAGFGIGVERL 310
|
330
....*....|....*..
gi 501964611 477 CMLLTNTTTIRDVLLFP 493
Cdd:PRK06462 311 TRYICGLRHIREVQPFP 327
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
65-495 |
1.40e-10 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 63.20 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 65 IAGRLMTKRGKGKVGFAHLQDRQGQIQIYVRKDSvGDDNYDIFKKADLGDFIGVEGDIMCTD--MGELSIKATKLTHLSK 142
Cdd:PRK03932 21 VRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDN-GEEYFEEIKKLTTGSSVIVTGTVVESPraGQGYELQATKIEVIGE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 143 SLR--PLPEKFHG---LTDIetiyrkRHLDLISNRsSFERFITRSKMISEIRRYLDGLGFLEVETPVLHNEAGGAAARPF 217
Cdd:PRK03932 100 DPEdyPIQKKRHSiefLREI------AHLRPRTNK-FGAVMRIRNTLAQAIHEFFNENGFVWVDTPIITASDCEGAGELF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 218 ITHHNAQDIDM-------VLRIAPELHLKRLIVgGMERVYEIGRIFRNEGMDAT-HNPEFTSIEVYEAYADYLDMMTLTE 289
Cdd:PRK03932 173 RVTTLDLDFSKdffgkeaYLTVSGQLYAEAYAM-ALGKVYTFGPTFRAENSNTRrHLAEFWMIEPEMAFADLEDNMDLAE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 290 GIIQHAAKAVkgegpIDYQGTEIKLHEPFRRVHMVDAIKEVTGIDFwPEMTFEEATALANEKHVP--------------- 354
Cdd:PRK03932 252 EMLKYVVKYV-----LENCPDDLEFLNRRVDKGDIERLENFIESPF-PRITYTEAIEILQKSGKKfefpvewgddlgseh 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 355 ----VEKHFTSvghiinaffeafvedtliqPTFVYGHPVEVSPL-AKKNPEDsrftdrfelfimtKEYANAftelnD--- 426
Cdd:PRK03932 326 erylAEEHFKK-------------------PVFVTNYPKDIKAFyMRLNPDG-------------KTVAAM-----Dlla 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 427 P-----------IDQLSRFKAQaaAKELGDDEAtgiDYDFVEAL-EYGMPPTGGLGIGIDRLCMLLTNTTTIRDVLLFPT 494
Cdd:PRK03932 369 PgigeiiggsqrEERLDVLEAR--IKELGLNKE---DYWWYLDLrRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPR 443
|
.
gi 501964611 495 M 495
Cdd:PRK03932 444 T 444
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
230-493 |
3.08e-10 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 62.35 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 230 LRIAPELHLKRLiVGGMERVYEIGRIFRNEGMDAT-HNPEFTSIEVYEAYADYLDMMTLTEGIIQHAAKAVkgegpIDYQ 308
Cdd:PTZ00425 328 LTVSGQLSLENL-CSSMGDVYTFGPTFRAENSHTSrHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGYV-----LNNN 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 309 GTEIKLHEPFRRVHMVDAIKEVTGIDFwPEMTFEEATAL----ANEKHVPVEkhftsVGHIINAFFEAFV-EDTLIQPTF 383
Cdd:PTZ00425 402 FDDIYYFEENVETGLISRLKNILDEDF-AKITYTNVIDLlqpySDSFEVPVK-----WGMDLQSEHERFVaEQIFKKPVI 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 384 VYGHPVEVSPLAKKNPEDSRFTDRFELFIMTKEYANAFTELNDPIDQLSRFKAQaaaKELGDDEAtgidYDFVEALEYGM 463
Cdd:PTZ00425 476 VYNYPKDLKAFYMKLNEDQKTVAAMDVLVPKIGEVIGGSQREDNLERLDKMIKE---KKLNMESY----WWYRQLRKFGS 548
|
250 260 270
....*....|....*....|....*....|
gi 501964611 464 PPTGGLGIGIDRLCMLLTNTTTIRDVLLFP 493
Cdd:PTZ00425 549 HPHAGFGLGFERLIMLVTGVDNIKDTIPFP 578
|
|
| pheS |
TIGR00468 |
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ... |
183-273 |
6.13e-07 |
|
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are heterodimeric, with 2 alpha (pheS) and 2 beta (pheT) subunits. This model describes the alpha subunit, which shows some similarity to class II aminoacyl-tRNA ligases. Mitochondrial phenylalanyl-tRNA synthetase is a single polypeptide chain, active as a monomer, and similar to this chain rather than to the beta chain, but excluded from this model. An interesting feature of the alignment of all sequences captured by this model is a deep split between non-spirochete bacterial examples and all other examples; supporting this split is a relative deletion of about 50 residues in the former set between two motifs well conserved throughout the alignment. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273095 [Multi-domain] Cd Length: 293 Bit Score: 51.16 E-value: 6.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 183 KMISEIRRYLDGLGFLEVETPVLHNEAGGAAARPFITHHNAQDI--------DMVLRI---APELHLKRLIVGGMERVYE 251
Cdd:TIGR00468 76 RVIDEIRDIFLGLGFTEETGPEVETDFWNFDALNIPQDHPARDMqdtfyikdRLLLRThttAVQLRTMEEQEKPPIRIFS 155
|
90 100
....*....|....*....|..
gi 501964611 252 IGRIFRNEGMDATHNPEFTSIE 273
Cdd:TIGR00468 156 PGRVFRNDTVDATHLPEFHQVE 177
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
37-168 |
1.19e-05 |
|
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli aspartyl-tRNA synthetase (AspRS), the human mitochondrial (mt) AspRS-2, the discriminating (D) Thermus thermophilus AspRS-1, and the nondiscriminating (ND) Helicobacter pylori AspRS. These homodimeric enzymes are class2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. Human mtAspRS participates in mitochondrial biosynthesis; this enzyme been shown to charge E.coli native tRNAsp in addition to in vitro transcribed human mitochondrial tRNAsp. T. thermophilus is rare among bacteria in having both a D_AspRS and a ND_AspRS. H.pylori ND-AspRS can charge both tRNAASp and tRNAAsn, it is fractionally more efficient at aminoacylating tRNAAsp over tRNAAsn. The H.pylori genome does not contain AsnRS.
Pssm-ID: 239812 [Multi-domain] Cd Length: 135 Bit Score: 44.82 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 37 RTTNSGELKEKYSDKTkedlqelqatAIIAGRLMTKRGKGKVGFAHLQDRQGQIQIYVRKDSvgDDNYDIFKKADLGDFI 116
Cdd:cd04317 1 RTHYCGELRESHVGQE----------VTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPEE--APEFELAEKLRNESVI 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501964611 117 GVEGDI-----------MCTdmGELSIKATKLTHLSKSlRPLP----EKFHGLTDIEtiYRKRHLDL 168
Cdd:cd04317 69 QVTGKVrarpegtvnpkLPT--GEIEVVASELEVLNKA-KTLPfeidDDVNVSEELR--LKYRYLDL 130
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
62-148 |
2.66e-05 |
|
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the homodimeric non-discriminating (ND) Pyrococcus kodakaraensis aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. P. kodakaraensis AspRS is a class 2b aaRS. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. P. kodakaraensis ND-AspRS can charge both tRNAAsp and tRNAAsn. Some of the enzymes in this group may be discriminating, based on the presence of homologs of asparaginyl-tRNA synthetase (AsnRS) in their completed genomes.
Pssm-ID: 239811 [Multi-domain] Cd Length: 108 Bit Score: 43.07 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 62 TAIIAGRLMTKRGKGKVGFAHLQDRQGQIQIYVRKDSVGDDNYDIFKKADLGDFIGVEGDIMCTDM--GELSIKATKLTH 139
Cdd:cd04316 14 EVTVAGWVHEIRDLGGIKFVILRDREGIVQVTAPKKKVDKELFKTVRKLSRESVISVTGTVKAEPKapNGVEIIPEEIEV 93
|
....*....
gi 501964611 140 LSKSLRPLP 148
Cdd:cd04316 94 LSEAKTPLP 102
|
|
| PheRS_alpha_core |
cd00496 |
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ... |
182-273 |
1.27e-03 |
|
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. While class II aaRSs generally aminoacylate the 3'-OH ribose of the appropriate tRNA, PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. PheRS is an alpha-2/ beta-2 tetramer.
Pssm-ID: 238277 [Multi-domain] Cd Length: 218 Bit Score: 40.22 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 182 SKMISEIRRYLDGLGFLEVETPVLHNEAGGAAARPFITHHNAQDI----------DMVLRIAPELHLKRLIVGGME--RV 249
Cdd:cd00496 4 NKVIEEIEDIFVSMGFTEVEGPEVETDFYNFDALNIPQDHPARDMqdtfyindpaRLLLRTHTSAVQARALAKLKPpiRI 83
|
90 100
....*....|....*....|....
gi 501964611 250 YEIGRIFRNEGMDATHNPEFTSIE 273
Cdd:cd00496 84 FSIGRVYRNDEIDATHLPEFHQIE 107
|
|
| PLN02853 |
PLN02853 |
Probable phenylalanyl-tRNA synthetase alpha chain |
248-273 |
2.10e-03 |
|
Probable phenylalanyl-tRNA synthetase alpha chain
Pssm-ID: 215458 [Multi-domain] Cd Length: 492 Bit Score: 40.43 E-value: 2.10e-03
10 20
....*....|....*....|....*.
gi 501964611 248 RVYEIGRIFRNEGMDATHNPEFTSIE 273
Cdd:PLN02853 344 RYFSIDRVFRNEAVDRTHLAEFHQVE 369
|
|
| PTZ00326 |
PTZ00326 |
phenylalanyl-tRNA synthetase alpha chain; Provisional |
219-273 |
2.18e-03 |
|
phenylalanyl-tRNA synthetase alpha chain; Provisional
Pssm-ID: 240361 [Multi-domain] Cd Length: 494 Bit Score: 40.34 E-value: 2.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 501964611 219 THHNAQDIDMVLRIAPELHLKRLIVGGmeRVYEIGRIFRNEGMDATHNPEFTSIE 273
Cdd:PTZ00326 332 THTTAVSARMLYKLAQEYKKTGPFKPK--KYFSIDRVFRNETLDATHLAEFHQVE 384
|
|
| tRNA-synt_2d |
pfam01409 |
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ... |
182-273 |
2.78e-03 |
|
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only phenylalanyl-tRNA synthetases. This is the core catalytic domain.
Pssm-ID: 396130 [Multi-domain] Cd Length: 245 Bit Score: 39.49 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964611 182 SKMISEIRRYLDGLGFLEVETPVLH---------NEAGGAAAR------PFITHHNAQDIDMVLRI------APELHLKR 240
Cdd:pfam01409 20 TRTLERIRDIFLGMGFEEVEGPEVEsdfynfdalNIPQDHPARdmqdtfYLKKPLKPVARRLLLRThttpvqARTLAKKP 99
|
90 100 110
....*....|....*....|....*....|...
gi 501964611 241 LIVGgmeRVYEIGRIFRNEGMDATHNPEFTSIE 273
Cdd:pfam01409 100 KPPI---KIFSIGRVFRRDQVDATHLPEFHQVE 129
|
|
| |
