|
Name |
Accession |
Description |
Interval |
E-value |
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
13-501 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 906.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 13 QEENKLIAQRKEKLAAVREARAIAFPNDFRRDAYFADLQKQYADKTKEELEAAAIPVKVAGRIMLNRG----SFIVLQDS 88
Cdd:PRK00484 1 EELNEQIAVRREKLAELREQGIDPYPNKFERTHTAAELRAKYDDKEKEELEELEIEVSVAGRVMLKRVmgkaSFATLQDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 89 SERLQVYVNRKTLPEETLAEIKTWDLGDIIGAEGVLARSGKGDLYVDMTSVRLLTKSLRPLPDKHHGLTDTEQRYRQRYV 168
Cdd:PRK00484 81 SGRIQLYVSKDDVGEEALEAFKKLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLPDKFHGLTDVETRYRQRYV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 169 DLMVNEETRHTFRVRSQVIAHIRRFLSERGFLEVETPMLQTIPGGAAAKPFETHHNALDMAMFLRIAPELYLKRLVVGGF 248
Cdd:PRK00484 161 DLIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLIVGGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 249 EKVFEINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQSVLGTTDVPYGDKVFHFGEPFVRLSVFDS 328
Cdd:PRK00484 241 ERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTYQGTEIDFGPPFKRLTMVDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 329 ILKYnpeiTAADLN--DVEKARAIAKKAGAKVLGHEGLGKLQVMIFEELVEHKLEQPHFITRYPFEVSPLARRNDEDPSV 406
Cdd:PRK00484 321 IKEY----TGVDFDdmTDEEARALAKELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEISPLAKRHREDPGL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 407 TDRFELFIGGREIANAYSELNDAEDQAERFMLQVKEKDAGDDEAMHYDADFINALEYGMPPTAGEGIGIDRLVMLLTNSP 486
Cdd:PRK00484 397 TERFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSP 476
|
490
....*....|....*
gi 15598896 487 SIRDVILFPHMRPQA 501
Cdd:PRK00484 477 SIRDVILFPLMRPEK 491
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
12-501 |
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: 871.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 12 QQEENKLIAQRKEKLAAVREARAIAFPNDFRRDAYFADLQKQYADKTKEELEAaaIPVKVAGRIMLNRG----SFIVLQD 87
Cdd:COG1190 4 EEDLNEQIRVRREKLEELREAGIDPYPNKFPRTHTAAEIREKYDELEAEEETG--DEVSVAGRIMAKRDmgkaSFADLQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 88 SSERLQVYVNRKTLPEETLAEIKTWDLGDIIGAEGVLARSGKGDLYVDMTSVRLLTKSLRPLPDKHHGLTDTEQRYRQRY 167
Cdd:COG1190 82 GSGRIQLYLRRDELGEEAYELFKLLDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDPETRYRQRY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 168 VDLMVNEETRHTFRVRSQVIAHIRRFLSERGFLEVETPMLQTIPGGAAAKPFETHHNALDMAMFLRIAPELYLKRLVVGG 247
Cdd:COG1190 162 VDLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 248 FEKVFEINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQSVLGTTDVPYGDKVFHFGEPFVRLSVFD 327
Cdd:COG1190 242 FERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTYQGQEIDLSPPWRRITMVE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 328 SILKYNpEITAADLNDVEKARAIAKKAGAKVLGHEGLGKLQVMIFEELVEHKLEQPHFITRYPFEVSPLARRNDEDPSVT 407
Cdd:COG1190 322 AIKEAT-GIDVTPLTDDEELRALAKELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTDYPVEVSPLAKRHRDDPGLT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 408 DRFELFIGGREIANAYSELNDAEDQAERFMLQVKEKDAGDDEAMHYDADFINALEYGMPPTAGEGIGIDRLVMLLTNSPS 487
Cdd:COG1190 401 ERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPS 480
|
490
....*....|....
gi 15598896 488 IRDVILFPHMRPQA 501
Cdd:COG1190 481 IRDVILFPLMRPEK 494
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
14-500 |
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: 652.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 14 EENKLIAQRKEKLAAVREARAIAFPNDFRRDAYFADLQKQYADKTKEELEAAAIPVKVAGRIMLNRG----SFIVLQDSS 89
Cdd:TIGR00499 1 ELNDQAQQRLEKLNRLRQTGNNPYLHKFERTHSAQEFQEKYADLSNEELKEKELKVSIAGRIKAIRSmgkaTFITLQDES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 90 ERLQVYVNRKTLPEEtLAEIK--TWDLGDIIGAEGVLARSGKGDLYVDMTSVRLLTKSLRPLPDKHHGLTDTEQRYRQRY 167
Cdd:TIGR00499 81 GQIQLYVNKNKLPED-FYEFDeyLLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQETRYRQRY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 168 VDLMVNEETRHTFRVRSQVIAHIRRFLSERGFLEVETPMLQTIPGGAAAKPFETHHNALDMAMFLRIAPELYLKRLVVGG 247
Cdd:TIGR00499 160 LDLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKRLIVGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 248 FEKVFEINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQSVLGTTDVPYGDKVFHFGEPFVRLSVFD 327
Cdd:TIGR00499 240 LEKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINYNDLEIDLKPPWKRITMVD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 328 SILKYNPeITAADLNDVEKARAIAKKAGAKVLGHE-GLGKLQVMIFEELVEHKLEQPHFITRYPFEVSPLARRNDEDPSV 406
Cdd:TIGR00499 320 ALEMVTG-IDFDILKDDETAKALAKEHGIEVAEDSlTLGHILNKFFEQFLEHTLIQPTFITHYPAEISPLAKRDPSNPEF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 407 TDRFELFIGGREIANAYSELNDAEDQAERFMLQVKEKDAGDDEAMHYDADFINALEYGMPPTAGEGIGIDRLVMLLTNSP 486
Cdd:TIGR00499 399 TERFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGIGIDRLVMLLTDAP 478
|
490
....*....|....
gi 15598896 487 SIRDVILFPHMRPQ 500
Cdd:TIGR00499 479 SIRDVLLFPQLRPQ 492
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
1-500 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 610.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 1 MSDQQLDQHELQQEENKLIAQRKEKLAAVREaRAIAFPNDFRRDAYFADLQKQYADKTKEELEAAAIPVKVAGRIMLNR- 79
Cdd:PRK12445 1 MSEQETRGANEAIDFNDELRNRREKLAALRQ-QGVAFPNDFRRDHTSDQLHEEFDAKDNQELESLNIEVSVAGRMMTRRi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 80 ---GSFIVLQDSSERLQVYVNRKTLPEETLAE-IKTWDLGDIIGAEGVLARSGKGDLYVDMTSVRLLTKSLRPLPDKHHG 155
Cdd:PRK12445 80 mgkASFVTLQDVGGRIQLYVARDSLPEGVYNDqFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 156 LTDTEQRYRQRYVDLMVNEETRHTFRVRSQVIAHIRRFLSERGFLEVETPMLQTIPGGAAAKPFETHHNALDMAMFLRIA 235
Cdd:PRK12445 160 LQDQEVRYRQRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 236 PELYLKRLVVGGFEKVFEINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQSVLGTTDVPYGDKVFH 315
Cdd:PRK12445 240 PELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 316 FGEPFVRLSVFDSILKYNPEITAADLNDVEKARAIAKKAGAKVLGHEGLGKLQVMIFEELVEHKLEQPHFITRYPFEVSP 395
Cdd:PRK12445 320 FGKPFEKLTMREAIKKYRPETDMADLDNFDAAKALAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 396 LARRNDEDPSVTDRFELFIGGREIANAYSELNDAEDQAERFMLQVKEKDAGDDEAMHYDADFINALEYGMPPTAGEGIGI 475
Cdd:PRK12445 400 LARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGI 479
|
490 500
....*....|....*....|....*
gi 15598896 476 DRLVMLLTNSPSIRDVILFPHMRPQ 500
Cdd:PRK12445 480 DRMIMLFTNSHTIRDVILFPAMRPQ 504
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
20-500 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 595.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 20 AQRKEKLAAVREARAIAFPNDFRRDAYFADLQKQYADKTK-EELEAAAipVKVAGRIMLNRGS----FIVLQDSSERLQV 94
Cdd:PLN02502 63 ANRLKKVEALRAKGVEPYPYKFDVTHTAPELQEKYGSLENgEELEDVS--VSVAGRIMAKRAFgklaFYDLRDDGGKIQL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 95 YVNRK--TLPEETLAEIKTW-DLGDIIGAEGVLARSGKGDLYVDMTSVRLLTKSLRPLPDKHHGLTDTEQRYRQRYVDLM 171
Cdd:PLN02502 141 YADKKrlDLDEEEFEKLHSLvDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLPDKYHGLTDQETRYRQRYLDLI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 172 VNEETRHTFRVRSQVIAHIRRFLSERGFLEVETPMLQTIPGGAAAKPFETHHNALDMAMFLRIAPELYLKRLVVGGFEKV 251
Cdd:PLN02502 221 ANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRIATELHLKRLVVGGFERV 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 252 FEINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQSVLGTTDVPYGDKVFHFGEPFVRLSVFDSILK 331
Cdd:PLN02502 301 YEIGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYHGIEIDFTPPFRRISMISLVEE 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 332 YNPEITAADLNDVEKAR---AIAKKAGAKVLGHEGLGKLQVMIFEELVEHKLEQPHFITRYPFEVSPLARRNDEDPSVTD 408
Cdd:PLN02502 381 ATGIDFPADLKSDEANAyliAACEKFDVKCPPPQTTGRLLNELFEEFLEETLVQPTFVLDHPVEMSPLAKPHRSKPGLTE 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 409 RFELFIGGREIANAYSELNDAEDQAERFMLQVKEKDAGDDEAMHYDADFINALEYGMPPTAGEGIGIDRLVMLLTNSPSI 488
Cdd:PLN02502 461 RFELFINGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVMLLTDSASI 540
|
490
....*....|..
gi 15598896 489 RDVILFPHMRPQ 500
Cdd:PLN02502 541 RDVIAFPAMKPQ 552
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
173-499 |
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: 539.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 173 NEETRHTFRVRSQVIAHIRRFLSERGFLEVETPMLQTIPGGAAAKPFETHHNALDMAMFLRIAPELYLKRLVVGGFEKVF 252
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 253 EINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQSVLGTTDVPYGDKVFHFGEPFVRLSVFDSILKY 332
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEYGGKELDFTPPFKRVTMVDALKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 333 NPEIT--AADLNDVEKARAIAKKAGAKVLGHEGLGKLQVMIFEELVEHKLEQPHFITRYPFEVSPLARRNDEDPSVTDRF 410
Cdd:cd00775 161 TGIDFpeLDLEQPEELAKLLAKLIKEKIEKPRTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRHRSNPGLTERF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 411 ELFIGGREIANAYSELNDAEDQAERFMLQVKEKDAGDDEAMHYDADFINALEYGMPPTAGEGIGIDRLVMLLTNSPSIRD 490
Cdd:cd00775 241 ELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRD 320
|
....*....
gi 15598896 491 VILFPHMRP 499
Cdd:cd00775 321 VILFPAMRP 329
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
22-500 |
1.73e-164 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 494.10 E-value: 1.73e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 22 RKEKLAAVREARAIAFPNDFRRDAYFADLqkqyADKTKEEleaaaiPVKVAGRIMLNRG----SFIVLQDSSERLQVYVN 97
Cdd:PRK02983 617 RLAKLEALRAAGVDPYPVGVPPTHTVAEA----LDAPTGE------EVSVSGRVLRIRDyggvLFADLRDWSGELQVLLD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 98 RKTLPEETLAEIK-TWDLGDIIGAEGVLARSGKGDLYVDMTSVRLLTKSLRPLPDKHHGLTDTEQRYRQRYVDLMVNEET 176
Cdd:PRK02983 687 ASRLEQGSLADFRaAVDLGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLDLAVNPEA 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 177 RHTFRVRSQVIAHIRRFLSERGFLEVETPMLQTIPGGAAAKPFETHHNALDMAMFLRIAPELYLKRLVVGGFEKVFEINR 256
Cdd:PRK02983 767 RDLLRARSAVVRAVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVERVFELGR 846
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 257 NFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQSVLGTTDVPYGDKvfHFGEPFVRLS-------VFDSI 329
Cdd:PRK02983 847 NFRNEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGAPVVMRPDG--DGVLEPVDISgpwpvvtVHDAV 924
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 330 -LKYNPEITAAdlNDVEKARAIAKKAGAKVLGHEGLGKLQVMIFEELVEHKLEQPHFITRYPFEVSPLARRNDEDPSVTD 408
Cdd:PRK02983 925 sEALGEEIDPD--TPLAELRKLCDAAGIPYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPHRSDPGLAE 1002
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 409 RFELFIGGREIANAYSELNDAEDQAERFMLQVKEKDAGDDEAMHYDADFINALEYGMPPTAGEGIGIDRLVMLLTNSpSI 488
Cdd:PRK02983 1003 RWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLTGR-SI 1081
|
490
....*....|..
gi 15598896 489 RDVILFPHMRPQ 500
Cdd:PRK02983 1082 RETLPFPLVKPR 1093
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
2-499 |
9.87e-128 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 383.98 E-value: 9.87e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 2 SDQQLDQHELQQE---ENKLIAQRKEKLAAVREARAI-AFPNDFRRDAYFADLQKQYAD-KTKEELEAAaiPVKVAGRIM 76
Cdd:PTZ00417 65 SVQASKDKKKEEEaevDPRLYYENRSKFIQEQKAKGInPYPHKFERTITVPEFVEKYQDlASGEHLEDT--ILNVTGRIM 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 77 LNRGS-----FIVLQDSSERLQVYVN------RKTLPEETLAEIKTwdlGDIIGAEGVLARSGKGDLYVDMTSVRLLTKS 145
Cdd:PTZ00417 143 RVSASgqklrFFDLVGDGAKIQVLANfafhdhTKSNFAECYDKIRR---GDIVGIVGFPGKSKKGELSIFPKETIILSPC 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 146 LRPLPDKHhGLTDTEQRYRQRYVDLMVNEETRHTFRVRSQVIAHIRRFLSERGFLEVETPMLQTIPGGAAAKPFETHHNA 225
Cdd:PTZ00417 220 LHMLPMKY-GLKDTEIRYRQRYLDLMINESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHND 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 226 LDMAMFLRIAPELYLKRLVVGGFEKVFEINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQSVLGT- 304
Cdd:PTZ00417 299 LDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGTy 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 305 -----TDVPYGDKV-FHFGEPFVRLSVFDSILKYNPEITAADLND---VEKARAIAKKAGAKVLGHEGLGKLQVMIFEEL 375
Cdd:PTZ00417 379 kilynKDGPEKDPIeIDFTPPYPKVSIVEELEKLTNTKLEQPFDSpetINKMINLIKENKIEMPNPPTAAKLLDQLASHF 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 376 VEHKL-EQPHFITRYPFEVSPLARRNDEDPSVTDRFELFIGGREIANAYSELNDAEDQAERFMLQVKEKDAGDDEAMHYD 454
Cdd:PTZ00417 459 IENKYpNKPFFIIEHPQIMSPLAKYHRSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFD 538
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15598896 455 ADFINALEYGMPPTAGEGIGIDRLVMLLTNSPSIRDVILFPHMRP 499
Cdd:PTZ00417 539 AAFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFPTMRP 583
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
158-498 |
3.53e-124 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 365.35 E-value: 3.53e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 158 DTEQRYRQRYVDLmVNEETRHTFRVRSQVIAHIRRFLSERGFLEVETPMLQTIPGGAAAKPFETHHNALDMAMFLRIAPE 237
Cdd:pfam00152 1 DEETRLKYRYLDL-RRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 238 LYLKRLVVGGFEKVFEINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQSVLGTTDVPYGDKVFHFG 317
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 318 EPFVRLSVFDSILKYNPEITAADLNDVEKAraiakkagakvlgheglgKLQVMIfEELVEHKLEQPHFITRYPFEVSPLA 397
Cdd:pfam00152 160 KPFPRITYAEAIEKLNGKDVEELGYGSDKP------------------DLRFLL-ELVIDKNKFNPLWVTDFPAEHHPFT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 398 RRNDED-PSVTDRFELFIGGREIANAYSELNDAEDQAERFmlqvKEKDAGDDEAMHYDADFINALEYGMPPTAGEGIGID 476
Cdd:pfam00152 221 MPKDEDdPALAEAFDLVLNGVEIGGGSIRIHDPELQEERF----EEQGLDPEEAEEKFGFYLDALKYGAPPHGGLGIGLD 296
|
330 340
....*....|....*....|..
gi 15598896 477 RLVMLLTNSPSIRDVILFPHMR 498
Cdd:pfam00152 297 RLVMLLTGLESIREVIAFPKTR 318
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
180-499 |
2.94e-115 |
|
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: 340.61 E-value: 2.94e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 180 FRVRSQVIAHIRRFLSERGFLEVETPMLQTIPGGAAAKPFETHHNALDMAMFLRIAPELYLKRLVVGGFEKVFEINRNFR 259
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 260 NEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQSVLGTTDVPYGDKVFHFGEPFVRLSvfdsilkynpeitaa 339
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGFELEDFGLPFPRLT--------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 340 dlndvekaraiakkagakvlgheglgklqvmiFEELVEhKLEQPHFITRYPFE-VSPLARRNDEDPSVTDRFELFIGGRE 418
Cdd:cd00669 146 --------------------------------YREALE-RYGQPLFLTDYPAEmHSPLASPHDVNPEIADAFDLFINGVE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 419 IANAYSELNDAEDQAERFMLQVKEKDAGddeaMHYDADFINALEYGMPPTAGEGIGIDRLVMLLTNSPSIRDVILFPHMR 498
Cdd:cd00669 193 VGNGSSRLHDPDIQAEVFQEQGINKEAG----MEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMR 268
|
.
gi 15598896 499 P 499
Cdd:cd00669 269 R 269
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
64-498 |
3.88e-113 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 348.95 E-value: 3.88e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 64 AAAIPVKVAGRIM----LNRGSFIVLQDSSERLQVYVN-RKTLPEETLAEIK-TWDLGDIIGAEGVLARSGKGDLYVDMT 137
Cdd:PTZ00385 105 AAQATVRVAGRVTsvrdIGKIIFVTIRSNGNELQVVGQvGEHFTREDLKKLKvSLRVGDIIGADGVPCRMQRGELSVAAS 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 138 SVRLLT------KSLRPLPDKHHGLTDTEQRYRQRYVDLMVNEETRHTFRVRSQVIAHIRRFLSERGFLEVETPMLQTIP 211
Cdd:PTZ00385 185 RMLILSpyvctdQVVCPNLRGFTVLQDNDVKYRYRFTDMMTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPVLHTVA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 212 GGAAAKPFETHHNALDMAMFLRIAPELYLKRLVVGGFEKVFEINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTE 291
Cdd:PTZ00385 265 SGANAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDLMPMTE 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 292 ELFRELAQSVLGTTDV------PYGDKV-FHFGEPFVRLSVFDSILKYNpEITAADLNDVEKARAIAKKAgAKVLGHE-- 362
Cdd:PTZ00385 345 DIFRQLAMRVNGTTVVqiypenAHGNPVtVDLGKPFRRVSVYDEIQRMS-GVEFPPPNELNTPKGIAYMS-VVMLRYNip 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 363 -GLGKLQVMIFEELVE----HKLEQPHFITRYPFEVSPLARRNDEDPSVTDRFELFIGGREIANAYSELNDAEDQAERFM 437
Cdd:PTZ00385 423 lPPVRTAAKMFEKLIDffitDRVVEPTFVMDHPLFMSPLAKEQVSRPGLAERFELFVNGIEYCNAYSELNDPHEQYHRFQ 502
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598896 438 LQVKEKDAGDDEAMHYDADFINALEYGMPPTAGEGIGIDRLVMLLTNSPSIRDVILFPHMR 498
Cdd:PTZ00385 503 QQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLR 563
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
176-492 |
4.95e-81 |
|
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: 254.26 E-value: 4.95e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 176 TRHTFRVRSQVIAHIRRFLSERGFLEVETPMLQTIPGGAAA-KPFET---HHNALDMAMFLRIAPELYLKRLVVGGFEKV 251
Cdd:COG2269 2 SREALRARARLLAAIRAFFAERGVLEVETPALSVAPGTDPHlDSFATefiGPDGGGRPLYLHTSPEFAMKRLLAAGSGPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 252 FEINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQSVLGttdvpygdkvfhfgEPFVRLSVFDSILK 331
Cdd:COG2269 82 YQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAAGF--------------APAERLSYQEAFLR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 332 Y---NP-EITAADLndvekaRAIAKKAGAKV---LGHEGLgkLQVmIFEELVEHKL--EQPHFITRYPFEVSPLARRNDE 402
Cdd:COG2269 148 YlgiDPlTADLDEL------AAAAAAAGLRVaddDDRDDL--LDL-LLSERVEPQLgrDRPTFLYDYPASQAALARISPD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 403 DPSVTDRFELFIGGREIANAYSELNDAEDQAERFMLQVKEKDAGDDEAMHYDADFINALEYGMPPTAGEGIGIDRLVMLL 482
Cdd:COG2269 219 DPRVAERFELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLA 298
|
330
....*....|
gi 15598896 483 TNSPSIRDVI 492
Cdd:COG2269 299 LGAERIDDVL 308
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
193-492 |
2.11e-76 |
|
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: 241.69 E-value: 2.11e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 193 FLSERGFLEVETPMLQTIPGGAAA-KPFETH---HNALDMAMFLRIAPELYLKRLVVGGFEKVFEINRNFRNEGVSTRHN 268
Cdd:TIGR00462 1 FFAERGVLEVETPLLSPAPVTDPHlDAFATEfvgPDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 269 PEFTMLEFYQAYADYEDNMDLTEELFRELAQsvlgttdvpygdkvfHFGEPFVRLSVFDSILKY---NPEITaadlnDVE 345
Cdd:TIGR00462 81 PEFTMLEWYRPGFDYHDLMDEVEALLQELLG---------------DPFAPAERLSYQEAFLRYagiDPLTA-----SLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 346 KARAIAKKAGakVLGHEGLGK---LQVmIFEELVEHKL--EQPHFITRYPFEVSPLARRNDEDPSVTDRFELFIGGREIA 420
Cdd:TIGR00462 141 ELQAAAAAHG--IRASEEDDRddlLDL-LFSEKVEPHLgfGRPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELA 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598896 421 NAYSELNDAEDQAERFMLQVKEKDAGDDEAMHYDADFINALEYGMPPTAGEGIGIDRLVMLLTNSPSIRDVI 492
Cdd:TIGR00462 218 NGFHELTDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVL 289
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
183-491 |
5.48e-60 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 199.77 E-value: 5.48e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 183 RSQVIAHIRRFLSERGFLEVETPMLQTIPG-GAAAKPFETHHNALDMA----MFLRIAPELYLKRLVVGGFEKVFEINRN 257
Cdd:PRK09350 8 RAKIIAEIRRFFADRGVLEVETPILSQATVtDIHLVPFETRFVGPGASqgktLWLMTSPEYHMKRLLAAGSGPIFQICKS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 258 FRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQSvlgttdvpygdkvfhfgEPFVRLSVFDSILKY-NPEI 336
Cdd:PRK09350 88 FRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDC-----------------EPAESLSYQQAFLRYlGIDP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 337 TAADLndvEKARAIAKKAGAKVLGH--EGLGKLQVMIFEELVEHKL--EQPHFITRYPFEVSPLARRNDEDPSVTDRFEL 412
Cdd:PRK09350 151 LSADK---TQLREVAAKLGLSNIADeeEDRDTLLQLLFTFGVEPNIgkEKPTFVYHFPASQAALAKISTEDHRVAERFEV 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598896 413 FIGGREIANAYSELNDAEDQAERFMLQVKEKDAGDDEAMHYDADFINALEYGMPPTAGEGIGIDRLVMLLTNSPSIRDV 491
Cdd:PRK09350 228 YFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALGVDRLIMLALGAESISEV 306
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
69-170 |
5.99e-50 |
|
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: 166.50 E-value: 5.99e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 69 VKVAGRIMLNRGS----FIVLQDSSERLQVYVNRKTLPEETLAEIK-TWDLGDIIGAEGVLARSGKGDLYVDMTSVRLLT 143
Cdd:cd04322 2 VSVAGRIMSKRGSgklsFADLQDESGKIQVYVNKDDLGEEEFEDFKkLLDLGDIIGVTGTPFKTKTGELSIFVKEFTLLS 81
|
90 100
....*....|....*....|....*..
gi 15598896 144 KSLRPLPDKHHGLTDTEQRYRQRYVDL 170
Cdd:cd04322 82 KSLRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
43-498 |
6.12e-48 |
|
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: 171.00 E-value: 6.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 43 RDAYFADLQKQYADKTkeeleaaaipVKVAGRIMLNRGS----FIVLQDSSERLQVYVNRKTLPE-ETLAEIKTwdlGDI 117
Cdd:COG0017 1 KRTYIKDLLPEHVGQE----------VTVAGWVRTKRDSggisFLILRDGSGFIQVVVKKDKLENfEEAKKLTT---ESS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 118 IGAEGVLARSG--KGDLYVDMTSVRLLTKSLRPLP--DKHHGLtdtEQRYRQRYVDLMVNEeTRHTFRVRSQVIAHIRRF 193
Cdd:COG0017 68 VEVTGTVVESPraPQGVELQAEEIEVLGEADEPYPlqPKRHSL---EFLLDNRHLRLRTNR-FGAIFRIRSELARAIREF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 194 LSERGFLEVETPMLqtIPGGA--AAKPFETHHnaLDMAMFLRIAPELYlKRLVVGGFEKVFEINRNFRNEGVST-RHNPE 270
Cdd:COG0017 144 FQERGFVEVHTPII--TASATegGGELFPVDY--FGKEAYLTQSGQLY-KEALAMALEKVYTFGPTFRAEKSNTrRHLAE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 271 FTMLEFYQAYADYEDNMDLTEELFRELAQSVLGTtdvpYGDKVFHFGEPFVRLSVfdsILKYN-PEITAADlndvekARA 349
Cdd:COG0017 219 FWMIEPEMAFADLEDVMDLAEEMLKYIIKYVLEN----CPEELEFLGRDVERLEK---VPESPfPRITYTE------AIE 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 350 IAKKAGAKV-----LG--HEglgklqvmifEELVEHKLEQPHFITRYPFEVSPL-ARRNDEDPSVTDRFELfiggreIAN 421
Cdd:COG0017 286 ILKKSGEKVewgddLGteHE----------RYLGEEFFKKPVFVTDYPKEIKAFyMKPNPDDPKTVAAFDL------LAP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 422 AYSEL-------NDAEDQAERFmlqvkeKDAGDDEAmHYDaDFINALEYGMPPTAGEGIGIDRLVMLLTNSPSIRDVILF 494
Cdd:COG0017 350 GIGEIiggsqreHRYDVLVERI------KEKGLDPE-DYE-WYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPF 421
|
....
gi 15598896 495 PHMR 498
Cdd:COG0017 422 PRDP 425
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
82-498 |
9.40e-43 |
|
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: 157.29 E-value: 9.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 82 FIVLQDSSERLQVYVNRKTLPEETLAEIKTWDLGDIIGAEGVLARSGK--GDLYVDMTSVRLLTKSLRPLP----DKHHG 155
Cdd:TIGR00458 32 FVLLRDREGLIQITAPAKKVSKNLFKWAKKLNLESVVAVRGIVKIKEKapGGFEIIPTKIEVINEAKEPLPldptEKVPA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 156 LTDTeqRYRQRYVDLMvNEETRHTFRVRSQVIAHIRRFLSERGFLEVETPMLQTIPGGAAAKPFETHHnaLDMAMFLRIA 235
Cdd:TIGR00458 112 ELDT--RLDYRFLDLR-RPTVQAIFRIRSGVLESVREFLAEEGFIEVHTPKLVASATEGGTELFPITY--FEREAFLGQS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 236 PELYLKRLVVGGFEKVFEINRNFRNEGVST-RHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQSVLGTTDVPYGDKVF 314
Cdd:TIGR00458 187 PQLYKQQLMAAGFERVYEIGPIFRAEEHNThRHLNEATSIDIEMAFEDHHDVMDILEELVVRVFEDVPERCAHQLETLEF 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 315 HF---GEPFVRLSVfdsilkynpeitaadlndvEKARAIAKKAGAKVLGHEGLGKLQvmifEELVEHKLEQPHFITRYPF 391
Cdd:TIGR00458 267 KLekpEGKFVRLTY-------------------DEAIEMANAKGVEIGWGEDLSTEA----EKALGEEMDGLYFITDWPT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 392 EVSPLARRNDED-PSVTDRFELFIGGREIANAYSELNDAEdqaerfMLQVKEKDAGddeaMHYDA--DFINALEYGMPPT 468
Cdd:TIGR00458 324 EIRPFYTMPDEDnPEISKSFDLMYRDLEISSGAQRIHLHD------LLVERIKAKG----LNPEGfkDYLEAFSYGMPPH 393
|
410 420 430
....*....|....*....|....*....|
gi 15598896 469 AGEGIGIDRLVMLLTNSPSIRDVILFPHMR 498
Cdd:TIGR00458 394 AGWGLGAERFVMFLLGLKNIREAVLFPRDR 423
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
69-495 |
1.69e-42 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 156.50 E-value: 1.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 69 VKVAG---RIM-LNRGSFIVLQDSSERLQVYVNRKTLPEeTLAEIKTWDLGDIIGAEGVLARSGK--GDLYVDMTSVRLL 142
Cdd:PRK05159 19 VTLAGwvhEIRdLGGIAFLILRDRSGIIQVVVKKKVDEE-LFETIKKLKRESVVSVTGTVKANPKapGGVEVIPEEIEVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 143 TKSLRPLPDKHHG--LTDTEQRYRQRYVDLMvNEETRHTFRVRSQVIAHIRRFLSERGFLEVETPML--QTIPGGAAAKP 218
Cdd:PRK05159 98 NKAEEPLPLDISGkvLAELDTRLDNRFLDLR-RPRVRAIFKIRSEVLRAFREFLYENGFTEIFTPKIvaSGTEGGAELFP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 219 ---FEthHNAldmamFLRIAPELYLKRLVVGGFEKVFEINRNFRNEGVST-RHNPEFTMLEFYQAYAD-YEDNMDLTEEL 293
Cdd:PRK05159 177 idyFE--KEA-----YLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTsRHLNEYTSIDVEMGFIDdHEDVMDLLENL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 294 FRELAQSVlgttdvpygdkVFHFGEPFVRLSV-FDSILKYNPEITAADlndvekARAIAKKAGAKV-----LGHEGLGKL 367
Cdd:PRK05159 250 LRYMYEDV-----------AENCEKELELLGIeLPVPETPIPRITYDE------AIEILKSKGNEIswgddLDTEGERLL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 368 QvmifeELVEHKLEQPH-FITRYPFEVSPL-ARRNDEDPSVTDRFELFIGGREIANAYSELNDAEDQAERFmlqvKEKDa 445
Cdd:PRK05159 313 G-----EYVKEEYGSDFyFITDYPSEKRPFyTMPDEDDPEISKSFDLLFRGLEITSGGQRIHRYDMLVESI----KEKG- 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 15598896 446 GDDEAMHYdadFINALEYGMPPTAGEGIGIDRLVMLLTNSPSIRDVILFP 495
Cdd:PRK05159 383 LNPESFEF---YLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
158-495 |
5.24e-39 |
|
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: 144.25 E-value: 5.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 158 DTEQRYRQRYVDLMvNEETRHTFRVRSQVIAHIRRFLSERGFLEVETPMLQTIP--GGAAAKP---FETHhnaldmaMFL 232
Cdd:cd00776 3 NLETLLDNRHLDLR-TPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDteGGAELFKvsyFGKP-------AYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 233 RIAPELYlKRLVVGGFEKVFEINRNFRNEGVST-RHNPEFTMLEFYQAYA-DYEDNMDLTEELFRELAQSVL------GT 304
Cdd:cd00776 75 AQSPQLY-KEMLIAALERVYEIGPVFRAEKSNTrRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLercakeLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 305 TDVPYGDKVFHFGEPFVRLSvfdsilkYnpeitaadlndvEKARAIAKKAGAKV-------LGHEGLGKLqvmifeelVE 377
Cdd:cd00776 154 LVNQLNRELLKPLEPFPRIT-------Y------------DEAIELLREKGVEEevkwgedLSTEHERLL--------GE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 378 HKLEQPHFITRYPFEVSPL-ARRNDEDPSVTDRFELFI-GGREIANAYSELNDAEDQAERFmlqvkeKDAGDDEAMHYDa 455
Cdd:cd00776 207 IVKGDPVFVTDYPKEIKPFyMKPDDDNPETVESFDLLMpGVGEIVGGSQRIHDYDELEERI------KEHGLDPESFEW- 279
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15598896 456 dFINALEYGMPPTAGEGIGIDRLVMLLTNSPSIRDVILFP 495
Cdd:cd00776 280 -YLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
180-495 |
4.50e-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: 129.62 E-value: 4.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 180 FRVRSQVIAHIRRFLSERGFLEVETPML-QTIPGGAA--AKPFETHHNaldmaMF--LRIAPELYLKRLVVGGFEKVFEI 254
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILtKSTPEGARdfLVPSRLHPG-----KFyaLPQSPQLFKQLLMVSGFDRYFQI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 255 NRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQSVLGTTDVpygdkvfhfgEPFVRLSVFDSILKYnp 334
Cdd:cd00777 76 ARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGVELT----------TPFPRMTYAEAMERY-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 335 eitaadlndvekaraiakkagakvlgheGLGKLQVMIF------EElvEHKLEQPHfitrYPF-----EVSPLARRNDED 403
Cdd:cd00777 144 ----------------------------GFKFLWIVDFplfewdEE--EGRLVSAH----HPFtapkeEDLDLLEKDPED 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 404 pSVTDRFELFIGGREIANAYSELNDAEDQAERFmlqvkeKDAGDDEAMHYD--ADFINALEYGMPPTAGEGIGIDRLVML 481
Cdd:cd00777 190 -ARAQAYDLVLNGVELGGGSIRIHDPDIQEKVF------EILGLSEEEAEEkfGFLLEAFKYGAPPHGGIALGLDRLVML 262
|
330
....*....|....
gi 15598896 482 LTNSPSIRDVILFP 495
Cdd:cd00777 263 LTGSESIRDVIAFP 276
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
160-495 |
1.46e-29 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 122.10 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 160 EQRYRQRYVDLMvNEETRHTFRVRSQVIAHIRRFLSERGFLEVETPML--QTiPGGAAakpfethhnalDmamFL---RI 234
Cdd:PRK00476 122 ELRLKYRYLDLR-RPEMQKNLKLRSKVTSAIRNFLDDNGFLEIETPILtkST-PEGAR-----------D---YLvpsRV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 235 ----------APELYLKRLVVGGFEKVFEINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQSVLGT 304
Cdd:PRK00476 186 hpgkfyalpqSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEFTQIDIEMSFVTQEDVMALMEGLIRHVFKEVLGV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 305 tDVPygdkvfhfgEPFVRLSVFDSILKY--------NP-EIT--------------AADLNDVEKARAI----------- 350
Cdd:PRK00476 266 -DLP---------TPFPRMTYAEAMRRYgsdkpdlrFGlELVdvtdlfkdsgfkvfAGAANDGGRVKAIrvpggaaqlsr 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 351 ---------AKKAGAKVLG-----------------------------------------------HEGLGKLQVMIFEE 374
Cdd:PRK00476 336 kqideltefAKIYGAKGLAyikvnedglkgpiakflseeelaallertgakdgdliffgadkakvvNDALGALRLKLGKE 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 375 --LVEHKLEQPHFITRYP-FEVSPLARR-----------NDEDPsvtDRFELFIGGREIANAY------SEL-------N 427
Cdd:PRK00476 416 lgLIDEDKFAFLWVVDFPmFEYDEEEGRwvaahhpftmpKDEDL---DELETTDPGKARAYAYdlvlngYELgggsiriH 492
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598896 428 DAEDQAERFmlqvkekdagddEAMHYDAD--------FINALEYGMPPTAGEGIGIDRLVMLLTNSPSIRDVILFP 495
Cdd:PRK00476 493 RPEIQEKVF------------EILGISEEeaeekfgfLLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
82-495 |
3.87e-29 |
|
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: 120.87 E-value: 3.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 82 FIVLQDSSERLQVYVNRKTLPEetlaeikTWDLGDIIGAEGVLARSGK---------------GDLYVDMTSVRLLTKSl 146
Cdd:COG0173 36 FIDLRDRYGITQVVFDPDDSAE-------AFEKAEKLRSEYVIAVTGKvrarpegtvnpklptGEIEVLASELEILNKA- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 147 RPLPDKHHGLTDT--EQRYRQRYVDLMvNEETRHTFRVRSQVIAHIRRFLSERGFLEVETPMLQ--TiPGGAAakpfeth 222
Cdd:COG0173 108 KTPPFQIDDDTDVseELRLKYRYLDLR-RPEMQKNLILRHKVTKAIRNYLDENGFLEIETPILTksT-PEGAR------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 223 hnalDmamFL---RI----------APELYLKRLVVGGFEKVFEINRNFRNEgvSTRHN--PEFTMLEFYQAYADYEDNM 287
Cdd:COG0173 179 ----D---YLvpsRVhpgkfyalpqSPQLFKQLLMVSGFDRYFQIARCFRDE--DLRADrqPEFTQLDIEMSFVDQEDVF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 288 DLTEELFRELAQSVLGTtDVPygdkvfhfgEPFVRLSVFDSILKY--------NP-EITaaDLNDVEKA----------- 347
Cdd:COG0173 250 ELMEGLIRHLFKEVLGV-ELP---------TPFPRMTYAEAMERYgsdkpdlrFGlELV--DVTDIFKDsgfkvfagaae 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 348 -----RAI-------------------AKKAGAKVLG------------------------------------------- 360
Cdd:COG0173 318 nggrvKAInvpggaslsrkqideltefAKQYGAKGLAyikvnedglkspiakflseeelaailerlgakpgdliffvadk 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 361 ----HEGLGKLQVMIFEEL---VEHKLEqPHFITRYP-FEVSPLARR-----------NDEDpsvtdrFELFIG--GREI 419
Cdd:COG0173 398 pkvvNKALGALRLKLGKELgliDEDEFA-FLWVVDFPlFEYDEEEGRwvamhhpftmpKDED------LDLLETdpGKVR 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 420 ANAY------SEL-------NDAEDQAERFmlqvkekdagddEAMHYDAD--------FINALEYGMPPTAGEGIGIDRL 478
Cdd:COG0173 471 AKAYdlvlngYELgggsiriHDPELQEKVF------------ELLGISEEeaeekfgfLLEAFKYGAPPHGGIAFGLDRL 538
|
570
....*....|....*..
gi 15598896 479 VMLLTNSPSIRDVILFP 495
Cdd:COG0173 539 VMLLAGEDSIRDVIAFP 555
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
11-495 |
1.02e-27 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 116.34 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 11 LQQEENKLIAQRKEKLAAVREARAIAFPNDFRRDAyfadLQKQYADKTKEEL-----------------EAAAIPVKVAG 73
Cdd:PLN02850 13 ISKKAAKKAAAKAEKLRREATAKAAAASLEDEDDP----LASNYGDVPLEELqskvtgrewtdvsdlgeELAGSEVLIRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 74 RIMLNRG----SFIVLQDSSERLQ--VYVNRKTLPEETLAEIKTWDLGDIIGAEGVLA------RSGKGDLYVDMTSVRL 141
Cdd:PLN02850 89 RVHTIRGkgksAFLVLRQSGFTVQcvVFVSEVTVSKGMVKYAKQLSRESVVDVEGVVSvpkkpvKGTTQQVEIQVRKIYC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 142 LTKSLRPLP-----------DKHHGLTDTEQRYRqryvdlmVNEETR--------------HTFRVRSQVIAHIRRFLSE 196
Cdd:PLN02850 169 VSKALATLPfnvedaarsesEIEKALQTGEQLVR-------VGQDTRlnnrvldlrtpanqAIFRIQSQVCNLFREFLLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 197 RGFLEVETPML--QTIPGGAAAkpFETHHNAldMAMFLRIAPELYLKRLVVGGFEKVFEINRNFRNEGVST-RHNPEFTM 273
Cdd:PLN02850 242 KGFVEIHTPKLiaGASEGGSAV--FRLDYKG--QPACLAQSPQLHKQMAICGDFRRVFEIGPVFRAEDSFThRHLCEFTG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 274 LEFYQAYAD-YEDNMDLTEELFRELAQSV-------LGTTDVPYGDKVFHFGEPFVRLsvfdsilkynpeitaadlnDVE 345
Cdd:PLN02850 318 LDLEMEIKEhYSEVLDVVDELFVAIFDGLnerckkeLEAIREQYPFEPLKYLPKTLRL-------------------TFA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 346 KARAIAKKAGAKVLGHEGLGKLQVMIFEELVEHKLEQPHFI-TRYPFEVSPLARRND-EDPSVTDRFELFIGGREIANAY 423
Cdd:PLN02850 379 EGIQMLKEAGVEVDPLGDLNTESERKLGQLVKEKYGTDFYIlHRYPLAVRPFYTMPCpDDPKYSNSFDVFIRGEEIISGA 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598896 424 SELNDAEDQAERfmlqVKEK--DAGDdeamhyDADFINALEYGMPPTAGEGIGIDRLVMLLTNSPSIRDVILFP 495
Cdd:PLN02850 459 QRVHDPELLEKR----AEECgiDVKT------ISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFP 522
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
171-495 |
4.21e-25 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 105.87 E-value: 4.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 171 MVNEETRHTFRVRSQVIAHIRRFLSERGFLEVETPMLQTI-----PGGAAAKPFETHHNALDMAMFLRIAPELYlKRLVV 245
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPStdplmGLGSDLPVKQISIDFYGVEYYLADSMILH-KQLAL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 246 GGFEKVFEINRNFRNEGV---STRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQSVLGTTD---VPYGDKVFHFGEP 319
Cdd:PRK06462 100 RMLGKIFYLSPNFRLEPVdkdTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEdelEFFGRDLPHLKRP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 320 FVRLSVFDsilkynpeitAADLNDVEKARAIAKKagakVLGHEGlgklqvmifEELVEHKLEQPHFITRYPFEVSPLARR 399
Cdd:PRK06462 180 FKRITHKE----------AVEILNEEGCRGIDLE----ELGSEG---------EKSLSEHFEEPFWIIDIPKGSREFYDR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 400 ndEDPSVTDRFELF-----------IGGREIANAYSELNDaedqaerfmlqvKEKDAGDDEAmHYDaDFINALEYGMPPT 468
Cdd:PRK06462 237 --EDPERPGVLRNYdlllpegygeaVSGGEREYEYEEIVE------------RIREHGVDPE-KYK-WYLEMAKEGPLPS 300
|
330 340
....*....|....*....|....*..
gi 15598896 469 AGEGIGIDRLVMLLTNSPSIRDVILFP 495
Cdd:PRK06462 301 AGFGIGVERLTRYICGLRHIREVQPFP 327
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
69-495 |
1.15e-23 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 104.49 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 69 VKVAGRIMLNRG----SFIVLQDSSERLQVYVNRKTLPE--ETLAEIKtwdLGDIIGAEGVL-ARSGK--------GDLY 133
Cdd:PLN02903 75 VTLCGWVDLHRDmgglTFLDVRDHTGIVQVVTLPDEFPEahRTANRLR---NEYVVAVEGTVrSRPQEspnkkmktGSVE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 134 VDMTSVRLLTKSLRPLP------DKHHGLTDTEQRYRQRYVDLMVNEETRHtFRVRSQVIAHIRRFLSER-GFLEVETPM 206
Cdd:PLN02903 152 VVAESVDILNVVTKSLPflvttaDEQKDSIKEEVRLRYRVLDLRRPQMNAN-LRLRHRVVKLIRRYLEDVhGFVEIETPI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 207 L-QTIPGGAAAKPFETHhnaLDMAMF--LRIAPELYLKRLVVGGFEKVFEINRNFRNEGVSTRHNPEFTMLEFYQAYADY 283
Cdd:PLN02903 231 LsRSTPEGARDYLVPSR---VQPGTFyaLPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDMELAFTPL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 284 EDNMDLTEELFRELAQSVLGtTDVP--------------YG-DKV-FHFGEPFVRLS---------VF------------ 326
Cdd:PLN02903 308 EDMLKLNEDLIRQVFKEIKG-VQLPnpfprltyaeamskYGsDKPdLRYGLELVDVSdvfaessfkVFagalesggvvka 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 327 -----------DSILK----YN----------PEITAADLNDVEKARAIAKK------------------------AGAK 357
Cdd:PLN02903 387 icvpdgkkisnNTALKkgdiYNeaiksgakglAFLKVLDDGELEGIKALVESlspeqaeqllaacgagpgdlilfaAGPT 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 358 VLGHEGLGKLQVMIFEE--LVEHKLEQPHFITRYP-FEVSPLARR-----------NDEDPS--VTDR---FELFIGGRE 418
Cdd:PLN02903 467 SSVNKTLDRLRQFIAKTldLIDPSRHSILWVTDFPmFEWNEDEQRlealhhpftapNPEDMGdlSSARalaYDMVYNGVE 546
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598896 419 IANAYSELNDAEDQAERFMLqvkeKDAGDDEAMHYDADFINALEYGMPPTAGEGIGIDRLVMLLTNSPSIRDVILFP 495
Cdd:PLN02903 547 IGGGSLRIYRRDVQQKVLEA----IGLSPEEAESKFGYLLEALDMGAPPHGGIAYGLDRLVMLLAGAKSIRDVIAFP 619
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
162-501 |
1.27e-22 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 101.60 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 162 RYRQRYVDLMVNEETRHTFRvRSQVIAHIRRFLSERGFLEVETPML-QTIPGGAAAK--PFETHHNALdmaMFLRIAPEL 238
Cdd:PRK12820 139 RLQYRYLDIRRPAMQDHLAK-RHRIIKCARDFLDSRGFLEIETPILtKSTPEGARDYlvPSRIHPKEF---YALPQSPQL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 239 YLKRLVVGGFEKVFEINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQsvLGTTDV-------PYGD 311
Cdd:PRK12820 215 FKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFTQLDIEASFIDEEFIFELIEELTARMFA--IGGIALprpfprmPYAE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 312 KV---------FHFGEPFV---------RLSVFDSILKYNPEITAADLN-----------DVEKARAIAKKAGAKVLG-- 360
Cdd:PRK12820 293 AMdttgsdrpdLRFDLKFAdatdifentRYGIFKQILQRGGRIKGINIKgqseklsknvlQNEYAKEIAPSFGAKGMTwm 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 361 ---------------------------HEGLGKLQVMIFE---ELVEHKLEQ------------------PHFITRYP-F 391
Cdd:PRK12820 373 raeaggldsnivqffsadekealkrrfHAEDGDVIIMIADascAIVLSALGQlrlhladrlglipegvfhPLWITDFPlF 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 392 EVS----------PLAR--RNDEDP-------SVTDR-FELFIGGREIANAYSELNDAEDQAERF-MLQVKEKDAGDDEA 450
Cdd:PRK12820 453 EATddggvtsshhPFTApdREDFDPgdieellDLRSRaYDLVVNGEELGGGSIRINDKDIQLRIFaALGLSEEDIEDKFG 532
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 15598896 451 MhydadFINALEYGMPPTAGEGIGIDRLVMLLTNSPSIRDVILFPHMRPQA 501
Cdd:PRK12820 533 F-----FLRAFDFAAPPHGGIALGLDRVVSMILQTPSIREVIAFPKNRSAA 578
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
50-497 |
3.85e-20 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 92.86 E-value: 3.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 50 LQKQYADKTkeeleaaaipVKVAGRIMLNRGS----FIVLQDSS--ERLQVYVNRKtlpEETLAEIKTWDLGDIIGAEGV 123
Cdd:PRK03932 10 LKGKYVGQE----------VTVRGWVRTKRDSgkiaFLQLRDGScfKQLQVVKDNG---EEYFEEIKKLTTGSSVIVTGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 124 LARS-GKGDLY-VDMTSVRLLTKSLR--PLPDKHHGLtDT--EQRY-RQRyvdlmvneeTR---HTFRVRSQVIAHIRRF 193
Cdd:PRK03932 77 VVESpRAGQGYeLQATKIEVIGEDPEdyPIQKKRHSI-EFlrEIAHlRPR---------TNkfgAVMRIRNTLAQAIHEF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 194 LSERGFLEVETPMLQTIPGGAAAKPFETHHNALDMAM-------FLRIAPELYLKRLVVgGFEKVFEINRNFRNEGVST- 265
Cdd:PRK03932 147 FNENGFVWVDTPIITASDCEGAGELFRVTTLDLDFSKdffgkeaYLTVSGQLYAEAYAM-ALGKVYTFGPTFRAENSNTr 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 266 RHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQSVL--------------GTTDVpygDKVFHFGE-PFVRLSvfdsil 330
Cdd:PRK03932 226 RHLAEFWMIEPEMAFADLEDNMDLAEEMLKYVVKYVLencpddleflnrrvDKGDI---ERLENFIEsPFPRIT------ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 331 kYnpeitaadlndvEKARAIAKKAGAKV---------LGHEglgklqvmifEE--LVEHKLEQPHFITRYPFEVSPLARR 399
Cdd:PRK03932 297 -Y------------TEAIEILQKSGKKFefpvewgddLGSE----------HEryLAEEHFKKPVFVTNYPKDIKAFYMR 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 400 NDEDPSVTDRFELF-------IGG--REianayselndaedqaERF-MLQVKEKDAG-DDEAMHYDADfinaL-EYGMPP 467
Cdd:PRK03932 354 LNPDGKTVAAMDLLapgigeiIGGsqRE---------------ERLdVLEARIKELGlNKEDYWWYLD----LrRYGSVP 414
|
490 500 510
....*....|....*....|....*....|
gi 15598896 468 TAGEGIGIDRLVMLLTNSPSIRDVILFPHM 497
Cdd:PRK03932 415 HSGFGLGFERLVAYITGLDNIRDVIPFPRT 444
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
182-300 |
5.59e-20 |
|
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: 88.33 E-value: 5.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 182 VRSQVIAHIRRFLSERGFLEVETPMLQTIPGGAAA----KPFETHHNALDMAMFLRIAPELYLKRLVVG----GFEKVFE 253
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAghepKDLLPVGAENEEDLYLRPTLEPGLVRLFVShirkLPLRLAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 15598896 254 INRNFRNEG--VSTRHNPEFTMLEFYQAYADYEDN------MDLTEELFRELAQS 300
Cdd:cd00768 81 IGPAFRNEGgrRGLRRVREFTQLEGEVFGEDGEEAsefeelIELTEELLRALGIK 135
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
55-495 |
1.08e-19 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 91.98 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 55 ADKTKEELEAAAIPVKVAGRIMLNRG--SFIVLQDSSERLQVYVN-RKTLPEET---LAEIKTWDLGDI----IGAEGVL 124
Cdd:PTZ00401 69 AVLSKPELVDKTVLIRARVSTTRKKGkmAFMVLRDGSDSVQAMAAvEGDVPKEMidfIGQIPTESIVDVeatvCKVEQPI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 125 ARSGKGDLYVDMTSVRLLTKSLRPLP----DKHHGLTDT------EQRYRQRYVDLMvNEETRHTFRVRSQVIAHIRRFL 194
Cdd:PTZ00401 149 TSTSHSDIELKVKKIHTVTESLRTLPftleDASRKESDEgakvnfDTRLNSRWMDLR-TPASGAIFRLQSRVCQYFRQFL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 195 SERGFLEVETPMLQTIPGGAAAKPFETHHnaLDMAMFLRIAPELYLKRLVVGGFEKVFEINRNFRNEGVST-RHNPEFTM 273
Cdd:PTZ00401 228 IDSDFCEIHSPKIINAPSEGGANVFKLEY--FNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNThRHLTEFVG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 274 LEFYQAYAD-YEDNMDLTEELFRELAQSVLGTTDVPYGDKVFHFGEPFVRLSVFDSILKYNPEITAADLNDVEKARAIAK 352
Cdd:PTZ00401 306 LDVEMRINEhYYEVLDLAESLFNYIFERLATHTKELKAVCQQYPFEPLVWKLTPERMKELGVGVISEGVEPTDKYQARVH 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 353 KAGAKVLGHEGLGKLQVM--IFEE------------------LVEHKLEQPHFIT-RYPFEVSPL-ARRNDEDPSVTDRF 410
Cdd:PTZ00401 386 NMDSRMLRINYMHCIELLntVLEEkmaptddinttnekllgkLVKERYGTDFFISdRFPSSARPFyTMECKDDERFTNSY 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 411 ELFIGGREIANAYSELNDAEDQAERF-MLQVkekDAGDDEamhydaDFINALEYGMPPTAGEGIGIDRLVMLLTNSPSIR 489
Cdd:PTZ00401 466 DMFIRGEEISSGAQRIHDPDLLLARAkMLNV---DLTPIK------EYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVR 536
|
....*.
gi 15598896 490 DVILFP 495
Cdd:PTZ00401 537 LASLFP 542
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
231-495 |
6.61e-11 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 64.66 E-value: 6.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 231 FLRIAPELYLKRLVvGGFEKVFEINRNFRNEGVST-RHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQSVLGTtdvpY 309
Cdd:PTZ00425 327 FLTVSGQLSLENLC-SSMGDVYTFGPTFRAENSHTsRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGYVLNN----N 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 310 GDKVFHFGEPFVR--LSVFDSILKYN-PEITAAdlNDVEKARAIAKKAGAKVlgHEGLgKLQVMIFEELVEHKLEQPHFI 386
Cdd:PTZ00425 402 FDDIYYFEENVETglISRLKNILDEDfAKITYT--NVIDLLQPYSDSFEVPV--KWGM-DLQSEHERFVAEQIFKKPVIV 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 387 TRYPFEVSPLARRNDEDPSVTDRFELF-------IGGREianayselndAEDQAERFMLQVKEKDAGDDEAMHYDadfiN 459
Cdd:PTZ00425 477 YNYPKDLKAFYMKLNEDQKTVAAMDVLvpkigevIGGSQ----------REDNLERLDKMIKEKKLNMESYWWYR----Q 542
|
250 260 270
....*....|....*....|....*....|....*.
gi 15598896 460 ALEYGMPPTAGEGIGIDRLVMLLTNSPSIRDVILFP 495
Cdd:PTZ00425 543 LRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFP 578
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
69-144 |
3.22e-10 |
|
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: 56.42 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 69 VKVAGRIMLNRGS----FIVLQDSSERLQVYVNRKTLPEETlAEIKTWDLGDIIGAEGVLARS-----GKGDLYVDMTSV 139
Cdd:cd04100 2 VTLAGWVHSRRDHggliFIDLRDGSGIVQVVVNKEELGEFF-EEAEKLRTESVVGVTGTVVKRpegnlATGEIELQAEEL 80
|
....*
gi 15598896 140 RLLTK 144
Cdd:cd04100 81 EVLSK 85
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
69-142 |
6.47e-10 |
|
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: 55.32 E-value: 6.47e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598896 69 VKVAGRIMLNRGS-----FIVLQDSSERLQVYVNrktlPEETLAEIKTWDLGDIIGAEGVLARSGKGDLYVDMTSVRLL 142
Cdd:pfam01336 1 VTVAGRVTSIRRSggkllFLTLRDGTGSIQVVVF----KEEAEKLAKKLKEGDVVRVTGKVKKRKGGELELVVEEIELL 75
|
|
| pylS |
PRK09537 |
pyrrolysine--tRNA(Pyl) ligase; |
190-278 |
7.26e-06 |
|
pyrrolysine--tRNA(Pyl) ligase;
Pssm-ID: 236555 [Multi-domain] Cd Length: 417 Bit Score: 48.30 E-value: 7.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 190 IRRFLSERGFLEVETPMLqtIPGGAAAK---PFETHHNA----LDMAMFLR--IAPELY--LKRL--VVGGFEKVFEINR 256
Cdd:PRK09537 213 ITKFFVDRGFLEIKSPIL--IPAEYIERmgiDNDTELSKqifrVDKNFCLRpmLAPGLYnyLRKLdrILPDPIKIFEIGP 290
|
90 100
....*....|....*....|..
gi 15598896 257 NFRNEGVSTRHNPEFTMLEFYQ 278
Cdd:PRK09537 291 CYRKESDGKEHLEEFTMVNFCQ 312
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
181-495 |
1.23e-05 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 47.66 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 181 RVRSQVIAHIRRFLSERGFLEVETPMLQT---------------IPGGA--AAKPFE----THHNALDMAM-------FL 232
Cdd:PLN02603 227 RVRNALAYATHKFFQENGFVWVSSPIITAsdcegageqfcvttlIPNSAenGGSLVDdipkTKDGLIDWSQdffgkpaFL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 233 RIAPELYLKRLVVGgFEKVFEINRNFRNEGVST-RHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQSVLGTT--DVPY 309
Cdd:PLN02603 307 TVSGQLNGETYATA-LSDVYTFGPTFRAENSNTsRHLAEFWMIEPELAFADLNDDMACATAYLQYVVKYILENCkeDMEF 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 310 GDKVFHFG----------EPFVRLSVFDSI---LKYNPEIT-----AADLNDvEKARAIAKKAgakvlghegLGKlqvmi 371
Cdd:PLN02603 386 FNTWIEKGiidrlsdvveKNFVQLSYTDAIellLKAKKKFEfpvkwGLDLQS-EHERYITEEA---------FGG----- 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 372 feelvehkleQPHFITRYPFEVSPLARRNDEDPSVTDRFELFIggreiaNAYSELNDAEDQAERfmLQVKEkDAGDDEAM 451
Cdd:PLN02603 451 ----------RPVIIRDYPKEIKAFYMRENDDGKTVAAMDMLV------PRVGELIGGSQREER--LEYLE-ARLDELKL 511
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 15598896 452 HYDAD--FINALEYGMPPTAGEGIGIDRLVMLLTNSPSIRDVILFP 495
Cdd:PLN02603 512 NKESYwwYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFP 557
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
69-151 |
9.71e-03 |
|
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: 35.75 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598896 69 VKVAGRIM----LNRGSFIVLQDSSERLQVYVNRKTLPEETLAEIKTWDLGDIIGAEGVLARSGKGDLYVDM--TSVRLL 142
Cdd:cd04316 15 VTVAGWVHeirdLGGIKFVILRDREGIVQVTAPKKKVDKELFKTVRKLSRESVISVTGTVKAEPKAPNGVEIipEEIEVL 94
|
....*....
gi 15598896 143 TKSLRPLPD 151
Cdd:cd04316 95 SEAKTPLPL 103
|
|
| |
