|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
43-606 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 900.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 43 PLSdrRSELKRRLKAEKKLAEKEAKQKELSEKQlnqttaAAATNHTADNGVGAEEETLDPNQYYKIRSQAVQQLKVSGED 122
Cdd:PLN02502 7 PLS--KNALKKRLKAKQAEEEKAAKEEAKAAAA------AAAAKGRSRKSAAADDETMDPTQYRANRLKKVEALRAKGVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 123 PYPHKFHVDISLTQFIQEYSHLQPGDHLTDITLKVAGRIHAKRASGgKLIFYDLRGEGVKLQVMANSRNY-KSEEEFVHI 201
Cdd:PLN02502 79 PYPYKFDVTHTAPELQEKYGSLENGEELEDVSVSVAGRIMAKRAFG-KLAFYDLRDDGGKIQLYADKKRLdLDEEEFEKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 202 NNKLRRGDIIGVEGNPGKTKKGELSIVPREMTLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFVRQKFIIRSKIIT 281
Cdd:PLN02502 158 HSLVDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLPDKYHGLTDQETRYRQRYLDLIANPEVRDIFRTRAKIIS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 282 YIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHN 361
Cdd:PLN02502 238 YIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRIATELHLKRLVVGGFERVYEIGRQFRNEGISTRHN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 362 PEFTTCEFYMAYADYHDLMEITEKMLSGMVRSITGSYKITYHpdgpegqAYEIDFTPPFRRISMVEELEKVLGVKLPEts 441
Cdd:PLN02502 318 PEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYH-------GIEIDFTPPFRRISMISLVEEATGIDFPA-- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 442 LFETEETRKILDDICVARAVECPPPRTTARLLDKLVGEFLEVTCISPTFICDHPQIMSPLAKWHRCKEGLTERFELFVMK 521
Cdd:PLN02502 389 DLKSDEANAYLIAACEKFDVKCPPPQTTGRLLNELFEEFLEETLVQPTFVLDHPVEMSPLAKPHRSKPGLTERFELFING 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 522 KEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVTMFLTDSNNIKEVLLFPA 601
Cdd:PLN02502 469 RELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFPA 548
|
....*
gi 55741637 602 MKPED 606
Cdd:PLN02502 549 MKPQD 553
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
97-607 |
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: 703.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 97 EETLDPNQYYKIRSQAVQQLKVSGEDPYPHKFHVDISLTQFIQEYSHLQPGDhLTDITLKVAGRIHAKRaSGGKLIFYDL 176
Cdd:COG1190 2 SEEEDLNEQIRVRREKLEELREAGIDPYPNKFPRTHTAAEIREKYDELEAEE-ETGDEVSVAGRIMAKR-DMGKASFADL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 177 RGEGVKLQVMAnSRNYKSEEEFVHINnKLRRGDIIGVEGNPGKTKKGELSIVPREMTLLSPCLHMLPHLHFGLKDKETRY 256
Cdd:COG1190 80 QDGSGRIQLYL-RRDELGEEAYELFK-LLDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDPETRY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 257 RQRYLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKML 336
Cdd:COG1190 158 RQRYVDLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 337 VVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSGMVRSITGSYKITYhpdgpegQAYEIDF 416
Cdd:COG1190 238 IVGGFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTY-------QGQEIDL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 417 TPPFRRISMVEELEKVLGVklPETSLFETEETRKILDdicvARAVECPPPRTTARLLDKLVGEFLEVTCISPTFICDHPQ 496
Cdd:COG1190 311 SPPWRRITMVEAIKEATGI--DVTPLTDDEELRALAK----ELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTDYPV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 497 IMSPLAKWHRCKEGLTERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGW 576
Cdd:COG1190 385 EVSPLAKRHRDDPGLTERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGL 464
|
490 500 510
....*....|....*....|....*....|.
gi 55741637 577 GMGIDRVTMFLTDSNNIKEVLLFPAMKPEDK 607
Cdd:COG1190 465 GIGIDRLVMLLTDSPSIRDVILFPLMRPEKK 495
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
101-606 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 698.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 101 DPNQYYKIRSQAVQQLKVSGEDPYPHKFHVDISLTQFIQEYSHLQPGD-HLTDITLKVAGRIHAKRaSGGKLIFYDLRGE 179
Cdd:PRK00484 2 ELNEQIAVRREKLAELREQGIDPYPNKFERTHTAAELRAKYDDKEKEElEELEIEVSVAGRVMLKR-VMGKASFATLQDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 180 GVKLQVMAnSRNYKSEEEFVHINnKLRRGDIIGVEGNPGKTKKGELSIVPREMTLLSPCLHMLPHLHFGLKDKETRYRQR 259
Cdd:PRK00484 81 SGRIQLYV-SKDDVGEEALEAFK-KLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLPDKFHGLTDVETRYRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 260 YLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVG 339
Cdd:PRK00484 159 YVDLIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLIVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 340 GIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSGMVRSITGSYKITYhpdgpegQAYEIDFTPP 419
Cdd:PRK00484 239 GFERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTY-------QGTEIDFGPP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 420 FRRISMVEELEKVLGVKLPETSlfeTEETRKILDdicvARAVECPPPRTTARLLDKLVGEFLEVTCISPTFICDHPQIMS 499
Cdd:PRK00484 312 FKRLTMVDAIKEYTGVDFDDMT---DEEARALAK----ELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEIS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 500 PLAKWHRCKEGLTERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMG 579
Cdd:PRK00484 385 PLAKRHREDPGLTERFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIG 464
|
490 500
....*....|....*....|....*..
gi 55741637 580 IDRVTMFLTDSNNIKEVLLFPAMKPED 606
Cdd:PRK00484 465 IDRLVMLLTDSPSIRDVILFPLMRPEK 491
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
96-604 |
0e+00 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 646.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 96 EEETLDPNQYYKIRSQAVQQLKVSGEDPYPHKFHVDISLTQFIQEYSHLQPGDHLTDITLKVAGRIHAKRASGGKLIFYD 175
Cdd:PTZ00417 76 EEAEVDPRLYYENRSKFIQEQKAKGINPYPHKFERTITVPEFVEKYQDLASGEHLEDTILNVTGRIMRVSASGQKLRFFD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 176 LRGEGVKLQVMAN-SRNYKSEEEFVHINNKLRRGDIIGVEGNPGKTKKGELSIVPREMTLLSPCLHMLPhLHFGLKDKET 254
Cdd:PTZ00417 156 LVGDGAKIQVLANfAFHDHTKSNFAECYDKIRRGDIVGIVGFPGKSKKGELSIFPKETIILSPCLHMLP-MKYGLKDTEI 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 255 RYRQRYLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHK 334
Cdd:PTZ00417 235 RYRQRYLDLMINESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHNDLDLDLYLRIATELPLK 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 335 MLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSGMVRSITGSYKITYHPDGPEGQAYEI 414
Cdd:PTZ00417 315 MLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGTYKILYNKDGPEKDPIEI 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 415 DFTPPFRRISMVEELEKVLGVKLPETslFETEETRKILDDICVARAVECPPPRTTARLLDKLVGEFLEVTCIS-PTFICD 493
Cdd:PTZ00417 395 DFTPPYPKVSIVEELEKLTNTKLEQP--FDSPETINKMINLIKENKIEMPNPPTAAKLLDQLASHFIENKYPNkPFFIIE 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 494 HPQIMSPLAKWHRCKEGLTERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPT 573
Cdd:PTZ00417 473 HPQIMSPLAKYHRSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPT 552
|
490 500 510
....*....|....*....|....*....|.
gi 55741637 574 AGWGMGIDRVTMFLTDSNNIKEVLLFPAMKP 604
Cdd:PTZ00417 553 GGLGLGIDRITMFLTNKNCIKDVILFPTMRP 583
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
101-604 |
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: 635.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 101 DPNQYYKIRSQAVQQLKVSGEDPYPHKFHVDISLTQFIQEYSHLQPGDH-LTDITLKVAGRIHAKRaSGGKLIFYDLRGE 179
Cdd:TIGR00499 1 ELNDQAQQRLEKLNRLRQTGNNPYLHKFERTHSAQEFQEKYADLSNEELkEKELKVSIAGRIKAIR-SMGKATFITLQDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 180 GVKLQVMANSRNYKseEEFVHINNK-LRRGDIIGVEGNPGKTKKGELSIVPREMTLLSPCLHMLPHLHFGLKDKETRYRQ 258
Cdd:TIGR00499 80 SGQIQLYVNKNKLP--EDFYEFDEYlLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQETRYRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 259 RYLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVV 338
Cdd:TIGR00499 158 RYLDLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKRLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 339 GGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSGMVRSITGSYKITYhpdgpegQAYEIDFTP 418
Cdd:TIGR00499 238 GGLEKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINY-------NDLEIDLKP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 419 PFRRISMVEELEKVLGVKLpetSLFETEETRKILDDICVARAVECPPprTTARLLDKLVGEFLEVTCISPTFICDHPQIM 498
Cdd:TIGR00499 311 PWKRITMVDALEMVTGIDF---DILKDDETAKALAKEHGIEVAEDSL--TLGHILNKFFEQFLEHTLIQPTFITHYPAEI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 499 SPLAKWHRCKEGLTERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGM 578
Cdd:TIGR00499 386 SPLAKRDPSNPEFTERFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGI 465
|
490 500
....*....|....*....|....*.
gi 55741637 579 GIDRVTMFLTDSNNIKEVLLFPAMKP 604
Cdd:TIGR00499 466 GIDRLVMLLTDAPSIRDVLLFPQLRP 491
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
266-604 |
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: 623.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 266 NDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVY 345
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 346 EIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSGMVRSITGSYKITYhpdgpegQAYEIDFTPPFRRISM 425
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEY-------GGKELDFTPPFKRVTM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 426 VEELEKVLGVKLPETSLFETEETRKILDDICvarAVECPPPRTTARLLDKLVGEFLEVTCISPTFICDHPQIMSPLAKWH 505
Cdd:cd00775 154 VDALKEKTGIDFPELDLEQPEELAKLLAKLI---KEKIEKPRTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 506 RCKEGLTERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVTM 585
Cdd:cd00775 231 RSNPGLTERFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVM 310
|
330
....*....|....*....
gi 55741637 586 FLTDSNNIKEVLLFPAMKP 604
Cdd:cd00775 311 LLTDSNSIRDVILFPAMRP 329
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
133-603 |
7.07e-146 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 437.54 E-value: 7.07e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 133 SLTQFIQEYSHLQPGDHLTDITLKVAGRIHAKRaSGGKLIFYDLRGEGVKLQVMANSRNYKSEEEFVHINNKLRRGDIIG 212
Cdd:PTZ00385 88 PISEVRERYGYLASGDRAAQATVRVAGRVTSVR-DIGKIIFVTIRSNGNELQVVGQVGEHFTREDLKKLKVSLRVGDIIG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 213 VEGNPGKTKKGELSIVPREMTLLSP--CLHML--PHLH-FG-LKDKETRYRQRYLDLILNDFVRQKFIIRSKIITYIRSF 286
Cdd:PTZ00385 167 ADGVPCRMQRGELSVAASRMLILSPyvCTDQVvcPNLRgFTvLQDNDVKYRYRFTDMMTNPCVIETIKKRHVMLQALRDY 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 287 LDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTT 366
Cdd:PTZ00385 247 FNERNFVEVETPVLHTVASGANAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTS 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 367 CEFYMAYADYHDLMEITEKMLSGMVRSITGSYKITYHPDGPEGQAYEIDFTPPFRRISMVEELEKVLGVKLPETSLFETE 446
Cdd:PTZ00385 327 CEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTVVQIYPENAHGNPVTVDLGKPFRRVSVYDEIQRMSGVEFPPPNELNTP 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 447 ETRKILDDICVARAVECPPPRTTARLLDKLVGEFLEVTCISPTFICDHPQIMSPLAKWHRCKEGLTERFELFVMKKEICN 526
Cdd:PTZ00385 407 KGIAYMSVVMLRYNIPLPPVRTAAKMFEKLIDFFITDRVVEPTFVMDHPLFMSPLAKEQVSRPGLAERFELFVNGIEYCN 486
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55741637 527 AYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVTMFLTDSNNIKEVLLFPAMK 603
Cdd:PTZ00385 487 AYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLR 563
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
116-606 |
1.44e-142 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 441.71 E-value: 1.44e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 116 LKVSGEDPYPhkfhVDISLTQFIQEyshlqPGDHLTDITLKVAGRIHAKRASGGkLIFYDLRGEGVKLQVMANsrnyKSE 195
Cdd:PRK02983 624 LRAAGVDPYP----VGVPPTHTVAE-----ALDAPTGEEVSVSGRVLRIRDYGG-VLFADLRDWSGELQVLLD----ASR 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 196 EEFVHINNKLR---RGDIIGVEGNPGKTKKGELSIVPREMTLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFVRQK 272
Cdd:PRK02983 690 LEQGSLADFRAavdLGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLDLAVNPEARDL 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 273 FIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFR 352
Cdd:PRK02983 770 LRARSAVVRAVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVERVFELGRNFR 849
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 353 NEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSGMVRSITGSYKITYhpDGPEGQAYEIDFTPPFRRISMVEELEKV 432
Cdd:PRK02983 850 NEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGAPVVMR--PDGDGVLEPVDISGPWPVVTVHDAVSEA 927
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 433 LGVKL-PETSLfetEETRKilddICVARAVECPPPRTTARLLDKLVGEFLEVTCISPTFICDHPQIMSPLAKWHRCKEGL 511
Cdd:PRK02983 928 LGEEIdPDTPL---AELRK----LCDAAGIPYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPHRSDPGL 1000
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 512 TERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVTMFLTdSN 591
Cdd:PRK02983 1001 AERWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLT-GR 1079
|
490
....*....|....*
gi 55741637 592 NIKEVLLFPAMKPED 606
Cdd:PRK02983 1080 SIRETLPFPLVKPRQ 1094
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
97-605 |
2.90e-134 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 402.52 E-value: 2.90e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 97 EETLDPNQYYKIRSQAVQQLKVSGEdPYPHKFHVDISLTQFIQEYShLQPGDHLT--DITLKVAGRIHAKRASGgKLIFY 174
Cdd:PRK12445 10 NEAIDFNDELRNRREKLAALRQQGV-AFPNDFRRDHTSDQLHEEFD-AKDNQELEslNIEVSVAGRMMTRRIMG-KASFV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 175 DLRGEGVKLQVMAnSRNYKSEEEFVHINNKLRRGDIIGVEGNPGKTKKGELSIVPREMTLLSPCLHMLPHLHFGLKDKET 254
Cdd:PRK12445 87 TLQDVGGRIQLYV-ARDSLPEGVYNDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 255 RYRQRYLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHK 334
Cdd:PRK12445 166 RYRQRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 335 MLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSGMVRSITGSYKITYhpdgpegQAYEI 414
Cdd:PRK12445 246 RLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTY-------GEHVF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 415 DFTPPFRRISMVEELEKvlgvKLPETSLFEteetrkiLDDICVARA------VECPPPRTTARLLDKLVGEFLEVTCISP 488
Cdd:PRK12445 319 DFGKPFEKLTMREAIKK----YRPETDMAD-------LDNFDAAKAlaesigITVEKSWGLGRIVTEIFDEVAEAHLIQP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 489 TFICDHPQIMSPLAKWHRCKEGLTERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEY 568
Cdd:PRK12445 388 TFITEYPAEVSPLARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEY 467
|
490 500 510
....*....|....*....|....*....|....*..
gi 55741637 569 GLPPTAGWGMGIDRVTMFLTDSNNIKEVLLFPAMKPE 605
Cdd:PRK12445 468 GLPPTAGLGIGIDRMIMLFTNSHTIRDVILFPAMRPQ 504
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
251-603 |
7.40e-121 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 361.11 E-value: 7.40e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 251 DKETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPE 330
Cdd:pfam00152 1 DEETRLKYRYLDL-RRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 331 LYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSGMVRSITGSYKITYHPdgpegq 410
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGG------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 411 aYEIDFTPPFRRISMVEELEKVLGVKLPETslfeteetrkiLDDIcvaravecppPRTTARLLDKLVgefLEVTCISPTF 490
Cdd:pfam00152 154 -TLLDLKKPFPRITYAEAIEKLNGKDVEEL-----------GYGS----------DKPDLRFLLELV---IDKNKFNPLW 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 491 ICDHPQIMSPLAKWHRCK-EGLTERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKaagdDEAMFIDENFCTALEYG 569
Cdd:pfam00152 209 VTDFPAEHHPFTMPKDEDdPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDP----EEAEEKFGFYLDALKYG 284
|
330 340 350
....*....|....*....|....*....|....
gi 55741637 570 LPPTAGWGMGIDRVTMFLTDSNNIKEVLLFPAMK 603
Cdd:pfam00152 285 APPHGGLGIGLDRLVMLLTGLESIREVIAFPKTR 318
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
273-604 |
1.05e-91 |
|
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: 284.37 E-value: 1.05e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 273 FIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFR 352
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 353 NEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSGMVRSITGSYKITYhpdgpegQAYEIDFTPPFRRISMVEELEKV 432
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTY-------GFELEDFGLPFPRLTYREALERY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 433 LgvklpetslfeteetrkilddicvaravecppprttarlldklvgeflevtciSPTFICDHP-QIMSPLAKWHRCKEGL 511
Cdd:cd00669 154 G-----------------------------------------------------QPLFLTDYPaEMHSPLASPHDVNPEI 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 512 TERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGddeaMFIDENFCTALEYGLPPTAGWGMGIDRVTMFLTDSN 591
Cdd:cd00669 181 ADAFDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINKEAG----MEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSP 256
|
330
....*....|...
gi 55741637 592 NIKEVLLFPAMKP 604
Cdd:cd00669 257 TIREVIAFPKMRR 269
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
286-597 |
3.17e-56 |
|
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: 192.00 E-value: 3.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 286 FLDELGFLEIETPMMniIPGG-------AVAKPFITYHNElDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDL 358
Cdd:TIGR00462 1 FFAERGVLEVETPLL--SPAPvtdphldAFATEFVGPDGQ-GRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 359 THNPEFTTCEFYMAYADYHDLMEITEKMLSGMVRsitgsykityhpdgpegqayeiDFTPPFRRISMVEELEKVLGVKLP 438
Cdd:TIGR00462 78 RHNPEFTMLEWYRPGFDYHDLMDEVEALLQELLG----------------------DPFAPAERLSYQEAFLRYAGIDPL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 439 ETSLFEteetrkiLDDICVARAVECPPPRTTARLLDKLVGEFLEVT--CISPTFICDHPQIMSPLAKWHRCKEGLTERFE 516
Cdd:TIGR00462 136 TASLAE-------LQAAAAAHGIRASEEDDRDDLLDLLFSEKVEPHlgFGRPTFLYDYPASQAALARISPDDPRVAERFE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 517 LFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVTMFLTDSNNIKEV 596
Cdd:TIGR00462 209 LYIKGLELANGFHELTDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDV 288
|
.
gi 55741637 597 L 597
Cdd:TIGR00462 289 L 289
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
276-597 |
3.83e-54 |
|
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: 186.85 E-value: 3.83e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 276 RSKIITYIRSFLDELGFLEIETPMMNIIPGGAVA-KPFITY---HNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQF 351
Cdd:COG2269 9 RARLLAAIRAFFAERGVLEVETPALSVAPGTDPHlDSFATEfigPDGGGRPLYLHTSPEFAMKRLLAAGSGPIYQIAKVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 352 RNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSgmvrsitgsykityhpdgpegQAYEIDFTPPFRRISMVEELEK 431
Cdd:COG2269 89 RNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQ---------------------LVLGAAGFAPAERLSYQEAFLR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 432 VLGVKLPETSLFEteetrkiLDDICVARAVECPPPRTTARLLDKLVGEFLEVT--CISPTFICDHPQIMSPLAKwhRCKE 509
Cdd:COG2269 148 YLGIDPLTADLDE-------LAAAAAAAGLRVADDDDRDDLLDLLLSERVEPQlgRDRPTFLYDYPASQAALAR--ISPD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 510 G--LTERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVTMFL 587
Cdd:COG2269 219 DprVAERFELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLA 298
|
330
....*....|
gi 55741637 588 TDSNNIKEVL 597
Cdd:COG2269 299 LGAERIDDVL 308
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
154-263 |
1.38e-52 |
|
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: 175.74 E-value: 1.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 154 TLKVAGRIHAKRASGgKLIFYDLRGEGVKLQVMANSRNYkSEEEFVHINNKLRRGDIIGVEGNPGKTKKGELSIVPREMT 233
Cdd:cd04322 1 EVSVAGRIMSKRGSG-KLSFADLQDESGKIQVYVNKDDL-GEEEFEDFKKLLDLGDIIGVTGTPFKTKTGELSIFVKEFT 78
|
90 100 110
....*....|....*....|....*....|
gi 55741637 234 LLSPCLHMLPHLHFGLKDKETRYRQRYLDL 263
Cdd:cd04322 79 LLSKSLRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
276-596 |
3.07e-41 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 152.01 E-value: 3.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 276 RSKIITYIRSFLDELGFLEIETPMM--------NIIPggaVAKPFITYHNELDMNLYMRIAPElYH-KMLVVGGIDRVYE 346
Cdd:PRK09350 8 RAKIIAEIRRFFADRGVLEVETPILsqatvtdiHLVP---FETRFVGPGASQGKTLWLMTSPE-YHmKRLLAAGSGPIFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 347 IGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSgmvrsitgsykityhpdgpegqayEIDFTPPFRRISMV 426
Cdd:PRK09350 84 ICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQ------------------------QVLDCEPAESLSYQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 427 EELEKVLGV---------------KLPETSLFETEETRKILDDICVARAVEcppprttarllDKLVGEflevtciSPTFI 491
Cdd:PRK09350 140 QAFLRYLGIdplsadktqlrevaaKLGLSNIADEEEDRDTLLQLLFTFGVE-----------PNIGKE-------KPTFV 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 492 CDHPQIMSPLAKWHRCKEGLTERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLP 571
Cdd:PRK09350 202 YHFPASQAALAKISTEDHRVAERFEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLP 281
|
330 340
....*....|....*....|....*
gi 55741637 572 PTAGWGMGIDRVTMFLTDSNNIKEV 596
Cdd:PRK09350 282 DCSGVALGVDRLIMLALGAESISEV 306
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
157-600 |
1.04e-40 |
|
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: 153.44 E-value: 1.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 157 VAGRIHAKRASGGkLIFYDLRGEGVKLQVMANSRnyKSEEEFVHINNKLRRGDIIGVEGNPGKTKK--GELSIVPREMTL 234
Cdd:TIGR00458 17 FMGWVHEIRDLGG-LIFVLLRDREGLIQITAPAK--KVSKNLFKWAKKLNLESVVAVRGIVKIKEKapGGFEIIPTKIEV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 235 LSPCLHMLPHLhfgLKDK-----ETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIP--GGA 307
Cdd:TIGR00458 94 INEAKEPLPLD---PTEKvpaelDTRLDYRFLDL-RRPTVQAIFRIRSGVLESVREFLAEEGFIEVHTPKLVASAteGGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 308 VAKPfITYhneLDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLT-HNPEFTTCEFYMAYADYHDLMEITEKM 386
Cdd:TIGR00458 170 ELFP-ITY---FEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHrHLNEATSIDIEMAFEDHHDVMDILEEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 387 LsgmVRSITGSYKITYHPDGPEGQAYEIDFTPpFRRISMVEELEkvlgvklpetslfeteetrkilddICVARAVECPPP 466
Cdd:TIGR00458 246 V---VRVFEDVPERCAHQLETLEFKLEKPEGK-FVRLTYDEAIE------------------------MANAKGVEIGWG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 467 RTTARLLDKLVGEFLEvtciSPTFICDHPQ------IMSPLAKWHRCKEglterFELFVMKKEICNAYTElndpVRQRQL 540
Cdd:TIGR00458 298 EDLSTEAEKALGEEMD----GLYFITDWPTeirpfyTMPDEDNPEISKS-----FDLMYRDLEISSGAQR----IHLHDL 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 541 FEEQAKAKAAGDDEAmfidENFCTALEYGLPPTAGWGMGIDRVTMFLTDSNNIKEVLLFP 600
Cdd:TIGR00458 365 LVERIKAKGLNPEGF----KDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFP 420
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
154-600 |
6.06e-37 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 143.02 E-value: 6.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 154 TLKVAGRIHAKRASGGkLIFYDLRGEGVKLQVMAnsRNYKSEEEFVHINnKLRRGDIIGVEG----NPgKTKKGeLSIVP 229
Cdd:PRK05159 18 EVTLAGWVHEIRDLGG-IAFLILRDRSGIIQVVV--KKKVDEELFETIK-KLKRESVVSVTGtvkaNP-KAPGG-VEVIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 230 REMTLLSPCLHMLPhlhFGLKDK-----ETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPmmNIIP 304
Cdd:PRK05159 92 EEIEVLNKAEEPLP---LDISGKvlaelDTRLDNRFLDL-RRPRVRAIFKIRSEVLRAFREFLYENGFTEIFTP--KIVA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 305 ----GGAVAKPfITYHNEldmNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLT-HNPEFTTCEFYMAYAD-YHD 378
Cdd:PRK05159 166 sgteGGAELFP-IDYFEK---EAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSrHLNEYTSIDVEMGFIDdHED 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 379 LMEITEKMLSGMVRSITGSYKityhpdgPEGQAYEIDF---TPPFRRISMVEELEKV--LGVKLPETSLFETEETRKILD 453
Cdd:PRK05159 242 VMDLLENLLRYMYEDVAENCE-------KELELLGIELpvpETPIPRITYDEAIEILksKGNEISWGDDLDTEGERLLGE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 454 DIcvaravecppprttarlLDKLVGEFLevtcisptFICDHPQIMSPL-AKWHRCKEGLTERFELfvMKK--EICNAYTE 530
Cdd:PRK05159 315 YV-----------------KEEYGSDFY--------FITDYPSEKRPFyTMPDEDDPEISKSFDL--LFRglEITSGGQR 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 531 LNDpvrqRQLFEEQAKAKaaGDDEAMFidENFCTALEYGLPPTAGWGMGIDRVTMFLTDSNNIKEVLLFP 600
Cdd:PRK05159 368 IHR----YDMLVESIKEK--GLNPESF--EFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
154-600 |
2.57e-30 |
|
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: 123.62 E-value: 2.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 154 TLKVAGRIHAKRASGgKLIFYDLR-GEGVkLQVMANSRNYKSEEEFvhinNKLRRGDIIGVEG----NPGKtkKGELSIV 228
Cdd:COG0017 16 EVTVAGWVRTKRDSG-GISFLILRdGSGF-IQVVVKKDKLENFEEA----KKLTTESSVEVTGtvveSPRA--PQGVELQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 229 PREMTLLSPCLHMLPhlhFGLKDK--ETRYRQRYLDLILNDFvRQKFIIRSKIITYIRSFLDELGFLEIETPmmnIIPGG 306
Cdd:COG0017 88 AEEIEVLGEADEPYP---LQPKRHslEFLLDNRHLRLRTNRF-GAIFRIRSELARAIREFFQERGFVEVHTP---IITAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 307 AV---AKPF-ITYHNEldmNLYMRIAPELYHKMLVvGGIDRVYEIGRQFRNEGIDLT-HNPEFTTCEFYMAYADYHDLME 381
Cdd:COG0017 161 ATeggGELFpVDYFGK---EAYLTQSGQLYKEALA-MALEKVYTFGPTFRAEKSNTRrHLAEFWMIEPEMAFADLEDVMD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 382 ITEKMLSGMVRSItgsykITYHPDgpEGQAYEIDFT-------PPFRRISM---VEELEKvLGVKLPETSLFETEETRKI 451
Cdd:COG0017 237 LAEEMLKYIIKYV-----LENCPE--ELEFLGRDVErlekvpeSPFPRITYteaIEILKK-SGEKVEWGDDLGTEHERYL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 452 lddicvaravecppprtTARLLDKLVgeflevtcisptFICDHPqimsplakwhrckeglterfelfvmkKEICNAYTEL 531
Cdd:COG0017 309 -----------------GEEFFKKPV------------FVTDYP--------------------------KEIKAFYMKP 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 532 N--DP--VR----------------QRqlfEEQ-----AKAKAAGDDEAMF---IDenfctALEYGLPPTAGWGMGIDRV 583
Cdd:COG0017 334 NpdDPktVAafdllapgigeiiggsQR---EHRydvlvERIKEKGLDPEDYewyLD-----LRRYGSVPHAGFGLGLERL 405
|
490
....*....|....*..
gi 55741637 584 TMFLTDSNNIKEVLLFP 600
Cdd:COG0017 406 VMWLTGLENIREVIPFP 422
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
154-600 |
1.70e-28 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 120.17 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 154 TLKVAGRIHAKRASGGkLIFYDLRG-EGVkLQVMANSrnyksEEEFVHINNKLRRGDIIGVEG----------NPgKTKK 222
Cdd:PRK00476 19 TVTLCGWVHRRRDHGG-LIFIDLRDrEGI-VQVVFDP-----DAEAFEVAESLRSEYVIQVTGtvrarpegtvNP-NLPT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 223 GELSIVPREMTLLSPClHMLPhlhFGLKDK-----ETRYRQRYLDLilndfvR-----QKFIIRSKIITYIRSFLDELGF 292
Cdd:PRK00476 91 GEIEVLASELEVLNKS-KTLP---FPIDDEedvseELRLKYRYLDL------RrpemqKNLKLRSKVTSAIRNFLDDNGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 293 LEIETPMMniI---PGGA----VakPfityhneldmnlyMRI----------APELYHKMLVVGGIDRVYEIGRQFRNEg 355
Cdd:PRK00476 161 LEIETPIL--TkstPEGArdylV--P-------------SRVhpgkfyalpqSPQLFKQLLMVAGFDRYYQIARCFRDE- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 356 iDLTHN--PEFTT--CEfyMAYADYHDLMEITEKMLSGMVRSITGsykityhpdgpegqayeIDFTPPFRRIS------- 424
Cdd:PRK00476 223 -DLRADrqPEFTQidIE--MSFVTQEDVMALMEGLIRHVFKEVLG-----------------VDLPTPFPRMTyaeamrr 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 425 -------------------------------MVEELEKVLGVKLPETSlfeTEETRKILDD---------------ICV- 457
Cdd:PRK00476 283 ygsdkpdlrfglelvdvtdlfkdsgfkvfagAANDGGRVKAIRVPGGA---AQLSRKQIDEltefakiygakglayIKVn 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 458 --------------------ARAVECPP----------PRTTARLLDKL---VGEFLEVT---CISPTFICDHpqimsPL 501
Cdd:PRK00476 360 edglkgpiakflseeelaalLERTGAKDgdliffgadkAKVVNDALGALrlkLGKELGLIdedKFAFLWVVDF-----PM 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 502 AKW----------H----RCKEGLTERFELFVMKKEICNAY------TEL-------NDPVRQRQLF------EEQAKAK 548
Cdd:PRK00476 435 FEYdeeegrwvaaHhpftMPKDEDLDELETTDPGKARAYAYdlvlngYELgggsiriHRPEIQEKVFeilgisEEEAEEK 514
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 55741637 549 AAGddeamFIDenfctALEYGLPPTAGWGMGIDRVTMFLTDSNNIKEVLLFP 600
Cdd:PRK00476 515 FGF-----LLD-----ALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
154-600 |
5.62e-28 |
|
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: 118.95 E-value: 5.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 154 TLKVAGRIHAKRASGGkLIFYDLRG-EGVkLQVMANSrnyKSEEEFVHINNKLRRGDIIGVEG----------NPgKTKK 222
Cdd:COG0173 18 EVTLSGWVHRRRDHGG-LIFIDLRDrYGI-TQVVFDP---DDSAEAFEKAEKLRSEYVIAVTGkvrarpegtvNP-KLPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 223 GELSIVPREMTLLSPClHMLPhlhFGLKDK-----ETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFLDELGFLEIET 297
Cdd:COG0173 92 GEIEVLASELEILNKA-KTPP---FQIDDDtdvseELRLKYRYLDL-RRPEMQKNLILRHKVTKAIRNYLDENGFLEIET 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 298 PMMNI-IPGGA----VakPFityhneldmnlymRI----------APELYHKMLVVGGIDRVYEIGRQFRNEgiDLTHN- 361
Cdd:COG0173 167 PILTKsTPEGArdylV--PS-------------RVhpgkfyalpqSPQLFKQLLMVSGFDRYFQIARCFRDE--DLRADr 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 362 -PEFTT--CEfyMAYADYHDLMEITEKMLSGMVRSITGsykityhpdgpegqayeIDFTPPFRRIS-------------- 424
Cdd:COG0173 230 qPEFTQldIE--MSFVDQEDVFELMEGLIRHLFKEVLG-----------------VELPTPFPRMTyaeamerygsdkpd 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 425 ------------------------MVEELEKVLGVKLPETSLFeteeTRKILDD---------------ICV-ARAVECP 464
Cdd:COG0173 291 lrfglelvdvtdifkdsgfkvfagAAENGGRVKAINVPGGASL----SRKQIDEltefakqygakglayIKVnEDGLKSP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 465 -----PPRTTARLLDKL---VGEFLevtcispTFICDHPQIMSPLAKWHRCK----EGLTER-------------FEL-- 517
Cdd:COG0173 367 iakflSEEELAAILERLgakPGDLI-------FFVADKPKVVNKALGALRLKlgkeLGLIDEdefaflwvvdfplFEYde 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 518 -----------FVMKKE-------------ICNAY------TEL-------NDPVRQRQLF------EEQAKAKAAGdde 554
Cdd:COG0173 440 eegrwvamhhpFTMPKDedldlletdpgkvRAKAYdlvlngYELgggsiriHDPELQEKVFellgisEEEAEEKFGF--- 516
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 55741637 555 amFIDenfctALEYGLPPTAGWGMGIDRVTMFLTDSNNIKEVLLFP 600
Cdd:COG0173 517 --LLE-----AFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
273-600 |
2.88e-27 |
|
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: 111.51 E-value: 2.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 273 FIIRSKIITYIRSFLDELGFLEIETPMMN-IIPGGA----VakPFITYHNE---LDMnlymriAPELYHKMLVVGGIDRV 344
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTkSTPEGArdflV--PSRLHPGKfyaLPQ------SPQLFKQLLMVSGFDRY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 345 YEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSGMVRSITGsykityhpdgpegqayeIDFTPPFRRIS 424
Cdd:cd00777 73 FQIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG-----------------VELTTPFPRMT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 425 MVEELEKvLGVKL------PetsLFE-TEETRKIlddicvaravecppprttarlldklvgEFLEvtcisptficdHPQI 497
Cdd:cd00777 136 YAEAMER-YGFKFlwivdfP---LFEwDEEEGRL---------------------------VSAH-----------HPFT 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 498 MsPLAKWHRCKEGLTER-----FELFVMKKEICNAYTELNDPVRQRQLFE------EQAKAKAAGddeamfidenFCTAL 566
Cdd:cd00777 174 A-PKEEDLDLLEKDPEDaraqaYDLVLNGVELGGGSIRIHDPDIQEKVFEilglseEEAEEKFGF----------LLEAF 242
|
330 340 350
....*....|....*....|....*....|....
gi 55741637 567 EYGLPPTAGWGMGIDRVTMFLTDSNNIKEVLLFP 600
Cdd:cd00777 243 KYGAPPHGGIALGLDRLVMLLTGSESIRDVIAFP 276
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
253-600 |
1.30e-26 |
|
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: 110.73 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 253 ETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMM--NIIPGGAVAKPfITYHNEldmNLYMRIAPE 330
Cdd:cd00776 5 ETLLDNRHLDL-RTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKItsTDTEGGAELFK-VSYFGK---PAYLAQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 331 LYHKMLVvGGIDRVYEIGRQFRNEGIDLT-HNPEFTTCEFYMAYA-DYHDLMEITEKMLSGMVRSITGSYK-----ITYH 403
Cdd:cd00776 80 LYKEMLI-AALERVYEIGPVFRAEKSNTRrHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAkelelVNQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 404 PDGPEGqayeidFTPPFRRISMVEelekvlGVKLpetsLFETEETRKILDDICVARAVEcppprttaRLLDKLVGEflev 483
Cdd:cd00776 159 NRELLK------PLEPFPRITYDE------AIEL----LREKGVEEEVKWGEDLSTEHE--------RLLGEIVKG---- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 484 tciSPTFICDHPQIMSPL-AKWHRCKEGLTERFELFVMKK-EICNAYTELNDPvrqrQLFEEQAKAKaaGDDEAMFidEN 561
Cdd:cd00776 211 ---DPVFVTDYPKEIKPFyMKPDDDNPETVESFDLLMPGVgEIVGGSQRIHDY----DELEERIKEH--GLDPESF--EW 279
|
330 340 350
....*....|....*....|....*....|....*....
gi 55741637 562 FCTALEYGLPPTAGWGMGIDRVTMFLTDSNNIKEVLLFP 600
Cdd:cd00776 280 YLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
157-431 |
1.41e-24 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 108.72 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 157 VAGRIHAKRASGGkLIFYDLRGEGVKLQVMANSRNYKseeEFVHINNKLRRGDIIGVEG----------NPgKTKKGELS 226
Cdd:PLN02903 77 LCGWVDLHRDMGG-LTFLDVRDHTGIVQVVTLPDEFP---EAHRTANRLRNEYVVAVEGtvrsrpqespNK-KMKTGSVE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 227 IVPREMTLLSPCLHMLPHLHFGLKD------KETRYRQRYLDLILNDFVRQkFIIRSKIITYIRSFL-DELGFLEIETPM 299
Cdd:PLN02903 152 VVAESVDILNVVTKSLPFLVTTADEqkdsikEEVRLRYRVLDLRRPQMNAN-LRLRHRVVKLIRRYLeDVHGFVEIETPI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 300 MN---------------IIPGGAVAKPfityhneldmnlymrIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEF 364
Cdd:PLN02903 231 LSrstpegardylvpsrVQPGTFYALP---------------QSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEF 295
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55741637 365 TTCEFYMAYADYHDLMEITEKMLSGMVRSITGsykityhpdgpegqayeIDFTPPFRRISMVEELEK 431
Cdd:PLN02903 296 TQLDMELAFTPLEDMLKLNEDLIRQVFKEIKG-----------------VQLPNPFPRLTYAEAMSK 345
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
154-237 |
2.29e-18 |
|
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: 79.92 E-value: 2.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 154 TLKVAGRIHAKRASGgKLIFYDLRGEGVKLQVMANSRNyksEEEFVHINNKLRRGDIIGVEGNPGKT-----KKGELSIV 228
Cdd:cd04100 1 EVTLAGWVHSRRDHG-GLIFIDLRDGSGIVQVVVNKEE---LGEFFEEAEKLRTESVVGVTGTVVKRpegnlATGEIELQ 76
|
....*....
gi 55741637 229 PREMTLLSP 237
Cdd:cd04100 77 AEELEVLSK 85
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
56-600 |
7.33e-18 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 87.07 E-value: 7.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 56 KAEKKLAEKEAKQKELSEKQLNQTTAAAATnhtadngvGAEEETLDPNqyYKIRSQAVQQLKVSGedpyphKFHVDISlt 135
Cdd:PLN02850 12 KISKKAAKKAAAKAEKLRREATAKAAAASL--------EDEDDPLASN--YGDVPLEELQSKVTG------REWTDVS-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 136 qfiqeyshlQPGDHLTDITLKVAGRIHAKRASGgKLIFYDLRGEGVKLQVMANSRNYKSEEEFVHINNKLRRGDIIGVEG 215
Cdd:PLN02850 74 ---------DLGEELAGSEVLIRGRVHTIRGKG-KSAFLVLRQSGFTVQCVVFVSEVTVSKGMVKYAKQLSRESVVDVEG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 216 ---NPGKTKKG---ELSIVPREMTLLSPCLHMLPhlhFGLKD----------------------KETRYRQRYLDLIL-- 265
Cdd:PLN02850 144 vvsVPKKPVKGttqQVEIQVRKIYCVSKALATLP---FNVEDaarseseiekalqtgeqlvrvgQDTRLNNRVLDLRTpa 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 266 NDFVrqkFIIRSKIITYIRSFLDELGFLEIETPmmNIIPG-----GAVAKpfityhneLDmnlYMRI------APELYHK 334
Cdd:PLN02850 221 NQAI---FRIQSQVCNLFREFLLSKGFVEIHTP--KLIAGaseggSAVFR--------LD---YKGQpaclaqSPQLHKQ 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 335 MLVVGGIDRVYEIGRQFRNEGiDLTHNP--EFTTCEFYMAYAD-YHDLMEITEKMLSGMVRSITGSYKI------TYHPD 405
Cdd:PLN02850 285 MAICGDFRRVFEIGPVFRAED-SFTHRHlcEFTGLDLEMEIKEhYSEVLDVVDELFVAIFDGLNERCKKeleairEQYPF 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 406 GPegqayeIDFTPPFRRISMVE--ELEKVLGVKLPETSLFETEETRKiLDDICVARAvecpppRTTARLLDKL---VGEF 480
Cdd:PLN02850 364 EP------LKYLPKTLRLTFAEgiQMLKEAGVEVDPLGDLNTESERK-LGQLVKEKY------GTDFYILHRYplaVRPF 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 481 LEVTCIsptficDHPQimsplakwhrckegLTERFELFVMKKEICNAYTELNDPvrqrQLFEEQAKAKAAG-DDEAMFID 559
Cdd:PLN02850 431 YTMPCP------DDPK--------------YSNSFDVFIRGEEIISGAQRVHDP----ELLEKRAEECGIDvKTISTYID 486
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 55741637 560 enfctALEYGLPPTAGWGMGIDRVTMFLTDSNNIKEVLLFP 600
Cdd:PLN02850 487 -----SFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFP 522
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
148-600 |
2.52e-17 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 85.43 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 148 DHLTDITLKVAGRIHAKRASGgKLIFYDLRGEGVKLQVMANSRNyKSEEEFVHINNKLRRGDIIGVEGNPGK-------T 220
Cdd:PTZ00401 74 PELVDKTVLIRARVSTTRKKG-KMAFMVLRDGSDSVQAMAAVEG-DVPKEMIDFIGQIPTESIVDVEATVCKveqpitsT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 221 KKGELSIVPREMTLLSPCLHMLPhlhFGLKDK-------------ETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFL 287
Cdd:PTZ00401 152 SHSDIELKVKKIHTVTESLRTLP---FTLEDAsrkesdegakvnfDTRLNSRWMDL-RTPASGAIFRLQSRVCQYFRQFL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 288 DELGFLEIETPMMNIIPGGAVAKPF-ITYHNEldmNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDL-THNPEFT 365
Cdd:PTZ00401 228 IDSDFCEIHSPKIINAPSEGGANVFkLEYFNR---FAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNThRHLTEFV 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 366 TCEFYMAYAD-YHDLMEITEKMLSGMVRSITGsykityHPDGPEGQAYEIDFTPPFRRISmvEELEKVLGVKLPETSLFE 444
Cdd:PTZ00401 305 GLDVEMRINEhYYEVLDLAESLFNYIFERLAT------HTKELKAVCQQYPFEPLVWKLT--PERMKELGVGVISEGVEP 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 445 T------------------------------EETRKILDDICVaravecppprTTARLLDKLVGEFLEVTcispTFICDH 494
Cdd:PTZ00401 377 TdkyqarvhnmdsrmlrinymhciellntvlEEKMAPTDDINT----------TNEKLLGKLVKERYGTD----FFISDR 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 495 -PQIMSPLAKWhRCK--EGLTERFELFVMKKEICNAYTELNDPvrqrQLFeeQAKAKAAGDDEAMFIDenFCTALEYGLP 571
Cdd:PTZ00401 443 fPSSARPFYTM-ECKddERFTNSYDMFIRGEEISSGAQRIHDP----DLL--LARAKMLNVDLTPIKE--YVDSFRLGAW 513
|
490 500
....*....|....*....|....*....
gi 55741637 572 PTAGWGMGIDRVTMFLTDSNNIKEVLLFP 600
Cdd:PTZ00401 514 PHGGFGVGLERVVMLYLGLSNVRLASLFP 542
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
275-388 |
2.56e-17 |
|
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: 81.01 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 275 IRSKIITYIRSFLDELGFLEIETPMMNIIPG----GAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGI----DRVYE 346
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLlekaGHEPKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIrklpLRLAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 55741637 347 IGRQFRNEGI--DLTHNPEFTTCEFYMAYAD------YHDLMEITEKMLS 388
Cdd:cd00768 81 IGPAFRNEGGrrGLRRVREFTQLEGEVFGEDgeeaseFEELIELTEELLR 130
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
143-390 |
9.20e-17 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 84.27 E-value: 9.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 143 HLQPGDHLTDITLkvAGRIHAKRASGGkLIFYDLRGEGVKLQVM-----ANSRNYK-----SEEEFVHINNKLRRgDIIG 212
Cdd:PRK12820 11 HLSLDDTGREVCL--AGWVDAFRDHGE-LLFIHLRDRNGFIQAVfspeaAPADVYElaaslRAEFCVALQGEVQK-RLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 213 VEgNPgKTKKGELSIVPREMTLLSPCLhMLPhlhFGLKDK----------------ETRYRQRYLDlILNDFVRQKFIIR 276
Cdd:PRK12820 87 TE-NP-HIETGDIEVFVRELSILAASE-ALP---FAISDKamtagagsagadavneDLRLQYRYLD-IRRPAMQDHLAKR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 277 SKIITYIRSFLDELGFLEIETPMMNI-IPGGAvaKPFITYHNELDMNLY-MRIAPELYHKMLVVGGIDRVYEIGRQFRNE 354
Cdd:PRK12820 160 HRIIKCARDFLDSRGFLEIETPILTKsTPEGA--RDYLVPSRIHPKEFYaLPQSPQLFKQLLMIAGFERYFQLARCFRDE 237
|
250 260 270
....*....|....*....|....*....|....*.
gi 55741637 355 GIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSGM 390
Cdd:PRK12820 238 DLRPNRQPEFTQLDIEASFIDEEFIFELIEELTARM 273
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
156-235 |
1.90e-15 |
|
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: 71.50 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 156 KVAGRIHAKRASGGKLIFYDLRGEGVKLQVMANSrnykseEEFVHINNKLRRGDIIGVEGNPGKTKKGELSIVPREMTLL 235
Cdd:pfam01336 2 TVAGRVTSIRRSGGKLLFLTLRDGTGSIQVVVFK------EEAEKLAKKLKEGDVVRVTGKVKKRKGGELELVVEEIELL 75
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
275-600 |
1.99e-13 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 71.97 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 275 IRSKIITYIRSFLDELGFLEIETPMMN-----IIPGGA---VAKPFITYHNEldmnlYMRIAPEL-YHKMLVVGGIDRVY 345
Cdd:PRK06462 32 VQSSILRYTREFLDGRGFVEVLPPIISpstdpLMGLGSdlpVKQISIDFYGV-----EYYLADSMiLHKQLALRMLGKIF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 346 EIGRQFRNEGID---LTHNPEFTTCEFYMAYADYHDLMEITEKMLSGMVRSITGSYK---ITYHPDGPEgqayeidFTPP 419
Cdd:PRK06462 107 YLSPNFRLEPVDkdtGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEdelEFFGRDLPH-------LKRP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 420 FRRISMvEELEKVLGVKLPETSLFEteetrKILDDicvaravecppprttarlldklvGE-FLEVTCISPTFICDHPQIM 498
Cdd:PRK06462 180 FKRITH-KEAVEILNEEGCRGIDLE-----ELGSE-----------------------GEkSLSEHFEEPFWIIDIPKGS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 499 SPL-AKWHRCKEGLTERFELFVMKK--EICNAyTElndpvRQRQLFEEQAKAKAAGDDEAMFidENFCTALEYGLPPTAG 575
Cdd:PRK06462 231 REFyDREDPERPGVLRNYDLLLPEGygEAVSG-GE-----REYEYEEIVERIREHGVDPEKY--KWYLEMAKEGPLPSAG 302
|
330 340
....*....|....*....|....*
gi 55741637 576 WGMGIDRVTMFLTDSNNIKEVLLFP 600
Cdd:PRK06462 303 FGIGVERLTRYICGLRHIREVQPFP 327
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
154-263 |
1.00e-07 |
|
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: 51.37 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 154 TLKVAGRIHAKRASGGkLIFYDLR-GEGVkLQVMANSRNYKSEEEFvhinNKLRRGDIIGVEG----------NPgKTKK 222
Cdd:cd04317 16 EVTLCGWVQRRRDHGG-LIFIDLRdRYGI-VQVVFDPEEAPEFELA----EKLRNESVIQVTGkvrarpegtvNP-KLPT 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 55741637 223 GELSIVPREMTLLSPClhmlPHLHFGLKDK-----ETRYRQRYLDL 263
Cdd:cd04317 89 GEIEVVASELEVLNKA----KTLPFEIDDDvnvseELRLKYRYLDL 130
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
154-236 |
4.59e-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: 42.69 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 154 TLKVAGRIHAKRASGGkLIFYDLRGEGVKLQVMANSRnyKSEEEFVHINNKLRRGDIIGVEGNPGKTKK--GELSIVPRE 231
Cdd:cd04316 14 EVTVAGWVHEIRDLGG-IKFVILRDREGIVQVTAPKK--KVDKELFKTVRKLSRESVISVTGTVKAEPKapNGVEIIPEE 90
|
....*
gi 55741637 232 MTLLS 236
Cdd:cd04316 91 IEVLS 95
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
159-222 |
3.00e-04 |
|
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae and human cytoplasmic aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). 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.
Pssm-ID: 239815 [Multi-domain] Cd Length: 102 Bit Score: 40.24 E-value: 3.00e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55741637 159 GRIHAKRASGGKLIFYDLRGEGVKLQVMANSRNYKSEEEFVHINNKLRRGDIIGVEGNPGKTKK 222
Cdd:cd04320 6 ARVHTSRAQGAKLAFLVLRQQGYTIQGVLAASAEGVSKQMVKWAGSLSKESIVDVEGTVKKPEE 69
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
568-600 |
1.21e-03 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 41.63 E-value: 1.21e-03
10 20 30
....*....|....*....|....*....|...
gi 55741637 568 YGLPPTAGWGMGIDRVTMFLTDSNNIKEVLLFP 600
Cdd:PRK03932 410 YGSVPHSGFGLGFERLVAYITGLDNIRDVIPFP 442
|
|
| pylS |
PRK09537 |
pyrrolysine--tRNA(Pyl) ligase; |
283-369 |
3.28e-03 |
|
pyrrolysine--tRNA(Pyl) ligase;
Pssm-ID: 236555 [Multi-domain] Cd Length: 417 Bit Score: 40.21 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741637 283 IRSFLDELGFLEIETPMMniIPGGAVAKPFITYHNEL-------DMNLYMR--IAPELYHKMLVVGGI--D--RVYEIGR 349
Cdd:PRK09537 213 ITKFFVDRGFLEIKSPIL--IPAEYIERMGIDNDTELskqifrvDKNFCLRpmLAPGLYNYLRKLDRIlpDpiKIFEIGP 290
|
90 100
....*....|....*....|
gi 55741637 350 QFRNEGIDLTHNPEFTTCEF 369
Cdd:PRK09537 291 CYRKESDGKEHLEEFTMVNF 310
|
|
| PheRS_alpha_core |
cd00496 |
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ... |
342-404 |
8.94e-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: 37.91 E-value: 8.94e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55741637 342 DRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYAD--YHDLMEITEKMLSGMVRSITG-SYKITYHP 404
Cdd:cd00496 81 IRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKGltFADLKGTLEEFAKELFGPITKvRFRPSYFP 146
|
|
| |
