|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
63-602 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 1014.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 63 SGEPPKESAADDEEMDPTQYYENRLKALDSLKATGVNPYPHKFLANITVADYIEKYKSMNVGDKLVDVTECLAGRIMTKR 142
Cdd:PLN02502 42 KGRSRKSAAADDETMDPTQYRANRLKKVEALRAKGVEPYPYKFDVTHTAPELQEKYGSLENGEELEDVSVSVAGRIMAKR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 143 AqSSKLLFYDLYGGGEKVQVFADARTSELEDNEFIKFHSTLKRGDIVGVCGYPGKSKRGELSIFPKKIVVLSPCLHMMPR 222
Cdd:PLN02502 122 A-FGKLAFYDLRDDGGKIQLYADKKRLDLDEEEFEKLHSLVDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLPD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 223 QKSEgsavptpwapgmgrniekyvLRDQETRYRQRYLDLMVNHEVRHIFKTRSKVVSFIRKFLDGLDFLEVETPMMNMIA 302
Cdd:PLN02502 201 KYHG--------------------LTDQETRYRQRYLDLIANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPMLNMIA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 303 GGAAARPFVTHHNELNMRLYMRIAPELYLKELVVGGLDRVYEIGKQFRNEGIDLTHNPEFTTCEFYMAYADYNDLIELTE 382
Cdd:PLN02502 261 GGAAARPFVTHHNDLNMDLYLRIATELHLKRLVVGGFERVYEIGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 383 TMLSGMVKELTGGYKIKYHAngvekppIEIDFTPPFRKIDMIEELEAMAKLNIPKDLSSDEANKYLIDACAKYDVKCPPP 462
Cdd:PLN02502 341 EMVSGMVKELTGSYKIKYHG-------IEIDFTPPFRRISMISLVEEATGIDFPADLKSDEANAYLIAACEKFDVKCPPP 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 463 QTTTRLLDKLVGHFLEETCVNPTFIINHPEIMSPLAKWHRSRPGLTERFELFVNKHEVCNAYTELNDPVVQRQRFEEQLK 542
Cdd:PLN02502 414 QTTGRLLNELFEEFLEETLVQPTFVLDHPVEMSPLAKPHRSKPGLTERFELFINGRELANAFSELTDPVDQRERFEEQVK 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 543 DRQSGDDEAMALDETFCTALEYGLPPTGGWGLGIDRLTMLLTDSQNIKEVLLFPAMKPQD 602
Cdd:PLN02502 494 QHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFPAMKPQD 553
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
77-602 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 683.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 77 MDPTQYYENRLKALDSLKATGVNPYPHKFLANITVADYIEKYKSMN---VGDKLVDVTecLAGRIMTKRAQSsKLLFYDL 153
Cdd:PRK00484 1 EELNEQIAVRREKLAELREQGIDPYPNKFERTHTAAELRAKYDDKEkeeLEELEIEVS--VAGRVMLKRVMG-KASFATL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 154 YGGGEKVQVFADARTSELEDNEFIKfhsTLKRGDIVGVCGYPGKSKRGELSIFPKKIVVLSPCLHMMPrqksegsavptp 233
Cdd:PRK00484 78 QDGSGRIQLYVSKDDVGEEALEAFK---KLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLP------------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 234 wapgmgrniEKYV-LRDQETRYRQRYLDLMVNHEVRHIFKTRSKVVSFIRKFLDGLDFLEVETPMMNMIAGGAAARPFVT 312
Cdd:PRK00484 143 ---------DKFHgLTDVETRYRQRYVDLIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFIT 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 313 HHNELNMRLYMRIAPELYLKELVVGGLDRVYEIGKQFRNEGIDLTHNPEFTTCEFYMAYADYNDLIELTETMLSGMVKEL 392
Cdd:PRK00484 214 HHNALDIDLYLRIAPELYLKRLIVGGFERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 393 TGGYKIKYHANgvekppiEIDFTPPFRKIDMIEELEAMAKLNIpKDLSSDEANKylidACAKYDVKCPPPQTTTRLLDKL 472
Cdd:PRK00484 294 LGTTKVTYQGT-------EIDFGPPFKRLTMVDAIKEYTGVDF-DDMTDEEARA----LAKELGIEVEKSWGLGKLINEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 473 VGHFLEETCVNPTFIINHPEIMSPLAKWHRSRPGLTERFELFVNKHEVCNAYTELNDPVVQRQRFEEQLKDRQSGDDEAM 552
Cdd:PRK00484 362 FEEFVEPKLIQPTFITDYPVEISPLAKRHREDPGLTERFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAM 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 55583785 553 ALDETFCTALEYGLPPTGGWGLGIDRLTMLLTDSQNIKEVLLFPAMKPQD 602
Cdd:PRK00484 442 FMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFPLMRPEK 491
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
75-602 |
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: 683.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 75 EEMDPTQYYENRLKALDSLKATGVNPYPHKFLANITVADYIEKYKSMNVGDKLvDVTECLAGRIMTKRAQSsKLLFYDLY 154
Cdd:COG1190 3 EEEDLNEQIRVRREKLEELREAGIDPYPNKFPRTHTAAEIREKYDELEAEEET-GDEVSVAGRIMAKRDMG-KASFADLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 155 GGGEKVQVFAdaRTSELEDNEFIKFHsTLKRGDIVGVCGYPGKSKRGELSIFPKKIVVLSPCLHMMPrqksegsavptpw 234
Cdd:COG1190 81 DGSGRIQLYL--RRDELGEEAYELFK-LLDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLP------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 235 apgmgrniEKY-VLRDQETRYRQRYLDLMVNHEVRHIFKTRSKVVSFIRKFLDGLDFLEVETPMMNMIAGGAAARPFVTH 313
Cdd:COG1190 145 --------EKFhGLTDPETRYRQRYVDLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 314 HNELNMRLYMRIAPELYLKELVVGGLDRVYEIGKQFRNEGIDLTHNPEFTTCEFYMAYADYNDLIELTETMLSGMVKELT 393
Cdd:COG1190 217 HNALDMDLYLRIAPELYLKRLIVGGFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 394 GGYKIKYhaNGVekppiEIDFTPPFRKIDMIEELEAMAKLNIpKDLSSDEAnkyLIDACAKYDVKCPPPQTTTRLLDKLV 473
Cdd:COG1190 297 GTTKVTY--QGQ-----EIDLSPPWRRITMVEAIKEATGIDV-TPLTDDEE---LRALAKELGIEVDPGWGRGKLIDELF 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 474 GHFLEETCVNPTFIINHPEIMSPLAKWHRSRPGLTERFELFVNKHEVCNAYTELNDPVVQRQRFEEQLKDRQSGDDEAMA 553
Cdd:COG1190 366 EELVEPKLIQPTFVTDYPVEVSPLAKRHRDDPGLTERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMP 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 55583785 554 LDETFCTALEYGLPPTGGWGLGIDRLTMLLTDSQNIKEVLLFPAMKPQD 602
Cdd:COG1190 446 MDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFPLMRPEK 494
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
63-600 |
0e+00 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 649.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 63 SGEPPKESAADDE-EMDPTQYYENRLKALDSLKATGVNPYPHKFLANITVADYIEKYKSMNVGDKLVDVTECLAGRIMTK 141
Cdd:PTZ00417 65 SVQASKDKKKEEEaEVDPRLYYENRSKFIQEQKAKGINPYPHKFERTITVPEFVEKYQDLASGEHLEDTILNVTGRIMRV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 142 RAQSSKLLFYDLYGGGEKVQVFADARTSELEDNEFIKFHSTLKRGDIVGVCGYPGKSKRGELSIFPKKIVVLSPCLHMMP 221
Cdd:PTZ00417 145 SASGQKLRFFDLVGDGAKIQVLANFAFHDHTKSNFAECYDKIRRGDIVGIVGFPGKSKKGELSIFPKETIILSPCLHMLP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 222 RqksegsavptpwapgmgrnieKYVLRDQETRYRQRYLDLMVNHEVRHIFKTRSKVVSFIRKFLDGLDFLEVETPMMNMI 301
Cdd:PTZ00417 225 M---------------------KYGLKDTEIRYRQRYLDLMINESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 302 AGGAAARPFVTHHNELNMRLYMRIAPELYLKELVVGGLDRVYEIGKQFRNEGIDLTHNPEFTTCEFYMAYADYNDLIELT 381
Cdd:PTZ00417 284 AGGANARPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWS 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 382 ETMLSGMVKELTGGYKIKYHANGVEKPPIEIDFTPPFRKIDMIEELEAMAKLNIPKDLSSDEANKYLIDACAKYDVKCPP 461
Cdd:PTZ00417 364 EDFFSQLVMHLFGTYKILYNKDGPEKDPIEIDFTPPYPKVSIVEELEKLTNTKLEQPFDSPETINKMINLIKENKIEMPN 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 462 PQTTTRLLDKLVGHFLEETCVN-PTFIINHPEIMSPLAKWHRSRPGLTERFELFVNKHEVCNAYTELNDPVVQRQRFEEQ 540
Cdd:PTZ00417 444 PPTAAKLLDQLASHFIENKYPNkPFFIIEHPQIMSPLAKYHRSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQ 523
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 541 LKDRQSGDDEAMALDETFCTALEYGLPPTGGWGLGIDRLTMLLTDSQNIKEVLLFPAMKP 600
Cdd:PTZ00417 524 QKDREKGDAEAFQFDAAFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFPTMRP 583
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
78-601 |
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: 608.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 78 DPTQYYENRLKALDSLKATGVNPYPHKFLANITVADYIEKYKSM-NVGDKLVDVTECLAGRIMTKRAQSsKLLFYDLYGG 156
Cdd:TIGR00499 1 ELNDQAQQRLEKLNRLRQTGNNPYLHKFERTHSAQEFQEKYADLsNEELKEKELKVSIAGRIKAIRSMG-KATFITLQDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 157 GEKVQVFAdaRTSELEDNEFIKFHSTLKRGDIVGVCGYPGKSKRGELSIFPKKIVVLSPCLHMMPrQKSEGsavptpwap 236
Cdd:TIGR00499 80 SGQIQLYV--NKNKLPEDFYEFDEYLLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLP-DKWHG--------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 237 gmgrniekyvLRDQETRYRQRYLDLMVNHEVRHIFKTRSKVVSFIRKFLDGLDFLEVETPMMNMIAGGAAARPFVTHHNE 316
Cdd:TIGR00499 148 ----------LTDQETRYRQRYLDLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 317 LNMRLYMRIAPELYLKELVVGGLDRVYEIGKQFRNEGIDLTHNPEFTTCEFYMAYADYNDLIELTETMLSGMVKELTGGY 396
Cdd:TIGR00499 218 LDMDLYLRIAPELYLKRLIVGGLEKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTF 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 397 KIKYHAngvekppIEIDFTPPFRKIDMIEELEamakLNIPKDLSSDEANKYLIDACAKYDVKCP-PPQTTTRLLDKLVGH 475
Cdd:TIGR00499 298 IINYND-------LEIDLKPPWKRITMVDALE----MVTGIDFDILKDDETAKALAKEHGIEVAeDSLTLGHILNKFFEQ 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 476 FLEETCVNPTFIINHPEIMSPLAKWHRSRPGLTERFELFVNKHEVCNAYTELNDPVVQRQRFEEQLKDRQSGDDEAMALD 555
Cdd:TIGR00499 367 FLEHTLIQPTFITHYPAEISPLAKRDPSNPEFTERFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVD 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 55583785 556 ETFCTALEYGLPPTGGWGLGIDRLTMLLTDSQNIKEVLLFPAMKPQ 601
Cdd:TIGR00499 447 EDFVEALEYGMPPTGGLGIGIDRLVMLLTDAPSIRDVLLFPQLRPQ 492
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
264-600 |
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: 584.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 264 NHEVRHIFKTRSKVVSFIRKFLDGLDFLEVETPMMNMIAGGAAARPFVTHHNELNMRLYMRIAPELYLKELVVGGLDRVY 343
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 344 EIGKQFRNEGIDLTHNPEFTTCEFYMAYADYNDLIELTETMLSGMVKELTGGYKIKYhangvekPPIEIDFTPPFRKIDM 423
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEY-------GGKELDFTPPFKRVTM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 424 IEELEAMAKLNIPK--DLSSDEANKYLIDACAKydvKCPPPQTTTRLLDKLVGHFLEETCVNPTFIINHPEIMSPLAKWH 501
Cdd:cd00775 154 VDALKEKTGIDFPEldLEQPEELAKLLAKLIKE---KIEKPRTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 502 RSRPGLTERFELFVNKHEVCNAYTELNDPVVQRQRFEEQLKDRQSGDDEAMALDETFCTALEYGLPPTGGWGLGIDRLTM 581
Cdd:cd00775 231 RSNPGLTERFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVM 310
|
330
....*....|....*....
gi 55583785 582 LLTDSQNIKEVLLFPAMKP 600
Cdd:cd00775 311 LLTDSNSIRDVILFPAMRP 329
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
105-602 |
2.24e-151 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 451.02 E-value: 2.24e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 105 FLANITVADYIEKYKSMNVGDKLVDVTECLAGRIMTKRaQSSKLLFYDLYGGGEKVQVFADARTSELEDnEFIKFHSTLK 184
Cdd:PTZ00385 83 FRGITPISEVRERYGYLASGDRAAQATVRVAGRVTSVR-DIGKIIFVTIRSNGNELQVVGQVGEHFTRE-DLKKLKVSLR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 185 RGDIVGVCGYPGKSKRGELSIFPKKIVVLSPclHMMPRQksegsaVPTPWAPGMGrniekyVLRDQETRYRQRYLDLMVN 264
Cdd:PTZ00385 161 VGDIIGADGVPCRMQRGELSVAASRMLILSP--YVCTDQ------VVCPNLRGFT------VLQDNDVKYRYRFTDMMTN 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 265 HEVRHIFKTRSKVVSFIRKFLDGLDFLEVETPMMNMIAGGAAARPFVTHHNELNMRLYMRIAPELYLKELVVGGLDRVYE 344
Cdd:PTZ00385 227 PCVIETIKKRHVMLQALRDYFNERNFVEVETPVLHTVASGANAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 345 IGKQFRNEGIDLTHNPEFTTCEFYMAYADYNDLIELTETMLSGMVKELTGGYKIKYHANGVEKPPIEIDFTPPFRKIDMI 424
Cdd:PTZ00385 307 IGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTVVQIYPENAHGNPVTVDLGKPFRRVSVY 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 425 EELEAMAKLNIP--KDLSSDEANKYLIDACAKYDVKCPPPQTTTRLLDKLVGHFLEETCVNPTFIINHPEIMSPLAKWHR 502
Cdd:PTZ00385 387 DEIQRMSGVEFPppNELNTPKGIAYMSVVMLRYNIPLPPVRTAAKMFEKLIDFFITDRVVEPTFVMDHPLFMSPLAKEQV 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 503 SRPGLTERFELFVNKHEVCNAYTELNDPVVQRQRFEEQLKDRQSGDDEAMALDETFCTALEYGLPPTGGWGLGIDRLTML 582
Cdd:PTZ00385 467 SRPGLAERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALML 546
|
490 500
....*....|....*....|
gi 55583785 583 LTDSQNIKEVLLFPAMKpQD 602
Cdd:PTZ00385 547 LTNSSNIRDGIIFPLLR-QD 565
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
63-602 |
5.30e-144 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 444.79 E-value: 5.30e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 63 SGEPPKESAADDEEMDP--TQYYENRLKALDSLKATGVNPYPHKFLANITVADYIekyksmnvgDKLVDVTECLAGRIMT 140
Cdd:PRK02983 592 DGSAPDVAATAPDAPEPrlPEQVRVRLAKLEALRAAGVDPYPVGVPPTHTVAEAL---------DAPTGEEVSVSGRVLR 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 141 KRaQSSKLLFYDLYGGGEKVQVFADArtSELEDNEFIKFHSTLKRGDIVGVCGYPGKSKRGELSIFPKKIVVLSPCLHMM 220
Cdd:PRK02983 663 IR-DYGGVLFADLRDWSGELQVLLDA--SRLEQGSLADFRAAVDLGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPL 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 221 PRqksegsavptPWAPgmgrniekyvLRDQETRYRQRYLDLMVNHEVRHIFKTRSKVVSFIRKFLDGLDFLEVETPMMNM 300
Cdd:PRK02983 740 PD----------KWKG----------LTDPEARVRQRYLDLAVNPEARDLLRARSAVVRAVRETLVARGFLEVETPILQQ 799
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 301 IAGGAAARPFVTHHNELNMRLYMRIAPELYLKELVVGGLDRVYEIGKQFRNEGIDLTHNPEFTTCEFYMAYADYNDLIEL 380
Cdd:PRK02983 800 VHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVERVFELGRNFRNEGVDATHNPEFTLLEAYQAHADYDTMRDL 879
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 381 TETMLSGMVKELTGGYKI-KYHANGVEKPpieIDFTPPFRKIDMIEELEAMAKLNIPKDLSSDEankyLIDACAKYDVKC 459
Cdd:PRK02983 880 TRELIQNAAQAAHGAPVVmRPDGDGVLEP---VDISGPWPVVTVHDAVSEALGEEIDPDTPLAE----LRKLCDAAGIPY 952
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 460 PPPQTTTRLLDKLVGHFLEETCVNPTFIINHPEIMSPLAKWHRSRPGLTERFELFVNKHEVCNAYTELNDPVVQRQRFEE 539
Cdd:PRK02983 953 RTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPHRSDPGLAERWDLVAWGVELGTAYSELTDPVEQRRRLTE 1032
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55583785 540 QLKDRQSGDDEAMALDETFCTALEYGLPPTGGWGLGIDRLTMLLTdSQNIKEVLLFPAMKPQD 602
Cdd:PRK02983 1033 QSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLT-GRSIRETLPFPLVKPRQ 1094
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
68-601 |
1.47e-125 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 379.41 E-value: 1.47e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 68 KESAADDEEMDPTQYYENRLKALDSLKATGVnPYPHKFLANITVADYIEKYKSMNvGDKL--VDVTECLAGRIMTKRAQS 145
Cdd:PRK12445 4 QETRGANEAIDFNDELRNRREKLAALRQQGV-AFPNDFRRDHTSDQLHEEFDAKD-NQELesLNIEVSVAGRMMTRRIMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 146 sKLLFYDLYGGGEKVQVFA--DARTSELEDNEFIKFhstlKRGDIVGVCGYPGKSKRGELSIFPKKIVVLSPCLHMMPrQ 223
Cdd:PRK12445 82 -KASFVTLQDVGGRIQLYVarDSLPEGVYNDQFKKW----DLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLP-D 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 224 KSEGsavptpwapgmgrniekyvLRDQETRYRQRYLDLMVNHEVRHIFKTRSKVVSFIRKFLDGLDFLEVETPMMNMIAG 303
Cdd:PRK12445 156 KFHG-------------------LQDQEVRYRQRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 304 GAAARPFVTHHNELNMRLYMRIAPELYLKELVVGGLDRVYEIGKQFRNEGIDLTHNPEFTTCEFYMAYADYNDLIELTET 383
Cdd:PRK12445 217 GASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTES 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 384 MLSGMVKELTGGYKIKYHANgvekppiEIDFTPPFRKIDMIEELEAMAKLNIPKDLSSDEANKYLIDACAkydVKCPPPQ 463
Cdd:PRK12445 297 LFRTLAQEVLGTTKVTYGEH-------VFDFGKPFEKLTMREAIKKYRPETDMADLDNFDAAKALAESIG---ITVEKSW 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 464 TTTRLLDKLVGHFLEETCVNPTFIINHPEIMSPLAKWHRSRPGLTERFELFVNKHEVCNAYTELNDPVVQRQRFEEQLKD 543
Cdd:PRK12445 367 GLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNA 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 55583785 544 RQSGDDEAMALDETFCTALEYGLPPTGGWGLGIDRLTMLLTDSQNIKEVLLFPAMKPQ 601
Cdd:PRK12445 447 KAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFPAMRPQ 504
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
249-599 |
1.03e-123 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 367.66 E-value: 1.03e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 249 DQETRYRQRYLDLmVNHEVRHIFKTRSKVVSFIRKFLDGLDFLEVETPMMNMIAGGAAARPFVTHHNELNMRLYMRIAPE 328
Cdd:pfam00152 1 DEETRLKYRYLDL-RRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 329 LYLKELVVGGLDRVYEIGKQFRNEGIDLTHNPEFTTCEFYMAYADYNDLIELTETMLSGMVKELTGGYKIKYhangvekP 408
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELE-------G 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 409 PIEIDFTPPFRKIDMIeelEAMAKLNipkdlsSDEANKYLIDacakydvkCPPPQttTRLLDKLVghfLEETCVNPTFII 488
Cdd:pfam00152 153 GTLLDLKKPFPRITYA---EAIEKLN------GKDVEELGYG--------SDKPD--LRFLLELV---IDKNKFNPLWVT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 489 NHPEIMSPLAKWHRS-RPGLTERFELFVNKHEVCNAYTELNDPVVQRQRFEEQLKDRqsgdDEAMALDETFCTALEYGLP 567
Cdd:pfam00152 211 DFPAEHHPFTMPKDEdDPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDP----EEAEEKFGFYLDALKYGAP 286
|
330 340 350
....*....|....*....|....*....|..
gi 55583785 568 PTGGWGLGIDRLTMLLTDSQNIKEVLLFPAMK 599
Cdd:pfam00152 287 PHGGLGIGLDRLVMLLTGLESIREVIAFPKTR 318
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
271-600 |
1.95e-95 |
|
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of class II aminoacyl-tRNA synthetases of the subgroup containing aspartyl, lysyl, and asparaginyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. Nearly all class II tRNA synthetases are dimers and enzymes in this subgroup are homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238358 [Multi-domain] Cd Length: 269 Bit Score: 293.23 E-value: 1.95e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 271 FKTRSKVVSFIRKFLDGLDFLEVETPMMNMIAGGAAARPFVTHHNELNMRLYMRIAPELYLKELVVGGLDRVYEIGKQFR 350
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 351 NEGIDLTHNPEFTTCEFYMAYADYNDLIELTETMLSGMVKELTGGYKikyhangVEKPPIEIDFTPPFRKIDMIEELEam 430
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTA-------VTYGFELEDFGLPFPRLTYREALE-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 431 aklnipkdlssdeanKYLidacakydvkcpppqtttrlldklvghfleetcvNPTFIINHP-EIMSPLAKWHRSRPGLTE 509
Cdd:cd00669 152 ---------------RYG----------------------------------QPLFLTDYPaEMHSPLASPHDVNPEIAD 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 510 RFELFVNKHEVCNAYTELNDPVVQRQRFEEQLKDRqsgdDEAMALDETFCTALEYGLPPTGGWGLGIDRLTMLLTDSQNI 589
Cdd:cd00669 183 AFDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINK----EAGMEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTI 258
|
330
....*....|.
gi 55583785 590 KEVLLFPAMKP 600
Cdd:cd00669 259 REVIAFPKMRR 269
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
284-593 |
6.26e-57 |
|
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: 193.54 E-value: 6.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 284 FLDGLDFLEVETPMMNmIAGGAAA--RPFVTH---HNELNMRLYMRIAPELYLKELVVGGLDRVYEIGKQFRNEGIDLTH 358
Cdd:TIGR00462 1 FFAERGVLEVETPLLS-PAPVTDPhlDAFATEfvgPDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 359 NPEFTTCEFYMAYADYNDLIELTETMLSGMVKeltggykikyhangvekppieiDFTPPFRKIDMIEELEAMAKLNIpkd 438
Cdd:TIGR00462 80 NPEFTMLEWYRPGFDYHDLMDEVEALLQELLG----------------------DPFAPAERLSYQEAFLRYAGIDP--- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 439 LSSDEANkyLIDACAKYDVKCPPPQTTTRLLDKLVGHFLEET--CVNPTFIINHPEIMSPLAKWHRSRPGLTERFELFVN 516
Cdd:TIGR00462 135 LTASLAE--LQAAAAAHGIRASEEDDRDDLLDLLFSEKVEPHlgFGRPTFLYDYPASQAALARISPDDPRVAERFELYIK 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55583785 517 KHEVCNAYTELNDPVVQRQRFEEQLKDRQSGDDEAMALDETFCTALEYGLPPTGGWGLGIDRLTMLLTDSQNIKEVL 593
Cdd:TIGR00462 213 GLELANGFHELTDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVL 289
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
268-593 |
2.68e-55 |
|
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: 189.55 E-value: 2.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 268 RHIFKTRSKVVSFIRKFLDGLDFLEVETPMMNmIAGGAAA--RPFVT---HHNELNMRLYMRIAPELYLKELVVGGLDRV 342
Cdd:COG2269 3 REALRARARLLAAIRAFFAERGVLEVETPALS-VAPGTDPhlDSFATefiGPDGGGRPLYLHTSPEFAMKRLLAAGSGPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 343 YEIGKQFRNEGIDLTHNPEFTTCEFYMAYADYNDLIELTETMLSgMVKELTGgykikyhangvekppieidfTPPFRKID 422
Cdd:COG2269 82 YQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQ-LVLGAAG--------------------FAPAERLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 423 MIEELEAMAKLNIpkdLSSDEANkyLIDACAKYDVkcPPPQTTTR--LLDKLVGHFLE-----ETcvnPTFIINHPEIMS 495
Cdd:COG2269 141 YQEAFLRYLGIDP---LTADLDE--LAAAAAAAGL--RVADDDDRddLLDLLLSERVEpqlgrDR---PTFLYDYPASQA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 496 PLAKWHRSRPGLTERFELFVNKHEVCNAYTELNDPVVQRQRFEEQLKDRQSGDDEAMALDETFCTALEYGLPPTGGWGLG 575
Cdd:COG2269 211 ALARISPDDPRVAERFELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALG 290
|
330
....*....|....*...
gi 55583785 576 IDRLTMLLTDSQNIKEVL 593
Cdd:COG2269 291 FDRLLMLALGAERIDDVL 308
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
133-261 |
1.25e-43 |
|
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: 151.09 E-value: 1.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 133 CLAGRIMTKRAqSSKLLFYDLYGGGEKVQVFADARtsELEDNEFIKFHSTLKRGDIVGVCGYPGKSKRGELSIFPKKIVV 212
Cdd:cd04322 3 SVAGRIMSKRG-SGKLSFADLQDESGKIQVYVNKD--DLGEEEFEDFKKLLDLGDIIGVTGTPFKTKTGELSIFVKEFTL 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 55583785 213 LSPCLHMMPRQKSEgsavptpwapgmgrniekyvLRDQETRYRQRYLDL 261
Cdd:cd04322 80 LSKSLRPLPEKFHG--------------------LTDVETRYRQRYLDL 108
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
270-592 |
1.49e-40 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 149.69 E-value: 1.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 270 IFKTRSKVVSFIRKFLDGLDFLEVETPMM--------NMIaggaaarPFVTH----HNELNMRLYMRIAPELYLKELVVG 337
Cdd:PRK09350 4 NLLKRAKIIAEIRRFFADRGVLEVETPILsqatvtdiHLV-------PFETRfvgpGASQGKTLWLMTSPEYHMKRLLAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 338 GLDRVYEIGKQFRNEGIDLTHNPEFTTCEFYMAYADYNDLIELTETMLsgmvkeltggykikyhangvekppIEIDFTPP 417
Cdd:PRK09350 77 GSGPIFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLL------------------------QQVLDCEP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 418 FRKIDMIEELEAMAKLNIpkdLSSDEANkyLIDACAKYDVKCPPPQTTTRllDKLVgHFLEETCV-------NPTFIINH 490
Cdd:PRK09350 133 AESLSYQQAFLRYLGIDP---LSADKTQ--LREVAAKLGLSNIADEEEDR--DTLL-QLLFTFGVepnigkeKPTFVYHF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 491 PEIMSPLAKWHRSRPGLTERFELFVNKHEVCNAYTELNDPVVQRQRFEEQLKDRQSGDDEAMALDETFCTALEYGLPPTG 570
Cdd:PRK09350 205 PASQAALAKISTEDHRVAERFEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCS 284
|
330 340
....*....|....*....|..
gi 55583785 571 GWGLGIDRLTMLLTDSQNIKEV 592
Cdd:PRK09350 285 GVALGVDRLIMLALGAESISEV 306
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
183-596 |
2.32e-36 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 141.10 E-value: 2.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 183 LKRGDIVGVCGYP---GKSKRGeLSIFPKKIVVLSPclhmmprqksegSAVPTPWapgmgrNIEKYVLRDQETRYRQRYL 259
Cdd:PRK05159 65 LKRESVVSVTGTVkanPKAPGG-VEVIPEEIEVLNK------------AEEPLPL------DISGKVLAELDTRLDNRFL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 260 DLMvNHEVRHIFKTRSKVVSFIRKFLDGLDFLEVETPmmNMIA----GGAAARPFVTHHNELnmrlYMRIAPELYLKELV 335
Cdd:PRK05159 126 DLR-RPRVRAIFKIRSEVLRAFREFLYENGFTEIFTP--KIVAsgteGGAELFPIDYFEKEA----YLAQSPQLYKQMMV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 336 VGGLDRVYEIGKQFRNEGIDLT-HNPEFTTCEFYMAYAD-YNDLIELTETMLSGMVKELTGGYKIKYHANGVEKPPIEId 413
Cdd:PRK05159 199 GAGFERVFEIGPVFRAEEHNTSrHLNEYTSIDVEMGFIDdHEDVMDLLENLLRYMYEDVAENCEKELELLGIELPVPET- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 414 ftpPFRKIDMieeLEAMAKLNipkdlssdeankylidacAKYDVKCPPPQTTT---RLLDKlvgHFLEETCVNPTFIINH 490
Cdd:PRK05159 278 ---PIPRITY---DEAIEILK------------------SKGNEISWGDDLDTegeRLLGE---YVKEEYGSDFYFITDY 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 491 PEIMSPL-AKWHRSRPGLTERFELFVNKHEVCNAYTELNDpvvqRQRFEEQLKDRqsG-DDEAMaldETFCTALEYGLPP 568
Cdd:PRK05159 331 PSEKRPFyTMPDEDDPEISKSFDLLFRGLEITSGGQRIHR----YDMLVESIKEK--GlNPESF---EFYLEAFKYGMPP 401
|
410 420
....*....|....*....|....*...
gi 55583785 569 TGGWGLGIDRLTMLLTDSQNIKEVLLFP 596
Cdd:PRK05159 402 HGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
133-596 |
3.03e-34 |
|
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: 134.79 E-value: 3.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 133 CLAGRIMTKRaQSSKLLFYDLYGGGEKVQVFADArtSELEDNEFIKfhsTLKRGDIVGVCGYPGKSKR--GELSIFPKKI 210
Cdd:COG0017 18 TVAGWVRTKR-DSGGISFLILRDGSGFIQVVVKK--DKLENFEEAK---KLTTESSVEVTGTVVESPRapQGVELQAEEI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 211 VVLSPCLHMMPRQKSEGSavptpwapgmgrniekyvlrdQETRYRQRYLDLMvNHEVRHIFKTRSKVVSFIRKFLDGLDF 290
Cdd:COG0017 92 EVLGEADEPYPLQPKRHS---------------------LEFLLDNRHLRLR-TNRFGAIFRIRSELARAIREFFQERGF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 291 LEVETPMMnmIAGGA--AARPF-VTHHNElnmRLYMRIAPELYlKELVVGGLDRVYEIGKQFRNEGIDLT-HNPEFTTCE 366
Cdd:COG0017 150 VEVHTPII--TASATegGGELFpVDYFGK---EAYLTQSGQLY-KEALAMALEKVYTFGPTFRAEKSNTRrHLAEFWMIE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 367 FYMAYADYNDLIELTETMLSGMVKELtggykIKYHAN-----GVEKPPIEIDFTPPFRKIDM---IEELEAM-AKLNIPK 437
Cdd:COG0017 224 PEMAFADLEDVMDLAEEMLKYIIKYV-----LENCPEeleflGRDVERLEKVPESPFPRITYteaIEILKKSgEKVEWGD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 438 DLSSdEANKYLidaCAKYDVKcpppqtttrlldklvghfleetcvnPTFIINHP-EIMSPLAKWHRSRPGLTERFELFVN 516
Cdd:COG0017 299 DLGT-EHERYL---GEEFFKK-------------------------PVFVTDYPkEIKAFYMKPNPDDPKTVAAFDLLAP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 517 KhevcnaYTEL-------NDPVVQRQRFEEQlkdrqsG-DDEAMA--LDetfctALEYGLPPTGGWGLGIDRLTMLLTDS 586
Cdd:COG0017 350 G------IGEIiggsqreHRYDVLVERIKEK------GlDPEDYEwyLD-----LRRYGSVPHAGFGLGLERLVMWLTGL 412
|
490
....*....|
gi 55583785 587 QNIKEVLLFP 596
Cdd:COG0017 413 ENIREVIPFP 422
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
249-596 |
8.37e-31 |
|
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: 122.67 E-value: 8.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 249 DQETRYRQRYLDLMVNhEVRHIFKTRSKVVSFIRKFLDGLDFLEVETPMMnmIA----GGAAARPFVTHHNELnmrlYMR 324
Cdd:cd00776 3 NLETLLDNRHLDLRTP-KVQAIFRIRSEVLRAFREFLRENGFTEVHTPKI--TStdteGGAELFKVSYFGKPA----YLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 325 IAPELYlKELVVGGLDRVYEIGKQFRNEGIDLT-HNPEFTTCEFYMAYA-DYNDLIELTETMLSGMVKELTggykikyha 402
Cdd:cd00776 76 QSPQLY-KEMLIAALERVYEIGPVFRAEKSNTRrHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVL--------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 403 ngvEKPPIEIDFtppfrkIDMIEELEAMAKLNIPKdLSSDEANKYLidacAKYDVKCPPPQT---TTRLLDKLVGHFLEE 479
Cdd:cd00776 146 ---ERCAKELEL------VNQLNRELLKPLEPFPR-ITYDEAIELL----REKGVEEEVKWGedlSTEHERLLGEIVKGD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 480 tcvnPTFIINHP-EIMSPLAKWHRSRPGLTERFELFVNKH-EVCNAYTELNDPVVQRQRFEEQlkdrqsGDDEAmaLDET 557
Cdd:cd00776 212 ----PVFVTDYPkEIKPFYMKPDDDNPETVESFDLLMPGVgEIVGGSQRIHDYDELEERIKEH------GLDPE--SFEW 279
|
330 340 350
....*....|....*....|....*....|....*....
gi 55583785 558 FCTALEYGLPPTGGWGLGIDRLTMLLTDSQNIKEVLLFP 596
Cdd:cd00776 280 YLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
134-596 |
2.92e-29 |
|
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: 120.70 E-value: 2.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 134 LAGRIMTKRAQSsKLLFYDLYGGGEKVQVFADARTSEledNEFIKFHSTLKRGDIVGVCGYPGKSKR--GELSIFPKKIV 211
Cdd:TIGR00458 17 FMGWVHEIRDLG-GLIFVLLRDREGLIQITAPAKKVS---KNLFKWAKKLNLESVVAVRGIVKIKEKapGGFEIIPTKIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 212 VLSPC---LHMMPRQKSEGSAvptpwapgmgrniekyvlrdqETRYRQRYLDLMvNHEVRHIFKTRSKVVSFIRKFLDGL 288
Cdd:TIGR00458 93 VINEAkepLPLDPTEKVPAEL---------------------DTRLDYRFLDLR-RPTVQAIFRIRSGVLESVREFLAEE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 289 DFLEVETPMMNMIA--GGAAARPFVTHHNELnmrlYMRIAPELYLKELVVGGLDRVYEIGKQFRNEGIDLT-HNPEFTTC 365
Cdd:TIGR00458 151 GFIEVHTPKLVASAteGGTELFPITYFEREA----FLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHrHLNEATSI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 366 EFYMAYADYNDLIELTETMLSGMVKELTGGYKIKYHANGVEKPPIEIdftpPFRKIDMIEELEAMAKLNIP----KDLSS 441
Cdd:TIGR00458 227 DIEMAFEDHHDVMDILEELVVRVFEDVPERCAHQLETLEFKLEKPEG----KFVRLTYDEAIEMANAKGVEigwgEDLST 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 442 dEANKYLIDacaKYDvkcpppqtttrlldklvGHFleetcvnptFIINHPEIMSPL-AKWHRSRPGLTERFELFVNKHEV 520
Cdd:TIGR00458 303 -EAEKALGE---EMD-----------------GLY---------FITDWPTEIRPFyTMPDEDNPEISKSFDLMYRDLEI 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55583785 521 CNAYTELNDpvvqRQRFEEQLKdRQSGDDEAMaldETFCTALEYGLPPTGGWGLGIDRLTMLLTDSQNIKEVLLFP 596
Cdd:TIGR00458 353 SSGAQRIHL----HDLLVERIK-AKGLNPEGF---KDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFP 420
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
251-596 |
2.47e-28 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 119.79 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 251 ETRYRQRYLDLMvNHEVRHIFKTRSKVVSFIRKFLDGLDFLEVETPMMnmiagGAA----ARPFV----THHNElnmrLY 322
Cdd:PRK00476 122 ELRLKYRYLDLR-RPEMQKNLKLRSKVTSAIRNFLDDNGFLEIETPIL-----TKStpegARDYLvpsrVHPGK----FY 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 323 mriA----PELYLKELVVGGLDRVYEIGKQFRNEgiDLTHN--PEFTT--CEfyMAYADYNDLIELTETMLSGMVKElTG 394
Cdd:PRK00476 192 ---AlpqsPQLFKQLLMVAGFDRYYQIARCFRDE--DLRADrqPEFTQidIE--MSFVTQEDVMALMEGLIRHVFKE-VL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 395 GYKI--------------KYhanGVEKP----PIEI-DFTPPFRKID-----------------------------MIEE 426
Cdd:PRK00476 264 GVDLptpfprmtyaeamrRY---GSDKPdlrfGLELvDVTDLFKDSGfkvfagaandggrvkairvpggaaqlsrkQIDE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 427 LEAMAKLN------------------IPKDLSSDEANKyLIDAC-AK--------YDvkcpPPQTTTRLLDKL---VGHF 476
Cdd:PRK00476 341 LTEFAKIYgakglayikvnedglkgpIAKFLSEEELAA-LLERTgAKdgdliffgAD----KAKVVNDALGALrlkLGKE 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 477 L---EETCVNPTFIINHP--EIMSPLAKWHRS-------RPGLTERFELfVNKHE--------VCNAYtEL-------ND 529
Cdd:PRK00476 416 LgliDEDKFAFLWVVDFPmfEYDEEEGRWVAAhhpftmpKDEDLDELET-TDPGKarayaydlVLNGY-ELgggsiriHR 493
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55583785 530 PVVQRQRFeeqlkdrqsgddEAMALDET--------FCTALEYGLPPTGGWGLGIDRLTMLLTDSQNIKEVLLFP 596
Cdd:PRK00476 494 PEIQEKVF------------EILGISEEeaeekfgfLLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
271-596 |
4.24e-28 |
|
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: 113.82 E-value: 4.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 271 FKTRSKVVSFIRKFLDGLDFLEVETPMMN-MIAGGAaaRPFV----THHNelnmRLY-MRIAPELYLKELVVGGLDRVYE 344
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTkSTPEGA--RDFLvpsrLHPG----KFYaLPQSPQLFKQLLMVSGFDRYFQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 345 IGKQFRNEGIDLTHNPEFTTCEFYMAYADYNDLIELTETMLSGMVKELTGgykikyhangvekppieIDFTPPFRKIdmi 424
Cdd:cd00777 75 IARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG-----------------VELTTPFPRM--- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 425 eeleamaklnipkdlSSDEA-NKYLIDACAKYDvkcpPPqtttrLLDklvghFLEETcvnPTFIINHPEIMSPLAKWH-- 501
Cdd:cd00777 135 ---------------TYAEAmERYGFKFLWIVD----FP-----LFE-----WDEEE---GRLVSAHHPFTAPKEEDLdl 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 502 -RSRPG--LTERFELFVNKHEVCNAYTELNDPVVQRQRFEEQLKDrqsgDDEAMALDETFCTALEYGLPPTGGWGLGIDR 578
Cdd:cd00777 183 lEKDPEdaRAQAYDLVLNGVELGGGSIRIHDPDIQEKVFEILGLS----EEEAEEKFGFLLEAFKYGAPPHGGIALGLDR 258
|
330
....*....|....*...
gi 55583785 579 LTMLLTDSQNIKEVLLFP 596
Cdd:cd00777 259 LVMLLTGSESIRDVIAFP 276
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
251-596 |
1.03e-25 |
|
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: 111.63 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 251 ETRYRQRYLDLMvNHEVRHIFKTRSKVVSFIRKFLDGLDFLEVETPMMnmiagGAA----ARPFV----THHNElnmrLY 322
Cdd:COG0173 123 ELRLKYRYLDLR-RPEMQKNLILRHKVTKAIRNYLDENGFLEIETPIL-----TKStpegARDYLvpsrVHPGK----FY 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 323 mriA----PELYlKE-LVVGGLDRVYEIGKQFRNEgiDLTHN--PEFTT--CEfyMAYADYNDLIELTETMLSGMVKElT 393
Cdd:COG0173 193 ---AlpqsPQLF-KQlLMVSGFDRYFQIARCFRDE--DLRADrqPEFTQldIE--MSFVDQEDVFELMEGLIRHLFKE-V 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 394 GGYKI--------------KYhanGVEKP----PIEI-DFTPPFRKID----------------------------MIEE 426
Cdd:COG0173 264 LGVELptpfprmtyaeameRY---GSDKPdlrfGLELvDVTDIFKDSGfkvfagaaenggrvkainvpggaslsrkQIDE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 427 LEAMAKL------------------NIPKDLSSDEANKyLIDACakyDVK--------CPPPQTTTRLLDKL---VGHFL 477
Cdd:COG0173 341 LTEFAKQygakglayikvnedglksPIAKFLSEEELAA-ILERL---GAKpgdliffvADKPKVVNKALGALrlkLGKEL 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 478 ---EETCVNPTFIINHP--EIMSPLAKWHRS-------RPGLTERFElfVNKHEV-CNAY------TEL-------NDPV 531
Cdd:COG0173 417 gliDEDEFAFLWVVDFPlfEYDEEEGRWVAMhhpftmpKDEDLDLLE--TDPGKVrAKAYdlvlngYELgggsiriHDPE 494
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 532 VQRQRFEeqlkdrqsGDDEAMA-----LDetfctALEYGLPPTGGWGLGIDRLTMLLTDSQNIKEVLLFP 596
Cdd:COG0173 495 LQEKVFEll----giSEEEAEEkfgflLE-----AFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
122-596 |
1.24e-18 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 89.38 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 122 NVGDKLVDVTECLAGRIMTKRAQSsKLLFYDLYGGGEKVQVFADARTSELEDNeFIKFHSTLKRGDIVGVCG---YPGKS 198
Cdd:PLN02850 74 DLGEELAGSEVLIRGRVHTIRGKG-KSAFLVLRQSGFTVQCVVFVSEVTVSKG-MVKYAKQLSRESVVDVEGvvsVPKKP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 199 KRG---ELSIFPKKIVVLSPCLHMMPRQ-----KSEgSAVPTPWAPGmgrniEKYVLRDQETRYRQRYLDLMV--NHEvr 268
Cdd:PLN02850 152 VKGttqQVEIQVRKIYCVSKALATLPFNvedaaRSE-SEIEKALQTG-----EQLVRVGQDTRLNNRVLDLRTpaNQA-- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 269 hIFKTRSKVVSFIRKFLDGLDFLEVETPmmNMIAG----GAAArpFVTHHNELNMRLYMriAPELYLKELVVGGLDRVYE 344
Cdd:PLN02850 224 -IFRIQSQVCNLFREFLLSKGFVEIHTP--KLIAGasegGSAV--FRLDYKGQPACLAQ--SPQLHKQMAICGDFRRVFE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 345 IGKQFRNEGiDLTHNP--EFTTCEFYMAYAD-YNDLIELTETMLSGMVKELTGGYKIKYHANGVEKPPIEIDFTPPFRKI 421
Cdd:PLN02850 297 IGPVFRAED-SFTHRHlcEFTGLDLEMEIKEhYSEVLDVVDELFVAIFDGLNERCKKELEAIREQYPFEPLKYLPKTLRL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 422 DMIEELEAMAKLNIPKDLSSD---EANKYLIDAC-AKYDvkcpppqTTTRLLDKL---VGHFLEETCVNptfiinhpeim 494
Cdd:PLN02850 376 TFAEGIQMLKEAGVEVDPLGDlntESERKLGQLVkEKYG-------TDFYILHRYplaVRPFYTMPCPD----------- 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 495 splakwhrsRPGLTERFELFVNKHEVCNAYTELNDPVVQRQRFEEQLKDRQSGddeamaldETFCTALEYGLPPTGGWGL 574
Cdd:PLN02850 438 ---------DPKYSNSFDVFIRGEEIISGAQRVHDPELLEKRAEECGIDVKTI--------STYIDSFRYGAPPHGGFGV 500
|
490 500
....*....|....*....|..
gi 55583785 575 GIDRLTMLLTDSQNIKEVLLFP 596
Cdd:PLN02850 501 GLERVVMLFCGLNNIRKTSLFP 522
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
273-386 |
1.12e-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: 81.78 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 273 TRSKVVSFIRKFLDGLDFLEVETPMMNMIAGGAAAR----PFVTHHNELNMRLYMRIAPELYLKELVVGGL----DRVYE 344
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGhepkDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIrklpLRLAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 55583785 345 IGKQFRNEGI--DLTHNPEFTTCEFYMAYAD------YNDLIELTETMLS 386
Cdd:cd00768 81 IGPAFRNEGGrrGLRRVREFTQLEGEVFGEDgeeaseFEELIELTEELLR 130
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
125-596 |
5.74e-16 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 81.19 E-value: 5.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 125 DKLVDVTECLAGRIMTKRaQSSKLLFYDLYGGGEKVQvfADARTSELEDNEFIKFHSTLKRGDIVGV----CGYP---GK 197
Cdd:PTZ00401 74 PELVDKTVLIRARVSTTR-KKGKMAFMVLRDGSDSVQ--AMAAVEGDVPKEMIDFIGQIPTESIVDVeatvCKVEqpiTS 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 198 SKRGELSIFPKKIVVLSPCLHMMPRQKSEGSAvptpwapgmgRNIEKYVLRDQETRYRQRYLDLMVNHEvRHIFKTRSKV 277
Cdd:PTZ00401 151 TSHSDIELKVKKIHTVTESLRTLPFTLEDASR----------KESDEGAKVNFDTRLNSRWMDLRTPAS-GAIFRLQSRV 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 278 VSFIRKFLDGLDFLEVETPMMNMIAGGAAARPFVTHHneLNMRLYMRIAPELYLKELVVGGLDRVYEIGKQFRNEGIDL- 356
Cdd:PTZ00401 220 CQYFRQFLIDSDFCEIHSPKIINAPSEGGANVFKLEY--FNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTh 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 357 THNPEFTTCEFYMAYAD-YNDLIELTETMLSGMVKELTGgykikyHANGVEKPPIEIDFTPPFRKI--DMIEEL--EAMA 431
Cdd:PTZ00401 298 RHLTEFVGLDVEMRINEhYYEVLDLAESLFNYIFERLAT------HTKELKAVCQQYPFEPLVWKLtpERMKELgvGVIS 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 432 KLNIPKDLSsdEANKYLIDA---------CAK-----YDVKCPPPQTTTRLLDKLVGHFLEETCVNPTFIINH-PEIMSP 496
Cdd:PTZ00401 372 EGVEPTDKY--QARVHNMDSrmlrinymhCIEllntvLEEKMAPTDDINTTNEKLLGKLVKERYGTDFFISDRfPSSARP 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 497 LAKWH-RSRPGLTERFELFVNKHEVCNAYTELNDPVVQRQRFEEQLKDRQSGDDeamaldetFCTALEYGLPPTGGWGLG 575
Cdd:PTZ00401 450 FYTMEcKDDERFTNSYDMFIRGEEISSGAQRIHDPDLLLARAKMLNVDLTPIKE--------YVDSFRLGAWPHGGFGVG 521
|
490 500
....*....|....*....|.
gi 55583785 576 IDRLTMLLTDSQNIKEVLLFP 596
Cdd:PTZ00401 522 LERVVMLYLGLSNVRLASLFP 542
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
262-596 |
7.82e-16 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 78.91 E-value: 7.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 262 MVNHEVRHIFKTRSKVVSFIRKFLDGLDFLEVETPMMNMIA-----GGAAARPFVTHHNELNMRLYMRIAPELYlKELVV 336
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPSTdplmgLGSDLPVKQISIDFYGVEYYLADSMILH-KQLAL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 337 GGLDRVYEIGKQFRNEG---IDLTHNPEFTTCEFYMAYADYNDLIELTETMLSGMVKELTGGYKIKYHANGVEKPpieiD 413
Cdd:PRK06462 100 RMLGKIFYLSPNFRLEPvdkDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEDELEFFGRDLP----H 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 414 FTPPFRKI---DMIEELEAMAKLNIPKDLSSDEANKYLIdacakydvkcpppqtttrlldklvGHFLEetcvnPTFIINH 490
Cdd:PRK06462 176 LKRPFKRIthkEAVEILNEEGCRGIDLEELGSEGEKSLS------------------------EHFEE-----PFWIIDI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 491 PEIMSPL-AKWHRSRPG--------LTERFELFVNKHEVCNAYTElndpVVQRQrfeeqlkdRQSGDDEA-------MAL 554
Cdd:PRK06462 227 PKGSREFyDREDPERPGvlrnydllLPEGYGEAVSGGEREYEYEE----IVERI--------REHGVDPEkykwyleMAK 294
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 55583785 555 DetfctaleyGLPPTGGWGLGIDRLTMLLTDSQNIKEVLLFP 596
Cdd:PRK06462 295 E---------GPLPSAGFGIGVERLTRYICGLRHIREVQPFP 327
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
134-215 |
1.11e-15 |
|
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. Class 2b aaRSs include the homodimeric aspartyl-, asparaginyl-, and lysyl-tRNA synthetases (AspRS, AsnRS, and LysRS). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Included in this group are archeal and archeal-like AspRSs which are non-discriminating and can charge both tRNAAsp and tRNAAsn. E. coli cells have two isoforms of LysRSs (LysS and LysU) encoded by two distinct genes, which are differentially regulated. The cytoplasmic and the mitochondrial isoforms of human LysRS are encoded by a single gene. Yeast cytoplasmic and mitochondrial LysRSs participate in mitochondrial import of cytoplasmic tRNAlysCUU. In addition to their housekeeping role, human LysRS may function as a signaling molecule that activates immune cells. Tomato LysRS may participate in a process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging. AsnRS is immunodominant antigen of the filarial nematode Brugia malayai and is of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.
Pssm-ID: 239766 [Multi-domain] Cd Length: 85 Bit Score: 72.21 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 134 LAGRIMTKRAQSsKLLFYDLYGGGEKVQVFADARtselEDNEFIKFHSTLKRGDIVGVCGYPGKSKR-----GELSIFPK 208
Cdd:cd04100 4 LAGWVHSRRDHG-GLIFIDLRDGSGIVQVVVNKE----ELGEFFEEAEKLRTESVVGVTGTVVKRPEgnlatGEIELQAE 78
|
....*..
gi 55583785 209 KIVVLSP 215
Cdd:cd04100 79 ELEVLSK 85
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
250-432 |
2.78e-15 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 79.06 E-value: 2.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 250 QETRYRQRYLDLMVNHEVRHIfKTRSKVVSFIRKFL-DGLDFLEVETPMMNMiAGGAAARPFVTHHNELNMRLY-MRIAP 327
Cdd:PLN02903 183 EEVRLRYRVLDLRRPQMNANL-RLRHRVVKLIRRYLeDVHGFVEIETPILSR-STPEGARDYLVPSRVQPGTFYaLPQSP 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 328 ELYLKELVVGGLDRVYEIGKQFRNEGIDLTHNPEFTTCEFYMAYADYNDLIELTETMLSGMVKELTGgykikyhangvek 407
Cdd:PLN02903 261 QLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDMELAFTPLEDMLKLNEDLIRQVFKEIKG------------- 327
|
170 180
....*....|....*....|....*
gi 55583785 408 ppieIDFTPPFRKIDMIeelEAMAK 432
Cdd:PLN02903 328 ----VQLPNPFPRLTYA---EAMSK 345
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
201-596 |
1.45e-14 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 76.95 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 201 GELSIFPKKIVVLSPCLhMMPRQKSEGSAVPtpwapGMGRNIEKYVLRDQETRYRqrYLDLMVNHEVRHIFKtRSKVVSF 280
Cdd:PRK12820 95 GDIEVFVRELSILAASE-ALPFAISDKAMTA-----GAGSAGADAVNEDLRLQYR--YLDIRRPAMQDHLAK-RHRIIKC 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 281 IRKFLDGLDFLEVETPMMNMiAGGAAARPFVTHHNELNMRLY-MRIAPELYLKELVVGGLDRVYEIGKQFRNEGIDLTHN 359
Cdd:PRK12820 166 ARDFLDSRGFLEIETPILTK-STPEGARDYLVPSRIHPKEFYaLPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQ 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 360 PEFTTCEFYMAYADYNDLIELTETMLSGMVKelTGG-----------YKIKYHANGVEKPPIE-----IDFTPPFRK--- 420
Cdd:PRK12820 245 PEFTQLDIEASFIDEEFIFELIEELTARMFA--IGGialprpfprmpYAEAMDTTGSDRPDLRfdlkfADATDIFENtry 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 421 ---------------IDMIEELEAMAK-------------------------------LNIPKDLSSDE----------- 443
Cdd:PRK12820 323 gifkqilqrggrikgINIKGQSEKLSKnvlqneyakeiapsfgakgmtwmraeaggldSNIVQFFSADEkealkrrfhae 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 444 -ANKYLIDACAKYD-VKCPPPQTTTRLLDKLvgHFLEETCVNPTFIINHPEIMS-----------PLAKWHRSR--PG-- 506
Cdd:PRK12820 403 dGDVIIMIADASCAiVLSALGQLRLHLADRL--GLIPEGVFHPLWITDFPLFEAtddggvtsshhPFTAPDREDfdPGdi 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 507 -----LTER-FELFVNKHEVCNAYTELNDPVVQRQRF------EEQLKDRQSgddeamaldeTFCTALEYGLPPTGGWGL 574
Cdd:PRK12820 481 eelldLRSRaYDLVVNGEELGGGSIRINDKDIQLRIFaalglsEEDIEDKFG----------FFLRAFDFAAPPHGGIAL 550
|
490 500
....*....|....*....|..
gi 55583785 575 GIDRLTMLLTDSQNIKEVLLFP 596
Cdd:PRK12820 551 GLDRVVSMILQTPSIREVIAFP 572
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
134-213 |
1.82e-12 |
|
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: 62.64 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 134 LAGRIMTKRAQSSKLLFYDLYGGGEKVQVFADartseleDNEFIKFHSTLKRGDIVGVCGYPGKSKRGELSIFPKKIVVL 213
Cdd:pfam01336 3 VAGRVTSIRRSGGKLLFLTLRDGTGSIQVVVF-------KEEAEKLAKKLKEGDVVRVTGKVKKRKGGELELVVEEIELL 75
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
125-596 |
1.30e-06 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 51.26 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 125 DKLVDVTECLAGRIMTKRaQSSKLLFYDLYGGG--EKVQVFADArtsELEDNEFIKfhsTLKRGDIVGVCGY----PGKS 198
Cdd:PRK03932 12 GKYVGQEVTVRGWVRTKR-DSGKIAFLQLRDGScfKQLQVVKDN---GEEYFEEIK---KLTTGSSVIVTGTvvesPRAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 199 KRGELSIfpKKIVVLSPCLHMMPRQKSEGSavptpwapgmgrnIEKyvLRDQetryrqRYLDLMVNhEVRHIFKTRSKVV 278
Cdd:PRK03932 85 QGYELQA--TKIEVIGEDPEDYPIQKKRHS-------------IEF--LREI------AHLRPRTN-KFGAVMRIRNTLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 279 SFIRKFLDGLDFLEVETPMMNMIAGGAAARPFVTHHNELNMRL-------YMRIAPELYLkELVVGGLDRVYEIGKQFRN 351
Cdd:PRK03932 141 QAIHEFFNENGFVWVDTPIITASDCEGAGELFRVTTLDLDFSKdffgkeaYLTVSGQLYA-EAYAMALGKVYTFGPTFRA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 352 EGIDLT-HNPEFTTCEFYMAYADYNDLIELTETMLSGMVKELtggykikyhangVEKPPIEIDFTPPFRKIDMIEELEAM 430
Cdd:PRK03932 220 ENSNTRrHLAEFWMIEPEMAFADLEDNMDLAEEMLKYVVKYV------------LENCPDDLEFLNRRVDKGDIERLENF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 431 AKLNIPKdLSSDEANKYLIDACAKYDVKcpppqtttrlldklVGH----------FLEETCVN-PTFIINHP-EI----M 494
Cdd:PRK03932 288 IESPFPR-ITYTEAIEILQKSGKKFEFP--------------VEWgddlgseherYLAEEHFKkPVFVTNYPkDIkafyM 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 495 SP------------LAkwhrsrPGLTE---------RFELFVnkhevcnaytelndpvvqrQRFEEqlkdrqsgddeaMA 553
Cdd:PRK03932 353 RLnpdgktvaamdlLA------PGIGEiiggsqreeRLDVLE-------------------ARIKE------------LG 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 55583785 554 LDETfctALE-------YGLPPTGGWGLGIDRLTMLLTDSQNIKEVLLFP 596
Cdd:PRK03932 396 LNKE---DYWwyldlrrYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFP 442
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
136-215 |
2.69e-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: 40.62 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583785 136 GRIMTKRAQSSKLLFYDLYGGGEKVQVFADArTSELEDNEFIKFHSTLKRGDIVGVCGY------PGKS---KRGELSIf 206
Cdd:cd04320 6 ARVHTSRAQGAKLAFLVLRQQGYTIQGVLAA-SAEGVSKQMVKWAGSLSKESIVDVEGTvkkpeePIKSctqQDVELHI- 83
|
....*....
gi 55583785 207 pKKIVVLSP 215
Cdd:cd04320 84 -EKIYVVSE 91
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
563-596 |
1.72e-03 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 41.16 E-value: 1.72e-03
10 20 30
....*....|....*....|....*....|....
gi 55583785 563 EYGLPPTGGWGLGIDRLTMLLTDSQNIKEVLLFP 596
Cdd:PTZ00425 545 KFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFP 578
|
|
| |
