|
Name |
Accession |
Description |
Interval |
E-value |
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
1-580 |
0e+00 |
|
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: 1005.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 1 MRRTHYAGSLRETHVGEEVVLEGWVNRRRDLGGLIFLDLRDREGLVQLVAHP--ASPAYATAERVRPEWVVRAKGLVRLR 78
Cdd:COG0173 1 MYRTHYCGELRESDVGQEVTLSGWVHRRRDHGGLIFIDLRDRYGITQVVFDPddSAEAFEKAEKLRSEYVIAVTGKVRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 79 PE--PNPRLATGRVEVELSALEVLAEAKTPPFPVDAGwrgeeeKEASEELRLK---------YryldlrrrrMQENLRLR 147
Cdd:COG0173 81 PEgtVNPKLPTGEIEVLASELEILNKAKTPPFQIDDD------TDVSEELRLKyryldlrrpE---------MQKNLILR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 148 HRVIKAIWDFLDREGFVQVETPFLTKSTPEGARDFLVPYRHEPGLFYALPQSPQLFKQMLMVAGLDRYFQIARCFRDEDL 227
Cdd:COG0173 146 HKVTKAIRNYLDENGFLEIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFRDEDL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 228 RADRQPDFTQLDLEMSFVEVEDVLELNERLMAHVFREALGVELPLPFPRLSYEEAMERYGSDKPDLRFGLELKEVGPLFR 307
Cdd:COG0173 226 RADRQPEFTQLDIEMSFVDQEDVFELMEGLIRHLFKEVLGVELPTPFPRMTYAEAMERYGSDKPDLRFGLELVDVTDIFK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 308 QSGFRVFQEA----ESVKALALPKA--LSRKEVAELEEVAKRHKAQGLAWARVEEGGFSGGVAKFLEP-VREALLQATEA 380
Cdd:COG0173 306 DSGFKVFAGAaengGRVKAINVPGGasLSRKQIDELTEFAKQYGAKGLAYIKVNEDGLKSPIAKFLSEeELAAILERLGA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 381 RPGDTLLFVAGPRKVAATALGAVRLRAADLLGL-KREGFRFLWVVDFPLLEWDEEEEAWTYMHHPFTSPHPEDLPLLEKD 459
Cdd:COG0173 386 KPGDLIFFVADKPKVVNKALGALRLKLGKELGLiDEDEFAFLWVVDFPLFEYDEEEGRWVAMHHPFTMPKDEDLDLLETD 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 460 PGRVRALAYDLVLNGVEVGGGSIRIHDPRLQARVFRLLGIGEEEQREKFGFFLEALEYGAPPHGGIAWGLDRLLALMTGS 539
Cdd:COG0173 466 PGKVRAKAYDLVLNGYELGGGSIRIHDPELQEKVFELLGISEEEAEEKFGFLLEAFKYGAPPHGGIAFGLDRLVMLLAGE 545
|
570 580 590 600
....*....|....*....|....*....|....*....|.
1G51_B 540 PSIREVIAFPKNKEGKDPLTGAPSPVPEEQLRELGLMVVRP 580
Cdd:COG0173 546 DSIRDVIAFPKTQSAQDLMTGAPSEVDEKQLKELHIRLRPP 586
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
1-580 |
0e+00 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 997.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 1 MRRTHYAGSLRETHVGEEVVLEGWVNRRRDLGGLIFLDLRDREGLVQLVAHPASPAYATAERVRPEWVVRAKGLVRLRPE 80
Cdd:PRK00476 2 MMRTHYCGELRESHVGQTVTLCGWVHRRRDHGGLIFIDLRDREGIVQVVFDPDAEAFEVAESLRSEYVIQVTGTVRARPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 81 --PNPRLATGRVEVELSALEVLAEAKTPPFPVDagwrgeEEKEASEELRLKYRYLDLRRRRMQENLRLRHRVIKAIWDFL 158
Cdd:PRK00476 82 gtVNPNLPTGEIEVLASELEVLNKSKTLPFPID------DEEDVSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 159 DREGFVQVETPFLTKSTPEGARDFLVPYRHEPGLFYALPQSPQLFKQMLMVAGLDRYFQIARCFRDEDLRADRQPDFTQL 238
Cdd:PRK00476 156 DDNGFLEIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEFTQI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 239 DLEMSFVEVEDVLELNERLMAHVFREALGVELPLPFPRLSYEEAMERYGSDKPDLRFGLELKEVGPLFRQSGFRVFQEA- 317
Cdd:PRK00476 236 DIEMSFVTQEDVMALMEGLIRHVFKEVLGVDLPTPFPRMTYAEAMRRYGSDKPDLRFGLELVDVTDLFKDSGFKVFAGAa 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 318 ---ESVKALALPKA---LSRKEVAELEEVAKRHKAQGLAWARVEEGGFSGGVAKFL-EPVREALLQATEARPGDTLLFVA 390
Cdd:PRK00476 316 ndgGRVKAIRVPGGaaqLSRKQIDELTEFAKIYGAKGLAYIKVNEDGLKGPIAKFLsEEELAALLERTGAKDGDLIFFGA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 391 GPRKVAATALGAVRLRAADLLGL-KREGFRFLWVVDFPLLEWDEEEEAWTYMHHPFTSPHPEDLPLLEK-DPGRVRALAY 468
Cdd:PRK00476 396 DKAKVVNDALGALRLKLGKELGLiDEDKFAFLWVVDFPMFEYDEEEGRWVAAHHPFTMPKDEDLDELETtDPGKARAYAY 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 469 DLVLNGVEVGGGSIRIHDPRLQARVFRLLGIGEEEQREKFGFFLEALEYGAPPHGGIAWGLDRLLALMTGSPSIREVIAF 548
Cdd:PRK00476 476 DLVLNGYELGGGSIRIHRPEIQEKVFEILGISEEEAEEKFGFLLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAF 555
|
570 580 590
....*....|....*....|....*....|..
1G51_B 549 PKNKEGKDPLTGAPSPVPEEQLRELGLMVVRP 580
Cdd:PRK00476 556 PKTQSAQDLLTGAPSPVDEKQLRELGIRLRKK 587
|
|
| aspS_bact |
TIGR00459 |
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be ... |
2-573 |
0e+00 |
|
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be discriminating (6.1.1.12) or nondiscriminating (6.1.1.23). 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_bact, represents aspartyl-tRNA synthetases from the Bacteria and from mitochondria. In some species, this enzyme aminoacylates tRNA for both Asp and Asn; Asp-tRNA(asn) is subsequently transamidated to Asn-tRNA(asn). This model generates very low scores for the archaeal type of aspS and for asnS; scores between the trusted and noise cutoffs represent fragmentary sequences. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 211576 [Multi-domain] Cd Length: 583 Bit Score: 732.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 2 RRTHYAGSLRETHVGEEVVLEGWVNRRRDLGGLIFLDLRDREGLVQLVAHPASPAYATAERVRPEWVVRAKGLVRLRPEP 81
Cdd:TIGR00459 1 MRTHYCGQLRTEHLGQTVTLAGWVNRRRDLGGLIFIDLRDRSGIVQVVCDPDADALKLAKGLRNEDVVQVKGKVSARPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 82 --NPRLATGRVEVELSALEVLAEAKTPPFPVDagwrgeeEKEASEELRLKYRYLDLRRRRMQENLRLRHRVIKAIWDFLD 159
Cdd:TIGR00459 81 niNRNLDTGEIEILAESITLLNKSKTPPLIIE-------KTDAEEEVRLKYRYLDLRRPEMQQRLKLRHKVTKAVRNFLD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 160 REGFVQVETPFLTKSTPEGARDFLVPYRHEPGLFYALPQSPQLFKQMLMVAGLDRYFQIARCFRDEDLRADRQPDFTQLD 239
Cdd:TIGR00459 154 QQGFLEIETPMLTKSTPEGARDYLVPSRVHKGEFYALPQSPQLFKQLLMVSGVDRYYQIARCFRDEDLRADRQPEFTQID 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 240 LEMSFVEVEDVLELNERLMAHVFREALGVELPLPFPRLSYEEAMERYGSDKPDLRFGLELKEVGPLFRQSGFRVFQEA-- 317
Cdd:TIGR00459 234 MEMSFMTQEDVMELIEKLVSHVFLEVKGIDLKKPFPVMTYAEAMERYGSDKPDLRFPLELIDVTDLFKDSEFKVFSNLin 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 318 --ESVKALALPKA---LSRKEVAELEEVAKRHKAQGLAWARVEEGGFSGGVAKFL-EPVREALLQATEARPGDTLLFVAG 391
Cdd:TIGR00459 314 dgGRVKAIRVPGGwaeLSRKSIKELRKFAKEYGAKGLAYLKVNEDGINSPIKKFLdEKKGKILLERTDAQNGDILLFGAG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 392 PRKVAATALGAVRLRAADLLGLKREG-FRFLWVVDFPLLEWDEEEEaWTYMHHPFTSPHPEDLPLLEKDPGRVRALAYDL 470
Cdd:TIGR00459 394 SKKIVLDALGALRLKLGKDLGLVDPDlFSFLWVVDFPMFEKDKEGR-LCAAHHPFTMPKDEDLENLEAAPEEALAEAYDL 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 471 VLNGVEVGGGSIRIHDPRLQARVFRLLGIGEEEQREKFGFFLEALEYGAPPHGGIAWGLDRLLALMTGSPSIREVIAFPK 550
Cdd:TIGR00459 473 VLNGVELGGGSIRIHDPEVQKKVFEILGIDPEEAREKFGFLLEAFKYGTPPHAGFALGLDRLMMLLTGTDNIRDVIAFPK 552
|
570 580
....*....|....*....|...
1G51_B 551 NKEGKDPLTGAPSPVPEEQLREL 573
Cdd:TIGR00459 553 TTAAACLMTEAPSFIDEKQLEEL 575
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
2-580 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 659.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 2 RRTHYAGSLRETHVGEEVVLEGWVNRRRDLGGLIFLDLRDREGLVQLVAHPASP--AYATAERVRPEWVVRAKGLVRLRP 79
Cdd:PLN02903 58 SRSHLCGALSVNDVGSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDEFpeAHRTANRLRNEYVVAVEGTVRSRP 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 80 E--PNPRLATGRVEVELSALEVLAEAKTP-PFPVDAGwrGEEEKEASEELRLKYRYLDLRRRRMQENLRLRHRVIKAIWD 156
Cdd:PLN02903 138 QesPNKKMKTGSVEVVAESVDILNVVTKSlPFLVTTA--DEQKDSIKEEVRLRYRVLDLRRPQMNANLRLRHRVVKLIRR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 157 FL-DREGFVQVETPFLTKSTPEGARDFLVPYRHEPGLFYALPQSPQLFKQMLMVAGLDRYFQIARCFRDEDLRADRQPDF 235
Cdd:PLN02903 216 YLeDVHGFVEIETPILSRSTPEGARDYLVPSRVQPGTFYALPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEF 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 236 TQLDLEMSFVEVEDVLELNERLMAHVFREALGVELPLPFPRLSYEEAMERYGSDKPDLRFGLELKEVGPLFRQSGFRVFQ 315
Cdd:PLN02903 296 TQLDMELAFTPLEDMLKLNEDLIRQVFKEIKGVQLPNPFPRLTYAEAMSKYGSDKPDLRYGLELVDVSDVFAESSFKVFA 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 316 EAES----VKALALPKA-----LSRKEVAELEEVAKRHKAQGLAWARVEEGGFSGGVAKFLE----PVREALLQATEARP 382
Cdd:PLN02903 376 GALEsggvVKAICVPDGkkisnNTALKKGDIYNEAIKSGAKGLAFLKVLDDGELEGIKALVEslspEQAEQLLAACGAGP 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 383 GDTLLFVAGPRKVAATALGAVRLRAADLLGLKREG-FRFLWVVDFPLLEWDEEEEAWTYMHHPFTSPHPEDLplleKDPG 461
Cdd:PLN02903 456 GDLILFAAGPTSSVNKTLDRLRQFIAKTLDLIDPSrHSILWVTDFPMFEWNEDEQRLEALHHPFTAPNPEDM----GDLS 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 462 RVRALAYDLVLNGVEVGGGSIRIHDPRLQARVFRLLGIGEEEQREKFGFFLEALEYGAPPHGGIAWGLDRLLALMTGSPS 541
Cdd:PLN02903 532 SARALAYDMVYNGVEIGGGSLRIYRRDVQQKVLEAIGLSPEEAESKFGYLLEALDMGAPPHGGIAYGLDRLVMLLAGAKS 611
|
570 580 590
....*....|....*....|....*....|....*....
1G51_B 542 IREVIAFPKNKEGKDPLTGAPSPVPEEQLRELGLMVVRP 580
Cdd:PLN02903 612 IRDVIAFPKTTTAQCALTRAPSEVDDKQLQDLSIASTAP 650
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
6-576 |
0e+00 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 548.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 6 YAGSLRETHVGEEVVLEGWVNRRRDLGGLIFLDLRDREGLVQLVAHP-ASPA--YATAERVRPEWVVRAKGLVRLRPE-- 80
Cdd:PRK12820 8 FCGHLSLDDTGREVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPeAAPAdvYELAASLRAEFCVALQGEVQKRLEet 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 81 PNPRLATGRVEVELSALEVLAEAKTPPFPVD-----AGWRGEEEKEASEELRLKYRYLDLRRRRMQENLRLRHRVIKAIW 155
Cdd:PRK12820 88 ENPHIETGDIEVFVRELSILAASEALPFAISdkamtAGAGSAGADAVNEDLRLQYRYLDIRRPAMQDHLAKRHRIIKCAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 156 DFLDREGFVQVETPFLTKSTPEGARDFLVPYRHEPGLFYALPQSPQLFKQMLMVAGLDRYFQIARCFRDEDLRADRQPDF 235
Cdd:PRK12820 168 DFLDSRGFLEIETPILTKSTPEGARDYLVPSRIHPKEFYALPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 236 TQLDLEMSFVEVEDVLELNERLMAHVFrEALGVELPLPFPRLSYEEAMERYGSDKPDLRFGLELKEVGPLFRQSGFRVF- 314
Cdd:PRK12820 248 TQLDIEASFIDEEFIFELIEELTARMF-AIGGIALPRPFPRMPYAEAMDTTGSDRPDLRFDLKFADATDIFENTRYGIFk 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 315 ---QEAESVKAL-------ALPKALSRKEVAelEEVAKRHKAQGLAWARVEEGGFSGGVAKFL-EPVREALLQATEARPG 383
Cdd:PRK12820 327 qilQRGGRIKGInikgqseKLSKNVLQNEYA--KEIAPSFGAKGMTWMRAEAGGLDSNIVQFFsADEKEALKRRFHAEDG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 384 DTLLFVAGPR-KVAATALGAVRLRAADLLGLKREG-FRFLWVVDFPLLEwDEEEEAWTYMHHPFTSPHPEDLpllekDPG 461
Cdd:PRK12820 405 DVIIMIADAScAIVLSALGQLRLHLADRLGLIPEGvFHPLWITDFPLFE-ATDDGGVTSSHHPFTAPDREDF-----DPG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 462 RV------RALAYDLVLNGVEVGGGSIRIHDPRLQARVFRLLGIGEEEQREKFGFFLEALEYGAPPHGGIAWGLDRLLAL 535
Cdd:PRK12820 479 DIeelldlRSRAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDIEDKFGFFLRAFDFAAPPHGGIALGLDRVVSM 558
|
570 580 590 600
....*....|....*....|....*....|....*....|.
1G51_B 536 MTGSPSIREVIAFPKNKEGKDPLTGAPSPVPEEQLRELGLM 576
Cdd:PRK12820 559 ILQTPSIREVIAFPKNRSAACPLTGAPSEVAQEQLAELGLL 599
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
144-552 |
1.42e-178 |
|
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: 505.19 E-value: 1.42e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 144 LRLRHRVIKAIWDFLDREGFVQVETPFLTKSTPEGARDFLVPYRHEPGLFYALPQSPQLFKQMLMVAGLDRYFQIARCFR 223
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGARDFLVPSRLHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 224 DEDLRADRQPDFTQLDLEMSFVEVEDVLELNERLMAHVFREALGVELPLPFPRLSYEEAMERYgsdkpdlrfglelkevg 303
Cdd:cd00777 81 DEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGVELTTPFPRMTYAEAMERY----------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 304 plfrqsgfrvfqeaesvkalalpkalsrkevaeleevakrhkaqglawarveeggfsggvakflepvreallqatearpg 383
Cdd:cd00777 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 384 dtllfvagprkvaatalgavrlraadllglkreGFRFLWVVDFPLLEWDEEEEAWTYMHHPFTSPHPEDLPLLEKDPGRV 463
Cdd:cd00777 144 ---------------------------------GFKFLWIVDFPLFEWDEEEGRLVSAHHPFTAPKEEDLDLLEKDPEDA 190
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 464 RALAYDLVLNGVEVGGGSIRIHDPRLQARVFRLLGIGEEEQREKFGFFLEALEYGAPPHGGIAWGLDRLLALMTGSPSIR 543
Cdd:cd00777 191 RAQAYDLVLNGVELGGGSIRIHDPDIQEKVFEILGLSEEEAEEKFGFLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIR 270
|
....*....
1G51_B 544 EVIAFPKNK 552
Cdd:cd00777 271 DVIAFPKTQ 279
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
140-552 |
1.49e-135 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 397.32 E-value: 1.49e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 140 MQENLRLRHRVIKAIWDFLDREGFVQVETPFLTKS-TPEGARDFLVPYRHEpGLFYALPQSPQLFKQMLMVAGLDRYFQI 218
Cdd:pfam00152 18 MQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSaTPEGARDFLVPSRAL-GKFYALPQSPQLYKQLLMVAGFDRVFQI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 219 ARCFRDEDLRADRQPDFTQLDLEMSFVEVEDVLELNERLMAHVFREALGV----------ELPLPFPRLSYEEAMER--- 285
Cdd:pfam00152 97 ARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIakeleggtllDLKKPFPRITYAEAIEKlng 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 286 -------YGSDKPDLRFGLELKevgplfrqsgfrvfqeaesvkalalpkalsrkevaeleevakrhkaqglawarveegg 358
Cdd:pfam00152 177 kdveelgYGSDKPDLRFLLELV---------------------------------------------------------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 359 fsggvakflepvreallqatearpgdtllfvagprkvaatalgavrlraadllgLKREGFRFLWVVDFPLlewdeeeeaw 438
Cdd:pfam00152 199 ------------------------------------------------------IDKNKFNPLWVTDFPA---------- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 439 tyMHHPFTSPHPEDLPllekdpgrVRALAYDLVLNGVEVGGGSIRIHDPRLQARVFRLLGIGEEEQREKFGFFLEALEYG 518
Cdd:pfam00152 215 --EHHPFTMPKDEDDP--------ALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPEEAEEKFGFYLDALKYG 284
|
410 420 430
....*....|....*....|....*....|....
1G51_B 519 APPHGGIAWGLDRLLALMTGSPSIREVIAFPKNK 552
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 ... |
144-553 |
1.21e-111 |
|
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: 334.06 E-value: 1.21e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 144 LRLRHRVIKAIWDFLDREGFVQVETPFLTKSTP-EGARDFLVPYRHePGLFYALPQSPQLFKQMLMVAGLDRYFQIARCF 222
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGgAGARPFLVKYNA-LGLDYYLRISPQLFKKRLMVGGLDRVFEINRNF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 223 RDEDLRADRQPDFTQLDLEMSFVEVEDVLELNERLMAHVFREALGV----------ELPLPFPRLSYEEAMERYGsdkpd 292
Cdd:cd00669 80 RNEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVtavtygfeleDFGLPFPRLTYREALERYG----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 293 lrfglelkevgplfrqsgfrvfqeaesvkalalpkalsrkevaeleevakrhkaqglawarveeggfsggvakflepvre 372
Cdd:cd00669 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 373 allqatearpgdtllfvagprkvaatalgavrlraadllglkregfRFLWVVDFPLLewdeeeeawtyMHHPFTSPHPED 452
Cdd:cd00669 155 ----------------------------------------------QPLFLTDYPAE-----------MHSPLASPHDVN 177
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 453 lpllekdpgRVRALAYDLVLNGVEVGGGSIRIHDPRLQARVFRLLGIGEEEQREKFGFFLEALEYGAPPHGGIAWGLDRL 532
Cdd:cd00669 178 ---------PEIADAFDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINKEAGMEYFEFYLKALEYGLPPHGGLGIGIDRL 248
|
410 420
....*....|....*....|.
1G51_B 533 LALMTGSPSIREVIAFPKNKE 553
Cdd:cd00669 249 IMLMTNSPTIREVIAFPKMRR 269
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
1-549 |
1.57e-68 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 228.15 E-value: 1.57e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 1 MRRTHYAGSLRETHVGEEVVLEGWVNRRRDLGGLIFLDLRDREGLVQLVA--HPASPAYATAERVRPEWVVRAKGLVrlr 78
Cdd:PRK05159 1 MMKRHLTSELTPELDGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVkkKVDEELFETIKKLKRESVVSVTGTV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 79 pEPNPRlATGRVEVELSALEVLAEAKTPPfPVD-AGWrgeeeKEASEELRLKYRYLDLRRRRMQENLRLRHRVIKAIWDF 157
Cdd:PRK05159 78 -KANPK-APGGVEVIPEEIEVLNKAEEPL-PLDiSGK-----VLAELDTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 158 LDREGFVQVETPFLTKSTPE-GARDFLVPYRHEPGLfyaLPQSPQLFKQMLMVAGLDRYFQIARCFRDEDLRADRQ-PDF 235
Cdd:PRK05159 150 LYENGFTEIFTPKIVASGTEgGAELFPIDYFEKEAY---LAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRHlNEY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 236 TQLDLEMSFVE-VEDVLELNERLMAHVFR----------EALGVELPLP---FPRLSYEEAMERYGSDkpdlrfGLELKE 301
Cdd:PRK05159 227 TSIDVEMGFIDdHEDVMDLLENLLRYMYEdvaencekelELLGIELPVPetpIPRITYDEAIEILKSK------GNEISW 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 302 VGPLFRqsgfrvfqEAEsvkalalpKALSRkevaeleevakrhkaqglaWARVEEGGFsggvakflepvreallqatear 381
Cdd:PRK05159 301 GDDLDT--------EGE--------RLLGE-------------------YVKEEYGSD---------------------- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 382 pgdtllfvagprkvaatalgavrlraadllglkregfrFLWVVDFPllewdeeEEAwtymhHPF-TSPHPEDlPLLEKdp 460
Cdd:PRK05159 324 --------------------------------------FYFITDYP-------SEK-----RPFyTMPDEDD-PEISK-- 350
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 461 grvralAYDLVLNGVEVGGGSIRIHDPRLQARVFRLLGigeeEQREKFGFFLEALEYGAPPHGGIAWGLDRLLALMTGSP 540
Cdd:PRK05159 351 ------SFDLLFRGLEITSGGQRIHRYDMLVESIKEKG----LNPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLE 420
|
....*....
1G51_B 541 SIREVIAFP 549
Cdd:PRK05159 421 NIREAVLFP 429
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
3-549 |
3.20e-59 |
|
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: 203.36 E-value: 3.20e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 3 RTHYAGSLRETHVGEEVVLEGWVNRRRDLGGLIFLDLRDREGLVQLVAHPAS-PAYATAERVRPEWVVRAKGLVRlrpeP 81
Cdd:COG0017 1 KRTYIKDLLPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKlENFEEAKKLTTESSVEVTGTVV----E 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 82 NPRlATGRVEVELSALEVLAEAKTPpFPVDAGWRGEEEKEASEELRLKyryldlrRRRMQENLRLRHRVIKAIWDFLDRE 161
Cdd:COG0017 77 SPR-APQGVELQAEEIEVLGEADEP-YPLQPKRHSLEFLLDNRHLRLR-------TNRFGAIFRIRSELARAIREFFQER 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 162 GFVQVETPFLTKSTPEGARD-FLVPYRHEPGlfYaLPQSPQLFKQMlMVAGLDRYFQIARCFRDEDLRADRQ-PDFTQLD 239
Cdd:COG0017 148 GFVEVHTPIITASATEGGGElFPVDYFGKEA--Y-LTQSGQLYKEA-LAMALEKVYTFGPTFRAEKSNTRRHlAEFWMIE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 240 LEMSFVEVEDVLELNERLMAHVFR----------EALGVE-------LPLPFPRLSYEEAMERYGSDKPDLRFGLELkev 302
Cdd:COG0017 224 PEMAFADLEDVMDLAEEMLKYIIKyvlencpeelEFLGRDverlekvPESPFPRITYTEAIEILKKSGEKVEWGDDL--- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 303 gplfrQSgfrvfqEAEsvKALAlpkalsrkevaelEEVAKRHkaqglawarveeggfsggvakflepvreallqatearp 382
Cdd:COG0017 301 -----GT------EHE--RYLG-------------EEFFKKP-------------------------------------- 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 383 gdtlLFVAG-PRKVAAtalgavrlraadllglkregFrflwvvdfpllewdeeeeawtYMHhpftsPHPEdlpllekDPG 461
Cdd:COG0017 317 ----VFVTDyPKEIKA--------------------F---------------------YMK-----PNPD-------DPK 339
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 462 RVRalAYDLVLNGV-EVGGGSIRIHDP-RLQARvFRLLGIGEEEqrekFGFFLEALEYGAPPHGGIAWGLDRLLALMTGS 539
Cdd:COG0017 340 TVA--AFDLLAPGIgEIIGGSQREHRYdVLVER-IKEKGLDPED----YEWYLDLRRYGSVPHAGFGLGLERLVMWLTGL 412
|
570
....*....|
1G51_B 540 PSIREVIAFP 549
Cdd:COG0017 413 ENIREVIPFP 422
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
3-111 |
7.47e-52 |
|
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: 173.86 E-value: 7.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 3 RTHYAGSLRETHVGEEVVLEGWVNRRRDLGGLIFLDLRDREGLVQLVAHPAS-PAYATAERVRPEWVVRAKGLVRLRPE- 80
Cdd:cd04317 1 RTHYCGELRESHVGQEVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPEEaPEFELAEKLRNESVIQVTGKVRARPEg 80
|
90 100 110
....*....|....*....|....*....|..
1G51_B 81 -PNPRLATGRVEVELSALEVLAEAKTPPFPVD 111
Cdd:cd04317 81 tVNPKLPTGEIEVVASELEVLNKAKTLPFEID 112
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
144-550 |
4.28e-35 |
|
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: 134.62 E-value: 4.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 144 LRLRHRVIKAIWDFLDREGFVQVETPFLTKSTPE-GARDFLVPYRHEPGLfyaLPQSPQLFKQMlMVAGLDRYFQIARCF 222
Cdd:cd00776 24 FRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEgGAELFKVSYFGKPAY---LAQSPQLYKEM-LIAALERVYEIGPVF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 223 RDEDLRADRQ-PDFTQLDLEMSFVE-VEDVLELNERLMAHVFR-------------EALGVELPL---PFPRLSYEEAME 284
Cdd:cd00776 100 RAEKSNTRRHlSEFWMLEAEMAFIEdYNEVMDLIEELIKYIFKrvlercakelelvNQLNRELLKplePFPRITYDEAIE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 285 RygsdkpdlrfgleLKEVGPlfrqsgfrvfqeaesvkalalpkalsRKEVAELEEVAKRHKaqglawarveeggfsggva 364
Cdd:cd00776 180 L-------------LREKGV--------------------------EEEVKWGEDLSTEHE------------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 365 kflepvreallqatearpgdtllfvagpRKVAATALGavrlraadllglkregfRFLWVVDFPLLEwdeeeeawtymhHP 444
Cdd:cd00776 202 ----------------------------RLLGEIVKG-----------------DPVFVTDYPKEI------------KP 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 445 F-TSPHPEDLPLlekdpgrvrALAYDLVLNGV-EVGGGSIRIHDP-RLQARvFRLLGIgeeeQREKFGFFLEALEYGAPP 521
Cdd:cd00776 225 FyMKPDDDNPET---------VESFDLLMPGVgEIVGGSQRIHDYdELEER-IKEHGL----DPESFEWYLDLRKYGMPP 290
|
410 420
....*....|....*....|....*....
1G51_B 522 HGGIAWGLDRLLALMTGSPSIREVIAFPK 550
Cdd:cd00776 291 HGGFGLGLERLVMWLLGLDNIREAILFPR 319
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
2-549 |
9.53e-29 |
|
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: 119.75 E-value: 9.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 2 RRTHYAGSLRETH--------VGEEVVLEGWVNRRRDLGGLIFLDLRDREGLVQLVAHPAS---PAYATAERV------- 63
Cdd:COG1190 34 PRTHTAAEIREKYdeleaeeeTGDEVSVAGRIMAKRDMGKASFADLQDGSGRIQLYLRRDElgeEAYELFKLLdlgdivg 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 64 ---------RPEWVVRAKGLV----RLRPEPNPRlaTGRVEVELSA------LEVLAEAKtppfpvdagwrgeeekease 124
Cdd:COG1190 114 vegtvfrtkTGELSVKVEELTllskSLRPLPEKF--HGLTDPETRYrqryvdLIVNPEVR-------------------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 125 elrlkyryldlrrrrmqENLRLRHRVIKAIWDFLDREGFVQVETPFLTkSTPEGA--RDFlVPYrHEpglfyALPQ---- 198
Cdd:COG1190 172 -----------------ETFRKRSKIIRAIRRFLDERGFLEVETPMLQ-PIAGGAaaRPF-ITH-HN-----ALDMdlyl 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 199 --SPQLFKQMLMVAGLDRYFQIARCFRDEDLRADRQPDFTQLDLEMSFVEVEDVLELNERLMAHVFREALG--------- 267
Cdd:COG1190 227 riAPELYLKRLIVGGFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGttkvtyqgq 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 268 -VELPLPFPRLSYEEAMERYGsdkpdlrfglelkevgplfrqsGFRVFQEaesvkalalpkalsrKEVAELEEVAKRHka 346
Cdd:COG1190 307 eIDLSPPWRRITMVEAIKEAT----------------------GIDVTPL---------------TDDEELRALAKEL-- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 347 qGLAWarveEGGFSGG--VAKFLEP-VREALLQATearpgdtllfvagprkvaatalgavrlraadllglkregfrflWV 423
Cdd:COG1190 348 -GIEV----DPGWGRGklIDELFEElVEPKLIQPT-------------------------------------------FV 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 424 VDFPLlewdeeeeawtymhhpFTSP----HPEDlpllekdPGRV-RalaYDLVLNGVEVGGGSIRIHDPRLQARVFrllg 498
Cdd:COG1190 380 TDYPV----------------EVSPlakrHRDD-------PGLTeR---FELFIAGREIANAFSELNDPIDQRERF---- 429
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
1G51_B 499 igEEEQREKFGF----------FLEALEYGAPPHGGIAWGLDRLLALMTGSPSIREVIAFP 549
Cdd:COG1190 430 --EEQLELKAAGddeampmdedFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 488
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
142-549 |
1.73e-28 |
|
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: 116.14 E-value: 1.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 142 ENLRLRHRVIKAIWDFLDREGFVQVETPFLtKSTPEG--ARDFlVPYRHEPGLFYALPQSPQLFKQMLMVAGLDRYFQIA 219
Cdd:cd00775 6 QTFIVRSKIISYIRKFLDDRGFLEVETPML-QPIAGGaaARPF-ITHHNALDMDLYLRIAPELYLKRLIVGGFERVYEIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 220 RCFRDEDLRADRQPDFTQLDLEMSFVEVEDVLELNERLMAHVFREALG--------VELPL--PFPRLSYEEAMERY-GS 288
Cdd:cd00775 84 RNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGktkieyggKELDFtpPFKRVTMVDALKEKtGI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 289 DKPDLrfglelkevgplfrqsgfRVFQEAESVKALALPKAlsrkevaeLEEVAKRHKAQGLAwarveeggfsggvAKFLE 368
Cdd:cd00775 164 DFPEL------------------DLEQPEELAKLLAKLIK--------EKIEKPRTLGKLLD-------------KLFEE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 369 PVREALLQATearpgdtllfvagprkvaatalgavrlraadllglkregfrflWVVDFPLlewdeeeeawtyMHHPFTSP 448
Cdd:cd00775 205 FVEPTLIQPT-------------------------------------------FIIDHPV------------EISPLAKR 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 449 HPEDLPLLEKdpgrvralaYDLVLNGVEVGGGSIRIHDPRLQARVF----RLLGIGEEEQREKFGFFLEALEYGAPPHGG 524
Cdd:cd00775 230 HRSNPGLTER---------FELFICGKEIANAYTELNDPFDQRERFeeqaKQKEAGDDEAMMMDEDFVTALEYGMPPTGG 300
|
410 420
....*....|....*....|....*
1G51_B 525 IAWGLDRLLALMTGSPSIREVIAFP 549
Cdd:cd00775 301 LGIGIDRLVMLLTDSNSIRDVILFP 325
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
8-562 |
1.13e-27 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 117.11 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 8 GSLRETHVGEEVVLEGWVNRRRDLGGLIFLDLRDREGLVQLVAHpASPAYATAERVR------PEWVVRAKGLVRLRPEP 81
Cdd:PLN02850 73 SDLGEELAGSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQCVVF-VSEVTVSKGMVKyakqlsRESVVDVEGVVSVPKKP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 82 nPRLATGRVEVELSALEVLAEAKTP-PFPVDAGWRGEEEKEaseelrlKYRYLDLRRRRMQENLRLRHRVI-------KA 153
Cdd:PLN02850 152 -VKGTTQQVEIQVRKIYCVSKALATlPFNVEDAARSESEIE-------KALQTGEQLVRVGQDTRLNNRVLdlrtpanQA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 154 IW-----------DFLDREGFVQVETPFLTKSTPEGARD-FLVPYRHEPGlfyALPQSPQLFKQMLMVAGLDRYFQIARC 221
Cdd:PLN02850 224 IFriqsqvcnlfrEFLLSKGFVEIHTPKLIAGASEGGSAvFRLDYKGQPA---CLAQSPQLHKQMAICGDFRRVFEIGPV 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 222 FRDEDLRADRQ-PDFTQLDLEMSFVE-VEDVLELNERLMAHVFrealgvelplpfprlsyeeamerygsDKPDLRFGLEL 299
Cdd:PLN02850 301 FRAEDSFTHRHlCEFTGLDLEMEIKEhYSEVLDVVDELFVAIF--------------------------DGLNERCKKEL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 300 KEVGplfRQSGFrvfqeaESVKalALPKALSrkevaeleevakrhkaqgLAWarvEEGgfsggvakfLEPVREAllqATE 379
Cdd:PLN02850 355 EAIR---EQYPF------EPLK--YLPKTLR------------------LTF---AEG---------IQMLKEA---GVE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 380 ARP-GDtlLFVAGPRKvaataLGAvrlraadlLGLKREGFRFLWVVDFPLlewdeeeeawtyMHHPF-TSPHPEDlPLLE 457
Cdd:PLN02850 391 VDPlGD--LNTESERK-----LGQ--------LVKEKYGTDFYILHRYPL------------AVRPFyTMPCPDD-PKYS 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 458 KdpgrvralAYDLVLNGVEVGGGSIRIHDPRLQARVFRLLGIGEEEQREkfgfFLEALEYGAPPHGGIAWGLDRLLALMT 537
Cdd:PLN02850 443 N--------SFDVFIRGEEIISGAQRVHDPELLEKRAEECGIDVKTIST----YIDSFRYGAPPHGGFGVGLERVVMLFC 510
|
570 580
....*....|....*....|....*
1G51_B 538 GSPSIREVIAFPknkegKDPLTGAP 562
Cdd:PLN02850 511 GLNNIRKTSLFP-----RDPQRLAP 530
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
18-102 |
1.38e-27 |
|
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: 106.11 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 18 EVVLEGWVNRRRDLGGLIFLDLRDREGLVQLVAHP--ASPAYATAERVRPEWVVRAKGLVRLRPEPNprLATGRVEVELS 95
Cdd:cd04100 1 EVTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKeeLGEFFEEAEKLRTESVVGVTGTVVKRPEGN--LATGEIELQAE 78
|
....*..
1G51_B 96 ALEVLAE 102
Cdd:cd04100 79 ELEVLSK 85
|
|
| GAD |
pfam02938 |
GAD domain; This domain is found in some members of the GatB and aspartyl tRNA synthetases. |
314-400 |
2.61e-27 |
|
GAD domain; This domain is found in some members of the GatB and aspartyl tRNA synthetases.
Pssm-ID: 397199 [Multi-domain] Cd Length: 94 Bit Score: 105.42 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 314 FQEA----ESVKALALPKA--LSRKEVAELEEVAKRHKAQGLAWARVEEGGFSGGVAKFL-EPVREALLQATEARPGDTL 386
Cdd:pfam02938 1 FSEAlksgGSVKALRVPGAagLSRKEIDELERFAKEYGAKGLAWIKVEGGGHTGPIAKFLtEEEVEKLLEAVGAEDGDAL 80
|
90
....*....|....
1G51_B 387 LFVAGPRKVAATAL 400
Cdd:pfam02938 81 LFVADKKKTVNKAL 94
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
142-549 |
2.17e-24 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 106.71 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 142 ENLRLRHRVIKAIWDFLDREGFVQVETPFLtKSTPEG--ARDFlVPYrHEpglfyALPQ------SPQLFKQMLMVAGLD 213
Cdd:PRK00484 170 ETFRKRSKIISAIRRFLDNRGFLEVETPML-QPIAGGaaARPF-ITH-HN-----ALDIdlylriAPELYLKRLIVGGFE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 214 RYFQIARCFRDEDLRADRQPDFTQLDLEMSFVEVEDVLELNERLMAHVFREALG----------VELPLPFPRLSYEEAm 283
Cdd:PRK00484 242 RVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGttkvtyqgteIDFGPPFKRLTMVDA- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 284 erygsdkpdlrfgleLKEvgplfrqsgfrvfqeaesvkalALPKALSRKEVAELEEVAKRHKAQglawarvEEGGFSGG- 362
Cdd:PRK00484 321 ---------------IKE----------------------YTGVDFDDMTDEEARALAKELGIE-------VEKSWGLGk 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 363 -VAKFLEP-VREALLQATearpgdtllfvagprkvaatalgavrlraadllglkregfrFlwVVDFPLlewdeeeEAwty 440
Cdd:PRK00484 357 lINELFEEfVEPKLIQPT-----------------------------------------F--ITDYPV-------EI--- 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 441 mhHPFTSPHPEDLPLLEKdpgrvralaYDLVLNGVEVGGGSIRIHDPRLQARVFrllgigEEEQREK-------FGF--- 510
Cdd:PRK00484 384 --SPLAKRHREDPGLTER---------FELFIGGREIANAFSELNDPIDQRERF------EAQVEAKeagddeaMFMded 446
|
410 420 430
....*....|....*....|....*....|....*....
1G51_B 511 FLEALEYGAPPHGGIAWGLDRLLALMTGSPSIREVIAFP 549
Cdd:PRK00484 447 FLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
2-549 |
7.67e-24 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 105.88 E-value: 7.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 2 RRTHYAGSLRETHVGEEVVleGWVNRRRDLGGLIFLDLRDREGLVQLVAHpaspayaTAERVRPEWVVRAKGLVR----L 77
Cdd:PTZ00385 95 RYGYLASGDRAAQATVRVA--GRVTSVRDIGKIIFVTIRSNGNELQVVGQ-------VGEHFTREDLKKLKVSLRvgdiI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 78 RPEPNP-RLATGRVEVELSALEVLAEAKTPPFPVDAGWRGEEEKEASEELRLKYRYLDLRRRRMQENLRLRHRVIKAIWD 156
Cdd:PTZ00385 166 GADGVPcRMQRGELSVAASRMLILSPYVCTDQVVCPNLRGFTVLQDNDVKYRYRFTDMMTNPCVIETIKKRHVMLQALRD 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 157 FLDREGFVQVETPFL-TKSTPEGARDFLVPYR-HEPGLFyaLPQSPQLFKQMLMVAGLDRYFQIARCFRDEDLRADRQPD 234
Cdd:PTZ00385 246 YFNERNFVEVETPVLhTVASGANAKSFVTHHNaNAMDLF--LRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 235 FTQLDLEMSFVEVEDVLELNERLMAHVFREALGVELPLPFPRLSYEEAMErygsdkpdlrfglelKEVGPLFRQsgFRVF 314
Cdd:PTZ00385 324 FTSCEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTVVQIYPENAHGNPVT---------------VDLGKPFRR--VSVY 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 315 QEAESVKALALP---KALSRKEVAELEEVAKRHKAQglawarveeggfsggvakfLEPVReallqaTEARPGDTLL-FVA 390
Cdd:PTZ00385 387 DEIQRMSGVEFPppnELNTPKGIAYMSVVMLRYNIP-------------------LPPVR------TAAKMFEKLIdFFI 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 391 GPRKVAATalgavrlraadllglkregfrflWVVDFPLlewdeeeeawtymhhpFTSPhpedlplLEKDPGRVRALA--Y 468
Cdd:PTZ00385 442 TDRVVEPT-----------------------FVMDHPL----------------FMSP-------LAKEQVSRPGLAerF 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 469 DLVLNGVEVGGGSIRIHDPRLQARVFRLLGI----GEEEQREKFGFFLEALEYGAPPHGGIAWGLDRLLALMTGSPSIRE 544
Cdd:PTZ00385 476 ELFVNGIEYCNAYSELNDPHEQYHRFQQQLVdrqgGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRD 555
|
....*
1G51_B 545 VIAFP 549
Cdd:PTZ00385 556 GIIFP 560
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
1-549 |
1.78e-23 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 103.26 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 1 MRRTHYAGSLRETHVGEEVVLEGWVNRRRDLGGLIFLDLRDREGLVQL--VAHPASPAYATAERVRPEWVVRAKGLVRLR 78
Cdd:PRK03932 1 MMRVSIKDILKGKYVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLqvVKDNGEEYFEEIKKLTTGSSVIVTGTVVES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 79 PEpnprlATGRVEVELSALEVLAEAkTPPFPVDAGWRGEEEKEASEELRLKYRYldlrrrrMQENLRLRHRVIKAIWDFL 158
Cdd:PRK03932 81 PR-----AGQGYELQATKIEVIGED-PEDYPIQKKRHSIEFLREIAHLRPRTNK-------FGAVMRIRNTLAQAIHEFF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 159 DREGFVQVETPFLTKSTPEGARD-FLVPYRHepgLFYA---------LPQSPQLFKQMLMVAgLDRYFQIARCFRDEDLR 228
Cdd:PRK03932 148 NENGFVWVDTPIITASDCEGAGElFRVTTLD---LDFSkdffgkeayLTVSGQLYAEAYAMA-LGKVYTFGPTFRAENSN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 229 ADRQ-PDFTQLDLEMSFVEVEDVLELNERLMAHVFREAL------------GVELPL----------PFPRLSYEEAMEr 285
Cdd:PRK03932 224 TRRHlAEFWMIEPEMAFADLEDNMDLAEEMLKYVVKYVLencpddleflnrRVDKGDierlenfiesPFPRITYTEAIE- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 286 ygsdkpdlrfglELKEVGPLFRqsgFRV-----FQeAESVKALAlpkalsrkevaelEEVAKRhkaqglawarveeggfs 360
Cdd:PRK03932 303 ------------ILQKSGKKFE---FPVewgddLG-SEHERYLA-------------EEHFKK----------------- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 361 ggvakflePVreallqatearpgdtllFVAG-PRKVAAtalgavrlraadllglkregFrflwvvdfpllewdeeeeawt 439
Cdd:PRK03932 337 --------PV-----------------FVTNyPKDIKA--------------------F--------------------- 350
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 440 YMHhpftsphpedlplleKDPGRVRALAYDLVLNGV-EVGGGSIRIHDP-RLQARVfRLLGIGEEEqrekFGFFLEALEY 517
Cdd:PRK03932 351 YMR---------------LNPDGKTVAAMDLLAPGIgEIIGGSQREERLdVLEARI-KELGLNKED----YWWYLDLRRY 410
|
570 580 590
....*....|....*....|....*....|..
1G51_B 518 GAPPHGGIAWGLDRLLALMTGSPSIREVIAFP 549
Cdd:PRK03932 411 GSVPHSGFGLGFERLVAYITGLDNIRDVIPFP 442
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
145-549 |
6.17e-20 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 93.52 E-value: 6.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 145 RLRHRVIKAIWDFLDREGFVQVETPFLtKSTPEGA--RDFlVPYRHEPGLFYALPQSPQLFKQMLMVAGLDRYFQIARCF 222
Cdd:PLN02502 230 RTRAKIISYIRRFLDDRGFLEVETPML-NMIAGGAaaRPF-VTHHNDLNMDLYLRIATELHLKRLVVGGFERVYEIGRQF 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 223 RDEDLRADRQPDFTQLDLEMSFVEVEDVLELNERLMAHVFREALG--------VELPL--PFPRLSYEEamerygsdkpd 292
Cdd:PLN02502 308 RNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGsykikyhgIEIDFtpPFRRISMIS----------- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 293 lrfglELKEVGPLfrqsgfRVFQEAESVKALALPKALSRKEVAELEevakrhKAQglawarveeggfsgGVAKFLEPVRE 372
Cdd:PLN02502 377 -----LVEEATGI------DFPADLKSDEANAYLIAACEKFDVKCP------PPQ--------------TTGRLLNELFE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 373 ALLQATEARPGdtllfvagprkvaatalgavrlraadllglkregfrflWVVDFPLLewdeeeeawtyMhHPFTSPHPED 452
Cdd:PLN02502 426 EFLEETLVQPT--------------------------------------FVLDHPVE-----------M-SPLAKPHRSK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 453 LPLLEKdpgrvralaYDLVLNGVEVGGGSIRIHDP-----RLQARVfRLLGIGEEEQREKFGFFLEALEYGAPPHGGIAW 527
Cdd:PLN02502 456 PGLTER---------FELFINGRELANAFSELTDPvdqreRFEEQV-KQHNAGDDEAMALDEDFCTALEYGLPPTGGWGL 525
|
410 420
....*....|....*....|..
1G51_B 528 GLDRLLALMTGSPSIREVIAFP 549
Cdd:PLN02502 526 GIDRLVMLLTDSASIRDVIAFP 547
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
5-111 |
1.40e-19 |
|
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: 84.29 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 5 HYAGSLRETHVGEEVVLEGWVNRRRDLGGLIFLDLRDREGLVQLVA---HPASPAYATAERVRPEWVVRAKGLVrlrpEP 81
Cdd:cd04316 1 HYSAEITPELDGEEVTVAGWVHEIRDLGGIKFVILRDREGIVQVTApkkKVDKELFKTVRKLSRESVISVTGTV----KA 76
|
90 100 110
....*....|....*....|....*....|
1G51_B 82 NPRLATGrVEVELSALEVLAEAKTPPfPVD 111
Cdd:cd04316 77 EPKAPNG-VEIIPEEIEVLSEAKTPL-PLD 104
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
2-549 |
1.19e-18 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 90.41 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 2 RRTHYAGSLRETHVGEEVVLEGWVNRRRDLGGLIFLDLRDREGLVQLVA-----HPASPAY------------ATAERVR 64
Cdd:PRK02983 637 PPTHTVAEALDAPTGEEVSVSGRVLRIRDYGGVLFADLRDWSGELQVLLdasrlEQGSLADfraavdlgdlveVTGTMGT 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 65 P----------EWVVRAKGLvrlRPEPNPRLAtgrveveLSALEVLAEAKTPPFPVDAGWRgeeekeaseelrlkyryld 134
Cdd:PRK02983 717 SrngtlsllvtSWRLAGKCL---RPLPDKWKG-------LTDPEARVRQRYLDLAVNPEAR------------------- 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 135 lrrrrmqENLRLRHRVIKAIWDFLDREGFVQVETPFLtkSTPEG---ARDFLVPYR-HEPGLFyaLPQSPQLFKQMLMVA 210
Cdd:PRK02983 768 -------DLLRARSAVVRAVRETLVARGFLEVETPIL--QQVHGganARPFVTHINaYDMDLY--LRIAPELYLKRLCVG 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 211 GLDRYFQIARCFRDEDLRADRQPDFTQLDLEMSFVEVEDVLELNERLMAHVFREALGVELplpFPRLSYEEAMERYGSDK 290
Cdd:PRK02983 837 GVERVFELGRNFRNEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGAPV---VMRPDGDGVLEPVDISG 913
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 291 PdlrfglelkevgplfrqsgFRVFQEAESVKAlALPKALS-RKEVAELEEVAKRHkaqGLAWARVEEGGfsggvAKFLEp 369
Cdd:PRK02983 914 P-------------------WPVVTVHDAVSE-ALGEEIDpDTPLAELRKLCDAA---GIPYRTDWDAG-----AVVLE- 964
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 370 VREALLQATEARPgdtllfvagprkvaatalgavrlraadllglkregfrfLWVVDFPLlewdeeEEAwtymhhPFTSPH 449
Cdd:PRK02983 965 LYEHLVEDRTTFP--------------------------------------TFYTDFPT------SVS------PLTRPH 994
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 450 PEDLPLLEKdpgrvralaYDLVLNGVEVGGGSIRIHDP-----RLQARVFRLLGiGEEEQREKFGFFLEALEYGAPPHGG 524
Cdd:PRK02983 995 RSDPGLAER---------WDLVAWGVELGTAYSELTDPveqrrRLTEQSLLAAG-GDPEAMELDEDFLQALEYAMPPTGG 1064
|
570 580
....*....|....*....|....*
1G51_B 525 IAWGLDRLLALMTGSpSIREVIAFP 549
Cdd:PRK02983 1065 LGMGVDRLVMLLTGR-SIRETLPFP 1088
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
18-555 |
4.99e-18 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 87.42 E-value: 4.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 18 EVVLEGWVNRRRDLGGLIFLDLRDREGLVQL-VAHPASPAYATAERVRpEW----VVRAKGLVRlrpepnpRLATGRVEV 92
Cdd:PRK12445 67 EVSVAGRMMTRRIMGKASFVTLQDVGGRIQLyVARDSLPEGVYNDQFK-KWdlgdIIGARGTLF-------KTQTGELSI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 93 ELSALEVLAEAKTPPFPVDAGWRGEEEKEASEELRLkyryldLRRRRMQENLRLRHRVIKAIWDFLDREGFVQVETPFLt 172
Cdd:PRK12445 139 HCTELRLLTKALRPLPDKFHGLQDQEVRYRQRYLDL------IANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMM- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 173 KSTPEGA--RDFLVpYRHEPGLFYALPQSPQLFKQMLMVAGLDRYFQIARCFRDEDLRADRQPDFTQLDLEMSFVEVEDV 250
Cdd:PRK12445 212 QVIPGGAsaRPFIT-HHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 251 LELNERLMAHVFREALGvelplpfprlsyeeamerygsdKPDLRFGLELKEVGPLFRQSGFRvfqeaESVKalalpKALS 330
Cdd:PRK12445 291 IELTESLFRTLAQEVLG----------------------TTKVTYGEHVFDFGKPFEKLTMR-----EAIK-----KYRP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 331 RKEVAELEEV-AKRHKAQGLAWARVEEGGFSGGVAKFLEPVREA-LLQATearpgdtlLFVAGPRKVAATAlgavrlRAA 408
Cdd:PRK12445 339 ETDMADLDNFdAAKALAESIGITVEKSWGLGRIVTEIFDEVAEAhLIQPT--------FITEYPAEVSPLA------RRN 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 409 DLlglkregfrflwvvdfpllewdeeeeawtymhhpftSPHPEDlpllekdpgrvralAYDLVLNGVEVGGGSIRIHDPR 488
Cdd:PRK12445 405 DV------------------------------------NPEITD--------------RFEFFIGGREIGNGFSELNDAE 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1G51_B 489 LQARVFR----LLGIGEEEQREKFGFFLEALEYGAPPHGGIAWGLDRLLALMTGSPSIREVIAFPKNKEGK 555
Cdd:PRK12445 435 DQAERFQeqvnAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFPAMRPQK 505
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
11-557 |
3.77e-17 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 84.66 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 11 RETHVGEEVVLEGWVNRRRDLGGLIFLDLRDREGLVQLVAhpaspayATAERVRPEWV-----------VRAKGLVRLRP 79
Cdd:PTZ00401 73 KPELVDKTVLIRARVSTTRKKGKMAFMVLRDGSDSVQAMA-------AVEGDVPKEMIdfigqiptesiVDVEATVCKVE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 80 EPNPRLATGRVEVELSALEVLAEA-KTPPFPVDAGWRGEEEKEASEEL--RLKYRYLDLRRRRMQENLRLRHRVIKAIWD 156
Cdd:PTZ00401 146 QPITSTSHSDIELKVKKIHTVTESlRTLPFTLEDASRKESDEGAKVNFdtRLNSRWMDLRTPASGAIFRLQSRVCQYFRQ 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 157 FLDREGFVQVETPFLTKSTPEG-ARDFLVPYRHEpglFYALPQSPQLFKQMLMVAGLDRYFQIARCFRDEDLRADRQ-PD 234
Cdd:PTZ00401 226 FLIDSDFCEIHSPKIINAPSEGgANVFKLEYFNR---FAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHlTE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 235 FTQLDLEMSFVE-VEDVLELNERLMAHVF-------REALGVELPLPFPRLSYEEAMERygsdkpdlrfgleLKEVGplf 306
Cdd:PTZ00401 303 FVGLDVEMRINEhYYEVLDLAESLFNYIFerlathtKELKAVCQQYPFEPLVWKLTPER-------------MKELG--- 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 307 rqsgfrVFQEAESVKALALPKALSRKEVAELEEVAKRHkaqglawarveeggfsggVAKFLEPVREALLQATEarpgdtl 386
Cdd:PTZ00401 367 ------VGVISEGVEPTDKYQARVHNMDSRMLRINYMH------------------CIELLNTVLEEKMAPTD------- 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 387 lfvagprkvaatalgAVRLRAADLLG---LKREGFRFLWVVDFPllewdeeeeawtYMHHPF-TSPHPEDLPLLEkdpgr 462
Cdd:PTZ00401 416 ---------------DINTTNEKLLGklvKERYGTDFFISDRFP------------SSARPFyTMECKDDERFTN----- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 463 vralAYDLVLNGVEVGGGSIRIHDPRLQARVFRLLGIGEEEQREkfgfFLEALEYGAPPHGGIAWGLDRLLALMTGSPSI 542
Cdd:PTZ00401 464 ----SYDMFIRGEEISSGAQRIHDPDLLLARAKMLNVDLTPIKE----YVDSFRLGAWPHGGFGVGLERVVMLYLGLSNV 535
|
570
....*....|....*
1G51_B 543 REVIAFPKNKEGKDP 557
Cdd:PTZ00401 536 RLASLFPRDPQRTTP 550
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
144-303 |
9.25e-16 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 78.52 E-value: 9.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 144 LRLRHRVIKAIWDFLDREGFVQVETPFLTKST--------PEGARDFLVPYrhePGLFYALPQSPQLFKQmLMVAGLDRY 215
Cdd:PRK06462 30 LKVQSSILRYTREFLDGRGFVEVLPPIISPSTdplmglgsDLPVKQISIDF---YGVEYYLADSMILHKQ-LALRMLGKI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 216 FQIARCFRDEDLRADRQP---DFTQLDLEMSFVEVEDVLELNERLMAHVFREAL----------GVELP---LPFPRLSY 279
Cdd:PRK06462 106 FYLSPNFRLEPVDKDTGRhlyEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLeehedeleffGRDLPhlkRPFKRITH 185
|
170 180
....*....|....*....|....
1G51_B 280 EEAMERYGSDKPDlrfGLELKEVG 303
Cdd:PRK06462 186 KEAVEILNEEGCR---GIDLEELG 206
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
146-287 |
1.40e-14 |
|
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: 72.92 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 146 LRHRVIKAIWDFLDREGFVQVETPFLTKSTPEGARDFLVPYRH----EPGLFYALPQSPQLFKQMLMVAGL----DRYFQ 217
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKDLLpvgaENEEDLYLRPTLEPGLVRLFVSHIrklpLRLAE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1G51_B 218 IARCFRDEDLRAD--RQPDFTQLDLEMSFVEVEDVLELNE--RLMAHVFReALGVELPlPFPRLSYEEAMERYG 287
Cdd:cd00768 81 IGPAFRNEGGRRGlrRVREFTQLEGEVFGEDGEEASEFEEliELTEELLR-ALGIKLD-IVFVEKTPGEFSPGG 152
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
147-549 |
2.89e-14 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 75.82 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 147 RHRVIKAIWDFLDREGFVQVETPFLT-KSTPEGARDFLVpYRHEPGLFYALPQSPQLFKQMLMVAGLDRYFQIARCFRDE 225
Cdd:PTZ00417 256 RTKIINYLRNFLNDRGFIEVETPTMNlVAGGANARPFIT-HHNDLDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFRNE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 226 DLRADRQPDFTQLDLEMSFVEVEDVLELNERLMAHVFREALGvelplpfprlSYEEAmerYGSDKPDlRFGLELKEVGPL 305
Cdd:PTZ00417 335 GIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFG----------TYKIL---YNKDGPE-KDPIEIDFTPPY 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 306 FRQSgfrVFQEAESVKALALPKALSRKE-VAELEEVAKRHKAqglawarveEGGFSGGVAKFLEPVREALLQAtearpgd 384
Cdd:PTZ00417 401 PKVS---IVEELEKLTNTKLEQPFDSPEtINKMINLIKENKI---------EMPNPPTAAKLLDQLASHFIEN------- 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 385 tllfvagprkvaatalgavrlraadllglkregfrflwvvdfpllewdeeeeawTYMHHP-FTSPHPEDLPLLEK----D 459
Cdd:PTZ00417 462 ------------------------------------------------------KYPNKPfFIIEHPQIMSPLAKyhrsK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 460 PGRVRALayDLVLNGVEVGGGSIRIHDPRLQARVFRLlgigEEEQREK-----FGF---FLEALEYGAPPHGGIAWGLDR 531
Cdd:PTZ00417 488 PGLTERL--EMFICGKEVLNAYTELNDPFKQKECFSA----QQKDREKgdaeaFQFdaaFCTSLEYGLPPTGGLGLGIDR 561
|
410
....*....|....*...
1G51_B 532 LLALMTGSPSIREVIAFP 549
Cdd:PTZ00417 562 ITMFLTNKNCIKDVILFP 579
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
19-100 |
3.12e-14 |
|
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: 67.65 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 19 VVLEGWV-NRRRDLGGLIFLDLRDREGLVQLVAHPASpAYATAERVRPEWVVRAKGLVRLRPEpnprlatGRVEVELSAL 97
Cdd:pfam01336 1 VTVAGRVtSIRRSGGKLLFLTLRDGTGSIQVVVFKEE-AEKLAKKLKEGDVVRVTGKVKKRKG-------GELELVVEEI 72
|
...
1G51_B 98 EVL 100
Cdd:pfam01336 73 ELL 75
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
157-547 |
4.05e-13 |
|
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: 70.27 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 157 FLDREGFVQVETPFLTKST-PEG-----ARDFLVPYRHEPGLFyaLPQSPQLFKQMLMVAGLDRYFQIARCFRDEDLRAD 230
Cdd:TIGR00462 1 FFAERGVLEVETPLLSPAPvTDPhldafATEFVGPDGQGRPLY--LQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 231 RQPDFTQL-------DLE--MSfvEVEDVLelnerlmahvfREALGvELPLPFPRLSYEEAMERYGSdkpdlrfglelke 301
Cdd:TIGR00462 79 HNPEFTMLewyrpgfDYHdlMD--EVEALL-----------QELLG-DPFAPAERLSYQEAFLRYAG------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 302 VGPLfrqsgfrvfqeaesvkalalpkalsRKEVAELEEVAKRHkaqglawarveeggfsgGVAKFLEPVREALLQatear 381
Cdd:TIGR00462 132 IDPL-------------------------TASLAELQAAAAAH-----------------GIRASEEDDRDDLLD----- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 382 pgdtLLFVagpRKVAaTALGAVRLraadllglkregfrfLWVVDFPllewdEEEEAwtymhhpftsphpedLPLLEKDPG 461
Cdd:TIGR00462 165 ----LLFS---EKVE-PHLGFGRP---------------TFLYDYP-----ASQAA---------------LARISPDDP 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 462 RVrALAYDLVLNGVEVGGGSIRIHDPRLQARVFRLlgigEEEQREKFG--------FFLEALEYGAPPHGGIAWGLDRLL 533
Cdd:TIGR00462 202 RV-AERFELYIKGLELANGFHELTDAAEQRRRFEA----DNALRKALGlprypldeRFLAALEAGLPECSGVALGVDRLL 276
|
410
....*....|....
1G51_B 534 ALMTGSPSIREVIA 547
Cdd:TIGR00462 277 MLALGADSIDDVLA 290
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
140-545 |
1.31e-08 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 56.48 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 140 MQENLRLRHRVIKAIWDFLDREGFVQVETPFLTKSTPEGAR------DFLVPYRHEPGLFYaLPQSPQLFKQMLMVAGLD 213
Cdd:PRK09350 1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILSQATVTDIHlvpfetRFVGPGASQGKTLW-LMTSPEYHMKRLLAAGSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 214 RYFQIARCFRDEDLRADRQPDFTQL-------DLEMSFVEVEDVLElnerlmahvfrEALGVElplPFPRLSYEEAMERY 286
Cdd:PRK09350 80 PIFQICKSFRNEEAGRYHNPEFTMLewyrphyDMYRLMNEVDDLLQ-----------QVLDCE---PAESLSYQQAFLRY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 287 gsdkpdlrfglelKEVGPLfrqsgfrvfqeaesvkalalpkalsRKEVAELEEVAKRHKAQGLAwaRVEEGgfsggvakf 366
Cdd:PRK09350 146 -------------LGIDPL-------------------------SADKTQLREVAAKLGLSNIA--DEEED--------- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 367 lepvREALLQatearpgdtLLFVAGprkVAATalgavrlraadlLGLKREGFrflwVVDFPllewdeEEEAwtymhhPFT 446
Cdd:PRK09350 177 ----RDTLLQ---------LLFTFG---VEPN------------IGKEKPTF----VYHFP------ASQA------ALA 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 447 SPHPEDLpllekdpgRVrALAYDLVLNGVEVGGGSIRIHDPRLQARVFRLlgigEEEQREKFGF--------FLEALEYG 518
Cdd:PRK09350 213 KISTEDH--------RV-AERFEVYFKGIELANGFHELTDAREQRQRFEQ----DNRKRAARGLpqqpidenLIAALEAG 279
|
410 420
....*....|....*....|....*..
1G51_B 519 APPHGGIAWGLDRLLALMTGSPSIREV 545
Cdd:PRK09350 280 LPDCSGVALGVDRLIMLALGAESISEV 306
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
18-100 |
6.78e-08 |
|
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae mitochondrial (mt) 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 fungal 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. Mutations in the gene for S. cerevisiae mtAspRS result in a "petite" phenotype typical for a mutation in a nuclear gene that results in a non-functioning mitochondrial protein synthesis system.
Pssm-ID: 239816 [Multi-domain] Cd Length: 86 Bit Score: 50.01 E-value: 6.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 18 EVVLEGWVNRRRDLGG-LIFLDLRDREG-LVQLVAHPASPAYATAERVRPEWVVRAKGLVRLRpEPNPRLATGRVEVELS 95
Cdd:cd04321 1 KVTLNGWIDRKPRIVKkLSFADLRDPNGdIIQLVSTAKKDAFSLLKSITAESPVQVRGKLQLK-EAKSSEKNDEWELVVD 79
|
....*
1G51_B 96 ALEVL 100
Cdd:cd04321 80 DIQTL 84
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
18-112 |
2.28e-07 |
|
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus horikoshii AsnRS asparaginyl-tRNA synthetase (AsnRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The archeal 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.
Pssm-ID: 239814 [Multi-domain] Cd Length: 103 Bit Score: 49.06 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 18 EVVLEGWVNRRRDLGGLIFLDLRDREGLVQLV--AHPASPAYATAERVRPEWVVRAKGLVRLRPEpnprlATGRVEVELS 95
Cdd:cd04319 1 KVTLAGWVYRKREVGKKAFIVLRDSTGIVQAVfsKDLNEEAYREAKKVGIESSVIVEGAVKADPR-----APGGAEVHGE 75
|
90
....*....|....*..
1G51_B 96 ALEVLAEAKTPPFPVDA 112
Cdd:cd04319 76 KLEIIQNVEFFPITEDA 92
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
18-102 |
5.70e-07 |
|
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and Saccharomyces cerevisiae cytoplasmic asparaginyl-tRNA synthetase (AsnRS), in Brugia malayai AsnRs and, in various putative bacterial AsnRSs. 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 synthesis, whereas the other exclusively with mitochondrial protein synthesis. AsnRS is immunodominant antigen of the filarial nematode B. malayai and 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: 239818 [Multi-domain] Cd Length: 84 Bit Score: 47.61 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 18 EVVLEGWVNRRRDLGGLIFLDLRDREGLVQ-LVAHPASPAYATAERVRPEWVVRAKGlvRLRPEPNPRLATGRVEVELSA 96
Cdd:cd04323 1 RVKVFGWVHRLRSQKKLMFLVLRDGTGFLQcVLSKKLVTEFYDAKSLTQESSVEVTG--EVKEDPRAKQAPGGYELQVDY 78
|
....*.
1G51_B 97 LEVLAE 102
Cdd:cd04323 79 LEIIGE 84
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
457-550 |
2.33e-06 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 50.36 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 457 EKDPGRVRAlAYDLVLNGV-EVGGGSIRihDPRLQARVFRLlgigeEEQ---REKFGFFLEALEYGAPPHGGIAWGLDRL 532
Cdd:PLN02603 469 ENDDGKTVA-AMDMLVPRVgELIGGSQR--EERLEYLEARL-----DELklnKESYWWYLDLRRYGSVPHAGFGLGFERL 540
|
90
....*....|....*...
1G51_B 533 LALMTGSPSIREVIAFPK 550
Cdd:PLN02603 541 VQFATGIDNIRDAIPFPR 558
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| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
18-102 |
9.30e-05 |
|
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli asparaginyl-tRNA synthetase (AsnRS) and, in Arabidopsis thaliana and Saccharomyces cerevisiae mitochondrial (mt) AsnRS. 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. S. cerevisiae mtAsnRS can charge E.coli tRNA with asparagines. Mutations in the gene for S. cerevisiae mtAsnRS has been found to induce a "petite" phenotype typical for a mutation in a nuclear gene that results in a non-functioning mitochondrial protein synthesis system.
Pssm-ID: 239813 [Multi-domain] Cd Length: 82 Bit Score: 41.01 E-value: 9.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 18 EVVLEGWVNRRRDLGGLIFLDLRDreGL----VQLVAHPASPAYATAERVRPEWVVRAKGLVRLRPEpnprlATGRVEVE 93
Cdd:cd04318 1 EVTVNGWVRSVRDSKKISFIELND--GSclknLQVVVDKELTNFKEILKLSTGSSIRVEGVLVKSPG-----AKQPFELQ 73
|
....*....
1G51_B 94 LSALEVLAE 102
Cdd:cd04318 74 AEKIEVLGE 82
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
18-111 |
2.56e-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: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 18 EVVLEGWVNRRRDLGG-LIFLDLRDREGLVQLVAHpASPAYAT------AERVRPEWVVRAKGLVRLRPEPNPRLATGRV 90
Cdd:cd04320 1 EVLIRARVHTSRAQGAkLAFLVLRQQGYTIQGVLA-ASAEGVSkqmvkwAGSLSKESIVDVEGTVKKPEEPIKSCTQQDV 79
|
90 100
....*....|....*....|..
1G51_B 91 EVELSALEVLAEAKTP-PFPVD 111
Cdd:cd04320 80 ELHIEKIYVVSEAAEPlPFQLE 101
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
504-555 |
4.64e-04 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 42.93 E-value: 4.64e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
1G51_B 504 QREKFGFFLEALEYGAPPHGGIAWGLDRLLALMTGSPSIREVIAFPKNKeGK 555
Cdd:PLN02532 580 PREQYEWYLDLRRHGTVKHSGFSLGFELMVLFATGLPDVRDAIPFPRSW-GK 630
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
449-550 |
5.08e-04 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 43.09 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G51_B 449 HPEDLPL----LEKDPGRVRALayDLVLNGV-EVGGGSIRIHDPRLQARVfrllgIGEEE-QREKFGFFLEALEYGAPPH 522
Cdd:PTZ00425 479 YPKDLKAfymkLNEDQKTVAAM--DVLVPKIgEVIGGSQREDNLERLDKM-----IKEKKlNMESYWWYRQLRKFGSHPH 551
|
90 100
....*....|....*....|....*...
1G51_B 523 GGIAWGLDRLLALMTGSPSIREVIAFPK 550
Cdd:PTZ00425 552 AGFGLGFERLIMLVTGVDNIKDTIPFPR 579
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
489-550 |
4.50e-03 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 39.98 E-value: 4.50e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1G51_B 489 LQARVFRLLGIGEEEQR---------------EKFGFFLEALEYGAPPHGGIAWGLDRLLALMTGSPSIREVIAFPK 550
Cdd:PLN02221 489 LVPKVGELIGGSQREERydvikqrieemglpiEPYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPR 565
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