|
Name |
Accession |
Description |
Interval |
E-value |
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
49-616 |
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: 788.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 49 RTNTCGELRSSHLGQEVTLCGWIQYRRQN---TFLVLRDCHGLVQILIPQDES------AASVRRilceapvESVVRVSG 119
Cdd:COG0173 3 RTHYCGELRESDVGQEVTLSGWVHRRRDHgglIFIDLRDRYGITQVVFDPDDSaeafekAEKLRS-------EYVIAVTG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 120 TVISRPPGQENPKMPTGEIEIKVKTAELLNACKKLPFEIKDFVKKTEALRLQYRYLDLRSFQMQYNLRLRSQMVMKMREY 199
Cdd:COG0173 76 KVRARPEGTVNPKLPTGEIEVLASELEILNKAKTPPFQIDDDTDVSEELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 200 LCNlHGFVDIETPTLFKRTPGGAKEFLVPSR-EPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFT 278
Cdd:COG0173 156 LDE-NGFLEIETPILTKSTPEGARDYLVPSRvHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADRQPEFT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 279 QIDIEMSFVEQTGIQRLVEGLLQYSWP--GDKDpLVTPFPSMTFAEALATYGTDKPDTRFGMKIVDVSDVFRNTELRFLQ 356
Cdd:COG0173 235 QLDIEMSFVDQEDVFELMEGLIRHLFKevLGVE-LPTPFPRMTYAEAMERYGSDKPDLRFGLELVDVTDIFKDSGFKVFA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 357 DAlAKPQGTVKAICVHDGAEvLP---------------------IFLNAKKnWSSPFAKFIMEEERLELARSMEIQEEDI 415
Cdd:COG0173 314 GA-AENGGRVKAINVPGGAS-LSrkqideltefakqygakglayIKVNEDG-LKSPIAKFLSEEELAAILERLGAKPGDL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 416 VLLTAGEHEKACSLLGKLRLECADLLEmrgavLRDPAVFSFLWVVDFPLFlakEESPTE--LESAHHPFTAPNSSDIHLL 493
Cdd:COG0173 391 IFFVADKPKVVNKALGALRLKLGKELG-----LIDEDEFAFLWVVDFPLF---EYDEEEgrWVAMHHPFTMPKDEDLDLL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 494 YTEPEKVRGQHYDLVLNGNEIGGGSVRIHDAQLQRYILETL--LKEDVKL-LSHLLQALDYGAPPHGGIALGLDRLVCLV 570
Cdd:COG0173 463 ETDPGKVRAKAYDLVLNGYELGGGSIRIHDPELQEKVFELLgiSEEEAEEkFGFLLEAFKYGAPPHGGIAFGLDRLVMLL 542
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 568910675 571 TGAPSIRDVIAFPKSYRGQDLMSNAPDSVSPEELKPYHIHVLWPAD 616
Cdd:COG0173 543 AGEDSIRDVIAFPKTQSAQDLMTGAPSEVDEKQLKELHIRLRPPEK 588
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
49-615 |
0e+00 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 772.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 49 RTNTCGELRSSHLGQEVTLCGWIQYRRQN---TFLVLRDCHGLVQILIPQD----ESAASVRRilceapvESVVRVSGTV 121
Cdd:PRK00476 4 RTHYCGELRESHVGQTVTLCGWVHRRRDHgglIFIDLRDREGIVQVVFDPDaeafEVAESLRS-------EYVIQVTGTV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 122 ISRPPGQENPKMPTGEIEIKVKTAELLNACKKLPFEIKDFVKKTEALRLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLc 201
Cdd:PRK00476 77 RARPEGTVNPNLPTGEIEVLASELEVLNKSKTLPFPIDDEEDVSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFL- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 202 NLHGFVDIETPTLFKRTPGGAKEFLVPSR-EPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQI 280
Cdd:PRK00476 156 DDNGFLEIETPILTKSTPEGARDYLVPSRvHPGKFYALPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEFTQI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 281 DIEMSFVEQTGIQRLVEGLLQYSWpgdKD----PLVTPFPSMTFAEALATYGTDKPDTRFGMKIVDVSDVFRNTELRFLQ 356
Cdd:PRK00476 236 DIEMSFVTQEDVMALMEGLIRHVF---KEvlgvDLPTPFPRMTYAEAMRRYGSDKPDLRFGLELVDVTDLFKDSGFKVFA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 357 DALAKpQGTVKAICVHDGAEVLP---------------------IFLNAKKnWSSPFAKFIMEEERLELARSMEIQEEDI 415
Cdd:PRK00476 313 GAAND-GGRVKAIRVPGGAAQLSrkqideltefakiygakglayIKVNEDG-LKGPIAKFLSEEELAALLERTGAKDGDL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 416 VLLTAGEHEKACSLLGKLRLECADLLEmrgavLRDPAVFSFLWVVDFPLFLAKEESPTeLESAHHPFTAPNSSDIH-LLY 494
Cdd:PRK00476 391 IFFGADKAKVVNDALGALRLKLGKELG-----LIDEDKFAFLWVVDFPMFEYDEEEGR-WVAAHHPFTMPKDEDLDeLET 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 495 TEPEKVRGQHYDLVLNGNEIGGGSVRIHDAQLQRYILETL--LKEDVKL-LSHLLQALDYGAPPHGGIALGLDRLVCLVT 571
Cdd:PRK00476 465 TDPGKARAYAYDLVLNGYELGGGSIRIHRPEIQEKVFEILgiSEEEAEEkFGFLLDALKYGAPPHGGIAFGLDRLVMLLA 544
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 568910675 572 GAPSIRDVIAFPKSYRGQDLMSNAPDSVSPEELKPYHIHVLWPA 615
Cdd:PRK00476 545 GADSIRDVIAFPKTQSAQDLLTGAPSPVDEKQLRELGIRLRKKE 588
|
|
| aspS_bact |
TIGR00459 |
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be ... |
49-609 |
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: 586.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 49 RTNTCGELRSSHLGQEVTLCGWIQYRRQN---TFLVLRDCHGLVQILIPQD----ESAASVRRilceapvESVVRVSGTV 121
Cdd:TIGR00459 2 RTHYCGQLRTEHLGQTVTLAGWVNRRRDLgglIFIDLRDRSGIVQVVCDPDadalKLAKGLRN-------EDVVQVKGKV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 122 ISRPPGQENPKMPTGEIEIKVKTAELLNACKKLPFEIKDfVKKTEALRLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLc 201
Cdd:TIGR00459 75 SARPEGNINRNLDTGEIEILAESITLLNKSKTPPLIIEK-TDAEEEVRLKYRYLDLRRPEMQQRLKLRHKVTKAVRNFL- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 202 NLHGFVDIETPTLFKRTPGGAKEFLVPSR-EPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQI 280
Cdd:TIGR00459 153 DQQGFLEIETPMLTKSTPEGARDYLVPSRvHKGEFYALPQSPQLFKQLLMVSGVDRYYQIARCFRDEDLRADRQPEFTQI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 281 DIEMSFVEQTGIQRLVEGLLQYSWPGDKD-PLVTPFPSMTFAEALATYGTDKPDTRFGMKIVDVSDVFRNTELRFLQdAL 359
Cdd:TIGR00459 233 DMEMSFMTQEDVMELIEKLVSHVFLEVKGiDLKKPFPVMTYAEAMERYGSDKPDLRFPLELIDVTDLFKDSEFKVFS-NL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 360 AKPQGTVKAICVHDGAEVLP---------------------IFLNAKKNwSSPFAKFIMEEERLELARSMEIQEEDIVLL 418
Cdd:TIGR00459 312 INDGGRVKAIRVPGGWAELSrksikelrkfakeygakglayLKVNEDGI-NSPIKKFLDEKKGKILLERTDAQNGDILLF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 419 TAGEHEKACSLLGKLRLECADLLEmrgavLRDPAVFSFLWVVDFPLFLAKEESptELESAHHPFTAPNSSDIHLLYTEPE 498
Cdd:TIGR00459 391 GAGSKKIVLDALGALRLKLGKDLG-----LVDPDLFSFLWVVDFPMFEKDKEG--RLCAAHHPFTMPKDEDLENLEAAPE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 499 KVRGQHYDLVLNGNEIGGGSVRIHDAQLQRYILETL---LKEDVKLLSHLLQALDYGAPPHGGIALGLDRLVCLVTGAPS 575
Cdd:TIGR00459 464 EALAEAYDLVLNGVELGGGSIRIHDPEVQKKVFEILgidPEEAREKFGFLLEAFKYGTPPHAGFALGLDRLMMLLTGTDN 543
|
570 580 590
....*....|....*....|....*....|....
gi 568910675 576 IRDVIAFPKSYRGQDLMSNAPDSVSPEELKPYHI 609
Cdd:TIGR00459 544 IRDVIAFPKTTAAACLMTEAPSFIDEKQLEELSI 577
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
36-609 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 542.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 36 SSQRIPEFSSFVARTNTCGELRSSHLGQEVTLCGWIQYRRQN---TFLVLRDCHGLVQIlIPQDESAASVRRILCEAPVE 112
Cdd:PLN02903 46 AVDSMSSQLTWPSRSHLCGALSVNDVGSRVTLCGWVDLHRDMgglTFLDVRDHTGIVQV-VTLPDEFPEAHRTANRLRNE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 113 SVVRVSGTVISRPPGQENPKMPTGEIEIKVKTAELLNAC-KKLPFEI------KDFVKktEALRLQYRYLDLRSFQMQYN 185
Cdd:PLN02903 125 YVVAVEGTVRSRPQESPNKKMKTGSVEVVAESVDILNVVtKSLPFLVttadeqKDSIK--EEVRLRYRVLDLRRPQMNAN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 186 LRLRSQMVMKMREYLCNLHGFVDIETPTLFKRTPGGAKEFLVPSR-EPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCY 264
Cdd:PLN02903 203 LRLRHRVVKLIRRYLEDVHGFVEIETPILSRSTPEGARDYLVPSRvQPGTFYALPQSPQLFKQMLMVSGFDRYYQIARCF 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 265 RDEGSRPDRQPEFTQIDIEMSFVEQTGIQRLVEGLLQYSWPGDKD-PLVTPFPSMTFAEALATYGTDKPDTRFGMKIVDV 343
Cdd:PLN02903 283 RDEDLRADRQPEFTQLDMELAFTPLEDMLKLNEDLIRQVFKEIKGvQLPNPFPRLTYAEAMSKYGSDKPDLRYGLELVDV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 344 SDVFRNTELRFLQDALAKpQGTVKAICVHDGAEV-----LP---IFLNAKKNWSS--PFAKF---------------IME 398
Cdd:PLN02903 363 SDVFAESSFKVFAGALES-GGVVKAICVPDGKKIsnntaLKkgdIYNEAIKSGAKglAFLKVlddgelegikalvesLSP 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 399 EERLELARSMEIQEEDIVLLTAGEHEKACSLLGKLRLECADLLEMRgavlrDPAVFSFLWVVDFPLFlakEESPTE--LE 476
Cdd:PLN02903 442 EQAEQLLAACGAGPGDLILFAAGPTSSVNKTLDRLRQFIAKTLDLI-----DPSRHSILWVTDFPMF---EWNEDEqrLE 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 477 SAHHPFTAPNSSDIHLLytepEKVRGQHYDLVLNGNEIGGGSVRIHDAQLQRYILET--LLKEDVK-LLSHLLQALDYGA 553
Cdd:PLN02903 514 ALHHPFTAPNPEDMGDL----SSARALAYDMVYNGVEIGGGSLRIYRRDVQQKVLEAigLSPEEAEsKFGYLLEALDMGA 589
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 568910675 554 PPHGGIALGLDRLVCLVTGAPSIRDVIAFPKSYRGQDLMSNAPDSVSPEELKPYHI 609
Cdd:PLN02903 590 PPHGGIAYGLDRLVMLLAGAKSIRDVIAFPKTTTAQCALTRAPSEVDDKQLQDLSI 645
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
53-605 |
6.49e-153 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 457.53 E-value: 6.49e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 53 CGELRSSHLGQEVTLCGWIQYRRQN---TFLVLRDCHGLVQILIPQDESAASVRRILCEAPVESVVRVSGTVISRPPGQE 129
Cdd:PRK12820 9 CGHLSLDDTGREVCLAGWVDAFRDHgelLFIHLRDRNGFIQAVFSPEAAPADVYELAASLRAEFCVALQGEVQKRLEETE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 130 NPKMPTGEIEIKVKTAELLNACKKLPFEIKDFVKK-----------TEALRLQYRYLDLRSFQMQYNLRLRSQMVMKMRE 198
Cdd:PRK12820 89 NPHIETGDIEVFVRELSILAASEALPFAISDKAMTagagsagadavNEDLRLQYRYLDIRRPAMQDHLAKRHRIIKCARD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 199 YLcNLHGFVDIETPTLFKRTPGGAKEFLVPSR-EPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEF 277
Cdd:PRK12820 169 FL-DSRGFLEIETPILTKSTPEGARDYLVPSRiHPKEFYALPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 278 TQIDIEMSFVEQTGIQRLVEGLLQYSWPGDKDPLVTPFPSMTFAEALATYGTDKPDTRFGMKIVDVSDVFRNTELRFLQD 357
Cdd:PRK12820 248 TQLDIEASFIDEEFIFELIEELTARMFAIGGIALPRPFPRMPYAEAMDTTGSDRPDLRFDLKFADATDIFENTRYGIFKQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 358 ALAKpQGTVKAICVHD--------------GAEVLPIFLNAKKNW--------SSPFAKFIMEEERLELARSMEIQEEDI 415
Cdd:PRK12820 328 ILQR-GGRIKGINIKGqseklsknvlqneyAKEIAPSFGAKGMTWmraeagglDSNIVQFFSADEKEALKRRFHAEDGDV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 416 VLLTA-GEHEKACSLLGKLRLECADLLEmrgavLRDPAVFSFLWVVDFPLFLAKEESptELESAHHPFTAPNSSDIHLLY 494
Cdd:PRK12820 407 IIMIAdASCAIVLSALGQLRLHLADRLG-----LIPEGVFHPLWITDFPLFEATDDG--GVTSSHHPFTAPDREDFDPGD 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 495 TEP-EKVRGQHYDLVLNGNEIGGGSVRIHDAQLQRYILET--LLKEDVK-LLSHLLQALDYGAPPHGGIALGLDRLVCLV 570
Cdd:PRK12820 480 IEElLDLRSRAYDLVVNGEELGGGSIRINDKDIQLRIFAAlgLSEEDIEdKFGFFLRAFDFAAPPHGGIALGLDRVVSMI 559
|
570 580 590
....*....|....*....|....*....|....*
gi 568910675 571 TGAPSIRDVIAFPKSYRGQDLMSNAPDSVSPEELK 605
Cdd:PRK12820 560 LQTPSIREVIAFPKNRSAACPLTGAPSEVAQEQLA 594
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
186-585 |
4.89e-147 |
|
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: 426.99 E-value: 4.89e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 186 LRLRSQMVMKMREYLCNlHGFVDIETPTLFKRTPGGAKEFLVPSR-EPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCY 264
Cdd:cd00777 1 LRLRSRVIKAIRNFLDE-QGFVEIETPILTKSTPEGARDFLVPSRlHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 265 RDEGSRPDRQPEFTQIDIEMSFVEQTGIQRLVEGLLQYSWPGDKD-PLVTPFPSMTFAEALATYGtdkpdtrfgmkivdv 343
Cdd:cd00777 80 RDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGvELTTPFPRMTYAEAMERYG--------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 344 sdvfrntelrflqdalakpqgtvkaicvhdgaevlpiflnakknwsspfakfimeeerlelarsmeiqeedivlltageh 423
Cdd:cd00777 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 424 ekacsllgklrlecadllemrgavlrdpavFSFLWVVDFPLFLaKEESPTELESAHHPFTAPNSSDIHLLYTEPEKVRGQ 503
Cdd:cd00777 145 ------------------------------FKFLWIVDFPLFE-WDEEEGRLVSAHHPFTAPKEEDLDLLEKDPEDARAQ 193
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 504 HYDLVLNGNEIGGGSVRIHDAQLQRYILETLLK---EDVKLLSHLLQALDYGAPPHGGIALGLDRLVCLVTGAPSIRDVI 580
Cdd:cd00777 194 AYDLVLNGVELGGGSIRIHDPDIQEKVFEILGLseeEAEEKFGFLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVI 273
|
....*
gi 568910675 581 AFPKS 585
Cdd:cd00777 274 AFPKT 278
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
166-584 |
5.04e-121 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 361.88 E-value: 5.04e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 166 EALRLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLCNlHGFVDIETPTLFK-RTPGGAKEFLVPSREPGKFYSLPQSPQQ 244
Cdd:pfam00152 2 EETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDE-NGFLEVETPILTKsATPEGARDFLVPSRALGKFYALPQSPQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 245 FKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEMSFVEQTGIQRLVEGLLQYSW-----------PGDKDPLVT 313
Cdd:pfam00152 81 YKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFkevegiakeleGGTLLDLKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 314 PFPSMTFAEAL----------ATYGTDKPDTRFGMKIVdvsdvfrntelrflqdalakpqgtvkaicvhdgaevlpifln 383
Cdd:pfam00152 161 PFPRITYAEAIeklngkdveeLGYGSDKPDLRFLLELV------------------------------------------ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 384 akknwsspfakfimeeerlelarsmeiqeedivlltagehekacsllgklrlecadllemrgavlRDPAVFSFLWVVDFP 463
Cdd:pfam00152 199 -----------------------------------------------------------------IDKNKFNPLWVTDFP 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 464 lflakeespteleSAHHPFTAPNSSDIhllytepeKVRGQHYDLVLNGNEIGGGSVRIHDAQLQRYILETLL---KEDVK 540
Cdd:pfam00152 214 -------------AEHHPFTMPKDEDD--------PALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGldpEEAEE 272
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 568910675 541 LLSHLLQALDYGAPPHGGIALGLDRLVCLVTGAPSIRDVIAFPK 584
Cdd:pfam00152 273 KFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFPK 316
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
49-182 |
6.49e-64 |
|
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: 206.99 E-value: 6.49e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 49 RTNTCGELRSSHLGQEVTLCGWIQYRRQN---TFLVLRDCHGLVQILIPQDESAASvrRILCEAPVESVVRVSGTVISRP 125
Cdd:cd04317 1 RTHYCGELRESHVGQEVTLCGWVQRRRDHgglIFIDLRDRYGIVQVVFDPEEAPEF--ELAEKLRNESVIQVTGKVRARP 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 568910675 126 PGQENPKMPTGEIEIKVKTAELLNACKKLPFEIKDFVKKTEALRLQYRYLDLRSFQM 182
Cdd:cd04317 79 EGTVNPKLPTGEIEVVASELEVLNKAKTLPFEIDDDVNVSEELRLKYRYLDLRRPKM 135
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
186-587 |
2.53e-63 |
|
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: 210.41 E-value: 2.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 186 LRLRSQMVMKMREYLCNlHGFVDIETPTLFKRTPG-GAKEFLVPSREPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCY 264
Cdd:cd00669 1 FKVRSKIIKAIRDFMDD-RGFLEVETPMLQKITGGaGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 265 RDEGSRPDRQPEFTQIDIEMSFVEQTGIQRLVEGLLQYSW------------PGDKDPLVtPFPSMTFAEALATYGtdkp 332
Cdd:cd00669 80 RNEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLArevlgvtavtygFELEDFGL-PFPRLTYREALERYG---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 333 dtrfgmkivdvsdvfrntelrflqdalakpqgtvkaicvhdgaevlpiflnakknwsspfakfimeeerlelarsmeiqe 412
Cdd:cd00669 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 413 edivlltagehekacsllgklrlecadllemrgavlrdpavfSFLWVVDFPLFlakeesptelesAHHPFTAPNSSDihl 492
Cdd:cd00669 155 ------------------------------------------QPLFLTDYPAE------------MHSPLASPHDVN--- 177
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 493 lytePEKVRGqhYDLVLNGNEIGGGSVRIHDAQLQ-RYILETLLKEDVKLLS--HLLQALDYGAPPHGGIALGLDRLVCL 569
Cdd:cd00669 178 ----PEIADA--FDLFINGVEVGNGSSRLHDPDIQaEVFQEQGINKEAGMEYfeFYLKALEYGLPPHGGLGIGIDRLIML 251
|
410
....*....|....*...
gi 568910675 570 VTGAPSIRDVIAFPKSYR 587
Cdd:cd00669 252 MTNSPTIREVIAFPKMRR 269
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
49-583 |
1.24e-60 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 208.51 E-value: 1.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 49 RTNTCGELRSSHLGQEVTLCGWIQYRR---QNTFLVLRDCHGLVQILIPQDESAASVRRILcEAPVESVVRVSGTVisrp 125
Cdd:PRK05159 3 KRHLTSELTPELDGEEVTLAGWVHEIRdlgGIAFLILRDRSGIIQVVVKKKVDEELFETIK-KLKRESVVSVTGTV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 126 pgQENPKMPTGeIEIKVKTAELLN-ACKKLPFEIKDFVKKTEALRLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLCNlH 204
Cdd:PRK05159 78 --KANPKAPGG-VEVIPEEIEVLNkAEEPLPLDISGKVLAELDTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYE-N 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 205 GFVDIETPTLFKR-TPGGAKEFLVPSREPGKFysLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQ-PEFTQIDI 282
Cdd:PRK05159 154 GFTEIFTPKIVASgTEGGAELFPIDYFEKEAY--LAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRHlNEYTSIDV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 283 EMSFVE-QTGIQRLVEGLLQYswpgdkdplvtpfpsmTFAEALATYGtdkpdtrfgmkivdvsdvfrnTELRFLQDALAK 361
Cdd:PRK05159 232 EMGFIDdHEDVMDLLENLLRY----------------MYEDVAENCE---------------------KELELLGIELPV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 362 PQGTVKAIcvhdgaevlpiflnakknwssPFakfimeEERLELARSMEIQ---EEDivLLTAGEHekacsLLGKlrleca 438
Cdd:PRK05159 275 PETPIPRI---------------------TY------DEAIEILKSKGNEiswGDD--LDTEGER-----LLGE------ 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 439 DLLEMRGAvlrdpavfSFLWVVDFPlflakeespteleSAHHPF-TAPNSSDihllytePEKVRGqhYDLVLNGNEIGGG 517
Cdd:PRK05159 315 YVKEEYGS--------DFYFITDYP-------------SEKRPFyTMPDEDD-------PEISKS--FDLLFRGLEITSG 364
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568910675 518 SVRIHDAQLqryiLETLLKE---DVKLLSHLLQALDYGAPPHGGIALGLDRLVCLVTGAPSIRDVIAFP 583
Cdd:PRK05159 365 GQRIHRYDM----LVESIKEkglNPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
49-583 |
1.87e-52 |
|
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: 186.03 E-value: 1.87e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 49 RTNTCGELRSSHLGQEVTLCGWIQYRRQN---TFLVLRDCHGLVQILIPQDESA--ASVRRIlceaPVESVVRVSGTVis 123
Cdd:COG0017 1 KRTYIKDLLPEHVGQEVTVAGWVRTKRDSggiSFLILRDGSGFIQVVVKKDKLEnfEEAKKL----TTESSVEVTGTV-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 124 rppgQENPKMPTGeIEIKVKTAELLNACKK-LPFEIK----DFvkktealRLQYRYLDLRSFQMQYNLRLRSQMVMKMRE 198
Cdd:COG0017 75 ----VESPRAPQG-VELQAEEIEVLGEADEpYPLQPKrhslEF-------LLDNRHLRLRTNRFGAIFRIRSELARAIRE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 199 YLcNLHGFVDIETPTLfkrTP----GGAKEFLVpsrepgKFY----SLPQSPQQFKQLlMVGGLDRYFQVARCYRDEGSR 270
Cdd:COG0017 143 FF-QERGFVEVHTPII---TAsateGGGELFPV------DYFgkeaYLTQSGQLYKEA-LAMALEKVYTFGPTFRAEKSN 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 271 PDRQ-PEFTQIDIEMSFVEQTGIQRLVEGLLQYswpgdkdplvtpfpsmTFAEALATYGtdkpdtrfgmkivdvsdvfrn 349
Cdd:COG0017 212 TRRHlAEFWMIEPEMAFADLEDVMDLAEEMLKY----------------IIKYVLENCP--------------------- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 350 TELRFLQDALAKpqgtvkaicvhdgaevLPIFLNakknwsSPFAKFIMEE--ERLElARSMEIQ-EEDIvlltAGEHEKA 426
Cdd:COG0017 255 EELEFLGRDVER----------------LEKVPE------SPFPRITYTEaiEILK-KSGEKVEwGDDL----GTEHERY 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 427 cslLGKlrlecadllemrgaVLRDPAVFsflwVVDFplflakeesPTELEsahhPF-TAPNSSDihllytePEKVRGqhY 505
Cdd:COG0017 308 ---LGE--------------EFFKKPVF----VTDY---------PKEIK----AFyMKPNPDD-------PKTVAA--F 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 506 DLVLNG-NEIGGGSVRIHDAQLqryiLETLLKE---DVKLLSHLLQALDYGAPPHGGIALGLDRLVCLVTGAPSIRDVIA 581
Cdd:COG0017 345 DLLAPGiGEIIGGSQREHRYDV----LVERIKEkglDPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIP 420
|
..
gi 568910675 582 FP 583
Cdd:COG0017 421 FP 422
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
169-584 |
1.09e-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: 125.37 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 169 RLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLcNLHGFVDIETPTLFKR-TPGGAKEFlvpsrePGKFYS----LPQSPQ 243
Cdd:cd00776 7 LLDNRHLDLRTPKVQAIFRIRSEVLRAFREFL-RENGFTEVHTPKITSTdTEGGAELF------KVSYFGkpayLAQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 244 QFKQlLMVGGLDRYFQVARCYRDEGSRPDRQ-PEFTQIDIEMSFVEQ-TGIQRLVEGLLQYswpgdkdplvtpfpsmtfa 321
Cdd:cd00776 80 LYKE-MLIAALERVYEIGPVFRAEKSNTRRHlSEFWMLEAEMAFIEDyNEVMDLIEELIKY------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 322 ealatygtdkpdtrfgmkivdvsdVFRNTELRFLQDALAKPQGTvkaicvhdgaEVLPIFLnakknwsSPFAKfIMEEER 401
Cdd:cd00776 140 ------------------------IFKRVLERCAKELELVNQLN----------RELLKPL-------EPFPR-ITYDEA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 402 LELARSMEIQE-----EDIvlltAGEHEKacsLLGKLrlecadllemrgavLRDPAVFsflwVVDFPlflakeesptele 476
Cdd:cd00776 178 IELLREKGVEEevkwgEDL----STEHER---LLGEI--------------VKGDPVF----VTDYP------------- 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 477 SAHHPFTAPNSSDihllytEPEKVRGqhYDLVLNGN-EIGGGSVRIHDAQ-LQRYILEtlLKEDVKLLSHLLQALDYGAP 554
Cdd:cd00776 220 KEIKPFYMKPDDD------NPETVES--FDLLMPGVgEIVGGSQRIHDYDeLEERIKE--HGLDPESFEWYLDLRKYGMP 289
|
410 420 430
....*....|....*....|....*....|
gi 568910675 555 PHGGIALGLDRLVCLVTGAPSIRDVIAFPK 584
Cdd:cd00776 290 PHGGFGLGLERLVMWLLGLDNIREAILFPR 319
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
54-584 |
4.28e-31 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 127.52 E-value: 4.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 54 GELRSSHLGQEVTLCGWIQYRR---QNTFLVLRDCHGLVQILIPQDESAASVRRI--LCEAPVESVVRVSGTVIsrppgq 128
Cdd:PLN02850 73 SDLGEELAGSEVLIRGRVHTIRgkgKSAFLVLRQSGFTVQCVVFVSEVTVSKGMVkyAKQLSRESVVDVEGVVS------ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 129 eNPKMP----TGEIEIKVKTAELLN-ACKKLPFEIKD-----------------FVKKTEALRLQYRYLDLRSFQMQYNL 186
Cdd:PLN02850 147 -VPKKPvkgtTQQVEIQVRKIYCVSkALATLPFNVEDaarseseiekalqtgeqLVRVGQDTRLNNRVLDLRTPANQAIF 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 187 RLRSQMVMKMREYLCNlHGFVDIETPTLFK-RTPGGAKEFLVPSRepGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYR 265
Cdd:PLN02850 226 RIQSQVCNLFREFLLS-KGFVEIHTPKLIAgASEGGSAVFRLDYK--GQPACLAQSPQLHKQMAICGDFRRVFEIGPVFR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 266 DEGSRPDRQ-PEFTQIDIEMSFVEQ-TGIQRLVEGLlqyswpgdkdplvtpFPSMtFaealatygtDKPDTRFGMKIVDV 343
Cdd:PLN02850 303 AEDSFTHRHlCEFTGLDLEMEIKEHySEVLDVVDEL---------------FVAI-F---------DGLNERCKKELEAI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 344 SDVFRNTELRFLQDA--LAKPQGTvkAICVHDGAEVLPIflnakknwsspfakfimeeerlelarsmeiqeEDIvlltAG 421
Cdd:PLN02850 358 REQYPFEPLKYLPKTlrLTFAEGI--QMLKEAGVEVDPL--------------------------------GDL----NT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 422 EHEKAcslLGKLrlecadLLEMRGAvlrdpavfSFLWVVDFPLflakeesptelesAHHPF-TAPNSSDIhlLYTepekv 500
Cdd:PLN02850 400 ESERK---LGQL------VKEKYGT--------DFYILHRYPL-------------AVRPFyTMPCPDDP--KYS----- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 501 rgQHYDLVLNGNEIGGGSVRIHDAQLqryiLETLLKE---DVKLLSHLLQALDYGAPPHGGIALGLDRLVCLVTGAPSIR 577
Cdd:PLN02850 443 --NSFDVFIRGEEIISGAQRVHDPEL----LEKRAEEcgiDVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIR 516
|
....*..
gi 568910675 578 DVIAFPK 584
Cdd:PLN02850 517 KTSLFPR 523
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
49-583 |
5.76e-27 |
|
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: 114.75 E-value: 5.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 49 RTNTCGELRSSH--------LGQEVTLCGWIQYRR---QNTFLVLRDCHGLVQILIPQDEsaasvrriLCEAPVESV--- 114
Cdd:COG1190 35 RTHTAAEIREKYdeleaeeeTGDEVSVAGRIMAKRdmgKASFADLQDGSGRIQLYLRRDE--------LGEEAYELFkll 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 115 -----VRVSGTVI-SRppgqenpkmpTGEIEIKVKTAELLN-ACKKLP---FEIKDfvkkTEaLRLQYRYLDL----RSF 180
Cdd:COG1190 107 dlgdiVGVEGTVFrTK----------TGELSVKVEELTLLSkSLRPLPekfHGLTD----PE-TRYRQRYVDLivnpEVR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 181 QMqynLRLRSQMVMKMREYLcNLHGFVDIETPTLfKRTPGGA--KEF--------------------Lvpsrepgkfysl 238
Cdd:COG1190 172 ET---FRKRSKIIRAIRRFL-DERGFLEVETPML-QPIAGGAaaRPFithhnaldmdlylriapelyL------------ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 239 pqspqqfKQLLmVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEMSFVEQTGIQRLVEGLLQYSwpgdkdplvtpfpsm 318
Cdd:COG1190 235 -------KRLI-VGGFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREA--------------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 319 tfaeALATYGTDKpdTRFGMKIVDVSDVFRntELRFLQdalakpqgtvkAICVHDGAEVLPIflnakknwsspfakfiME 398
Cdd:COG1190 292 ----AEAVLGTTK--VTYQGQEIDLSPPWR--RITMVE-----------AIKEATGIDVTPL----------------TD 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 399 EERL-ELARSMEIQEEDivllTAGehekacslLGKLrlecadLLEMRGAV----LRDPaVFsflwVVDFPlflaKEESPt 473
Cdd:COG1190 337 DEELrALAKELGIEVDP----GWG--------RGKL------IDELFEELvepkLIQP-TF----VTDYP----VEVSP- 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 474 elesahhpFTAPNSSDihllytePEKV-RgqhYDLVLNGNEIGGGSVRIHDAQLQRYILETLLK-------------EDv 539
Cdd:COG1190 389 --------LAKRHRDD-------PGLTeR---FELFIAGREIANAFSELNDPIDQRERFEEQLElkaagddeampmdED- 449
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 568910675 540 kllshLLQALDYGAPPHGGIALGLDRLVCLVTGAPSIRDVIAFP 583
Cdd:COG1190 450 -----FLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 488
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
34-583 |
2.62e-25 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 109.79 E-value: 2.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 34 ALSSQRIPEFSSFVARTNTCGELRSSH----------LGQEVTLCGWIQYRR---QNTFLVLRDCHGLVQILIPQDEsaa 100
Cdd:PRK00484 16 ELREQGIDPYPNKFERTHTAAELRAKYddkekeeleeLEIEVSVAGRVMLKRvmgKASFATLQDGSGRIQLYVSKDD--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 101 svrriLCEAPVESV--------VRVSGTVIsrppgqenpKMPTGEIEIKVKTAELLN-ACKKLPfeikdfVK----KTEA 167
Cdd:PRK00484 93 -----VGEEALEAFkkldlgdiIGVEGTLF---------KTKTGELSVKATELTLLTkSLRPLP------DKfhglTDVE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 168 LRLQYRYLDL----RSFQMqynLRLRSQMVMKMREYLCNlHGFVDIETPTLfKRTPGG--AKEFL-------VPsrepgk 234
Cdd:PRK00484 153 TRYRQRYVDLivnpESRET---FRKRSKIISAIRRFLDN-RGFLEVETPML-QPIAGGaaARPFIthhnaldID------ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 235 FYsLPQSPQQF-KQLLmVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEMSFVEQTGIQRLVEGLLQYSwpgdkdplvt 313
Cdd:PRK00484 222 LY-LRIAPELYlKRLI-VGGFERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHL---------- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 314 pfpsmtfaeALATYGTDKpdTRFGMKIVDVSDVFRntELRFlqdalakpqgtVKAICVHDGAEVLPIflnakknwsspfa 393
Cdd:PRK00484 290 ---------AQAVLGTTK--VTYQGTEIDFGPPFK--RLTM-----------VDAIKEYTGVDFDDM------------- 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 394 kfiMEEERLELARSMEIqeedivlltagEHEKACSLlGKLrlecadLLEMRGAV----LRDPavfSFlwVVDFPlflaKE 469
Cdd:PRK00484 333 ---TDEEARALAKELGI-----------EVEKSWGL-GKL------INELFEEFvepkLIQP---TF--ITDYP----VE 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 470 ESPtelesahhpFTAPNSSDIHLlyTEpekvRgqhYDLVLNGNEIGGGSVRIHDA--QLQRYILETLLK----------- 536
Cdd:PRK00484 383 ISP---------LAKRHREDPGL--TE----R---FELFIGGREIANAFSELNDPidQRERFEAQVEAKeagddeamfmd 444
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 568910675 537 EDvkllshLLQALDYGAPPHGGIALGLDRLVCLVTGAPSIRDVIAFP 583
Cdd:PRK00484 445 ED------FLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
79-584 |
3.05e-25 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 110.08 E-value: 3.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 79 FLVLRDCHGLVQILIPQDESA-ASVRRILCEAPVESVVRVSGTVIsrppGQENPKMPTG--EIEIKVKTAELLN-ACKKL 154
Cdd:PTZ00401 98 FMVLRDGSDSVQAMAAVEGDVpKEMIDFIGQIPTESIVDVEATVC----KVEQPITSTShsDIELKVKKIHTVTeSLRTL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 155 PFEIKDFVKKTEA--------LRLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLCNlHGFVDIETPTLFKR-TPGGAKEF 225
Cdd:PTZ00401 174 PFTLEDASRKESDegakvnfdTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLID-SDFCEIHSPKIINApSEGGANVF 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 226 LVPSREpgKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQ-PEFTQIDIEMSFVEQ-TGIQRLVEGLLQYS 303
Cdd:PTZ00401 253 KLEYFN--RFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHlTEFVGLDVEMRINEHyYEVLDLAESLFNYI 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 304 WP------GDKDPLVTPFPSMTFAEALAtygtdkPDTrfgMKIVDVSDVFRNTElrflqdalakPQGTVKAICVHDGAEV 377
Cdd:PTZ00401 331 FErlathtKELKAVCQQYPFEPLVWKLT------PER---MKELGVGVISEGVE----------PTDKYQARVHNMDSRM 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 378 LPIflnakkNWSSPFAKF-IMEEERLELARSMEIQEEdivlltagehekacSLLGKLRLEcadllemrgavlrdpavfsf 456
Cdd:PTZ00401 392 LRI------NYMHCIELLnTVLEEKMAPTDDINTTNE--------------KLLGKLVKE-------------------- 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 457 LWVVDFplFLAKeesptELESAHHPF-TAPNSSDIHLLYTepekvrgqhYDLVLNGNEIGGGSVRIHDAQ--LQRyilET 533
Cdd:PTZ00401 432 RYGTDF--FISD-----RFPSSARPFyTMECKDDERFTNS---------YDMFIRGEEISSGAQRIHDPDllLAR---AK 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 568910675 534 LLKEDVKLLSHLLQALDYGAPPHGGIALGLDRLVCLVTGAPSIRDVIAFPK 584
Cdd:PTZ00401 493 MLNVDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPR 543
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
186-583 |
4.58e-24 |
|
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: 103.43 E-value: 4.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 186 LRLRSQMVMKMREYLCNlHGFVDIETPTLfKRTPGGA--KEFLVPSREPG-KFYsLPQSPQQFKQLLMVGGLDRYFQVAR 262
Cdd:cd00775 8 FIVRSKIISYIRKFLDD-RGFLEVETPML-QPIAGGAaaRPFITHHNALDmDLY-LRIAPELYLKRLIVGGFERVYEIGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 263 CYRDEGSRPDRQPEFTQIDIEMSFVEQTGIQRLVEGLLQYSwpgdkdplvtpfpsmtfaeALATYGTDKPDtrFGMKIVD 342
Cdd:cd00775 85 NFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGL-------------------VKKINGKTKIE--YGGKELD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 343 VSDVFRNTELrflqdalakpqgtVKAICvhdgaEVLPIFLNAKknwsspfAKFIMEEERLELARSmeiqeedivlltAGE 422
Cdd:cd00775 144 FTPPFKRVTM-------------VDALK-----EKTGIDFPEL-------DLEQPEELAKLLAKL------------IKE 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 423 HEKACSLLGKLRLECAD-LLEMRgavLRDPAVfsflwVVDFPlflaKEESPteLESAHHpftapnssdihllyTEPEKVr 501
Cdd:cd00775 187 KIEKPRTLGKLLDKLFEeFVEPT---LIQPTF-----IIDHP----VEISP--LAKRHR--------------SNPGLT- 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 502 gQHYDLVLNGNEIGGGSVRIHDAQLQRYILETLLK-------EDVKLLSHLLQALDYGAPPHGGIALGLDRLVCLVTGAP 574
Cdd:cd00775 238 -ERFELFICGKEIANAYTELNDPFDQRERFEEQAKqkeagddEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTDSN 316
|
....*....
gi 568910675 575 SIRDVIAFP 583
Cdd:cd00775 317 SIRDVILFP 325
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
44-583 |
4.14e-23 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 103.22 E-value: 4.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 44 SSFVARTNTcgELRSshLGQEVTLCGWIQYRR---QNTFLVLRDCHGLVQILIPQDESAASV-RRILCEAPVESVVRVSG 119
Cdd:PRK12445 51 EEFDAKDNQ--ELES--LNIEVSVAGRMMTRRimgKASFVTLQDVGGRIQLYVARDSLPEGVyNDQFKKWDLGDIIGARG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 120 TVIsrppgqenpKMPTGEIEIKVKTAELLN-ACKKLPFEIKDFvkKTEALRLQYRYLDL-RSFQMQYNLRLRSQMVMKMR 197
Cdd:PRK12445 127 TLF---------KTQTGELSIHCTELRLLTkALRPLPDKFHGL--QDQEVRYRQRYLDLiANDKSRQTFVVRSKILAAIR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 198 EYLCnLHGFVDIETPtLFKRTPGGA--KEFLVPSREPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQP 275
Cdd:PRK12445 196 QFMV-ARGFMEVETP-MMQVIPGGAsaRPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 276 EFTQIDIEMSFVEQTGIQRLVEGLLQyswpgdkdplvtpfpsmtfaeALATYGTDKPDTRFGMKIVDVSDVFRNTELRfl 355
Cdd:PRK12445 274 EFTMMELYMAYADYHDLIELTESLFR---------------------TLAQEVLGTTKVTYGEHVFDFGKPFEKLTMR-- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 356 qDALAK--PQGTVKAICVHDGAEVL--PIFLNAKKNWSspfakfimeeerlelarsmeiqeedivlltagehekacslLG 431
Cdd:PRK12445 331 -EAIKKyrPETDMADLDNFDAAKALaeSIGITVEKSWG----------------------------------------LG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 432 KLRLECADllEMRGAVLRDPAvfsflWVVDFPlflaKEESPTelesAHHPFTAPNSSDihllytepekvrgqHYDLVLNG 511
Cdd:PRK12445 370 RIVTEIFD--EVAEAHLIQPT-----FITEYP----AEVSPL----ARRNDVNPEITD--------------RFEFFIGG 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568910675 512 NEIGGGSVRIHDA--QLQRYILETLLK-----EDVKLLSHLLQALDYGAPPHGGIALGLDRLVCLVTGAPSIRDVIAFP 583
Cdd:PRK12445 421 REIGNGFSELNDAedQAERFQEQVNAKaagddEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
47-583 |
6.88e-22 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 100.81 E-value: 6.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 47 VARTNTCGELRSSHLGQEVTLCGWIQYRRQN---TFLVLRDCHGLVQILIPQDES-AASVRRILCEAPVESVVRVSGTVI 122
Cdd:PRK02983 636 VPPTHTVAEALDAPTGEEVSVSGRVLRIRDYggvLFADLRDWSGELQVLLDASRLeQGSLADFRAAVDLGDLVEVTGTMG 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 123 -SRppgqenpkmpTGEIEIKVKTAELLNAC-KKLPFEIKDFVKKtEAlRLQYRYLDL----RSFQMqynLRLRSQMVMKM 196
Cdd:PRK02983 716 tSR----------NGTLSLLVTSWRLAGKClRPLPDKWKGLTDP-EA-RVRQRYLDLavnpEARDL---LRARSAVVRAV 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 197 REYLcNLHGFVDIETPTLfKRTPGGA--KEFLVPSREpgkfYSLPQ----SPQQFKQLLMVGGLDRYFQVARCYRDEGSR 270
Cdd:PRK02983 781 RETL-VARGFLEVETPIL-QQVHGGAnaRPFVTHINA----YDMDLylriAPELYLKRLCVGGVERVFELGRNFRNEGVD 854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 271 PDRQPEFTQIDIEMSFVEQTGIQRLVEGLLQyswpgdkdplvtpfpsmtfAEALATYGTD---KPDTRFGMKIVDVSDVF 347
Cdd:PRK02983 855 ATHNPEFTLLEAYQAHADYDTMRDLTRELIQ-------------------NAAQAAHGAPvvmRPDGDGVLEPVDISGPW 915
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 348 RntelrflqdalakpqgtvkAICVHD------GAEVLPiflnakknwSSPFakfimeEERLELARSMEIQeedivlltAG 421
Cdd:PRK02983 916 P-------------------VVTVHDavsealGEEIDP---------DTPL------AELRKLCDAAGIP--------YR 953
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 422 EHEKAcsllGKLrlecadLLEMRGAVLRDPAVF-SFlwVVDFPLflakEESptelesahhPFTAPNSSDIHLlytepekv 500
Cdd:PRK02983 954 TDWDA----GAV------VLELYEHLVEDRTTFpTF--YTDFPT----SVS---------PLTRPHRSDPGL-------- 1000
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 501 rGQHYDLVLNGNEIGGGSVRIHDAQLQRYILE--TLLK-----EDVKLLSHLLQALDYGAPPHGGIALGLDRLVCLVTGA 573
Cdd:PRK02983 1001 -AERWDLVAWGVELGTAYSELTDPVEQRRRLTeqSLLAaggdpEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLTGR 1079
|
570
....*....|
gi 568910675 574 pSIRDVIAFP 583
Cdd:PRK02983 1080 -SIRETLPFP 1088
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
64-149 |
2.67e-21 |
|
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: 88.39 E-value: 2.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 64 EVTLCGWIQYRRQN---TFLVLRDCHGLVQILIPQDESAASVRRILcEAPVESVVRVSGTVISRPPGQenpkMPTGEIEI 140
Cdd:cd04100 1 EVTLAGWVHSRRDHgglIFIDLRDGSGIVQVVVNKEELGEFFEEAE-KLRTESVVGVTGTVVKRPEGN----LATGEIEL 75
|
....*....
gi 568910675 141 KVKTAELLN 149
Cdd:cd04100 76 QAEELEVLS 84
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
62-583 |
7.34e-21 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 96.60 E-value: 7.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 62 GQEVTLCGWIQYRRQN---TFLVLRDCHGLVQILIPQ---DESAASVRRILCEAPVESVVRVSGTvisrpPGqenpKMPT 135
Cdd:PLN02502 108 DVSVSVAGRIMAKRAFgklAFYDLRDDGGKIQLYADKkrlDLDEEEFEKLHSLVDRGDIVGVTGT-----PG----KTKK 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 136 GEIEIKVKTAELLNAC-KKLP---FEIKDFVKktealRLQYRYLDL-RSFQMQYNLRLRSQMVMKMREYLCNLhGFVDIE 210
Cdd:PLN02502 179 GELSIFPTSFEVLTKClLMLPdkyHGLTDQET-----RYRQRYLDLiANPEVRDIFRTRAKIISYIRRFLDDR-GFLEVE 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 211 TPTLfKRTPGGA--KEFLVPSREPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEMSFVE 288
Cdd:PLN02502 253 TPML-NMIAGGAaaRPFVTHHNDLNMDLYLRIATELHLKRLVVGGFERVYEIGRQFRNEGISTRHNPEFTTCEFYQAYAD 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 289 QTGIQRLVEGLLQYSwpgdkdplvtpfpsmtfaeALATYGTDKPDtrFGMKIVDVSDVFRNtelrflqdalakpqgtvka 368
Cdd:PLN02502 332 YNDMMELTEEMVSGM-------------------VKELTGSYKIK--YHGIEIDFTPPFRR------------------- 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 369 ICVHDGAEvlpiflnakknwsspfakfimEEERLELARSMEIQEEDIVLLTAGEHEK----ACSLLGKLrlecadLLEMR 444
Cdd:PLN02502 372 ISMISLVE---------------------EATGIDFPADLKSDEANAYLIAACEKFDvkcpPPQTTGRL------LNELF 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 445 GAVLRDPAV---FsflwVVDFPlflaKEESPteLESAH--HPFTapnssdihllyTEpekvrgqHYDLVLNGNEIGGGSV 519
Cdd:PLN02502 425 EEFLEETLVqptF----VLDHP----VEMSP--LAKPHrsKPGL-----------TE-------RFELFINGRELANAFS 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568910675 520 RIHDAQLQRYILETLLK-------EDVKLLSHLLQALDYGAPPHGGIALGLDRLVCLVTGAPSIRDVIAFP 583
Cdd:PLN02502 477 ELTDPVDQRERFEEQVKqhnagddEAMALDEDFCTALEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFP 547
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
132-583 |
9.19e-15 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 77.36 E-value: 9.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 132 KMPTGEIEIKVKTAELLNAC-KKLPfeIKDFVKKTEaLRLQYRYLDLR-SFQMQYNLRLRSQMVMKMREYLcNLHGFVDI 209
Cdd:PTZ00417 200 KSKKGELSIFPKETIILSPClHMLP--MKYGLKDTE-IRYRQRYLDLMiNESTRSTFITRTKIINYLRNFL-NDRGFIEV 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 210 ETPTLfKRTPGGA--KEFLVPSREPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTqidiemsfv 287
Cdd:PTZ00417 276 ETPTM-NLVAGGAnaRPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFT--------- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 288 eqtgiqrlvegllqyswpgdkdplvtpfpSMTFAEALAtygtdkpdtrfgmkivDVSDVFRNTElRFLQDALAKPQGTVK 367
Cdd:PTZ00417 346 -----------------------------SCEFYWAYA----------------DFYDLIKWSE-DFFSQLVMHLFGTYK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 368 AICVHDGAEVLPIFLnakkNWSSPFAKFIMEEERLELARSMEIQEEDivllTAGEHEKACSLLGKLRLECADllEMRGAV 447
Cdd:PTZ00417 380 ILYNKDGPEKDPIEI----DFTPPYPKVSIVEELEKLTNTKLEQPFD----SPETINKMINLIKENKIEMPN--PPTAAK 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 448 LRDPAVFSFL--WVVDFPLFLAKeesptelesahHPFTAPNSSDIHllYTEPEKVrgQHYDLVLNGNEIGGGSVRIHDAQ 525
Cdd:PTZ00417 450 LLDQLASHFIenKYPNKPFFIIE-----------HPQIMSPLAKYH--RSKPGLT--ERLEMFICGKEVLNAYTELNDPF 514
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568910675 526 LQRYILETLLK-------EDVKLLSHLLQALDYGAPPHGGIALGLDRLVCLVTGAPSIRDVIAFP 583
Cdd:PTZ00417 515 KQKECFSAQQKdrekgdaEAFQFDAAFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFP 579
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
204-304 |
3.53e-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: 71.77 E-value: 3.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 204 HGFVDIETP-----TLFKRTPGGAKEFLVPSREPGKFYSLPQSPQQFKQLLMVGGL----DRYFQVARCYRDEGSR--PD 272
Cdd:cd00768 16 LGFQEVETPiverePLLEKAGHEPKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIrklpLRLAEIGPAFRNEGGRrgLR 95
|
90 100 110
....*....|....*....|....*....|..
gi 568910675 273 RQPEFTQIDIEMsFVEQTGIQRLVEGLLQYSW 304
Cdd:cd00768 96 RVREFTQLEGEV-FGEDGEEASEFEELIELTE 126
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
132-583 |
1.02e-13 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 74.30 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 132 KMPTGEIEIKVKTAELLNackklPFEIKDFVK----------KTEALRLQYRYLDLRSFQMQYN-LRLRSQMVMKMREYL 200
Cdd:PTZ00385 173 RMQRGELSVAASRMLILS-----PYVCTDQVVcpnlrgftvlQDNDVKYRYRFTDMMTNPCVIEtIKKRHVMLQALRDYF 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 201 cNLHGFVDIETPTLFKRTPGG-AKEFLVPSREPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTq 279
Cdd:PTZ00385 248 -NERNFVEVETPVLHTVASGAnAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFT- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 280 idiemsfveqtgiqrlvegllqyswpgdkdplvtpfpSMTFAEALATYgtdkpdtrfgmkivdvSDVFRNTELRFLQDAL 359
Cdd:PTZ00385 326 -------------------------------------SCEFYAAYHTY----------------EDLMPMTEDIFRQLAM 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 360 aKPQGTVKAICVHDGAEVLPIFLNAKKnwssPFAKFIMEEErLELARSMEIQEEDIVLLTAG-EHEKACSLLGKLRL--- 435
Cdd:PTZ00385 353 -RVNGTTVVQIYPENAHGNPVTVDLGK----PFRRVSVYDE-IQRMSGVEFPPPNELNTPKGiAYMSVVMLRYNIPLppv 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 436 -ECADLLEMRGAVLRDPAVFSFLWVVDFPLFLakeeSPTELESAHHPFTApnssdihllytepekvrgQHYDLVLNGNEI 514
Cdd:PTZ00385 427 rTAAKMFEKLIDFFITDRVVEPTFVMDHPLFM----SPLAKEQVSRPGLA------------------ERFELFVNGIEY 484
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568910675 515 GGGSVRIHDAQLQRYILETLL-------KEDVKLLSHLLQALDYGAPPHGGIALGLDRLVCLVTGAPSIRDVIAFP 583
Cdd:PTZ00385 485 CNAYSELNDPHEQYHRFQQQLvdrqggdEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFP 560
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
56-587 |
1.58e-13 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 73.22 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 56 LRSSHLGQEVTLCGWIQYRRQN---TFLVLRDCHGLVQILIPQDESAASVRRILcEAPVESVVRVSGTVIsrppgqENPK 132
Cdd:PRK03932 10 LKGKYVGQEVTVRGWVRTKRDSgkiAFLQLRDGSCFKQLQVVKDNGEEYFEEIK-KLTTGSSVIVTGTVV------ESPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 133 MPTGeIEIKVKTAELLNACKKlPFEIKdfvKK---TEALRlQYRYLDLRSFQMQYNLRLRSQMVMKMREYLcNLHGFVDI 209
Cdd:PRK03932 83 AGQG-YELQATKIEVIGEDPE-DYPIQ---KKrhsIEFLR-EIAHLRPRTNKFGAVMRIRNTLAQAIHEFF-NENGFVWV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 210 ETPTLfkrTPG---GAKE-FLVPSREP-------GKFYSLPQSpqqfKQL---LMVGGLDRYFQVARCYRDEGSRPDRQ- 274
Cdd:PRK03932 156 DTPII---TASdceGAGElFRVTTLDLdfskdffGKEAYLTVS----GQLyaeAYAMALGKVYTFGPTFRAENSNTRRHl 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 275 PEFTQIDIEMSFVEQTGIQRLVEGLLQYswpgdkdplvtpfpsmtfaealatygtdkpdtrfgmkivdvsdVFRNT---- 350
Cdd:PRK03932 229 AEFWMIEPEMAFADLEDNMDLAEEMLKY-------------------------------------------VVKYVlenc 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 351 --ELRFLQDALAKpqgtvKAIcvhdgaEVLPIFLNakknwsSPFAKfIMEEERLELARSMEIQEEDIV-----LltAGEH 423
Cdd:PRK03932 266 pdDLEFLNRRVDK-----GDI------ERLENFIE------SPFPR-ITYTEAIEILQKSGKKFEFPVewgddL--GSEH 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 424 EKAcslLGKLRLECadllemrgavlrdPaVFsflwVVDFPlflakeesptelesahhpftapnsSDIHLLYTEP----EK 499
Cdd:PRK03932 326 ERY---LAEEHFKK-------------P-VF----VTNYP------------------------KDIKAFYMRLnpdgKT 360
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 500 VRGqhYDLVLNG-NEIGGGSVRIHDaqlqryiLETLLK--EDVKL-LSHLLQALD---YGAPPHGGIALGLDRLVCLVTG 572
Cdd:PRK03932 361 VAA--MDLLAPGiGEIIGGSQREER-------LDVLEAriKELGLnKEDYWWYLDlrrYGSVPHSGFGLGFERLVAYITG 431
|
570
....*....|....*
gi 568910675 573 APSIRDVIAFPKSYR 587
Cdd:PRK03932 432 LDNIRDVIPFPRTPG 446
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
62-158 |
5.12e-11 |
|
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: 60.02 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 62 GQEVTLCGWIQYRRQ---NTFLVLRDCHGLVQILIPQDESAASVRRILCEAPVESVVRVSGTVisrppgQENPKMPTGeI 138
Cdd:cd04316 12 GEEVTVAGWVHEIRDlggIKFVILRDREGIVQVTAPKKKVDKELFKTVRKLSRESVISVTGTV------KAEPKAPNG-V 84
|
90 100
....*....|....*....|.
gi 568910675 139 EIKVKTAELLNACKK-LPFEI 158
Cdd:cd04316 85 EIIPEEIEVLSEAKTpLPLDP 105
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
507-581 |
3.61e-09 |
|
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: 58.33 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 507 LVLNGNEIGGGSVRIHDAQLQRYILET-------LLKEDVKLLSHLLQALDYGAPPHGGIALGLDRLVCLVTGAPSIRDV 579
Cdd:TIGR00462 209 LYIKGLELANGFHELTDAAEQRRRFEAdnalrkaLGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDV 288
|
..
gi 568910675 580 IA 581
Cdd:TIGR00462 289 LA 290
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
65-148 |
5.19e-09 |
|
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: 53.01 E-value: 5.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 65 VTLCGWIQYRRQN----TFLVLRDCHGLVQILIPQDESAASVRRIlceaPVESVVRVSGTVISRppgqenpkmPTGEIEI 140
Cdd:pfam01336 1 VTVAGRVTSIRRSggklLFLTLRDGTGSIQVVVFKEEAEKLAKKL----KEGDVVRVTGKVKKR---------KGGELEL 67
|
....*...
gi 568910675 141 KVKTAELL 148
Cdd:pfam01336 68 VVEEIELL 75
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
64-150 |
3.05e-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: 51.16 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 64 EVTLCGWIQYRR----QNTFLVLRDCHG-LVQILIPQDESAASVRRilcEAPVESVVRVSGTVISRppgQENPKMPTGEI 138
Cdd:cd04321 1 KVTLNGWIDRKPrivkKLSFADLRDPNGdIIQLVSTAKKDAFSLLK---SITAESPVQVRGKLQLK---EAKSSEKNDEW 74
|
90
....*....|..
gi 568910675 139 EIKVKTAELLNA 150
Cdd:cd04321 75 ELVVDDIQTLNA 86
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
57-589 |
5.59e-08 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 55.80 E-value: 5.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 57 RSSHLGQEVTLCGWIQYRRQN-----TFLVLRD--CHGLVQILIpqDESAASVRRILcEAPVESVVRVSGTVISRPPGQE 129
Cdd:PTZ00425 76 KNKYIDQIITVCGWSKAVRKQgggrfCFVNLNDgsCHLNLQIIV--DQSIENYEKLL-KCGVGCCFRFTGKLIISPVQNE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 130 NPKMPTGE-IEIKVKTAELLN--------ACKKLPFEIKDFVKktEALRlQYRYLDLRSFQMQYNLRLRSQMVMKMREYL 200
Cdd:PTZ00425 153 NKKGLLKEnVELALKDNSIHNfeiygenlDPQKYPLSKKNHGK--EFLR-EVAHLRPRSYFISSVIRIRNALAIATHLFF 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 201 CNlHGFVDIETPTLFKR-TPGGAKEFLVPS--REPGKFYSLPQSPQQFKqllmvGGLDRYFQVARCYRDEGSRPDR---- 273
Cdd:PTZ00425 230 QS-RGFLYIHTPLITTSdCEGGGEMFTVTTllGEDADYRAIPRVNKKNK-----KGEKREDILNTCNANNNNGNSSssna 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 274 -----QPEFTQIDIEMSFVEQTGI-----QRLVEGLLqySWPGDkdplVTPFPSMTFAEA------LATYGTDKPDTRFg 337
Cdd:PTZ00425 304 vsspaYPDQYLIDYKKDFFSKQAFltvsgQLSLENLC--SSMGD----VYTFGPTFRAENshtsrhLAEFWMIEPEIAF- 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 338 mkivdvSDVFRNTELrflqdalakPQGTVKaICVhdgAEVLpiflnakknwSSPFAKFIMEEERLE---LARSMEIQEED 414
Cdd:PTZ00425 377 ------ADLYDNMEL---------AESYIK-YCI---GYVL----------NNNFDDIYYFEENVEtglISRLKNILDED 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 415 IVLLTageHEKACSLLgklrLECADLLEMRgavlrdpavfsFLWVVDfplflakeespteLESAHHPFTAPN-------- 486
Cdd:PTZ00425 428 FAKIT---YTNVIDLL----QPYSDSFEVP-----------VKWGMD-------------LQSEHERFVAEQifkkpviv 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 487 ---SSDIHLLY---TEPEKVRGQHYDLVLNGNEIGGGSVRIHDAQ-LQRYILETLLKEDVKLLSHLLQalDYGAPPHGGI 559
Cdd:PTZ00425 477 ynyPKDLKAFYmklNEDQKTVAAMDVLVPKIGEVIGGSQREDNLErLDKMIKEKKLNMESYWWYRQLR--KFGSHPHAGF 554
|
570 580 590
....*....|....*....|....*....|
gi 568910675 560 ALGLDRLVCLVTGAPSIRDVIAFPKsYRGQ 589
Cdd:PTZ00425 555 GLGFERLIMLVTGVDNIKDTIPFPR-YPGH 583
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
64-155 |
1.04e-06 |
|
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: 47.52 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 64 EVTLCGWIQYRR---QNTFLVLRDCHGLVQILIPQDESAASVRRILcEAPVESVVRVSGTVisrppgQENPKMPTGeIEI 140
Cdd:cd04319 1 KVTLAGWVYRKRevgKKAFIVLRDSTGIVQAVFSKDLNEEAYREAK-KVGIESSVIVEGAV------KADPRAPGG-AEV 72
|
90
....*....|....*
gi 568910675 141 KVKTAELLNACKKLP 155
Cdd:cd04319 73 HGEKLEIIQNVEFFP 87
|
|
| GAD |
pfam02938 |
GAD domain; This domain is found in some members of the GatB and aspartyl tRNA synthetases. |
360-430 |
2.29e-06 |
|
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: 46.10 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 360 AKPQGTVKAICVHDGAEVLPIFLN-----AKKN------W--------SSPFAKFIMEEERLELARSMEIQEEDIVLLTA 420
Cdd:pfam02938 5 LKSGGSVKALRVPGAAGLSRKEIDelerfAKEYgakglaWikveggghTGPIAKFLTEEEVEKLLEAVGAEDGDALLFVA 84
|
90
....*....|
gi 568910675 421 GEHEKACSLL 430
Cdd:pfam02938 85 DKKKTVNKAL 94
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
497-579 |
2.45e-06 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 49.93 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 497 PEKVR-GQHYDLVLNGNEIGGGSVRIHDA--QLQRYILETLLKEDVKLLS-----HLLQALDYGAPPHGGIALGLDRLVC 568
Cdd:PRK09350 216 TEDHRvAERFEVYFKGIELANGFHELTDAreQRQRFEQDNRKRAARGLPQqpideNLIAALEAGLPDCSGVALGVDRLIM 295
|
90
....*....|.
gi 568910675 569 LVTGAPSIRDV 579
Cdd:PRK09350 296 LALGAESISEV 306
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
64-132 |
4.28e-06 |
|
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: 44.92 E-value: 4.28e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568910675 64 EVTLCGWIQ-YRRQN--TFLVLRDCHGLVQILIPQDE-----SAASVRRilceapvESVVRVSGTVISRPPGQENPK 132
Cdd:cd04323 1 RVKVFGWVHrLRSQKklMFLVLRDGTGFLQCVLSKKLvtefyDAKSLTQ-------ESSVEVTGEVKEDPRAKQAPG 70
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
551-584 |
9.08e-06 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 48.82 E-value: 9.08e-06
10 20 30
....*....|....*....|....*....|....
gi 568910675 551 YGAPPHGGIALGLDRLVCLVTGAPSIRDVIAFPK 584
Cdd:PLN02603 525 YGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPR 558
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
551-586 |
1.19e-04 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 45.25 E-value: 1.19e-04
10 20 30
....*....|....*....|....*....|....*.
gi 568910675 551 YGAPPHGGIALGLDRLVCLVTGAPSIRDVIAFPKSY 586
Cdd:PLN02532 593 HGTVKHSGFSLGFELMVLFATGLPDVRDAIPFPRSW 628
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
551-589 |
9.92e-04 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 42.29 E-value: 9.92e-04
10 20 30
....*....|....*....|....*....|....*....
gi 568910675 551 YGAPPHGGIALGLDRLVCLVTGAPSIRDVIAFPKsYRGQ 589
Cdd:PLN02221 532 YGTVKHCGFGLGFERMILFATGIDNIRDVIPFPR-YPGK 569
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
186-325 |
2.41e-03 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 40.39 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 186 LRLRSQMVMKMREYLCNlHGFVDIETPTLFKRT----PGGAKEFL-VPSRE-PGKFYSLPQSPQQFKQLlMVGGLDRYFQ 259
Cdd:PRK06462 30 LKVQSSILRYTREFLDG-RGFVEVLPPIISPSTdplmGLGSDLPVkQISIDfYGVEYYLADSMILHKQL-ALRMLGKIFY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910675 260 VARCYRDEGSRPDRQP---EFTQIDIEMSFVEQTGIQRLVEGLLQYSWPGDKDP--------------LVTPFPSMTFAE 322
Cdd:PRK06462 108 LSPNFRLEPVDKDTGRhlyEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEhedeleffgrdlphLKRPFKRITHKE 187
|
...
gi 568910675 323 ALA 325
Cdd:PRK06462 188 AVE 190
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