|
Name |
Accession |
Description |
Interval |
E-value |
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
49-637 |
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: 796.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 49 RTNTCGELRSSHLGQEVTLCGWIQYRRQN---TFLVLRDCHGLVQILIPQDES------AASVRRilceapvESVVRVSG 119
Cdd:COG0173 3 RTHYCGELRESDVGQEVTLSGWVHRRRDHgglIFIDLRDRYGITQVVFDPDDSaeafekAEKLRS-------EYVIAVTG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 120 TVISRPPGQENPKMPTGEIEIKVKTAELLNACKKLPFEIKDFVKKTEALRLQYRYLDLRSFQMQYNLRLRSQMVMKMREY 199
Cdd:COG0173 76 KVRARPEGTVNPKLPTGEIEVLASELEILNKAKTPPFQIDDDTDVSEELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 200 LCNlHGFVDIETPTLFKRTPGGAKEFLVPSR-EPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFT 278
Cdd:COG0173 156 LDE-NGFLEIETPILTKSTPEGARDYLVPSRvHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADRQPEFT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 279 QIDIEMSFVEQTGIQRLVEGLLQYSWP--GDKDpLVTPFPSMTFAEALATYGTDKPDTRFGMKIVDVSDVFRNTELRFLQ 356
Cdd:COG0173 235 QLDIEMSFVDQEDVFELMEGLIRHLFKevLGVE-LPTPFPRMTYAEAMERYGSDKPDLRFGLELVDVTDIFKDSGFKVFA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 357 DAlAKPQGTVKAICVHDGAKYLRKEdIEFIRKFAVHHFSQEVLPIFLNAKKnWSSPFAKFIMEEERLELARSMEIQEEDI 436
Cdd:COG0173 314 GA-AENGGRVKAINVPGGASLSRKQ-IDELTEFAKQYGAKGLAYIKVNEDG-LKSPIAKFLSEEELAAILERLGAKPGDL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 437 VLLTAGEHEKACSLLGKLRLECADLLEmrgavLRDPAVFSFLWVVDFPLFlakEESPTE--LESAHHPFTAPNSSDIHLL 514
Cdd:COG0173 391 IFFVADKPKVVNKALGALRLKLGKELG-----LIDEDEFAFLWVVDFPLF---EYDEEEgrWVAMHHPFTMPKDEDLDLL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 515 YTEPEKVRGQHYDLVLNGNEIGGGSVRIHDAQLQRYILETL--LKEDVKL-LSHLLQALDYGAPPHGGIALGLDRLVCLV 591
Cdd:COG0173 463 ETDPGKVRAKAYDLVLNGYELGGGSIRIHDPELQEKVFELLgiSEEEAEEkFGFLLEAFKYGAPPHGGIAFGLDRLVMLL 542
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 27369928 592 TGAPSIRDVIAFPKSYRGQDLMSNAPDSVSPEELKPYHIHVLWPAD 637
Cdd:COG0173 543 AGEDSIRDVIAFPKTQSAQDLMTGAPSEVDEKQLKELHIRLRPPEK 588
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
49-636 |
0e+00 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 775.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 49 RTNTCGELRSSHLGQEVTLCGWIQYRRQN---TFLVLRDCHGLVQILIPQD----ESAASVRRilceapvESVVRVSGTV 121
Cdd:PRK00476 4 RTHYCGELRESHVGQTVTLCGWVHRRRDHgglIFIDLRDREGIVQVVFDPDaeafEVAESLRS-------EYVIQVTGTV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 122 ISRPPGQENPKMPTGEIEIKVKTAELLNACKKLPFEIKDFVKKTEALRLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLc 201
Cdd:PRK00476 77 RARPEGTVNPNLPTGEIEVLASELEVLNKSKTLPFPIDDEEDVSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFL- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 202 NLHGFVDIETPTLFKRTPGGAKEFLVPSR-EPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQI 280
Cdd:PRK00476 156 DDNGFLEIETPILTKSTPEGARDYLVPSRvHPGKFYALPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEFTQI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 281 DIEMSFVEQTGIQRLVEGLLQYSWpgdKD----PLVTPFPSMTFAEALATYGTDKPDTRFGMKIVDVSDVFRNTELRFLQ 356
Cdd:PRK00476 236 DIEMSFVTQEDVMALMEGLIRHVF---KEvlgvDLPTPFPRMTYAEAMRRYGSDKPDLRFGLELVDVTDLFKDSGFKVFA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 357 DALAKpQGTVKAICVHDGA-KYLRKEdIEFIRKFAVHHFSQEVLPIFLNAKKnWSSPFAKFIMEEERLELARSMEIQEED 435
Cdd:PRK00476 313 GAAND-GGRVKAIRVPGGAaQLSRKQ-IDELTEFAKIYGAKGLAYIKVNEDG-LKGPIAKFLSEEELAALLERTGAKDGD 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 436 IVLLTAGEHEKACSLLGKLRLECADLLEmrgavLRDPAVFSFLWVVDFPLFLAKEESPTeLESAHHPFTAPNSSDIH-LL 514
Cdd:PRK00476 390 LIFFGADKAKVVNDALGALRLKLGKELG-----LIDEDKFAFLWVVDFPMFEYDEEEGR-WVAAHHPFTMPKDEDLDeLE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 515 YTEPEKVRGQHYDLVLNGNEIGGGSVRIHDAQLQRYILETL--LKEDVKL-LSHLLQALDYGAPPHGGIALGLDRLVCLV 591
Cdd:PRK00476 464 TTDPGKARAYAYDLVLNGYELGGGSIRIHRPEIQEKVFEILgiSEEEAEEkFGFLLDALKYGAPPHGGIAFGLDRLVMLL 543
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 27369928 592 TGAPSIRDVIAFPKSYRGQDLMSNAPDSVSPEELKPYHIHVLWPA 636
Cdd:PRK00476 544 AGADSIRDVIAFPKTQSAQDLLTGAPSPVDEKQLRELGIRLRKKE 588
|
|
| aspS_bact |
TIGR00459 |
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be ... |
49-630 |
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: 602.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 49 RTNTCGELRSSHLGQEVTLCGWIQYRRQN---TFLVLRDCHGLVQILIPQD----ESAASVRRilceapvESVVRVSGTV 121
Cdd:TIGR00459 2 RTHYCGQLRTEHLGQTVTLAGWVNRRRDLgglIFIDLRDRSGIVQVVCDPDadalKLAKGLRN-------EDVVQVKGKV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 122 ISRPPGQENPKMPTGEIEIKVKTAELLNACKKLPFEIKDfVKKTEALRLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLc 201
Cdd:TIGR00459 75 SARPEGNINRNLDTGEIEILAESITLLNKSKTPPLIIEK-TDAEEEVRLKYRYLDLRRPEMQQRLKLRHKVTKAVRNFL- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 202 NLHGFVDIETPTLFKRTPGGAKEFLVPSR-EPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQI 280
Cdd:TIGR00459 153 DQQGFLEIETPMLTKSTPEGARDYLVPSRvHKGEFYALPQSPQLFKQLLMVSGVDRYYQIARCFRDEDLRADRQPEFTQI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 281 DIEMSFVEQTGIQRLVEGLLQYSWPGDKD-PLVTPFPSMTFAEALATYGTDKPDTRFGMKIVDVSDVFRNTELRFLQdAL 359
Cdd:TIGR00459 233 DMEMSFMTQEDVMELIEKLVSHVFLEVKGiDLKKPFPVMTYAEAMERYGSDKPDLRFPLELIDVTDLFKDSEFKVFS-NL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 360 AKPQGTVKAICVHDGAKYLRKEDIEFIRKFAVHHFSQEVLPIFLNAKKNwSSPFAKFIMEEERLELARSMEIQEEDIVLL 439
Cdd:TIGR00459 312 INDGGRVKAIRVPGGWAELSRKSIKELRKFAKEYGAKGLAYLKVNEDGI-NSPIKKFLDEKKGKILLERTDAQNGDILLF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 440 TAGEHEKACSLLGKLRLECADLLEmrgavLRDPAVFSFLWVVDFPLFLAKEESptELESAHHPFTAPNSSDIHLLYTEPE 519
Cdd:TIGR00459 391 GAGSKKIVLDALGALRLKLGKDLG-----LVDPDLFSFLWVVDFPMFEKDKEG--RLCAAHHPFTMPKDEDLENLEAAPE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 520 KVRGQHYDLVLNGNEIGGGSVRIHDAQLQRYILETL---LKEDVKLLSHLLQALDYGAPPHGGIALGLDRLVCLVTGAPS 596
Cdd:TIGR00459 464 EALAEAYDLVLNGVELGGGSIRIHDPEVQKKVFEILgidPEEAREKFGFLLEAFKYGTPPHAGFALGLDRLMMLLTGTDN 543
|
570 580 590
....*....|....*....|....*....|....
gi 27369928 597 IRDVIAFPKSYRGQDLMSNAPDSVSPEELKPYHI 630
Cdd:TIGR00459 544 IRDVIAFPKTTAAACLMTEAPSFIDEKQLEELSI 577
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
36-630 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 547.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 36 SSQRIPEFSSFVARTNTCGELRSSHLGQEVTLCGWIQYRRQN---TFLVLRDCHGLVQIlIPQDESAASVRRILCEAPVE 112
Cdd:PLN02903 46 AVDSMSSQLTWPSRSHLCGALSVNDVGSRVTLCGWVDLHRDMgglTFLDVRDHTGIVQV-VTLPDEFPEAHRTANRLRNE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 113 SVVRVSGTVISRPPGQENPKMPTGEIEIKVKTAELLNAC-KKLPFEI------KDFVKktEALRLQYRYLDLRSFQMQYN 185
Cdd:PLN02903 125 YVVAVEGTVRSRPQESPNKKMKTGSVEVVAESVDILNVVtKSLPFLVttadeqKDSIK--EEVRLRYRVLDLRRPQMNAN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 186 LRLRSQMVMKMREYLCNLHGFVDIETPTLFKRTPGGAKEFLVPSR-EPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCY 264
Cdd:PLN02903 203 LRLRHRVVKLIRRYLEDVHGFVEIETPILSRSTPEGARDYLVPSRvQPGTFYALPQSPQLFKQMLMVSGFDRYYQIARCF 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 265 RDEGSRPDRQPEFTQIDIEMSFVEQTGIQRLVEGLLQYSWPGDKD-PLVTPFPSMTFAEALATYGTDKPDTRFGMKIVDV 343
Cdd:PLN02903 283 RDEDLRADRQPEFTQLDMELAFTPLEDMLKLNEDLIRQVFKEIKGvQLPNPFPRLTYAEAMSKYGSDKPDLRYGLELVDV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 344 SDVFRNTELRFLQDALAKpQGTVKAICVHDGAKY-----LRKEDI--EFIRKFAvhhfsqEVLPiFLNAKKNWSSPFAKF 416
Cdd:PLN02903 363 SDVFAESSFKVFAGALES-GGVVKAICVPDGKKIsnntaLKKGDIynEAIKSGA------KGLA-FLKVLDDGELEGIKA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 417 IME----EERLELARSMEIQEEDIVLLTAGEHEKACSLLGKLRLECADLLEMrgavlRDPAVFSFLWVVDFPLFlakEES 492
Cdd:PLN02903 435 LVEslspEQAEQLLAACGAGPGDLILFAAGPTSSVNKTLDRLRQFIAKTLDL-----IDPSRHSILWVTDFPMF---EWN 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 493 PTE--LESAHHPFTAPNSSDIHLLytepEKVRGQHYDLVLNGNEIGGGSVRIHDAQLQRYILET--LLKEDVK-LLSHLL 567
Cdd:PLN02903 507 EDEqrLEALHHPFTAPNPEDMGDL----SSARALAYDMVYNGVEIGGGSLRIYRRDVQQKVLEAigLSPEEAEsKFGYLL 582
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27369928 568 QALDYGAPPHGGIALGLDRLVCLVTGAPSIRDVIAFPKSYRGQDLMSNAPDSVSPEELKPYHI 630
Cdd:PLN02903 583 EALDMGAPPHGGIAYGLDRLVMLLAGAKSIRDVIAFPKTTTAQCALTRAPSEVDDKQLQDLSI 645
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
53-626 |
2.13e-155 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 464.84 E-value: 2.13e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 53 CGELRSSHLGQEVTLCGWIQYRRQN---TFLVLRDCHGLVQILIPQDESAASVRRILCEAPVESVVRVSGTVISRPPGQE 129
Cdd:PRK12820 9 CGHLSLDDTGREVCLAGWVDAFRDHgelLFIHLRDRNGFIQAVFSPEAAPADVYELAASLRAEFCVALQGEVQKRLEETE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 130 NPKMPTGEIEIKVKTAELLNACKKLPFEIKDFVKK-----------TEALRLQYRYLDLRSFQMQYNLRLRSQMVMKMRE 198
Cdd:PRK12820 89 NPHIETGDIEVFVRELSILAASEALPFAISDKAMTagagsagadavNEDLRLQYRYLDIRRPAMQDHLAKRHRIIKCARD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 199 YLcNLHGFVDIETPTLFKRTPGGAKEFLVPSR-EPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEF 277
Cdd:PRK12820 169 FL-DSRGFLEIETPILTKSTPEGARDYLVPSRiHPKEFYALPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 278 TQIDIEMSFVEQTGIQRLVEGLLQYSWPGDKDPLVTPFPSMTFAEALATYGTDKPDTRFGMKIVDVSDVFRNTELRFLQD 357
Cdd:PRK12820 248 TQLDIEASFIDEEFIFELIEELTARMFAIGGIALPRPFPRMPYAEAMDTTGSDRPDLRFDLKFADATDIFENTRYGIFKQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 358 ALAKpQGTVKAICVHDGAKYLRKEDIEfirkfavHHFSQEVLPIFLNAKKNW--------SSPFAKFIMEEERLELARSM 429
Cdd:PRK12820 328 ILQR-GGRIKGINIKGQSEKLSKNVLQ-------NEYAKEIAPSFGAKGMTWmraeagglDSNIVQFFSADEKEALKRRF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 430 EIQEEDIVLLTA-GEHEKACSLLGKLRLECADLLEmrgavLRDPAVFSFLWVVDFPLFLAKEESptELESAHHPFTAPNS 508
Cdd:PRK12820 400 HAEDGDVIIMIAdASCAIVLSALGQLRLHLADRLG-----LIPEGVFHPLWITDFPLFEATDDG--GVTSSHHPFTAPDR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 509 SDIHLLYTEP-EKVRGQHYDLVLNGNEIGGGSVRIHDAQLQRYILET--LLKEDVK-LLSHLLQALDYGAPPHGGIALGL 584
Cdd:PRK12820 473 EDFDPGDIEElLDLRSRAYDLVVNGEELGGGSIRINDKDIQLRIFAAlgLSEEDIEdKFGFFLRAFDFAAPPHGGIALGL 552
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 27369928 585 DRLVCLVTGAPSIRDVIAFPKSYRGQDLMSNAPDSVSPEELK 626
Cdd:PRK12820 553 DRVVSMILQTPSIREVIAFPKNRSAACPLTGAPSEVAQEQLA 594
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
186-606 |
5.60e-143 |
|
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: 417.36 E-value: 5.60e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 186 LRLRSQMVMKMREYLCNlHGFVDIETPTLFKRTPGGAKEFLVPSR-EPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCY 264
Cdd:cd00777 1 LRLRSRVIKAIRNFLDE-QGFVEIETPILTKSTPEGARDFLVPSRlHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 265 RDEGSRPDRQPEFTQIDIEMSFVEQTGIQRLVEGLLQYSWPGDKD-PLVTPFPSMTFAEALATYGtdkpdtrfgmkivdv 343
Cdd:cd00777 80 RDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGvELTTPFPRMTYAEAMERYG--------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 344 sdvfrntelrflqdalakpqgtvkaicvhdgakylrkediefirkfavhhfsqevlpiflnakknwsspfakfimeeerl 423
Cdd:cd00777 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 424 elarsmeiqeedivlltagehekacsllgklrlecadllemrgavlrdpavFSFLWVVDFPLFLaKEESPTELESAHHPF 503
Cdd:cd00777 145 ---------------------------------------------------FKFLWIVDFPLFE-WDEEEGRLVSAHHPF 172
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 504 TAPNSSDIHLLYTEPEKVRGQHYDLVLNGNEIGGGSVRIHDAQLQRYILETLLK---EDVKLLSHLLQALDYGAPPHGGI 580
Cdd:cd00777 173 TAPKEEDLDLLEKDPEDARAQAYDLVLNGVELGGGSIRIHDPDIQEKVFEILGLseeEAEEKFGFLLEAFKYGAPPHGGI 252
|
410 420
....*....|....*....|....*.
gi 27369928 581 ALGLDRLVCLVTGAPSIRDVIAFPKS 606
Cdd:cd00777 253 ALGLDRLVMLLTGSESIRDVIAFPKT 278
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
166-605 |
6.00e-117 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 351.87 E-value: 6.00e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 166 EALRLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLCNlHGFVDIETPTLFK-RTPGGAKEFLVPSREPGKFYSLPQSPQQ 244
Cdd:pfam00152 2 EETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDE-NGFLEVETPILTKsATPEGARDFLVPSRALGKFYALPQSPQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 245 FKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEMSFVEQTGIQRLVEGLLQYSW-----------PGDKDPLVT 313
Cdd:pfam00152 81 YKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFkevegiakeleGGTLLDLKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 314 PFPSMTFAEAL----------ATYGTDKPDTRFGMKIVdvsdvfrntelrflqdalakpqgtvkaicvhdgakylrkedi 383
Cdd:pfam00152 161 PFPRITYAEAIeklngkdveeLGYGSDKPDLRFLLELV------------------------------------------ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 384 efirkfavhhfsqevlpiflnakknwsspfakfimeeerlelarsmeiqeedivlltagehekacsllgklrlecadlle 463
Cdd:pfam00152 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 464 mrgavlRDPAVFSFLWVVDFPlflakeespteleSAHHPFTAPNSSDIhllytepeKVRGQHYDLVLNGNEIGGGSVRIH 543
Cdd:pfam00152 199 ------IDKNKFNPLWVTDFP-------------AEHHPFTMPKDEDD--------PALAEAFDLVLNGVEIGGGSIRIH 251
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27369928 544 DAQLQRYILETLL---KEDVKLLSHLLQALDYGAPPHGGIALGLDRLVCLVTGAPSIRDVIAFPK 605
Cdd:pfam00152 252 DPELQEERFEEQGldpEEAEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFPK 316
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
49-182 |
1.38e-63 |
|
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: 206.60 E-value: 1.38e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 49 RTNTCGELRSSHLGQEVTLCGWIQYRRQN---TFLVLRDCHGLVQILIPQDESAASvrRILCEAPVESVVRVSGTVISRP 125
Cdd:cd04317 1 RTHYCGELRESHVGQEVTLCGWVQRRRDHgglIFIDLRDRYGIVQVVFDPEEAPEF--ELAEKLRNESVIQVTGKVRARP 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 27369928 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 ... |
186-608 |
3.70e-61 |
|
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: 205.02 E-value: 3.70e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 186 LRLRSQMVMKMREYLCNlHGFVDIETPTLFKRTPG-GAKEFLVPSREPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCY 264
Cdd:cd00669 1 FKVRSKIIKAIRDFMDD-RGFLEVETPMLQKITGGaGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 265 RDEGSRPDRQPEFTQIDIEMSFVEQTGIQRLVEGLLQYSWpgdkdplvtpfpsmtfAEALATYgtdkpdtrfgmkivdvs 344
Cdd:cd00669 80 RNEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLA----------------REVLGVT----------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 345 dvfrntelrflqdalakpqgtvkaicvhdgAKYLRKEDIEFIRKFavhhfsqevlpiflnakknwsspfakfimeeERLE 424
Cdd:cd00669 127 ------------------------------AVTYGFELEDFGLPF-------------------------------PRLT 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 425 LARSMEIqeedivlltagehekacsllgklrlecadllemrgavLRDPavfsfLWVVDFPLFlakeesptelesAHHPFT 504
Cdd:cd00669 146 YREALER-------------------------------------YGQP-----LFLTDYPAE------------MHSPLA 171
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 505 APNSSDihllytePEKVRGqhYDLVLNGNEIGGGSVRIHDAQLQ-RYILETLLKEDVKLLS--HLLQALDYGAPPHGGIA 581
Cdd:cd00669 172 SPHDVN-------PEIADA--FDLFINGVEVGNGSSRLHDPDIQaEVFQEQGINKEAGMEYfeFYLKALEYGLPPHGGLG 242
|
410 420
....*....|....*....|....*..
gi 27369928 582 LGLDRLVCLVTGAPSIRDVIAFPKSYR 608
Cdd:cd00669 243 IGIDRLIMLMTNSPTIREVIAFPKMRR 269
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
49-604 |
2.03e-57 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 200.03 E-value: 2.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 49 RTNTCGELRSSHLGQEVTLCGWIQYRR---QNTFLVLRDCHGLVQILIPQDESAASVRRILcEAPVESVVRVSGTVisrp 125
Cdd:PRK05159 3 KRHLTSELTPELDGEEVTLAGWVHEIRdlgGIAFLILRDRSGIIQVVVKKKVDEELFETIK-KLKRESVVSVTGTV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 126 pgQENPKMPTGeIEIKVKTAELLN-ACKKLPFEIKDFVKKTEALRLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLCNlH 204
Cdd:PRK05159 78 --KANPKAPGG-VEVIPEEIEVLNkAEEPLPLDISGKVLAELDTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYE-N 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 205 GFVDIETPTLFKR-TPGGAKEFLVPSREPGKFysLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQ-PEFTQIDI 282
Cdd:PRK05159 154 GFTEIFTPKIVASgTEGGAELFPIDYFEKEAY--LAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRHlNEYTSIDV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 283 EMSFVE-QTGIQRLVEGLLQYswpgdkdplvtpfpsmTFAEALATYGtdkpdtrfgmkivdvsdvfrnTELRFLQDALAK 361
Cdd:PRK05159 232 EMGFIDdHEDVMDLLENLLRY----------------MYEDVAENCE---------------------KELELLGIELPV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 362 PQGTVKAIcvhdgakylrkediefirkfavhHFsqevlpiflnakknwsspfakfimeEERLELARSMEIQ---EEDivL 438
Cdd:PRK05159 275 PETPIPRI-----------------------TY-------------------------DEAIEILKSKGNEiswGDD--L 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 439 LTAGEHekacsLLGKlrlecaDLLEMRGAvlrdpavfSFLWVVDFPlflakeespteleSAHHPF-TAPNSSDihllyte 517
Cdd:PRK05159 305 DTEGER-----LLGE------YVKEEYGS--------DFYFITDYP-------------SEKRPFyTMPDEDD------- 345
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 518 PEKVRGqhYDLVLNGNEIGGGSVRIHDAQLqryiLETLLKE---DVKLLSHLLQALDYGAPPHGGIALGLDRLVCLVTGA 594
Cdd:PRK05159 346 PEISKS--FDLLFRGLEITSGGQRIHRYDM----LVESIKEkglNPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGL 419
|
570
....*....|
gi 27369928 595 PSIRDVIAFP 604
Cdd:PRK05159 420 ENIREAVLFP 429
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
49-604 |
2.57e-51 |
|
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: 183.33 E-value: 2.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 49 RTNTCGELRSSHLGQEVTLCGWIQYRRQN---TFLVLRDCHGLVQILIPQDESA--ASVRRIlceaPVESVVRVSGTVis 123
Cdd:COG0017 1 KRTYIKDLLPEHVGQEVTVAGWVRTKRDSggiSFLILRDGSGFIQVVVKKDKLEnfEEAKKL----TTESSVEVTGTV-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 124 rppgQENPKMPTGeIEIKVKTAELLNACKK-LPFEIK----DFvkktealRLQYRYLDLRSFQMQYNLRLRSQMVMKMRE 198
Cdd:COG0017 75 ----VESPRAPQG-VELQAEEIEVLGEADEpYPLQPKrhslEF-------LLDNRHLRLRTNRFGAIFRIRSELARAIRE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 199 YLcNLHGFVDIETPTLfkrTP----GGAKEFLVpsrepgKFY----SLPQSPQQFKQLlMVGGLDRYFQVARCYRDEGSR 270
Cdd:COG0017 143 FF-QERGFVEVHTPII---TAsateGGGELFPV------DYFgkeaYLTQSGQLYKEA-LAMALEKVYTFGPTFRAEKSN 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 271 PDRQ-PEFTQIDIEMSFVEQTGIQRLVEGLLQYSwpgdkdplvtpfpsmtfaealatygtdkpdtrfgmkivdVSDVFRN 349
Cdd:COG0017 212 TRRHlAEFWMIEPEMAFADLEDVMDLAEEMLKYI---------------------------------------IKYVLEN 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 350 telrflqdalakpqgtvkaicvhdgakylRKEDIEFIRKFAvhhfsqEVLPIFLNakknwsSPFAKFIMEE--ERLElAR 427
Cdd:COG0017 253 -----------------------------CPEELEFLGRDV------ERLEKVPE------SPFPRITYTEaiEILK-KS 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 428 SMEIQ-EEDIvlltAGEHEKAcslLGKlrlecadllemrgaVLRDPAVFsflwVVDFplflakeesPTELEsahhPF-TA 505
Cdd:COG0017 291 GEKVEwGDDL----GTEHERY---LGE--------------EFFKKPVF----VTDY---------PKEIK----AFyMK 332
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 506 PNSSDihllytePEKVRGqhYDLVLNG-NEIGGGSVRIHDAQLqryiLETLLKE---DVKLLSHLLQALDYGAPPHGGIA 581
Cdd:COG0017 333 PNPDD-------PKTVAA--FDLLAPGiGEIIGGSQREHRYDV----LVERIKEkglDPEDYEWYLDLRRYGSVPHAGFG 399
|
570 580
....*....|....*....|...
gi 27369928 582 LGLDRLVCLVTGAPSIRDVIAFP 604
Cdd:COG0017 400 LGLERLVMWLTGLENIREVIPFP 422
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
169-605 |
2.90e-30 |
|
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: 121.52 E-value: 2.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 169 RLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLcNLHGFVDIETPTLFKR-TPGGAKEFlvpsrePGKFYS----LPQSPQ 243
Cdd:cd00776 7 LLDNRHLDLRTPKVQAIFRIRSEVLRAFREFL-RENGFTEVHTPKITSTdTEGGAELF------KVSYFGkpayLAQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 244 QFKQlLMVGGLDRYFQVARCYRDEGSRPDRQ-PEFTQIDIEMSFVEQ-TGIQRLVEGLLQYswpgdkdplvtpfpsmTFA 321
Cdd:cd00776 80 LYKE-MLIAALERVYEIGPVFRAEKSNTRRHlSEFWMLEAEMAFIEDyNEVMDLIEELIKY----------------IFK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 322 EALATYGTDkpdtrfgMKIVDVsdvfrnteLRFLQDALAKPqgtVKAICVHDGAKYLRKEDIEFirkfavhhfsqevlpi 401
Cdd:cd00776 143 RVLERCAKE-------LELVNQ--------LNRELLKPLEP---FPRITYDEAIELLREKGVEE---------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 402 flnaKKNWsspfakfimeeerlelarsmeiqEEDIvlltAGEHEKacsLLGKLrlecadllemrgavLRDPAVFsflwVV 481
Cdd:cd00776 189 ----EVKW-----------------------GEDL----STEHER---LLGEI--------------VKGDPVF----VT 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 482 DFPlflakeespteleSAHHPFTAPNSSDihllytEPEKVRGqhYDLVLNGN-EIGGGSVRIHDAQ-LQRYILEtlLKED 559
Cdd:cd00776 217 DYP-------------KEIKPFYMKPDDD------NPETVES--FDLLMPGVgEIVGGSQRIHDYDeLEERIKE--HGLD 273
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 27369928 560 VKLLSHLLQALDYGAPPHGGIALGLDRLVCLVTGAPSIRDVIAFPK 605
Cdd:cd00776 274 PESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFPR 319
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
54-605 |
1.54e-29 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 123.28 E-value: 1.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 54 GELRSSHLGQEVTLCGWIQYRR---QNTFLVLRDCHGLVQILIPQDESAASVRRI--LCEAPVESVVRVSGTVIsrppgq 128
Cdd:PLN02850 73 SDLGEELAGSEVLIRGRVHTIRgkgKSAFLVLRQSGFTVQCVVFVSEVTVSKGMVkyAKQLSRESVVDVEGVVS------ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 129 eNPKMP----TGEIEIKVKTAELLN-ACKKLPFEIKD-----------------FVKKTEALRLQYRYLDLRSFQMQYNL 186
Cdd:PLN02850 147 -VPKKPvkgtTQQVEIQVRKIYCVSkALATLPFNVEDaarseseiekalqtgeqLVRVGQDTRLNNRVLDLRTPANQAIF 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 187 RLRSQMVMKMREYLCNlHGFVDIETPTLFK-RTPGGAKEFLVPSRepGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYR 265
Cdd:PLN02850 226 RIQSQVCNLFREFLLS-KGFVEIHTPKLIAgASEGGSAVFRLDYK--GQPACLAQSPQLHKQMAICGDFRRVFEIGPVFR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 266 DEGSRPDRQ-PEFTQIDIEMSFVEQ-TGIQRLVEGLlqyswpgdkdplvtpFPSMtFaealatygtDKPDTRFGMKIVDV 343
Cdd:PLN02850 303 AEDSFTHRHlCEFTGLDLEMEIKEHySEVLDVVDEL---------------FVAI-F---------DGLNERCKKELEAI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 344 sdvfrNTELRFlqdalakpqgtvkaicvhdgakylrkEDIEFIRKFAVHHFsqevlpiflnakknwsspfakfimeEERL 423
Cdd:PLN02850 358 -----REQYPF--------------------------EPLKYLPKTLRLTF-------------------------AEGI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 424 ELARSMEIQEEDIVLLTaGEHEKAcslLGKLrlecadLLEMRGAvlrdpavfSFLWVVDFPLflakeesptelesAHHPF 503
Cdd:PLN02850 382 QMLKEAGVEVDPLGDLN-TESERK---LGQL------VKEKYGT--------DFYILHRYPL-------------AVRPF 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 504 -TAPNSSDIhlLYTepekvrgQHYDLVLNGNEIGGGSVRIHDAQLqryiLETLLKE---DVKLLSHLLQALDYGAPPHGG 579
Cdd:PLN02850 431 yTMPCPDDP--KYS-------NSFDVFIRGEEIISGAQRVHDPEL----LEKRAEEcgiDVKTISTYIDSFRYGAPPHGG 497
|
570 580
....*....|....*....|....*.
gi 27369928 580 IALGLDRLVCLVTGAPSIRDVIAFPK 605
Cdd:PLN02850 498 FGVGLERVVMLFCGLNNIRKTSLFPR 523
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
49-604 |
1.37e-24 |
|
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: 107.81 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 49 RTNTCGELRSSH--------LGQEVTLCGWIQYRR---QNTFLVLRDCHGLVQILIPQDEsaasvrriLCEAPVESV--- 114
Cdd:COG1190 35 RTHTAAEIREKYdeleaeeeTGDEVSVAGRIMAKRdmgKASFADLQDGSGRIQLYLRRDE--------LGEEAYELFkll 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 115 -----VRVSGTVI-SRppgqenpkmpTGEIEIKVKTAELLN-ACKKLP---FEIKDfvkkTEaLRLQYRYLDL----RSF 180
Cdd:COG1190 107 dlgdiVGVEGTVFrTK----------TGELSVKVEELTLLSkSLRPLPekfHGLTD----PE-TRYRQRYVDLivnpEVR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 181 QMqynLRLRSQMVMKMREYLcNLHGFVDIETPTLfKRTPGGA--KEF--------------------Lvpsrepgkfysl 238
Cdd:COG1190 172 ET---FRKRSKIIRAIRRFL-DERGFLEVETPML-QPIAGGAaaRPFithhnaldmdlylriapelyL------------ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 239 pqspqqfKQLLmVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEMSFVEQTGIQRLVEGLLQYSwpgdkdplvtpfpsm 318
Cdd:COG1190 235 -------KRLI-VGGFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREA--------------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 319 tfaeALATYGTDKpdTRFGMKIVDVSDVFRntelrflqdalakpqgtvkaicvhdgakylRKEDIEFIRKFAVHHFSQev 398
Cdd:COG1190 292 ----AEAVLGTTK--VTYQGQEIDLSPPWR------------------------------RITMVEAIKEATGIDVTP-- 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 399 lpiflnakknwsspfakfIMEEERL-ELARSMEIQEEDivllTAGehekacslLGKLrlecadLLEMRGAV----LRDPa 473
Cdd:COG1190 334 ------------------LTDDEELrALAKELGIEVDP----GWG--------RGKL------IDELFEELvepkLIQP- 376
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 474 VFsflwVVDFPlflaKEESPtelesahhpFTAPNSSDihllytePEKV-RgqhYDLVLNGNEIGGGSVRIHDAQLQRYIL 552
Cdd:COG1190 377 TF----VTDYP----VEVSP---------LAKRHRDD-------PGLTeR---FELFIAGREIANAFSELNDPIDQRERF 429
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27369928 553 ETLLK-------------EDvkllshLLQALDYGAPPHGGIALGLDRLVCLVTGAPSIRDVIAFP 604
Cdd:COG1190 430 EEQLElkaagddeampmdED------FLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 488
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
79-605 |
2.66e-24 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 107.39 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 79 FLVLRDCHGLVQILIP-QDESAASVRRILCEAPVESVVRVSGTVIsrppGQENPKMPTG--EIEIKVKTAELLN-ACKKL 154
Cdd:PTZ00401 98 FMVLRDGSDSVQAMAAvEGDVPKEMIDFIGQIPTESIVDVEATVC----KVEQPITSTShsDIELKVKKIHTVTeSLRTL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 155 PFEIKDFVKKTEA--------LRLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLCNlHGFVDIETPTLFKR-TPGGAKEF 225
Cdd:PTZ00401 174 PFTLEDASRKESDegakvnfdTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLID-SDFCEIHSPKIINApSEGGANVF 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 226 LVPSREpgKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQ-PEFTQIDIEMSFVEQTgiqrlvegllqysw 304
Cdd:PTZ00401 253 KLEYFN--RFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHlTEFVGLDVEMRINEHY-------------- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 305 pgdkdplvtpFPSMTFAEALATYgtdkpdtrfgmkivdvsdVFRNtelrflqdaLAKPQGTVKAIC-VHDGAKYLRKEDI 383
Cdd:PTZ00401 317 ----------YEVLDLAESLFNY------------------IFER---------LATHTKELKAVCqQYPFEPLVWKLTP 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 384 EFIRKFAVHHFSQEVLP--IFLNAKKNWSSpfakfimeeerlelaRSMEIQEEDIVLLTAGEHEKACSLLGKLRLECADL 461
Cdd:PTZ00401 360 ERMKELGVGVISEGVEPtdKYQARVHNMDS---------------RMLRINYMHCIELLNTVLEEKMAPTDDINTTNEKL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 462 LemrGAVLRDPAVFSFLWVVDFPlflakeespteleSAHHPF-TAPNSSDIHLLYTepekvrgqhYDLVLNGNEIGGGSV 540
Cdd:PTZ00401 425 L---GKLVKERYGTDFFISDRFP-------------SSARPFyTMECKDDERFTNS---------YDMFIRGEEISSGAQ 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27369928 541 RIHDAQ--LQRyilETLLKEDVKLLSHLLQALDYGAPPHGGIALGLDRLVCLVTGAPSIRDVIAFPK 605
Cdd:PTZ00401 480 RIHDPDllLAR---AKMLNVDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPR 543
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
34-604 |
2.30e-22 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 100.93 E-value: 2.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 34 ALSSQRIPEFSSFVARTNTCGELRSSH----------LGQEVTLCGWIQYRR---QNTFLVLRDCHGLVQILIPQDEsaa 100
Cdd:PRK00484 16 ELREQGIDPYPNKFERTHTAAELRAKYddkekeeleeLEIEVSVAGRVMLKRvmgKASFATLQDGSGRIQLYVSKDD--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 101 svrriLCEAPVESV--------VRVSGTVIsrppgqenpKMPTGEIEIKVKTAELLN-ACKKLPfeikdfVK----KTEA 167
Cdd:PRK00484 93 -----VGEEALEAFkkldlgdiIGVEGTLF---------KTKTGELSVKATELTLLTkSLRPLP------DKfhglTDVE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 168 LRLQYRYLDL----RSFQMqynLRLRSQMVMKMREYLCNlHGFVDIETPTLfKRTPGG--AKEFL-------VPsrepgk 234
Cdd:PRK00484 153 TRYRQRYVDLivnpESRET---FRKRSKIISAIRRFLDN-RGFLEVETPML-QPIAGGaaARPFIthhnaldID------ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 235 FYsLPQSPQQF-KQLLmVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEMSFVEQTGIQRLVEGLLQYSwpgdkdplvt 313
Cdd:PRK00484 222 LY-LRIAPELYlKRLI-VGGFERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHL---------- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 314 pfpsmtfaeALATYGTDKpdTRFGMKIVDVSDVFRntELRFlqdalakpqgtVKAICVHDGAKyLRKEDIEFIRKFAVHH 393
Cdd:PRK00484 290 ---------AQAVLGTTK--VTYQGTEIDFGPPFK--RLTM-----------VDAIKEYTGVD-FDDMTDEEARALAKEL 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 394 FsqevlpifLNAKKNWSspFAKFIMEeerlelarsmeIQEEdivllTAGEHekacsllgklrlecadllemrgavLRDPa 473
Cdd:PRK00484 345 G--------IEVEKSWG--LGKLINE-----------LFEE-----FVEPK------------------------LIQP- 373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 474 vfSFlwVVDFPlflaKEESPtelesahhpFTAPNSSDIHLlyTEpekvRgqhYDLVLNGNEIGGGSVRIHDA--QLQRYI 551
Cdd:PRK00484 374 --TF--ITDYP----VEISP---------LAKRHREDPGL--TE----R---FELFIGGREIANAFSELNDPidQRERFE 427
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27369928 552 LETLLK-----------EDvkllshLLQALDYGAPPHGGIALGLDRLVCLVTGAPSIRDVIAFP 604
Cdd:PRK00484 428 AQVEAKeagddeamfmdED------FLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
186-604 |
1.50e-21 |
|
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: 96.11 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 186 LRLRSQMVMKMREYLCNlHGFVDIETPTLfKRTPGG--AKEFLVPSREPG-KFYsLPQSPQQFKQLLMVGGLDRYFQVAR 262
Cdd:cd00775 8 FIVRSKIISYIRKFLDD-RGFLEVETPML-QPIAGGaaARPFITHHNALDmDLY-LRIAPELYLKRLIVGGFERVYEIGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 263 CYRDEGSRPDRQPEFTQIDIEMSFVEQTGIQRLVEGLLQYSwpgdkdplvtpfpsmtfaeALATYGTDKPDtrfgmkivd 342
Cdd:cd00775 85 NFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGL-------------------VKKINGKTKIE--------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 343 vsdvFRNTELRFlqdalaKPqgtvkaicvhdgaKYLRKEDIEFIRkfavhhfsqEVLPIFLNAKknwsspfAKFIMEEER 422
Cdd:cd00775 137 ----YGGKELDF------TP-------------PFKRVTMVDALK---------EKTGIDFPEL-------DLEQPEELA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 423 LELARSmeiqeedivlltAGEHEKACSLLGKLRLECAD-LLEMRgavLRDPAVfsflwVVDFPlflaKEESPteLESAHH 501
Cdd:cd00775 178 KLLAKL------------IKEKIEKPRTLGKLLDKLFEeFVEPT---LIQPTF-----IIDHP----VEISP--LAKRHR 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 502 pftapnssdihllyTEPEKVrgQHYDLVLNGNEIGGGSVRIHDAQLQRYILETLLK-------EDVKLLSHLLQALDYGA 574
Cdd:cd00775 232 --------------SNPGLT--ERFELFICGKEIANAYTELNDPFDQRERFEEQAKqkeagddEAMMMDEDFVTALEYGM 295
|
410 420 430
....*....|....*....|....*....|
gi 27369928 575 PPHGGIALGLDRLVCLVTGAPSIRDVIAFP 604
Cdd:cd00775 296 PPTGGLGIGIDRLVMLLTDSNSIRDVILFP 325
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
64-149 |
2.99e-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: 2.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 64 EVTLCGWIQYRRQN---TFLVLRDCHGLVQILIPQDESAASVRRILcEAPVESVVRVSGTVISRPPGQenpkMPTGEIEI 140
Cdd:cd04100 1 EVTLAGWVHSRRDHgglIFIDLRDGSGIVQVVVNKEELGEFFEEAE-KLRTESVVGVTGTVVKRPEGN----LATGEIEL 75
|
....*....
gi 27369928 141 KVKTAELLN 149
Cdd:cd04100 76 QAEELEVLS 84
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
44-604 |
3.97e-21 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 97.05 E-value: 3.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 44 SSFVARTNTcgELRSshLGQEVTLCGWIQYRR---QNTFLVLRDCHGLVQILIPQDESAASV-RRILCEAPVESVVRVSG 119
Cdd:PRK12445 51 EEFDAKDNQ--ELES--LNIEVSVAGRMMTRRimgKASFVTLQDVGGRIQLYVARDSLPEGVyNDQFKKWDLGDIIGARG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 120 TVIsrppgqenpKMPTGEIEIKVKTAELLN-ACKKLPFEIKDFvkKTEALRLQYRYLDL-RSFQMQYNLRLRSQMVMKMR 197
Cdd:PRK12445 127 TLF---------KTQTGELSIHCTELRLLTkALRPLPDKFHGL--QDQEVRYRQRYLDLiANDKSRQTFVVRSKILAAIR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 198 EYLCnLHGFVDIETPtLFKRTPGGA--KEFLVPSREPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQP 275
Cdd:PRK12445 196 QFMV-ARGFMEVETP-MMQVIPGGAsaRPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 276 EFTQIDIEMSFVEQTGIQRLVEGLLQyswpgdkdplvtpfpsmtfaeALATYGTDKPDTRFGMKIVDVSDVFRNTELRfl 355
Cdd:PRK12445 274 EFTMMELYMAYADYHDLIELTESLFR---------------------TLAQEVLGTTKVTYGEHVFDFGKPFEKLTMR-- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 356 qDALAK--PQGTVKAICVHDGAKYLRKEdiefirkfavhhfsqevlpIFLNAKKNWSspfakfimeeerlelarsmeiqe 433
Cdd:PRK12445 331 -EAIKKyrPETDMADLDNFDAAKALAES-------------------IGITVEKSWG----------------------- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 434 edivlltagehekacslLGKLRLECADllEMRGAVLRDPAvfsflWVVDFPlflaKEESPTelesAHHPFTAPNSSDihl 513
Cdd:PRK12445 368 -----------------LGRIVTEIFD--EVAEAHLIQPT-----FITEYP----AEVSPL----ARRNDVNPEITD--- 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 514 lytepekvrgqHYDLVLNGNEIGGGSVRIHDA--QLQRYILETLLK-----EDVKLLSHLLQALDYGAPPHGGIALGLDR 586
Cdd:PRK12445 413 -----------RFEFFIGGREIGNGFSELNDAedQAERFQEQVNAKaagddEAMFYDEDYVTALEYGLPPTAGLGIGIDR 481
|
570
....*....|....*...
gi 27369928 587 LVCLVTGAPSIRDVIAFP 604
Cdd:PRK12445 482 MIMLFTNSHTIRDVILFP 499
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
62-604 |
7.78e-20 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 93.52 E-value: 7.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 62 GQEVTLCGWIQYRRQN---TFLVLRDCHGLVQILIPQ---DESAASVRRILCEAPVESVVRVSGTvisrpPGqenpKMPT 135
Cdd:PLN02502 108 DVSVSVAGRIMAKRAFgklAFYDLRDDGGKIQLYADKkrlDLDEEEFEKLHSLVDRGDIVGVTGT-----PG----KTKK 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 136 GEIEIKVKTAELLNAC-KKLP---FEIKDFVKktealRLQYRYLDL-RSFQMQYNLRLRSQMVMKMREYLCNLhGFVDIE 210
Cdd:PLN02502 179 GELSIFPTSFEVLTKClLMLPdkyHGLTDQET-----RYRQRYLDLiANPEVRDIFRTRAKIISYIRRFLDDR-GFLEVE 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 211 TPTLfKRTPGGA--KEFLVPSREPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEMSFve 288
Cdd:PLN02502 253 TPML-NMIAGGAaaRPFVTHHNDLNMDLYLRIATELHLKRLVVGGFERVYEIGRQFRNEGISTRHNPEFTTCEFYQAY-- 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 289 qtgiqrlvegllqyswpgdkdplvtpfpsmtfaealatygtdkpdtrfgmkiVDVSDVFRNTELRFlqdalakpQGTVKA 368
Cdd:PLN02502 330 ----------------------------------------------------ADYNDMMELTEEMV--------SGMVKE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 369 ICvhdGAKYLRKEDIEF-----IRKFAVHHFSQEVLPIFLNakknwsspfakfimeeerlELARSMEIQEEDIVLLTAGE 443
Cdd:PLN02502 350 LT---GSYKIKYHGIEIdftppFRRISMISLVEEATGIDFP-------------------ADLKSDEANAYLIAACEKFD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 444 HE-KACSLLGKLrlecadLLEMRGAVLRDPAV---FsflwVVDFPlflaKEESPteLESAH--HPFTapnssdihllyTE 517
Cdd:PLN02502 408 VKcPPPQTTGRL------LNELFEEFLEETLVqptF----VLDHP----VEMSP--LAKPHrsKPGL-----------TE 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 518 pekvrgqHYDLVLNGNEIGGGSVRIHDAQLQRYILETLLK-------EDVKLLSHLLQALDYGAPPHGGIALGLDRLVCL 590
Cdd:PLN02502 461 -------RFELFINGRELANAFSELTDPVDQRERFEEQVKqhnagddEAMALDEDFCTALEYGLPPTGGWGLGIDRLVML 533
|
570
....*....|....
gi 27369928 591 VTGAPSIRDVIAFP 604
Cdd:PLN02502 534 LTDSASIRDVIAFP 547
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
47-604 |
1.57e-19 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 93.49 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 47 VARTNTCGELRSSHLGQEVTLCGWIQYRRQN---TFLVLRDCHGLVQILIPQDES-AASVRRILCEAPVESVVRVSGTVI 122
Cdd:PRK02983 636 VPPTHTVAEALDAPTGEEVSVSGRVLRIRDYggvLFADLRDWSGELQVLLDASRLeQGSLADFRAAVDLGDLVEVTGTMG 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 123 -SRppgqenpkmpTGEIEIKVKTAELLNAC-KKLPFEIKDFVKKtEAlRLQYRYLDL----RSFQMqynLRLRSQMVMKM 196
Cdd:PRK02983 716 tSR----------NGTLSLLVTSWRLAGKClRPLPDKWKGLTDP-EA-RVRQRYLDLavnpEARDL---LRARSAVVRAV 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 197 REYLcNLHGFVDIETPTLfKRTPGGA--KEFLVPSREpgkfYSLPQ----SPQQFKQLLMVGGLDRYFQVARCYRDEGSR 270
Cdd:PRK02983 781 RETL-VARGFLEVETPIL-QQVHGGAnaRPFVTHINA----YDMDLylriAPELYLKRLCVGGVERVFELGRNFRNEGVD 854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 271 PDRQPEFTQIDIEMSFVEQTGIQRLVEGLLQyswpgdkdplvtpfpsmtfAEALATYGTD---KPDTRFGMKIVDVSDVF 347
Cdd:PRK02983 855 ATHNPEFTLLEAYQAHADYDTMRDLTRELIQ-------------------NAAQAAHGAPvvmRPDGDGVLEPVDISGPW 915
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 348 RntelrflqdalakpqgtvkAICVHDgakylrkediefirkfAVHH-FSQEVLPiflnakknwSSPFakfimeEERLELA 426
Cdd:PRK02983 916 P-------------------VVTVHD----------------AVSEaLGEEIDP---------DTPL------AELRKLC 945
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 427 RSMEIQeedivlltAGEHEKAcsllGKLrlecadLLEMRGAVLRDPAVF-SFlwVVDFPLflakEESptelesahhPFTA 505
Cdd:PRK02983 946 DAAGIP--------YRTDWDA----GAV------VLELYEHLVEDRTTFpTF--YTDFPT----SVS---------PLTR 992
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 506 PNSSDIHLlytepekvrGQHYDLVLNGNEIGGGSVRIHDAQLQRYILE--TLLK-----EDVKLLSHLLQALDYGAPPHG 578
Cdd:PRK02983 993 PHRSDPGL---------AERWDLVAWGVELGTAYSELTDPVEQRRRLTeqSLLAaggdpEAMELDEDFLQALEYAMPPTG 1063
|
570 580
....*....|....*....|....*.
gi 27369928 579 GIALGLDRLVCLVTGApSIRDVIAFP 604
Cdd:PRK02983 1064 GLGMGVDRLVMLLTGR-SIRETLPFP 1088
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
204-304 |
5.28e-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: 71.38 E-value: 5.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 204 HGFVDIETP-----TLFKRTPGGAKEFLVPSREPGKFYSLPQSPQQFKQLLMVGGL----DRYFQVARCYRDEGSR--PD 272
Cdd:cd00768 16 LGFQEVETPiverePLLEKAGHEPKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIrklpLRLAEIGPAFRNEGGRrgLR 95
|
90 100 110
....*....|....*....|....*....|..
gi 27369928 273 RQPEFTQIDIEMsFVEQTGIQRLVEGLLQYSW 304
Cdd:cd00768 96 RVREFTQLEGEV-FGEDGEEASEFEELIELTE 126
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
56-608 |
9.16e-14 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 73.99 E-value: 9.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 56 LRSSHLGQEVTLCGWIQYRRQN---TFLVLRDCHGLVQILIPQDESAASVRRILcEAPVESVVRVSGTVIsrppgqENPK 132
Cdd:PRK03932 10 LKGKYVGQEVTVRGWVRTKRDSgkiAFLQLRDGSCFKQLQVVKDNGEEYFEEIK-KLTTGSSVIVTGTVV------ESPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 133 MPTGeIEIKVKTAELLNACKKlPFEIKdfvKK---TEALRlQYRYLDLRSFQMQYNLRLRSQMVMKMREYLcNLHGFVDI 209
Cdd:PRK03932 83 AGQG-YELQATKIEVIGEDPE-DYPIQ---KKrhsIEFLR-EIAHLRPRTNKFGAVMRIRNTLAQAIHEFF-NENGFVWV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 210 ETPTLfkrTPG---GAKE-FLVPSREP-------GKFYSLPQSpqqfKQL---LMVGGLDRYFQVARCYRDEGSRPDRQ- 274
Cdd:PRK03932 156 DTPII---TASdceGAGElFRVTTLDLdfskdffGKEAYLTVS----GQLyaeAYAMALGKVYTFGPTFRAENSNTRRHl 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 275 PEFTQIDIEMSFVEQTGIQRLVEGLLQYSwpgdkdplvtpfpsmtfaealatygtdkpdtrfgmkivdVSDVFRN--TEL 352
Cdd:PRK03932 229 AEFWMIEPEMAFADLEDNMDLAEEMLKYV---------------------------------------VKYVLENcpDDL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 353 RFLqdalakpqgtvkaicvhdgAKYLRKEDIEFIRKFAVHHFSQ----EVLPIFLNAKKnwsspfaKFimeeerlelars 428
Cdd:PRK03932 270 EFL-------------------NRRVDKGDIERLENFIESPFPRitytEAIEILQKSGK-------KF------------ 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 429 mEIQEE---DIvlltAGEHEKAcslLGKLRLECadllemrgavlrdPaVFsflwVVDFPlflakeesptelesahhpfta 505
Cdd:PRK03932 312 -EFPVEwgdDL----GSEHERY---LAEEHFKK-------------P-VF----VTNYP--------------------- 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 506 pnsSDIHLLYTEP----EKVRGqhYDLVLNG-NEIGGGSVRIHDaqlqryiLETLLK--EDVKL-LSHLLQALD---YGA 574
Cdd:PRK03932 345 ---KDIKAFYMRLnpdgKTVAA--MDLLAPGiGEIIGGSQREER-------LDVLEAriKELGLnKEDYWWYLDlrrYGS 412
|
570 580 590
....*....|....*....|....*....|....
gi 27369928 575 PPHGGIALGLDRLVCLVTGAPSIRDVIAFPKSYR 608
Cdd:PRK03932 413 VPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPG 446
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
132-604 |
5.90e-13 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 71.99 E-value: 5.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 132 KMPTGEIEIKVKTAELLNackklPFEIKDFVK----------KTEALRLQYRYLDLRSFQMQYN-LRLRSQMVMKMREYL 200
Cdd:PTZ00385 173 RMQRGELSVAASRMLILS-----PYVCTDQVVcpnlrgftvlQDNDVKYRYRFTDMMTNPCVIEtIKKRHVMLQALRDYF 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 201 cNLHGFVDIETPTLFKRTPGG-AKEFLVPSREPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTq 279
Cdd:PTZ00385 248 -NERNFVEVETPVLHTVASGAnAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFT- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 280 idiemsfveqtgiqrlvegllqyswpgdkdplvtpfpSMTFAEALATYgtdkpdtrfgmkivdvSDVFRNTELRFLQDAL 359
Cdd:PTZ00385 326 -------------------------------------SCEFYAAYHTY----------------EDLMPMTEDIFRQLAM 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 360 AKPQGTVKAICVHDGAKYLRKEDI-EFIRKFAVHHFSQEVLPIFLNAKKNWSSPFAKFIMeeerlelarSMEIQEEDIVL 438
Cdd:PTZ00385 353 RVNGTTVVQIYPENAHGNPVTVDLgKPFRRVSVYDEIQRMSGVEFPPPNELNTPKGIAYM---------SVVMLRYNIPL 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 439 LTAgehEKACSLLGKLrlecADLLEMRGAVlrDPAvfsflWVVDFPLFLakeeSPTELESAHHPFTApnssdihllytep 518
Cdd:PTZ00385 424 PPV---RTAAKMFEKL----IDFFITDRVV--EPT-----FVMDHPLFM----SPLAKEQVSRPGLA------------- 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 519 ekvrgQHYDLVLNGNEIGGGSVRIHDAQLQRYILETLL-------KEDVKLLSHLLQALDYGAPPHGGIALGLDRLVCLV 591
Cdd:PTZ00385 473 -----ERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLvdrqggdEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLL 547
|
490
....*....|...
gi 27369928 592 TGAPSIRDVIAFP 604
Cdd:PTZ00385 548 TNSSNIRDGIIFP 560
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
132-604 |
4.50e-12 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 68.88 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 132 KMPTGEIEIKVKTAELLNAC-KKLPfeIKDFVKKTEaLRLQYRYLDLR-SFQMQYNLRLRSQMVMKMREYLcNLHGFVDI 209
Cdd:PTZ00417 200 KSKKGELSIFPKETIILSPClHMLP--MKYGLKDTE-IRYRQRYLDLMiNESTRSTFITRTKIINYLRNFL-NDRGFIEV 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 210 ETPTLfKRTPGGA--KEFLVPSREPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEMSFV 287
Cdd:PTZ00417 276 ETPTM-NLVAGGAnaRPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYA 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 288 EQTGIQRLVEGLLQ-------------YSWPG-DKDPL----VTPFPSMTFAEALatygtdkpdtrfgmkivdvsDVFRN 349
Cdd:PTZ00417 355 DFYDLIKWSEDFFSqlvmhlfgtykilYNKDGpEKDPIeidfTPPYPKVSIVEEL--------------------EKLTN 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 350 TElrfLQDALAKPQGTVKAICVhdgakyLRKEDIEFIRKFAVHHFSQEVLPIFLNAKKNwSSPFakFIMeeerlelarsm 429
Cdd:PTZ00417 415 TK---LEQPFDSPETINKMINL------IKENKIEMPNPPTAAKLLDQLASHFIENKYP-NKPF--FII----------- 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 430 eiqeedivlltagEHEKACSLLGKLRLECADLLEMrgavlrdpavfsflwvvdFPLFLAKEESPTELESAHHPFtapnss 509
Cdd:PTZ00417 472 -------------EHPQIMSPLAKYHRSKPGLTER------------------LEMFICGKEVLNAYTELNDPF------ 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 510 dihllyTEPEKVRGQHYDlvlngNEIGggsvrihDAqlqryiletllkEDVKLLSHLLQALDYGAPPHGGIALGLDRLVC 589
Cdd:PTZ00417 515 ------KQKECFSAQQKD-----REKG-------DA------------EAFQFDAAFCTSLEYGLPPTGGLGLGIDRITM 564
|
490
....*....|....*
gi 27369928 590 LVTGAPSIRDVIAFP 604
Cdd:PTZ00417 565 FLTNKNCIKDVILFP 579
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
62-158 |
5.30e-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: 5.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 62 GQEVTLCGWIQYRRQ---NTFLVLRDCHGLVQILIPQDESAASVRRILCEAPVESVVRVSGTVisrppgQENPKMPTGeI 138
Cdd:cd04316 12 GEEVTVAGWVHEIRDlggIKFVILRDREGIVQVTAPKKKVDKELFKTVRKLSRESVISVTGTV------KAEPKAPNG-V 84
|
90 100
....*....|....*....|.
gi 27369928 139 EIKVKTAELLNACKK-LPFEI 158
Cdd:cd04316 85 EIIPEEIEVLSEAKTpLPLDP 105
|
|
| GAD |
pfam02938 |
GAD domain; This domain is found in some members of the GatB and aspartyl tRNA synthetases. |
360-451 |
1.96e-10 |
|
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: 57.66 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 360 AKPQGTVKAICVHDGAKYLRKEdIEFIRKFAVHHFSQEVlpIFLNAKKN-WSSPFAKFIMEEERLELARSMEIQEEDIVL 438
Cdd:pfam02938 5 LKSGGSVKALRVPGAAGLSRKE-IDELERFAKEYGAKGL--AWIKVEGGgHTGPIAKFLTEEEVEKLLEAVGAEDGDALL 81
|
90
....*....|...
gi 27369928 439 LTAGEHEKACSLL 451
Cdd:pfam02938 82 FVADKKKTVNKAL 94
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
528-602 |
3.81e-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: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 528 LVLNGNEIGGGSVRIHDAQLQRYILET-------LLKEDVKLLSHLLQALDYGAPPHGGIALGLDRLVCLVTGAPSIRDV 600
Cdd:TIGR00462 209 LYIKGLELANGFHELTDAAEQRRRFEAdnalrkaLGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDV 288
|
..
gi 27369928 601 IA 602
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 |
5.37e-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: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 65 VTLCGWIQYRRQN----TFLVLRDCHGLVQILIPQDESAASVRRIlceaPVESVVRVSGTVISRppgqenpkmPTGEIEI 140
Cdd:pfam01336 1 VTVAGRVTSIRRSggklLFLTLRDGTGSIQVVVFKEEAEKLAKKL----KEGDVVRVTGKVKKR---------KGGELEL 67
|
....*...
gi 27369928 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 |
3.45e-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: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 64 EVTLCGWIQYRR----QNTFLVLRDCHG-LVQILIPQDESAASVRRilcEAPVESVVRVSGTVISRppgQENPKMPTGEI 138
Cdd:cd04321 1 KVTLNGWIDRKPrivkKLSFADLRDPNGdIIQLVSTAKKDAFSLLK---SITAESPVQVRGKLQLK---EAKSSEKNDEW 74
|
90
....*....|..
gi 27369928 139 EIKVKTAELLNA 150
Cdd:cd04321 75 ELVVDDIQTLNA 86
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
495-610 |
1.17e-06 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 51.56 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 495 ELESAHHPFTAPN-----------SSDIHLLY---TEPEKVRGQHYDLVLNGNEIGGGSVRIHDAQ-LQRYILETLLKED 559
Cdd:PTZ00425 456 DLQSEHERFVAEQifkkpvivynyPKDLKAFYmklNEDQKTVAAMDVLVPKIGEVIGGSQREDNLErLDKMIKEKKLNME 535
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 27369928 560 VKLLSHLLQalDYGAPPHGGIALGLDRLVCLVTGAPSIRDVIAFPKsYRGQ 610
Cdd:PTZ00425 536 SYWWYRQLR--KFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPR-YPGH 583
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
64-155 |
1.21e-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: 47.13 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 64 EVTLCGWIQYRR---QNTFLVLRDCHGLVQILIPQDESAASVRRILcEAPVESVVRVSGTVisrppgQENPKMPTGeIEI 140
Cdd:cd04319 1 KVTLAGWVYRKRevgKKAFIVLRDSTGIVQAVFSKDLNEEAYREAK-KVGIESSVIVEGAV------KADPRAPGG-AEV 72
|
90
....*....|....*
gi 27369928 141 KVKTAELLNACKKLP 155
Cdd:cd04319 73 HGEKLEIIQNVEFFP 87
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
518-600 |
3.03e-06 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 49.54 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 518 PEKVR-GQHYDLVLNGNEIGGGSVRIHDA--QLQRYILETLLKEDVKLLS-----HLLQALDYGAPPHGGIALGLDRLVC 589
Cdd:PRK09350 216 TEDHRvAERFEVYFKGIELANGFHELTDAreQRQRFEQDNRKRAARGLPQqpideNLIAALEAGLPDCSGVALGVDRLIM 295
|
90
....*....|.
gi 27369928 590 LVTGAPSIRDV 600
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 |
4.70e-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: 4.70e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27369928 64 EVTLCGWIQ-YRRQN--TFLVLRDCHGLVQILIPQDE-----SAASVRRilceapvESVVRVSGTVISRPPGQENPK 132
Cdd:cd04323 1 RVKVFGWVHrLRSQKklMFLVLRDGTGFLQCVLSKKLvtefyDAKSLTQ-------ESSVEVTGEVKEDPRAKQAPG 70
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
572-605 |
9.50e-06 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 48.82 E-value: 9.50e-06
10 20 30
....*....|....*....|....*....|....
gi 27369928 572 YGAPPHGGIALGLDRLVCLVTGAPSIRDVIAFPK 605
Cdd:PLN02603 525 YGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPR 558
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
572-607 |
1.26e-04 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 45.25 E-value: 1.26e-04
10 20 30
....*....|....*....|....*....|....*.
gi 27369928 572 YGAPPHGGIALGLDRLVCLVTGAPSIRDVIAFPKSY 607
Cdd:PLN02532 593 HGTVKHSGFSLGFELMVLFATGLPDVRDAIPFPRSW 628
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
572-610 |
1.03e-03 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 42.29 E-value: 1.03e-03
10 20 30
....*....|....*....|....*....|....*....
gi 27369928 572 YGAPPHGGIALGLDRLVCLVTGAPSIRDVIAFPKsYRGQ 610
Cdd:PLN02221 532 YGTVKHCGFGLGFERMILFATGIDNIRDVIPFPR-YPGK 569
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
186-325 |
3.12e-03 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 40.39 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 186 LRLRSQMVMKMREYLCNlHGFVDIETPTLFKRT----PGGAKEFL-VPSRE-PGKFYSLPQSPQQFKQLlMVGGLDRYFQ 259
Cdd:PRK06462 30 LKVQSSILRYTREFLDG-RGFVEVLPPIISPSTdplmGLGSDLPVkQISIDfYGVEYYLADSMILHKQL-ALRMLGKIFY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369928 260 VARCYRDEGSRPDRQP---EFTQIDIEMSFVEQTGIQRLVEGLLQYSWPGDKDP--------------LVTPFPSMTFAE 322
Cdd:PRK06462 108 LSPNFRLEPVDKDTGRhlyEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEhedeleffgrdlphLKRPFKRITHKE 187
|
...
gi 27369928 323 ALA 325
Cdd:PRK06462 188 AVE 190
|
|
| |
