|
Name |
Accession |
Description |
Interval |
E-value |
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
50-599 |
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: 705.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 50 RTNTCGELRSSHLGQEVTLCGWIQYRRQN---TFLVLRDFDGLVQVIIPQDESAASVKKILcEAPVESVVQVSGTVISRP 126
Cdd:COG0173 3 RTHYCGELRESDVGQEVTLSGWVHRRRDHgglIFIDLRDRYGITQVVFDPDDSAEAFEKAE-KLRSEYVIAVTGKVRARP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 127 AGQENPKMPTGEIEIKVKTAELLNACKKLPFEIKNFVKKTEALRLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLCNlHG 206
Cdd:COG0173 82 EGTVNPKLPTGEIEVLASELEILNKAKTPPFQIDDDTDVSEELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDE-NG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 207 FVDIETPTLFKRTPGGAKEFLVPSR-EPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEM 285
Cdd:COG0173 161 FLEIETPILTKSTPEGARDYLVPSRvHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADRQPEFTQLDIEM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 286 SFVDQTGIQSLIEGLLQYSWPNDKD-PVVVPFPTMTFAEVLATYGTDKPDTRFGMKIIDISDVFRNTEIGFLQDALsKPH 364
Cdd:COG0173 241 SFVDQEDVFELMEGLIRHLFKEVLGvELPTPFPRMTYAEAMERYGSDKPDLRFGLELVDVTDIFKDSGFKVFAGAA-ENG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 365 GTVKAICIPEGAKYlKRKDIESIRNFAADH---------FNQEilpvflnanrNWNSPVANFIMESQRLELIRLMETQEE 435
Cdd:COG0173 320 GRVKAINVPGGASL-SRKQIDELTEFAKQYgakglayikVNED----------GLKSPIAKFLSEEELAAILERLGAKPG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 436 DVVLLTAGEHNKACSLLGKLRLECADLLEtrgvvLRDPTLFSFLWVVDFPLFLPKEENPReLESAHHPFTAPHPSDIHLL 515
Cdd:COG0173 389 DLIFFVADKPKVVNKALGALRLKLGKELG-----LIDEDEFAFLWVVDFPLFEYDEEEGR-WVAMHHPFTMPKDEDLDLL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 516 YTEPKK------------------------EDV--KMLS--------------HLLQALDYGAPPHGGIALGLDRLICLV 555
Cdd:COG0173 463 ETDPGKvrakaydlvlngyelgggsirihdPELqeKVFEllgiseeeaeekfgFLLEAFKYGAPPHGGIAFGLDRLVMLL 542
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 119611366 556 TGSPSIRDVIAFPKSFRGHDLMSNTPDSVPPEELKPYHIRVSKP 599
Cdd:COG0173 543 AGEDSIRDVIAFPKTQSAQDLMTGAPSEVDEKQLKELHIRLRPP 586
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
50-599 |
0e+00 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 699.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 50 RTNTCGELRSSHLGQEVTLCGWIQYRRQN---TFLVLRDFDGLVQVIIPQD----ESAASVKKilceapvESVVQVSGTV 122
Cdd:PRK00476 4 RTHYCGELRESHVGQTVTLCGWVHRRRDHgglIFIDLRDREGIVQVVFDPDaeafEVAESLRS-------EYVIQVTGTV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 123 ISRPAGQENPKMPTGEIEIKVKTAELLNACKKLPFEIKNFVKKTEALRLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLc 202
Cdd:PRK00476 77 RARPEGTVNPNLPTGEIEVLASELEVLNKSKTLPFPIDDEEDVSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFL- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 203 NLHGFVDIETPTLFKRTPGGAKEFLVPSR-EPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQI 281
Cdd:PRK00476 156 DDNGFLEIETPILTKSTPEGARDYLVPSRvHPGKFYALPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEFTQI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 282 DIEMSFVDQTGIQSLIEGLLQYSWPNDKD-PVVVPFPTMTFAEVLATYGTDKPDTRFGMKIIDISDVFRNTEIGFLQDAL 360
Cdd:PRK00476 236 DIEMSFVTQEDVMALMEGLIRHVFKEVLGvDLPTPFPRMTYAEAMRRYGSDKPDLRFGLELVDVTDLFKDSGFKVFAGAA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 361 sKPHGTVKAICIPEGAKYLKRKDIESIRNFAADhFNQEILPVFLNANRNWNSPVANFIMESQRLELIRLMETQEEDVVLL 440
Cdd:PRK00476 316 -NDGGRVKAIRVPGGAAQLSRKQIDELTEFAKI-YGAKGLAYIKVNEDGLKGPIAKFLSEEELAALLERTGAKDGDLIFF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 441 TAGEHNKACSLLGKLRLECADLLEtrgvvLRDPTLFSFLWVVDFPLFLPKEENPReLESAHHPFTAPHPSDIH-LLYTEP 519
Cdd:PRK00476 394 GADKAKVVNDALGALRLKLGKELG-----LIDEDKFAFLWVVDFPMFEYDEEEGR-WVAAHHPFTMPKDEDLDeLETTDP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 520 KK------------------------EDV--KMLS--------------HLLQALDYGAPPHGGIALGLDRLICLVTGSP 559
Cdd:PRK00476 468 GKarayaydlvlngyelgggsirihrPEIqeKVFEilgiseeeaeekfgFLLDALKYGAPPHGGIAFGLDRLVMLLAGAD 547
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 119611366 560 SIRDVIAFPKSFRGHDLMSNTPDSVPPEELKPYHIRVSKP 599
Cdd:PRK00476 548 SIRDVIAFPKTQSAQDLLTGAPSPVDEKQLRELGIRLRKK 587
|
|
| aspS_bact |
TIGR00459 |
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be ... |
50-595 |
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: 548.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 50 RTNTCGELRSSHLGQEVTLCGWIQYRRQN---TFLVLRDFDGLVQVIIPQDESAASVKKILCEapvESVVQVSGTVISRP 126
Cdd:TIGR00459 2 RTHYCGQLRTEHLGQTVTLAGWVNRRRDLgglIFIDLRDRSGIVQVVCDPDADALKLAKGLRN---EDVVQVKGKVSARP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 127 AGQENPKMPTGEIEIKVKTAELLNACKKLPFEIKNfVKKTEALRLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLcNLHG 206
Cdd:TIGR00459 79 EGNINRNLDTGEIEILAESITLLNKSKTPPLIIEK-TDAEEEVRLKYRYLDLRRPEMQQRLKLRHKVTKAVRNFL-DQQG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 207 FVDIETPTLFKRTPGGAKEFLVPSR-EPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEM 285
Cdd:TIGR00459 157 FLEIETPMLTKSTPEGARDYLVPSRvHKGEFYALPQSPQLFKQLLMVSGVDRYYQIARCFRDEDLRADRQPEFTQIDMEM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 286 SFVDQTGIQSLIEGLLQYSWPNDKD-PVVVPFPTMTFAEVLATYGTDKPDTRFGMKIIDISDVFRNTEIG-FLQDALSKp 363
Cdd:TIGR00459 237 SFMTQEDVMELIEKLVSHVFLEVKGiDLKKPFPVMTYAEAMERYGSDKPDLRFPLELIDVTDLFKDSEFKvFSNLINDG- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 364 hGTVKAICIPEGAKYLKRKDIESIRNFAADHFNQEILPVFLNaNRNWNSPVANFIMESQRLELIRLMETQEEDVVLLTAG 443
Cdd:TIGR00459 316 -GRVKAIRVPGGWAELSRKSIKELRKFAKEYGAKGLAYLKVN-EDGINSPIKKFLDEKKGKILLERTDAQNGDILLFGAG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 444 EHNKACSLLGKLRLEcadLLETRGVVlrDPTLFSFLWVVDFPLFLPKEENprELESAHHPFTAPHPSDIHLLYTEPKK-- 521
Cdd:TIGR00459 394 SKKIVLDALGALRLK---LGKDLGLV--DPDLFSFLWVVDFPMFEKDKEG--RLCAAHHPFTMPKDEDLENLEAAPEEal 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 522 --------------------------------------EDVKMLSHLLQALDYGAPPHGGIALGLDRLICLVTGSPSIRD 563
Cdd:TIGR00459 467 aeaydlvlngvelgggsirihdpevqkkvfeilgidpeEAREKFGFLLEAFKYGTPPHAGFALGLDRLMMLLTGTDNIRD 546
|
570 580 590
....*....|....*....|....*....|..
gi 119611366 564 VIAFPKSFRGHDLMSNTPDSVPPEELKPYHIR 595
Cdd:TIGR00459 547 VIAFPKTTAAACLMTEAPSFIDEKQLEELSIK 578
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
36-599 |
1.47e-170 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 500.09 E-value: 1.47e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 36 SSQRRIPEFSSFVVRTNTCGELRSSHLGQEVTLCGWIQYRRQN---TFLVLRDFDGLVQVIIPQDEsAASVKKILCEAPV 112
Cdd:PLN02903 45 SAVDSMSSQLTWPSRSHLCGALSVNDVGSRVTLCGWVDLHRDMgglTFLDVRDHTGIVQVVTLPDE-FPEAHRTANRLRN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 113 ESVVQVSGTVISRPAGQENPKMPTGEIEIKVKTAELLNAC-KKLPFEI------KNFVKktEALRLQYRYLDLRSFQMQY 185
Cdd:PLN02903 124 EYVVAVEGTVRSRPQESPNKKMKTGSVEVVAESVDILNVVtKSLPFLVttadeqKDSIK--EEVRLRYRVLDLRRPQMNA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 186 NLRLRSQMVMKMREYLCNLHGFVDIETPTLFKRTPGGAKEFLVPSR-EPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARC 264
Cdd:PLN02903 202 NLRLRHRVVKLIRRYLEDVHGFVEIETPILSRSTPEGARDYLVPSRvQPGTFYALPQSPQLFKQMLMVSGFDRYYQIARC 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 265 YRDEGSRPDRQPEFTQIDIEMSFVDQTGIQSLIEGLLQYSWPNDKD-PVVVPFPTMTFAEVLATYGTDKPDTRFGMKIID 343
Cdd:PLN02903 282 FRDEDLRADRQPEFTQLDMELAFTPLEDMLKLNEDLIRQVFKEIKGvQLPNPFPRLTYAEAMSKYGSDKPDLRYGLELVD 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 344 ISDVFRNTEIGFLQDALSKpHGTVKAICIPEGAKY-----LKRKDI--ESIRNFAADhfnqeiLPvFLNANRNWNSPVAN 416
Cdd:PLN02903 362 VSDVFAESSFKVFAGALES-GGVVKAICVPDGKKIsnntaLKKGDIynEAIKSGAKG------LA-FLKVLDDGELEGIK 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 417 FIMES----QRLELIRLMETQEEDVVLLTAGEHNKACSLLGKLRLECADLLEtrgvvLRDPTLFSFLWVVDFPLFlpkEE 492
Cdd:PLN02903 434 ALVESlspeQAEQLLAACGAGPGDLILFAAGPTSSVNKTLDRLRQFIAKTLD-----LIDPSRHSILWVTDFPMF---EW 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 493 NPRE--LESAHHPFTAPHPSDI-----------HLLYTEPK---------KEDV--KMLS--------------HLLQAL 534
Cdd:PLN02903 506 NEDEqrLEALHHPFTAPNPEDMgdlssaralayDMVYNGVEigggslriyRRDVqqKVLEaiglspeeaeskfgYLLEAL 585
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119611366 535 DYGAPPHGGIALGLDRLICLVTGSPSIRDVIAFPKSFRGHDLMSNTPDSVPPEELKPYHIRVSKP 599
Cdd:PLN02903 586 DMGAPPHGGIAYGLDRLVMLLAGAKSIRDVIAFPKTTTAQCALTRAPSEVDDKQLQDLSIASTAP 650
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
54-590 |
5.09e-134 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 408.22 E-value: 5.09e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 54 CGELRSSHLGQEVTLCGWIQYRRQN---TFLVLRDFDGLVQVIIPQDESAASVKKILCEAPVESVVQVSGTVISRPAGQE 130
Cdd:PRK12820 9 CGHLSLDDTGREVCLAGWVDAFRDHgelLFIHLRDRNGFIQAVFSPEAAPADVYELAASLRAEFCVALQGEVQKRLEETE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 131 NPKMPTGEIEIKVKTAELLNACKKLPFEI--KNFVKK---------TEALRLQYRYLDLRSFQMQYNLRLRSQMVMKMRE 199
Cdd:PRK12820 89 NPHIETGDIEVFVRELSILAASEALPFAIsdKAMTAGagsagadavNEDLRLQYRYLDIRRPAMQDHLAKRHRIIKCARD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 200 YLcNLHGFVDIETPTLFKRTPGGAKEFLVPSR-EPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEF 278
Cdd:PRK12820 169 FL-DSRGFLEIETPILTKSTPEGARDYLVPSRiHPKEFYALPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 279 TQIDIEMSFVDQTGIQSLIEGLLQYSWPNDKDPVVVPFPTMTFAEVLATYGTDKPDTRFGMKIIDISDVFRNTEIGFLQD 358
Cdd:PRK12820 248 TQLDIEASFIDEEFIFELIEELTARMFAIGGIALPRPFPRMPYAEAMDTTGSDRPDLRFDLKFADATDIFENTRYGIFKQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 359 ALSKpHGTVKAICIPEGAKYLKrkdiesiRNFAADHFNQEILPVFLNANRNW--------NSPVANFIMESQRLELIRLM 430
Cdd:PRK12820 328 ILQR-GGRIKGINIKGQSEKLS-------KNVLQNEYAKEIAPSFGAKGMTWmraeagglDSNIVQFFSADEKEALKRRF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 431 ETQEEDVVLLTA-GEHNKACSLLGKLRLECADLLEtrgvvLRDPTLFSFLWVVDFPLFLPKEENprELESAHHPFTAP-- 507
Cdd:PRK12820 400 HAEDGDVIIMIAdASCAIVLSALGQLRLHLADRLG-----LIPEGVFHPLWITDFPLFEATDDG--GVTSSHHPFTAPdr 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 508 ---HPSDIHLLYTEPKK-----------------------------------EDVK-MLSHLLQALDYGAPPHGGIALGL 548
Cdd:PRK12820 473 edfDPGDIEELLDLRSRaydlvvngeelgggsirindkdiqlrifaalglseEDIEdKFGFFLRAFDFAAPPHGGIALGL 552
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 119611366 549 DRLICLVTGSPSIRDVIAFPKSFRGHDLMSNTPDSVPPEELK 590
Cdd:PRK12820 553 DRVVSMILQTPSIREVIAFPKNRSAACPLTGAPSEVAQEQLA 594
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
187-572 |
5.97e-115 |
|
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: 343.79 E-value: 5.97e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 187 LRLRSQMVMKMREYLCNlHGFVDIETPTLFKRTPGGAKEFLVPSR-EPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCY 265
Cdd:cd00777 1 LRLRSRVIKAIRNFLDE-QGFVEIETPILTKSTPEGARDFLVPSRlHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 266 RDEGSRPDRQPEFTQIDIEMSFVDQTGIQSLIEGLLQYSWPNDKD-PVVVPFPTMTFAEVLATYGtdkpdtrfgmkiidi 344
Cdd:cd00777 80 RDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGvELTTPFPRMTYAEAMERYG--------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 345 sdvfrnteigflqdalskphgtvkaicipegakylkrkdiesirnfaadhfnqeilpvflnanrnwnspvanfimesqrl 424
Cdd:cd00777 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 425 elirlmetqeedvvlltagehnkacsllgklrlecadlletrgvvlrdptlFSFLWVVDFPLFLPKEENPReLESAHHPF 504
Cdd:cd00777 145 ---------------------------------------------------FKFLWIVDFPLFEWDEEEGR-LVSAHHPF 172
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 505 TAPHPSDIHLLYTEPKK----------------------------------------EDVKMLSHLLQALDYGAPPHGGI 544
Cdd:cd00777 173 TAPKEEDLDLLEKDPEDaraqaydlvlngvelgggsirihdpdiqekvfeilglseeEAEEKFGFLLEAFKYGAPPHGGI 252
|
410 420
....*....|....*....|....*...
gi 119611366 545 ALGLDRLICLVTGSPSIRDVIAFPKSFR 572
Cdd:cd00777 253 ALGLDRLVMLLTGSESIRDVIAFPKTQN 280
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
167-569 |
3.92e-95 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 294.47 E-value: 3.92e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 167 EALRLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLCNlHGFVDIETPTLFK-RTPGGAKEFLVPSREPGKFYSLPQSPQQ 245
Cdd:pfam00152 2 EETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDE-NGFLEVETPILTKsATPEGARDFLVPSRALGKFYALPQSPQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 246 FKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEMSFVDQTGIQSLIEGLLQYSWPNDKD-----------PVVV 314
Cdd:pfam00152 81 YKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGiakeleggtllDLKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 315 PFPTMTFAEVL----------ATYGTDKPDTRFGMKIIdisdvfrnteigflqdalskphgtvkaicipegakylkrkdi 384
Cdd:pfam00152 161 PFPRITYAEAIeklngkdveeLGYGSDKPDLRFLLELV------------------------------------------ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 385 esirnfaadhfnqeilpvflnanrnwnspvanfimesqrlelirlmetqeedvvlltagehnkacsllgklrlecadlle 464
Cdd:pfam00152 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 465 trgvvlRDPTLFSFLWVVDFPlflpkeenpreleSAHHPFTAPHPSDIHLL----------------YTE---P------ 519
Cdd:pfam00152 199 ------IDKNKFNPLWVTDFP-------------AEHHPFTMPKDEDDPALaeafdlvlngveigggSIRihdPelqeer 259
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 119611366 520 -------KKEDVKMLSHLLQALDYGAPPHGGIALGLDRLICLVTGSPSIRDVIAFPK 569
Cdd:pfam00152 260 feeqgldPEEAEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFPK 316
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
50-183 |
3.31e-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: 3.31e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 50 RTNTCGELRSSHLGQEVTLCGWIQYRRQN---TFLVLRDFDGLVQVIIPQDESAAsvKKILCEAPVESVVQVSGTVISRP 126
Cdd:cd04317 1 RTHYCGELRESHVGQEVTLCGWVQRRRDHgglIFIDLRDRYGIVQVVFDPEEAPE--FELAEKLRNESVIQVTGKVRARP 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 119611366 127 AGQENPKMPTGEIEIKVKTAELLNACKKLPFEIKNFVKKTEALRLQYRYLDLRSFQM 183
Cdd:cd04317 79 EGTVNPKLPTGEIEVVASELEVLNKAKTLPFEIDDDVNVSEELRLKYRYLDLRRPKM 135
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
50-568 |
9.96e-54 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 189.25 E-value: 9.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 50 RTNTCGELRSSHLGQEVTLCGWIQYRR---QNTFLVLRDFDGLVQVIIPQDESAASVKKILcEAPVESVVQVSGTVisrp 126
Cdd:PRK05159 3 KRHLTSELTPELDGEEVTLAGWVHEIRdlgGIAFLILRDRSGIIQVVVKKKVDEELFETIK-KLKRESVVSVTGTV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 127 agQENPKMPTGeIEIKVKTAELLN-ACKKLPFEIKNFVKKTEALRLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLCNlH 205
Cdd:PRK05159 78 --KANPKAPGG-VEVIPEEIEVLNkAEEPLPLDISGKVLAELDTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYE-N 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 206 GFVDIETPTLFKR-TPGGAKEFLVPSREPGKFysLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQ-PEFTQIDI 283
Cdd:PRK05159 154 GFTEIFTPKIVASgTEGGAELFPIDYFEKEAY--LAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRHlNEYTSIDV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 284 EMSFVD-QTGIQSLIEGLLQYswpndkdpvvvpfptmTFAEVLATYGtdkpdtrfgmkiidisdvfrnTEIGFLQDALSK 362
Cdd:PRK05159 232 EMGFIDdHEDVMDLLENLLRY----------------MYEDVAENCE---------------------KELELLGIELPV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 363 PHGTVKAICIPEGAKYLKRKDIEsirnfaadhfnqeilpvflnanRNWnspvanfimesqrlelirlmetqEEDvvLLTA 442
Cdd:PRK05159 275 PETPIPRITYDEAIEILKSKGNE----------------------ISW-----------------------GDD--LDTE 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 443 GEHnkacsLLGKlrlecaDLLETRGVvlrdptlfSFLWVVDFPL----F--LPKEENP----------RELESA------ 500
Cdd:PRK05159 308 GER-----LLGE------YVKEEYGS--------DFYFITDYPSekrpFytMPDEDDPeisksfdllfRGLEITsggqri 368
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 501 HhpftaphpsDIHLLYT--EPKKEDVKMLSHLLQALDYGAPPHGGIALGLDRLICLVTGSPSIRDVIAFP 568
Cdd:PRK05159 369 H---------RYDMLVEsiKEKGLNPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
187-569 |
2.76e-48 |
|
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: 169.58 E-value: 2.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 187 LRLRSQMVMKMREYLCNlHGFVDIETPTLFKRTPG-GAKEFLVPSREPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCY 265
Cdd:cd00669 1 FKVRSKIIKAIRDFMDD-RGFLEVETPMLQKITGGaGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 266 RDEGSRPDRQPEFTQIDIEMSFVDQTGIQSLIEGLLQYSW------------PNDKDPvVVPFPTMTFAEVLATYGTDKP 333
Cdd:cd00669 80 RNEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLArevlgvtavtygFELEDF-GLPFPRLTYREALERYGQPLF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 334 DTRFGMkiidisdvfrnteigFLQDALSKPHGTVKAICipegakylkrkdiesirnfaaDHFNQEILPVflnanrnwnsP 413
Cdd:cd00669 159 LTDYPA---------------EMHSPLASPHDVNPEIA---------------------DAFDLFINGV----------E 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 414 VANfimesqrlelirlmetqeedvvlltagehnkacsllGKLRLECADLLETRgvvlrdptlfsflwvvdFPLFLPKEEN 493
Cdd:cd00669 193 VGN------------------------------------GSSRLHDPDIQAEV-----------------FQEQGINKEA 219
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119611366 494 PRElesahhpftaphpsdihllytepKKEDvkmlshLLQALDYGAPPHGGIALGLDRLICLVTGSPSIRDVIAFPK 569
Cdd:cd00669 220 GME-----------------------YFEF------YLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPK 266
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
50-568 |
6.97e-45 |
|
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: 164.84 E-value: 6.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 50 RTNTCGELRSSHLGQEVTLCGWIQYRRQN---TFLVLRDFDGLVQVIIPQDESA--ASVKKIlceaPVESVVQVSGTVis 124
Cdd:COG0017 1 KRTYIKDLLPEHVGQEVTVAGWVRTKRDSggiSFLILRDGSGFIQVVVKKDKLEnfEEAKKL----TTESSVEVTGTV-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 125 rpagQENPKMPTGeIEIKVKTAELLNACKK-LPFEIKnfvKKTEALRLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLcN 203
Cdd:COG0017 75 ----VESPRAPQG-VELQAEEIEVLGEADEpYPLQPK---RHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFF-Q 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 204 LHGFVDIETPTLfkrTP----GGAKEFLVpsrepgKFY----SLPQSPQQFKQLlMVGGLDRYFQVARCYRDEGSRPDRQ 275
Cdd:COG0017 146 ERGFVEVHTPII---TAsateGGGELFPV------DYFgkeaYLTQSGQLYKEA-LAMALEKVYTFGPTFRAEKSNTRRH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 276 -PEFTQIDIEMSFVDQTGIQSLIEGLLQY--------------SWPNDKD--PVVV--PFPTMTFAEVLATYGTDKPDTR 336
Cdd:COG0017 216 lAEFWMIEPEMAFADLEDVMDLAEEMLKYiikyvlencpeeleFLGRDVErlEKVPesPFPRITYTEAIEILKKSGEKVE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 337 FGMkiiDISdvfrnteigflqdalskphgtvkaiciPEGAKYLkrkdiesirnfaADHFNQEilPVFlnanrnwnspVAN 416
Cdd:COG0017 296 WGD---DLG---------------------------TEHERYL------------GEEFFKK--PVF----------VTD 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 417 FIMEsqrlelIR--LMETQEED--VVLltagehnkacsllgklrleCADLL-----E-----TRgvvlrdptlfsflwvv 482
Cdd:COG0017 322 YPKE------IKafYMKPNPDDpkTVA-------------------AFDLLapgigEiiggsQR---------------- 360
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 483 dfplflpkEENPRELESAhhpftaphpsdihllyTEPKKEDVKMLSHLLQALDYGAPPHGGIALGLDRLICLVTGSPSIR 562
Cdd:COG0017 361 --------EHRYDVLVER----------------IKEKGLDPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIR 416
|
....*.
gi 119611366 563 DVIAFP 568
Cdd:COG0017 417 EVIPFP 422
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
48-568 |
2.44e-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: 106.66 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 48 VVRTNTCGELRSSH--------LGQEVTLCGWIQYRR---QNTFLVLRDFDGLVQVIIPQDEsaasvkkiLCEAPVESV- 115
Cdd:COG1190 33 FPRTHTAAEIREKYdeleaeeeTGDEVSVAGRIMAKRdmgKASFADLQDGSGRIQLYLRRDE--------LGEEAYELFk 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 116 -------VQVSGTVI-SRpagqenpkmpTGEIEIKVKTAELLN-ACKKLPFEIKNFvKKTEaLRLQYRYLDL----RSFQ 182
Cdd:COG1190 105 lldlgdiVGVEGTVFrTK----------TGELSVKVEELTLLSkSLRPLPEKFHGL-TDPE-TRYRQRYVDLivnpEVRE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 183 MqynLRLRSQMVMKMREYLcNLHGFVDIETPTLfKRTPGGA--KEF--------------------Lvpsrepgkfyslp 240
Cdd:COG1190 173 T---FRKRSKIIRAIRRFL-DERGFLEVETPML-QPIAGGAaaRPFithhnaldmdlylriapelyL------------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 241 qspqqfKQLLmVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEMSFVDQTGIQSLIEGLLQYSwpndkdpvvvpfptmt 320
Cdd:COG1190 235 ------KRLI-VGGFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREA---------------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 321 faeVLATYGTDKpdTRFGMKIIDISDVFRntEIGFLqDALSKPHG-TVKAIcipegakylkrKDIESIRNFAADHfNQEI 399
Cdd:COG1190 292 ---AEAVLGTTK--VTYQGQEIDLSPPWR--RITMV-EAIKEATGiDVTPL-----------TDDEELRALAKEL-GIEV 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 400 LPvflnanrNWNspvanfimesqRLELIrlMETQEEDVvlltagEHNkacsllgklrlecadlletrgvvLRDPTlfsfl 479
Cdd:COG1190 352 DP-------GWG-----------RGKLI--DELFEELV------EPK-----------------------LIQPT----- 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 480 WVVDFPLFL-----PKEENPR-----EL-----ESAhhpfTAphpsdihllYTE---PK------KEDVKMLSH------ 529
Cdd:COG1190 378 FVTDYPVEVsplakRHRDDPGlterfELfiagrEIA----NA---------FSElndPIdqrerfEEQLELKAAgddeam 444
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 119611366 530 -----LLQALDYGAPPHGGIALGLDRLICLVTGSPSIRDVIAFP 568
Cdd:COG1190 445 pmdedFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 488
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
55-286 |
3.87e-24 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 106.33 E-value: 3.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 55 GELRSSHLGQEVTLCGWIQYRR---QNTFLVLRDFDGLVQVIIPQDESAASVK--KILCEAPVESVVQVSGTVIsrpagq 129
Cdd:PLN02850 73 SDLGEELAGSEVLIRGRVHTIRgkgKSAFLVLRQSGFTVQCVVFVSEVTVSKGmvKYAKQLSRESVVDVEGVVS------ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 130 eNPKMP----TGEIEIKVKTAELLN-ACKKLPFEI-----------------KNFVKKTEALRLQYRYLDLRSFQMQYNL 187
Cdd:PLN02850 147 -VPKKPvkgtTQQVEIQVRKIYCVSkALATLPFNVedaarseseiekalqtgEQLVRVGQDTRLNNRVLDLRTPANQAIF 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 188 RLRSQMVMKMREYLCNlHGFVDIETPTLFK-RTPGGAKEFLVPSRepGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYR 266
Cdd:PLN02850 226 RIQSQVCNLFREFLLS-KGFVEIHTPKLIAgASEGGSAVFRLDYK--GQPACLAQSPQLHKQMAICGDFRRVFEIGPVFR 302
|
250 260
....*....|....*....|.
gi 119611366 267 DEGSRPDRQ-PEFTQIDIEMS 286
Cdd:PLN02850 303 AEDSFTHRHlCEFTGLDLEME 323
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
170-572 |
1.38e-23 |
|
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: 101.87 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 170 RLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLcNLHGFVDIETPTLFKR-TPGGAKEFlvpsrePGKFYS----LPQSPQ 244
Cdd:cd00776 7 LLDNRHLDLRTPKVQAIFRIRSEVLRAFREFL-RENGFTEVHTPKITSTdTEGGAELF------KVSYFGkpayLAQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 245 QFKQlLMVGGLDRYFQVARCYRDEGSRPDRQ-PEFTQIDIEMSFV-DQTGIQSLIEGLLQYSW----------------- 305
Cdd:cd00776 80 LYKE-MLIAALERVYEIGPVFRAEKSNTRRHlSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFkrvlercakelelvnql 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 306 PNDKDPVVVPFPTMTFAEvlatygtdkpdtrfgmkIIDI-SDVFRNTEIGFLQDaLSKPHgtvkaicipegAKYLkrkdi 384
Cdd:cd00776 159 NRELLKPLEPFPRITYDE-----------------AIELlREKGVEEEVKWGED-LSTEH-----------ERLL----- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 385 esirnfaADHFNQEilPVFLNanrNWNSPVANFIM--ESQRLELIRLMetqeeDVVLLTAGEhnkACSllGKLRLECADL 462
Cdd:cd00776 205 -------GEIVKGD--PVFVT---DYPKEIKPFYMkpDDDNPETVESF-----DLLMPGVGE---IVG--GSQRIHDYDE 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 463 LETRgvvlrdptlfsflwvvdfplflPKEE--NPRELESahhpftaphpsdihllYTEPKKedvkmlshllqaldYGAPP 540
Cdd:cd00776 263 LEER----------------------IKEHglDPESFEW----------------YLDLRK--------------YGMPP 290
|
410 420 430
....*....|....*....|....*....|..
gi 119611366 541 HGGIALGLDRLICLVTGSPSIRDVIAFPKSFR 572
Cdd:cd00776 291 HGGFGLGLERLVMWLLGLDNIREAILFPRDPK 322
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
65-150 |
4.51e-23 |
|
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: 93.40 E-value: 4.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 65 EVTLCGWIQYRRQN---TFLVLRDFDGLVQVIIPQDESAASVKKILcEAPVESVVQVSGTVISRPAGQenpkMPTGEIEI 141
Cdd:cd04100 1 EVTLAGWVHSRRDHgglIFIDLRDGSGIVQVVVNKEELGEFFEEAE-KLRTESVVGVTGTVVKRPEGN----LATGEIEL 75
|
....*....
gi 119611366 142 KVKTAELLN 150
Cdd:cd04100 76 QAEELEVLS 84
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
41-568 |
8.68e-22 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 99.01 E-value: 8.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 41 IPEFSSFVVRTNTCGELRSSH----------LGQEVTLCGWIQYRR---QNTFLVLRDFDGLVQVIIPQDESAASVKKIL 107
Cdd:PRK00484 22 IDPYPNKFERTHTAAELRAKYddkekeeleeLEIEVSVAGRVMLKRvmgKASFATLQDGSGRIQLYVSKDDVGEEALEAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 108 CEAPVESVVQVSGTVIsrpagqenpKMPTGEIEIKVKTAELLN-ACKKLPfeiknfVK----KTEALRLQYRYLDL---- 178
Cdd:PRK00484 102 KKLDLGDIIGVEGTLF---------KTKTGELSVKATELTLLTkSLRPLP------DKfhglTDVETRYRQRYVDLivnp 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 179 RSFQMqynLRLRSQMVMKMREYLCNlHGFVDIETPTLfKRTPGG--AKEFL-------VPsrepgkFYsLPQSPQQF-KQ 248
Cdd:PRK00484 167 ESRET---FRKRSKIISAIRRFLDN-RGFLEVETPML-QPIAGGaaARPFIthhnaldID------LY-LRIAPELYlKR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 249 LLmVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEMSFVDQTGIQSLIEGLLQYSwpndkdpvvvpfptmtfaeVLATY 328
Cdd:PRK00484 235 LI-VGGFERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHL-------------------AQAVL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 329 GTDKpdTRFGMKIIDISDVFRntEIGFLqDALSKphgtvkaicipEGAKYLKRKDIESIRNFAADHfNQEILPvflnanr 408
Cdd:PRK00484 295 GTTK--VTYQGTEIDFGPPFK--RLTMV-DAIKE-----------YTGVDFDDMTDEEARALAKEL-GIEVEK------- 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 409 NWNspvanfimesqRLELIrlMETQEEDVvlltagEHNkacsllgklrlecadlletrgvvLRDPTlfsFlwVVDFPLfl 488
Cdd:PRK00484 351 SWG-----------LGKLI--NELFEEFV------EPK-----------------------LIQPT---F--ITDYPV-- 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 489 pkeenprELeSahhPFTAPHPSDIHLL---------------YTE---P------------KKE---DVKMlsHL----L 531
Cdd:PRK00484 382 -------EI-S---PLAKRHREDPGLTerfelfiggreianaFSElndPidqrerfeaqveAKEagdDEAM--FMdedfL 448
|
570 580 590
....*....|....*....|....*....|....*..
gi 119611366 532 QALDYGAPPHGGIALGLDRLICLVTGSPSIRDVIAFP 568
Cdd:PRK00484 449 RALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
63-568 |
1.29e-20 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 95.83 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 63 GQEVTLCGWIQYRRQN---TFLVLRDFDGLVQVIIPQ---DESAASVKKILCEAPVESVVQVSGTVisrpagqenPKMPT 136
Cdd:PLN02502 108 DVSVSVAGRIMAKRAFgklAFYDLRDDGGKIQLYADKkrlDLDEEEFEKLHSLVDRGDIVGVTGTP---------GKTKK 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 137 GEIEIKVKTAELLNAC-KKLP---FEIKNFVKktealRLQYRYLDL-RSFQMQYNLRLRSQMVMKMREYLCNLhGFVDIE 211
Cdd:PLN02502 179 GELSIFPTSFEVLTKClLMLPdkyHGLTDQET-----RYRQRYLDLiANPEVRDIFRTRAKIISYIRRFLDDR-GFLEVE 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 212 TPTLfKRTPGGA--KEFLVPSREPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEMSFVD 289
Cdd:PLN02502 253 TPML-NMIAGGAaaRPFVTHHNDLNMDLYLRIATELHLKRLVVGGFERVYEIGRQFRNEGISTRHNPEFTTCEFYQAYAD 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 290 QTGIQSLIEGLLQYSwpndkdpvvvpfptmtfaeVLATYGTDKPDtrFGMKIIDISDVFRN-TEIGFLQDALSkphgtvk 368
Cdd:PLN02502 332 YNDMMELTEEMVSGM-------------------VKELTGSYKIK--YHGIEIDFTPPFRRiSMISLVEEATG------- 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 369 aICIPEGAKylkrkdiesirnfaadhfnqeilpvflnanrnwnSPVANFimesqrleliRLMETQEEDVVLLtagehnKA 448
Cdd:PLN02502 384 -IDFPADLK----------------------------------SDEANA----------YLIAACEKFDVKC------PP 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 449 CSLLGKLRLEC-ADLLETRGV----VLRDPTLFSFL--W-------VVDFPLFLpkeeNPRELESAHHPFTAP------- 507
Cdd:PLN02502 413 PQTTGRLLNELfEEFLEETLVqptfVLDHPVEMSPLakPhrskpglTERFELFI----NGRELANAFSELTDPvdqrerf 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119611366 508 ------HPSDihllytepKKEDVKMLSHLLQALDYGAPPHGGIALGLDRLICLVTGSPSIRDVIAFP 568
Cdd:PLN02502 489 eeqvkqHNAG--------DDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFP 547
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
187-568 |
3.94e-19 |
|
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: 88.80 E-value: 3.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 187 LRLRSQMVMKMREYLCNlHGFVDIETPTLfKRTPGGA--KEFLVPSREPG-KFYsLPQSPQQFKQLLMVGGLDRYFQVAR 263
Cdd:cd00775 8 FIVRSKIISYIRKFLDD-RGFLEVETPML-QPIAGGAaaRPFITHHNALDmDLY-LRIAPELYLKRLIVGGFERVYEIGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 264 CYRDEGSRPDRQPEFTQIDIEMSFVDQTGIQSLIEGLLQYSwpndkdpvvvpfptmtfaeVLATYGTDKPDtrFGMKIID 343
Cdd:cd00775 85 NFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGL-------------------VKKINGKTKIE--YGGKELD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 344 ISDVFRNTEIgflQDALSKPHGTvkaicipegakYLKRKDIESIRnfaadhfnqeilpvflnanrnwnspvanfimESQR 423
Cdd:cd00775 144 FTPPFKRVTM---VDALKEKTGI-----------DFPELDLEQPE-------------------------------ELAK 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 424 LELIRLMETQEEDVvlltagehnkacsLLGKLRLECAD-LLETRgvvLRDPTlfsflWVVDFPLFLPkeenprelesahh 502
Cdd:cd00775 179 LLAKLIKEKIEKPR-------------TLGKLLDKLFEeFVEPT---LIQPT-----FIIDHPVEIS------------- 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 503 PFTAPHPSDIHLL---------------YTE---PKKEDVKMLSHL-----------------LQALDYGAPPHGGIALG 547
Cdd:cd00775 225 PLAKRHRSNPGLTerfelficgkeianaYTElndPFDQRERFEEQAkqkeagddeammmdedfVTALEYGMPPTGGLGIG 304
|
410 420
....*....|....*....|.
gi 119611366 548 LDRLICLVTGSPSIRDVIAFP 568
Cdd:cd00775 305 IDRLVMLLTDSNSIRDVILFP 325
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
80-569 |
1.63e-18 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 89.28 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 80 FLVLRDFDGLVQVIIP-QDESAASVKKILCEAPVESVVQVSGTVisrpAGQENPKMPTG--EIEIKVKTAELLN-ACKKL 155
Cdd:PTZ00401 98 FMVLRDGSDSVQAMAAvEGDVPKEMIDFIGQIPTESIVDVEATV----CKVEQPITSTShsDIELKVKKIHTVTeSLRTL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 156 PFEIKNFVKKTEA--------LRLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLCNlHGFVDIETPTLFKR-TPGGAKEF 226
Cdd:PTZ00401 174 PFTLEDASRKESDegakvnfdTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLID-SDFCEIHSPKIINApSEGGANVF 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 227 LVPSREpgKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQ-PEFTQIDIEMSFVDQtgiqsliegllqysw 305
Cdd:PTZ00401 253 KLEYFN--RFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHlTEFVGLDVEMRINEH--------------- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 306 pndkdpvvvpfptmtFAEVLatygtdkpdtrfgmkiiDISDVFRNteigFLQDALSKPHGTVKAIC------------IP 373
Cdd:PTZ00401 316 ---------------YYEVL-----------------DLAESLFN----YIFERLATHTKELKAVCqqypfeplvwklTP 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 374 EGAKYLKRKDIESirnfaadhfNQEILPVFLNANRNWNSPvanfIMESQRLELIRLMETQEEDVVLLTAGEHNKACSLLG 453
Cdd:PTZ00401 360 ERMKELGVGVISE---------GVEPTDKYQARVHNMDSR----MLRINYMHCIELLNTVLEEKMAPTDDINTTNEKLLG 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 454 KLrlecadLLETRGVVL----RDPTLFSFLWVVDFP----------LFLPKEENPRELESAHHPftaphpsDIHLLYTEP 519
Cdd:PTZ00401 427 KL------VKERYGTDFfisdRFPSSARPFYTMECKdderftnsydMFIRGEEISSGAQRIHDP-------DLLLARAKM 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 119611366 520 KKEDVKMLSHLLQALDYGAPPHGGIALGLDRLICLVTGSPSIRDVIAFPK 569
Cdd:PTZ00401 494 LNVDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPR 543
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
62-568 |
2.87e-18 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 88.20 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 62 LGQEVTLCGWIQYRR---QNTFLVLRDFDGLVQVIIPQDESAASV-KKILCEAPVESVVQVSGTVIsrpagqenpKMPTG 137
Cdd:PRK12445 64 LNIEVSVAGRMMTRRimgKASFVTLQDVGGRIQLYVARDSLPEGVyNDQFKKWDLGDIIGARGTLF---------KTQTG 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 138 EIEIKVKTAELLN-ACKKLPFEIKNFvkKTEALRLQYRYLDL-RSFQMQYNLRLRSQMVMKMREYLCnLHGFVDIETPtL 215
Cdd:PRK12445 135 ELSIHCTELRLLTkALRPLPDKFHGL--QDQEVRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMV-ARGFMEVETP-M 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 216 FKRTPGGA--KEFLVPSREPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEMSFVDQTGI 293
Cdd:PRK12445 211 MQVIPGGAsaRPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 294 QSLIEGLLQyswpndkdpvvvpfptmtfaeVLATYGTDKPDTRFGMKIIDISDVFRNTEigfLQDALSkphgtvkaicip 373
Cdd:PRK12445 291 IELTESLFR---------------------TLAQEVLGTTKVTYGEHVFDFGKPFEKLT---MREAIK------------ 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 374 egaKYLKRKDIESIRNFAADHFNQEILPVFLNANRNWNSPVANFIMESQRLELIRLMETQEEDVVLLTAGEHNkacsllg 453
Cdd:PRK12445 335 ---KYRPETDMADLDNFDAAKALAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRN------- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 454 KLRLECADLLETRGVVLRDPTLFSFLwvvdfplflpkEENPRELESAHHPFTAPHPSDIHLLYTEpkkEDvkmlshLLQA 533
Cdd:PRK12445 405 DVNPEITDRFEFFIGGREIGNGFSEL-----------NDAEDQAERFQEQVNAKAAGDDEAMFYD---ED------YVTA 464
|
490 500 510
....*....|....*....|....*....|....*
gi 119611366 534 LDYGAPPHGGIALGLDRLICLVTGSPSIRDVIAFP 568
Cdd:PRK12445 465 LEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
50-568 |
4.98e-17 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 85.40 E-value: 4.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 50 RTNTCGELRSSHLGQEVTLCGWIQYRRQN---TFLVLRDFDGLVQVII----PQDESAASVKKilcEAPVESVVQVSGTV 122
Cdd:PRK02983 638 PTHTVAEALDAPTGEEVSVSGRVLRIRDYggvLFADLRDWSGELQVLLdasrLEQGSLADFRA---AVDLGDLVEVTGTM 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 123 I-SRpagqenpkmpTGEIEIKVKTAELLNAC-KKLPFEIKNFVKKtEAlRLQYRYLDL----RSFQMqynLRLRSQMVMK 196
Cdd:PRK02983 715 GtSR----------NGTLSLLVTSWRLAGKClRPLPDKWKGLTDP-EA-RVRQRYLDLavnpEARDL---LRARSAVVRA 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 197 MREYLcNLHGFVDIETPTLfKRTPGGA--KEFLVPSREpgkfYSLPQ----SPQQFKQLLMVGGLDRYFQVARCYRDEGS 270
Cdd:PRK02983 780 VRETL-VARGFLEVETPIL-QQVHGGAnaRPFVTHINA----YDMDLylriAPELYLKRLCVGGVERVFELGRNFRNEGV 853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 271 RPDRQPEFTQIDIEMSFVDQTGIQSLIEGLLQyswpndkdpvvvpfptmtfAEVLATYGTD---KPDTRFGMKIIDISDV 347
Cdd:PRK02983 854 DATHNPEFTLLEAYQAHADYDTMRDLTRELIQ-------------------NAAQAAHGAPvvmRPDGDGVLEPVDISGP 914
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 348 FRNTEIgflQDALSKPHGTvkaicipegakylkrkdiesirnfaadhfnqEILPvflnanrnwNSPVAnfimesqrlELI 427
Cdd:PRK02983 915 WPVVTV---HDAVSEALGE-------------------------------EIDP---------DTPLA---------ELR 942
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 428 RLMETQEedvvlLTAGEHNKAcsllGKLRLECAD-LLETRGVVlrdPTLFSflwvvDFPLflpkeenprelESAhhPFTA 506
Cdd:PRK02983 943 KLCDAAG-----IPYRTDWDA----GAVVLELYEhLVEDRTTF---PTFYT-----DFPT-----------SVS--PLTR 992
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 507 PHPSDIHLL---------------YTE----------------------PK----KEDvkmlshLLQALDYGAPPHGGIA 545
Cdd:PRK02983 993 PHRSDPGLAerwdlvawgvelgtaYSEltdpveqrrrlteqsllaaggdPEamelDED------FLQALEYAMPPTGGLG 1066
|
570 580
....*....|....*....|...
gi 119611366 546 LGLDRLICLVTGSpSIRDVIAFP 568
Cdd:PRK02983 1067 MGVDRLVMLLTGR-SIRETLPFP 1088
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
133-568 |
1.04e-14 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 77.36 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 133 KMPTGEIEIKVKTAELLNAC-KKLPfeIKNFVKKTEaLRLQYRYLDLR-SFQMQYNLRLRSQMVMKMREYLcNLHGFVDI 210
Cdd:PTZ00417 200 KSKKGELSIFPKETIILSPClHMLP--MKYGLKDTE-IRYRQRYLDLMiNESTRSTFITRTKIINYLRNFL-NDRGFIEV 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 211 ETPTLfKRTPGGA--KEFLVPSREPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEMSFV 288
Cdd:PTZ00417 276 ETPTM-NLVAGGAnaRPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYA 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 289 DQTGIQSLIE-----------GLLQYSWPND---KDPVVV----PFPTMTFAEVLATYGTDKPDTRFGM--KIIDISDVF 348
Cdd:PTZ00417 355 DFYDLIKWSEdffsqlvmhlfGTYKILYNKDgpeKDPIEIdftpPYPKVSIVEELEKLTNTKLEQPFDSpeTINKMINLI 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 349 RNTEIgflqdALSKPhgtvkaiciPEGAKYLKrkdiESIRNFAADHFNQEilPVFLNANRNWNSPVANFIME----SQRL 424
Cdd:PTZ00417 435 KENKI-----EMPNP---------PTAAKLLD----QLASHFIENKYPNK--PFFIIEHPQIMSPLAKYHRSkpglTERL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 425 ELIrlmetqeedvvlltagehnkacsLLGKLRLECAdlletrgVVLRDPtlfsflwvvdfplFLPKE-----ENPRELES 499
Cdd:PTZ00417 495 EMF-----------------------ICGKEVLNAY-------TELNDP-------------FKQKEcfsaqQKDREKGD 531
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119611366 500 AhhpftaphpsdihllytepkkEDVKMLSHLLQALDYGAPPHGGIALGLDRLICLVTGSPSIRDVIAFP 568
Cdd:PTZ00417 532 A---------------------EAFQFDAAFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFP 579
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
205-305 |
1.28e-13 |
|
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: 70.22 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 205 HGFVDIETP-----TLFKRTPGGAKEFLVPSREPGKFYSLPQSPQQFKQLLMVGGL----DRYFQVARCYRDEGSR--PD 273
Cdd:cd00768 16 LGFQEVETPiverePLLEKAGHEPKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIrklpLRLAEIGPAFRNEGGRrgLR 95
|
90 100 110
....*....|....*....|....*....|..
gi 119611366 274 RQPEFTQIDIEMsFVDQTGIQSLIEGLLQYSW 305
Cdd:cd00768 96 RVREFTQLEGEV-FGEDGEEASEFEELIELTE 126
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
63-159 |
1.29e-13 |
|
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: 67.34 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 63 GQEVTLCGWIQYRRQ---NTFLVLRDFDGLVQVIIPQDESAASVKKILCEAPVESVVQVSGTVisrpagQENPKMPTGeI 139
Cdd:cd04316 12 GEEVTVAGWVHEIRDlggIKFVILRDREGIVQVTAPKKKVDKELFKTVRKLSRESVISVTGTV------KAEPKAPNG-V 84
|
90 100
....*....|....*....|.
gi 119611366 140 EIKVKTAELLNACKK-LPFEI 159
Cdd:cd04316 85 EIIPEEIEVLSEAKTpLPLDP 105
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
133-575 |
1.32e-13 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 73.91 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 133 KMPTGEIEIKVKTAELLN--ACKK---LPfEIKNF-VKKTEALRLQYRYLDLRSFQMQYN-LRLRSQMVMKMREYLcNLH 205
Cdd:PTZ00385 173 RMQRGELSVAASRMLILSpyVCTDqvvCP-NLRGFtVLQDNDVKYRYRFTDMMTNPCVIEtIKKRHVMLQALRDYF-NER 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 206 GFVDIETPTLFKRTPGG-AKEFLVPSREPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQidie 284
Cdd:PTZ00385 251 NFVEVETPVLHTVASGAnAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTS---- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 285 msfvdqtgiqsliegllqyswpndkdpvvvpfptmtfAEVLATYGTdkpdtrfgmkiidISDVFRNTEIGFLQDALsKPH 364
Cdd:PTZ00385 327 -------------------------------------CEFYAAYHT-------------YEDLMPMTEDIFRQLAM-RVN 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 365 GTVKAICIPEGAKYLKRK-DI-ESIRNFAADHFNQEILPVFLNANRNWNSPVANFIMEsqrlelirlmetqeedVVLLTA 442
Cdd:PTZ00385 356 GTTVVQIYPENAHGNPVTvDLgKPFRRVSVYDEIQRMSGVEFPPPNELNTPKGIAYMS----------------VVMLRY 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 443 GEHNKACSLLGKLRLECADLLETRGVVlrDPTlfsflWVVDFPLF---LPKEENPR--------------ELESAHHPFT 505
Cdd:PTZ00385 420 NIPLPPVRTAAKMFEKLIDFFITDRVV--EPT-----FVMDHPLFmspLAKEQVSRpglaerfelfvngiEYCNAYSELN 492
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119611366 506 APHPS----DIHLLYTEPKKEDVKMLSH-LLQALDYGAPPHGGIALGLDRLICLVTGSPSIRDVIAFP---KSFRGHD 575
Cdd:PTZ00385 493 DPHEQyhrfQQQLVDRQGGDEEAMPLDEtFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPllrQDIRSHD 570
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
57-303 |
4.31e-13 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 71.68 E-value: 4.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 57 LRSSHLGQEVTLCGWIQYRRQN---TFLVLRDFDGLVQVIIPQDESAASVKKILcEAPVESVVQVSGTVIsrpagqENPK 133
Cdd:PRK03932 10 LKGKYVGQEVTVRGWVRTKRDSgkiAFLQLRDGSCFKQLQVVKDNGEEYFEEIK-KLTTGSSVIVTGTVV------ESPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 134 MPTGeIEIKVKTAELLNACKKlPFEIKnfvKK---TEALRlQYRYLDLRSFQMQYNLRLRSQMVMKMREYLcNLHGFVDI 210
Cdd:PRK03932 83 AGQG-YELQATKIEVIGEDPE-DYPIQ---KKrhsIEFLR-EIAHLRPRTNKFGAVMRIRNTLAQAIHEFF-NENGFVWV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 211 ETPTLfkrTPG---GAKE-FLVPSREP-------GKFYSLPQSpqqfKQL---LMVGGLDRYFQVARCYRDEGSRPDRQ- 275
Cdd:PRK03932 156 DTPII---TASdceGAGElFRVTTLDLdfskdffGKEAYLTVS----GQLyaeAYAMALGKVYTFGPTFRAENSNTRRHl 228
|
250 260
....*....|....*....|....*...
gi 119611366 276 PEFTQIDIEMSFVDQTGIQSLIEGLLQY 303
Cdd:PRK03932 229 AEFWMIEPEMAFADLEDNMDLAEEMLKY 256
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
66-149 |
8.01e-10 |
|
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: 55.32 E-value: 8.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 66 VTLCGWIQYRRQN----TFLVLRDFDGLVQVIIPQDESAASVKKIlceaPVESVVQVSGTVISRpagqenpkmPTGEIEI 141
Cdd:pfam01336 1 VTVAGRVTSIRRSggklLFLTLRDGTGSIQVVVFKEEAEKLAKKL----KEGDVVRVTGKVKKR---------KGGELEL 67
|
....*...
gi 119611366 142 KVKTAELL 149
Cdd:pfam01336 68 VVEEIELL 75
|
|
| GAD |
pfam02938 |
GAD domain; This domain is found in some members of the GatB and aspartyl tRNA synthetases. |
362-452 |
1.00e-09 |
|
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: 55.73 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 362 KPHGTVKAICIPeGAKYLKRKDIESIRNFAADHFNQEIlpVFLNANRN-WNSPVANFIMESQRLELIRLMETQEEDVVLL 440
Cdd:pfam02938 6 KSGGSVKALRVP-GAAGLSRKEIDELERFAKEYGAKGL--AWIKVEGGgHTGPIAKFLTEEEVEKLLEAVGAEDGDALLF 82
|
90
....*....|..
gi 119611366 441 TAGEHNKACSLL 452
Cdd:pfam02938 83 VADKKKTVNKAL 94
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
529-566 |
6.24e-08 |
|
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: 54.48 E-value: 6.24e-08
10 20 30
....*....|....*....|....*....|....*...
gi 119611366 529 HLLQALDYGAPPHGGIALGLDRLICLVTGSPSIRDVIA 566
Cdd:TIGR00462 253 RFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVLA 290
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
65-151 |
1.22e-07 |
|
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: 49.62 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 65 EVTLCGWIQYRR----QNTFLVLRDFDG-LVQVIipqDESAASVKKILCEAPVESVVQVSGTVISRpagQENPKMPTGEI 139
Cdd:cd04321 1 KVTLNGWIDRKPrivkKLSFADLRDPNGdIIQLV---STAKKDAFSLLKSITAESPVQVRGKLQLK---EAKSSEKNDEW 74
|
90
....*....|..
gi 119611366 140 EIKVKTAELLNA 151
Cdd:cd04321 75 ELVVDDIQTLNA 86
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
65-156 |
1.37e-07 |
|
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus horikoshii AsnRS asparaginyl-tRNA synthetase (AsnRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The archeal enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose.
Pssm-ID: 239814 [Multi-domain] Cd Length: 103 Bit Score: 49.83 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 65 EVTLCGWIQYRR---QNTFLVLRDFDGLVQVIIPQDESAASVKKILcEAPVESVVQVSGTVisrpagQENPKMPTGeIEI 141
Cdd:cd04319 1 KVTLAGWVYRKRevgKKAFIVLRDSTGIVQAVFSKDLNEEAYREAK-KVGIESSVIVEGAV------KADPRAPGG-AEV 72
|
90
....*....|....*
gi 119611366 142 KVKTAELLNACKKLP 156
Cdd:cd04319 73 HGEKLEIIQNVEFFP 87
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
65-133 |
6.05e-07 |
|
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and Saccharomyces cerevisiae cytoplasmic asparaginyl-tRNA synthetase (AsnRS), in Brugia malayai AsnRs and, in various putative bacterial AsnRSs. This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. AsnRS is immunodominant antigen of the filarial nematode B. malayai and of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.
Pssm-ID: 239818 [Multi-domain] Cd Length: 84 Bit Score: 47.61 E-value: 6.05e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119611366 65 EVTLCGWIQ-YRRQN--TFLVLRDFDGLVQVIIPQDE-SAASVKKILCEapvESVVQVSGTVISRPAGQENPK 133
Cdd:cd04323 1 RVKVFGWVHrLRSQKklMFLVLRDGTGFLQCVLSKKLvTEFYDAKSLTQ---ESSVEVTGEVKEDPRAKQAPG 70
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
532-574 |
2.40e-06 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 50.41 E-value: 2.40e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 119611366 532 QALDYGAPPHGGIALGLDRLICLVTGSPSIRDVIAFPKsFRGH 574
Cdd:PTZ00425 542 QLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPR-YPGH 583
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
536-569 |
2.34e-05 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 47.28 E-value: 2.34e-05
10 20 30
....*....|....*....|....*....|....
gi 119611366 536 YGAPPHGGIALGLDRLICLVTGSPSIRDVIAFPK 569
Cdd:PLN02603 525 YGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPR 558
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
529-564 |
1.56e-04 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 44.15 E-value: 1.56e-04
10 20 30
....*....|....*....|....*....|....*.
gi 119611366 529 HLLQALDYGAPPHGGIALGLDRLICLVTGSPSIRDV 564
Cdd:PRK09350 271 NLIAALEAGLPDCSGVALGVDRLIMLALGAESISEV 306
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
536-574 |
2.51e-04 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 44.09 E-value: 2.51e-04
10 20 30
....*....|....*....|....*....|....*....
gi 119611366 536 YGAPPHGGIALGLDRLICLVTGSPSIRDVIAFPKSfRGH 574
Cdd:PLN02532 593 HGTVKHSGFSLGFELMVLFATGLPDVRDAIPFPRS-WGK 630
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
65-178 |
3.99e-04 |
|
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These enzymes are homodimeric class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Included in this group are E. coli LysS and LysU. These two isoforms of LysRS are encoded by distinct genes which are differently regulated. Eukaryotes contain 2 sets of aaRSs, both of which encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Saccharomyces cerevisiae cytoplasmic and mitochondrial LysRSs have been shown to participate in the mitochondrial import of the only nuclear-encoded tRNA of S. cerevisiae (tRNAlysCUU). The gene for human LysRS encodes both the cytoplasmic and the mitochondrial isoforms of LysRS. In addition to their housekeeping role, human lysRS may function as a signaling molecule that activates immune cells and tomato LysRS may participate in a root-specific process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging.
Pssm-ID: 239817 [Multi-domain] Cd Length: 108 Bit Score: 40.15 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 65 EVTLCGWIQYRR---QNTFLVLRDFDGLVQVIIPQD----ESAASVKKILceaPVESVVQVSGTVIsrpagqenpKMPTG 137
Cdd:cd04322 1 EVSVAGRIMSKRgsgKLSFADLQDESGKIQVYVNKDdlgeEEFEDFKKLL---DLGDIIGVTGTPF---------KTKTG 68
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 119611366 138 EIEIKVKTAELLNAC-KKLPFEIKNFvKKTEAlRLQYRYLDL 178
Cdd:cd04322 69 ELSIFVKEFTLLSKSlRPLPEKFHGL-TDVET-RYRQRYLDL 108
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
536-569 |
7.86e-04 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 42.29 E-value: 7.86e-04
10 20 30
....*....|....*....|....*....|....
gi 119611366 536 YGAPPHGGIALGLDRLICLVTGSPSIRDVIAFPK 569
Cdd:PLN02221 532 YGTVKHCGFGLGFERMILFATGIDNIRDVIPFPR 565
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
187-303 |
9.36e-04 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 41.93 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611366 187 LRLRSQMVMKMREYLCNlHGFVDIETPTLFKRT----PGGAKEFL-VPSRE-PGKFYSLPQSPQQFKQLlMVGGLDRYFQ 260
Cdd:PRK06462 30 LKVQSSILRYTREFLDG-RGFVEVLPPIISPSTdplmGLGSDLPVkQISIDfYGVEYYLADSMILHKQL-ALRMLGKIFY 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 119611366 261 VARCYRDEGSRPDRQP---EFTQIDIEMSFVDQTGIQSLIEGLLQY 303
Cdd:PRK06462 108 LSPNFRLEPVDKDTGRhlyEFTQLDIEIEGADLDEVMDLIEDLIKY 153
|
|
| |
