|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
52-545 |
0e+00 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 1011.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 52 SLNVEDDPLSANYGDVPLSDLQSKeaKDVANWTQVGSLTGELKDKYVILRGRIQTIRAVAKkMAFLVVREKGFTVQCVVS 131
Cdd:PLN02850 40 SLEDEDDPLASNYGDVPLEELQSK--VTGREWTDVSDLGEELAGSEVLIRGRVHTIRGKGK-SAFLVLRQSGFTVQCVVF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 132 EQPELVSRQMVKYVVGLSRESIVDVEGVVSVPNVAIKGATQQVEIQVRKVYCISKAMPSLPINIEDAARSEAEIEKALQA 211
Cdd:PLN02850 117 VSEVTVSKGMVKYAKQLSRESVVDVEGVVSVPKKPVKGTTQQVEIQVRKIYCVSKALATLPFNVEDAARSESEIEKALQT 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 212 GEQLVRVNQDTRLNYRVLDMRTPANQGIFRIQCQVGTIFRQFLLSEGFVEIHTPKLIGGSSEGGASVFRLDYKGQPACLA 291
Cdd:PLN02850 197 GEQLVRVGQDTRLNNRVLDLRTPANQAIFRIQSQVCNLFREFLLSKGFVEIHTPKLIAGASEGGSAVFRLDYKGQPACLA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 292 QSPQLHKQMSICGDFGRVFEIGPVFRAEDSFTHRHLCEFTGLDVEMEIKTHYSEVMDIVDRLFVSMFDSMNQNCKKELEA 371
Cdd:PLN02850 277 QSPQLHKQMAICGDFRRVFEIGPVFRAEDSFTHRHLCEFTGLDLEMEIKEHYSEVLDVVDELFVAIFDGLNERCKKELEA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 372 IDKQYPFEPLKYLRNTLRLTFEEGIQMLKDAGVEIDPLGDLNTEAERKLGRLVLEKYGTEFYILHRYPLSVRPFYTMPCH 451
Cdd:PLN02850 357 IREQYPFEPLKYLPKTLRLTFAEGIQMLKEAGVEVDPLGDLNTESERKLGQLVKEKYGTDFYILHRYPLAVRPFYTMPCP 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 452 DNPTYSNSFDVFIRGEEIISGAQRVHVPEFLTERAQACGIDVKTIETYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIR 531
Cdd:PLN02850 437 DDPKYSNSFDVFIRGEEIISGAQRVHDPELLEKRAEECGIDVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIR 516
|
490
....*....|....
gi 1279768844 532 KTSLFPRDPQRIAP 545
Cdd:PLN02850 517 KTSLFPRDPQRLAP 530
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
64-545 |
4.03e-172 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 497.98 E-value: 4.03e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 64 YGDVPLsdLQSKEAKDvANWTQVGSLTGE-LKDKYVILRGRIQTIRAVAKkMAFLVVREKGFTVQCVVSEQPElVSRQMV 142
Cdd:PTZ00401 49 FGAAPM--VQSTTYKS-RTFIPVAVLSKPeLVDKTVLIRARVSTTRKKGK-MAFMVLRDGSDSVQAMAAVEGD-VPKEMI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 143 KYVVGLSRESIVDVEGVVSVPNVAIKGATQQ-VEIQVRKVYCISKAMPSLPINIEDAARSEAEiekalqageQLVRVNQD 221
Cdd:PTZ00401 124 DFIGQIPTESIVDVEATVCKVEQPITSTSHSdIELKVKKIHTVTESLRTLPFTLEDASRKESD---------EGAKVNFD 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 222 TRLNYRVLDMRTPANQGIFRIQCQVGTIFRQFLLSEGFVEIHTPKLIGGSSEGGASVFRLDYKGQPACLAQSPQLHKQMS 301
Cdd:PTZ00401 195 TRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDSDFCEIHSPKIINAPSEGGANVFKLEYFNRFAYLAQSPQLYKQMV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 302 ICGDFGRVFEIGPVFRAEDSFTHRHLCEFTGLDVEMEIKTHYSEVMDIVDRLFVSMFDSMNQNcKKELEAIDKQYPFEPL 381
Cdd:PTZ00401 275 LQGDVPRVFEVGPVFRSENSNTHRHLTEFVGLDVEMRINEHYYEVLDLAESLFNYIFERLATH-TKELKAVCQQYPFEPL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 382 -------------------------KY---LRNT----LRLTFEEGIQMLKDAGVE-IDPLGDLNTEAERKLGRLVLEKY 428
Cdd:PTZ00401 354 vwkltpermkelgvgvisegveptdKYqarVHNMdsrmLRINYMHCIELLNTVLEEkMAPTDDINTTNEKLLGKLVKERY 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 429 GTEFYILHRYPLSVRPFYTMPCHDNPTYSNSFDVFIRGEEIISGAQRVHVPEFLTERAQACGIDVKTIETYIDSFRYGAP 508
Cdd:PTZ00401 434 GTDFFISDRFPSSARPFYTMECKDDERFTNSYDMFIRGEEISSGAQRIHDPDLLLARAKMLNVDLTPIKEYVDSFRLGAW 513
|
490 500 510
....*....|....*....|....*....|....*..
gi 1279768844 509 PHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQRIAP 545
Cdd:PTZ00401 514 PHGGFGVGLERVVMLYLGLSNVRLASLFPRDPQRTTP 550
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
217-541 |
1.13e-165 |
|
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: 472.82 E-value: 1.13e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 217 RVNQDTRLNYRVLDMRTPANQGIFRIQCQVGTIFRQFLLSEGFVEIHTPKLIGGSSEGGASVFRLDYKGQPACLAQSPQL 296
Cdd:cd00776 1 DANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 297 HKQMSICGdFGRVFEIGPVFRAEDSFTHRHLCEFTGLDVEMEIKTHYSEVMDIVDRLFVSMFDSMNQNCKKELEAIdKQY 376
Cdd:cd00776 81 YKEMLIAA-LERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRVLERCAKELELV-NQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 377 PFEPLKYLRNTLRLTFEEGIQMLKDAGV--EIDPLGDLNTEAERKLGrlvlEKYGTEFYILHRYPLSVRPFYTMPCHDNP 454
Cdd:cd00776 159 NRELLKPLEPFPRITYDEAIELLREKGVeeEVKWGEDLSTEHERLLG----EIVKGDPVFVTDYPKEIKPFYMKPDDDNP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 455 TYSNSFDVFIRG-EEIISGAQRVHVPEFLTERAQACGIDVKTIETYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKT 533
Cdd:cd00776 235 ETVESFDLLMPGvGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREA 314
|
....*...
gi 1279768844 534 SLFPRDPQ 541
Cdd:cd00776 315 ILFPRDPK 322
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
89-545 |
8.81e-157 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 454.65 E-value: 8.81e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 89 LTGELKDKYVILRGRIQTIRAVaKKMAFLVVREKGFTVQCVVSEQPELVSRQMVKyvvGLSRESIVDVEGVVSVPNVAIK 168
Cdd:PRK05159 10 LTPELDGEEVTLAGWVHEIRDL-GGIAFLILRDRSGIIQVVVKKKVDEELFETIK---KLKRESVVSVTGTVKANPKAPG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 169 GatqqVEIQVRKVYCISKAMPSLPINIEDaaRSEAEIekalqageqlvrvnqDTRLNYRVLDMRTPANQGIFRIQCQVGT 248
Cdd:PRK05159 86 G----VEVIPEEIEVLNKAEEPLPLDISG--KVLAEL---------------DTRLDNRFLDLRRPRVRAIFKIRSEVLR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 249 IFRQFLLSEGFVEIHTPKLIGGSSEGGASVFRLDYKGQPACLAQSPQLHKQMSICGDFGRVFEIGPVFRAEDSFTHRHLC 328
Cdd:PRK05159 145 AFREFLYENGFTEIFTPKIVASGTEGGAELFPIDYFEKEAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRHLN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 329 EFTGLDVEMEIKTHYSEVMDIVDRLFVSMFDSMNQNCKKELEAIDKQYPFEPLKYLRntlrLTFEEGIQMLKDAGVEIDP 408
Cdd:PRK05159 225 EYTSIDVEMGFIDDHEDVMDLLENLLRYMYEDVAENCEKELELLGIELPVPETPIPR----ITYDEAIEILKSKGNEISW 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 409 LGDLNTEAERKLGRLVLEKYGTEFYILHRYPLSVRPFYTMPCHDNPTYSNSFDVFIRGEEIISGAQRVHVPEFLTERAQA 488
Cdd:PRK05159 301 GDDLDTEGERLLGEYVKEEYGSDFYFITDYPSEKRPFYTMPDEDDPEISKSFDLLFRGLEITSGGQRIHRYDMLVESIKE 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1279768844 489 CGIDVKTIETYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQRIAP 545
Cdd:PRK05159 381 KGLNPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPRDRHRLTP 437
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
82-545 |
4.16e-148 |
|
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: 432.17 E-value: 4.16e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 82 NWTQVGSLTGELKDKYVILRGRIQTIRaVAKKMAFLVVREKGFTVQCVVsEQPELVSRQMVKyvvGLSRESIVDVEGVVs 161
Cdd:COG0017 1 KRTYIKDLLPEHVGQEVTVAGWVRTKR-DSGGISFLILRDGSGFIQVVV-KKDKLENFEEAK---KLTTESSVEVTGTV- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 162 vpnVAIKGATQQVEIQVRKVYCISKAMPSLPIniedaarseaeiekalqageQLVRVNQDTRLNYRVLDMRTPANQGIFR 241
Cdd:COG0017 75 ---VESPRAPQGVELQAEEIEVLGEADEPYPL--------------------QPKRHSLEFLLDNRHLRLRTNRFGAIFR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 242 IQCQVGTIFRQFLLSEGFVEIHTPKLIGGSSEGGASVFRLDYKGQPACLAQSPQLHKQMSICGdFGRVFEIGPVFRAEDS 321
Cdd:COG0017 132 IRSELARAIREFFQERGFVEVHTPIITASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMA-LEKVYTFGPTFRAEKS 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 322 FTHRHLCEFTGLDVEMEIKTHYsEVMDIVDRLFVSMFDSMNQNCKKELEAIDKQypFEPLKYLRNT--LRLTFEEGIQML 399
Cdd:COG0017 211 NTRRHLAEFWMIEPEMAFADLE-DVMDLAEEMLKYIIKYVLENCPEELEFLGRD--VERLEKVPESpfPRITYTEAIEIL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 400 KDAGVEIDPLGDLNTEAERKLGrlvlEKYGTEFYILHRYPLSVRPFYTMPCHDNPTYSNSFDVFIRG-EEIISGAQRVHV 478
Cdd:COG0017 288 KKSGEKVEWGDDLGTEHERYLG----EEFFKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGiGEIIGGSQREHR 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1279768844 479 PEFLTERAQACGIDVKTIETYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQRIAP 545
Cdd:COG0017 364 YDVLVERIKEKGLDPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
92-545 |
5.42e-143 |
|
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, aspS_arch, represents aspartyl-tRNA synthetases from the eukaryotic cytosol and from the Archaea. In some species, this enzyme aminoacylates tRNA for both Asp and Asn; Asp-tRNA(asn) is subsequently transamidated to Asn-tRNA(asn). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273087 [Multi-domain] Cd Length: 428 Bit Score: 419.23 E-value: 5.42e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 92 ELKDKYVILRGRIQTIRAVAKkMAFLVVREKGFTVQCVVSEQPelVSRQMVKYVVGLSRESIVDVEGVVSVPNVAIKGat 171
Cdd:TIGR00458 9 EMDGQEVTFMGWVHEIRDLGG-LIFVLLRDREGLIQITAPAKK--VSKNLFKWAKKLNLESVVAVRGIVKIKEKAPGG-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 172 qqVEIQVRKVYCISKAMPSLPINIEDaaRSEAEIekalqageqlvrvnqDTRLNYRVLDMRTPANQGIFRIQCQVGTIFR 251
Cdd:TIGR00458 84 --FEIIPTKIEVINEAKEPLPLDPTE--KVPAEL---------------DTRLDYRFLDLRRPTVQAIFRIRSGVLESVR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 252 QFLLSEGFVEIHTPKLIGGSSEGGASVFRLDYKGQPACLAQSPQLHKQMSICGDFGRVFEIGPVFRAEDSFTHRHLCEFT 331
Cdd:TIGR00458 145 EFLAEEGFIEVHTPKLVASATEGGTELFPITYFEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHRHLNEAT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 332 GLDVEMEIKTHySEVMDIVDRLFVSMFDSMNQNCKKELEAIDKQYPFEPLKYlrntLRLTFEEGIQMLKDAGVEIDPLGD 411
Cdd:TIGR00458 225 SIDIEMAFEDH-HDVMDILEELVVRVFEDVPERCAHQLETLEFKLEKPEGKF----VRLTYDEAIEMANAKGVEIGWGED 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 412 LNTEAERKLGrlvlEKYGTEFYILHrYPLSVRPFYTMPCHDNPTYSNSFDVFIRGEEIISGAQRVHVPEFLTERAQACGI 491
Cdd:TIGR00458 300 LSTEAEKALG----EEMDGLYFITD-WPTEIRPFYTMPDEDNPEISKSFDLMYRDLEISSGAQRIHLHDLLVERIKAKGL 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1279768844 492 DVKTIETYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQRIAP 545
Cdd:TIGR00458 375 NPEGFKDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRKRLTP 428
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
219-540 |
1.03e-96 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 296.40 E-value: 1.03e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 219 NQDTRLNYRVLDMRTPANQGIFRIQCQVGTIFRQFLLSEGFVEIHTPKLIGGSSEGGASVFRL--DYKGQPACLAQSPQL 296
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVpsRALGKFYALPQSPQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 297 HKQMSICGDFGRVFEIGPVFRAEDSFTHRHLcEFTGLDVEMEIKThYSEVMDIVDRLFVSMFDSMNqNCKKELEA---ID 373
Cdd:pfam00152 81 YKQLLMVAGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVD-YEDVMDLTEELIKEIFKEVE-GIAKELEGgtlLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 374 KQYPFEplkylrntlRLTFEEGIQMLKDAGVEiDPLGDLNTEAERKLGRLVLEKYGTEFYILHRYPLSVRPFYTMPCHDN 453
Cdd:pfam00152 158 LKKPFP---------RITYAEAIEKLNGKDVE-ELGYGSDKPDLRFLLELVIDKNKFNPLWVTDFPAEHHPFTMPKDEDD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 454 PTYSNSFDVFIRGEEIISGAQRVHVPEFLTERAQACGIDVKTIET----YIDSFRYGAPPHGGFGVGLERVVMLFCGLNN 529
Cdd:pfam00152 228 PALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPEEAEEkfgfYLDALKYGAPPHGGLGIGLDRLVMLLTGLES 307
|
330
....*....|.
gi 1279768844 530 IRKTSLFPRDP 540
Cdd:pfam00152 308 IREVIAFPKTR 318
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
94-545 |
6.58e-72 |
|
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, asnS, represents asparaginyl-tRNA synthetases from the three domains of life. Some species lack this enzyme and charge tRNA(asn) by misacylation with Asp, followed by transamidation of Asp to Asn. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273086 [Multi-domain] Cd Length: 453 Bit Score: 236.51 E-value: 6.58e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 94 KDKYVILRGRIQTIRAvAKKMAFLVVREKGF--TVQCVVSEQPELVSRQMVKyvvGLSRESIVDVEGVVsvpnVAIKGAT 171
Cdd:TIGR00457 15 VGDEVTVSGWVRTKRS-SKKIIFLELNDGSSlgPIQAVINGEDNPYLFQLLK---SLTTGSSVSVTGKV----VESPGKG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 172 QQVEIQVRKVYCISKAMP-SLPiniedaarseaeiekaLQAGEQlvrvNQDTRLNYRVLDMRTPANQGIFRIQCQVGTIF 250
Cdd:TIGR00457 87 QPVELQVKKIEVVGEAEPdDYP----------------LQKKEH----SLEFLRDIAHLRLRTNTLGAVMRVRNALSQAI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 251 RQFLLSEGFVEIHTPKLIGGSSEGGASVFRL---------DYKGQPACLAQSPQLHKQMSICGdFGRVFEIGPVFRAEDS 321
Cdd:TIGR00457 147 HRYFQENGFTWVSPPILTSNDCEGAGELFRVstgnidfsqDFFGKEAYLTVSGQLYLETYALA-LSKVYTFGPTFRAEKS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 322 FTHRHLCEFTGLDVEMEIKThYSEVMDIVDRLFVSMFDSMNQNCKKELEAIDKQYPFEPLKYLRNTL-----RLTFEEGI 396
Cdd:TIGR00457 226 NTSRHLSEFWMIEPEMAFAN-LNDLLQLAETLIKYIIKAVLENCSQELKFLEKNFDKDLIKRLENIInnkfaRITYTDAI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 397 QMLKDAG--VEIDPL-G-DLNTEAERKLGrlvlEKYGTEFYILHRYPLSVRPFYTMPCHDNPTYSnSFDVFIRG-EEIIS 471
Cdd:TIGR00457 305 EILKESDknFEYEDFwGdDLQTEHERFLA----EEYFKPPVFVTNYPKDIKAFYMKLNDDGKTVA-AMDLLAPGiGEIIG 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1279768844 472 GAQRVHVPEFLTERAQACGIDVKTIETYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQRIAP 545
Cdd:TIGR00457 380 GSEREDDLDKLENRMKEMGLDTDALNWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 453
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
89-545 |
1.52e-70 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 233.08 E-value: 1.52e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 89 LTGELKDKYVILRGRIQTIRaVAKKMAFLVVREkG---FTVQCVVSEQPELVSRqmvkyVVGLSRESIVDVEGVVsvpnV 165
Cdd:PRK03932 10 LKGKYVGQEVTVRGWVRTKR-DSGKIAFLQLRD-GscfKQLQVVKDNGEEYFEE-----IKKLTTGSSVIVTGTV----V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 166 AIKGATQQVEIQVRKVYCISKAMPSLPIniedaarseaeiekalQAGEQLVrvnqDTRLNYRVLDMRTPANQGIFRIQCQ 245
Cdd:PRK03932 79 ESPRAGQGYELQATKIEVIGEDPEDYPI----------------QKKRHSI----EFLREIAHLRPRTNKFGAVMRIRNT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 246 VGTIFRQFLLSEGFVEIHTPKLIGGSSEGGASVFRL---------DYKGQPACLAQSPQLHKQMSICGdFGRVFEIGPVF 316
Cdd:PRK03932 139 LAQAIHEFFNENGFVWVDTPIITASDCEGAGELFRVttldldfskDFFGKEAYLTVSGQLYAEAYAMA-LGKVYTFGPTF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 317 RAEDSFTHRHLCEFTGLDVEMEIKTHySEVMDIVDRLFVSMFDSMNQNCKKELEAIDKQYPFEPLKYLRNTL-----RLT 391
Cdd:PRK03932 218 RAENSNTRRHLAEFWMIEPEMAFADL-EDNMDLAEEMLKYVVKYVLENCPDDLEFLNRRVDKGDIERLENFIespfpRIT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 392 FEEGIQMLKDAGVEIDPL---G-DLNTEAERklgrlvlekYGTEFY-----ILHRYPLSVRPFYTMPCHDNPTYSnSFDV 462
Cdd:PRK03932 297 YTEAIEILQKSGKKFEFPvewGdDLGSEHER---------YLAEEHfkkpvFVTNYPKDIKAFYMRLNPDGKTVA-AMDL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 463 FIRG-EEIISGAQRVHVPEFLTERAQACGIDVKTIETYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQ 541
Cdd:PRK03932 367 LAPGiGEIIGGSQREERLDVLEARIKELGLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPG 446
|
....
gi 1279768844 542 RIAP 545
Cdd:PRK03932 447 RAEF 450
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
240-539 |
1.69e-58 |
|
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: 195.77 E-value: 1.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 240 FRIQCQVGTIFRQFLLSEGFVEIHTPKLIGGSSEGGASVFRLDY--KGQPACLAQSPQLHKQMSICGDFGRVFEIGPVFR 317
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYnaLGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 318 AEDSfTHRHLCEFTGLDVEMEIKThYSEVMDIVDRLFVSMFDSMNQNCKKELEAIDKQY--PFEplkylrntlRLTFEEg 395
Cdd:cd00669 81 NEDL-RARHQPEFTMMDLEMAFAD-YEDVIELTERLVRHLAREVLGVTAVTYGFELEDFglPFP---------RLTYRE- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 396 iqmlkdagveidplgdlnteAERKLGRlvlekygteFYILHRYPLSVRPFYTMPCHDNPTYSNSFDVFIRGEEIISGAQR 475
Cdd:cd00669 149 --------------------ALERYGQ---------PLFLTDYPAEMHSPLASPHDVNPEIADAFDLFINGVEVGNGSSR 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1279768844 476 VHVPEFLTERAQACGID----VKTIETYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRD 539
Cdd:cd00669 200 LHDPDIQAEVFQEQGINkeagMEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKM 267
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
231-545 |
3.28e-48 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 170.20 E-value: 3.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 231 MRTPANQGIFRIQCQVGTIFRQFLLSEGFVEIHTP-------KLIGGSSEGGASVFRLDYKGQPACLAQSPQLHKQMSIc 303
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPiispstdPLMGLGSDLPVKQISIDFYGVEYYLADSMILHKQLAL- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 304 GDFGRVFEIGPVFRAE--DSFTHRHLCEFTGLDVEMEiKTHYSEVMDIVDRLFVSMFDSMNQNCKKELEAIDKQYPfepl 381
Cdd:PRK06462 100 RMLGKIFYLSPNFRLEpvDKDTGRHLYEFTQLDIEIE-GADLDEVMDLIEDLIKYLVKELLEEHEDELEFFGRDLP---- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 382 KYLRNTLRLTFEEGIQMLKDAGVEIDPLGDLNTEAERKLgrlvLEKYGTEFYILHrYPLSVRPFYTMPCHDNPTYSNSFD 461
Cdd:PRK06462 175 HLKRPFKRITHKEAVEILNEEGCRGIDLEELGSEGEKSL----SEHFEEPFWIID-IPKGSREFYDREDPERPGVLRNYD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 462 VFIR---GEeIISGAQRVHVPEFLTERAQACGIDVKTIETYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPR 538
Cdd:PRK06462 250 LLLPegyGE-AVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFPR 328
|
....*..
gi 1279768844 539 DPQRIAP 545
Cdd:PRK06462 329 VPGIVAL 335
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
97-197 |
2.01e-42 |
|
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae and human cytoplasmic aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis.
Pssm-ID: 239815 [Multi-domain] Cd Length: 102 Bit Score: 146.94 E-value: 2.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 97 YVILRGRIQTIRAVAKKMAFLVVREKGFTVQCVVSEQPELVSRQMVKYVVGLSRESIVDVEGVVSVPNVAIKGATQQ-VE 175
Cdd:cd04320 1 EVLIRARVHTSRAQGAKLAFLVLRQQGYTIQGVLAASAEGVSKQMVKWAGSLSKESIVDVEGTVKKPEEPIKSCTQQdVE 80
|
90 100
....*....|....*....|..
gi 1279768844 176 IQVRKVYCISKAMPSLPINIED 197
Cdd:cd04320 81 LHIEKIYVVSEAAEPLPFQLED 102
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
87-537 |
1.12e-41 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 157.92 E-value: 1.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 87 GSLTGELKDKYVILRGRIQTIRavaK--KMAFLVVREKGFTVQCVVSEQPELVSRqmvkyVVGLSRESIVDVEGVV---S 161
Cdd:PRK00476 9 GELRESHVGQTVTLCGWVHRRR---DhgGLIFIDLRDREGIVQVVFDPDAEAFEV-----AESLRSEYVIQVTGTVrarP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 162 VPNVAIKGATQQVEIQVRKVYCISKAMPsLPINIEDaarseaEIEkalqageqlvrVNQDTRLNYRVLDMRTPANQGIFR 241
Cdd:PRK00476 81 EGTVNPNLPTGEIEVLASELEVLNKSKT-LPFPIDD------EED-----------VSEELRLKYRYLDLRRPEMQKNLK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 242 IQCQVGTIFRQFLLSEGFVEIHTPKLIgGSSEGGASVF----RLdYKGQPACLAQSPQLHKQMSICGDFGRVFEIGPVFR 317
Cdd:PRK00476 143 LRSKVTSAIRNFLDDNGFLEIETPILT-KSTPEGARDYlvpsRV-HPGKFYALPQSPQLFKQLLMVAGFDRYYQIARCFR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 318 AEDSFTHRHLcEFTGLDVEMeikthyS-----EVMDIVDRLFVSMFdsmnqnckKELEAIDKQYPFEPLKY--------- 383
Cdd:PRK00476 221 DEDLRADRQP-EFTQIDIEM------SfvtqeDVMALMEGLIRHVF--------KEVLGVDLPTPFPRMTYaeamrrygs 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 384 ----LRNTLRLT-------------FEEGIQM--------LKDAG-----VEID-------------------------- 407
Cdd:PRK00476 286 dkpdLRFGLELVdvtdlfkdsgfkvFAGAANDggrvkairVPGGAaqlsrKQIDeltefakiygakglayikvnedglkg 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 408 PLGDLNTEAERK---------------------------LGRLVLeKYGTEFYILHR----------YPL------SVR- 443
Cdd:PRK00476 366 PIAKFLSEEELAallertgakdgdliffgadkakvvndaLGALRL-KLGKELGLIDEdkfaflwvvdFPMfeydeeEGRw 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 444 -----PFyTMPCHD--------NPT--YSNSFDVFIRGEEIISGAQRVHVPEfLTERA-QACGIDVKTIET----YIDSF 503
Cdd:PRK00476 445 vaahhPF-TMPKDEdldelettDPGkaRAYAYDLVLNGYELGGGSIRIHRPE-IQEKVfEILGISEEEAEEkfgfLLDAL 522
|
570 580 590
....*....|....*....|....*....|....
gi 1279768844 504 RYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFP 537
Cdd:PRK00476 523 KYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
240-537 |
1.24e-38 |
|
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: 142.71 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 240 FRIQCQVGTIFRQFLLSEGFVEIHTPKLIGgSSEGGASVF----RLdYKGQPACLAQSPQLHKQMSICGDFGRVFEIGPV 315
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTK-STPEGARDFlvpsRL-HPGKFYALPQSPQLFKQLLMVSGFDRYFQIARC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 316 FRAEDSFTHRHlCEFTGLDVEMEIKTHySEVMDIVDRLFVSMFdsmnqnckKELEAIDKQYPFEplkylrntlRLTFEEG 395
Cdd:cd00777 79 FRDEDLRADRQ-PEFTQIDIEMSFVDQ-EDIMSLIEGLLKYVF--------KEVLGVELTTPFP---------RMTYAEA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 396 IQmlkDAGVE----ID-PLGDLNTEAERklgrlvlekygteFYILHRyplsvrPFyTMP-------CHDNPT--YSNSFD 461
Cdd:cd00777 140 ME---RYGFKflwiVDfPLFEWDEEEGR-------------LVSAHH------PF-TAPkeedldlLEKDPEdaRAQAYD 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 462 VFIRGEEIISGAQRVHVPEfLTERA-QACGIDVKTIET----YIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLF 536
Cdd:cd00777 197 LVLNGVELGGGSIRIHDPD-IQEKVfEILGLSEEEAEEkfgfLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVIAF 275
|
.
gi 1279768844 537 P 537
Cdd:cd00777 276 P 276
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
96-540 |
6.48e-37 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 144.35 E-value: 6.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 96 KYVILRGRIQTIRAvAKKMAFLVVREKGF--TVQCVVSeqPELVSRQMVKYVVGLSRESIVdVEGVVsvpnVAIKGATQQ 173
Cdd:PLN02603 108 KTLNVMGWVRTLRA-QSSVTFIEVNDGSClsNMQCVMT--PDAEGYDQVESGLITTGASVL-VQGTV----VSSQGGKQK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 174 VEIQVRKVYCISKAMPSLPINIEDAARseaeiekalqageQLVRVNQDTRlnyrvldMRTPANQGIFRIQCQVGTIFRQF 253
Cdd:PLN02603 180 VELKVSKIVVVGKSDPSYPIQKKRVSR-------------EFLRTKAHLR-------PRTNTFGAVARVRNALAYATHKF 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 254 LLSEGFVEIHTP-----------------KLIGGSSEGGASV-------------FRLDYKGQPACLAQSPQLHKQmSIC 303
Cdd:PLN02603 240 FQENGFVWVSSPiitasdcegageqfcvtTLIPNSAENGGSLvddipktkdglidWSQDFFGKPAFLTVSGQLNGE-TYA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 304 GDFGRVFEIGPVFRAEDSFTHRHLCEFTGLDVEMEIkTHYSEVMDIVDRLFVSMFDSMNQNCKKELEAIDKQYPFEPLKY 383
Cdd:PLN02603 319 TALSDVYTFGPTFRAENSNTSRHLAEFWMIEPELAF-ADLNDDMACATAYLQYVVKYILENCKEDMEFFNTWIEKGIIDR 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 384 L-----RNTLRLTFEEGIQMLKDAGVEID-PLG---DLNTEAERKLGRlvlEKYGTEFYILHRYPLSVRPFYTMPCHDNP 454
Cdd:PLN02603 398 LsdvveKNFVQLSYTDAIELLLKAKKKFEfPVKwglDLQSEHERYITE---EAFGGRPVIIRDYPKEIKAFYMRENDDGK 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 455 TYSnSFDVFI-RGEEIISGAQRVHVPEFLTERAQACGIDVKTIETYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKT 533
Cdd:PLN02603 475 TVA-AMDMLVpRVGELIGGSQREERLEYLEARLDELKLNKESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDA 553
|
....*..
gi 1279768844 534 SLFPRDP 540
Cdd:PLN02603 554 IPFPRVP 560
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
87-537 |
2.61e-35 |
|
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: 139.75 E-value: 2.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 87 GSLTGELKDKYVILRGRIQTIRAVAKkMAFLVVREKGFTVQCVVSEQpelVSRQMVKYVVGLSRESIVDVEGVVSV---- 162
Cdd:COG0173 8 GELRESDVGQEVTLSGWVHRRRDHGG-LIFIDLRDRYGITQVVFDPD---DSAEAFEKAEKLRSEYVIAVTGKVRArpeg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 163 ---PNVAikgaTQQVEIQVRKVYCISKAMPsLPINIEDaarseaEIEkalqageqlvrVNQDTRLNYRVLDMRTPANQGI 239
Cdd:COG0173 84 tvnPKLP----TGEIEVLASELEILNKAKT-PPFQIDD------DTD-----------VSEELRLKYRYLDLRRPEMQKN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 240 FRIQCQVGTIFRQFLLSEGFVEIHTPKLIGGSSEgGAsvfRlDY-------KGQPACLAQSPQLHKQMSICGDFGRVFEI 312
Cdd:COG0173 142 LILRHKVTKAIRNYLDENGFLEIETPILTKSTPE-GA---R-DYlvpsrvhPGKFYALPQSPQLFKQLLMVSGFDRYFQI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 313 GPVFRAEDSFTHRHLcEFTGLDVEMeikthyS-----EVMDIVDRLFVSMFdsmnqnckKELEAIDKQYPFEPLKY---- 383
Cdd:COG0173 217 ARCFRDEDLRADRQP-EFTQLDIEM------SfvdqeDVFELMEGLIRHLF--------KEVLGVELPTPFPRMTYaeam 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 384 ---------LRNTLRLT-------------FEEgiqMLKDAGV---------------EIDPLGD--------------L 412
Cdd:COG0173 282 erygsdkpdLRFGLELVdvtdifkdsgfkvFAG---AAENGGRvkainvpggaslsrkQIDELTEfakqygakglayikV 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 413 N------------TEAERK---------------------------LGRLVLE---KYG------------TEFyilhry 438
Cdd:COG0173 359 NedglkspiakflSEEELAailerlgakpgdliffvadkpkvvnkaLGALRLKlgkELGlidedefaflwvVDF------ 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 439 PL------SVR------PFyTMPC-------HDNPT--YSNSFDVFIRGEEIISGAQRVHVPEfLTERA-QACGIDVKTI 496
Cdd:COG0173 433 PLfeydeeEGRwvamhhPF-TMPKdedldllETDPGkvRAKAYDLVLNGYELGGGSIRIHDPE-LQEKVfELLGISEEEA 510
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1279768844 497 ET----YIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFP 537
Cdd:COG0173 511 EEkfgfLLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
240-537 |
7.16e-30 |
|
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: 119.61 E-value: 7.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 240 FRIQCQVGTIFRQFLLSEGFVEIHTPKLigGSSEGGAS---------VFRLDYKgqpacLAQSPQLHKQMSICGDFGRVF 310
Cdd:cd00775 8 FIVRSKIISYIRKFLDDRGFLEVETPML--QPIAGGAAarpfithhnALDMDLY-----LRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 311 EIGPVFRAEdSFTHRHLCEFTGLDVEMEIKThYSEVMDIVDRLFVSMFDSMNQNCKKELEA--IDKQYPFEplkylrntl 388
Cdd:cd00775 81 EIGRNFRNE-GIDLTHNPEFTMIEFYEAYAD-YNDMMDLTEDLFSGLVKKINGKTKIEYGGkeLDFTPPFK--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 389 RLTFEEGIQmlKDAGVEIDPLGDLNTEAERK---------------LGRLVLEKYGtEF---------YILHrYPLSVRP 444
Cdd:cd00775 150 RVTMVDALK--EKTGIDFPELDLEQPEELAKllaklikekiekprtLGKLLDKLFE-EFveptliqptFIID-HPVEISP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 445 FyTMPCHDNPTYSNSFDVFIRGEEIISG--------AQRVHVPEFLTERAQ----ACGIDvktiETYIDSFRYGAPPHGG 512
Cdd:cd00775 226 L-AKRHRSNPGLTERFELFICGKEIANAytelndpfDQRERFEEQAKQKEAgddeAMMMD----EDFVTALEYGMPPTGG 300
|
330 340
....*....|....*....|....*
gi 1279768844 513 FGVGLERVVMLFCGLNNIRKTSLFP 537
Cdd:cd00775 301 LGIGIDRLVMLLTDSNSIRDVILFP 325
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
282-542 |
1.38e-29 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 122.80 E-value: 1.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 282 DYKGQPACLAQSPQLHKQMSICGdFGRVFEIGPVFRAEDSFTHRHLCEFtgLDVEMEIK-THYSEVMDIVDRLFVSMFDS 360
Cdd:PLN02221 303 DFFGRQAFLTVSGQLQVETYACA-LSSVYTFGPTFRAENSHTSRHLAEF--WMVEPEIAfADLEDDMNCAEAYVKYMCKW 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 361 MNQNCKKELEAIDKQYP---FEPLKYLRNTL--RLTFEEGIQMLKDA---GVEID---PLG-DLNTEAERKLGRLVLEKY 428
Cdd:PLN02221 380 LLDKCFDDMELMAKNFDsgcIDRLRMVASTPfgRITYTEAIELLEEAvakGKEFDnnvEWGiDLASEHERYLTEVLFQKP 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 429 gtefYILHRYPLSVRPFYtMPCHDNPTYSNSFDVFI-RGEEIISGAQRVHVPEFLTERAQACGIDVKTIETYIDSFRYGA 507
Cdd:PLN02221 460 ----LIVYNYPKGIKAFY-MRLNDDEKTVAAMDVLVpKVGELIGGSQREERYDVIKQRIEEMGLPIEPYEWYLDLRRYGT 534
|
250 260 270
....*....|....*....|....*....|....*
gi 1279768844 508 PPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQR 542
Cdd:PLN02221 535 VKHCGFGLGFERMILFATGIDNIRDVIPFPRYPGK 569
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
87-545 |
1.55e-26 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 114.31 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 87 GSLTGELKDKYVILRGRIQTIRAVAKkMAFLVVREKGFTVQCVVSeqPELVSRQMVKYVVGLSRESIVDVEGVV-----S 161
Cdd:PRK12820 10 GHLSLDDTGREVCLAGWVDAFRDHGE-LLFIHLRDRNGFIQAVFS--PEAAPADVYELAASLRAEFCVALQGEVqkrleE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 162 VPNVAIKgaTQQVEIQVRKVYCISKAMpSLPINIEDaarseaeieKALQAGEQLVR---VNQDTRLNYRVLDMRTPANQG 238
Cdd:PRK12820 87 TENPHIE--TGDIEVFVRELSILAASE-ALPFAISD---------KAMTAGAGSAGadaVNEDLRLQYRYLDIRRPAMQD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 239 IFRIQCQVGTIFRQFLLSEGFVEIHTPKLIGGSSEgGASVFRLDYKGQPA---CLAQSPQLHKQMSICGDFGRVFEIGPV 315
Cdd:PRK12820 155 HLAKRHRIIKCARDFLDSRGFLEIETPILTKSTPE-GARDYLVPSRIHPKefyALPQSPQLFKQLLMIAGFERYFQLARC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 316 FRAEDSFTHRHlCEFTGLDVEMEI------------------------------KTHYSEVMD----------------- 348
Cdd:PRK12820 234 FRDEDLRPNRQ-PEFTQLDIEASFideefifelieeltarmfaiggialprpfpRMPYAEAMDttgsdrpdlrfdlkfad 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 349 ---IVDRLFVSMFDSMNQ--------NCKKELEAIDK-----QYPFE--------PLKYLR--------NTLRLTFEEGI 396
Cdd:PRK12820 313 atdIFENTRYGIFKQILQrggrikgiNIKGQSEKLSKnvlqnEYAKEiapsfgakGMTWMRaeaggldsNIVQFFSADEK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 397 QMLK------DAGVEI---DPLGDLNTEAERKL-----GRLVLEKYGTeFYIL--HRYPL-----------SVRPFyTMP 449
Cdd:PRK12820 393 EALKrrfhaeDGDVIImiaDASCAIVLSALGQLrlhlaDRLGLIPEGV-FHPLwiTDFPLfeatddggvtsSHHPF-TAP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 450 chDNPTY------------SNSFDVFIRGEEIISGAQRVHVPEFLTERAQACGIDVKTIET----YIDSFRYGAPPHGGF 513
Cdd:PRK12820 471 --DREDFdpgdieelldlrSRAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDIEDkfgfFLRAFDFAAPPHGGI 548
|
570 580 590
....*....|....*....|....*....|..
gi 1279768844 514 GVGLERVVMLFCGLNNIRKTSLFPRDPQRIAP 545
Cdd:PRK12820 549 ALGLDRVVSMILQTPSIREVIAFPKNRSAACP 580
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
239-540 |
4.00e-26 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 112.42 E-value: 4.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 239 IFRIQCQVGTIFRQFLLSEGFVEIHTPKLIGGSSEGGASVFR-------------------------------------- 280
Cdd:PTZ00425 214 VIRIRNALAIATHLFFQSRGFLYIHTPLITTSDCEGGGEMFTvttllgedadyraiprvnkknkkgekredilntcnann 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 281 ---------------------LDYK----GQPACLAQSPQLHKQmSICGDFGRVFEIGPVFRAEDSFTHRHLCEFTGLDV 335
Cdd:PTZ00425 294 nngnssssnavsspaypdqylIDYKkdffSKQAFLTVSGQLSLE-NLCSSMGDVYTFGPTFRAENSHTSRHLAEFWMIEP 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 336 EMEIKTHYSEvMDIVDRLFVSMFDSMNQNCKKELEAIDKQYPFEPLKYLRNTL-----RLTFEEGIQMLKDAG----VEI 406
Cdd:PTZ00425 373 EIAFADLYDN-MELAESYIKYCIGYVLNNNFDDIYYFEENVETGLISRLKNILdedfaKITYTNVIDLLQPYSdsfeVPV 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 407 DPLGDLNTEAERklgrLVLEKYGTEFYILHRYPLSVRPFYTMPCHDNPTYSnSFDVFI-RGEEIISGAQRVHVPEFLTER 485
Cdd:PTZ00425 452 KWGMDLQSEHER----FVAEQIFKKPVIVYNYPKDLKAFYMKLNEDQKTVA-AMDVLVpKIGEVIGGSQREDNLERLDKM 526
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1279768844 486 AQACGIDVKTIETYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDP 540
Cdd:PTZ00425 527 IKEKKLNMESYWWYRQLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPRYP 581
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
269-538 |
4.19e-26 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 112.66 E-value: 4.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 269 GGSSEGGASVFRLDYKGQPACLAQSPQLHKQMSICGdFGRVFEIGPVFRAEDSFTHRHLCEFTGLDVEMEIkTHYSEVMD 348
Cdd:PLN02532 353 GTSVKADKLSFSKDFFSRPTYLTVSGRLHLESYACA-LGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAF-SELEDAMN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 349 IVDRLFVSMFDSMNQNCKKELEAIDKQYPFEPLKYLRNTL-----RLTFEEGIQMLKDAgveIDPLGDLNTEAERKLGRL 423
Cdd:PLN02532 431 CAEDYFKFLCKWVLENCSEDMKFVSKRIDKTISTRLEAIIssslqRISYTEAVDLLKQA---TDKKFETKPEWGIALTTE 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 424 VLEKYGTEFY----ILHRYPLSVRPFYTMPCHDNPTYSnSFDVFI-RGEEIISGAQRVHVPEFLTERAQACGIDVKTIET 498
Cdd:PLN02532 508 HLSYLADEIYkkpvIIYNYPKELKPFYVRLNDDGKTVA-AFDLVVpKVGTVITGSQNEERMDILNARIEELGLPREQYEW 586
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1279768844 499 YIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPR 538
Cdd:PLN02532 587 YLDLRRHGTVKHSGFSLGFELMVLFATGLPDVRDAIPFPR 626
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
73-542 |
4.38e-26 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 111.69 E-value: 4.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 73 QSKEAKDVANWTQVGSLTGElkdkyVILRGRIQTiRAVAKKMAFLVVREKGFTVQCVVSEQ--PELVSRQMVKYVvglsr 150
Cdd:PRK12445 48 QLHEEFDAKDNQELESLNIE-----VSVAGRMMT-RRIMGKASFVTLQDVGGRIQLYVARDslPEGVYNDQFKKW----- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 151 esivDVEGVVSVPNVAIKGATQQVEIQVRKVYCISKAMPSLPINIEdaarseaeiekALQageqlvrvNQDTRLNYRVLD 230
Cdd:PRK12445 117 ----DLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFH-----------GLQ--------DQEVRYRQRYLD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 231 M-RTPANQGIFRIQCQVGTIFRQFLLSEGFVEIHTP--KLIGGSSEGGASVFRLDYKGQPACLAQSPQLHKQMSICGDFG 307
Cdd:PRK12445 174 LiANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPmmQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 308 RVFEIGPVFRAEdSFTHRHLCEFTgldvEMEIKTHYSEVMDIVDrLFVSMFDSMNQNCKKELEA------IDKQYPFEPL 381
Cdd:PRK12445 254 RVFEINRNFRNE-GISVRHNPEFT----MMELYMAYADYHDLIE-LTESLFRTLAQEVLGTTKVtygehvFDFGKPFEKL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 382 KYLRNTLRLTFEEGIQMLK--DAGVEIDPLGDLNTEAERKLGRLVLEKYG--TEFYILH-----RYPLSVRPFYTMpcHD 452
Cdd:PRK12445 328 TMREAIKKYRPETDMADLDnfDAAKALAESIGITVEKSWGLGRIVTEIFDevAEAHLIQptfitEYPAEVSPLARR--ND 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 453 -NPTYSNSFDVFIRGEEIISGAQRVHVPEFLTER------AQACGIDVKTI--ETYIDSFRYGAPPHGGFGVGLERVVML 523
Cdd:PRK12445 406 vNPEITDRFEFFIGGREIGNGFSELNDAEDQAERfqeqvnAKAAGDDEAMFydEDYVTALEYGLPPTAGLGIGIDRMIML 485
|
490 500
....*....|....*....|
gi 1279768844 524 FCGLNNIRKTSLFP-RDPQR 542
Cdd:PRK12445 486 FTNSHTIRDVILFPaMRPQK 505
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
61-538 |
6.43e-26 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 112.19 E-value: 6.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 61 SANYGDVPLSDLQSkeAKDVANWTQVGSLTGELKDKYVILRGRIQTIRAVAKKM---AFLVVREKGFTVQCVVSEQ--PE 135
Cdd:PLN02903 36 SAATVIPVVSAVDS--MSSQLTWPSRSHLCGALSVNDVGSRVTLCGWVDLHRDMgglTFLDVRDHTGIVQVVTLPDefPE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 136 ---LVSRQMVKYVVGlsresivdVEGVV-----SVPNVAIKgaTQQVEIQVRKVYCISKAMPSLPINIedaarSEAEIEK 207
Cdd:PLN02903 114 ahrTANRLRNEYVVA--------VEGTVrsrpqESPNKKMK--TGSVEVVAESVDILNVVTKSLPFLV-----TTADEQK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 208 ALqageqlvrVNQDTRLNYRVLDMRTPANQGIFRIQCQVGTIFRQFLLS-EGFVEIHTPKLIGGSSEGGasvfrLDY--- 283
Cdd:PLN02903 179 DS--------IKEEVRLRYRVLDLRRPQMNANLRLRHRVVKLIRRYLEDvHGFVEIETPILSRSTPEGA-----RDYlvp 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 284 -KGQPA---CLAQSPQLHKQMSICGDFGRVFEIGPVFRAEDSFTHRHlCEFTGLDVEMEIkTHYSEVMDIVDRLFVSMFd 359
Cdd:PLN02903 246 sRVQPGtfyALPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQ-PEFTQLDMELAF-TPLEDMLKLNEDLIRQVF- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 360 smnqnckKELEAIDKQYPFEPLKY-------------LRNTLRLT----------FEEGIQMLKDAGV------------ 404
Cdd:PLN02903 323 -------KEIKGVQLPNPFPRLTYaeamskygsdkpdLRYGLELVdvsdvfaessFKVFAGALESGGVvkaicvpdgkki 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 405 ---EIDPLGDLNTEA-----------------------------------------------------------ERKLGR 422
Cdd:PLN02903 396 snnTALKKGDIYNEAiksgakglaflkvlddgelegikalveslspeqaeqllaacgagpgdlilfaagptssvNKTLDR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 423 L---VLEKYG------------TEFYIL------HRYPLSVRPFyTMPCHDNP-TYSN----SFDVFIRGEEIISGAQRV 476
Cdd:PLN02903 476 LrqfIAKTLDlidpsrhsilwvTDFPMFewnedeQRLEALHHPF-TAPNPEDMgDLSSaralAYDMVYNGVEIGGGSLRI 554
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1279768844 477 HVPEFLTERAQACGIDVKTIET----YIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPR 538
Cdd:PLN02903 555 YRRDVQQKVLEAIGLSPEEAESkfgyLLEALDMGAPPHGGIAYGLDRLVMLLAGAKSIRDVIAFPK 620
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
102-537 |
7.58e-25 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 108.97 E-value: 7.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 102 GRIQTIRAVAKkMAFLVVREKGFTVQCVVSEQPELVSRQMVKYVVGLSRESIVDVEGVvsvPNVAIKG----ATQQVEIQ 177
Cdd:PTZ00385 114 GRVTSVRDIGK-IIFVTIRSNGNELQVVGQVGEHFTREDLKKLKVSLRVGDIIGADGV---PCRMQRGelsvAASRMLIL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 178 VRKVYCISKAMPSLpiniedaaRSEAEIEkalqageqlvrvNQDTRLNYRVLDMRT-PANQGIFRIQCQVGTIFRQFLLS 256
Cdd:PTZ00385 190 SPYVCTDQVVCPNL--------RGFTVLQ------------DNDVKYRYRFTDMMTnPCVIETIKKRHVMLQALRDYFNE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 257 EGFVEIHTPKLIGGSSEGGASVFRLDYKGQPA--CLAQSPQLHKQMSICGDFGRVFEIGPVFRAEDSfTHRHLCEFTGLD 334
Cdd:PTZ00385 250 RNFVEVETPVLHTVASGANAKSFVTHHNANAMdlFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDA-DRSHNPEFTSCE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 335 VEMEIKThYSEVMDIVDRLFVSMFDSMN---------QNCKKELEAIDKQYPFEplkylrntlRLTFEEGIQMLkdAGVE 405
Cdd:PTZ00385 329 FYAAYHT-YEDLMPMTEDIFRQLAMRVNgttvvqiypENAHGNPVTVDLGKPFR---------RVSVYDEIQRM--SGVE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 406 IDPLGDLNTEAERKLGRLVLEKYG----------------TEFYILHRYplsVRPFYTMpchDNPTY------------- 456
Cdd:PTZ00385 397 FPPPNELNTPKGIAYMSVVMLRYNiplppvrtaakmfeklIDFFITDRV---VEPTFVM---DHPLFmsplakeqvsrpg 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 457 -SNSFDVFIRGEEIISGAQRVHVPEFLTERAQACGID--------VKTIETYIDSFRYGAPPHGGFGVGLERVVMLFCGL 527
Cdd:PTZ00385 471 lAERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLVDrqggdeeaMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNS 550
|
490
....*....|
gi 1279768844 528 NNIRKTSLFP 537
Cdd:PTZ00385 551 SNIRDGIIFP 560
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
91-537 |
8.22e-25 |
|
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: 8.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 91 GELKDKYVILRGRIQTIRaVAKKMAFLVVREKGFTVQCVVS--EQPELVSRQMVKYVVGlsreSIVDVEGVVsvpnvaIK 168
Cdd:COG1190 52 EEETGDEVSVAGRIMAKR-DMGKASFADLQDGSGRIQLYLRrdELGEEAYELFKLLDLG----DIVGVEGTV------FR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 169 GATQQVEIQVRKVYCISKAMPSLPiniedaarseaEIEKALQAGEQLVR-------VNQDTRlnyRVLDMRTPANQGIfr 241
Cdd:COG1190 121 TKTGELSVKVEELTLLSKSLRPLP-----------EKFHGLTDPETRYRqryvdliVNPEVR---ETFRKRSKIIRAI-- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 242 iqcqvgtifRQFLLSEGFVEIHTPKLigGSSEGGASV--FR-----LDykgQPACLAQSPQLH-KQMsICGDFGRVFEIG 313
Cdd:COG1190 185 ---------RRFLDERGFLEVETPML--QPIAGGAAArpFIthhnaLD---MDLYLRIAPELYlKRL-IVGGFERVFEIG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 314 PVFRAEDSfTHRHLCEFTgldvEMEI----KThYSEVMDIVDRLFVSMFDSMNQNCKKEL--EAIDKQYPFEplkylrnt 387
Cdd:COG1190 250 RNFRNEGI-DTTHNPEFT----MLELyqayAD-YNDMMDLTEELIREAAEAVLGTTKVTYqgQEIDLSPPWR-------- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 388 lRLTFEEGIqmLKDAGVEIDPLGDLNT---EAERK---------LGRLVLEKYGT--E-------FYILhrYPLSVRPFy 446
Cdd:COG1190 316 -RITMVEAI--KEATGIDVTPLTDDEElraLAKELgievdpgwgRGKLIDELFEElvEpkliqptFVTD--YPVEVSPL- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 447 TMPCHDNPTYSNSFDVFIRGEEIisgA-----------QRvhvpEFLTERAQ--------ACGIDvktiETYIDSFRYGA 507
Cdd:COG1190 390 AKRHRDDPGLTERFELFIAGREI---AnafselndpidQR----ERFEEQLElkaagddeAMPMD----EDFLRALEYGM 458
|
490 500 510
....*....|....*....|....*....|
gi 1279768844 508 PPHGGFGVGLERVVMLFCGLNNIRKTSLFP 537
Cdd:COG1190 459 PPTGGLGIGIDRLVMLLTDSPSIRDVILFP 488
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
92-537 |
4.46e-23 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 102.76 E-value: 4.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 92 ELKDKYVILRGRIQTIRAVAKkMAFLVVREKGFTVQcVVSEQPELVSRQMV--KYVVGLSRESIVDVEGVVsvpnvaikG 169
Cdd:PLN02502 105 ELEDVSVSVAGRIMAKRAFGK-LAFYDLRDDGGKIQ-LYADKKRLDLDEEEfeKLHSLVDRGDIVGVTGTP--------G 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 170 ATQQVE--IQVRKVYCISKA---MPSLPINIEDaarseaeiekalqageqlvrvnQDTRLNYRVLDM-RTPANQGIFRIQ 243
Cdd:PLN02502 175 KTKKGElsIFPTSFEVLTKCllmLPDKYHGLTD----------------------QETRYRQRYLDLiANPEVRDIFRTR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 244 CQVGTIFRQFLLSEGFVEIHTPKLIGGSseGGASV--FRLDYK--GQPACLAQSPQLHKQMSICGDFGRVFEIGPVFRAE 319
Cdd:PLN02502 233 AKIISYIRRFLDDRGFLEVETPMLNMIA--GGAAArpFVTHHNdlNMDLYLRIATELHLKRLVVGGFERVYEIGRQFRNE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 320 DSFThRHLCEFTglDVEM-EIKTHYSEVMDIVDRLFVSMFDSMNQNCKKELEA--IDKQYPF---EPLKYLRNTLRLTFE 393
Cdd:PLN02502 311 GIST-RHNPEFT--TCEFyQAYADYNDMMELTEEMVSGMVKELTGSYKIKYHGieIDFTPPFrriSMISLVEEATGIDFP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 394 EGI--QMLKDAGVEIDPLGDLNTEAERKLGRLVLEKYGtEF---------YILHrYPLSVRPFyTMPCHDNPTYSNSFDV 462
Cdd:PLN02502 388 ADLksDEANAYLIAACEKFDVKCPPPQTTGRLLNELFE-EFleetlvqptFVLD-HPVEMSPL-AKPHRSKPGLTERFEL 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 463 FIRGEEIISG--------AQRVHVPEFLTERA----QACGIDvktiETYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNI 530
Cdd:PLN02502 465 FINGRELANAfseltdpvDQRERFEEQVKQHNagddEAMALD----EDFCTALEYGLPPTGGWGLGIDRLVMLLTDSASI 540
|
....*..
gi 1279768844 531 RKTSLFP 537
Cdd:PLN02502 541 RDVIAFP 547
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
92-537 |
3.24e-20 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 93.62 E-value: 3.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 92 ELKDKYVILRGRIQTIRaVAKKMAFLVVREKGFTVQCVVSeqPELVSRQMVKYVVGLSRESIVDVEGVVsvpnvaIKGAT 171
Cdd:PRK00484 51 EELEIEVSVAGRVMLKR-VMGKASFATLQDGSGRIQLYVS--KDDVGEEALEAFKKLDLGDIIGVEGTL------FKTKT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 172 QQVEIQVRKVYCISKAMPSLPiniedaarseaeiEK--ALQageqlvrvNQDTRLNYRVLDMRT-PANQGIFRIQCQVGT 248
Cdd:PRK00484 122 GELSVKATELTLLTKSLRPLP-------------DKfhGLT--------DVETRYRQRYVDLIVnPESRETFRKRSKIIS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 249 IFRQFLLSEGFVEIHTPKLiggSSE-GGASVfR--------LDykgQPACLAQSPQLH-KQMsICGDFGRVFEIGPVFRA 318
Cdd:PRK00484 181 AIRRFLDNRGFLEVETPML---QPIaGGAAA-RpfithhnaLD---IDLYLRIAPELYlKRL-IVGGFERVYEIGRNFRN 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 319 EDSFThRHLCEFTgldvEMEI----KThYSEVMDIVDRLFVSMFDSMNQNCKKEL--EAIDKQYPFEPLKYL-------- 384
Cdd:PRK00484 253 EGIDT-RHNPEFT----MLEFyqayAD-YNDMMDLTEELIRHLAQAVLGTTKVTYqgTEIDFGPPFKRLTMVdaikeytg 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 385 RNTLRLTFEEGIQMLKDAGVEIDPlgdlnteaERKLGRLVLEKYGtEF---------YILHrYPLSVRPFyTMPCHDNPT 455
Cdd:PRK00484 327 VDFDDMTDEEARALAKELGIEVEK--------SWGLGKLINELFE-EFvepkliqptFITD-YPVEISPL-AKRHREDPG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 456 YSNSFDVFIRGEEIISG----------AQRVHvpEFLTERAQ----ACGIDvktiETYIDSFRYGAPPHGGFGVGLERVV 521
Cdd:PRK00484 396 LTERFELFIGGREIANAfselndpidqRERFE--AQVEAKEAgddeAMFMD----EDFLRALEYGMPPTGGLGIGIDRLV 469
|
490
....*....|....*.
gi 1279768844 522 MLFCGLNNIRKTSLFP 537
Cdd:PRK00484 470 MLLTDSPSIRDVILFP 485
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
90-537 |
1.36e-14 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 76.59 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 90 TGE-LKDKYVILRGRIQTIRAVAKKMAFLVVREKGFTVQCVVSeqpeLVSRQMVKYVVGLSRESIV--DVEGVVSVPNVA 166
Cdd:PTZ00417 126 SGEhLEDTILNVTGRIMRVSASGQKLRFFDLVGDGAKIQVLAN----FAFHDHTKSNFAECYDKIRrgDIVGIVGFPGKS 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 167 IKGatqQVEIQVRKVYCISKAMPSLPINIedaARSEAEIekalqageqlvrvnqdtRLNYRVLD-MRTPANQGIFRIQCQ 245
Cdd:PTZ00417 202 KKG---ELSIFPKETIILSPCLHMLPMKY---GLKDTEI-----------------RYRQRYLDlMINESTRSTFITRTK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 246 VGTIFRQFLLSEGFVEIHTP--KLIGGSSEGGASVFRLDYKGQPACLAQSPQLHKQMSICGDFGRVFEIGPVFRAEdSFT 323
Cdd:PTZ00417 259 IINYLRNFLNDRGFIEVETPtmNLVAGGANARPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFRNE-GID 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 324 HRHLCEFTGLDVEMEIKTHYSEVM---DIVDRLFVSMFD----SMNQNC-KKELEAIDKQYPF------EPLKYLRNTL- 388
Cdd:PTZ00417 338 NTHNPEFTSCEFYWAYADFYDLIKwseDFFSQLVMHLFGtykiLYNKDGpEKDPIEIDFTPPYpkvsivEELEKLTNTKl 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 389 ------RLTFEEGIQMLKDAGVEIDplgdlNTEAERKLgrlvLEKYGTEFyILHRYPlsVRPFYTM-------PC----H 451
Cdd:PTZ00417 418 eqpfdsPETINKMINLIKENKIEMP-----NPPTAAKL----LDQLASHF-IENKYP--NKPFFIIehpqimsPLakyhR 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 452 DNPTYSNSFDVFIRGEEIISGAQRVHVPEFLTERAQACGIDVKTIET--------YIDSFRYGAPPHGGFGVGLERVVML 523
Cdd:PTZ00417 486 SKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAeafqfdaaFCTSLEYGLPPTGGLGLGIDRITMF 565
|
490
....*....|....
gi 1279768844 524 FCGLNNIRKTSLFP 537
Cdd:PTZ00417 566 LTNKNCIKDVILFP 579
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
219-537 |
7.10e-14 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 74.62 E-value: 7.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 219 NQDTRLNYRVLDMRT-PANQGIFRIQCQVGTIFRQFLLSEGFVEIHTPKLigGSSEGGAS----VFRLDYKGQPACLAQS 293
Cdd:PRK02983 748 DPEARVRQRYLDLAVnPEARDLLRARSAVVRAVRETLVARGFLEVETPIL--QQVHGGANarpfVTHINAYDMDLYLRIA 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 294 PQLH-KQMSIcGDFGRVFEIGPVFRAED-SFTHRHlcEFTGLDVeMEIKTHYSEVMDIVDRLFVSMfdSMNQNCKKELEA 371
Cdd:PRK02983 826 PELYlKRLCV-GGVERVFELGRNFRNEGvDATHNP--EFTLLEA-YQAHADYDTMRDLTRELIQNA--AQAAHGAPVVMR 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 372 IDKQYPFEPLkylrntlRLTFEEGIQMLKDA-----GVEIDPlgDLNTEAERKL--------------GRLVLEKYG--- 429
Cdd:PRK02983 900 PDGDGVLEPV-------DISGPWPVVTVHDAvsealGEEIDP--DTPLAELRKLcdaagipyrtdwdaGAVVLELYEhlv 970
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 430 ---TE---FYIlhRYPLSVRPFyTMPCHDNPTYSNSFDVFIRGEEIisGA----------QRvhvpEFLTERA-QACGID 492
Cdd:PRK02983 971 edrTTfptFYT--DFPTSVSPL-TRPHRSDPGLAERWDLVAWGVEL--GTayseltdpveQR----RRLTEQSlLAAGGD 1041
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1279768844 493 VKTI---ETYIDSFRYGAPPHGGFGVGLERVVMLFCGlNNIRKTSLFP 537
Cdd:PRK02983 1042 PEAMeldEDFLQALEYAMPPTGGLGMGVDRLVMLLTG-RSIRETLPFP 1088
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
98-186 |
1.36e-13 |
|
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: 66.05 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 98 VILRGRIQTIRAvAKKMAFLVVREKGFTVQCVVSEQPELVsrqMVKYVVGLSRESIVDVEG-VVSVPNVAIkgATQQVEI 176
Cdd:cd04100 2 VTLAGWVHSRRD-HGGLIFIDLRDGSGIVQVVVNKEELGE---FFEEAEKLRTESVVGVTGtVVKRPEGNL--ATGEIEL 75
|
90
....*....|
gi 1279768844 177 QVRKVYCISK 186
Cdd:cd04100 76 QAEELEVLSK 85
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
250-519 |
2.18e-12 |
|
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: 66.37 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 250 FRQFLLSEGFVEIHTPKLIGGSSEGGAS------VFRLDYKGQPACLAQSPQLHKQMS----ICGDFGRVFEIGPVFRAE 319
Cdd:cd00768 9 LRRFMAELGFQEVETPIVEREPLLEKAGhepkdlLPVGAENEEDLYLRPTLEPGLVRLfvshIRKLPLRLAEIGPAFRNE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 320 D-SFTHRHLCEFTGLDVEMeikthysevmdivdrlFVSmfdsmnqnckkeleaidkqyPFEPLKYLRNTLRLTFEegiqM 398
Cdd:cd00768 89 GgRRGLRRVREFTQLEGEV----------------FGE--------------------DGEEASEFEELIELTEE----L 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 399 LKDAGVEIDPlgdlnteaerklgrLVLEKYGTEFYILHrYPLSVRPFYTMPCHdnptysnsfdvfiRGEEIISGAQRVHV 478
Cdd:cd00768 129 LRALGIKLDI--------------VFVEKTPGEFSPGG-AGPGFEIEVDHPEG-------------RGLEIGSGGYRQDE 180
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1279768844 479 PEflteraqacgiDVKTIETYIDSFRYGAPPHGGFGVGLER 519
Cdd:cd00768 181 QA-----------RAADLYFLDEALEYRYPPTIGFGLGLER 210
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
87-234 |
4.36e-08 |
|
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: 52.14 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 87 GSLTGELKDKYVILRGRIQTIRaVAKKMAFLVVREKGFTVQCVVSEQPELVSRQMVKyvvgLSRESIVDVEGVVSV---P 163
Cdd:cd04317 6 GELRESHVGQEVTLCGWVQRRR-DHGGLIFIDLRDRYGIVQVVFDPEEAPEFELAEK----LRNESVIQVTGKVRArpeG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1279768844 164 NVAIKGATQQVEIQVRKVYCISKAMPsLPINIEDAarseaeiekalqageqlVRVNQDTRLNYRVLDMRTP 234
Cdd:cd04317 81 TVNPKLPTGEIEVVASELEVLNKAKT-LPFEIDDD-----------------VNVSEELRLKYRYLDLRRP 133
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
90-195 |
5.52e-08 |
|
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: 51.16 E-value: 5.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 90 TGELKDKYVILRGRIQTIRAVAKKmAFLVVREKGFTVQCVVSEQpeLVSRQMVKYVVGLSRESIVDVEGVVSvpnvAIKG 169
Cdd:cd04316 7 TPELDGEEVTVAGWVHEIRDLGGI-KFVILRDREGIVQVTAPKK--KVDKELFKTVRKLSRESVISVTGTVK----AEPK 79
|
90 100
....*....|....*....|....*.
gi 1279768844 170 ATQQVEIQVRKVYCISKAMPSLPINI 195
Cdd:cd04316 80 APNGVEIIPEEIEVLSEAKTPLPLDP 105
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
98-184 |
3.77e-06 |
|
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: 44.92 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 98 VILRGRIQTIRAVAKKMAFLVVREKGFTVQCVVSEQpelvsrQMVKYVVGLSRESIVDVEGVVSVPNvaikgaTQQVEIQ 177
Cdd:pfam01336 1 VTVAGRVTSIRRSGGKLLFLTLRDGTGSIQVVVFKE------EAEKLAKKLKEGDVVRVTGKVKKRK------GGELELV 68
|
....*..
gi 1279768844 178 VRKVYCI 184
Cdd:pfam01336 69 VEEIELL 75
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
98-200 |
3.24e-05 |
|
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: 42.90 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 98 VILRGRIQTIRAVAKKmAFLVVREKGFTVQCVVseqPELVSRQMVKYVVGLSRESIVDVEGVVSVPNVAIKGAtqqvEIQ 177
Cdd:cd04319 2 VTLAGWVYRKREVGKK-AFIVLRDSTGIVQAVF---SKDLNEEAYREAKKVGIESSVIVEGAVKADPRAPGGA----EVH 73
|
90 100
....*....|....*....|...
gi 1279768844 178 VRKVYCISKAMPsLPINiEDAAR 200
Cdd:cd04319 74 GEKLEIIQNVEF-FPIT-EDASD 94
|
|
| pylS |
PRK09537 |
pyrrolysine--tRNA(Pyl) ligase; |
121-384 |
1.39e-04 |
|
pyrrolysine--tRNA(Pyl) ligase;
Pssm-ID: 236555 [Multi-domain] Cd Length: 417 Bit Score: 44.45 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 121 EKGFTVQCVVSEQPELVSRQMVKYVV----GLSRESIVDVEGVVSVPNVAIKGATQQVEI--------QVRKVYCISKAM 188
Cdd:PRK09537 88 EDKTQVKVKVVSAPTKKKKAMPKSVVrapkPLENPVPAQAESSGSKPVPSIPVSTPEVKApapaltpsQKDRLETLLSPK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 189 PSLPINIEDAARSEAEIEKALQAGEQLVRVNQDTRLNYrvldmrtpanqgifriqcqVGTIFR---QFLLSEGFVEIHTP 265
Cdd:PRK09537 168 DKISLNSEKPKFKELESELVSRRKNDLKQMYEEDREDY-------------------LGKLERditKFFVDRGFLEIKSP 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 266 KLI--------GGSSEGGAS--VFRLDYKgqpACLAQ--SPQL----HKQMSICGDFGRVFEIGPVFRAEdSFTHRHLCE 329
Cdd:PRK09537 229 ILIpaeyiermGIDNDTELSkqIFRVDKN---FCLRPmlAPGLynylRKLDRILPDPIKIFEIGPCYRKE-SDGKEHLEE 304
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1279768844 330 FTGLDvemeikthysevmdivdrlfvsmFDSMNQNCKKE-LEAIDKQYpfepLKYL 384
Cdd:PRK09537 305 FTMVN-----------------------FCQMGSGCTREnLENIIDDF----LKHL 333
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
98-186 |
3.82e-04 |
|
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: 39.52 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279768844 98 VILRGRIQTIRaVAKKMAFLVVREKGFTVQCVVSEqpELVSRQMVkyVVGLSRESIVDVEGVVSVPNVAiKGATQQVEIQ 177
Cdd:cd04323 2 VKVFGWVHRLR-SQKKLMFLVLRDGTGFLQCVLSK--KLVTEFYD--AKSLTQESSVEVTGEVKEDPRA-KQAPGGYELQ 75
|
....*....
gi 1279768844 178 VRKVYCISK 186
Cdd:cd04323 76 VDYLEIIGE 84
|
|
| |
