|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
20-501 |
0e+00 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 732.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 20 AAEDYAKERYGISSMIQSQEKPD-RVLVRVKDLTVQKADDVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGD-HA 97
Cdd:PLN02850 43 DEDDPLASNYGDVPLEELQSKVTgREWTDVSDLGEELAGSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQCVVFVSEvTV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 98 SKQMVKFAANINKESIIDVEGVVRKVNQKIGSCTQQdVELHVQKIYVISLAEPRLPLQLDDAIRPEVEGEEDGR-----A 172
Cdd:PLN02850 123 SKGMVKYAKQLSRESVVDVEGVVSVPKKPVKGTTQQ-VEIQVRKIYCVSKALATLPFNVEDAARSESEIEKALQtgeqlV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 173 TVNQDTRLDNRVIDLRTSTSQAIFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQL 252
Cdd:PLN02850 202 RVGQDTRLNNRVLDLRTPANQAIFRIQSQVCNLFREFLLSKGFVEIHTPKLIAGASEGGSAVFRLDYKGQPACLAQSPQL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 253 YKQMCICADFEKVFCIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVVEEIADTLVQIFKGLQERFQTEIQTVSKQF 332
Cdd:PLN02850 282 HKQMAICGDFRRVFEIGPVFRAEDSFTHRHLCEFTGLDLEMEIKEHYSEVLDVVDELFVAIFDGLNERCKKELEAIREQY 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 333 PCEPFKFLEPTLRLEYCEALAMLREAGVEMDDEEDLSTPNEKLLGRLVKEKYDTDFYVLDKYPLAVRPFYTMPDPRNPKQ 412
Cdd:PLN02850 362 PFEPLKYLPKTLRLTFAEGIQMLKEAGVEVDPLGDLNTESERKLGQLVKEKYGTDFYILHRYPLAVRPFYTMPCPDDPKY 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 413 SNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMF 492
Cdd:PLN02850 442 SNSFDVFIRGEEIISGAQRVHDPELLEKRAEECGIDVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLF 521
|
....*....
gi 211065507 493 PRDPKRLTP 501
Cdd:PLN02850 522 PRDPQRLAP 530
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
6-501 |
0e+00 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 528.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 6 ASRKGQEKPREIVDAA--EDYaKERYGISSMIQSQEKPDRVLVRVKDLTVQK-ADDVVWVRARVHTSRAKGKQCFLVLRQ 82
Cdd:PTZ00401 25 AARLAEEKARAAEKAAlvEKY-KDVFGAAPMVQSTTYKSRTFIPVAVLSKPElVDKTVLIRARVSTTRKKGKMAFMVLRD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 83 QQFNVQALVAVGDHASKQMVKFAANINKESIIDVEGVVRKVNQKIGSCTQQDVELHVQKIYVISLAEPRLPLQLDDAIRP 162
Cdd:PTZ00401 104 GSDSVQAMAAVEGDVPKEMIDFIGQIPTESIVDVEATVCKVEQPITSTSHSDIELKVKKIHTVTESLRTLPFTLEDASRK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 163 EvegeEDGRATVNQDTRLDNRVIDLRTSTSQAIFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKN 242
Cdd:PTZ00401 184 E----SDEGAKVNFDTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDSDFCEIHSPKIINAPSEGGANVFKLEYFNR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 243 NAYLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVVEEIADTLVQIFKGLQERfQ 322
Cdd:PTZ00401 260 FAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHLTEFVGLDVEMRINEHYYEVLDLAESLFNYIFERLATH-T 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 323 TEIQTVSKQFPCEPFKF------------------LEPT--------------LRLEYCEALAMLREAGVE-MDDEEDLS 369
Cdd:PTZ00401 339 KELKAVCQQYPFEPLVWkltpermkelgvgvisegVEPTdkyqarvhnmdsrmLRINYMHCIELLNTVLEEkMAPTDDIN 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 370 TPNEKLLGRLVKEKYDTDFYVLDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGIDL 449
Cdd:PTZ00401 419 TTNEKLLGKLVKERYGTDFFISDRFPSSARPFYTMECKDDERFTNSYDMFIRGEEISSGAQRIHDPDLLLARAKMLNVDL 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 211065507 450 EKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 501
Cdd:PTZ00401 499 TPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPRDPQRTTP 550
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
174-497 |
1.04e-173 |
|
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: 491.31 E-value: 1.04e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 174 VNQDTRLDNRVIDLRTSTSQAIFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLY 253
Cdd:cd00776 2 ANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 254 KQMCICAdFEKVFCIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVVEEIADTLVQIFKGLQERFQTEIQTVsKQFP 333
Cdd:cd00776 82 KEMLIAA-LERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRVLERCAKELELV-NQLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 334 CEPFKFLEPTLRLEYCEALAMLREAGV--EMDDEEDLSTPNEKLLGRLVKekydTDFYVLDKYPLAVRPFYTMPDPRNPK 411
Cdd:cd00776 160 RELLKPLEPFPRITYDEAIELLREKGVeeEVKWGEDLSTEHERLLGEIVK----GDPVFVTDYPKEIKPFYMKPDDDNPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 412 QSNSYDMFMRG-EEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTS 490
Cdd:cd00776 236 TVESFDLLMPGvGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAI 315
|
....*..
gi 211065507 491 MFPRDPK 497
Cdd:cd00776 316 LFPRDPK 322
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
46-501 |
2.19e-166 |
|
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: 477.01 E-value: 2.19e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 46 VRVKDLTVQKADDVVWVRARVHTSRAKGKQCFLVLRQQQFNVQaLVAVGDHASKQMVKFAANINKESIIDVEGVVRkvnq 125
Cdd:TIGR00458 1 VYSADIKPEMDGQEVTFMGWVHEIRDLGGLIFVLLRDREGLIQ-ITAPAKKVSKNLFKWAKKLNLESVVAVRGIVK---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 126 kIGSCTQQDVELHVQKIYVISLAEPRLPLQLDDAIRPEVegeedgratvnqDTRLDNRVIDLRTSTSQAIFRLQSGICHL 205
Cdd:TIGR00458 76 -IKEKAPGGFEIIPTKIEVINEAKEPLPLDPTEKVPAEL------------DTRLDYRFLDLRRPTVQAIFRIRSGVLES 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 206 FRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNTHRHLTE 285
Cdd:TIGR00458 143 VREFLAEEGFIEVHTPKLVASATEGGTELFPITYFEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHRHLNE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 286 FVGLDIEMAFNYHyHEVVEEIADTLVQIFKGLQERFQTEIQTVSKQFPCEPFKFleptLRLEYCEALAMLREAGVEMDDE 365
Cdd:TIGR00458 223 ATSIDIEMAFEDH-HDVMDILEELVVRVFEDVPERCAHQLETLEFKLEKPEGKF----VRLTYDEAIEMANAKGVEIGWG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 366 EDLSTPNEKLLGrlvkEKYDTDFYVLDkYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHH 445
Cdd:TIGR00458 298 EDLSTEAEKALG----EEMDGLYFITD-WPTEIRPFYTMPDEDNPEISKSFDLMYRDLEISSGAQRIHLHDLLVERIKAK 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 211065507 446 GIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 501
Cdd:TIGR00458 373 GLNPEGFKDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRKRLTP 428
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
48-501 |
2.99e-158 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 456.57 E-value: 2.99e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 48 VKDLTVQKADDVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDhaSKQMVKFAANINKESIIDVEGVVRKVNQKI 127
Cdd:PRK05159 7 TSELTPELDGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKV--DEELFETIKKLKRESVVSVTGTVKANPKAP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 128 GSctqqdVELHVQKIYVISLAEPRLPLqlddairpEVEGEEDgrATVnqDTRLDNRVIDLRTSTSQAIFRLQSGICHLFR 207
Cdd:PRK05159 85 GG-----VEVIPEEIEVLNKAEEPLPL--------DISGKVL--AEL--DTRLDNRFLDLRRPRVRAIFKIRSEVLRAFR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 208 ETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNTHRHLTEFV 287
Cdd:PRK05159 148 EFLYENGFTEIFTPKIVASGTEGGAELFPIDYFEKEAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRHLNEYT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 288 GLDIEMAFNYHYHEVVEEIADTLVQIFKGLQERFQTEIQTVSKQFPCEPfkflEPTLRLEYCEALAMLREAGVEMDDEED 367
Cdd:PRK05159 228 SIDVEMGFIDDHEDVMDLLENLLRYMYEDVAENCEKELELLGIELPVPE----TPIPRITYDEAIEILKSKGNEISWGDD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 368 LSTPNEKLLGRLVKEKYDTDFYVLDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGI 447
Cdd:PRK05159 304 LDTEGERLLGEYVKEEYGSDFYFITDYPSEKRPFYTMPDEDDPEISKSFDLLFRGLEITSGGQRIHRYDMLVESIKEKGL 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 211065507 448 DLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 501
Cdd:PRK05159 384 NPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPRDRHRLTP 437
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
46-501 |
1.07e-155 |
|
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: 449.89 E-value: 1.07e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 46 VRVKDLTVQKADDVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMVKfaaNINKESIIDVEGVVRKVNQ 125
Cdd:COG0017 3 TYIKDLLPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKLENFEEAK---KLTTESSVEVTGTVVESPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 126 KigsctQQDVELHVQKIYVISLAEPRLPLQLDDAirpevegeedgratvNQDTRLDNRVIDLRTSTSQAIFRLQSGICHL 205
Cdd:COG0017 80 A-----PQGVELQAEEIEVLGEADEPYPLQPKRH---------------SLEFLLDNRHLRLRTNRFGAIFRIRSELARA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 206 FRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLYKQMCICAdFEKVFCIGPVFRAEDSNTHRHLTE 285
Cdd:COG0017 140 IREFFQERGFVEVHTPIITASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMA-LEKVYTFGPTFRAEKSNTRRHLAE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 286 FVGLDIEMAFnYHYHEVVEEIADTLVQIFKGLQERFQTEIQTVS------KQFPCEPFKfleptlRLEYCEALAMLREAG 359
Cdd:COG0017 219 FWMIEPEMAF-ADLEDVMDLAEEMLKYIIKYVLENCPEELEFLGrdverlEKVPESPFP------RITYTEAIEILKKSG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 360 VEMDDEEDLSTPNEKLLGrlvkEKYDTDFYVLDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRG-EEILSGAQRIHDPQLL 438
Cdd:COG0017 292 EKVEWGDDLGTEHERYLG----EEFFKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGiGEIIGGSQREHRYDVL 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 211065507 439 TERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 501
Cdd:COG0017 368 VERIKEKGLDPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
175-496 |
3.52e-102 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 309.11 E-value: 3.52e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 175 NQDTRLDNRVIDLRTSTSQAIFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNN--AYLAQSPQL 252
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGkfYALPQSPQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 253 YKQMCICADFEKVFCIGPVFRAEDSNTHRHLtEFVGLDIEMAFNyHYHEVVEEIADTLVQIFKGLQERFQTEIQTVSKQF 332
Cdd:pfam00152 81 YKQLLMVAGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFV-DYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 333 PcEPFKfleptlRLEYCEALAMLREAGVEmDDEEDLSTPNEKLLGRLVKEKYDTDFYVLDKYPLAVRPFYTMPDPRNPKQ 412
Cdd:pfam00152 159 K-KPFP------RITYAEAIEKLNGKDVE-ELGYGSDKPDLRFLLELVIDKNKFNPLWVTDFPAEHHPFTMPKDEDDPAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 413 SNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGIDLEKIKA----YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQ 488
Cdd:pfam00152 231 AEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPEEAEEkfgfYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIRE 310
|
....*...
gi 211065507 489 TSMFPRDP 496
Cdd:pfam00152 311 VIAFPKTR 318
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
46-501 |
1.34e-78 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 252.72 E-value: 1.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 46 VRVKDLTVQK-ADDVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQmvKFAANINKESIIDVEGVVRKVN 124
Cdd:PRK03932 4 VSIKDILKGKyVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDNGEEYF--EEIKKLTTGSSVIVTGTVVESP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 125 QKigsctQQDVELHVQKIYVISLAEPRLPLQLDdairpevegeedgRATVnqDTRLDNRVIDLRTSTSQAIFRLQSGICH 204
Cdd:PRK03932 82 RA-----GQGYELQATKIEVIGEDPEDYPIQKK-------------RHSI--EFLREIAHLRPRTNKFGAVMRIRNTLAQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 205 LFRETLINKGFVEIQTPKIISAASEGGANVFTVS---------YFKNNAYLAQSPQLYKQMCICAdFEKVFCIGPVFRAE 275
Cdd:PRK03932 142 AIHEFFNENGFVWVDTPIITASDCEGAGELFRVTtldldfskdFFGKEAYLTVSGQLYAEAYAMA-LGKVYTFGPTFRAE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 276 DSNTHRHLTEFVGLDIEMAFnYHyHEVVEEIADTLVQ-IFKGLQERFQTEIQTVSKQFPCEPFKFLEPTL-----RLEYC 349
Cdd:PRK03932 221 NSNTRRHLAEFWMIEPEMAF-AD-LEDNMDLAEEMLKyVVKYVLENCPDDLEFLNRRVDKGDIERLENFIespfpRITYT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 350 EALAMLREAGVEMDDE----EDLSTPNEKLLgrlVKEKYDTDFYVLDkYPLAVRPFYTMPDPRNpKQSNSYDMFMRG-EE 424
Cdd:PRK03932 299 EAIEILQKSGKKFEFPvewgDDLGSEHERYL---AEEHFKKPVFVTN-YPKDIKAFYMRLNPDG-KTVAAMDLLAPGiGE 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 211065507 425 ILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 501
Cdd:PRK03932 374 IIGGSQREERLDVLEARIKELGLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
46-501 |
1.45e-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: 237.28 E-value: 1.45e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 46 VRVKDLTVQ---KADDVVWVRARVHTSRAKGKQCFLVLRQQQF--NVQALVAVGDhaSKQMVKFAANINKESIIDVEGVV 120
Cdd:TIGR00457 2 AAIKDLLQQvykFVGDEVTVSGWVRTKRSSKKIIFLELNDGSSlgPIQAVINGED--NPYLFQLLKSLTTGSSVSVTGKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 121 RKVNQKigsctQQDVELHVQKIYVISLAEPR-LPLQLDDairpevegeedgratvnQDTRL--DNRVIDLRTSTSQAIFR 197
Cdd:TIGR00457 80 VESPGK-----GQPVELQVKKIEVVGEAEPDdYPLQKKE-----------------HSLEFlrDIAHLRLRTNTLGAVMR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 198 LQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVS---------YFKNNAYLAQSPQLYKQMCICAdFEKVFCI 268
Cdd:TIGR00457 138 VRNALSQAIHRYFQENGFTWVSPPILTSNDCEGAGELFRVStgnidfsqdFFGKEAYLTVSGQLYLETYALA-LSKVYTF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 269 GPVFRAEDSNTHRHLTEFVGLDIEMAFnYHYHEVVEEIADTLVQIFKGLQERFQTEIQTVSKQFPCEPFKFLEPTL---- 344
Cdd:TIGR00457 217 GPTFRAEKSNTSRHLSEFWMIEPEMAF-ANLNDLLQLAETLIKYIIKAVLENCSQELKFLEKNFDKDLIKRLENIInnkf 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 345 -RLEYCEALAMLREAGVEMDDEE----DLSTPNEKLLGrlvkEKYDTDFYVLDKYPLAVRPFYtMPDPRNPKQSNSYDMF 419
Cdd:TIGR00457 296 aRITYTDAIEILKESDKNFEYEDfwgdDLQTEHERFLA----EEYFKPPVFVTNYPKDIKAFY-MKLNDDGKTVAAMDLL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 420 MRG-EEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKR 498
Cdd:TIGR00457 371 APGiGEIIGGSEREDDLDKLENRMKEMGLDTDALNWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGN 450
|
...
gi 211065507 499 LTP 501
Cdd:TIGR00457 451 INF 453
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
196-495 |
5.54e-57 |
|
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: 190.38 E-value: 5.54e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 196 FRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFK--NNAYLAQSPQLYKQMCICADFEKVFCIGPVFR 273
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNAlgLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 274 AEDSNThRHLTEFVGLDIEMAF-NYH-YHEVVEEIADTLVQIFKGlqerfqteiqTVSKQFPCEPFKFLEPTLRLEYCEA 351
Cdd:cd00669 81 NEDLRA-RHQPEFTMMDLEMAFaDYEdVIELTERLVRHLAREVLG----------VTAVTYGFELEDFGLPFPRLTYREA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 352 LamlreagvemddeedlstpnekllgrlvkEKYDTDFYVLDkYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQR 431
Cdd:cd00669 150 L-----------------------------ERYGQPLFLTD-YPAEMHSPLASPHDVNPEIADAFDLFINGVEVGNGSSR 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 211065507 432 IHDPQLLTERALHHGID----LEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRD 495
Cdd:cd00669 200 LHDPDIQAEVFQEQGINkeagMEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKM 267
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
60-158 |
7.44e-50 |
|
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: 165.81 E-value: 7.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 60 VWVRARVHTSRAKG-KQCFLVLRQQQFNVQALVAVGDHA-SKQMVKFAANINKESIIDVEGVVRKVNQKIGSCTQQDVEL 137
Cdd:cd04320 2 VLIRARVHTSRAQGaKLAFLVLRQQGYTIQGVLAASAEGvSKQMVKWAGSLSKESIVDVEGTVKKPEEPIKSCTQQDVEL 81
|
90 100
....*....|....*....|.
gi 211065507 138 HVQKIYVISLAEPRLPLQLDD 158
Cdd:cd04320 82 HIEKIYVVSEAAEPLPFQLED 102
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
176-496 |
2.61e-49 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 172.51 E-value: 2.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 176 QDTRLDNRVIdLRTSTSQAIFRLQSGICHLFRETLINKGFVEIQTPkIISA--------ASEGGANVFTVSYFKNNAYLA 247
Cdd:PRK06462 11 EEFLRMSWKH-ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPP-IISPstdplmglGSDLPVKQISIDFYGVEYYLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 248 QSPQLYKQMCIcADFEKVFCIGPVFRAE--DSNTHRHLTEFVGLDIEMAfNYHYHEVVEEIADTLVQIFKGLQERFQTEI 325
Cdd:PRK06462 89 DSMILHKQLAL-RMLGKIFYLSPNFRLEpvDKDTGRHLYEFTQLDIEIE-GADLDEVMDLIEDLIKYLVKELLEEHEDEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 326 QTVSKQFPcepfKFLEPTLRLEYCEALAMLREAGVEMDDEEDLSTPNEKLLgrlvKEKYDTDFYVLDkYPLAVRPFYTMP 405
Cdd:PRK06462 167 EFFGRDLP----HLKRPFKRITHKEAVEILNEEGCRGIDLEELGSEGEKSL----SEHFEEPFWIID-IPKGSREFYDRE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 406 DPRNPKQSNSYDMFMR---GEeILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLG 482
Cdd:PRK06462 238 DPERPGVLRNYDLLLPegyGE-AVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICG 316
|
330
....*....|....
gi 211065507 483 LHNVRQTSMFPRDP 496
Cdd:PRK06462 317 LRHIREVQPFPRVP 330
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
66-493 |
7.20e-43 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 160.23 E-value: 7.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 66 VHTSRAKGKQCFLVLRQQQFNVQALVavgdHASKQMVKFAANINKESIIDVEGVVRK-----VNQKIGSctqQDVELHVQ 140
Cdd:PRK00476 26 VHRRRDHGGLIFIDLRDREGIVQVVF----DPDAEAFEVAESLRSEYVIQVTGTVRArpegtVNPNLPT---GEIEVLAS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 141 KIYVISLAEPrLPLQLDDairpevegEEDgratVNQDTRLDNRVIDLRTSTSQAIFRLQSGICHLFRETLINKGFVEIQT 220
Cdd:PRK00476 99 ELEVLNKSKT-LPFPIDD--------EED----VSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDNGFLEIET 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 221 PkIISAASEGGANVFTV-S-YFKNNAY-LAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNTHRhLTEFVGLDIEMAFny 297
Cdd:PRK00476 166 P-ILTKSTPEGARDYLVpSrVHPGKFYaLPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADR-QPEFTQIDIEMSF-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 298 hyheV-VEEIADTLVQIFKGL------------------QE------------RFQTEIQTVSKQFPCEPFK-FLEPTLR 345
Cdd:PRK00476 242 ----VtQEDVMALMEGLIRHVfkevlgvdlptpfprmtyAEamrrygsdkpdlRFGLELVDVTDLFKDSGFKvFAGAAND 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 346 LEYCEALAMLREAG----VEMDD-------------------EEDLSTP---------NEKLLGRLVKEKYDTDFYVLDK 393
Cdd:PRK00476 318 GGRVKAIRVPGGAAqlsrKQIDEltefakiygakglayikvnEDGLKGPiakflseeeLAALLERTGAKDGDLIFFGADK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 394 YPL------AVR----------------------------------------PFyTMPDP--------RNPKQ--SNSYD 417
Cdd:PRK00476 398 AKVvndalgALRlklgkelglidedkfaflwvvdfpmfeydeeegrwvaahhPF-TMPKDedldeletTDPGKarAYAYD 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 418 MFMRGEEILSGAQRIHDPQLLtERALHH-GIDLEKIKA----YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMF 492
Cdd:PRK00476 477 LVLNGYELGGGSIRIHRPEIQ-EKVFEIlGISEEEAEEkfgfLLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAF 555
|
.
gi 211065507 493 P 493
Cdd:PRK00476 556 P 556
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
196-493 |
2.91e-40 |
|
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: 146.57 E-value: 2.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 196 FRLQSGICHLFRETLINKGFVEIQTPkIISAASEGGANVFTVSY--FKNNAY-LAQSPQLYKQMCICADFEKVFCIGPVF 272
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETP-ILTKSTPEGARDFLVPSrlHPGKFYaLPQSPQLFKQLLMVSGFDRYFQIARCF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 273 RAEDSNTHRHlTEFVGLDIEMAFnYHYHEVVEEIADTLVQIFKglqERFQTEIQTvskqfpcePFKfleptlRLEYCEAl 352
Cdd:cd00777 80 RDEDLRADRQ-PEFTQIDIEMSF-VDQEDIMSLIEGLLKYVFK---EVLGVELTT--------PFP------RMTYAEA- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 353 amLREAGV-----------EMDDEEdlstpnekllGRLV---------KEKYDTDfyvLDKYPLAVRpfytmpdprnpkq 412
Cdd:cd00777 140 --MERYGFkflwivdfplfEWDEEE----------GRLVsahhpftapKEEDLDL---LEKDPEDAR------------- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 413 SNSYDMFMRGEEILSGAQRIHDPQlLTERALHH-GIDLEKIKA----YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVR 487
Cdd:cd00777 192 AQAYDLVLNGVELGGGSIRIHDPD-IQEKVFEIlGLSEEEAEEkfgfLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIR 270
|
....*.
gi 211065507 488 QTSMFP 493
Cdd:cd00777 271 DVIAFP 276
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
66-493 |
3.05e-38 |
|
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: 147.45 E-value: 3.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 66 VHTSRAKGKQCFLVLR------QqqfnvqalVAVGDHASKQMVKFAANINKESIIDVEGVVRK-----VNQKI--Gsctq 132
Cdd:COG0173 25 VHRRRDHGGLIFIDLRdrygitQ--------VVFDPDDSAEAFEKAEKLRSEYVIAVTGKVRArpegtVNPKLptG---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 133 qDVELHVQKIYVISLAEPrLPLQLDDAIrpevegeedgraTVNQDTRLDNRVIDLRTSTSQAIFRLQSGICHLFRETLIN 212
Cdd:COG0173 93 -EIEVLASELEILNKAKT-PPFQIDDDT------------DVSEELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 213 KGFVEIQTPkIISAASEGGANVFTV-------SYFknnAyLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNTHRHLtE 285
Cdd:COG0173 159 NGFLEIETP-ILTKSTPEGARDYLVpsrvhpgKFY---A-LPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADRQP-E 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 286 FVGLDIEMAFnyhyhevVEE-----IADTLVQ-IFKGL--------------QE------------RFQTEIQTVSKQFP 333
Cdd:COG0173 233 FTQLDIEMSF-------VDQedvfeLMEGLIRhLFKEVlgvelptpfprmtyAEamerygsdkpdlRFGLELVDVTDIFK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 334 CEPFK-FLEPTLRLEYCEALAM------------------------------LREAGVE------MDDEE---------- 366
Cdd:COG0173 306 DSGFKvFAGAAENGGRVKAINVpggaslsrkqideltefakqygakglayikVNEDGLKspiakfLSEEElaailerlga 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 367 ---DL-----STPNE--KLLGRL-----------VKEKYD----TDFyvldkyPL-----------AV-RPFyTMPDP-- 407
Cdd:COG0173 386 kpgDLiffvaDKPKVvnKALGALrlklgkelgliDEDEFAflwvVDF------PLfeydeeegrwvAMhHPF-TMPKDed 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 408 -----RNPKQ--SNSYDMFMRGEEILSGAQRIHDPQLLtERALHH-GIDLEKIKA----YIDSFRFGAPPHAGGGIGLER 475
Cdd:COG0173 459 ldlleTDPGKvrAKAYDLVLNGYELGGGSIRIHDPELQ-EKVFELlGISEEEAEEkfgfLLEAFKYGAPPHGGIAFGLDR 537
|
570
....*....|....*...
gi 211065507 476 VTMLFLGLHNVRQTSMFP 493
Cdd:COG0173 538 LVMLLAGEDSIRDVIAFP 555
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
2-493 |
1.38e-31 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 128.61 E-value: 1.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 2 PSTNASRKGQEKPREIVDAAEDYA-----------KERYGissMIQSQEKPDRVLVRVKdltvqkaddvvwvrARVHTSR 70
Cdd:PTZ00385 58 ATKTVTQEASRAPRSKLDLPAAYSsfrgitpisevRERYG---YLASGDRAAQATVRVA--------------GRVTSVR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 71 AKGKQCFLVLRQQQFNVQALVAVGDHASKQMVK-FAANINKESIIDVEGVvrkvnqkigSCTQQDVELHVQKIYVISLAe 149
Cdd:PTZ00385 121 DIGKIIFVTIRSNGNELQVVGQVGEHFTREDLKkLKVSLRVGDIIGADGV---------PCRMQRGELSVAASRMLILS- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 150 prlP-LQLDDAIRPEVEGeedgrATVNQDT--RLDNRVIDLRTSTSQ-AIFRLQSGICHLFRETLINKGFVEIQTPKIIS 225
Cdd:PTZ00385 191 ---PyVCTDQVVCPNLRG-----FTVLQDNdvKYRYRFTDMMTNPCViETIKKRHVMLQALRDYFNERNFVEVETPVLHT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 226 AASEGGANVFTVSYFKNNA--YLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNtHRHLTEFVGLDIEMAfnYH-YHEV 302
Cdd:PTZ00385 263 VASGANAKSFVTHHNANAMdlFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDAD-RSHNPEFTSCEFYAA--YHtYEDL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 303 VEEIADTLVQIFKGLQERFQTEIQTVSKQFPCEPFKFLEPTLRLEYCEALAmlREAGVEMDDEEDLSTPNEKLLGRLVKE 382
Cdd:PTZ00385 340 MPMTEDIFRQLAMRVNGTTVVQIYPENAHGNPVTVDLGKPFRRVSVYDEIQ--RMSGVEFPPPNELNTPKGIAYMSVVML 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 383 KYDT----------------DFYVLDKyplAVRPFYTMPDP-----------RNPKQSNSYDMFMRGEEILSGAQRIHDP 435
Cdd:PTZ00385 418 RYNIplppvrtaakmfekliDFFITDR---VVEPTFVMDHPlfmsplakeqvSRPGLAERFELFVNGIEYCNAYSELNDP 494
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 211065507 436 --------QLLTERalhHGIDLEKI---KAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 493
Cdd:PTZ00385 495 heqyhrfqQQLVDR---QGGDEEAMpldETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFP 560
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
41-496 |
3.94e-29 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 120.85 E-value: 3.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 41 PDRVLVRV-KDLTVQKaddvvWVRarvhTSRAKGKQCFLVLRQQQF--NVQALVAVGDHASKQMVkfAANINKESIIDVE 117
Cdd:PLN02603 99 EDEGLARVgKTLNVMG-----WVR----TLRAQSSVTFIEVNDGSClsNMQCVMTPDAEGYDQVE--SGLITTGASVLVQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 118 GVVRKvnqkiGSCTQQDVELHVQKIYVISLAEPRLPLQLDDAIRPEVEGEEDGRAtvnqdtrldnrvidlRTSTSQAIFR 197
Cdd:PLN02603 168 GTVVS-----SQGGKQKVELKVSKIVVVGKSDPSYPIQKKRVSREFLRTKAHLRP---------------RTNTFGAVAR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 198 LQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVS------------------------------YFKNNAYLA 247
Cdd:PLN02603 228 VRNALAYATHKFFQENGFVWVSSPIITASDCEGAGEQFCVTtlipnsaenggslvddipktkdglidwsqdFFGKPAFLT 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 248 QSPQLYKQMCICAdFEKVFCIGPVFRAEDSNTHRHLTEFVGLDIEMAF----------NYHYHEVVEEIADTLVQ----- 312
Cdd:PLN02603 308 VSGQLNGETYATA-LSDVYTFGPTFRAENSNTSRHLAEFWMIEPELAFadlnddmacaTAYLQYVVKYILENCKEdmeff 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 313 ---IFKGLQERFQteiQTVSKQFpcepfkfleptLRLEYCEALAMLREA----------GVEMDDEEDLSTPNEKLLGRL 379
Cdd:PLN02603 387 ntwIEKGIIDRLS---DVVEKNF-----------VQLSYTDAIELLLKAkkkfefpvkwGLDLQSEHERYITEEAFGGRP 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 380 VkekydtdfyVLDKYPLAVRPFYtMPDPRNPKQSNSYDMFM-RGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDS 458
Cdd:PLN02603 453 V---------IIRDYPKEIKAFY-MRENDDGKTVAAMDMLVpRVGELIGGSQREERLEYLEARLDELKLNKESYWWYLDL 522
|
490 500 510
....*....|....*....|....*....|....*...
gi 211065507 459 FRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDP 496
Cdd:PLN02603 523 RRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPRVP 560
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
61-501 |
2.25e-28 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 119.32 E-value: 2.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 61 WVRArvhtSRAKGKQCFLVLRQQQFNVQALVAvGDHASKQMVKFAANINKESIIDVEGVVRKVNQKIGS--CTQQDVELH 138
Cdd:PRK12820 26 WVDA----FRDHGELLFIHLRDRNGFIQAVFS-PEAAPADVYELAASLRAEFCVALQGEVQKRLEETENphIETGDIEVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 139 VQKIYVISLAEPrLPLQLDDaiRPEVEGEEDGRA-TVNQDTRLDNRVIDLRTSTSQAIFRLQSGICHLFRETLINKGFVE 217
Cdd:PRK12820 101 VRELSILAASEA-LPFAISD--KAMTAGAGSAGAdAVNEDLRLQYRYLDIRRPAMQDHLAKRHRIIKCARDFLDSRGFLE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 218 IQTPKIISAASEGGANVFTVSYFKNNAY--LAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNTHRHlTEFVGLDIEMAF 295
Cdd:PRK12820 178 IETPILTKSTPEGARDYLVPSRIHPKEFyaLPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQ-PEFTQLDIEASF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 296 --NYHYHEVVEEI------------------------------------------------ADTLVQIFKGLQERfQTEI 325
Cdd:PRK12820 257 idEEFIFELIEELtarmfaiggialprpfprmpyaeamdttgsdrpdlrfdlkfadatdifENTRYGIFKQILQR-GGRI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 326 QTVSKQFPCEpfKFLEPTLRLEYCEALA----------MLREAG------VEMDDEEDLstpnEKLLGRLVKEKYDTDFY 389
Cdd:PRK12820 336 KGINIKGQSE--KLSKNVLQNEYAKEIApsfgakgmtwMRAEAGgldsniVQFFSADEK----EALKRRFHAEDGDVIIM 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 390 VLDK----------------------------YPLAVRPF-----------------YTMP-----DPRNPK-----QSN 414
Cdd:PRK12820 410 IADAscaivlsalgqlrlhladrlglipegvfHPLWITDFplfeatddggvtsshhpFTAPdredfDPGDIEelldlRSR 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 415 SYDMFMRGEEILSGAQRIHDP--QLLTERALhhGIDLEKIKA----YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQ 488
Cdd:PRK12820 490 AYDLVVNGEELGGGSIRINDKdiQLRIFAAL--GLSEEDIEDkfgfFLRAFDFAAPPHGGIALGLDRVVSMILQTPSIRE 567
|
570
....*....|...
gi 211065507 489 TSMFPRDPKRLTP 501
Cdd:PRK12820 568 VIAFPKNRSAACP 580
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
50-494 |
5.83e-27 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 114.89 E-value: 5.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 50 DLTVQKADDVVWVRARVHTSRAKGKQCFLVLRQQQFNVQalVAVGDHASKQMVKFAANINKESIIDVEGVVRK-----VN 124
Cdd:PLN02903 65 ALSVNDVGSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQ--VVTLPDEFPEAHRTANRLRNEYVVAVEGTVRSrpqesPN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 125 QKIGSCTQQDVELHVQKIYVISLAEPRLplqlddairpeVEGEEDGRATVNQDTRLDNRVIDLRTSTSQAIFRLQSGICH 204
Cdd:PLN02903 143 KKMKTGSVEVVAESVDILNVVTKSLPFL-----------VTTADEQKDSIKEEVRLRYRVLDLRRPQMNANLRLRHRVVK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 205 LFRETLINK-GFVEIQTPKIISAASEGGANVFTVSYFKNNAYLA--QSPQLYKQMCICADFEKVFCIGPVFRAEDSNTHR 281
Cdd:PLN02903 212 LIRRYLEDVhGFVEIETPILSRSTPEGARDYLVPSRVQPGTFYAlpQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 282 HlTEFVGLDIEMAFNyhYHEVVEEIADTLV-QIFK---GLQ-----------------------ERFQTEIQTVSKQFPC 334
Cdd:PLN02903 292 Q-PEFTQLDMELAFT--PLEDMLKLNEDLIrQVFKeikGVQlpnpfprltyaeamskygsdkpdLRYGLELVDVSDVFAE 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 335 EPFKFLEPTL--------------------RLE-----YCEALAM----LREAGVEMDDE--------EDLSTPN-EKLL 376
Cdd:PLN02903 369 SSFKVFAGALesggvvkaicvpdgkkisnnTALkkgdiYNEAIKSgakgLAFLKVLDDGElegikalvESLSPEQaEQLL 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 377 GR----------------------------LVKEKYD------------TDFYVLDKYPLAVR------PFyTMPDPRNP 410
Cdd:PLN02903 449 AAcgagpgdlilfaagptssvnktldrlrqFIAKTLDlidpsrhsilwvTDFPMFEWNEDEQRlealhhPF-TAPNPEDM 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 411 KQSNS-----YDMFMRGEEILSGAQRIH--DPQLLTERALhhGIDLE----KIKAYIDSFRFGAPPHAGGGIGLERVTML 479
Cdd:PLN02903 528 GDLSSaralaYDMVYNGVEIGGGSLRIYrrDVQQKVLEAI--GLSPEeaesKFGYLLEALDMGAPPHGGIAYGLDRLVML 605
|
570
....*....|....*
gi 211065507 480 FLGLHNVRQTSMFPR 494
Cdd:PLN02903 606 LAGAKSIRDVIAFPK 620
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
33-498 |
2.59e-24 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 106.23 E-value: 2.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 33 SMIQSQEKPDRVLVRV----KDLTVQKADDVVWVRARVHTSRAKGKQCFLVLRQQQ----FNVQALVAVGDHASKQMVKF 104
Cdd:PLN02221 22 STVQKAQFSDRVLIRSildrPDGGAGLAGQKVRIGGWVKTGREQGKGTFAFLEVNDgscpANLQVMVDSSLYDLSTLVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 105 AaninkeSIIDVEGVVrKVNQKiGSCTQQDVELHVQKIYVISLAEP-RLPLQlddairpevegeedgRATVNQDTRLDNR 183
Cdd:PLN02221 102 G------TCVTVDGVL-KVPPE-GKGTKQKIELSVEKVIDVGTVDPtKYPLP---------------KTKLTLEFLRDVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 184 VIDLRTSTSQAIFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVS------------------------- 238
Cdd:PLN02221 159 HLRSRTNSISAVARIRNALAFATHSFFQEHSFLYIHTPIITTSDCEGAGEMFQVTtlinyterleqdlidnpppteadve 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 239 -----------------------------------------------------------------YFKNNAYLAQSPQLY 253
Cdd:PLN02221 239 aarlivkergevvaqlkaakaskeeitaavaelkiakeslahieersklkpglpkkdgkidyskdFFGRQAFLTVSGQLQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 254 KQMCICAdFEKVFCIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVveEIADTLVQ-IFKGLQERFQTEIQTVSKQF 332
Cdd:PLN02221 319 VETYACA-LSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFADLEDDM--NCAEAYVKyMCKWLLDKCFDDMELMAKNF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 333 PCEPFKFLE-----PTLRLEYCEALAMLREA---GVEMDDEE----DLSTPNEKLLGRLVKEKYdtdfYVLDKYPLAVRP 400
Cdd:PLN02221 396 DSGCIDRLRmvastPFGRITYTEAIELLEEAvakGKEFDNNVewgiDLASEHERYLTEVLFQKP----LIVYNYPKGIKA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 401 FYtMPDPRNPKQSNSYDMFM-RGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTML 479
Cdd:PLN02221 472 FY-MRLNDDEKTVAAMDVLVpKVGELIGGSQREERYDVIKQRIEEMGLPIEPYEWYLDLRRYGTVKHCGFGLGFERMILF 550
|
570
....*....|....*....
gi 211065507 480 FLGLHNVRQTSMFPRDPKR 498
Cdd:PLN02221 551 ATGIDNIRDVIPFPRYPGK 569
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
60-493 |
2.10e-23 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 103.22 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 60 VWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMVKFAANINKESIIDVEGVVRKVnqkigsctqQDVELHv 139
Cdd:PRK12445 68 VSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVYNDQFKKWDLGDIIGARGTLFKT---------QTGELS- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 140 qkiyvISLAEPRLplqLDDAIRP---EVEGEEDgratvnQDTRLDNRVIDL-RTSTSQAIFRLQSGICHLFRETLINKGF 215
Cdd:PRK12445 138 -----IHCTELRL---LTKALRPlpdKFHGLQD------QEVRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMVARGF 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 216 VEIQTPKIISAASEGGANVFTVSY--FKNNAYLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNThRHLTEFVGLDIEM 293
Cdd:PRK12445 204 MEVETPMMQVIPGGASARPFITHHnaLDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISV-RHNPEFTMMELYM 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 294 AFNyHYHEVVEeIADTLvqiFKGLQerfQTEIQTVSKQFPCEPFKFLEPTLRLEYCEALAMLR-----------EAGVEM 362
Cdd:PRK12445 283 AYA-DYHDLIE-LTESL---FRTLA---QEVLGTTKVTYGEHVFDFGKPFEKLTMREAIKKYRpetdmadldnfDAAKAL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 363 DDEEDLSTPNEKLLGRLVKEKYD-------TDFYVLDKYPLAVRPFYTMPDPrNPKQSNSYDMFMRGEEILSGAQRIHDP 435
Cdd:PRK12445 355 AESIGITVEKSWGLGRIVTEIFDevaeahlIQPTFITEYPAEVSPLARRNDV-NPEITDRFEFFIGGREIGNGFSELNDA 433
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 211065507 436 QLLTER------ALHHGIDLEKI--KAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 493
Cdd:PRK12445 434 EDQAERfqeqvnAKAAGDDEAMFydEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
196-493 |
1.54e-22 |
|
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: 98.43 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 196 FRLQSGICHLFRETLINKGFVEIQTPKIISAAseGGANV--FTVSY--FKNNAYLAQSPQLYKQMCICADFEKVFCIGPV 271
Cdd:cd00775 8 FIVRSKIISYIRKFLDDRGFLEVETPMLQPIA--GGAAArpFITHHnaLDMDLYLRIAPELYLKRLIVGGFERVYEIGRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 272 FRAEDSNThRHLTEFVGLDIEMAF-NYH-YHEVVEEIADTLVQ-IFKGLQERFQTEIQTVSKqfpcePFKfleptlRLEY 348
Cdd:cd00775 86 FRNEGIDL-THNPEFTMIEFYEAYaDYNdMMDLTEDLFSGLVKkINGKTKIEYGGKELDFTP-----PFK------RVTM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 349 CEALAmlREAGVEMDDEEDLSTPN-EKLLGRLVKEKYD---TDFYVLDK------------------YPLAVRPFyTMPD 406
Cdd:cd00775 154 VDALK--EKTGIDFPELDLEQPEElAKLLAKLIKEKIEkprTLGKLLDKlfeefveptliqptfiidHPVEISPL-AKRH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 407 PRNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTER-----ALHHGIDLEKI---KAYIDSFRFGAPPHAGGGIGLERVTM 478
Cdd:cd00775 231 RSNPGLTERFELFICGKEIANAYTELNDPFDQRERfeeqaKQKEAGDDEAMmmdEDFVTALEYGMPPTGGLGIGIDRLVM 310
|
330
....*....|....*
gi 211065507 479 LFLGLHNVRQTSMFP 493
Cdd:cd00775 311 LLTDSNSIRDVILFP 325
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
184-496 |
1.60e-22 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 100.87 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 184 VIDLRTSTSQAIfrlqsgicHLFRETlinKGFVEIQTPKIISAASEGGANVFTVS------------------------- 238
Cdd:PTZ00425 214 VIRIRNALAIAT--------HLFFQS---RGFLYIHTPLITTSDCEGGGEMFTVTtllgedadyraiprvnkknkkgekr 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 239 --------------------------------------YFKNNAYLAQSPQLYKQMcICADFEKVFCIGPVFRAEDSNTH 280
Cdd:PTZ00425 283 edilntcnannnngnssssnavsspaypdqylidykkdFFSKQAFLTVSGQLSLEN-LCSSMGDVYTFGPTFRAENSHTS 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 281 RHLTEFVGLDIEMAFNYHYHEVveEIADTLVQIFKG------------LQERFQTEIQTVSKQFPCEPFKFLEPT----L 344
Cdd:PTZ00425 362 RHLAEFWMIEPEIAFADLYDNM--ELAESYIKYCIGyvlnnnfddiyyFEENVETGLISRLKNILDEDFAKITYTnvidL 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 345 RLEYCEALAMLREAGVEMDDEEDlstpnekllgRLVKEKYDTDFYVLDKYPLAVRPFYtMPDPRNPKQSNSYDMFM-RGE 423
Cdd:PTZ00425 440 LQPYSDSFEVPVKWGMDLQSEHE----------RFVAEQIFKKPVIVYNYPKDLKAFY-MKLNEDQKTVAAMDVLVpKIG 508
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 211065507 424 EILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDP 496
Cdd:PTZ00425 509 EVIGGSQREDNLERLDKMIKEKKLNMESYWWYRQLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPRYP 581
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
235-494 |
3.82e-19 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 90.70 E-value: 3.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 235 FTVSYFKNNAYLAQSPQLYKQMCICAdFEKVFCIGPVFRAEDSNTHRHLTEFVGLDIEMAFNyHYHEVVEEIADTLVQIF 314
Cdd:PLN02532 363 FSKDFFSRPTYLTVSGRLHLESYACA-LGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFS-ELEDAMNCAEDYFKFLC 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 315 KGLQERFQTEIQTVSKQFPCEPFKFLE-----PTLRLEYCEALAMLREA-GVEMDDEEDLSTP-NEKLLGRLVKEKYDTD 387
Cdd:PLN02532 441 KWVLENCSEDMKFVSKRIDKTISTRLEaiissSLQRISYTEAVDLLKQAtDKKFETKPEWGIAlTTEHLSYLADEIYKKP 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 388 FYVLDkYPLAVRPFYTMPDpRNPKQSNSYDMFM-RGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPH 466
Cdd:PLN02532 521 VIIYN-YPKELKPFYVRLN-DDGKTVAAFDLVVpKVGTVITGSQNEERMDILNARIEELGLPREQYEWYLDLRRHGTVKH 598
|
250 260
....*....|....*....|....*...
gi 211065507 467 AGGGIGLERVTMLFLGLHNVRQTSMFPR 494
Cdd:PLN02532 599 SGFSLGFELMVLFATGLPDVRDAIPFPR 626
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
60-146 |
3.62e-17 |
|
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: 76.45 E-value: 3.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 60 VWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASkqMVKFAANINKESIIDVEGVVRKVnqKIGSCTQQDVELHV 139
Cdd:cd04100 2 VTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELGE--FFEEAEKLRTESVVGVTGTVVKR--PEGNLATGEIELQA 77
|
....*..
gi 211065507 140 QKIYVIS 146
Cdd:cd04100 78 EELEVLS 84
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
175-493 |
6.97e-17 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 83.52 E-value: 6.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 175 NQDTRLDNRVIDLRTS-TSQAIFRLQSGICHLFRETLINKGFVEIQTPKIISAAseGGANVFTVSYFKN----NAYLAQS 249
Cdd:PTZ00417 231 DTEIRYRQRYLDLMINeSTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVA--GGANARPFITHHNdldlDLYLRIA 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 250 PQLYKQMCICADFEKVFCIGPVFRAED-SNTHRhlTEFVGLDIEMAFNyHYHEVVEEIADTLVQIFKGLqerFQTEIQTV 328
Cdd:PTZ00417 309 TELPLKMLIVGGIDKVYEIGKVFRNEGiDNTHN--PEFTSCEFYWAYA-DFYDLIKWSEDFFSQLVMHL---FGTYKILY 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 329 SKQFP-CEPFK--FLEPTLRLEYCEALAMLREAGVE--------------MDDEEDLSTPN----EKLLGRLVKEkydtd 387
Cdd:PTZ00417 383 NKDGPeKDPIEidFTPPYPKVSIVEELEKLTNTKLEqpfdspetinkminLIKENKIEMPNpptaAKLLDQLASH----- 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 388 fYVLDKYPlaVRPFYTMPDPR-----------NPKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGIDLEKIKA-- 454
Cdd:PTZ00417 458 -FIENKYP--NKPFFIIEHPQimsplakyhrsKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAea 534
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 211065507 455 ------YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 493
Cdd:PTZ00417 535 fqfdaaFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFP 579
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
65-493 |
1.53e-16 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 82.06 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 65 RVHTSRAKGKQCFLVLRQQQFNVQALVAVgDHASKQMVKFAANINKESIIDVEGVVRKvnqkigscTQQDvEL--HVQKI 142
Cdd:PRK00484 62 RVMLKRVMGKASFATLQDGSGRIQLYVSK-DDVGEEALEAFKKLDLGDIIGVEGTLFK--------TKTG-ELsvKATEL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 143 YVISLAepRLPLqlddairPEV-EGEEDgratvnQDTRLDNRVIDLRTS-TSQAIFRLQSGICHLFRETLINKGFVEIQT 220
Cdd:PRK00484 132 TLLTKS--LRPL-------PDKfHGLTD------VETRYRQRYVDLIVNpESRETFRKRSKIISAIRRFLDNRGFLEVET 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 221 PKIISAAseGGANV--FTVSYfknNA-----YLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNThRHLTEFVGLDIEM 293
Cdd:PRK00484 197 PMLQPIA--GGAAArpFITHH---NAldidlYLRIAPELYLKRLIVGGFERVYEIGRNFRNEGIDT-RHNPEFTMLEFYQ 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 294 AF-NYH---------YHEVVEEIADTLVQIFKGLQERFQTEIQTVS-----KQFPCEPFKFLEPTlrleycEALAMLREA 358
Cdd:PRK00484 271 AYaDYNdmmdlteelIRHLAQAVLGTTKVTYQGTEIDFGPPFKRLTmvdaiKEYTGVDFDDMTDE------EARALAKEL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 359 GVEMDDEEDLSTPNEKLLGRLVKEKYDTDFYVLDkYPLAVRPFyTMPDPRNPKQSNSYDMFMRGEEILSG---------- 428
Cdd:PRK00484 345 GIEVEKSWGLGKLINELFEEFVEPKLIQPTFITD-YPVEISPL-AKRHREDPGLTERFELFIGGREIANAfselndpidq 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 211065507 429 AQRIHDpQLLtERAL----HHGIDLEkikaYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 493
Cdd:PRK00484 423 RERFEA-QVE-AKEAgddeAMFMDED----FLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
57-493 |
1.56e-16 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 82.35 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 57 DDVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMV--KFAANINKESIIDVEGVVRKvnQKIGsctqqd 134
Cdd:PLN02502 108 DVSVSVAGRIMAKRAFGKLAFYDLRDDGGKIQLYADKKRLDLDEEEfeKLHSLVDRGDIVGVTGTPGK--TKKG------ 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 135 vELHVQKIYVISLAEPRLPLqlddairPE-VEGEEDgratvnQDTRLDNRVIDLRTSTSQA-IFRLQSGICHLFRETLIN 212
Cdd:PLN02502 180 -ELSIFPTSFEVLTKCLLML-------PDkYHGLTD------QETRYRQRYLDLIANPEVRdIFRTRAKIISYIRRFLDD 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 213 KGFVEIQTPKIISAAseGGANVFTVSYFKN----NAYLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNThRHLTEFVG 288
Cdd:PLN02502 246 RGFLEVETPMLNMIA--GGAAARPFVTHHNdlnmDLYLRIATELHLKRLVVGGFERVYEIGRQFRNEGIST-RHNPEFTT 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 289 LDIEMAF-NYH-YHEVVEEIADTLV-QIFKGLQERFQ-TEIQTVskqfpcEPFK------FLEPTLRLEYCEAL--AMLR 356
Cdd:PLN02502 323 CEFYQAYaDYNdMMELTEEMVSGMVkELTGSYKIKYHgIEIDFT------PPFRrismisLVEEATGIDFPADLksDEAN 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 357 EAGVEMDDEEDLSTPN--------EKLLGRLVKEKYDTDFYVLDkYPLAVRPFyTMPDPRNPKQSNSYDMFMRGEEILSG 428
Cdd:PLN02502 397 AYLIAACEKFDVKCPPpqttgrllNELFEEFLEETLVQPTFVLD-HPVEMSPL-AKPHRSKPGLTERFELFINGRELANA 474
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 211065507 429 AQRIHDP----QLLTERALHHGIDLEKIKAYIDSF----RFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 493
Cdd:PLN02502 475 FSELTDPvdqrERFEEQVKQHNAGDDEAMALDEDFctalEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFP 547
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
175-493 |
7.59e-16 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 80.78 E-value: 7.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 175 NQDTRLDNRVIDLRTST-SQAIFRLQSGICHLFRETLINKGFVEIQTPkiISAASEGGANV--FTVSYfknNAY-----L 246
Cdd:PRK02983 748 DPEARVRQRYLDLAVNPeARDLLRARSAVVRAVRETLVARGFLEVETP--ILQQVHGGANArpFVTHI---NAYdmdlyL 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 247 AQSPQLY-KQMCIcADFEKVFCIGPVFRAE--------------------DSNTHRHLTEfvGLDIEMAFNYHYHEVV-- 303
Cdd:PRK02983 823 RIAPELYlKRLCV-GGVERVFELGRNFRNEgvdathnpeftlleayqahaDYDTMRDLTR--ELIQNAAQAAHGAPVVmr 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 304 --EEIADTLVQI---------FKGLQERFQTEIQtvskqfPCEPFkflePTLRlEYCEAlamlreAGVEMDDEEDLSTPN 372
Cdd:PRK02983 900 pdGDGVLEPVDIsgpwpvvtvHDAVSEALGEEID------PDTPL----AELR-KLCDA------AGIPYRTDWDAGAVV 962
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 373 EKLLGRLVkEKYDTD--FYVldKYPLAVRPFyTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDP----QLLTERAL-HH 445
Cdd:PRK02983 963 LELYEHLV-EDRTTFptFYT--DFPTSVSPL-TRPHRSDPGLAERWDLVAWGVELGTAYSELTDPveqrRRLTEQSLlAA 1038
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 211065507 446 GIDLEKI---KAYIDSFRFGAPPHAGGGIGLERVTMLFLGLhNVRQTSMFP 493
Cdd:PRK02983 1039 GGDPEAMeldEDFLQALEYAMPPTGGLGMGVDRLVMLLTGR-SIRETLPFP 1088
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
66-188 |
1.12e-10 |
|
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: 59.46 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 66 VHTSRAKGKQCFLVLRQQQFNVQALVavgDHASKQMVKFAANINKESIIDVEGVVRK-----VNQKIGSctqQDVELHVQ 140
Cdd:cd04317 23 VQRRRDHGGLIFIDLRDRYGIVQVVF---DPEEAPEFELAEKLRNESVIQVTGKVRArpegtVNPKLPT---GEIEVVAS 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 211065507 141 KIYVISLAEPrLPLQLDDAIrpevegeedgraTVNQDTRLDNRVIDLR 188
Cdd:cd04317 97 ELEVLNKAKT-LPFEIDDDV------------NVSEELRLKYRYLDLR 131
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
49-154 |
5.16e-10 |
|
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: 56.55 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 49 KDLTVQKADDVVWVRARVHTSRAKGKQCFLVLRQQQFNVQaLVAVGDHASKQMVKFAANINKESIIDVEGVVRKVNQKIG 128
Cdd:cd04316 4 AEITPELDGEEVTVAGWVHEIRDLGGIKFVILRDREGIVQ-VTAPKKKVDKELFKTVRKLSRESVISVTGTVKAEPKAPN 82
|
90 100
....*....|....*....|....*.
gi 211065507 129 sctqqDVELHVQKIYVISLAEPRLPL 154
Cdd:cd04316 83 -----GVEIIPEEIEVLSEAKTPLPL 103
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
206-308 |
5.91e-09 |
|
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: 55.97 E-value: 5.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 206 FRETLINKGFVEIQTPKIISAASEGGAN------VFTVSYFKNNAYLAQSPQLYKQM----CICADFEKVFCIGPVFRAE 275
Cdd:cd00768 9 LRRFMAELGFQEVETPIVEREPLLEKAGhepkdlLPVGAENEEDLYLRPTLEPGLVRlfvsHIRKLPLRLAEIGPAFRNE 88
|
90 100 110
....*....|....*....|....*....|....*....
gi 211065507 276 DSNTH-RHLTEFVGLDIEMAF-----NYHYHEVVEEIAD 308
Cdd:cd00768 89 GGRRGlRRVREFTQLEGEVFGedgeeASEFEELIELTEE 127
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
60-145 |
5.63e-07 |
|
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: 46.84 E-value: 5.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 60 VWVRARVHT-SRAKGKQCFLVLRQQQFNVQALVAvgdhaSKQMVKFAANINKESIIDVEGVVRKVNQKigsctqqDVELH 138
Cdd:pfam01336 1 VTVAGRVTSiRRSGGKLLFLTLRDGTGSIQVVVF-----KEEAEKLAKKLKEGDVVRVTGKVKKRKGG-------ELELV 68
|
....*..
gi 211065507 139 VQKIYVI 145
Cdd:pfam01336 69 VEEIELL 75
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
60-150 |
2.95e-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: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211065507 60 VWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAvgDHASKQMVKFAANINKESIIDVEGVVRKVNQKIGSctqqdVELHV 139
Cdd:cd04319 2 VTLAGWVYRKREVGKKAFIVLRDSTGIVQAVFS--KDLNEEAYREAKKVGIESSVIVEGAVKADPRAPGG-----AEVHG 74
|
90
....*....|.
gi 211065507 140 QKIYVISLAEP 150
Cdd:cd04319 75 EKLEIIQNVEF 85
|
|
| |
