|
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: 729.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 20 AAEDYAKERYGVSSMIQSQEKPD-RVLVRVKDLTVQKADEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGD-HA 97
Cdd:PLN02850 43 DEDDPLASNYGDVPLEELQSKVTgREWTDVSDLGEELAGSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQCVVFVSEvTV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 98 SKQMVKFAANINKESIIDVEGIVRKVNQKIGSCTQQdVELHVQKIYVISLAEPRLPLQLDDAIRPEVEGEEDGR-----A 172
Cdd:PLN02850 123 SKGMVKYAKQLSRESVVDVEGVVSVPKKPVKGTTQQ-VEIQVRKIYCVSKALATLPFNVEDAARSESEIEKALQtgeqlV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 173 TVNQDTRLDNRIIDLRTSTSQAIFHLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKSNAYLAQSPQL 252
Cdd:PLN02850 202 RVGQDTRLNNRVLDLRTPANQAIFRIQSQVCNLFREFLLSKGFVEIHTPKLIAGASEGGSAVFRLDYKGQPACLAQSPQL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 253 YKQMCICADFEKVFCIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVVEEIADTLVQIFKGLQERFQTEIQTVNKQF 332
Cdd:PLN02850 282 HKQMAICGDFRRVFEIGPVFRAEDSFTHRHLCEFTGLDLEMEIKEHYSEVLDVVDELFVAIFDGLNERCKKELEAIREQY 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 333 PCEPFKFLEPTLRLEYCEALAMLREAGVEMDDEEDLSTPNEKLLGRLVKEKYDTDFYVLDKYPLAVRPFYTMPDPRNPKQ 412
Cdd:PLN02850 362 PFEPLKYLPKTLRLTFAEGIQMLKEAGVEVDPLGDLNTESERKLGQLVKEKYGTDFYILHRYPLAVRPFYTMPCPDDPKY 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 413 SNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMF 492
Cdd:PLN02850 442 SNSFDVFIRGEEIISGAQRVHDPELLEKRAEECGIDVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLF 521
|
....*....
gi 16758642 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: 528.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 6 ASRKGQEKPREIVDAA--EDYaKERYGVSSMIQSQEKPDRVLVRVKDLTVQK-ADEVVWVRARVHTSRAKGKQCFLVLRQ 82
Cdd:PTZ00401 25 AARLAEEKARAAEKAAlvEKY-KDVFGAAPMVQSTTYKSRTFIPVAVLSKPElVDKTVLIRARVSTTRKKGKMAFMVLRD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 83 QQFNVQALVAVGDHASKQMVKFAANINKESIIDVEGIVRKVNQKIGSCTQQDVELHVQKIYVISLAEPRLPLQLDDAIRP 162
Cdd:PTZ00401 104 GSDSVQAMAAVEGDVPKEMIDFIGQIPTESIVDVEATVCKVEQPITSTSHSDIELKVKKIHTVTESLRTLPFTLEDASRK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 163 EvegeEDGRATVNQDTRLDNRIIDLRTSTSQAIFHLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKS 242
Cdd:PTZ00401 184 E----SDEGAKVNFDTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDSDFCEIHSPKIINAPSEGGANVFKLEYFNR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 243 NAYLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVVEEIADTLVQIFKGLQERfQ 322
Cdd:PTZ00401 260 FAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHLTEFVGLDVEMRINEHYYEVLDLAESLFNYIFERLATH-T 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 323 TEIQTVNKQFPCEPFKF------------------LEPT--------------LRLEYCEALAMLREAGVE-MDDEEDLS 369
Cdd:PTZ00401 339 KELKAVCQQYPFEPLVWkltpermkelgvgvisegVEPTdkyqarvhnmdsrmLRINYMHCIELLNTVLEEkMAPTDDIN 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 370 TPNEKLLGRLVKEKYDTDFYVLDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGIDL 449
Cdd:PTZ00401 419 TTNEKLLGKLVKERYGTDFFISDRFPSSARPFYTMECKDDERFTNSYDMFIRGEEISSGAQRIHDPDLLLARAKMLNVDL 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 16758642 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 |
5.19e-172 |
|
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: 487.07 E-value: 5.19e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 174 VNQDTRLDNRIIDLRTSTSQAIFHLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKSNAYLAQSPQLY 253
Cdd:cd00776 2 ANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 254 KQMCICAdFEKVFCIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVVEEIADTLVQIFKGLQERFQTEIQTVNkQFP 333
Cdd:cd00776 82 KEMLIAA-LERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRVLERCAKELELVN-QLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 334 CEPFKFLEPTLRLEYCEALAMLREAGV--EMDDEEDLSTPNEKLLGRLVKekydTDFYVLDKYPLAVRPFYTMPDPRNPK 411
Cdd:cd00776 160 RELLKPLEPFPRITYDEAIELLREKGVeeEVKWGEDLSTEHERLLGEIVK----GDPVFVTDYPKEIKPFYMKPDDDNPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 412 QSNSYDMFMRG-EEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTS 490
Cdd:cd00776 236 TVESFDLLMPGvGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAI 315
|
....*..
gi 16758642 491 MFPRDPK 497
Cdd:cd00776 316 LFPRDPK 322
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
46-501 |
5.40e-165 |
|
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: 473.54 E-value: 5.40e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 46 VRVKDLTVQKADEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQaLVAVGDHASKQMVKFAANINKESIIDVEGIVrkvnq 125
Cdd:TIGR00458 1 VYSADIKPEMDGQEVTFMGWVHEIRDLGGLIFVLLRDREGLIQ-ITAPAKKVSKNLFKWAKKLNLESVVAVRGIV----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 126 KIGSCTQQDVELHVQKIYVISLAEPRLPLQLDDAIRPEVegeedgratvnqDTRLDNRIIDLRTSTSQAIFHLQSGICHL 205
Cdd:TIGR00458 75 KIKEKAPGGFEIIPTKIEVINEAKEPLPLDPTEKVPAEL------------DTRLDYRFLDLRRPTVQAIFRIRSGVLES 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 206 FRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKSNAYLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNTHRHLTE 285
Cdd:TIGR00458 143 VREFLAEEGFIEVHTPKLVASATEGGTELFPITYFEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHRHLNE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 286 FVGLDIEMAFNYHyHEVVEEIADTLVQIFKGLQERFQTEIQTVNKQFPCEPFKFleptLRLEYCEALAMLREAGVEMDDE 365
Cdd:TIGR00458 223 ATSIDIEMAFEDH-HDVMDILEELVVRVFEDVPERCAHQLETLEFKLEKPEGKF----VRLTYDEAIEMANAKGVEIGWG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 366 EDLSTPNEKLLGrlvkEKYDTDFYVLDkYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHH 445
Cdd:TIGR00458 298 EDLSTEAEKALG----EEMDGLYFITD-WPTEIRPFYTMPDEDNPEISKSFDLMYRDLEISSGAQRIHLHDLLVERIKAK 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 16758642 446 GIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 501
Cdd:TIGR00458 373 GLNPEGFKDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRKRLTP 428
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
48-501 |
4.04e-157 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 453.88 E-value: 4.04e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 48 VKDLTVQKADEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDhaSKQMVKFAANINKESIIDVEGIVRKVNQKI 127
Cdd:PRK05159 7 TSELTPELDGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKV--DEELFETIKKLKRESVVSVTGTVKANPKAP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 128 GSctqqdVELHVQKIYVISLAEPRLPLqlddairpEVEGEEDgrATVnqDTRLDNRIIDLRTSTSQAIFHLQSGICHLFR 207
Cdd:PRK05159 85 GG-----VEVIPEEIEVLNKAEEPLPL--------DISGKVL--AEL--DTRLDNRFLDLRRPRVRAIFKIRSEVLRAFR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 208 ETLINKGFVEIQTPKIISAASEGGANVFTVSYFKSNAYLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNTHRHLTEFV 287
Cdd:PRK05159 148 EFLYENGFTEIFTPKIVASGTEGGAELFPIDYFEKEAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRHLNEYT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 288 GLDIEMAFNYHYHEVVEEIADTLVQIFKGLQERFQTEIQTVNKQFPCEPfkflEPTLRLEYCEALAMLREAGVEMDDEED 367
Cdd:PRK05159 228 SIDVEMGFIDDHEDVMDLLENLLRYMYEDVAENCEKELELLGIELPVPE----TPIPRITYDEAIEILKSKGNEISWGDD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 368 LSTPNEKLLGRLVKEKYDTDFYVLDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGI 447
Cdd:PRK05159 304 LDTEGERLLGEYVKEEYGSDFYFITDYPSEKRPFYTMPDEDDPEISKSFDLLFRGLEITSGGQRIHRYDMLVESIKEKGL 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 16758642 448 DLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 501
Cdd:PRK05159 384 NPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPRDRHRLTP 437
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
46-501 |
1.71e-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: 449.12 E-value: 1.71e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 46 VRVKDLTVQKADEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMVKfaaNINKESIIDVEGIVRKVNQ 125
Cdd:COG0017 3 TYIKDLLPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKLENFEEAK---KLTTESSVEVTGTVVESPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 126 KigsctQQDVELHVQKIYVISLAEPRLPLQLDDAirpevegeedgratvNQDTRLDNRIIDLRTSTSQAIFHLQSGICHL 205
Cdd:COG0017 80 A-----PQGVELQAEEIEVLGEADEPYPLQPKRH---------------SLEFLLDNRHLRLRTNRFGAIFRIRSELARA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 206 FRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKSNAYLAQSPQLYKQMCICAdFEKVFCIGPVFRAEDSNTHRHLTE 285
Cdd:COG0017 140 IREFFQERGFVEVHTPIITASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMA-LEKVYTFGPTFRAEKSNTRRHLAE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 286 FVGLDIEMAFnYHYHEVVEEIADTLVQIFKGLQERFQTEIQTVN------KQFPCEPFKfleptlRLEYCEALAMLREAG 359
Cdd:COG0017 219 FWMIEPEMAF-ADLEDVMDLAEEMLKYIIKYVLENCPEELEFLGrdverlEKVPESPFP------RITYTEAIEILKKSG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 360 VEMDDEEDLSTPNEKLLGrlvkEKYDTDFYVLDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRG-EEILSGAQRIHDPQLL 438
Cdd:COG0017 292 EKVEWGDDLGTEHERYLG----EEFFKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGiGEIIGGSQREHRYDVL 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758642 439 TERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 501
Cdd:COG0017 368 VERIKEKGLDPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
175-496 |
6.05e-101 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 306.03 E-value: 6.05e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 175 NQDTRLDNRIIDLRTSTSQAIFHLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVsyfKSNA-----YLAQS 249
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLV---PSRAlgkfyALPQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 250 PQLYKQMCICADFEKVFCIGPVFRAEDSNTHRHLtEFVGLDIEMAFNyHYHEVVEEIADTLVQIFKGLQERFQTEIQTVN 329
Cdd:pfam00152 78 PQLYKQLLMVAGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFV-DYEDVMDLTEELIKEIFKEVEGIAKELEGGTL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 330 KQFPcEPFKfleptlRLEYCEALAMLREAGVEmDDEEDLSTPNEKLLGRLVKEKYDTDFYVLDKYPLAVRPFYTMPDPRN 409
Cdd:pfam00152 156 LDLK-KPFP------RITYAEAIEKLNGKDVE-ELGYGSDKPDLRFLLELVIDKNKFNPLWVTDFPAEHHPFTMPKDEDD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 410 PKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGIDLEKIKA----YIDSFRFGAPPHAGGGIGLERVTMLFLGLHN 485
Cdd:pfam00152 228 PALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPEEAEEkfgfYLDALKYGAPPHGGLGIGLDRLVMLLTGLES 307
|
330
....*....|.
gi 16758642 486 VRQTSMFPRDP 496
Cdd:pfam00152 308 IREVIAFPKTR 318
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
46-501 |
2.65e-78 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 251.95 E-value: 2.65e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 46 VRVKDLTVQK-ADEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQmvKFAANINKESIIDVEGIVRKVN 124
Cdd:PRK03932 4 VSIKDILKGKyVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDNGEEYF--EEIKKLTTGSSVIVTGTVVESP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 125 QKigsctQQDVELHVQKIYVISLAEPRLPLQLDdairpevegeedgRATVnqDTRLDNRIIDLRTSTSQAIFHLQSGICH 204
Cdd:PRK03932 82 RA-----GQGYELQATKIEVIGEDPEDYPIQKK-------------RHSI--EFLREIAHLRPRTNKFGAVMRIRNTLAQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 205 LFRETLINKGFVEIQTPKIISAASEGGANVFTVS---------YFKSNAYLAQSPQLYKQMCICAdFEKVFCIGPVFRAE 275
Cdd:PRK03932 142 AIHEFFNENGFVWVDTPIITASDCEGAGELFRVTtldldfskdFFGKEAYLTVSGQLYAEAYAMA-LGKVYTFGPTFRAE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 276 DSNTHRHLTEFVGLDIEMAFnYHyHEVVEEIADTLVQ-IFKGLQERFQTEIQTVNKQFPCEPFKFLEPTL-----RLEYC 349
Cdd:PRK03932 221 NSNTRRHLAEFWMIEPEMAF-AD-LEDNMDLAEEMLKyVVKYVLENCPDDLEFLNRRVDKGDIERLENFIespfpRITYT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 350 EALAMLREAGVEMDDE----EDLSTPNEKLLgrlVKEKYDTDFYVLDkYPLAVRPFYTMPDPRNpKQSNSYDMFMRG-EE 424
Cdd:PRK03932 299 EAIEILQKSGKKFEFPvewgDDLGSEHERYL---AEEHFKKPVFVTN-YPKDIKAFYMRLNPDG-KTVAAMDLLAPGiGE 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758642 425 ILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 501
Cdd:PRK03932 374 IIGGSQREERLDVLEARIKELGLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
46-501 |
6.61e-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: 235.35 E-value: 6.61e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 46 VRVKDLTVQ---KADEVVWVRARVHTSRAKGKQCFLVLRQQQF--NVQALVAVGDhaSKQMVKFAANINKESIIDVEGIV 120
Cdd:TIGR00457 2 AAIKDLLQQvykFVGDEVTVSGWVRTKRSSKKIIFLELNDGSSlgPIQAVINGED--NPYLFQLLKSLTTGSSVSVTGKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 121 RKVNQKigsctQQDVELHVQKIYVISLAEPR-LPLQLDDairpevegeedgratvnQDTRL--DNRIIDLRTSTSQAIFH 197
Cdd:TIGR00457 80 VESPGK-----GQPVELQVKKIEVVGEAEPDdYPLQKKE-----------------HSLEFlrDIAHLRLRTNTLGAVMR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 198 LQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVS---------YFKSNAYLAQSPQLYKQMCICAdFEKVFCI 268
Cdd:TIGR00457 138 VRNALSQAIHRYFQENGFTWVSPPILTSNDCEGAGELFRVStgnidfsqdFFGKEAYLTVSGQLYLETYALA-LSKVYTF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 269 GPVFRAEDSNTHRHLTEFVGLDIEMAFnYHYHEVVEEIADTLVQIFKGLQERFQTEIQTVNKQFPCEPFKFLEPTL---- 344
Cdd:TIGR00457 217 GPTFRAEKSNTSRHLSEFWMIEPEMAF-ANLNDLLQLAETLIKYIIKAVLENCSQELKFLEKNFDKDLIKRLENIInnkf 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 345 -RLEYCEALAMLREAGVEMDDEE----DLSTPNEKLLGrlvkEKYDTDFYVLDKYPLAVRPFYtMPDPRNPKQSNSYDMF 419
Cdd:TIGR00457 296 aRITYTDAIEILKESDKNFEYEDfwgdDLQTEHERFLA----EEYFKPPVFVTNYPKDIKAFY-MKLNDDGKTVAAMDLL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 420 MRG-EEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKR 498
Cdd:TIGR00457 371 APGiGEIIGGSEREDDLDKLENRMKEMGLDTDALNWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGN 450
|
...
gi 16758642 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 |
1.10e-56 |
|
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: 189.61 E-value: 1.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 196 FHLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKS--NAYLAQSPQLYKQMCICADFEKVFCIGPVFR 273
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALglDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 274 AEDSNThRHLTEFVGLDIEMAF-NYH-YHEVVEEIADTLVQIFKGlqerfqteiqTVNKQFPCEPFKFLEPTLRLEYCEA 351
Cdd:cd00669 81 NEDLRA-RHQPEFTMMDLEMAFaDYEdVIELTERLVRHLAREVLG----------VTAVTYGFELEDFGLPFPRLTYREA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 352 LamlreagvemddeedlstpnekllgrlvkEKYDTDFYVLDkYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQR 431
Cdd:cd00669 150 L-----------------------------ERYGQPLFLTD-YPAEMHSPLASPHDVNPEIADAFDLFINGVEVGNGSSR 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758642 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 |
8.36e-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: 8.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 60 VWVRARVHTSRAKG-KQCFLVLRQQQFNVQALVAVGDHA-SKQMVKFAANINKESIIDVEGIVRKVNQKIGSCTQQDVEL 137
Cdd:cd04320 2 VLIRARVHTSRAQGaKLAFLVLRQQGYTIQGVLAASAEGvSKQMVKWAGSLSKESIVDVEGTVKKPEEPIKSCTQQDVEL 81
|
90 100
....*....|....*....|.
gi 16758642 138 HVQKIYVISLAEPRLPLQLDD 158
Cdd:cd04320 82 HIEKIYVVSEAAEPLPFQLED 102
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
187-496 |
6.23e-48 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 168.66 E-value: 6.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 187 LRTSTSQAIFHLQSGICHLFRETLINKGFVEIQTPkIISA--------ASEGGANVFTVSYFKSNAYLAQSPQLYKQMCI 258
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPP-IISPstdplmglGSDLPVKQISIDFYGVEYYLADSMILHKQLAL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 259 cADFEKVFCIGPVFRAE--DSNTHRHLTEFVGLDIEMAfNYHYHEVVEEIADTLVQIFKGLQERFQTEIQTVNKQFPcep 336
Cdd:PRK06462 100 -RMLGKIFYLSPNFRLEpvDKDTGRHLYEFTQLDIEIE-GADLDEVMDLIEDLIKYLVKELLEEHEDELEFFGRDLP--- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 337 fKFLEPTLRLEYCEALAMLREAGVEMDDEEDLSTPNEKLLgrlvKEKYDTDFYVLDkYPLAVRPFYTMPDPRNPKQSNSY 416
Cdd:PRK06462 175 -HLKRPFKRITHKEAVEILNEEGCRGIDLEELGSEGEKSL----SEHFEEPFWIID-IPKGSREFYDREDPERPGVLRNY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 417 DMFMR---GEeILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 493
Cdd:PRK06462 249 DLLLPegyGE-AVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFP 327
|
...
gi 16758642 494 RDP 496
Cdd:PRK06462 328 RVP 330
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
66-493 |
8.97e-41 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 154.45 E-value: 8.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 66 VHTSRAKGKQCFLVLRQQQFNVQALVavgdHASKQMVKFAANINKESIIDVEGIVRK-----VNQKIGSctqQDVELHVQ 140
Cdd:PRK00476 26 VHRRRDHGGLIFIDLRDREGIVQVVF----DPDAEAFEVAESLRSEYVIQVTGTVRArpegtVNPNLPT---GEIEVLAS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 141 KIYVISLAEPrLPLQLDDairpevegEEDgratVNQDTRLDNRIIDLRTSTSQAIFHLQSGICHLFRETLINKGFVEIQT 220
Cdd:PRK00476 99 ELEVLNKSKT-LPFPIDD--------EED----VSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDNGFLEIET 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 221 PkIISAASEGGANVFTV-------SYFksnAyLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNTHRhLTEFVGLDIEM 293
Cdd:PRK00476 166 P-ILTKSTPEGARDYLVpsrvhpgKFY---A-LPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADR-QPEFTQIDIEM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 294 AFnyhyheV-VEEIADTLVQIFKGL------------------QE------------RFQTEIQTVNKQFPCEPFK-FLE 341
Cdd:PRK00476 240 SF------VtQEDVMALMEGLIRHVfkevlgvdlptpfprmtyAEamrrygsdkpdlRFGLELVDVTDLFKDSGFKvFAG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 342 PTLRLEYCEALAMLREAG----VEMDD-------------------EEDLSTP---------NEKLLGRLVKEKYDTDFY 389
Cdd:PRK00476 314 AANDGGRVKAIRVPGGAAqlsrKQIDEltefakiygakglayikvnEDGLKGPiakflseeeLAALLERTGAKDGDLIFF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 390 VLDKYPL------AVR----------------------------------------PFyTMPDP--------RNPKQ--S 413
Cdd:PRK00476 394 GADKAKVvndalgALRlklgkelglidedkfaflwvvdfpmfeydeeegrwvaahhPF-TMPKDedldeletTDPGKarA 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 414 NSYDMFMRGEEILSGAQRIHDPQLLtERALHH-GIDLEKIKA----YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQ 488
Cdd:PRK00476 473 YAYDLVLNGYELGGGSIRIHRPEIQ-EKVFEIlGISEEEAEEkfgfLLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRD 551
|
....*
gi 16758642 489 TSMFP 493
Cdd:PRK00476 552 VIAFP 556
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
198-493 |
6.51e-39 |
|
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: 6.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 198 LQSGICHLFRETLINKGFVEIQTPkIISAASEGGANVFTVSY--FKSNAY-LAQSPQLYKQMCICADFEKVFCIGPVFRA 274
Cdd:cd00777 3 LRSRVIKAIRNFLDEQGFVEIETP-ILTKSTPEGARDFLVPSrlHPGKFYaLPQSPQLFKQLLMVSGFDRYFQIARCFRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 275 EDSNTHRHlTEFVGLDIEMAFnYHYHEVVEEIADTLVQIFKglqERFQTEIQTvnkqfpcePFKfleptlRLEYCEAlam 354
Cdd:cd00777 82 EDLRADRQ-PEFTQIDIEMSF-VDQEDIMSLIEGLLKYVFK---EVLGVELTT--------PFP------RMTYAEA--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 355 LREAGV-----------EMDDEEdlstpnekllGRLV---------KEKYDTDfyvLDKYPLAVRpfytmpdprnpkqSN 414
Cdd:cd00777 140 MERYGFkflwivdfplfEWDEEE----------GRLVsahhpftapKEEDLDL---LEKDPEDAR-------------AQ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 415 SYDMFMRGEEILSGAQRIHDPQlLTERALHH-GIDLEKIKA----YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQT 489
Cdd:cd00777 194 AYDLVLNGVELGGGSIRIHDPD-IQEKVFEIlGLSEEEAEEkfgfLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDV 272
|
....
gi 16758642 490 SMFP 493
Cdd:cd00777 273 IAFP 276
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
50-493 |
1.99e-36 |
|
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: 142.06 E-value: 1.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 50 DLTVQKADEVV----WVrarvHTSRAKGKQCFLVLR------QqqfnvqalVAVGDHASKQMVKFAANINKESIIDVEGI 119
Cdd:COG0173 9 ELRESDVGQEVtlsgWV----HRRRDHGGLIFIDLRdrygitQ--------VVFDPDDSAEAFEKAEKLRSEYVIAVTGK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 120 VRK-----VNQKI--GsctqqDVELHVQKIYVISLAEPrLPLQLDDAIrpevegeedgraTVNQDTRLDNRIIDLRTSTS 192
Cdd:COG0173 77 VRArpegtVNPKLptG-----EIEVLASELEILNKAKT-PPFQIDDDT------------DVSEELRLKYRYLDLRRPEM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 193 QAIFHLQSGICHLFRETLINKGFVEIQTPkIISAASEGGANVFTV-------SYFksnAyLAQSPQLYKQMCICADFEKV 265
Cdd:COG0173 139 QKNLILRHKVTKAIRNYLDENGFLEIETP-ILTKSTPEGARDYLVpsrvhpgKFY---A-LPQSPQLFKQLLMVSGFDRY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 266 FCIGPVFRAEDSNTHRHLtEFVGLDIEMAFnyhyhevVEE-----IADTLVQ-IFKGL--------------QE------ 319
Cdd:COG0173 214 FQIARCFRDEDLRADRQP-EFTQLDIEMSF-------VDQedvfeLMEGLIRhLFKEVlgvelptpfprmtyAEameryg 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 320 ------RFQTEIQTVNKQFPCEPFK-FLEPTLRLEYCEALAM------------------------------LREAGVE- 361
Cdd:COG0173 286 sdkpdlRFGLELVDVTDIFKDSGFKvFAGAAENGGRVKAINVpggaslsrkqideltefakqygakglayikVNEDGLKs 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 362 -----MDDEE-------------DL-----STPNE--KLLGRL-----------VKEKYD----TDFyvldkyPL----- 396
Cdd:COG0173 366 piakfLSEEElaailerlgakpgDLiffvaDKPKVvnKALGALrlklgkelgliDEDEFAflwvVDF------PLfeyde 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 397 ------AV-RPFyTMPDP-------RNPKQ--SNSYDMFMRGEEILSGAQRIHDPQLLtERALHH-GIDLEKIKA----Y 455
Cdd:COG0173 440 eegrwvAMhHPF-TMPKDedldlleTDPGKvrAKAYDLVLNGYELGGGSIRIHDPELQ-EKVFELlGISEEEAEEkfgfL 517
|
570 580 590
....*....|....*....|....*....|....*...
gi 16758642 456 IDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 493
Cdd:COG0173 518 LEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
2-493 |
8.31e-31 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 126.30 E-value: 8.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 2 PSANASRKGQEKPREIVDAAEDYA-----------KERYGvssMIQSQEKPDRVLVRVKdltvqkadevvwvrARVHTSR 70
Cdd:PTZ00385 58 ATKTVTQEASRAPRSKLDLPAAYSsfrgitpisevRERYG---YLASGDRAAQATVRVA--------------GRVTSVR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 71 AKGKQCFLVLRQQQFNVQALVAVGDHASKQMVK-FAANINKESIIDVEGIvrkvnqkigSCTQQDVELHVQKIYVISLAe 149
Cdd:PTZ00385 121 DIGKIIFVTIRSNGNELQVVGQVGEHFTREDLKkLKVSLRVGDIIGADGV---------PCRMQRGELSVAASRMLILS- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 150 prlP-LQLDDAIRPEVEGeedgrATVNQDT--RLDNRIIDLRTSTSQ-AIFHLQSGICHLFRETLINKGFVEIQTPKIIS 225
Cdd:PTZ00385 191 ---PyVCTDQVVCPNLRG-----FTVLQDNdvKYRYRFTDMMTNPCViETIKKRHVMLQALRDYFNERNFVEVETPVLHT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 226 AASEGGANVFtVSYFKSNA---YLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNtHRHLTEFVGLDIEMAfnYH-YHE 301
Cdd:PTZ00385 263 VASGANAKSF-VTHHNANAmdlFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDAD-RSHNPEFTSCEFYAA--YHtYED 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 302 VVEEIADTLVQIFKGLQERFQTEIQTVNKQFPCEPFKFLEPTLRLEYCEALAmlREAGVEMDDEEDLSTPNEKLLGRLVK 381
Cdd:PTZ00385 339 LMPMTEDIFRQLAMRVNGTTVVQIYPENAHGNPVTVDLGKPFRRVSVYDEIQ--RMSGVEFPPPNELNTPKGIAYMSVVM 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 382 EKYDT----------------DFYVLDKyplAVRPFYTMPDP-----------RNPKQSNSYDMFMRGEEILSGAQRIHD 434
Cdd:PTZ00385 417 LRYNIplppvrtaakmfekliDFFITDR---VVEPTFVMDHPlfmsplakeqvSRPGLAERFELFVNGIEYCNAYSELND 493
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 435 P--------QLLTERalhHGIDLEKI---KAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 493
Cdd:PTZ00385 494 PheqyhrfqQQLVDR---QGGDEEAMpldETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFP 560
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
61-501 |
2.44e-29 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 122.02 E-value: 2.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 61 WVRArvhtSRAKGKQCFLVLRQQQFNVQALVAvGDHASKQMVKFAANINKESIIDVEGIVRKVNQKIGS--CTQQDVELH 138
Cdd:PRK12820 26 WVDA----FRDHGELLFIHLRDRNGFIQAVFS-PEAAPADVYELAASLRAEFCVALQGEVQKRLEETENphIETGDIEVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 139 VQKIYVISLAEPrLPLQLDDaiRPEVEGEEDGRA-TVNQDTRLDNRIIDLRTSTSQAIFHLQSGICHLFRETLINKGFVE 217
Cdd:PRK12820 101 VRELSILAASEA-LPFAISD--KAMTAGAGSAGAdAVNEDLRLQYRYLDIRRPAMQDHLAKRHRIIKCARDFLDSRGFLE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 218 IQTPKIISAASEGGANVFTVSYFKSNAY--LAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNTHRHlTEFVGLDIEMAF 295
Cdd:PRK12820 178 IETPILTKSTPEGARDYLVPSRIHPKEFyaLPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQ-PEFTQLDIEASF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 296 --NYHYHEVVEEI------------------------------------------------ADTLVQIFKGLQERfQTEI 325
Cdd:PRK12820 257 idEEFIFELIEELtarmfaiggialprpfprmpyaeamdttgsdrpdlrfdlkfadatdifENTRYGIFKQILQR-GGRI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 326 QTVNKQFPCEpfKFLEPTLRLEYCEALA----------MLREAG------VEMDDEEDLstpnEKLLGRLVKEKYDTDFY 389
Cdd:PRK12820 336 KGINIKGQSE--KLSKNVLQNEYAKEIApsfgakgmtwMRAEAGgldsniVQFFSADEK----EALKRRFHAEDGDVIIM 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 390 VLDK----------------------------YPLAVRPF-----------------YTMP-----DPRNPK-----QSN 414
Cdd:PRK12820 410 IADAscaivlsalgqlrlhladrlglipegvfHPLWITDFplfeatddggvtsshhpFTAPdredfDPGDIEelldlRSR 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 415 SYDMFMRGEEILSGAQRIHDP--QLLTERALhhGIDLEKIKA----YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQ 488
Cdd:PRK12820 490 AYDLVVNGEELGGGSIRINDKdiQLRIFAAL--GLSEEDIEDkfgfFLRAFDFAAPPHGGIALGLDRVVSMILQTPSIRE 567
|
570
....*....|...
gi 16758642 489 TSMFPRDPKRLTP 501
Cdd:PRK12820 568 VIAFPKNRSAACP 580
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
41-496 |
7.03e-28 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 117.00 E-value: 7.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 41 PDRVLVRV-KDLTVQKadevvWVRarvhTSRAKGKQCFLVLRQQQF--NVQALVAVGDHASKQMVkfAANINKESIIDVE 117
Cdd:PLN02603 99 EDEGLARVgKTLNVMG-----WVR----TLRAQSSVTFIEVNDGSClsNMQCVMTPDAEGYDQVE--SGLITTGASVLVQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 118 GIVRKvnqkiGSCTQQDVELHVQKIYVISLAEPRLPLQLDDAIRPEVEGEEDGRAtvnqdtrldnriidlRTSTSQAIFH 197
Cdd:PLN02603 168 GTVVS-----SQGGKQKVELKVSKIVVVGKSDPSYPIQKKRVSREFLRTKAHLRP---------------RTNTFGAVAR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 198 LQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVS------------------------------YFKSNAYLA 247
Cdd:PLN02603 228 VRNALAYATHKFFQENGFVWVSSPIITASDCEGAGEQFCVTtlipnsaenggslvddipktkdglidwsqdFFGKPAFLT 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 248 QSPQLYKQMCICAdFEKVFCIGPVFRAEDSNTHRHLTEFVGLDIEMAF----------NYHYHEVVEEIADTLVQ----- 312
Cdd:PLN02603 308 VSGQLNGETYATA-LSDVYTFGPTFRAENSNTSRHLAEFWMIEPELAFadlnddmacaTAYLQYVVKYILENCKEdmeff 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 313 ---IFKGLQERFQteiQTVNKQFpcepfkfleptLRLEYCEALAMLREA----------GVEMDDEEDLSTPNEKLLGRL 379
Cdd:PLN02603 387 ntwIEKGIIDRLS---DVVEKNF-----------VQLSYTDAIELLLKAkkkfefpvkwGLDLQSEHERYITEEAFGGRP 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 380 VkekydtdfyVLDKYPLAVRPFYtMPDPRNPKQSNSYDMFM-RGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDS 458
Cdd:PLN02603 453 V---------IIRDYPKEIKAFY-MRENDDGKTVAAMDMLVpRVGELIGGSQREERLEYLEARLDELKLNKESYWWYLDL 522
|
490 500 510
....*....|....*....|....*....|....*...
gi 16758642 459 FRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDP 496
Cdd:PLN02603 523 RRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPRVP 560
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
50-494 |
7.30e-25 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 108.34 E-value: 7.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 50 DLTVQKADEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQalVAVGDHASKQMVKFAANINKESIIDVEGIVRK-----VN 124
Cdd:PLN02903 65 ALSVNDVGSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQ--VVTLPDEFPEAHRTANRLRNEYVVAVEGTVRSrpqesPN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 125 QKIGSCTQQDVELHVQKIYVISLAEPRLplqlddairpeVEGEEDGRATVNQDTRLDNRIIDLRTSTSQAIFHLQSGICH 204
Cdd:PLN02903 143 KKMKTGSVEVVAESVDILNVVTKSLPFL-----------VTTADEQKDSIKEEVRLRYRVLDLRRPQMNANLRLRHRVVK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 205 LFRETLINK-GFVEIQTPKIISAASEGGANVFTVSYFKSNAYLA--QSPQLYKQMCICADFEKVFCIGPVFRAEDSNTHR 281
Cdd:PLN02903 212 LIRRYLEDVhGFVEIETPILSRSTPEGARDYLVPSRVQPGTFYAlpQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 282 HlTEFVGLDIEMAFNyhYHEVVEEIADTLV-QIFK---GLQ-----------------------ERFQTEIQTVNKQFPC 334
Cdd:PLN02903 292 Q-PEFTQLDMELAFT--PLEDMLKLNEDLIrQVFKeikGVQlpnpfprltyaeamskygsdkpdLRYGLELVDVSDVFAE 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 335 EPFKFLEPTL--------------------RLE-----YCEALAM----LREAGVEMDDE--------EDLSTPN-EKLL 376
Cdd:PLN02903 369 SSFKVFAGALesggvvkaicvpdgkkisnnTALkkgdiYNEAIKSgakgLAFLKVLDDGElegikalvESLSPEQaEQLL 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 377 GR----------------------------LVKEKYD------------TDFYVLDKYPLAVR------PFyTMPDPRNP 410
Cdd:PLN02903 449 AAcgagpgdlilfaagptssvnktldrlrqFIAKTLDlidpsrhsilwvTDFPMFEWNEDEQRlealhhPF-TAPNPEDM 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 411 KQSNS-----YDMFMRGEEILSGAQRIH--DPQLLTERALhhGIDLE----KIKAYIDSFRFGAPPHAGGGIGLERVTML 479
Cdd:PLN02903 528 GDLSSaralaYDMVYNGVEIGGGSLRIYrrDVQQKVLEAI--GLSPEeaesKFGYLLEALDMGAPPHGGIAYGLDRLVML 605
|
570
....*....|....*
gi 16758642 480 FLGLHNVRQTSMFPR 494
Cdd:PLN02903 606 LAGAKSIRDVIAFPK 620
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
235-498 |
9.34e-24 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 104.69 E-value: 9.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 235 FTVSYFKSNAYLAQSPQLYKQMCICAdFEKVFCIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVveEIADTLVQ-I 313
Cdd:PLN02221 300 YSKDFFGRQAFLTVSGQLQVETYACA-LSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFADLEDDM--NCAEAYVKyM 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 314 FKGLQERFQTEIQTVNKQFPCEPFKFLE-----PTLRLEYCEALAMLREA---GVEMDDEE----DLSTPNEKLLGRLVK 381
Cdd:PLN02221 377 CKWLLDKCFDDMELMAKNFDSGCIDRLRmvastPFGRITYTEAIELLEEAvakGKEFDNNVewgiDLASEHERYLTEVLF 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 382 EKYdtdfYVLDKYPLAVRPFYtMPDPRNPKQSNSYDMFM-RGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFR 460
Cdd:PLN02221 457 QKP----LIVYNYPKGIKAFY-MRLNDDEKTVAAMDVLVpKVGELIGGSQREERYDVIKQRIEEMGLPIEPYEWYLDLRR 531
|
250 260 270
....*....|....*....|....*....|....*...
gi 16758642 461 FGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKR 498
Cdd:PLN02221 532 YGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRYPGK 569
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
60-493 |
9.73e-23 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 101.29 E-value: 9.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 60 VWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMVKFAANINKESIIDVEGIVRKVnqkigsctqQDVELHv 139
Cdd:PRK12445 68 VSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVYNDQFKKWDLGDIIGARGTLFKT---------QTGELS- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 140 qkiyvISLAEPRLplqLDDAIRP---EVEGEEDgratvnQDTRLDNRIIDL-RTSTSQAIFHLQSGICHLFRETLINKGF 215
Cdd:PRK12445 138 -----IHCTELRL---LTKALRPlpdKFHGLQD------QEVRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMVARGF 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 216 VEIQTPKIISAASEGGANVFTVSY--FKSNAYLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNThRHLTEFVGLDIEM 293
Cdd:PRK12445 204 MEVETPMMQVIPGGASARPFITHHnaLDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISV-RHNPEFTMMELYM 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 294 AFNyHYHEVVEeIADTLvqiFKGLQerfQTEIQTVNKQFPCEPFKFLEPTLRLEYCEALAMLR-----------EAGVEM 362
Cdd:PRK12445 283 AYA-DYHDLIE-LTESL---FRTLA---QEVLGTTKVTYGEHVFDFGKPFEKLTMREAIKKYRpetdmadldnfDAAKAL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 363 DDEEDLSTPNEKLLGRLVKEKYD-------TDFYVLDKYPLAVRPFYTMPDPrNPKQSNSYDMFMRGEEILSGAQRIHDP 435
Cdd:PRK12445 355 AESIGITVEKSWGLGRIVTEIFDevaeahlIQPTFITEYPAEVSPLARRNDV-NPEITDRFEFFIGGREIGNGFSELNDA 433
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758642 436 QLLTER------ALHHGIDLEKI--KAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 493
Cdd:PRK12445 434 EDQAERfqeqvnAKAAGDDEAMFydEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
184-496 |
4.06e-22 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 99.71 E-value: 4.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 184 IIDLRTSTSQAIfhlqsgicHLFRETlinKGFVEIQTPKIISAASEGGANVFTVS------------------------- 238
Cdd:PTZ00425 214 VIRIRNALAIAT--------HLFFQS---RGFLYIHTPLITTSDCEGGGEMFTVTtllgedadyraiprvnkknkkgekr 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 239 --------------------------------------YFKSNAYLAQSPQLYKQMcICADFEKVFCIGPVFRAEDSNTH 280
Cdd:PTZ00425 283 edilntcnannnngnssssnavsspaypdqylidykkdFFSKQAFLTVSGQLSLEN-LCSSMGDVYTFGPTFRAENSHTS 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 281 RHLTEFVGLDIEMAFNYHYHEVveEIADTLVQIFKG------------LQERFQTEIQTVNKQFPCEPFKFLEPT----L 344
Cdd:PTZ00425 362 RHLAEFWMIEPEIAFADLYDNM--ELAESYIKYCIGyvlnnnfddiyyFEENVETGLISRLKNILDEDFAKITYTnvidL 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 345 RLEYCEALAMLREAGVEMDDEEDlstpnekllgRLVKEKYDTDFYVLDKYPLAVRPFYtMPDPRNPKQSNSYDMFM-RGE 423
Cdd:PTZ00425 440 LQPYSDSFEVPVKWGMDLQSEHE----------RFVAEQIFKKPVIVYNYPKDLKAFY-MKLNEDQKTVAAMDVLVpKIG 508
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758642 424 EILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDP 496
Cdd:PTZ00425 509 EVIGGSQREDNLERLDKMIKEKKLNMESYWWYRQLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPRYP 581
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
196-493 |
1.97e-21 |
|
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a lysine to the 3' OH group of ribose of the appropriate tRNA. Its assignment to class II aaRS is based upon its structure and the presence of three characteristic sequence motifs in the core domain. It is found in eukaryotes as well as some prokaryotes and archaea. However, LysRS belongs to class I aaRS's in some prokaryotes and archaea. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.
Pssm-ID: 238398 [Multi-domain] Cd Length: 329 Bit Score: 94.96 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 196 FHLQSGICHLFRETLINKGFVEIQTPKIISAAseGGANV--FTVSY--FKSNAYLAQSPQLYKQMCICADFEKVFCIGPV 271
Cdd:cd00775 8 FIVRSKIISYIRKFLDDRGFLEVETPMLQPIA--GGAAArpFITHHnaLDMDLYLRIAPELYLKRLIVGGFERVYEIGRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 272 FRAEDSNThRHLTEFVGLDIEMAF-NYH-YHEVVEEIADTLVQ-IFKGLQERFQTEIQTVNKqfpcePFKfleptlRLEY 348
Cdd:cd00775 86 FRNEGIDL-THNPEFTMIEFYEAYaDYNdMMDLTEDLFSGLVKkINGKTKIEYGGKELDFTP-----PFK------RVTM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 349 CEALAmlREAGVEMDDEEDLSTPN-EKLLGRLVKEKYD---TDFYVLDK------------------YPLAVRPFyTMPD 406
Cdd:cd00775 154 VDALK--EKTGIDFPELDLEQPEElAKLLAKLIKEKIEkprTLGKLLDKlfeefveptliqptfiidHPVEISPL-AKRH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 407 PRNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTER-----ALHHGIDLEKI---KAYIDSFRFGAPPHAGGGIGLERVTM 478
Cdd:cd00775 231 RSNPGLTERFELFICGKEIANAYTELNDPFDQRERfeeqaKQKEAGDDEAMmmdEDFVTALEYGMPPTGGLGIGIDRLVM 310
|
330
....*....|....*
gi 16758642 479 LFLGLHNVRQTSMFP 493
Cdd:cd00775 311 LLTDSNSIRDVILFP 325
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
235-494 |
1.76e-18 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 88.39 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 235 FTVSYFKSNAYLAQSPQLYKQMCICAdFEKVFCIGPVFRAEDSNTHRHLTEFVGLDIEMAFNyHYHEVVEEIADTLVQIF 314
Cdd:PLN02532 363 FSKDFFSRPTYLTVSGRLHLESYACA-LGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFS-ELEDAMNCAEDYFKFLC 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 315 KGLQERFQTEIQTVNKQFPCEPFKFLE-----PTLRLEYCEALAMLREA-GVEMDDEEDLSTP-NEKLLGRLVKEKYDTD 387
Cdd:PLN02532 441 KWVLENCSEDMKFVSKRIDKTISTRLEaiissSLQRISYTEAVDLLKQAtDKKFETKPEWGIAlTTEHLSYLADEIYKKP 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 388 FYVLDkYPLAVRPFYTMPDpRNPKQSNSYDMFM-RGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPH 466
Cdd:PLN02532 521 VIIYN-YPKELKPFYVRLN-DDGKTVAAFDLVVpKVGTVITGSQNEERMDILNARIEELGLPREQYEWYLDLRRHGTVKH 598
|
250 260
....*....|....*....|....*...
gi 16758642 467 AGGGIGLERVTMLFLGLHNVRQTSMFPR 494
Cdd:PLN02532 599 SGFSLGFELMVLFATGLPDVRDAIPFPR 626
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
175-493 |
1.67e-17 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 85.45 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 175 NQDTRLDNRIIDLRTS-TSQAIFHLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSY--FKSNAYLAQSPQ 251
Cdd:PTZ00417 231 DTEIRYRQRYLDLMINeSTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHndLDLDLYLRIATE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 252 LYKQMCICADFEKVFCIGPVFRAED-SNTHRhlTEFVGLDIEMAFNyHYHEVVEEIADTLVQIFKGLqerFQTEIQTVNK 330
Cdd:PTZ00417 311 LPLKMLIVGGIDKVYEIGKVFRNEGiDNTHN--PEFTSCEFYWAYA-DFYDLIKWSEDFFSQLVMHL---FGTYKILYNK 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 331 QFP-CEPFK--FLEPTLRLEYCEALAMLREAGVE--------------MDDEEDLSTPN----EKLLGRLVKEkydtdfY 389
Cdd:PTZ00417 385 DGPeKDPIEidFTPPYPKVSIVEELEKLTNTKLEqpfdspetinkminLIKENKIEMPNpptaAKLLDQLASH------F 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 390 VLDKYPlaVRPFYTMPDPR-----------NPKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGIDLEKIKA---- 454
Cdd:PTZ00417 459 IENKYP--NKPFFIIEHPQimsplakyhrsKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAeafq 536
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 16758642 455 ----YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 493
Cdd:PTZ00417 537 fdaaFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFP 579
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
60-146 |
2.38e-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: 76.84 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 60 VWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASkqMVKFAANINKESIIDVEGIVRKVnqKIGSCTQQDVELHV 139
Cdd:cd04100 2 VTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELGE--FFEEAEKLRTESVVGVTGTVVKR--PEGNLATGEIELQA 77
|
....*..
gi 16758642 140 QKIYVIS 146
Cdd:cd04100 78 EELEVLS 84
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
65-493 |
9.10e-16 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 79.75 E-value: 9.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 65 RVHTSRAKGKQCFLVLRQQQFNVQALVAVgDHASKQMVKFAANINKESIIDVEGIVRKvnqkigscTQQDvEL--HVQKI 142
Cdd:PRK00484 62 RVMLKRVMGKASFATLQDGSGRIQLYVSK-DDVGEEALEAFKKLDLGDIIGVEGTLFK--------TKTG-ELsvKATEL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 143 YVISLAepRLPLqlddairPEV-EGEEDgratvnQDTRLDNRIIDLRTS-TSQAIFHLQSGICHLFRETLINKGFVEIQT 220
Cdd:PRK00484 132 TLLTKS--LRPL-------PDKfHGLTD------VETRYRQRYVDLIVNpESRETFRKRSKIISAIRRFLDNRGFLEVET 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 221 PKIISAAseGGANV--FTVsyfKSNA-----YLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNThRHLTEFVGLDIEM 293
Cdd:PRK00484 197 PMLQPIA--GGAAArpFIT---HHNAldidlYLRIAPELYLKRLIVGGFERVYEIGRNFRNEGIDT-RHNPEFTMLEFYQ 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 294 AF-NYH---------YHEVVEEIADTLVQIFKGlqerfqTEIqTVNKQFPCEPFK----------FLEPTLRleycEALA 353
Cdd:PRK00484 271 AYaDYNdmmdlteelIRHLAQAVLGTTKVTYQG------TEI-DFGPPFKRLTMVdaikeytgvdFDDMTDE----EARA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 354 MLREAGVEMDDEEDLSTPNEKLLGRLVKEKYDTDFYVLDkYPLAVRPFyTMPDPRNPKQSNSYDMFMRGEEILSG----- 428
Cdd:PRK00484 340 LAKELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITD-YPVEISPL-AKRHREDPGLTERFELFIGGREIANAfseln 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16758642 429 -----AQRIHDpQLLtERAL----HHGIDLEkikaYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 493
Cdd:PRK00484 418 dpidqRERFEA-QVE-AKEAgddeAMFMDED----FLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
57-493 |
2.74e-15 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 78.49 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 57 DEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMV--KFAANINKESIIDVEGIVRKvnQKIGsctqqd 134
Cdd:PLN02502 108 DVSVSVAGRIMAKRAFGKLAFYDLRDDGGKIQLYADKKRLDLDEEEfeKLHSLVDRGDIVGVTGTPGK--TKKG------ 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 135 vELHVQKIYVISLAEPRLPLqlddairPE-VEGEEDgratvnQDTRLDNRIIDLRTSTSQA-IFHLQSGICHLFRETLIN 212
Cdd:PLN02502 180 -ELSIFPTSFEVLTKCLLML-------PDkYHGLTD------QETRYRQRYLDLIANPEVRdIFRTRAKIISYIRRFLDD 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 213 KGFVEIQTPKIISAAseGGANV--FtVSYFKS---NAYLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNThRHLTEFV 287
Cdd:PLN02502 246 RGFLEVETPMLNMIA--GGAAArpF-VTHHNDlnmDLYLRIATELHLKRLVVGGFERVYEIGRQFRNEGIST-RHNPEFT 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 288 GLDIEMAF-NYH-YHEVVEEIADTLV-QIFKGLQERFQ-TEIQTVnkqfpcEPFK------FLEPTLRLEYCEAL--AML 355
Cdd:PLN02502 322 TCEFYQAYaDYNdMMELTEEMVSGMVkELTGSYKIKYHgIEIDFT------PPFRrismisLVEEATGIDFPADLksDEA 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 356 REAGVEMDDEEDLSTPN--------EKLLGRLVKEKYDTDFYVLDkYPLAVRPFyTMPDPRNPKQSNSYDMFMRGEEILS 427
Cdd:PLN02502 396 NAYLIAACEKFDVKCPPpqttgrllNELFEEFLEETLVQPTFVLD-HPVEMSPL-AKPHRSKPGLTERFELFINGRELAN 473
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16758642 428 GAQRIHDP----QLLTERALHHGIDLEKIKAYIDSF----RFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 493
Cdd:PLN02502 474 AFSELTDPvdqrERFEEQVKQHNAGDDEAMALDEDFctalEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFP 547
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
175-493 |
3.97e-15 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 78.47 E-value: 3.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 175 NQDTRLDNRIIDLRTST-SQAIFHLQSGICHLFRETLINKGFVEIQTPkiISAASEGGANV--FTVsyfKSNAY-----L 246
Cdd:PRK02983 748 DPEARVRQRYLDLAVNPeARDLLRARSAVVRAVRETLVARGFLEVETP--ILQQVHGGANArpFVT---HINAYdmdlyL 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 247 AQSPQLY-KQMCIcADFEKVFCIGPVFRAE--------------------DSNTHRHLTEfvGLDIEMAFNYHYHEVV-- 303
Cdd:PRK02983 823 RIAPELYlKRLCV-GGVERVFELGRNFRNEgvdathnpeftlleayqahaDYDTMRDLTR--ELIQNAAQAAHGAPVVmr 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 304 --EEIADTLVQI---------FKGLQERFQTEIQtvnkqfPCEPFkflePTLRlEYCEAlamlreAGVEMDDEEDLSTPN 372
Cdd:PRK02983 900 pdGDGVLEPVDIsgpwpvvtvHDAVSEALGEEID------PDTPL----AELR-KLCDA------AGIPYRTDWDAGAVV 962
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 373 EKLLGRLVkEKYDTD--FYVldKYPLAVRPFyTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDP----QLLTERAL-HH 445
Cdd:PRK02983 963 LELYEHLV-EDRTTFptFYT--DFPTSVSPL-TRPHRSDPGLAERWDLVAWGVELGTAYSELTDPveqrRRLTEQSLlAA 1038
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 16758642 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 ... |
50-188 |
1.81e-11 |
|
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: 61.77 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 50 DLTVQKADEVV----WVrarvHTSRAKGKQCFLVLRQQQFNVQALVavgDHASKQMVKFAANINKESIIDVEGIVRK--- 122
Cdd:cd04317 7 ELRESHVGQEVtlcgWV----QRRRDHGGLIFIDLRDRYGIVQVVF---DPEEAPEFELAEKLRNESVIQVTGKVRArpe 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758642 123 --VNQKIGSctqQDVELHVQKIYVISLAEPrLPLQLDDAIrpevegeedgraTVNQDTRLDNRIIDLR 188
Cdd:cd04317 80 gtVNPKLPT---GEIEVVASELEVLNKAKT-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 |
3.27e-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: 57.32 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 49 KDLTVQKADEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQaLVAVGDHASKQMVKFAANINKESIIDVEGIVRKVNQKIG 128
Cdd:cd04316 4 AEITPELDGEEVTVAGWVHEIRDLGGIKFVILRDREGIVQ-VTAPKKKVDKELFKTVRKLSRESVISVTGTVKAEPKAPN 82
|
90 100
....*....|....*....|....*.
gi 16758642 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 |
1.96e-08 |
|
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: 54.43 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 206 FRETLINKGFVEIQTPKIISAASEGGAN------VFTVSYFKSNAYLAQSPQLYKQM----CICADFEKVFCIGPVFRAE 275
Cdd:cd00768 9 LRRFMAELGFQEVETPIVEREPLLEKAGhepkdlLPVGAENEEDLYLRPTLEPGLVRlfvsHIRKLPLRLAEIGPAFRNE 88
|
90 100 110
....*....|....*....|....*....|....*....
gi 16758642 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 |
5.52e-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: 47.23 E-value: 5.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 60 VWVRARVHT-SRAKGKQCFLVLRQQQFNVQALVAvgdhaSKQMVKFAANINKESIIDVEGIVRKVNQKigsctqqDVELH 138
Cdd:pfam01336 1 VTVAGRVTSiRRSGGKLLFLTLRDGTGSIQVVVF-----KEEAEKLAKKLKEGDVVRVTGKVKKRKGG-------ELELV 68
|
....*..
gi 16758642 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 |
1.49e-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: 43.67 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 60 VWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAvgDHASKQMVKFAANINKESIIDVEGIVRKVNQKIGSctqqdVELHV 139
Cdd:cd04319 2 VTLAGWVYRKREVGKKAFIVLRDSTGIVQAVFS--KDLNEEAYREAKKVGIESSVIVEGAVKADPRAPGG-----AEVHG 74
|
90
....*....|.
gi 16758642 140 QKIYVISLAEP 150
Cdd:cd04319 75 EKLEIIQNVEF 85
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
60-146 |
6.59e-03 |
|
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: 35.67 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758642 60 VWVRARVHTSRAKGKQCFLVLRQQQFNVQAlVAVGDHASKQMVkfAANINKESIIDVEGIVRKVNQkiGSCTQQDVELHV 139
Cdd:cd04323 2 VKVFGWVHRLRSQKKLMFLVLRDGTGFLQC-VLSKKLVTEFYD--AKSLTQESSVEVTGEVKEDPR--AKQAPGGYELQV 76
|
....*..
gi 16758642 140 QKIYVIS 146
Cdd:cd04323 77 DYLEIIG 83
|
|
| |
