|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
3-501 |
0e+00 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 722.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 3 SASASRKSQEKPREI--------MDAAEDYAKERYGISSMIQSQEKPD-RVLVRVRDLTIQKADEVVWVRARVHTSRAKG 73
Cdd:PLN02850 18 AKKAAAKAEKLRREAtakaaaasLEDEDDPLASNYGDVPLEELQSKVTgREWTDVSDLGEELAGSEVLIRGRVHTIRGKG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 74 KQCFLVLRQQQFNVQALVAVGD-HASKQMVKFAANINKESIVDVEGVVRKVNQKIGSCTQQdVELHVQKIYVISLAEPRL 152
Cdd:PLN02850 98 KSAFLVLRQSGFTVQCVVFVSEvTVSKGMVKYAKQLSRESVVDVEGVVSVPKKPVKGTTQQ-VEIQVRKIYCVSKALATL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 153 PLQLDDA-----VRPEAEGEEEGRATVNQDTRLDNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAA 227
Cdd:PLN02850 177 PFNVEDAarsesEIEKALQTGEQLVRVGQDTRLNNRVLDLRTPANQAIFRIQSQVCNLFREFLLSKGFVEIHTPKLIAGA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 228 SEGGANVFTVSYFKNNAYLAQSPQLYKQMCICADFEKVFSIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVMEEIA 307
Cdd:PLN02850 257 SEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGDFRRVFEIGPVFRAEDSFTHRHLCEFTGLDLEMEIKEHYSEVLDVVD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 308 DTMVQIFKGLQERFQTEIQTVNKQFPCEPFKFLEPTLRLEYCEALAMLREAGVEMGDEDDLSTPNEKLLGHLVKEKYDTD 387
Cdd:PLN02850 337 ELFVAIFDGLNERCKKELEAIREQYPFEPLKYLPKTLRLTFAEGIQMLKEAGVEVDPLGDLNTESERKLGQLVKEKYGTD 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 388 FYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHA 467
Cdd:PLN02850 417 FYILHRYPLAVRPFYTMPCPDDPKYSNSFDVFIRGEEIISGAQRVHDPELLEKRAEECGIDVKTISTYIDSFRYGAPPHG 496
|
490 500 510
....*....|....*....|....*....|....
gi 45439306 468 GGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 501
Cdd:PLN02850 497 GFGVGLERVVMLFCGLNNIRKTSLFPRDPQRLAP 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: 524.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 6 ASRKSQEKPREIMDAA--EDYaKERYGISSMIQSQEKPDRVLVRVRDLTIQK-ADEVVWVRARVHTSRAKGKQCFLVLRQ 82
Cdd:PTZ00401 25 AARLAEEKARAAEKAAlvEKY-KDVFGAAPMVQSTTYKSRTFIPVAVLSKPElVDKTVLIRARVSTTRKKGKMAFMVLRD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 83 QQFNVQALVAVGDHASKQMVKFAANINKESIVDVEGVVRKVNQKIGSCTQQDVELHVQKIYVISLAEPRLPLQLDDAvrp 162
Cdd:PTZ00401 104 GSDSVQAMAAVEGDVPKEMIDFIGQIPTESIVDVEATVCKVEQPITSTSHSDIELKVKKIHTVTESLRTLPFTLEDA--- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 163 eAEGEEEGRATVNQDTRLDNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKN 242
Cdd:PTZ00401 181 -SRKESDEGAKVNFDTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDSDFCEIHSPKIINAPSEGGANVFKLEYFNR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 243 NAYLAQSPQLYKQMCICADFEKVFSIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVMeeiaDTMVQIFKGLQERFQ 322
Cdd:PTZ00401 260 FAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHLTEFVGLDVEMRINEHYYEVL----DLAESLFNYIFERLA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 323 T---EIQTVNKQFPCEPFKF------------------LEPT--------------LRLEYCEALAMLREAGVE-MGDED 366
Cdd:PTZ00401 336 ThtkELKAVCQQYPFEPLVWkltpermkelgvgvisegVEPTdkyqarvhnmdsrmLRINYMHCIELLNTVLEEkMAPTD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 367 DLSTPNEKLLGHLVKEKYDTDFYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHHG 446
Cdd:PTZ00401 416 DINTTNEKLLGKLVKERYGTDFFISDRFPSSARPFYTMECKDDERFTNSYDMFIRGEEISSGAQRIHDPDLLLARAKMLN 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 45439306 447 IDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 501
Cdd:PTZ00401 496 VDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPRDPQRTTP 550
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
174-497 |
8.80e-175 |
|
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: 494.01 E-value: 8.80e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 174 VNQDTRLDNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLY 253
Cdd:cd00776 2 ANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 254 KQMCICAdFEKVFSIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVMEEIADTMVQIFKGLQERFQTEIQTVNkQFP 333
Cdd:cd00776 82 KEMLIAA-LERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRVLERCAKELELVN-QLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 334 CEPFKFLEPTLRLEYCEALAMLREAGV--EMGDEDDLSTPNEKLLGhlvkEKYDTDFYILDKYPLAVRPFYTMPDPRNPK 411
Cdd:cd00776 160 RELLKPLEPFPRITYDEAIELLREKGVeeEVKWGEDLSTEHERLLG----EIVKGDPVFVTDYPKEIKPFYMKPDDDNPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 412 QSNSYDMFMRG-EEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTS 490
Cdd:cd00776 236 TVESFDLLMPGvGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAI 315
|
....*..
gi 45439306 491 MFPRDPK 497
Cdd:cd00776 316 LFPRDPK 322
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
46-501 |
1.20e-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: 477.78 E-value: 1.20e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 46 VRVRDLTIQKADEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQaLVAVGDHASKQMVKFAANINKESIVDVEGVVrkvnq 125
Cdd:TIGR00458 1 VYSADIKPEMDGQEVTFMGWVHEIRDLGGLIFVLLRDREGLIQ-ITAPAKKVSKNLFKWAKKLNLESVVAVRGIV----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 126 KIGSCTQQDVELHVQKIYVISLAEPRLPLQLDDAVRPEAegeeegratvnqDTRLDNRVIDLRTSTSQAVFRLQSGICHL 205
Cdd:TIGR00458 75 KIKEKAPGGFEIIPTKIEVINEAKEPLPLDPTEKVPAEL------------DTRLDYRFLDLRRPTVQAIFRIRSGVLES 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 206 FRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLYKQMCICADFEKVFSIGPVFRAEDSNTHRHLTE 285
Cdd:TIGR00458 143 VREFLAEEGFIEVHTPKLVASATEGGTELFPITYFEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHRHLNE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 286 FVGLDIEMAFNYHyHEVMEEIADTMVQIFKGLQERFQTEIQTVNKQFPCEPFKFleptLRLEYCEALAMLREAGVEMGDE 365
Cdd:TIGR00458 223 ATSIDIEMAFEDH-HDVMDILEELVVRVFEDVPERCAHQLETLEFKLEKPEGKF----VRLTYDEAIEMANAKGVEIGWG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 366 DDLSTPNEKLLGhlvkEKYDTDFYILDkYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHH 445
Cdd:TIGR00458 298 EDLSTEAEKALG----EEMDGLYFITD-WPTEIRPFYTMPDEDNPEISKSFDLMYRDLEISSGAQRIHLHDLLVERIKAK 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 45439306 446 GIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 501
Cdd:TIGR00458 373 GLNPEGFKDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRKRLTP 428
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
48-501 |
3.44e-160 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 461.58 E-value: 3.44e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 48 VRDLTIQKADEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDhaSKQMVKFAANINKESIVDVEGVVRKVNQKI 127
Cdd:PRK05159 7 TSELTPELDGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKV--DEELFETIKKLKRESVVSVTGTVKANPKAP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 128 GSctqqdVELHVQKIYVISLAEPRLPLQLDDAVRPEAegeeegratvnqDTRLDNRVIDLRTSTSQAVFRLQSGICHLFR 207
Cdd:PRK05159 85 GG-----VEVIPEEIEVLNKAEEPLPLDISGKVLAEL------------DTRLDNRFLDLRRPRVRAIFKIRSEVLRAFR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 208 ETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLYKQMCICADFEKVFSIGPVFRAEDSNTHRHLTEFV 287
Cdd:PRK05159 148 EFLYENGFTEIFTPKIVASGTEGGAELFPIDYFEKEAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRHLNEYT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 288 GLDIEMAFNYHYHEVMEEIADTMVQIFKGLQERFQTEIQTVNKQFPCEPfkflEPTLRLEYCEALAMLREAGVEMGDEDD 367
Cdd:PRK05159 228 SIDVEMGFIDDHEDVMDLLENLLRYMYEDVAENCEKELELLGIELPVPE----TPIPRITYDEAIEILKSKGNEISWGDD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 368 LSTPNEKLLGHLVKEKYDTDFYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGI 447
Cdd:PRK05159 304 LDTEGERLLGEYVKEEYGSDFYFITDYPSEKRPFYTMPDEDDPEISKSFDLLFRGLEITSGGQRIHRYDMLVESIKEKGL 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 45439306 448 DLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 501
Cdd:PRK05159 384 NPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPRDRHRLTP 437
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
46-501 |
1.44e-158 |
|
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: 457.21 E-value: 1.44e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 46 VRVRDLTIQKADEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMVKfaaNINKESIVDVEGVVRKVNQ 125
Cdd:COG0017 3 TYIKDLLPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKLENFEEAK---KLTTESSVEVTGTVVESPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 126 KigsctQQDVELHVQKIYVISLAEPRLPLQLDDAvrpeaegeeegratvNQDTRLDNRVIDLRTSTSQAVFRLQSGICHL 205
Cdd:COG0017 80 A-----PQGVELQAEEIEVLGEADEPYPLQPKRH---------------SLEFLLDNRHLRLRTNRFGAIFRIRSELARA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 206 FRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLYKQMCICAdFEKVFSIGPVFRAEDSNTHRHLTE 285
Cdd:COG0017 140 IREFFQERGFVEVHTPIITASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMA-LEKVYTFGPTFRAEKSNTRRHLAE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 286 FVGLDIEMAFnYHYHEVMEEIADTMVQIFKGLQERFQTEIQTVN------KQFPCEPFKfleptlRLEYCEALAMLREAG 359
Cdd:COG0017 219 FWMIEPEMAF-ADLEDVMDLAEEMLKYIIKYVLENCPEELEFLGrdverlEKVPESPFP------RITYTEAIEILKKSG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 360 VEMGDEDDLSTPNEKLLGhlvkEKYDTDFYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRG-EEILSGAQRIHDPQLL 438
Cdd:COG0017 292 EKVEWGDDLGTEHERYLG----EEFFKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGiGEIIGGSQREHRYDVL 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45439306 439 TERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 501
Cdd:COG0017 368 VERIKEKGLDPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
175-496 |
1.03e-101 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 307.96 E-value: 1.03e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 175 NQDTRLDNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNN--AYLAQSPQL 252
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGkfYALPQSPQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 253 YKQMCICADFEKVFSIGPVFRAEDSNTHRHLtEFVGLDIEMAFNyHYHEVMEEIADTMVQIFKGLQERFQTEIQTVNKQF 332
Cdd:pfam00152 81 YKQLLMVAGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFV-DYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 333 PcEPFKfleptlRLEYCEALAMLREAGVEMGDEDdLSTPNEKLLGHLVKEKYDTDFYILDKYPLAVRPFYTMPDPRNPKQ 412
Cdd:pfam00152 159 K-KPFP------RITYAEAIEKLNGKDVEELGYG-SDKPDLRFLLELVIDKNKFNPLWVTDFPAEHHPFTMPKDEDDPAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 413 SNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGIDLEKIKA----YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQ 488
Cdd:pfam00152 231 AEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPEEAEEkfgfYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIRE 310
|
....*...
gi 45439306 489 TSMFPRDP 496
Cdd:pfam00152 311 VIAFPKTR 318
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
46-501 |
3.06e-80 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 256.96 E-value: 3.06e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 46 VRVRDLTIQK-ADEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQmvKFAANINKESIVDVEGVVRKVN 124
Cdd:PRK03932 4 VSIKDILKGKyVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDNGEEYF--EEIKKLTTGSSVIVTGTVVESP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 125 QKigsctQQDVELHVQKIYVISLAEPRLPLQLDDAvrpeaegeeegratvNQDTRLDNRVIDLRTSTSQAVFRLQSGICH 204
Cdd:PRK03932 82 RA-----GQGYELQATKIEVIGEDPEDYPIQKKRH---------------SIEFLREIAHLRPRTNKFGAVMRIRNTLAQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 205 LFRETLINKGFVEIQTPKIISAASEGGANVFTVS---------YFKNNAYLAQSPQLYKQMCICAdFEKVFSIGPVFRAE 275
Cdd:PRK03932 142 AIHEFFNENGFVWVDTPIITASDCEGAGELFRVTtldldfskdFFGKEAYLTVSGQLYAEAYAMA-LGKVYTFGPTFRAE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 276 DSNTHRHLTEFVGLDIEMAFnYHYHEVMEeIADTMVQ-IFKGLQERFQTEIQTVNKQFPCEPFKFLEPTL-----RLEYC 349
Cdd:PRK03932 221 NSNTRRHLAEFWMIEPEMAF-ADLEDNMD-LAEEMLKyVVKYVLENCPDDLEFLNRRVDKGDIERLENFIespfpRITYT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 350 EALAMLREAG------VEMGDedDLSTPNEKLLghlVKEKYDTDFYILDkYPLAVRPFYTMPDPRNpKQSNSYDMFMRG- 422
Cdd:PRK03932 299 EAIEILQKSGkkfefpVEWGD--DLGSEHERYL---AEEHFKKPVFVTN-YPKDIKAFYMRLNPDG-KTVAAMDLLAPGi 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45439306 423 EEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 501
Cdd:PRK03932 372 GEIIGGSQREERLDVLEARIKELGLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
54-501 |
2.13e-74 |
|
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: 241.90 E-value: 2.13e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 54 QKADEVVWVRARVHTSRAKGKQCFLVLRQQQF--NVQALVAVGDhaSKQMVKFAANINKESIVDVEGVVRKVNQKigsct 131
Cdd:TIGR00457 13 KFVGDEVTVSGWVRTKRSSKKIIFLELNDGSSlgPIQAVINGED--NPYLFQLLKSLTTGSSVSVTGKVVESPGK----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 132 QQDVELHVQKIYVISLAEPR-LPLQLDDavrpeaegeeegratvnQDTRL--DNRVIDLRTSTSQAVFRLQSGICHLFRE 208
Cdd:TIGR00457 86 GQPVELQVKKIEVVGEAEPDdYPLQKKE-----------------HSLEFlrDIAHLRLRTNTLGAVMRVRNALSQAIHR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 209 TLINKGFVEIQTPKIISAASEGGANVFTVS---------YFKNNAYLAQSPQLYKQMCICAdFEKVFSIGPVFRAEDSNT 279
Cdd:TIGR00457 149 YFQENGFTWVSPPILTSNDCEGAGELFRVStgnidfsqdFFGKEAYLTVSGQLYLETYALA-LSKVYTFGPTFRAEKSNT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 280 HRHLTEFVGLDIEMAFnYHYHEVMEEIADTMVQIFKGLQERFQTEIQTVNKQFPCEPFKFLEPTL-----RLEYCEALAM 354
Cdd:TIGR00457 228 SRHLSEFWMIEPEMAF-ANLNDLLQLAETLIKYIIKAVLENCSQELKFLEKNFDKDLIKRLENIInnkfaRITYTDAIEI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 355 LREAGVEMGDED----DLSTPNEKLLGhlvkEKYDTDFYILDKYPLAVRPFYtMPDPRNPKQSNSYDMFMRG-EEILSGA 429
Cdd:TIGR00457 307 LKESDKNFEYEDfwgdDLQTEHERFLA----EEYFKPPVFVTNYPKDIKAFY-MKLNDDGKTVAAMDLLAPGiGEIIGGS 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45439306 430 QRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 501
Cdd:TIGR00457 382 EREDDLDKLENRMKEMGLDTDALNWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 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 |
1.94e-58 |
|
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of class II aminoacyl-tRNA synthetases of the subgroup containing aspartyl, lysyl, and asparaginyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. Nearly all class II tRNA synthetases are dimers and enzymes in this subgroup are homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238358 [Multi-domain] Cd Length: 269 Bit Score: 194.23 E-value: 1.94e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 196 FRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFK--NNAYLAQSPQLYKQMCICADFEKVFSIGPVFR 273
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNAlgLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 274 AEDSNThRHLTEFVGLDIEMAFNyHYHEVMEEIADTMVQIFKGLQErfqteiqTVNKQFPCEPFKFLEPTLRLEYCEALA 353
Cdd:cd00669 81 NEDLRA-RHQPEFTMMDLEMAFA-DYEDVIELTERLVRHLAREVLG-------VTAVTYGFELEDFGLPFPRLTYREALE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 354 MLREagvemgdeddlstpnekllghlvkekydtdFYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIH 433
Cdd:cd00669 152 RYGQ------------------------------PLFLTDYPAEMHSPLASPHDVNPEIADAFDLFINGVEVGNGSSRLH 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45439306 434 DPQLLTERALHHGID----LEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRD 495
Cdd:cd00669 202 DPDIQAEVFQEQGINkeagMEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKM 267
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
60-158 |
2.38e-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: 167.36 E-value: 2.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 60 VWVRARVHTSRAKG-KQCFLVLRQQQFNVQALVAVGDHA-SKQMVKFAANINKESIVDVEGVVRKVNQKIGSCTQQDVEL 137
Cdd:cd04320 2 VLIRARVHTSRAQGaKLAFLVLRQQGYTIQGVLAASAEGvSKQMVKWAGSLSKESIVDVEGTVKKPEEPIKSCTQQDVEL 81
|
90 100
....*....|....*....|.
gi 45439306 138 HVQKIYVISLAEPRLPLQLDD 158
Cdd:cd04320 82 HIEKIYVVSEAAEPLPFQLED 102
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
176-496 |
6.08e-50 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 174.05 E-value: 6.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 176 QDTRLDNRVIdLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPkIISA--------ASEGGANVFTVSYFKNNAYLA 247
Cdd:PRK06462 11 EEFLRMSWKH-ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPP-IISPstdplmglGSDLPVKQISIDFYGVEYYLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 248 QSPQLYKQMCIcADFEKVFSIGPVFRAE--DSNTHRHLTEFVGLDIEMAfNYHYHEVMEEIADTMVQIFKGLQERFQTEI 325
Cdd:PRK06462 89 DSMILHKQLAL-RMLGKIFYLSPNFRLEpvDKDTGRHLYEFTQLDIEIE-GADLDEVMDLIEDLIKYLVKELLEEHEDEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 326 QTVNKQFPcepfKFLEPTLRLEYCEALAMLREAGVEMGDEDDLSTPNEKLLghlvKEKYDTDFYILDkYPLAVRPFYTMP 405
Cdd:PRK06462 167 EFFGRDLP----HLKRPFKRITHKEAVEILNEEGCRGIDLEELGSEGEKSL----SEHFEEPFWIID-IPKGSREFYDRE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 406 DPRNPKQSNSYDMFMR---GEeILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLG 482
Cdd:PRK06462 238 DPERPGVLRNYDLLLPegyGE-AVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICG 316
|
330
....*....|....
gi 45439306 483 LHNVRQTSMFPRDP 496
Cdd:PRK06462 317 LRHIREVQPFPRVP 330
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
50-493 |
8.29e-44 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 162.93 E-value: 8.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 50 DLTIQKADEVV----WVrarvHTSRAKGKQCFLVLRQQQFNVQALVavgdHASKQMVKFAANINKESIVDVEGVVRK--- 122
Cdd:PRK00476 10 ELRESHVGQTVtlcgWV----HRRRDHGGLIFIDLRDREGIVQVVF----DPDAEAFEVAESLRSEYVIQVTGTVRArpe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 123 --VNQKIGSctqQDVELHVQKIYVISLAEPrLPLQLDDavrpeaegeeegRATVNQDTRLDNRVIDLRTSTSQAVFRLQS 200
Cdd:PRK00476 82 gtVNPNLPT---GEIEVLASELEVLNKSKT-LPFPIDD------------EEDVSEELRLKYRYLDLRRPEMQKNLKLRS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 201 GICHLFRETLINKGFVEIQTPkIISAASEGGANVFTV-S-YFKNNAY-LAQSPQLYKQMCICADFEKVFSIGPVFRAEDS 277
Cdd:PRK00476 146 KVTSAIRNFLDDNGFLEIETP-ILTKSTPEGARDYLVpSrVHPGKFYaLPQSPQLFKQLLMVAGFDRYYQIARCFRDEDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 278 NTHRhLTEFVGLDIEMAFnYHYHEVMEEIADTMVQIFKGL--------------QE------------RFQTEIQTVNKQ 331
Cdd:PRK00476 225 RADR-QPEFTQIDIEMSF-VTQEDVMALMEGLIRHVFKEVlgvdlptpfprmtyAEamrrygsdkpdlRFGLELVDVTDL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 332 FPCEPFK-FLEPT--------LRLEYC--------------------------------------------EALAMLREA 358
Cdd:PRK00476 303 FKDSGFKvFAGAAndggrvkaIRVPGGaaqlsrkqideltefakiygakglayikvnedglkgpiakflseEELAALLER 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 359 -GVEMGD-----EDDLSTPNE----------KLLGHLVKEKYD----TDFyildkyPL------AVR------PFyTMPD 406
Cdd:PRK00476 383 tGAKDGDliffgADKAKVVNDalgalrlklgKELGLIDEDKFAflwvVDF------PMfeydeeEGRwvaahhPF-TMPK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 407 P--------RNPKQ--SNSYDMFMRGEEILSGAQRIHDPQLLtERALHH-GIDLEKIKA----YIDSFRFGAPPHAGGGI 471
Cdd:PRK00476 456 DedldeletTDPGKarAYAYDLVLNGYELGGGSIRIHRPEIQ-EKVFEIlGISEEEAEEkfgfLLDALKYGAPPHGGIAF 534
|
570 580
....*....|....*....|..
gi 45439306 472 GLERVTMLFLGLHNVRQTSMFP 493
Cdd:PRK00476 535 GLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
50-493 |
5.33e-41 |
|
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: 155.16 E-value: 5.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 50 DLTIQKADEVV----WVrarvHTSRAKGKQCFLVLR------QqqfnvqalVAVGDHASKQMVKFAANINKESIVDVEGV 119
Cdd:COG0173 9 ELRESDVGQEVtlsgWV----HRRRDHGGLIFIDLRdrygitQ--------VVFDPDDSAEAFEKAEKLRSEYVIAVTGK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 120 VRK-----VNQKI--GsctqqDVELHVQKIYVISLAEPrLPLQLDDAVRpeaegeeegratVNQDTRLDNRVIDLRTSTS 192
Cdd:COG0173 77 VRArpegtVNPKLptG-----EIEVLASELEILNKAKT-PPFQIDDDTD------------VSEELRLKYRYLDLRRPEM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 193 QAVFRLQSGICHLFRETLINKGFVEIQTPkIISAASEGGANVFTV-------SYFknnAyLAQSPQLYKQMCICADFEKV 265
Cdd:COG0173 139 QKNLILRHKVTKAIRNYLDENGFLEIETP-ILTKSTPEGARDYLVpsrvhpgKFY---A-LPQSPQLFKQLLMVSGFDRY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 266 FSIGPVFRAEDSNTHRHLtEFVGLDIEMAF---NyhyhEVMEEIADTMVQIFKGL--------------QE--------- 319
Cdd:COG0173 214 FQIARCFRDEDLRADRQP-EFTQLDIEMSFvdqE----DVFELMEGLIRHLFKEVlgvelptpfprmtyAEamerygsdk 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 320 ---RFQTEIQTVNKQFPCEPFK-FLEPT--------LRLEYC-------------------------------------- 349
Cdd:COG0173 289 pdlRFGLELVDVTDIFKDSGFKvFAGAAenggrvkaINVPGGaslsrkqideltefakqygakglayikvnedglkspia 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 350 -----EALAMLREA-GVEMGD-----EDDLSTPNE----------KLLGHLVKEKYD----TDFyildkyPL-------- 396
Cdd:COG0173 369 kflseEELAAILERlGAKPGDliffvADKPKVVNKalgalrlklgKELGLIDEDEFAflwvVDF------PLfeydeeeg 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 397 ---AVR-PFyTMPDP-------RNPKQ--SNSYDMFMRGEEILSGAQRIHDPQLLtERALHH-GIDLEKIKA----YIDS 458
Cdd:COG0173 443 rwvAMHhPF-TMPKDedldlleTDPGKvrAKAYDLVLNGYELGGGSIRIHDPELQ-EKVFELlGISEEEAEEkfgfLLEA 520
|
570 580 590
....*....|....*....|....*....|....*
gi 45439306 459 FRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 493
Cdd:COG0173 521 FKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
196-493 |
9.57e-41 |
|
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: 147.72 E-value: 9.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 196 FRLQSGICHLFRETLINKGFVEIQTPkIISAASEGGANVFTVSY--FKNNAY-LAQSPQLYKQMCICADFEKVFSIGPVF 272
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETP-ILTKSTPEGARDFLVPSrlHPGKFYaLPQSPQLFKQLLMVSGFDRYFQIARCF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 273 RAEDSNTHRHlTEFVGLDIEMAFnYHYHEVMEEIADTMVQIFKglqERFQTEIQTvnkqfpcePFKfleptlRLEYCEAL 352
Cdd:cd00777 80 RDEDLRADRQ-PEFTQIDIEMSF-VDQEDIMSLIEGLLKYVFK---EVLGVELTT--------PFP------RMTYAEAM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 353 amlreagvemgdeddlstpnekllghlvkEKYDTDF-YILD-----------KYPLAVRPFyTMPDP-------RNPKQ- 412
Cdd:cd00777 141 -----------------------------ERYGFKFlWIVDfplfewdeeegRLVSAHHPF-TAPKEedldlleKDPEDa 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 413 -SNSYDMFMRGEEILSGAQRIHDPQlLTERALHH-GIDLEKIKA----YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNV 486
Cdd:cd00777 191 rAQAYDLVLNGVELGGGSIRIHDPD-IQEKVFEIlGLSEEEAEEkfgfLLEAFKYGAPPHGGIALGLDRLVMLLTGSESI 269
|
....*..
gi 45439306 487 RQTSMFP 493
Cdd:cd00777 270 RDVIAFP 276
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
2-493 |
3.42e-33 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 133.62 E-value: 3.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 2 PSASASRKSQEKPREIMDAAEDYAKERyGISSMIQSQEKPDRVLVRVRDltiqkADEVVWVRARVHTSRAKGKQCFLVLR 81
Cdd:PTZ00385 58 ATKTVTQEASRAPRSKLDLPAAYSSFR-GITPISEVRERYGYLASGDRA-----AQATVRVAGRVTSVRDIGKIIFVTIR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 82 QQQFNVQALVAVGDHASKQMVK-FAANINKESIVDVEGVvrkvnqkigSCTQQDVELHVQKIYVISLAeprlPLQLDDAV 160
Cdd:PTZ00385 132 SNGNELQVVGQVGEHFTREDLKkLKVSLRVGDIIGADGV---------PCRMQRGELSVAASRMLILS----PYVCTDQV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 161 RPEAEGEEEGRAtvNQDTRLDNRVIDLRTSTSQ-AVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSY 239
Cdd:PTZ00385 199 VCPNLRGFTVLQ--DNDVKYRYRFTDMMTNPCViETIKKRHVMLQALRDYFNERNFVEVETPVLHTVASGANAKSFVTHH 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 240 FKNNA--YLAQSPQLYKQMCICADFEKVFSIGPVFRAEDSNtHRHLTEFVGLDIEMAfnYH-YHEVMEEIADTMVQIFKG 316
Cdd:PTZ00385 277 NANAMdlFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDAD-RSHNPEFTSCEFYAA--YHtYEDLMPMTEDIFRQLAMR 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 317 LQERFQTEIQTVNKQFPCEPFKFLEPTLRLEYCEALAmlREAGVEMGDEDDLSTPNEKLLGHLVKEKYDT---------- 386
Cdd:PTZ00385 354 VNGTTVVQIYPENAHGNPVTVDLGKPFRRVSVYDEIQ--RMSGVEFPPPNELNTPKGIAYMSVVMLRYNIplppvrtaak 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 387 ------DFYILDKyplAVRPFYTMPDP-----------RNPKQSNSYDMFMRGEEILSGAQRIHDP--------QLLTER 441
Cdd:PTZ00385 432 mfekliDFFITDR---VVEPTFVMDHPlfmsplakeqvSRPGLAERFELFVNGIEYCNAYSELNDPheqyhrfqQQLVDR 508
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 45439306 442 alhHGIDLEKI---KAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 493
Cdd:PTZ00385 509 ---QGGDEEAMpldETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFP 560
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
114-496 |
3.09e-29 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 121.23 E-value: 3.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 114 VDVEGVVRKvnqkiGSCTQQDVELHVQKIYVISLAEPRLPLQlddavrpeaegeeegRATVNQDTRLDNRVIDLRTSTSQ 193
Cdd:PLN02603 164 VLVQGTVVS-----SQGGKQKVELKVSKIVVVGKSDPSYPIQ---------------KKRVSREFLRTKAHLRPRTNTFG 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 194 AVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVS------------------------------YFKNN 243
Cdd:PLN02603 224 AVARVRNALAYATHKFFQENGFVWVSSPIITASDCEGAGEQFCVTtlipnsaenggslvddipktkdglidwsqdFFGKP 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 244 AYLAQSPQLYKQMCICAdFEKVFSIGPVFRAEDSNTHRHLTEFVGLDIEMAF--------------NYHYHEVMEEIADT 309
Cdd:PLN02603 304 AFLTVSGQLNGETYATA-LSDVYTFGPTFRAENSNTSRHLAEFWMIEPELAFadlnddmacataylQYVVKYILENCKED 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 310 M----VQIFKGLQERFQteiQTVNKQFpcepfkfleptLRLEYCEALAMLREAG------VEMGDedDLSTPNEKllgHL 379
Cdd:PLN02603 383 MeffnTWIEKGIIDRLS---DVVEKNF-----------VQLSYTDAIELLLKAKkkfefpVKWGL--DLQSEHER---YI 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 380 VKEKYDTDFYILDKYPLAVRPFYtMPDPRNPKQSNSYDMFM-RGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDS 458
Cdd:PLN02603 444 TEEAFGGRPVIIRDYPKEIKAFY-MRENDDGKTVAAMDMLVpRVGELIGGSQREERLEYLEARLDELKLNKESYWWYLDL 522
|
410 420 430
....*....|....*....|....*....|....*...
gi 45439306 459 FRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDP 496
Cdd:PLN02603 523 RRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPRVP 560
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
61-501 |
1.06e-27 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 117.01 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 61 WVRArvhtSRAKGKQCFLVLRQQQFNVQALVAvGDHASKQMVKFAANINKESIVDVEGVVRKVNQKIGS--CTQQDVELH 138
Cdd:PRK12820 26 WVDA----FRDHGELLFIHLRDRNGFIQAVFS-PEAAPADVYELAASLRAEFCVALQGEVQKRLEETENphIETGDIEVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 139 VQKIYVISLAEPrLPLQLDDAVRPEAEGEEEGRAtVNQDTRLDNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEI 218
Cdd:PRK12820 101 VRELSILAASEA-LPFAISDKAMTAGAGSAGADA-VNEDLRLQYRYLDIRRPAMQDHLAKRHRIIKCARDFLDSRGFLEI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 219 QTPKIISAASEGGANVFTVSYFKNNAY--LAQSPQLYKQMCICADFEKVFSIGPVFRAEDSNTHRHlTEFVGLDIEMAF- 295
Cdd:PRK12820 179 ETPILTKSTPEGARDYLVPSRIHPKEFyaLPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQ-PEFTQLDIEASFi 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 296 -----------------------------NYHYHEVME----------------EIAD----TMVQIFKGLQERfQTEIQ 326
Cdd:PRK12820 258 deefifelieeltarmfaiggialprpfpRMPYAEAMDttgsdrpdlrfdlkfaDATDifenTRYGIFKQILQR-GGRIK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 327 TVNKQFPCEpfKFLEPTLRLEYCEALA----------MLREAG------VEMGDEDDLstpnEKLLGHLVKEKYDTDFYI 390
Cdd:PRK12820 337 GINIKGQSE--KLSKNVLQNEYAKEIApsfgakgmtwMRAEAGgldsniVQFFSADEK----EALKRRFHAEDGDVIIMI 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 391 LDK----------------------------YPLAVRPF-----------------YTMP-----DPRNPK-----QSNS 415
Cdd:PRK12820 411 ADAscaivlsalgqlrlhladrlglipegvfHPLWITDFplfeatddggvtsshhpFTAPdredfDPGDIEelldlRSRA 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 416 YDMFMRGEEILSGAQRIHDP--QLLTERALhhGIDLEKIKA----YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQT 489
Cdd:PRK12820 491 YDLVVNGEELGGGSIRINDKdiQLRIFAAL--GLSEEDIEDkfgfFLRAFDFAAPPHGGIALGLDRVVSMILQTPSIREV 568
|
570
....*....|..
gi 45439306 490 SMFPRDPKRLTP 501
Cdd:PRK12820 569 IAFPKNRSAACP 580
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
61-494 |
1.22e-27 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 116.81 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 61 WV-RARVHtsrakGKQCFLVLRQQQFNVQalVAVGDHASKQMVKFAANINKESIVDVEGVVRK-----VNQKIGSCTQQD 134
Cdd:PLN02903 80 WVdLHRDM-----GGLTFLDVRDHTGIVQ--VVTLPDEFPEAHRTANRLRNEYVVAVEGTVRSrpqesPNKKMKTGSVEV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 135 VELHVQKIYVISLAEPRLPLQLDDAvrpeaegeeegRATVNQDTRLDNRVIDLRTSTSQAVFRLQSGICHLFRETLINK- 213
Cdd:PLN02903 153 VAESVDILNVVTKSLPFLVTTADEQ-----------KDSIKEEVRLRYRVLDLRRPQMNANLRLRHRVVKLIRRYLEDVh 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 214 GFVEIQTPKIISAASEGGANVFTVSYFKNNAYLA--QSPQLYKQMCICADFEKVFSIGPVFRAEDSNTHRHlTEFVGLDI 291
Cdd:PLN02903 222 GFVEIETPILSRSTPEGARDYLVPSRVQPGTFYAlpQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQ-PEFTQLDM 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 292 EMAFNyHYHEVMEEIADTMVQIFK---GLQ-----------------------ERFQTEIQTVNKQFPCEPFKFLE---- 341
Cdd:PLN02903 301 ELAFT-PLEDMLKLNEDLIRQVFKeikGVQlpnpfprltyaeamskygsdkpdLRYGLELVDVSDVFAESSFKVFAgale 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 342 ---------------------------------------PTLR------LEYCEAL----------AMLREAGVEMGD-- 364
Cdd:PLN02903 380 sggvvkaicvpdgkkisnntalkkgdiyneaiksgakglAFLKvlddgeLEGIKALveslspeqaeQLLAACGAGPGDli 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 365 ---EDDLSTPNEKL--LGHLVKEKYD------------TDFYILDKYPLAVR------PFyTMPDPRNPKQSNS-----Y 416
Cdd:PLN02903 460 lfaAGPTSSVNKTLdrLRQFIAKTLDlidpsrhsilwvTDFPMFEWNEDEQRlealhhPF-TAPNPEDMGDLSSaralaY 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 417 DMFMRGEEILSGAQRIH--DPQLLTERALhhGIDLE----KIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTS 490
Cdd:PLN02903 539 DMVYNGVEIGGGSLRIYrrDVQQKVLEAI--GLSPEeaesKFGYLLEALDMGAPPHGGIAYGLDRLVMLLAGAKSIRDVI 616
|
....
gi 45439306 491 MFPR 494
Cdd:PLN02903 617 AFPK 620
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
33-498 |
1.43e-24 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 107.00 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 33 SMIQSQEKPDRVLVRV----RDLTIQKADEVVWVRARVHTSRAKGKQCFLVLRQQQ----FNVQALVAVGDHASKQMVKF 104
Cdd:PLN02221 22 STVQKAQFSDRVLIRSildrPDGGAGLAGQKVRIGGWVKTGREQGKGTFAFLEVNDgscpANLQVMVDSSLYDLSTLVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 105 AaninkeSIVDVEGVVrKVNQKiGSCTQQDVELHVQKIYVISLAEP-RLPLQlddavrpeaegeeegRATVNQDTRLDNR 183
Cdd:PLN02221 102 G------TCVTVDGVL-KVPPE-GKGTKQKIELSVEKVIDVGTVDPtKYPLP---------------KTKLTLEFLRDVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 184 VIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVS------------------------- 238
Cdd:PLN02221 159 HLRSRTNSISAVARIRNALAFATHSFFQEHSFLYIHTPIITTSDCEGAGEMFQVTtlinyterleqdlidnpppteadve 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 239 -----------------------------------------------------------------YFKNNAYLAQSPQLY 253
Cdd:PLN02221 239 aarlivkergevvaqlkaakaskeeitaavaelkiakeslahieersklkpglpkkdgkidyskdFFGRQAFLTVSGQLQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 254 KQMCICAdFEKVFSIGPVFRAEDSNTHRHLTEFVGLDIEMAFNyHYHEVMEeIADTMVQ-IFKGLQERFQTEIQTVNKQF 332
Cdd:PLN02221 319 VETYACA-LSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFA-DLEDDMN-CAEAYVKyMCKWLLDKCFDDMELMAKNF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 333 PCEPFKFLE-----PTLRLEYCEALAMLREAgVEMGDE--------DDLSTPNEKLLGHLVKEKYdtdfYILDKYPLAVR 399
Cdd:PLN02221 396 DSGCIDRLRmvastPFGRITYTEAIELLEEA-VAKGKEfdnnvewgIDLASEHERYLTEVLFQKP----LIVYNYPKGIK 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 400 PFYtMPDPRNPKQSNSYDMFM-RGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTM 478
Cdd:PLN02221 471 AFY-MRLNDDEKTVAAMDVLVpKVGELIGGSQREERYDVIKQRIEEMGLPIEPYEWYLDLRRYGTVKHCGFGLGFERMIL 549
|
570 580
....*....|....*....|
gi 45439306 479 LFLGLHNVRQTSMFPRDPKR 498
Cdd:PLN02221 550 FATGIDNIRDVIPFPRYPGK 569
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
175-493 |
3.45e-23 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 102.45 E-value: 3.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 175 NQDTRLDNRVIDL-RTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSY--FKNNAYLAQSPQ 251
Cdd:PRK12445 162 DQEVRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHnaLDLDMYLRIAPE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 252 LYKQMCICADFEKVFSIGPVFRAEDSNThRHLTEFVGLDIEMAFNyHYHEVMEeiadTMVQIFKGLQerfQTEIQTVNKQ 331
Cdd:PRK12445 242 LYLKRLVVGGFERVFEINRNFRNEGISV-RHNPEFTMMELYMAYA-DYHDLIE----LTESLFRTLA---QEVLGTTKVT 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 332 FPCEPFKFLEPTLRLEYCEALAMLREAgVEMGDEDDLSTPN----------EKL--LGHLVKEKYD-------TDFYILD 392
Cdd:PRK12445 313 YGEHVFDFGKPFEKLTMREAIKKYRPE-TDMADLDNFDAAKalaesigitvEKSwgLGRIVTEIFDevaeahlIQPTFIT 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 393 KYPLAVRPFYTMPDPrNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTER------ALHHGIDLEKI--KAYIDSFRFGAP 464
Cdd:PRK12445 392 EYPAEVSPLARRNDV-NPEITDRFEFFIGGREIGNGFSELNDAEDQAERfqeqvnAKAAGDDEAMFydEDYVTALEYGLP 470
|
330 340
....*....|....*....|....*....
gi 45439306 465 PHAGGGIGLERVTMLFLGLHNVRQTSMFP 493
Cdd:PRK12445 471 PTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
195-493 |
4.76e-23 |
|
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: 99.97 E-value: 4.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 195 VFRLQSGICHLFRETLINKGFVEIQTPKIISAAseGGANV--FTVSY--FKNNAYLAQSPQLYKQMCICADFEKVFSIGP 270
Cdd:cd00775 7 TFIVRSKIISYIRKFLDDRGFLEVETPMLQPIA--GGAAArpFITHHnaLDMDLYLRIAPELYLKRLIVGGFERVYEIGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 271 VFRAEDSNThRHLTEFVGLDIEMAfnYH-YHEVM---EEIADTMVQ-IFKGLQERFQTEIQTVNKqfpcePFKfleptlR 345
Cdd:cd00775 85 NFRNEGIDL-THNPEFTMIEFYEA--YAdYNDMMdltEDLFSGLVKkINGKTKIEYGGKELDFTP-----PFK------R 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 346 LEYCEALAmlREAGVEMGDEDDLSTPN-EKLLGHLVKEKYD---TDFYILDK------------------YPLAVRPFyT 403
Cdd:cd00775 151 VTMVDALK--EKTGIDFPELDLEQPEElAKLLAKLIKEKIEkprTLGKLLDKlfeefveptliqptfiidHPVEISPL-A 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 404 MPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTER-----ALHHGIDLEKI---KAYIDSFRFGAPPHAGGGIGLER 475
Cdd:cd00775 228 KRHRSNPGLTERFELFICGKEIANAYTELNDPFDQRERfeeqaKQKEAGDDEAMmmdEDFVTALEYGMPPTGGLGIGIDR 307
|
330
....*....|....*...
gi 45439306 476 VTMLFLGLHNVRQTSMFP 493
Cdd:cd00775 308 LVMLLTDSNSIRDVILFP 325
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
184-496 |
1.16e-22 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 101.25 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 184 VIDLRTSTSQAVfrlqsgicHLFRETlinKGFVEIQTPKIISAASEGGANVFTVS------------------------- 238
Cdd:PTZ00425 214 VIRIRNALAIAT--------HLFFQS---RGFLYIHTPLITTSDCEGGGEMFTVTtllgedadyraiprvnkknkkgekr 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 239 --------------------------------------YFKNNAYLAQSPQLYKQMcICADFEKVFSIGPVFRAEDSNTH 280
Cdd:PTZ00425 283 edilntcnannnngnssssnavsspaypdqylidykkdFFSKQAFLTVSGQLSLEN-LCSSMGDVYTFGPTFRAENSHTS 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 281 RHLTEFVGLDIEMAFNYHYHEVmeEIADTMVQIFKG--LQERFQtEIQTVNKQFPCEPFKFLEPTL-----RLEYCEALA 353
Cdd:PTZ00425 362 RHLAEFWMIEPEIAFADLYDNM--ELAESYIKYCIGyvLNNNFD-DIYYFEENVETGLISRLKNILdedfaKITYTNVID 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 354 MLR------EAGVEMGDedDLSTPNEKLlghlVKEKYDTDFYILDKYPLAVRPFYtMPDPRNPKQSNSYDMFM-RGEEIL 426
Cdd:PTZ00425 439 LLQpysdsfEVPVKWGM--DLQSEHERF----VAEQIFKKPVIVYNYPKDLKAFY-MKLNEDQKTVAAMDVLVpKIGEVI 511
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 427 SGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDP 496
Cdd:PTZ00425 512 GGSQREDNLERLDKMIKEKKLNMESYWWYRQLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPRYP 581
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
235-494 |
3.80e-20 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 93.78 E-value: 3.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 235 FTVSYFKNNAYLAQSPQLYKQMCICAdFEKVFSIGPVFRAEDSNTHRHLTEFVGLDIEMAFNyHYHEVMEEIADTMVQIF 314
Cdd:PLN02532 363 FSKDFFSRPTYLTVSGRLHLESYACA-LGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFS-ELEDAMNCAEDYFKFLC 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 315 KGLQERFQTEIQTVNKQFPCEPFKFLE-----PTLRLEYCEALAMLREA---GVEMGDEDDLSTPNEKLlGHLVKEKYDT 386
Cdd:PLN02532 441 KWVLENCSEDMKFVSKRIDKTISTRLEaiissSLQRISYTEAVDLLKQAtdkKFETKPEWGIALTTEHL-SYLADEIYKK 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 387 DFYILDkYPLAVRPFYTMPDpRNPKQSNSYDMFM-RGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPP 465
Cdd:PLN02532 520 PVIIYN-YPKELKPFYVRLN-DDGKTVAAFDLVVpKVGTVITGSQNEERMDILNARIEELGLPREQYEWYLDLRRHGTVK 597
|
250 260
....*....|....*....|....*....
gi 45439306 466 HAGGGIGLERVTMLFLGLHNVRQTSMFPR 494
Cdd:PLN02532 598 HSGFSLGFELMVLFATGLPDVRDAIPFPR 626
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
57-493 |
4.85e-20 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 93.13 E-value: 4.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 57 DEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMV--KFAANINKESIVDVEGVVRKvnQKIGsctqqd 134
Cdd:PLN02502 108 DVSVSVAGRIMAKRAFGKLAFYDLRDDGGKIQLYADKKRLDLDEEEfeKLHSLVDRGDIVGVTGTPGK--TKKG------ 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 135 vELHVQKIYVISLAEPRLPL-----QLDDavrpeaegeeegratvnQDTRLDNRVIDLRTSTSQA-VFRLQSGICHLFRE 208
Cdd:PLN02502 180 -ELSIFPTSFEVLTKCLLMLpdkyhGLTD-----------------QETRYRQRYLDLIANPEVRdIFRTRAKIISYIRR 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 209 TLINKGFVEIQTPKIISAAseGGANVFTVSYFKN----NAYLAQSPQLYKQMCICADFEKVFSIGPVFRAEDSNThRHLT 284
Cdd:PLN02502 242 FLDDRGFLEVETPMLNMIA--GGAAARPFVTHHNdlnmDLYLRIATELHLKRLVVGGFERVYEIGRQFRNEGIST-RHNP 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 285 EFVGLDIEMAFNyHYHEVM---EEIADTMV-QIFKGLQERFQ-TEIQTVnkqfpcEPFK------FLEPTLRLEYCEAL- 352
Cdd:PLN02502 319 EFTTCEFYQAYA-DYNDMMeltEEMVSGMVkELTGSYKIKYHgIEIDFT------PPFRrismisLVEEATGIDFPADLk 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 353 -AMLREAGVEMGDEDDLSTPN--------EKLLGHLVKEKYDTDFYILDkYPLAVRPFyTMPDPRNPKQSNSYDMFMRGE 423
Cdd:PLN02502 392 sDEANAYLIAACEKFDVKCPPpqttgrllNELFEEFLEETLVQPTFVLD-HPVEMSPL-AKPHRSKPGLTERFELFINGR 469
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45439306 424 EILSGAQRIHDP----QLLTERALHHGIDLEKIKAYIDSF----RFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 493
Cdd:PLN02502 470 ELANAFSELTDPvdqrERFEEQVKQHNAGDDEAMALDEDFctalEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFP 547
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
175-493 |
1.30e-18 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 88.91 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 175 NQDTRLDNRVIDLRTS-TSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAAseGGANVFTVSYFKN----NAYLAQS 249
Cdd:PTZ00417 231 DTEIRYRQRYLDLMINeSTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVA--GGANARPFITHHNdldlDLYLRIA 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 250 PQLYKQMCICADFEKVFSIGPVFRAED-SNTHRhlTEFVGLDIEMAFNyHYHEVMEEIADTMVQIFKGLqerFQTEIQTV 328
Cdd:PTZ00417 309 TELPLKMLIVGGIDKVYEIGKVFRNEGiDNTHN--PEFTSCEFYWAYA-DFYDLIKWSEDFFSQLVMHL---FGTYKILY 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 329 NKQFP-CEPFK--FLEPTLRLEYCEALAMLREAGVE--------------MGDEDDLSTPN--------EKLLGHLVKEK 383
Cdd:PTZ00417 383 NKDGPeKDPIEidFTPPYPKVSIVEELEKLTNTKLEqpfdspetinkminLIKENKIEMPNpptaakllDQLASHFIENK 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 384 Y-DTDFYILDkYPLAVRPFYTMPDPRnPKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGIDLEKIKA-------- 454
Cdd:PTZ00417 463 YpNKPFFIIE-HPQIMSPLAKYHRSK-PGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAeafqfdaa 540
|
330 340 350
....*....|....*....|....*....|....*....
gi 45439306 455 YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 493
Cdd:PTZ00417 541 FCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFP 579
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
60-146 |
2.18e-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: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 60 VWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASkqMVKFAANINKESIVDVEGVVRKVnqKIGSCTQQDVELHV 139
Cdd:cd04100 2 VTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELGE--FFEEAEKLRTESVVGVTGTVVKR--PEGNLATGEIELQA 77
|
....*..
gi 45439306 140 QKIYVIS 146
Cdd:cd04100 78 EELEVLS 84
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
175-493 |
2.43e-16 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 82.32 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 175 NQDTRLDNRVIDLRTST-SQAVFRLQSGICHLFRETLINKGFVEIQTPkiISAASEGGANV--FTVSYfknNAY-----L 246
Cdd:PRK02983 748 DPEARVRQRYLDLAVNPeARDLLRARSAVVRAVRETLVARGFLEVETP--ILQQVHGGANArpFVTHI---NAYdmdlyL 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 247 AQSPQLY-KQMCIcADFEKVFSIGPVFRAE--------------------DSNTHRHLTEfvGLDIEMAFNYH------- 298
Cdd:PRK02983 823 RIAPELYlKRLCV-GGVERVFELGRNFRNEgvdathnpeftlleayqahaDYDTMRDLTR--ELIQNAAQAAHgapvvmr 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 299 -YHEVMEEIAD-----TMVQIFKGLQERFQTEIQtvnkqfPCEPFkflePTLRlEYCEAlamlreAGVEMGDEDDLSTPN 372
Cdd:PRK02983 900 pDGDGVLEPVDisgpwPVVTVHDAVSEALGEEID------PDTPL----AELR-KLCDA------AGIPYRTDWDAGAVV 962
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 373 EKLLGHLVkEKYDTD--FYIldKYPLAVRPFyTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDP----QLLTERAL-HH 445
Cdd:PRK02983 963 LELYEHLV-EDRTTFptFYT--DFPTSVSPL-TRPHRSDPGLAERWDLVAWGVELGTAYSELTDPveqrRRLTEQSLlAA 1038
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 45439306 446 GIDLEKI---KAYIDSFRFGAPPHAGGGIGLERVTMLFLGLhNVRQTSMFP 493
Cdd:PRK02983 1039 GGDPEAMeldEDFLQALEYAMPPTGGLGMGVDRLVMLLTGR-SIRETLPFP 1088
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
65-493 |
2.01e-15 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 78.59 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 65 RVHTSRAKGKQCFLVLRQQQFNVQALVAVgDHASKQMVKFAANINKESIVDVEGVVRKvnqkigscTQQDvEL--HVQKI 142
Cdd:PRK00484 62 RVMLKRVMGKASFATLQDGSGRIQLYVSK-DDVGEEALEAFKKLDLGDIIGVEGTLFK--------TKTG-ELsvKATEL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 143 YVISLAEPRLP-----LQlddavrpeaegeeegratvNQDTRLDNRVIDLRTS-TSQAVFRLQSGICHLFRETLINKGFV 216
Cdd:PRK00484 132 TLLTKSLRPLPdkfhgLT-------------------DVETRYRQRYVDLIVNpESRETFRKRSKIISAIRRFLDNRGFL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 217 EIQTPKIISAAseGGANV--FTVSYfknNA-----YLAQSPQLYKQMCICADFEKVFSIGPVFRAEDSNThRHLTEFVGL 289
Cdd:PRK00484 193 EVETPMLQPIA--GGAAArpFITHH---NAldidlYLRIAPELYLKRLIVGGFERVYEIGRNFRNEGIDT-RHNPEFTML 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 290 DIEMAfnYH-YHEVM---EE-IADTMVQIFKGLQERFQ-TEIqTVNKQFPCEPFK----------FLEPTLRleycEALA 353
Cdd:PRK00484 267 EFYQA--YAdYNDMMdltEElIRHLAQAVLGTTKVTYQgTEI-DFGPPFKRLTMVdaikeytgvdFDDMTDE----EARA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 354 MLREAGVEMGDEDDLSTPNEKLLGHLVKEKYDTDFYILDkYPLAVRPFyTMPDPRNPKQSNSYDMFMRGEEILSG----- 428
Cdd:PRK00484 340 LAKELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITD-YPVEISPL-AKRHREDPGLTERFELFIGGREIANAfseln 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45439306 429 -----AQRIHDpQLLtERAL----HHGIDLEkikaYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 493
Cdd:PRK00484 418 dpidqRERFEA-QVE-AKEAgddeAMFMDED----FLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
50-188 |
2.05e-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: 61.38 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 50 DLTIQKADEVV----WVrarvHTSRAKGKQCFLVLRQQQFNVQALVavgDHASKQMVKFAANINKESIVDVEGVVRK--- 122
Cdd:cd04317 7 ELRESHVGQEVtlcgWV----QRRRDHGGLIFIDLRDRYGIVQVVF---DPEEAPEFELAEKLRNESVIQVTGKVRArpe 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45439306 123 --VNQKIGSctqQDVELHVQKIYVISLAEPrLPLQLDDAVRpeaegeeegratVNQDTRLDNRVIDLR 188
Cdd:cd04317 80 gtVNPKLPT---GEIEVVASELEVLNKAKT-LPFEIDDDVN------------VSEELRLKYRYLDLR 131
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
57-154 |
6.39e-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: 6.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 57 DEVVWVrARVHTSRAKGKQCFLVLRQQQFNVQaLVAVGDHASKQMVKFAANINKESIVDVEGVVRKVNQKIGsctqqDVE 136
Cdd:cd04316 13 EEVTVA-GWVHEIRDLGGIKFVILRDREGIVQ-VTAPKKKVDKELFKTVRKLSRESVISVTGTVKAEPKAPN-----GVE 85
|
90
....*....|....*...
gi 45439306 137 LHVQKIYVISLAEPRLPL 154
Cdd:cd04316 86 IIPEEIEVLSEAKTPLPL 103
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
206-308 |
2.25e-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: 57.51 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 206 FRETLINKGFVEIQTPKIISAASEGGAN------VFTVSYFKNNAYLAQSPQLYKQM----CICADFEKVFSIGPVFRAE 275
Cdd:cd00768 9 LRRFMAELGFQEVETPIVEREPLLEKAGhepkdlLPVGAENEEDLYLRPTLEPGLVRlfvsHIRKLPLRLAEIGPAFRNE 88
|
90 100 110
....*....|....*....|....*....|....*....
gi 45439306 276 DSNTH-RHLTEFVGLDIEMAF-----NYHYHEVMEEIAD 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 |
2.36e-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: 48.00 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 60 VWVRARVHT-SRAKGKQCFLVLRQQQFNVQALVAvgdhaSKQMVKFAANINKESIVDVEGVVRKVNQKigsctqqDVELH 138
Cdd:pfam01336 1 VTVAGRVTSiRRSGGKLLFLTLRDGTGSIQVVVF-----KEEAEKLAKKLKEGDVVRVTGKVKKRKGG-------ELELV 68
|
....*..
gi 45439306 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 |
1.42e-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: 44.05 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 60 VWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAvgDHASKQMVKFAANINKESIVDVEGVVRKVNQKIGSctqqdVELHV 139
Cdd:cd04319 2 VTLAGWVYRKREVGKKAFIVLRDSTGIVQAVFS--KDLNEEAYREAKKVGIESSVIVEGAVKADPRAPGG-----AEVHG 74
|
90
....*....|.
gi 45439306 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 |
3.96e-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: 36.44 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45439306 60 VWVRARVHTSRAKGKQCFLVLRQQQFNVQAlVAVGDHASKQMVkfAANINKESIVDVEGVVRKVNQkiGSCTQQDVELHV 139
Cdd:cd04323 2 VKVFGWVHRLRSQKKLMFLVLRDGTGFLQC-VLSKKLVTEFYD--AKSLTQESSVEVTGEVKEDPR--AKQAPGGYELQV 76
|
....*..
gi 45439306 140 QKIYVIS 146
Cdd:cd04323 77 DYLEIIG 83
|
|
| |
