|
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: 729.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 3 SANASRRSQEKPREI--------MDAAEDYAKERYGVSSMIQSQEKPD-RVLVRISDLTVQKAGEVVWVRARVHTSRAKG 73
Cdd:PLN02850 18 AKKAAAKAEKLRREAtakaaaasLEDEDDPLASNYGDVPLEELQSKVTgREWTDVSDLGEELAGSEVLIRGRVHTIRGKG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 74 KQCFLVLRQQQFNVQALVAVGD-HASKQMVKFAANINKESIVDVEGVVRKVNQKIGSCTQQdVELHVQKIYVISSAEPRL 152
Cdd:PLN02850 98 KSAFLVLRQSGFTVQCVVFVSEvTVSKGMVKYAKQLSRESVVDVEGVVSVPKKPVKGTTQQ-VEIQVRKIYCVSKALATL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 153 PLQLDDAVRPEVEGEEEGR-----ATVNQDTRLDNRVIDLRTSTSQAIFRLQSGICHPFRETLTNKGFVEIQTPKIISAA 227
Cdd:PLN02850 177 PFNVEDAARSESEIEKALQtgeqlVRVGQDTRLNNRVLDLRTPANQAIFRIQSQVCNLFREFLLSKGFVEIHTPKLIAGA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 228 SEGGANVFTVSYFKNNAYLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVVEEIA 307
Cdd:PLN02850 257 SEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGDFRRVFEIGPVFRAEDSFTHRHLCEFTGLDLEMEIKEHYSEVLDVVD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 308 DTLVQIFKGLQKRFQTEIQTVNKQFPCEPFKFLEPTLRLEYCEALAMLREAGIEMGDEEDLSTPNEKLLGRLVKEKYDTD 387
Cdd:PLN02850 337 ELFVAIFDGLNERCKKELEAIREQYPFEPLKYLPKTLRLTFAEGIQMLKEAGVEVDPLGDLNTESERKLGQLVKEKYGTD 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 388 FYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLVTERALHHGIDLEKIKAYIDSFRFGAPPHA 467
Cdd:PLN02850 417 FYILHRYPLAVRPFYTMPCPDDPKYSNSFDVFIRGEEIISGAQRVHDPELLEKRAEECGIDVKTISTYIDSFRYGAPPHG 496
|
490 500 510
....*....|....*....|....*....|....
gi 78045531 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: 529.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 6 ASRRSQEKPREIMDAA--EDYaKERYGVSSMIQSQEKPDRVLVRISDLTVQK-AGEVVWVRARVHTSRAKGKQCFLVLRQ 82
Cdd:PTZ00401 25 AARLAEEKARAAEKAAlvEKY-KDVFGAAPMVQSTTYKSRTFIPVAVLSKPElVDKTVLIRARVSTTRKKGKMAFMVLRD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 83 QQFNVQALVAVGDHASKQMVKFAANINKESIVDVEGVVRKVNQKIGSCTQQDVELHVQKIYVISSAEPRLPLQLDDAVRP 162
Cdd:PTZ00401 104 GSDSVQAMAAVEGDVPKEMIDFIGQIPTESIVDVEATVCKVEQPITSTSHSDIELKVKKIHTVTESLRTLPFTLEDASRK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 163 EvegEEEGrATVNQDTRLDNRVIDLRTSTSQAIFRLQSGICHPFRETLTNKGFVEIQTPKIISAASEGGANVFTVSYFKN 242
Cdd:PTZ00401 184 E---SDEG-AKVNFDTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDSDFCEIHSPKIINAPSEGGANVFKLEYFNR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 243 NAYLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVVEEIADTLVQIFKGLQKRfQ 322
Cdd:PTZ00401 260 FAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHLTEFVGLDVEMRINEHYYEVLDLAESLFNYIFERLATH-T 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 323 TEIQTVNKQFPCEPFKF------------------LEPT--------------LRLEYCEALAMLREAGIE-MGDEEDLS 369
Cdd:PTZ00401 339 KELKAVCQQYPFEPLVWkltpermkelgvgvisegVEPTdkyqarvhnmdsrmLRINYMHCIELLNTVLEEkMAPTDDIN 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 370 TPNEKLLGRLVKEKYDTDFYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLVTERALHHGIDL 449
Cdd:PTZ00401 419 TTNEKLLGKLVKERYGTDFFISDRFPSSARPFYTMECKDDERFTNSYDMFIRGEEISSGAQRIHDPDLLLARAKMLNVDL 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 78045531 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 |
3.99e-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: 487.46 E-value: 3.99e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 174 VNQDTRLDNRVIDLRTSTSQAIFRLQSGICHPFRETLTNKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLY 253
Cdd:cd00776 2 ANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 254 KQMCICAdFEKVFCIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVVEEIADTLVQIFKGLQKRFQTEIQTVNkQFP 333
Cdd:cd00776 82 KEMLIAA-LERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRVLERCAKELELVN-QLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 334 CEPFKFLEPTLRLEYCEALAMLREAGI--EMGDEEDLSTPNEKLLGRLVKekydTDFYILDKYPLAVRPFYTMPDPRNPK 411
Cdd:cd00776 160 RELLKPLEPFPRITYDEAIELLREKGVeeEVKWGEDLSTEHERLLGEIVK----GDPVFVTDYPKEIKPFYMKPDDDNPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 412 QSNSYDMFMRG-EEILSGAQRIHDPQLVTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTS 490
Cdd:cd00776 236 TVESFDLLMPGvGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAI 315
|
....*..
gi 78045531 491 MFPRDPK 497
Cdd:cd00776 316 LFPRDPK 322
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
46-501 |
6.83e-167 |
|
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: 478.16 E-value: 6.83e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 46 VRISDLTVQKAGEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQaLVAVGDHASKQMVKFAANINKESIVDVEGVVRkvnq 125
Cdd:TIGR00458 1 VYSADIKPEMDGQEVTFMGWVHEIRDLGGLIFVLLRDREGLIQ-ITAPAKKVSKNLFKWAKKLNLESVVAVRGIVK---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 126 kIGSCTQQDVELHVQKIYVISSAEPRLPLQLDDAVRPEVegeeegratvnqDTRLDNRVIDLRTSTSQAIFRLQSGICHP 205
Cdd:TIGR00458 76 -IKEKAPGGFEIIPTKIEVINEAKEPLPLDPTEKVPAEL------------DTRLDYRFLDLRRPTVQAIFRIRSGVLES 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 206 FRETLTNKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNTHRHLTE 285
Cdd:TIGR00458 143 VREFLAEEGFIEVHTPKLVASATEGGTELFPITYFEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHRHLNE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 286 FVGLDIEMAFNYHyHEVVEEIADTLVQIFKGLQKRFQTEIQTVNKQFPCEPFKFleptLRLEYCEALAMLREAGIEMGDE 365
Cdd:TIGR00458 223 ATSIDIEMAFEDH-HDVMDILEELVVRVFEDVPERCAHQLETLEFKLEKPEGKF----VRLTYDEAIEMANAKGVEIGWG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 366 EDLSTPNEKLLGrlvkEKYDTDFYILDkYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLVTERALHH 445
Cdd:TIGR00458 298 EDLSTEAEKALG----EEMDGLYFITD-WPTEIRPFYTMPDEDNPEISKSFDLMYRDLEISSGAQRIHLHDLLVERIKAK 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 78045531 446 GIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 501
Cdd:TIGR00458 373 GLNPEGFKDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRKRLTP 428
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
48-501 |
2.17e-159 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 459.66 E-value: 2.17e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 48 ISDLTVQKAGEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDhaSKQMVKFAANINKESIVDVEGVVRKVNQKI 127
Cdd:PRK05159 7 TSELTPELDGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKV--DEELFETIKKLKRESVVSVTGTVKANPKAP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 128 GSctqqdVELHVQKIYVISSAEPRLPLqlddavrpEVEGEEEgrATVnqDTRLDNRVIDLRTSTSQAIFRLQSGICHPFR 207
Cdd:PRK05159 85 GG-----VEVIPEEIEVLNKAEEPLPL--------DISGKVL--AEL--DTRLDNRFLDLRRPRVRAIFKIRSEVLRAFR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 208 ETLTNKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNTHRHLTEFV 287
Cdd:PRK05159 148 EFLYENGFTEIFTPKIVASGTEGGAELFPIDYFEKEAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRHLNEYT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 288 GLDIEMAFNYHYHEVVEEIADTLVQIFKGLQKRFQTEIQTVNKQFPCEPfkflEPTLRLEYCEALAMLREAGIEMGDEED 367
Cdd:PRK05159 228 SIDVEMGFIDDHEDVMDLLENLLRYMYEDVAENCEKELELLGIELPVPE----TPIPRITYDEAIEILKSKGNEISWGDD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 368 LSTPNEKLLGRLVKEKYDTDFYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLVTERALHHGI 447
Cdd:PRK05159 304 LDTEGERLLGEYVKEEYGSDFYFITDYPSEKRPFYTMPDEDDPEISKSFDLLFRGLEITSGGQRIHRYDMLVESIKEKGL 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 78045531 448 DLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 501
Cdd:PRK05159 384 NPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPRDRHRLTP 437
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
46-501 |
3.28e-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: 448.73 E-value: 3.28e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 46 VRISDLTVQKAGEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMVKfaaNINKESIVDVEGVVRKVNQ 125
Cdd:COG0017 3 TYIKDLLPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKLENFEEAK---KLTTESSVEVTGTVVESPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 126 KigsctQQDVELHVQKIYVISSAEPRLPLQLDDAvrpevegeeegratvNQDTRLDNRVIDLRTSTSQAIFRLQSGICHP 205
Cdd:COG0017 80 A-----PQGVELQAEEIEVLGEADEPYPLQPKRH---------------SLEFLLDNRHLRLRTNRFGAIFRIRSELARA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 206 FRETLTNKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLYKQMCICAdFEKVFCIGPVFRAEDSNTHRHLTE 285
Cdd:COG0017 140 IREFFQERGFVEVHTPIITASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMA-LEKVYTFGPTFRAEKSNTRRHLAE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 286 FVGLDIEMAFnYHYHEVVEEIADTLVQIFKGLQKRFQTEIQTVN------KQFPCEPFKfleptlRLEYCEALAMLREAG 359
Cdd:COG0017 219 FWMIEPEMAF-ADLEDVMDLAEEMLKYIIKYVLENCPEELEFLGrdverlEKVPESPFP------RITYTEAIEILKKSG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 360 IEMGDEEDLSTPNEKLLGrlvkEKYDTDFYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRG-EEILSGAQRIHDPQLV 438
Cdd:COG0017 292 EKVEWGDDLGTEHERYLG----EEFFKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGiGEIIGGSQREHRYDVL 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78045531 439 TERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 501
Cdd:COG0017 368 VERIKEKGLDPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
175-496 |
3.80e-99 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 301.41 E-value: 3.80e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 175 NQDTRLDNRVIDLRTSTSQAIFRLQSGICHPFRETLTNKGFVEIQTPKIISAASEGGANVFTVSYFKNN--AYLAQSPQL 252
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGkfYALPQSPQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 253 YKQMCICADFEKVFCIGPVFRAEDSNTHRHLtEFVGLDIEMAFNyHYHEVVEEIADTLVQIFKGLQKRFQTEIQTVNKQF 332
Cdd:pfam00152 81 YKQLLMVAGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFV-DYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 333 PcEPFKfleptlRLEYCEALAMLREAGIEMgDEEDLSTPNEKLLGRLVKEKYDTDFYILDKYPLAVRPFYTMPDPRNPKQ 412
Cdd:pfam00152 159 K-KPFP------RITYAEAIEKLNGKDVEE-LGYGSDKPDLRFLLELVIDKNKFNPLWVTDFPAEHHPFTMPKDEDDPAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 413 SNSYDMFMRGEEILSGAQRIHDPQLVTERALHHGIDLEKIKA----YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQ 488
Cdd:pfam00152 231 AEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPEEAEEkfgfYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIRE 310
|
....*...
gi 78045531 489 TSMFPRDP 496
Cdd:pfam00152 311 VIAFPKTR 318
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
46-501 |
4.42e-78 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 251.18 E-value: 4.42e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 46 VRISDLTVQK-AGEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQmvKFAANINKESIVDVEGVVRKVN 124
Cdd:PRK03932 4 VSIKDILKGKyVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDNGEEYF--EEIKKLTTGSSVIVTGTVVESP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 125 QKigsctQQDVELHVQKIYVISSAEPRLPLQLDdavrpevegeeegRATVnqDTRLDNRVIDLRTSTSQAIFRLQSGICH 204
Cdd:PRK03932 82 RA-----GQGYELQATKIEVIGEDPEDYPIQKK-------------RHSI--EFLREIAHLRPRTNKFGAVMRIRNTLAQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 205 PFRETLTNKGFVEIQTPKIISAASEGGANVFTVS---------YFKNNAYLAQSPQLYKQMCICAdFEKVFCIGPVFRAE 275
Cdd:PRK03932 142 AIHEFFNENGFVWVDTPIITASDCEGAGELFRVTtldldfskdFFGKEAYLTVSGQLYAEAYAMA-LGKVYTFGPTFRAE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 276 DSNTHRHLTEFVGLDIEMAFnYHyHEVVEEIADTLVQ-IFKGLQKRFQTEIQTVNKQFPCEPFKFLEPTL-----RLEYC 349
Cdd:PRK03932 221 NSNTRRHLAEFWMIEPEMAF-AD-LEDNMDLAEEMLKyVVKYVLENCPDDLEFLNRRVDKGDIERLENFIespfpRITYT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 350 EALAMLREAG------IEMGDeeDLSTPNEKLLgrlVKEKYDTDFYILDkYPLAVRPFYTMPDPRNpKQSNSYDMFMRG- 422
Cdd:PRK03932 299 EAIEILQKSGkkfefpVEWGD--DLGSEHERYL---AEEHFKKPVFVTN-YPKDIKAFYMRLNPDG-KTVAAMDLLAPGi 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78045531 423 EEILSGAQRIHDPQLVTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 501
Cdd:PRK03932 372 GEIIGGSQREERLDVLEARIKELGLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
54-501 |
1.73e-71 |
|
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: 234.20 E-value: 1.73e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 54 QKAGEVVWVRARVHTSRAKGKQCFLVLRQQQF--NVQALVAVGDhaSKQMVKFAANINKESIVDVEGVVRKVNQKigsct 131
Cdd:TIGR00457 13 KFVGDEVTVSGWVRTKRSSKKIIFLELNDGSSlgPIQAVINGED--NPYLFQLLKSLTTGSSVSVTGKVVESPGK----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 132 QQDVELHVQKIYVISSAEPR-LPLQLDDavrpevegeeegratvnQDTRL--DNRVIDLRTSTSQAIFRLQSGICHPFRE 208
Cdd:TIGR00457 86 GQPVELQVKKIEVVGEAEPDdYPLQKKE-----------------HSLEFlrDIAHLRLRTNTLGAVMRVRNALSQAIHR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 209 TLTNKGFVEIQTPKIISAASEGGANVFTVS---------YFKNNAYLAQSPQLYKQMCICAdFEKVFCIGPVFRAEDSNT 279
Cdd:TIGR00457 149 YFQENGFTWVSPPILTSNDCEGAGELFRVStgnidfsqdFFGKEAYLTVSGQLYLETYALA-LSKVYTFGPTFRAEKSNT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 280 HRHLTEFVGLDIEMAFnYHYHEVVEEIADTLVQIFKGLQKRFQTEIQTVNKQFPCEPFKFLEPTL-----RLEYCEALAM 354
Cdd:TIGR00457 228 SRHLSEFWMIEPEMAF-ANLNDLLQLAETLIKYIIKAVLENCSQELKFLEKNFDKDLIKRLENIInnkfaRITYTDAIEI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 355 LREAGIEMGDEE----DLSTPNEKLLGrlvkEKYDTDFYILDKYPLAVRPFYtMPDPRNPKQSNSYDMFMRG-EEILSGA 429
Cdd:TIGR00457 307 LKESDKNFEYEDfwgdDLQTEHERFLA----EEYFKPPVFVTNYPKDIKAFY-MKLNDDGKTVAAMDLLAPGiGEIIGGS 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78045531 430 QRIHDPQLVTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 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 |
7.45e-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: 187.68 E-value: 7.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 196 FRLQSGICHPFRETLTNKGFVEIQTPKIISAASEGGANVFTVSYFK--NNAYLAQSPQLYKQMCICADFEKVFCIGPVFR 273
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNAlgLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 274 AEDSNThRHLTEFVGLDIEMAF-NYH-YHEVVEEIADTLVQIFKGlqkrfqteiqTVNKQFPCEPFKFLEPTLRLEYCEA 351
Cdd:cd00669 81 NEDLRA-RHQPEFTMMDLEMAFaDYEdVIELTERLVRHLAREVLG----------VTAVTYGFELEDFGLPFPRLTYREA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 352 LAMLREagiemgdeedlstpnekllgrlvkekydtdFYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQR 431
Cdd:cd00669 150 LERYGQ------------------------------PLFLTDYPAEMHSPLASPHDVNPEIADAFDLFINGVEVGNGSSR 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78045531 432 IHDPQLVTERALHHGID----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 |
1.72e-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: 1.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 60 VWVRARVHTSRAKG-KQCFLVLRQQQFNVQALVAVGDHA-SKQMVKFAANINKESIVDVEGVVRKVNQKIGSCTQQDVEL 137
Cdd:cd04320 2 VLIRARVHTSRAQGaKLAFLVLRQQGYTIQGVLAASAEGvSKQMVKWAGSLSKESIVDVEGTVKKPEEPIKSCTQQDVEL 81
|
90 100
....*....|....*....|.
gi 78045531 138 HVQKIYVISSAEPRLPLQLDD 158
Cdd:cd04320 82 HIEKIYVVSEAAEPLPFQLED 102
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
176-496 |
3.32e-49 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 172.13 E-value: 3.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 176 QDTRLDNRVIdLRTSTSQAIFRLQSGICHPFRETLTNKGFVEIQTPkIISA--------ASEGGANVFTVSYFKNNAYLA 247
Cdd:PRK06462 11 EEFLRMSWKH-ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPP-IISPstdplmglGSDLPVKQISIDFYGVEYYLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 248 QSPQLYKQMCIcADFEKVFCIGPVFRAE--DSNTHRHLTEFVGLDIEMAfNYHYHEVVEEIADTLVQIFKGLQKRFQTEI 325
Cdd:PRK06462 89 DSMILHKQLAL-RMLGKIFYLSPNFRLEpvDKDTGRHLYEFTQLDIEIE-GADLDEVMDLIEDLIKYLVKELLEEHEDEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 326 QTVNKQFPcepfKFLEPTLRLEYCEALAMLREAGIEMGDEEDLSTPNEKLLgrlvKEKYDTDFYILDkYPLAVRPFYTMP 405
Cdd:PRK06462 167 EFFGRDLP----HLKRPFKRITHKEAVEILNEEGCRGIDLEELGSEGEKSL----SEHFEEPFWIID-IPKGSREFYDRE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 406 DPRNPKQSNSYDMFMR---GEeILSGAQRIHDPQLVTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLG 482
Cdd:PRK06462 238 DPERPGVLRNYDLLLPegyGE-AVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICG 316
|
330
....*....|....
gi 78045531 483 LHNVRQTSMFPRDP 496
Cdd:PRK06462 317 LRHIREVQPFPRVP 330
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
50-493 |
2.95e-43 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 161.39 E-value: 2.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 50 DLTVQKAGEVV----WVrarvHTSRAKGKQCFLVLRQQQFNVQALVavgdHASKQMVKFAANINKESIVDVEGVVRK--- 122
Cdd:PRK00476 10 ELRESHVGQTVtlcgWV----HRRRDHGGLIFIDLRDREGIVQVVF----DPDAEAFEVAESLRSEYVIQVTGTVRArpe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 123 --VNQKIGSctqQDVELHVQKIYVISSAEPrLPLQLDDavrpevegEEEgratVNQDTRLDNRVIDLRTSTSQAIFRLQS 200
Cdd:PRK00476 82 gtVNPNLPT---GEIEVLASELEVLNKSKT-LPFPIDD--------EED----VSEELRLKYRYLDLRRPEMQKNLKLRS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 201 GICHPFRETLTNKGFVEIQTPkIISAASEGGANVFTV-S-YFKNNAY-LAQSPQLYKQMCICADFEKVFCIGPVFRAEDS 277
Cdd:PRK00476 146 KVTSAIRNFLDDNGFLEIETP-ILTKSTPEGARDYLVpSrVHPGKFYaLPQSPQLFKQLLMVAGFDRYYQIARCFRDEDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 278 NTHRhLTEFVGLDIEMAFnyhyheV-VEEIADT----LVQIFK-----------------------GLQK---RFQTEIQ 326
Cdd:PRK00476 225 RADR-QPEFTQIDIEMSF------VtQEDVMALmeglIRHVFKevlgvdlptpfprmtyaeamrryGSDKpdlRFGLELV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 327 TVNKQFPCEPFK-FLEPT--------LRLEYC--------------------------------------------EALA 353
Cdd:PRK00476 298 DVTDLFKDSGFKvFAGAAndggrvkaIRVPGGaaqlsrkqideltefakiygakglayikvnedglkgpiakflseEELA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 354 MLREA-GIEMGD-------EEDLSTpneKLLGRL---VKEKYD------------TDFyildkyPL------AVR----- 399
Cdd:PRK00476 378 ALLERtGAKDGDliffgadKAKVVN---DALGALrlkLGKELGlidedkfaflwvVDF------PMfeydeeEGRwvaah 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 400 -PFyTMPDP--------RNPKQ--SNSYDMFMRGEEILSGAQRIHDPQlVTERALHH-GIDLEKIKA----YIDSFRFGA 463
Cdd:PRK00476 449 hPF-TMPKDedldeletTDPGKarAYAYDLVLNGYELGGGSIRIHRPE-IQEKVFEIlGISEEEAEEkfgfLLDALKYGA 526
|
570 580 590
....*....|....*....|....*....|
gi 78045531 464 PPHAGGGIGLERVTMLFLGLHNVRQTSMFP 493
Cdd:PRK00476 527 PPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
50-493 |
1.32e-38 |
|
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439943 [Multi-domain] Cd Length: 589 Bit Score: 148.22 E-value: 1.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 50 DLTVQKAGEVV----WVrarvHTSRAKGKQCFLVLR------QqqfnvqalVAVGDHASKQMVKFAANINKESIVDVEGV 119
Cdd:COG0173 9 ELRESDVGQEVtlsgWV----HRRRDHGGLIFIDLRdrygitQ--------VVFDPDDSAEAFEKAEKLRSEYVIAVTGK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 120 VRK-----VNQKI--GsctqqDVELHVQKIYVISSAEPrLPLQLDDAVrpevegeeegraTVNQDTRLDNRVIDLRTSTS 192
Cdd:COG0173 77 VRArpegtVNPKLptG-----EIEVLASELEILNKAKT-PPFQIDDDT------------DVSEELRLKYRYLDLRRPEM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 193 QAIFRLQSGICHPFRETLTNKGFVEIQTPkIISAASEGGANVFTV-------SYFknnAyLAQSPQLYKQMCICADFEKV 265
Cdd:COG0173 139 QKNLILRHKVTKAIRNYLDENGFLEIETP-ILTKSTPEGARDYLVpsrvhpgKFY---A-LPQSPQLFKQLLMVSGFDRY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 266 FCIGPVFRAEDSNTHRHLtEFVGLDIEMAFnyhyhevVEE-----IADTLVQ-IFK-----------------------G 316
Cdd:COG0173 214 FQIARCFRDEDLRADRQP-EFTQLDIEMSF-------VDQedvfeLMEGLIRhLFKevlgvelptpfprmtyaeameryG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 317 LQK---RFQTEIQTVNKQFPCEPFK-FLEPT--------LRLEYC----------------------------------- 349
Cdd:COG0173 286 SDKpdlRFGLELVDVTDIFKDSGFKvFAGAAenggrvkaINVPGGaslsrkqideltefakqygakglayikvnedglks 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 350 --------EALAMLREA-GIEMGD-------EEDLSTpneKLLGRL-----------VKEKYD----TDFyildkyPL-- 396
Cdd:COG0173 366 piakflseEELAAILERlGAKPGDliffvadKPKVVN---KALGALrlklgkelgliDEDEFAflwvVDF------PLfe 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 397 ---------AVR-PFyTMPDP-------RNPKQ--SNSYDMFMRGEEILSGAQRIHDPQlVTERALHH-GIDLEKIKA-- 454
Cdd:COG0173 437 ydeeegrwvAMHhPF-TMPKDedldlleTDPGKvrAKAYDLVLNGYELGGGSIRIHDPE-LQEKVFELlGISEEEAEEkf 514
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 78045531 455 --YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 493
Cdd:COG0173 515 gfLLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
196-493 |
1.48e-38 |
|
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. AspRS is a homodimer, which attaches a specific amino acid to the 3' OH group of ribose of the appropriate tRNA. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. AspRS in this family differ from those found in the AsxRS family by a GAD insert in the core domain.
Pssm-ID: 238400 [Multi-domain] Cd Length: 280 Bit Score: 141.94 E-value: 1.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 196 FRLQSGICHPFRETLTNKGFVEIQTPkIISAASEGGANVFTVSY--FKNNAY-LAQSPQLYKQMCICADFEKVFCIGPVF 272
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETP-ILTKSTPEGARDFLVPSrlHPGKFYaLPQSPQLFKQLLMVSGFDRYFQIARCF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 273 RAEDSNTHRHlTEFVGLDIEMAFnYHYHEVVEEIADTLVQIFKglqKRFQTEIQTvnkqfpcePFKfleptlRLEYCEAL 352
Cdd:cd00777 80 RDEDLRADRQ-PEFTQIDIEMSF-VDQEDIMSLIEGLLKYVFK---EVLGVELTT--------PFP------RMTYAEAM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 353 amlreagiemgdeedlstpnekllgrlvkEKYDTDF-YILD-----------KYPLAVRPFyTMPDP-------RNPKQ- 412
Cdd:cd00777 141 -----------------------------ERYGFKFlWIVDfplfewdeeegRLVSAHHPF-TAPKEedldlleKDPEDa 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 413 -SNSYDMFMRGEEILSGAQRIHDPQLvTERALHH-GIDLEKIKA----YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNV 486
Cdd:cd00777 191 rAQAYDLVLNGVELGGGSIRIHDPDI-QEKVFEIlGLSEEEAEEkfgfLLEAFKYGAPPHGGIALGLDRLVMLLTGSESI 269
|
....*..
gi 78045531 487 RQTSMFP 493
Cdd:cd00777 270 RDVIAFP 276
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
2-493 |
8.25e-33 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 132.46 E-value: 8.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 2 PSANASRRSQEKPREIMDAAEDYAKERyGVSSMIQSQEKPDRVLV--RISDLTVQKAGevvwvraRVHTSRAKGKQCFLV 79
Cdd:PTZ00385 58 ATKTVTQEASRAPRSKLDLPAAYSSFR-GITPISEVRERYGYLASgdRAAQATVRVAG-------RVTSVRDIGKIIFVT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 80 LRQQQFNVQALVAVGDHASKQMVK-FAANINKESIVDVEGVvrkvnqkigSCTQQDVELHV--QKIYVISSAEPRlplql 156
Cdd:PTZ00385 130 IRSNGNELQVVGQVGEHFTREDLKkLKVSLRVGDIIGADGV---------PCRMQRGELSVaaSRMLILSPYVCT----- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 157 DDAVRPEVEGEEEGRatvNQDTRLDNRVIDLRTSTSQ-AIFRLQSGICHPFRETLTNKGFVEIQTPKIISAASEGGANVF 235
Cdd:PTZ00385 196 DQVVCPNLRGFTVLQ---DNDVKYRYRFTDMMTNPCViETIKKRHVMLQALRDYFNERNFVEVETPVLHTVASGANAKSF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 236 TVSYFKNNA--YLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNtHRHLTEFVGLDIEMAfnYH-YHEVVEEIADTLVQ 312
Cdd:PTZ00385 273 VTHHNANAMdlFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDAD-RSHNPEFTSCEFYAA--YHtYEDLMPMTEDIFRQ 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 313 IFKGLQKRFQTEIQTVNKQFPCEPFKFLEPTLRLEYCEALAmlREAGIEMGDEEDLSTPNEKLLGRLVKEKYDT------ 386
Cdd:PTZ00385 350 LAMRVNGTTVVQIYPENAHGNPVTVDLGKPFRRVSVYDEIQ--RMSGVEFPPPNELNTPKGIAYMSVVMLRYNIplppvr 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 387 ----------DFYILDKyplAVRPFYTMPDP-----------RNPKQSNSYDMFMRGEEILSGAQRIHDPQLVTERALHH 445
Cdd:PTZ00385 428 taakmfekliDFFITDR---VVEPTFVMDHPlfmsplakeqvSRPGLAERFELFVNGIEYCNAYSELNDPHEQYHRFQQQ 504
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 78045531 446 GID--------LEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 493
Cdd:PTZ00385 505 LVDrqggdeeaMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFP 560
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
50-501 |
2.10e-30 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 125.48 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 50 DLTVQKAGEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAvGDHASKQMVKFAANINKESIVDVEGVVRKVNQKIGS 129
Cdd:PRK12820 11 HLSLDDTGREVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFS-PEAAPADVYELAASLRAEFCVALQGEVQKRLEETEN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 130 --CTQQDVELHVQKIYVISSAEPrLPLQLDDavRPEVEGEEEGRA-TVNQDTRLDNRVIDLRTSTSQAIFRLQSGICHPF 206
Cdd:PRK12820 90 phIETGDIEVFVRELSILAASEA-LPFAISD--KAMTAGAGSAGAdAVNEDLRLQYRYLDIRRPAMQDHLAKRHRIIKCA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 207 RETLTNKGFVEIQTPKIISAASEGGANVFTVSYFKNNAY--LAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNTHRHlT 284
Cdd:PRK12820 167 RDFLDSRGFLEIETPILTKSTPEGARDYLVPSRIHPKEFyaLPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQ-P 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 285 EFVGLDIEMAF--NYHYHEVVEEI------------------------------------------------ADTLVQIF 314
Cdd:PRK12820 246 EFTQLDIEASFidEEFIFELIEELtarmfaiggialprpfprmpyaeamdttgsdrpdlrfdlkfadatdifENTRYGIF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 315 KGLQKRfQTEIQTVNKQFPCEpfKFLEPTLRLEYCEALA----------MLREAG------IEMGDEEDLstpnEKLLGR 378
Cdd:PRK12820 326 KQILQR-GGRIKGINIKGQSE--KLSKNVLQNEYAKEIApsfgakgmtwMRAEAGgldsniVQFFSADEK----EALKRR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 379 LVKEKYDTDFYILDK----------------------------YPLAVRPF-----------------YTMP-----DPR 408
Cdd:PRK12820 399 FHAEDGDVIIMIADAscaivlsalgqlrlhladrlglipegvfHPLWITDFplfeatddggvtsshhpFTAPdredfDPG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 409 NPK-----QSNSYDMFMRGEEILSGAQRIHDP--QLVTERALhhGIDLEKIKA----YIDSFRFGAPPHAGGGIGLERVT 477
Cdd:PRK12820 479 DIEelldlRSRAYDLVVNGEELGGGSIRINDKdiQLRIFAAL--GLSEEDIEDkfgfFLRAFDFAAPPHGGIALGLDRVV 556
|
570 580
....*....|....*....|....
gi 78045531 478 MLFLGLHNVRQTSMFPRDPKRLTP 501
Cdd:PRK12820 557 SMILQTPSIREVIAFPKNRSAACP 580
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
43-496 |
7.86e-30 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 122.77 E-value: 7.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 43 RVLVRISDLT------VQKAGEVVWVRARVHTSRAKGKQCFLVLRQQQF--NVQALVAVGDHASKQMVkfAANINKESIV 114
Cdd:PLN02603 87 RKKLRIADVKggedegLARVGKTLNVMGWVRTLRAQSSVTFIEVNDGSClsNMQCVMTPDAEGYDQVE--SGLITTGASV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 115 DVEGVVRKvnqkiGSCTQQDVELHVQKIYVISSAEPRLPLQLDDAVRPEVEGEEEGRAtvnqdtrldnrvidlRTSTSQA 194
Cdd:PLN02603 165 LVQGTVVS-----SQGGKQKVELKVSKIVVVGKSDPSYPIQKKRVSREFLRTKAHLRP---------------RTNTFGA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 195 IFRLQSGICHPFRETLTNKGFVEIQTPKIISAASEGGANVFTVS------------------------------YFKNNA 244
Cdd:PLN02603 225 VARVRNALAYATHKFFQENGFVWVSSPIITASDCEGAGEQFCVTtlipnsaenggslvddipktkdglidwsqdFFGKPA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 245 YLAQSPQLYKQMCICAdFEKVFCIGPVFRAEDSNTHRHLTEFVGLDIEMAF----------NYHYHEVVEEIADTLVQ-- 312
Cdd:PLN02603 305 FLTVSGQLNGETYATA-LSDVYTFGPTFRAENSNTSRHLAEFWMIEPELAFadlnddmacaTAYLQYVVKYILENCKEdm 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 313 ------IFKGLQKRFQteiQTVNKQFpcepfkfleptLRLEYCEALAMLREA----------GIEMGDEEDLSTPNEKLL 376
Cdd:PLN02603 384 effntwIEKGIIDRLS---DVVEKNF-----------VQLSYTDAIELLLKAkkkfefpvkwGLDLQSEHERYITEEAFG 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 377 GRLVkekydtdfyILDKYPLAVRPFYtMPDPRNPKQSNSYDMFM-RGEEILSGAQRIHDPQLVTERALHHGIDLEKIKAY 455
Cdd:PLN02603 450 GRPV---------IIRDYPKEIKAFY-MRENDDGKTVAAMDMLVpRVGELIGGSQREERLEYLEARLDELKLNKESYWWY 519
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 78045531 456 IDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDP 496
Cdd:PLN02603 520 LDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPRVP 560
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
50-494 |
5.70e-28 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 117.58 E-value: 5.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 50 DLTVQKAGEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQalVAVGDHASKQMVKFAANINKESIVDVEGVVRK-----VN 124
Cdd:PLN02903 65 ALSVNDVGSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQ--VVTLPDEFPEAHRTANRLRNEYVVAVEGTVRSrpqesPN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 125 QKIGSCTqqdVELHVQKIYVISSAEPRLPLQlddavrpeVEGEEEGRATVNQDTRLDNRVIDLRTSTSQAIFRLQSGICH 204
Cdd:PLN02903 143 KKMKTGS---VEVVAESVDILNVVTKSLPFL--------VTTADEQKDSIKEEVRLRYRVLDLRRPQMNANLRLRHRVVK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 205 PFRETLTNK-GFVEIQTPKIISAASEGGANVFTVSYFKNNAYLA--QSPQLYKQMCICADFEKVFCIGPVFRAEDSNTHR 281
Cdd:PLN02903 212 LIRRYLEDVhGFVEIETPILSRSTPEGARDYLVPSRVQPGTFYAlpQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 282 HlTEFVGLDIEMAFNyhYHEVVEEIADTLV-QIFK-----------------------GLQK---RFQTEIQTVNKQFPC 334
Cdd:PLN02903 292 Q-PEFTQLDMELAFT--PLEDMLKLNEDLIrQVFKeikgvqlpnpfprltyaeamskyGSDKpdlRYGLELVDVSDVFAE 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 335 EPFKFLE-------------------------------------------PTLR------LEYCEAL----------AML 355
Cdd:PLN02903 369 SSFKVFAgalesggvvkaicvpdgkkisnntalkkgdiyneaiksgakglAFLKvlddgeLEGIKALveslspeqaeQLL 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 356 REAGIEMGD-----EEDLSTPNeKLLGRL---VKEKYD------------TDFYILDKYPLAVR------PFyTMPDPRN 409
Cdd:PLN02903 449 AACGAGPGDlilfaAGPTSSVN-KTLDRLrqfIAKTLDlidpsrhsilwvTDFPMFEWNEDEQRlealhhPF-TAPNPED 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 410 PKQSNS-----YDMFMRGEEILSGAQRIHDPQlVTERALHH-GIDLE----KIKAYIDSFRFGAPPHAGGGIGLERVTML 479
Cdd:PLN02903 527 MGDLSSaralaYDMVYNGVEIGGGSLRIYRRD-VQQKVLEAiGLSPEeaesKFGYLLEALDMGAPPHGGIAYGLDRLVML 605
|
570
....*....|....*
gi 78045531 480 FLGLHNVRQTSMFPR 494
Cdd:PLN02903 606 LAGAKSIRDVIAFPK 620
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
33-498 |
4.39e-25 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 108.54 E-value: 4.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 33 SMIQSQEKPDRVLVRI----SDLTVQKAGEVVWVRARVHTSRAKGKQCFLVLRQQQ----FNVQALVAVGDHASKQMVKF 104
Cdd:PLN02221 22 STVQKAQFSDRVLIRSildrPDGGAGLAGQKVRIGGWVKTGREQGKGTFAFLEVNDgscpANLQVMVDSSLYDLSTLVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 105 AaninkeSIVDVEGVVrKVNQKiGSCTQQDVELHVQKIYVISSAEP-RLPLQlddavrpevegeeegRATVNQDTRLDNR 183
Cdd:PLN02221 102 G------TCVTVDGVL-KVPPE-GKGTKQKIELSVEKVIDVGTVDPtKYPLP---------------KTKLTLEFLRDVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 184 VIDLRTSTSQAIFRLQSGICHPFRETLTNKGFVEIQTPKIISAASEGGANVFTVS------------------------- 238
Cdd:PLN02221 159 HLRSRTNSISAVARIRNALAFATHSFFQEHSFLYIHTPIITTSDCEGAGEMFQVTtlinyterleqdlidnpppteadve 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 239 -----------------------------------------------------------------YFKNNAYLAQSPQLY 253
Cdd:PLN02221 239 aarlivkergevvaqlkaakaskeeitaavaelkiakeslahieersklkpglpkkdgkidyskdFFGRQAFLTVSGQLQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 254 KQMCICAdFEKVFCIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVveEIADTLVQ-IFKGLQKRFQTEIQTVNKQF 332
Cdd:PLN02221 319 VETYACA-LSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFADLEDDM--NCAEAYVKyMCKWLLDKCFDDMELMAKNF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 333 PCEPFKFLE-----PTLRLEYCEALAMLREAgIEMGDEE--------DLSTPNEKLLGRLVKEKYdtdfYILDKYPLAVR 399
Cdd:PLN02221 396 DSGCIDRLRmvastPFGRITYTEAIELLEEA-VAKGKEFdnnvewgiDLASEHERYLTEVLFQKP----LIVYNYPKGIK 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 400 PFYtMPDPRNPKQSNSYDMFM-RGEEILSGAQRIHDPQLVTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTM 478
Cdd:PLN02221 471 AFY-MRLNDDEKTVAAMDVLVpKVGELIGGSQREERYDVIKQRIEEMGLPIEPYEWYLDLRRYGTVKHCGFGLGFERMIL 549
|
570 580
....*....|....*....|
gi 78045531 479 LFLGLHNVRQTSMFPRDPKR 498
Cdd:PLN02221 550 FATGIDNIRDVIPFPRYPGK 569
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
60-493 |
3.58e-23 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 102.45 E-value: 3.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 60 VWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMVKFAANINKESIVDVEGVVRKVNQKigsctqqDVELHV 139
Cdd:PRK12445 68 VSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVYNDQFKKWDLGDIIGARGTLFKTQTG-------ELSIHC 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 140 QKIYVISSAEPRLPlqlddavrpevegeEEGRATVNQDTRLDNRVIDL-RTSTSQAIFRLQSGICHPFRETLTNKGFVEI 218
Cdd:PRK12445 141 TELRLLTKALRPLP--------------DKFHGLQDQEVRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMVARGFMEV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 219 QTPKIISAASEGGANVFTVSY--FKNNAYLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNThRHLTEFVGLDIEMAFN 296
Cdd:PRK12445 207 ETPMMQVIPGGASARPFITHHnaLDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISV-RHNPEFTMMELYMAYA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 297 yHYHEVVEeIADTLvqiFKGLQkrfQTEIQTVNKQFPCEPFKFLEPTLRLEYCEALAMLR-----------EAGIEMGDE 365
Cdd:PRK12445 286 -DYHDLIE-LTESL---FRTLA---QEVLGTTKVTYGEHVFDFGKPFEKLTMREAIKKYRpetdmadldnfDAAKALAES 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 366 EDLSTPNEKLLGRLVKEKYD-------TDFYILDKYPLAVRPFYTMPDPrNPKQSNSYDMFMRGEEILSGAQRIHDPQLV 438
Cdd:PRK12445 358 IGITVEKSWGLGRIVTEIFDevaeahlIQPTFITEYPAEVSPLARRNDV-NPEITDRFEFFIGGREIGNGFSELNDAEDQ 436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78045531 439 TER------ALHHGIDLEKI--KAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 493
Cdd:PRK12445 437 AERfqeqvnAKAAGDDEAMFydEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
196-493 |
1.15e-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: 95.73 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 196 FRLQSGICHPFRETLTNKGFVEIQTPKIISAAseGGANV--FTVSY--FKNNAYLAQSPQLYKQMCICADFEKVFCIGPV 271
Cdd:cd00775 8 FIVRSKIISYIRKFLDDRGFLEVETPMLQPIA--GGAAArpFITHHnaLDMDLYLRIAPELYLKRLIVGGFERVYEIGRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 272 FRAEDSNThRHLTEFVGLDIEMAF-NYH-YHEVVEEIADTLVQ-IFKGLQKRFQTEIQTVNKqfpcePFKfleptlRLEY 348
Cdd:cd00775 86 FRNEGIDL-THNPEFTMIEFYEAYaDYNdMMDLTEDLFSGLVKkINGKTKIEYGGKELDFTP-----PFK------RVTM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 349 CEALAmlREAGIEMGDEEDLSTPN-EKLLGRLVKEKYD---TDFYILDK------------------YPLAVRPFyTMPD 406
Cdd:cd00775 154 VDALK--EKTGIDFPELDLEQPEElAKLLAKLIKEKIEkprTLGKLLDKlfeefveptliqptfiidHPVEISPL-AKRH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 407 PRNPKQSNSYDMFMRGEEILSGAQRIHDPQLVTER-----ALHHGIDLEKI---KAYIDSFRFGAPPHAGGGIGLERVTM 478
Cdd:cd00775 231 RSNPGLTERFELFICGKEIANAYTELNDPFDQRERfeeqaKQKEAGDDEAMmmdEDFVTALEYGMPPTGGLGIGIDRLVM 310
|
330
....*....|....*
gi 78045531 479 LFLGLHNVRQTSMFP 493
Cdd:cd00775 311 LLTDSNSIRDVILFP 325
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
239-496 |
2.07e-21 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 97.40 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 239 YFKNNAYLAQSPQLYKQMcICADFEKVFCIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVveEIADTLVQIFKG-- 316
Cdd:PTZ00425 321 FFSKQAFLTVSGQLSLEN-LCSSMGDVYTFGPTFRAENSHTSRHLAEFWMIEPEIAFADLYDNM--ELAESYIKYCIGyv 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 317 LQKRFQtEIQTVNKQFPCEPFKFLEPTL-----RLEYCEALAMLR------EAGIEMGdeEDLSTPNEkllgRLVKEKYD 385
Cdd:PTZ00425 398 LNNNFD-DIYYFEENVETGLISRLKNILdedfaKITYTNVIDLLQpysdsfEVPVKWG--MDLQSEHE----RFVAEQIF 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 386 TDFYILDKYPLAVRPFYtMPDPRNPKQSNSYDMFM-RGEEILSGAQRIHDPQLVTERALHHGIDLEKIKAYIDSFRFGAP 464
Cdd:PTZ00425 471 KKPVIVYNYPKDLKAFY-MKLNEDQKTVAAMDVLVpKIGEVIGGSQREDNLERLDKMIKEKKLNMESYWWYRQLRKFGSH 549
|
250 260 270
....*....|....*....|....*....|..
gi 78045531 465 PHAGGGIGLERVTMLFLGLHNVRQTSMFPRDP 496
Cdd:PTZ00425 550 PHAGFGLGFERLIMLVTGVDNIKDTIPFPRYP 581
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
175-493 |
5.31e-18 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 86.99 E-value: 5.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 175 NQDTRLDNRVIDLRTS-TSQAIFRLQSGICHPFRETLTNKGFVEIQTPKIISAAseGGANVFTVSYFKNNA----YLAQS 249
Cdd:PTZ00417 231 DTEIRYRQRYLDLMINeSTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVA--GGANARPFITHHNDLdldlYLRIA 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 250 PQLYKQMCICADFEKVFCIGPVFRAED-SNTHRhlTEFVGLDIEMAFNyHYHEVVEEIADTLVQIFKGLqkrFQTEIQTV 328
Cdd:PTZ00417 309 TELPLKMLIVGGIDKVYEIGKVFRNEGiDNTHN--PEFTSCEFYWAYA-DFYDLIKWSEDFFSQLVMHL---FGTYKILY 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 329 NKQFP-CEPFK--FLEPTLRLEYCEALAMLREAGIE--------------MGDEEDLSTPN----EKLLGRLVKEkydtd 387
Cdd:PTZ00417 383 NKDGPeKDPIEidFTPPYPKVSIVEELEKLTNTKLEqpfdspetinkminLIKENKIEMPNpptaAKLLDQLASH----- 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 388 fYILDKYPlaVRPFYTMPDPR-----------NPKQSNSYDMFMRGEEILSGAQRIHDPQLVTERALHHGIDLEKIKA-- 454
Cdd:PTZ00417 458 -FIENKYP--NKPFFIIEHPQimsplakyhrsKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAea 534
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 78045531 455 ------YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 493
Cdd:PTZ00417 535 fqfdaaFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFP 579
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
235-494 |
1.42e-17 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 85.69 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 235 FTVSYFKNNAYLAQSPQLYKQMCICAdFEKVFCIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYhyhevVEEIADTLVQIF 314
Cdd:PLN02532 363 FSKDFFSRPTYLTVSGRLHLESYACA-LGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFSE-----LEDAMNCAEDYF 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 315 KGLQKRF----QTEIQTVNKQFPCEPFKFLE-----PTLRLEYCEALAMLREA---GIEMGDEEDLSTPNEKLlGRLVKE 382
Cdd:PLN02532 437 KFLCKWVlencSEDMKFVSKRIDKTISTRLEaiissSLQRISYTEAVDLLKQAtdkKFETKPEWGIALTTEHL-SYLADE 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 383 KYDTDFYILDkYPLAVRPFYTMPDpRNPKQSNSYDMFM-RGEEILSGAQRIHDPQLVTERALHHGIDLEKIKAYIDSFRF 461
Cdd:PLN02532 516 IYKKPVIIYN-YPKELKPFYVRLN-DDGKTVAAFDLVVpKVGTVITGSQNEERMDILNARIEELGLPREQYEWYLDLRRH 593
|
250 260 270
....*....|....*....|....*....|...
gi 78045531 462 GAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPR 494
Cdd:PLN02532 594 GTVKHSGFSLGFELMVLFATGLPDVRDAIPFPR 626
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
60-146 |
3.19e-17 |
|
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. Class 2b aaRSs include the homodimeric aspartyl-, asparaginyl-, and lysyl-tRNA synthetases (AspRS, AsnRS, and LysRS). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Included in this group are archeal and archeal-like AspRSs which are non-discriminating and can charge both tRNAAsp and tRNAAsn. E. coli cells have two isoforms of LysRSs (LysS and LysU) encoded by two distinct genes, which are differentially regulated. The cytoplasmic and the mitochondrial isoforms of human LysRS are encoded by a single gene. Yeast cytoplasmic and mitochondrial LysRSs participate in mitochondrial import of cytoplasmic tRNAlysCUU. In addition to their housekeeping role, human LysRS may function as a signaling molecule that activates immune cells. Tomato LysRS may participate in a process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging. AsnRS is immunodominant antigen of the filarial nematode Brugia malayai and is of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.
Pssm-ID: 239766 [Multi-domain] Cd Length: 85 Bit Score: 76.45 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 60 VWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASkqMVKFAANINKESIVDVEGVVRKVnqKIGSCTQQDVELHV 139
Cdd:cd04100 2 VTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELGE--FFEEAEKLRTESVVGVTGTVVKR--PEGNLATGEIELQA 77
|
....*..
gi 78045531 140 QKIYVIS 146
Cdd:cd04100 78 EELEVLS 84
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
57-493 |
2.96e-15 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 78.11 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 57 GEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMV--KFAANINKESIVDVEGVVRKvnQKIGsctqqD 134
Cdd:PLN02502 108 DVSVSVAGRIMAKRAFGKLAFYDLRDDGGKIQLYADKKRLDLDEEEfeKLHSLVDRGDIVGVTGTPGK--TKKG-----E 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 135 VELHVQKIYVISSA---EPRLPLQLDDavrpevegeeegratvnQDTRLDNRVIDLRTSTSQA-IFRLQSGICHPFRETL 210
Cdd:PLN02502 181 LSIFPTSFEVLTKCllmLPDKYHGLTD-----------------QETRYRQRYLDLIANPEVRdIFRTRAKIISYIRRFL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 211 TNKGFVEIQTPKIISAAseGGANVFTVSYFKN----NAYLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNThRHLTEF 286
Cdd:PLN02502 244 DDRGFLEVETPMLNMIA--GGAAARPFVTHHNdlnmDLYLRIATELHLKRLVVGGFERVYEIGRQFRNEGIST-RHNPEF 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 287 VGLDIEMAF-NYH-YHEVVEEIADTLV-QIFKGLQKRFQ-TEIQTVnkqfpcEPFK------FLEPTLRLEYCEAL--AM 354
Cdd:PLN02502 321 TTCEFYQAYaDYNdMMELTEEMVSGMVkELTGSYKIKYHgIEIDFT------PPFRrismisLVEEATGIDFPADLksDE 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 355 LREAGIEMGDEEDLSTPN--------EKLLGRLVKEKYDTDFYILDkYPLAVRPFyTMPDPRNPKQSNSYDMFMRGEEIL 426
Cdd:PLN02502 395 ANAYLIAACEKFDVKCPPpqttgrllNELFEEFLEETLVQPTFVLD-HPVEMSPL-AKPHRSKPGLTERFELFINGRELA 472
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78045531 427 SGAQRIHDPqlVTERAL-------HHGIDLEKI---KAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 493
Cdd:PLN02502 473 NAFSELTDP--VDQRERfeeqvkqHNAGDDEAMaldEDFCTALEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFP 547
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
56-493 |
3.25e-15 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 78.85 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 56 AGEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMVKFAANINKESIVDVEGVVrkVNQKIGSCTqqdv 135
Cdd:PRK02983 650 TGEEVSVSGRVLRIRDYGGVLFADLRDWSGELQVLLDASRLEQGSLADFRAAVDLGDLVEVTGTM--GTSRNGTLS---- 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 136 eLHVQKIYVISSAEPRLPlqlddavrpevegeEEGRATVNQDTRLDNRVIDLRTST-SQAIFRLQSGICHPFRETLTNKG 214
Cdd:PRK02983 724 -LLVTSWRLAGKCLRPLP--------------DKWKGLTDPEARVRQRYLDLAVNPeARDLLRARSAVVRAVRETLVARG 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 215 FVEIQTPkiISAASEGGANV--FTVSYfknNAY-----LAQSPQLY-KQMCIcADFEKVFCIGPVFRAE----------- 275
Cdd:PRK02983 789 FLEVETP--ILQQVHGGANArpFVTHI---NAYdmdlyLRIAPELYlKRLCV-GGVERVFELGRNFRNEgvdathnpeft 862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 276 ---------DSNTHRHLTEfvGLDIEMAFNYHYHEVV----EEIADTLVQI---------FKGLQKRFQTEIQtvnkqfP 333
Cdd:PRK02983 863 lleayqahaDYDTMRDLTR--ELIQNAAQAAHGAPVVmrpdGDGVLEPVDIsgpwpvvtvHDAVSEALGEEID------P 934
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 334 CEPFkflePTLRlEYCEAlamlreAGIEMGDEEDLSTPNEKLLGRLVkEKYDTD--FYIldKYPLAVRPFyTMPDPRNPK 411
Cdd:PRK02983 935 DTPL----AELR-KLCDA------AGIPYRTDWDAGAVVLELYEHLV-EDRTTFptFYT--DFPTSVSPL-TRPHRSDPG 999
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 412 QSNSYDMFMRGEEILSGAQRIHDPqlVTERA-------LHHGIDLEKI---KAYIDSFRFGAPPHAGGGIGLERVTMLFL 481
Cdd:PRK02983 1000 LAERWDLVAWGVELGTAYSELTDP--VEQRRrlteqslLAAGGDPEAMeldEDFLQALEYAMPPTGGLGMGVDRLVMLLT 1077
|
490
....*....|..
gi 78045531 482 GLhNVRQTSMFP 493
Cdd:PRK02983 1078 GR-SIRETLPFP 1088
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
65-493 |
7.84e-15 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 76.67 E-value: 7.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 65 RVHTSRAKGKQCFLVLRQQQFNVQALVAVgDHASKQMVKFAANINKESIVDVEGVVRKvnqkigscTQQDvEL--HVQKI 142
Cdd:PRK00484 62 RVMLKRVMGKASFATLQDGSGRIQLYVSK-DDVGEEALEAFKKLDLGDIIGVEGTLFK--------TKTG-ELsvKATEL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 143 YVISSAepRLPLqlddavrPEV-EGEEegratvNQDTRLDNRVIDLRTS-TSQAIFRLQSGICHPFRETLTNKGFVEIQT 220
Cdd:PRK00484 132 TLLTKS--LRPL-------PDKfHGLT------DVETRYRQRYVDLIVNpESRETFRKRSKIISAIRRFLDNRGFLEVET 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 221 PKIISAAseGGANV--FTVSYfknNA-----YLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNThRHLTEFVGLDIEM 293
Cdd:PRK00484 197 PMLQPIA--GGAAArpFITHH---NAldidlYLRIAPELYLKRLIVGGFERVYEIGRNFRNEGIDT-RHNPEFTMLEFYQ 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 294 AF-NYH---------YHEVVEEIADTLVQIFKGlqkrfqTEIqTVNKQFPCEPFK----------FLEPTLRleycEALA 353
Cdd:PRK00484 271 AYaDYNdmmdlteelIRHLAQAVLGTTKVTYQG------TEI-DFGPPFKRLTMVdaikeytgvdFDDMTDE----EARA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 354 MLREAGIEMGDEEDLSTPNEKLLGRLVKEKYDTDFYILDkYPLAVRPFyTMPDPRNPKQSNSYDMFMRGEEILSGAQRIH 433
Cdd:PRK00484 340 LAKELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITD-YPVEISPL-AKRHREDPGLTERFELFIGGREIANAFSELN 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78045531 434 DP--QL------VTERAL----HHGIDLEkikaYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 493
Cdd:PRK00484 418 DPidQRerfeaqVEAKEAgddeAMFMDED----FLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
48-154 |
7.58e-12 |
|
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: 61.95 E-value: 7.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 48 ISDLTVQKAGEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQaLVAVGDHASKQMVKFAANINKESIVDVEGVVRKVNQKI 127
Cdd:cd04316 3 SAEITPELDGEEVTVAGWVHEIRDLGGIKFVILRDREGIVQ-VTAPKKKVDKELFKTVRKLSRESVISVTGTVKAEPKAP 81
|
90 100
....*....|....*....|....*..
gi 78045531 128 GsctqqDVELHVQKIYVISSAEPRLPL 154
Cdd:cd04316 82 N-----GVEIIPEEIEVLSEAKTPLPL 103
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
48-188 |
1.45e-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: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 48 ISDLTVQKAGEVV----WVrarvHTSRAKGKQCFLVLRQQQFNVQALVavgDHASKQMVKFAANINKESIVDVEGVVRK- 122
Cdd:cd04317 5 CGELRESHVGQEVtlcgWV----QRRRDHGGLIFIDLRDRYGIVQVVF---DPEEAPEFELAEKLRNESVIQVTGKVRAr 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 123 ----VNQKIGSctqQDVELHVQKIYVISSAEPrLPLQLDDAVrpevegeeegraTVNQDTRLDNRVIDLR 188
Cdd:cd04317 78 pegtVNPKLPT---GEIEVVASELEVLNKAKT-LPFEIDDDV------------NVSEELRLKYRYLDLR 131
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
206-321 |
2.71e-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: 57.13 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 206 FRETLTNKGFVEIQTPKIISAASEGGAN------VFTVSYFKNNAYLAQSPQLYKQM----CICADFEKVFCIGPVFRAE 275
Cdd:cd00768 9 LRRFMAELGFQEVETPIVEREPLLEKAGhepkdlLPVGAENEEDLYLRPTLEPGLVRlfvsHIRKLPLRLAEIGPAFRNE 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 78045531 276 DSNTH-RHLTEFVGLDIEMAF-----NYHYHEVVEEIADTLVQIFKGLQKRF 321
Cdd:cd00768 89 GGRRGlRRVREFTQLEGEVFGedgeeASEFEELIELTEELLRALGIKLDIVF 140
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
60-145 |
2.76e-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: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 60 VWVRARVHT-SRAKGKQCFLVLRQQQFNVQALVAvgdhaSKQMVKFAANINKESIVDVEGVVRKVNQKigsctqqDVELH 138
Cdd:pfam01336 1 VTVAGRVTSiRRSGGKLLFLTLRDGTGSIQVVVF-----KEEAEKLAKKLKEGDVVRVTGKVKKRKGG-------ELELV 68
|
....*..
gi 78045531 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 |
4.94e-05 |
|
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus horikoshii AsnRS asparaginyl-tRNA synthetase (AsnRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The archeal enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose.
Pssm-ID: 239814 [Multi-domain] Cd Length: 103 Bit Score: 42.51 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 60 VWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAvgDHASKQMVKFAANINKESIVDVEGVVRKVNQKIGSctqqdVELHV 139
Cdd:cd04319 2 VTLAGWVYRKREVGKKAFIVLRDSTGIVQAVFS--KDLNEEAYREAKKVGIESSVIVEGAVKADPRAPGG-----AEVHG 74
|
90
....*....|.
gi 78045531 140 QKIYVISSAEP 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 |
5.37e-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: 36.06 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78045531 60 VWVRARVHTSRAKGKQCFLVLRQQQFNVQAlVAVGDHASKQMVkfAANINKESIVDVEGVVRKVNQkiGSCTQQDVELHV 139
Cdd:cd04323 2 VKVFGWVHRLRSQKKLMFLVLRDGTGFLQC-VLSKKLVTEFYD--AKSLTQESSVEVTGEVKEDPR--AKQAPGGYELQV 76
|
....*..
gi 78045531 140 QKIYVIS 146
Cdd:cd04323 77 DYLEIIG 83
|
|
| |
