|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
1-468 |
0e+00 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 714.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 1 MIQSQEKPD-RVLVRVRDLTIQKADEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGD-HASKQMVKFAANINKE 78
Cdd:PLN02850 57 LEELQSKVTgREWTDVSDLGEELAGSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQCVVFVSEvTVSKGMVKYAKQLSRE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 79 SIVDVEGVVRKVNQKIGSCTQQdVELHVQKIYVISLAEPRLPLQLDDA-----VRPEAEGEEEGRATVNQDTRLDNRVID 153
Cdd:PLN02850 137 SVVDVEGVVSVPKKPVKGTTQQ-VEIQVRKIYCVSKALATLPFNVEDAarsesEIEKALQTGEQLVRVGQDTRLNNRVLD 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 154 LRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLYKQMCICADFEKVF 233
Cdd:PLN02850 216 LRTPANQAIFRIQSQVCNLFREFLLSKGFVEIHTPKLIAGASEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGDFRRVF 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 234 CIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVMEEIADTMVQIFKGLQERFQTEIQTVNKQFPCEPFKFLEPTLRL 313
Cdd:PLN02850 296 EIGPVFRAEDSFTHRHLCEFTGLDLEMEIKEHYSEVLDVVDELFVAIFDGLNERCKKELEAIREQYPFEPLKYLPKTLRL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 314 EYCEALAMLREAGVEMGDEDDLSTPNEKLLGHLVKEKYDTDFYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEIL 393
Cdd:PLN02850 376 TFAEGIQMLKEAGVEVDPLGDLNTESERKLGQLVKEKYGTDFYILHRYPLAVRPFYTMPCPDDPKYSNSFDVFIRGEEII 455
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622849660 394 SGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 468
Cdd:PLN02850 456 SGAQRVHDPELLEKRAEECGIDVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQRLAP 530
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
1-468 |
0e+00 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 516.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 1 MIQSQEKPDRVLVRVRDLTIQK-ADEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMVKFAANINKES 79
Cdd:PTZ00401 54 MVQSTTYKSRTFIPVAVLSKPElVDKTVLIRARVSTTRKKGKMAFMVLRDGSDSVQAMAAVEGDVPKEMIDFIGQIPTES 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 80 IVDVEGVVRKVNQKIGSCTQQDVELHVQKIYVISLAEPRLPLQLDDAvrpeAEGEEEGRATVNQDTRLDNRVIDLRTSTS 159
Cdd:PTZ00401 134 IVDVEATVCKVEQPITSTSHSDIELKVKKIHTVTESLRTLPFTLEDA----SRKESDEGAKVNFDTRLNSRWMDLRTPAS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 160 QAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLYKQMCICADFEKVFCIGPVF 239
Cdd:PTZ00401 210 GAIFRLQSRVCQYFRQFLIDSDFCEIHSPKIINAPSEGGANVFKLEYFNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVF 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 240 RAEDSNTHRHLTEFVGLDIEMAFNYHYHEVMeeiaDTMVQIFKGLQERFQT---EIQTVNKQFPCEPFKF---------- 306
Cdd:PTZ00401 290 RSENSNTHRHLTEFVGLDVEMRINEHYYEVL----DLAESLFNYIFERLAThtkELKAVCQQYPFEPLVWkltpermkel 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 307 --------LEPT--------------LRLEYCEALAMLREAGVE-MGDEDDLSTPNEKLLGHLVKEKYDTDFYILDKYPL 363
Cdd:PTZ00401 366 gvgvisegVEPTdkyqarvhnmdsrmLRINYMHCIELLNTVLEEkMAPTDDINTTNEKLLGKLVKERYGTDFFISDRFPS 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 364 AVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERV 443
Cdd:PTZ00401 446 SARPFYTMECKDDERFTNSYDMFIRGEEISSGAQRIHDPDLLLARAKMLNVDLTPIKEYVDSFRLGAWPHGGFGVGLERV 525
|
490 500
....*....|....*....|....*
gi 1622849660 444 TMLFLGLHNVRQTSMFPRDPKRLTP 468
Cdd:PTZ00401 526 VMLYLGLSNVRLASLFPRDPQRTTP 550
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
141-464 |
3.09e-176 |
|
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: 496.32 E-value: 3.09e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 141 VNQDTRLDNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLY 220
Cdd:cd00776 2 ANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 221 KQMCICAdFEKVFCIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVMEEIADTMVQIFKGLQERFQTEIQTVNkQFP 300
Cdd:cd00776 82 KEMLIAA-LERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRVLERCAKELELVN-QLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 301 CEPFKFLEPTLRLEYCEALAMLREAGV--EMGDEDDLSTPNEKLLGhlvkEKYDTDFYILDKYPLAVRPFYTMPDPRNPK 378
Cdd:cd00776 160 RELLKPLEPFPRITYDEAIELLREKGVeeEVKWGEDLSTEHERLLG----EIVKGDPVFVTDYPKEIKPFYMKPDDDNPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 379 QSNSYDMFMRG-EEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTS 457
Cdd:cd00776 236 TVESFDLLMPGvGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAI 315
|
....*..
gi 1622849660 458 MFPRDPK 464
Cdd:cd00776 316 LFPRDPK 322
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
13-468 |
1.55e-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: 478.55 E-value: 1.55e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 13 VRVRDLTIQKADEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQaLVAVGDHASKQMVKFAANINKESIVDVEGVVrkvnq 92
Cdd:TIGR00458 1 VYSADIKPEMDGQEVTFMGWVHEIRDLGGLIFVLLRDREGLIQ-ITAPAKKVSKNLFKWAKKLNLESVVAVRGIV----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 93 KIGSCTQQDVELHVQKIYVISLAEPRLPLQLDDAVRPEAegeeegratvnqDTRLDNRVIDLRTSTSQAVFRLQSGICHL 172
Cdd:TIGR00458 75 KIKEKAPGGFEIIPTKIEVINEAKEPLPLDPTEKVPAEL------------DTRLDYRFLDLRRPTVQAIFRIRSGVLES 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 173 FRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNTHRHLTE 252
Cdd:TIGR00458 143 VREFLAEEGFIEVHTPKLVASATEGGTELFPITYFEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHRHLNE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 253 FVGLDIEMAFNYHyHEVMEEIADTMVQIFKGLQERFQTEIQTVNKQFPCEPFKFleptLRLEYCEALAMLREAGVEMGDE 332
Cdd:TIGR00458 223 ATSIDIEMAFEDH-HDVMDILEELVVRVFEDVPERCAHQLETLEFKLEKPEGKF----VRLTYDEAIEMANAKGVEIGWG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 333 DDLSTPNEKLLGhlvkEKYDTDFYILDkYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHH 412
Cdd:TIGR00458 298 EDLSTEAEKALG----EEMDGLYFITD-WPTEIRPFYTMPDEDNPEISKSFDLMYRDLEISSGAQRIHLHDLLVERIKAK 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849660 413 GIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 468
Cdd:TIGR00458 373 GLNPEGFKDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRKRLTP 428
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
15-468 |
1.97e-160 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 460.81 E-value: 1.97e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 15 VRDLTIQKADEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDhaSKQMVKFAANINKESIVDVEGVVRKVNQKI 94
Cdd:PRK05159 7 TSELTPELDGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKV--DEELFETIKKLKRESVVSVTGTVKANPKAP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 95 GSctqqdVELHVQKIYVISLAEPRLPLQLDDAVRPEAegeeegratvnqDTRLDNRVIDLRTSTSQAVFRLQSGICHLFR 174
Cdd:PRK05159 85 GG-----VEVIPEEIEVLNKAEEPLPLDISGKVLAEL------------DTRLDNRFLDLRRPRVRAIFKIRSEVLRAFR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 175 ETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNTHRHLTEFV 254
Cdd:PRK05159 148 EFLYENGFTEIFTPKIVASGTEGGAELFPIDYFEKEAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRHLNEYT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 255 GLDIEMAFNYHYHEVMEEIADTMVQIFKGLQERFQTEIQTVNKQFPCEPfkflEPTLRLEYCEALAMLREAGVEMGDEDD 334
Cdd:PRK05159 228 SIDVEMGFIDDHEDVMDLLENLLRYMYEDVAENCEKELELLGIELPVPE----TPIPRITYDEAIEILKSKGNEISWGDD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 335 LSTPNEKLLGHLVKEKYDTDFYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGI 414
Cdd:PRK05159 304 LDTEGERLLGEYVKEEYGSDFYFITDYPSEKRPFYTMPDEDDPEISKSFDLLFRGLEITSGGQRIHRYDMLVESIKEKGL 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1622849660 415 DLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 468
Cdd:PRK05159 384 NPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPRDRHRLTP 437
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
13-468 |
2.03e-159 |
|
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: 457.98 E-value: 2.03e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 13 VRVRDLTIQKADEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMVKfaaNINKESIVDVEGVVRKVNQ 92
Cdd:COG0017 3 TYIKDLLPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKLENFEEAK---KLTTESSVEVTGTVVESPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 93 KigsctQQDVELHVQKIYVISLAEPRLPLQLDDAvrpeaegeeegratvNQDTRLDNRVIDLRTSTSQAVFRLQSGICHL 172
Cdd:COG0017 80 A-----PQGVELQAEEIEVLGEADEPYPLQPKRH---------------SLEFLLDNRHLRLRTNRFGAIFRIRSELARA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 173 FRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLYKQMCICAdFEKVFCIGPVFRAEDSNTHRHLTE 252
Cdd:COG0017 140 IREFFQERGFVEVHTPIITASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMA-LEKVYTFGPTFRAEKSNTRRHLAE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 253 FVGLDIEMAFnYHYHEVMEEIADTMVQIFKGLQERFQTEIQTVN------KQFPCEPFKfleptlRLEYCEALAMLREAG 326
Cdd:COG0017 219 FWMIEPEMAF-ADLEDVMDLAEEMLKYIIKYVLENCPEELEFLGrdverlEKVPESPFP------RITYTEAIEILKKSG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 327 VEMGDEDDLSTPNEKLLGhlvkEKYDTDFYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRG-EEILSGAQRIHDPQLL 405
Cdd:COG0017 292 EKVEWGDDLGTEHERYLG----EEFFKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGiGEIIGGSQREHRYDVL 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622849660 406 TERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 468
Cdd:COG0017 368 VERIKEKGLDPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
142-463 |
8.13e-103 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 309.50 E-value: 8.13e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 142 NQDTRLDNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNN--AYLAQSPQL 219
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGkfYALPQSPQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 220 YKQMCICADFEKVFCIGPVFRAEDSNTHRHLtEFVGLDIEMAFNyHYHEVMEEIADTMVQIFKGLQERFQTEIQTVNKQF 299
Cdd:pfam00152 81 YKQLLMVAGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFV-DYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 300 PcEPFKfleptlRLEYCEALAMLREAGVEMGDEDdLSTPNEKLLGHLVKEKYDTDFYILDKYPLAVRPFYTMPDPRNPKQ 379
Cdd:pfam00152 159 K-KPFP------RITYAEAIEKLNGKDVEELGYG-SDKPDLRFLLELVIDKNKFNPLWVTDFPAEHHPFTMPKDEDDPAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 380 SNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGIDLEKIKA----YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQ 455
Cdd:pfam00152 231 AEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPEEAEEkfgfYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIRE 310
|
....*...
gi 1622849660 456 TSMFPRDP 463
Cdd:pfam00152 311 VIAFPKTR 318
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
13-468 |
8.11e-81 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 257.34 E-value: 8.11e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 13 VRVRDLTIQK-ADEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQmvKFAANINKESIVDVEGVVRKVN 91
Cdd:PRK03932 4 VSIKDILKGKyVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDNGEEYF--EEIKKLTTGSSVIVTGTVVESP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 92 QKigsctQQDVELHVQKIYVISLAEPRLPLQLDDAvrpeaegeeegratvNQDTRLDNRVIDLRTSTSQAVFRLQSGICH 171
Cdd:PRK03932 82 RA-----GQGYELQATKIEVIGEDPEDYPIQKKRH---------------SIEFLREIAHLRPRTNKFGAVMRIRNTLAQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 172 LFRETLINKGFVEIQTPKIISAASEGGANVFTVS---------YFKNNAYLAQSPQLYKQMCICAdFEKVFCIGPVFRAE 242
Cdd:PRK03932 142 AIHEFFNENGFVWVDTPIITASDCEGAGELFRVTtldldfskdFFGKEAYLTVSGQLYAEAYAMA-LGKVYTFGPTFRAE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 243 DSNTHRHLTEFVGLDIEMAFnYHYHEVMEeIADTMVQ-IFKGLQERFQTEIQTVNKQFPCEPFKFLEPTL-----RLEYC 316
Cdd:PRK03932 221 NSNTRRHLAEFWMIEPEMAF-ADLEDNMD-LAEEMLKyVVKYVLENCPDDLEFLNRRVDKGDIERLENFIespfpRITYT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 317 EALAMLREAG------VEMGDedDLSTPNEKLLghlVKEKYDTDFYILDkYPLAVRPFYTMPDPRNpKQSNSYDMFMRG- 389
Cdd:PRK03932 299 EAIEILQKSGkkfefpVEWGD--DLGSEHERYL---AEEHFKKPVFVTN-YPKDIKAFYMRLNPDG-KTVAAMDLLAPGi 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849660 390 EEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 468
Cdd:PRK03932 372 GEIIGGSQREERLDVLEARIKELGLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
21-468 |
3.08e-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: 240.36 E-value: 3.08e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 21 QKADEVVWVRARVHTSRAKGKQCFLVLRQQQF--NVQALVAVGDhaSKQMVKFAANINKESIVDVEGVVRKVNQKigsct 98
Cdd:TIGR00457 13 KFVGDEVTVSGWVRTKRSSKKIIFLELNDGSSlgPIQAVINGED--NPYLFQLLKSLTTGSSVSVTGKVVESPGK----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 99 QQDVELHVQKIYVISLAEPR-LPLQLDDavrpeaegeeegratvnQDTRL--DNRVIDLRTSTSQAVFRLQSGICHLFRE 175
Cdd:TIGR00457 86 GQPVELQVKKIEVVGEAEPDdYPLQKKE-----------------HSLEFlrDIAHLRLRTNTLGAVMRVRNALSQAIHR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 176 TLINKGFVEIQTPKIISAASEGGANVFTVS---------YFKNNAYLAQSPQLYKQMCICAdFEKVFCIGPVFRAEDSNT 246
Cdd:TIGR00457 149 YFQENGFTWVSPPILTSNDCEGAGELFRVStgnidfsqdFFGKEAYLTVSGQLYLETYALA-LSKVYTFGPTFRAEKSNT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 247 HRHLTEFVGLDIEMAFnYHYHEVMEEIADTMVQIFKGLQERFQTEIQTVNKQFPCEPFKFLEPTL-----RLEYCEALAM 321
Cdd:TIGR00457 228 SRHLSEFWMIEPEMAF-ANLNDLLQLAETLIKYIIKAVLENCSQELKFLEKNFDKDLIKRLENIInnkfaRITYTDAIEI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 322 LREAGVEMGDED----DLSTPNEKLLGhlvkEKYDTDFYILDKYPLAVRPFYtMPDPRNPKQSNSYDMFMRG-EEILSGA 396
Cdd:TIGR00457 307 LKESDKNFEYEDfwgdDLQTEHERFLA----EEYFKPPVFVTNYPKDIKAFY-MKLNDDGKTVAAMDLLAPGiGEIIGGS 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622849660 397 QRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP 468
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 ... |
163-462 |
2.06e-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: 193.46 E-value: 2.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 163 FRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFK--NNAYLAQSPQLYKQMCICADFEKVFCIGPVFR 240
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNAlgLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 241 AEDSNThRHLTEFVGLDIEMAFNyHYHEVMEEIADTMVQIFKGLQErfqteiqTVNKQFPCEPFKFLEPTLRLEYCEALA 320
Cdd:cd00669 81 NEDLRA-RHQPEFTMMDLEMAFA-DYEDVIELTERLVRHLAREVLG-------VTAVTYGFELEDFGLPFPRLTYREALE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 321 MLREagvemgdeddlstpnekllghlvkekydtdFYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIH 400
Cdd:cd00669 152 RYGQ------------------------------PLFLTDYPAEMHSPLASPHDVNPEIADAFDLFINGVEVGNGSSRLH 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849660 401 DPQLLTERALHHGID----LEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRD 462
Cdd:cd00669 202 DPDIQAEVFQEQGINkeagMEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKM 267
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
143-463 |
4.77e-51 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 175.98 E-value: 4.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 143 QDTRLDNRVIdLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPkIISA--------ASEGGANVFTVSYFKNNAYLA 214
Cdd:PRK06462 11 EEFLRMSWKH-ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPP-IISPstdplmglGSDLPVKQISIDFYGVEYYLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 215 QSPQLYKQMCIcADFEKVFCIGPVFRAE--DSNTHRHLTEFVGLDIEMAfNYHYHEVMEEIADTMVQIFKGLQERFQTEI 292
Cdd:PRK06462 89 DSMILHKQLAL-RMLGKIFYLSPNFRLEpvDKDTGRHLYEFTQLDIEIE-GADLDEVMDLIEDLIKYLVKELLEEHEDEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 293 QTVNKQFPcepfKFLEPTLRLEYCEALAMLREAGVEMGDEDDLSTPNEKLLghlvKEKYDTDFYILDkYPLAVRPFYTMP 372
Cdd:PRK06462 167 EFFGRDLP----HLKRPFKRITHKEAVEILNEEGCRGIDLEELGSEGEKSL----SEHFEEPFWIID-IPKGSREFYDRE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 373 DPRNPKQSNSYDMFMR---GEeILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLG 449
Cdd:PRK06462 238 DPERPGVLRNYDLLLPegyGE-AVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICG 316
|
330
....*....|....
gi 1622849660 450 LHNVRQTSMFPRDP 463
Cdd:PRK06462 317 LRHIREVQPFPRVP 330
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
27-125 |
1.73e-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: 166.97 E-value: 1.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 27 VWVRARVHTSRAKG-KQCFLVLRQQQFNVQALVAVGDHA-SKQMVKFAANINKESIVDVEGVVRKVNQKIGSCTQQDVEL 104
Cdd:cd04320 2 VLIRARVHTSRAQGaKLAFLVLRQQGYTIQGVLAASAEGvSKQMVKWAGSLSKESIVDVEGTVKKPEEPIKSCTQQDVEL 81
|
90 100
....*....|....*....|.
gi 1622849660 105 HVQKIYVISLAEPRLPLQLDD 125
Cdd:cd04320 82 HIEKIYVVSEAAEPLPFQLED 102
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
17-460 |
1.24e-43 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 161.77 E-value: 1.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 17 DLTIQKADEVV----WVrarvHTSRAKGKQCFLVLRQQQFNVQALVavgdHASKQMVKFAANINKESIVDVEGVVRK--- 89
Cdd:PRK00476 10 ELRESHVGQTVtlcgWV----HRRRDHGGLIFIDLRDREGIVQVVF----DPDAEAFEVAESLRSEYVIQVTGTVRArpe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 90 --VNQKIGSctqQDVELHVQKIYVISLAEPrLPLQLDDAvrpeaegeeegrATVNQDTRLDNRVIDLRTSTSQAVFRLQS 167
Cdd:PRK00476 82 gtVNPNLPT---GEIEVLASELEVLNKSKT-LPFPIDDE------------EDVSEELRLKYRYLDLRRPEMQKNLKLRS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 168 GICHLFRETLINKGFVEIQTPkIISAASEGGANVFTV-S-YFKNNAY-LAQSPQLYKQMCICADFEKVFCIGPVFRAEDS 244
Cdd:PRK00476 146 KVTSAIRNFLDDNGFLEIETP-ILTKSTPEGARDYLVpSrVHPGKFYaLPQSPQLFKQLLMVAGFDRYYQIARCFRDEDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 245 NTHRhLTEFVGLDIEMAFnYHYHEVMEEIADTMVQIFKGL--------------QE------------RFQTEIQTVNKQ 298
Cdd:PRK00476 225 RADR-QPEFTQIDIEMSF-VTQEDVMALMEGLIRHVFKEVlgvdlptpfprmtyAEamrrygsdkpdlRFGLELVDVTDL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 299 FPCEPFK-FLEPT--------LRLEYC--------------------------------------------EALAMLREA 325
Cdd:PRK00476 303 FKDSGFKvFAGAAndggrvkaIRVPGGaaqlsrkqideltefakiygakglayikvnedglkgpiakflseEELAALLER 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 326 -GVEMGD-----EDDLSTPNE----------KLLGHLVKEKYD----TDFyildkyPL------AVR------PFyTMPD 373
Cdd:PRK00476 383 tGAKDGDliffgADKAKVVNDalgalrlklgKELGLIDEDKFAflwvVDF------PMfeydeeEGRwvaahhPF-TMPK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 374 P--------RNPKQ--SNSYDMFMRGEEILSGAQRIHDPQLLtERALHH-GIDLEKIKA----YIDSFRFGAPPHAGGGI 438
Cdd:PRK00476 456 DedldeletTDPGKarAYAYDLVLNGYELGGGSIRIHRPEIQ-EKVFEIlGISEEEAEEkfgfLLDALKYGAPPHGGIAF 534
|
570 580
....*....|....*....|..
gi 1622849660 439 GLERVTMLFLGLHNVRQTSMFP 460
Cdd:PRK00476 535 GLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
17-460 |
7.49e-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: 154.00 E-value: 7.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 17 DLTIQKADEVV----WVrarvHTSRAKGKQCFLVLR------QqqfnvqalVAVGDHASKQMVKFAANINKESIVDVEGV 86
Cdd:COG0173 9 ELRESDVGQEVtlsgWV----HRRRDHGGLIFIDLRdrygitQ--------VVFDPDDSAEAFEKAEKLRSEYVIAVTGK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 87 VRK-----VNQKI--GsctqqDVELHVQKIYVISLAEPrLPLQLDDAVRpeaegeeegratVNQDTRLDNRVIDLRTSTS 159
Cdd:COG0173 77 VRArpegtVNPKLptG-----EIEVLASELEILNKAKT-PPFQIDDDTD------------VSEELRLKYRYLDLRRPEM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 160 QAVFRLQSGICHLFRETLINKGFVEIQTPkIISAASEGGANVFTV-------SYFknnAyLAQSPQLYKQMCICADFEKV 232
Cdd:COG0173 139 QKNLILRHKVTKAIRNYLDENGFLEIETP-ILTKSTPEGARDYLVpsrvhpgKFY---A-LPQSPQLFKQLLMVSGFDRY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 233 FCIGPVFRAEDSNTHRHLtEFVGLDIEMAF---NyhyhEVMEEIADTMVQIFKGL--------------QE--------- 286
Cdd:COG0173 214 FQIARCFRDEDLRADRQP-EFTQLDIEMSFvdqE----DVFELMEGLIRHLFKEVlgvelptpfprmtyAEamerygsdk 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 287 ---RFQTEIQTVNKQFPCEPFK-FLEPT--------LRLEYC-------------------------------------- 316
Cdd:COG0173 289 pdlRFGLELVDVTDIFKDSGFKvFAGAAenggrvkaINVPGGaslsrkqideltefakqygakglayikvnedglkspia 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 317 -----EALAMLREA-GVEMGD-----EDDLSTPNE----------KLLGHLVKEKYD----TDFyildkyPL-------- 363
Cdd:COG0173 369 kflseEELAAILERlGAKPGDliffvADKPKVVNKalgalrlklgKELGLIDEDEFAflwvVDF------PLfeydeeeg 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 364 ---AVR-PFyTMPDP-------RNPKQ--SNSYDMFMRGEEILSGAQRIHDPQLLtERALHH-GIDLEKIKA----YIDS 425
Cdd:COG0173 443 rwvAMHhPF-TMPKDedldlleTDPGKvrAKAYDLVLNGYELGGGSIRIHDPELQ-EKVFELlGISEEEAEEkfgfLLEA 520
|
570 580 590
....*....|....*....|....*....|....*
gi 1622849660 426 FRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 460
Cdd:COG0173 521 FKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
163-460 |
1.28e-40 |
|
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. AspRS is a homodimer, which attaches a specific amino acid to the 3' OH group of ribose of the appropriate tRNA. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. AspRS in this family differ from those found in the AsxRS family by a GAD insert in the core domain.
Pssm-ID: 238400 [Multi-domain] Cd Length: 280 Bit Score: 146.95 E-value: 1.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 163 FRLQSGICHLFRETLINKGFVEIQTPkIISAASEGGANVFTVSY--FKNNAY-LAQSPQLYKQMCICADFEKVFCIGPVF 239
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETP-ILTKSTPEGARDFLVPSrlHPGKFYaLPQSPQLFKQLLMVSGFDRYFQIARCF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 240 RAEDSNTHRHlTEFVGLDIEMAFnYHYHEVMEEIADTMVQIFKglqERFQTEIQTvnkqfpcePFKfleptlRLEYCEAL 319
Cdd:cd00777 80 RDEDLRADRQ-PEFTQIDIEMSF-VDQEDIMSLIEGLLKYVFK---EVLGVELTT--------PFP------RMTYAEAM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 320 amlreagvemgdeddlstpnekllghlvkEKYDTDF-YILD-----------KYPLAVRPFyTMPDP-------RNPKQ- 379
Cdd:cd00777 141 -----------------------------ERYGFKFlWIVDfplfewdeeegRLVSAHHPF-TAPKEedldlleKDPEDa 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 380 -SNSYDMFMRGEEILSGAQRIHDPQlLTERALHH-GIDLEKIKA----YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNV 453
Cdd:cd00777 191 rAQAYDLVLNGVELGGGSIRIHDPD-IQEKVFEIlGLSEEEAEEkfgfLLEAFKYGAPPHGGIALGLDRLVMLLTGSESI 269
|
....*..
gi 1622849660 454 RQTSMFP 460
Cdd:cd00777 270 RDVIAFP 276
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
21-460 |
5.99e-31 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 126.30 E-value: 5.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 21 QKADEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMVK-FAANINKESIVDVEGVvrkvnqkigSCTQ 99
Cdd:PTZ00385 104 RAAQATVRVAGRVTSVRDIGKIIFVTIRSNGNELQVVGQVGEHFTREDLKkLKVSLRVGDIIGADGV---------PCRM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 100 QDVELHVQKIYVISLAeprlPLQLDDAVRPEAEGEEEGRAtvNQDTRLDNRVIDLRTSTSQ-AVFRLQSGICHLFRETLI 178
Cdd:PTZ00385 175 QRGELSVAASRMLILS----PYVCTDQVVCPNLRGFTVLQ--DNDVKYRYRFTDMMTNPCViETIKKRHVMLQALRDYFN 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 179 NKGFVEIQTPKIISAASEGGANVFTVSYFKNNA--YLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNtHRHLTEFVGL 256
Cdd:PTZ00385 249 ERNFVEVETPVLHTVASGANAKSFVTHHNANAMdlFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDAD-RSHNPEFTSC 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 257 DIEMAfnYH-YHEVMEEIADTMVQIFKGLQERFQTEIQTVNKQFPCEPFKFLEPTLRLEYCEALAmlREAGVEMGDEDDL 335
Cdd:PTZ00385 328 EFYAA--YHtYEDLMPMTEDIFRQLAMRVNGTTVVQIYPENAHGNPVTVDLGKPFRRVSVYDEIQ--RMSGVEFPPPNEL 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 336 STPNEKLLGHLVKEKYDT----------------DFYILDKyplAVRPFYTMPDP-----------RNPKQSNSYDMFMR 388
Cdd:PTZ00385 404 NTPKGIAYMSVVMLRYNIplppvrtaakmfekliDFFITDR---VVEPTFVMDHPlfmsplakeqvSRPGLAERFELFVN 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 389 GEEILSGAQRIHDP--------QLLTERalhHGIDLEKI---KAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTS 457
Cdd:PTZ00385 481 GIEYCNAYSELNDPheqyhrfqQQLVDR---QGGDEEAMpldETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGI 557
|
...
gi 1622849660 458 MFP 460
Cdd:PTZ00385 558 IFP 560
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
81-463 |
4.58e-29 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 120.08 E-value: 4.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 81 VDVEGVVRKvnqkiGSCTQQDVELHVQKIYVISLAEPRLPLQlddavrpeaegeeegRATVNQDTRLDNRVIDLRTSTSQ 160
Cdd:PLN02603 164 VLVQGTVVS-----SQGGKQKVELKVSKIVVVGKSDPSYPIQ---------------KKRVSREFLRTKAHLRPRTNTFG 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 161 AVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVS------------------------------YFKNN 210
Cdd:PLN02603 224 AVARVRNALAYATHKFFQENGFVWVSSPIITASDCEGAGEQFCVTtlipnsaenggslvddipktkdglidwsqdFFGKP 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 211 AYLAQSPQLYKQMCICAdFEKVFCIGPVFRAEDSNTHRHLTEFVGLDIEMAF--------------NYHYHEVMEEIADT 276
Cdd:PLN02603 304 AFLTVSGQLNGETYATA-LSDVYTFGPTFRAENSNTSRHLAEFWMIEPELAFadlnddmacataylQYVVKYILENCKED 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 277 M----VQIFKGLQERFQteiQTVNKQFpcepfkfleptLRLEYCEALAMLREAG------VEMGDedDLSTPNEKllgHL 346
Cdd:PLN02603 383 MeffnTWIEKGIIDRLS---DVVEKNF-----------VQLSYTDAIELLLKAKkkfefpVKWGL--DLQSEHER---YI 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 347 VKEKYDTDFYILDKYPLAVRPFYtMPDPRNPKQSNSYDMFM-RGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDS 425
Cdd:PLN02603 444 TEEAFGGRPVIIRDYPKEIKAFY-MRENDDGKTVAAMDMLVpRVGELIGGSQREERLEYLEARLDELKLNKESYWWYLDL 522
|
410 420 430
....*....|....*....|....*....|....*...
gi 1622849660 426 FRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDP 463
Cdd:PLN02603 523 RRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPRVP 560
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
28-468 |
8.01e-28 |
|
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: 8.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 28 WVRArvhtSRAKGKQCFLVLRQQQFNVQALVAvGDHASKQMVKFAANINKESIVDVEGVVRKVNQKIGS--CTQQDVELH 105
Cdd:PRK12820 26 WVDA----FRDHGELLFIHLRDRNGFIQAVFS-PEAAPADVYELAASLRAEFCVALQGEVQKRLEETENphIETGDIEVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 106 VQKIYVISLAEPrLPLQLDDAVRPEAEGEEEGRAtVNQDTRLDNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEI 185
Cdd:PRK12820 101 VRELSILAASEA-LPFAISDKAMTAGAGSAGADA-VNEDLRLQYRYLDIRRPAMQDHLAKRHRIIKCARDFLDSRGFLEI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 186 QTPKIISAASEGGANVFTVSYFKNNAY--LAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNTHRHlTEFVGLDIEMAF- 262
Cdd:PRK12820 179 ETPILTKSTPEGARDYLVPSRIHPKEFyaLPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQ-PEFTQLDIEASFi 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 263 -----------------------------NYHYHEVME----------------EIAD----TMVQIFKGLQERfQTEIQ 293
Cdd:PRK12820 258 deefifelieeltarmfaiggialprpfpRMPYAEAMDttgsdrpdlrfdlkfaDATDifenTRYGIFKQILQR-GGRIK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 294 TVNKQFPCEpfKFLEPTLRLEYCEALA----------MLREAG------VEMGDEDDLstpnEKLLGHLVKEKYDTDFYI 357
Cdd:PRK12820 337 GINIKGQSE--KLSKNVLQNEYAKEIApsfgakgmtwMRAEAGgldsniVQFFSADEK----EALKRRFHAEDGDVIIMI 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 358 LDK----------------------------YPLAVRPF-----------------YTMP-----DPRNPK-----QSNS 382
Cdd:PRK12820 411 ADAscaivlsalgqlrlhladrlglipegvfHPLWITDFplfeatddggvtsshhpFTAPdredfDPGDIEelldlRSRA 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 383 YDMFMRGEEILSGAQRIHDP--QLLTERALhhGIDLEKIKA----YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQT 456
Cdd:PRK12820 491 YDLVVNGEELGGGSIRINDKdiQLRIFAAL--GLSEEDIEDkfgfFLRAFDFAAPPHGGIALGLDRVVSMILQTPSIREV 568
|
570
....*....|..
gi 1622849660 457 SMFPRDPKRLTP 468
Cdd:PRK12820 569 IAFPKNRSAACP 580
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
28-461 |
8.77e-28 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 116.81 E-value: 8.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 28 WV-RARVHtsrakGKQCFLVLRQQQFNVQalVAVGDHASKQMVKFAANINKESIVDVEGVVRK-----VNQKIGSCTQQD 101
Cdd:PLN02903 80 WVdLHRDM-----GGLTFLDVRDHTGIVQ--VVTLPDEFPEAHRTANRLRNEYVVAVEGTVRSrpqesPNKKMKTGSVEV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 102 VELHVQKIYVISLAEPRLPLQLDDAvrpeaegeeegRATVNQDTRLDNRVIDLRTSTSQAVFRLQSGICHLFRETLINK- 180
Cdd:PLN02903 153 VAESVDILNVVTKSLPFLVTTADEQ-----------KDSIKEEVRLRYRVLDLRRPQMNANLRLRHRVVKLIRRYLEDVh 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 181 GFVEIQTPKIISAASEGGANVFTVSYFKNNAYLA--QSPQLYKQMCICADFEKVFCIGPVFRAEDSNTHRHlTEFVGLDI 258
Cdd:PLN02903 222 GFVEIETPILSRSTPEGARDYLVPSRVQPGTFYAlpQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQ-PEFTQLDM 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 259 EMAFNyHYHEVMEEIADTMVQIFK---GLQ-----------------------ERFQTEIQTVNKQFPCEPFKFLE---- 308
Cdd:PLN02903 301 ELAFT-PLEDMLKLNEDLIRQVFKeikGVQlpnpfprltyaeamskygsdkpdLRYGLELVDVSDVFAESSFKVFAgale 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 309 ---------------------------------------PTLR------LEYCEAL----------AMLREAGVEMGD-- 331
Cdd:PLN02903 380 sggvvkaicvpdgkkisnntalkkgdiyneaiksgakglAFLKvlddgeLEGIKALveslspeqaeQLLAACGAGPGDli 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 332 ---EDDLSTPNEKL--LGHLVKEKYD------------TDFYILDKYPLAVR------PFyTMPDPRNPKQSNS-----Y 383
Cdd:PLN02903 460 lfaAGPTSSVNKTLdrLRQFIAKTLDlidpsrhsilwvTDFPMFEWNEDEQRlealhhPF-TAPNPEDMGDLSSaralaY 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 384 DMFMRGEEILSGAQRIH--DPQLLTERALhhGIDLE----KIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTS 457
Cdd:PLN02903 539 DMVYNGVEIGGGSLRIYrrDVQQKVLEAI--GLSPEeaesKFGYLLEALDMGAPPHGGIAYGLDRLVMLLAGAKSIRDVI 616
|
....
gi 1622849660 458 MFPR 461
Cdd:PLN02903 617 AFPK 620
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
202-465 |
5.11e-24 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 105.08 E-value: 5.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 202 FTVSYFKNNAYLAQSPQLYKQMCICAdFEKVFCIGPVFRAEDSNTHRHLTEFVGLDIEMAFNyHYHEVMEeIADTMVQ-I 280
Cdd:PLN02221 300 YSKDFFGRQAFLTVSGQLQVETYACA-LSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFA-DLEDDMN-CAEAYVKyM 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 281 FKGLQERFQTEIQTVNKQFPCEPFKFLE-----PTLRLEYCEALAMLREAgVEMGDE--------DDLSTPNEKLLGHLV 347
Cdd:PLN02221 377 CKWLLDKCFDDMELMAKNFDSGCIDRLRmvastPFGRITYTEAIELLEEA-VAKGKEfdnnvewgIDLASEHERYLTEVL 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 348 KEKYdtdfYILDKYPLAVRPFYtMPDPRNPKQSNSYDMFM-RGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSF 426
Cdd:PLN02221 456 FQKP----LIVYNYPKGIKAFY-MRLNDDEKTVAAMDVLVpKVGELIGGSQREERYDVIKQRIEEMGLPIEPYEWYLDLR 530
|
250 260 270
....*....|....*....|....*....|....*....
gi 1622849660 427 RFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKR 465
Cdd:PLN02221 531 RYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRYPGK 569
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
142-460 |
4.44e-23 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 101.68 E-value: 4.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 142 NQDTRLDNRVIDL-RTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSY--FKNNAYLAQSPQ 218
Cdd:PRK12445 162 DQEVRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHnaLDLDMYLRIAPE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 219 LYKQMCICADFEKVFCIGPVFRAEDSNThRHLTEFVGLDIEMAFNyHYHEVMEeiadTMVQIFKGLQerfQTEIQTVNKQ 298
Cdd:PRK12445 242 LYLKRLVVGGFERVFEINRNFRNEGISV-RHNPEFTMMELYMAYA-DYHDLIE----LTESLFRTLA---QEVLGTTKVT 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 299 FPCEPFKFLEPTLRLEYCEALAMLREAgVEMGDEDDLSTPN----------EKL--LGHLVKEKYD-------TDFYILD 359
Cdd:PRK12445 313 YGEHVFDFGKPFEKLTMREAIKKYRPE-TDMADLDNFDAAKalaesigitvEKSwgLGRIVTEIFDevaeahlIQPTFIT 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 360 KYPLAVRPFYTMPDPrNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTER------ALHHGIDLEKI--KAYIDSFRFGAP 431
Cdd:PRK12445 392 EYPAEVSPLARRNDV-NPEITDRFEFFIGGREIGNGFSELNDAEDQAERfqeqvnAKAAGDDEAMFydEDYVTALEYGLP 470
|
330 340
....*....|....*....|....*....
gi 1622849660 432 PHAGGGIGLERVTMLFLGLHNVRQTSMFP 460
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 ... |
162-460 |
1.26e-22 |
|
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a lysine to the 3' OH group of ribose of the appropriate tRNA. Its assignment to class II aaRS is based upon its structure and the presence of three characteristic sequence motifs in the core domain. It is found in eukaryotes as well as some prokaryotes and archaea. However, LysRS belongs to class I aaRS's in some prokaryotes and archaea. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.
Pssm-ID: 238398 [Multi-domain] Cd Length: 329 Bit Score: 98.43 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 162 VFRLQSGICHLFRETLINKGFVEIQTPKIISAAseGGANV--FTVSY--FKNNAYLAQSPQLYKQMCICADFEKVFCIGP 237
Cdd:cd00775 7 TFIVRSKIISYIRKFLDDRGFLEVETPMLQPIA--GGAAArpFITHHnaLDMDLYLRIAPELYLKRLIVGGFERVYEIGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 238 VFRAEDSNThRHLTEFVGLDIEMAfnYH-YHEVM---EEIADTMVQ-IFKGLQERFQTEIQTVNKqfpcePFKfleptlR 312
Cdd:cd00775 85 NFRNEGIDL-THNPEFTMIEFYEA--YAdYNDMMdltEDLFSGLVKkINGKTKIEYGGKELDFTP-----PFK------R 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 313 LEYCEALAmlREAGVEMGDEDDLSTPN-EKLLGHLVKEKYD---TDFYILDK------------------YPLAVRPFyT 370
Cdd:cd00775 151 VTMVDALK--EKTGIDFPELDLEQPEElAKLLAKLIKEKIEkprTLGKLLDKlfeefveptliqptfiidHPVEISPL-A 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 371 MPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTER-----ALHHGIDLEKI---KAYIDSFRFGAPPHAGGGIGLER 442
Cdd:cd00775 228 KRHRSNPGLTERFELFICGKEIANAYTELNDPFDQRERfeeqaKQKEAGDDEAMmmdEDFVTALEYGMPPTGGLGIGIDR 307
|
330
....*....|....*...
gi 1622849660 443 VTMLFLGLHNVRQTSMFP 460
Cdd:cd00775 308 LVMLLTDSNSIRDVILFP 325
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
151-463 |
1.81e-22 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 100.48 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 151 VIDLRTSTSQAVfrlqsgicHLFRETlinKGFVEIQTPKIISAASEGGANVFTVS------------------------- 205
Cdd:PTZ00425 214 VIRIRNALAIAT--------HLFFQS---RGFLYIHTPLITTSDCEGGGEMFTVTtllgedadyraiprvnkknkkgekr 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 206 --------------------------------------YFKNNAYLAQSPQLYKQMcICADFEKVFCIGPVFRAEDSNTH 247
Cdd:PTZ00425 283 edilntcnannnngnssssnavsspaypdqylidykkdFFSKQAFLTVSGQLSLEN-LCSSMGDVYTFGPTFRAENSHTS 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 248 RHLTEFVGLDIEMAFNYHYHEVmeEIADTMVQIFKG--LQERFQtEIQTVNKQFPCEPFKFLEPTL-----RLEYCEALA 320
Cdd:PTZ00425 362 RHLAEFWMIEPEIAFADLYDNM--ELAESYIKYCIGyvLNNNFD-DIYYFEENVETGLISRLKNILdedfaKITYTNVID 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 321 MLR------EAGVEMGDedDLSTPNEKLlghlVKEKYDTDFYILDKYPLAVRPFYtMPDPRNPKQSNSYDMFM-RGEEIL 393
Cdd:PTZ00425 439 LLQpysdsfEVPVKWGM--DLQSEHERF----VAEQIFKKPVIVYNYPKDLKAFY-MKLNEDQKTVAAMDVLVpKIGEVI 511
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 394 SGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDP 463
Cdd:PTZ00425 512 GGSQREDNLERLDKMIKEKKLNMESYWWYRQLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPRYP 581
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
24-460 |
5.20e-20 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 92.75 E-value: 5.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 24 DEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMV--KFAANINKESIVDVEGVVRKVnqKIGsctqqd 101
Cdd:PLN02502 108 DVSVSVAGRIMAKRAFGKLAFYDLRDDGGKIQLYADKKRLDLDEEEfeKLHSLVDRGDIVGVTGTPGKT--KKG------ 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 102 vELhvqKIYVIS---LAEPRLPL-----QLDDavrpeaegeeegratvnQDTRLDNRVIDLRTSTSQA-VFRLQSGICHL 172
Cdd:PLN02502 180 -EL---SIFPTSfevLTKCLLMLpdkyhGLTD-----------------QETRYRQRYLDLIANPEVRdIFRTRAKIISY 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 173 FRETLINKGFVEIQTPKIISAAseGGANVFTVSYFKN----NAYLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNThR 248
Cdd:PLN02502 239 IRRFLDDRGFLEVETPMLNMIA--GGAAARPFVTHHNdlnmDLYLRIATELHLKRLVVGGFERVYEIGRQFRNEGIST-R 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 249 HLTEFVGLDIEMAFNyHYHEVM---EEIADTMV-QIFKGLQERFQ-TEIQTVnkqfpcEPFK------FLEPTLRLEYCE 317
Cdd:PLN02502 316 HNPEFTTCEFYQAYA-DYNDMMeltEEMVSGMVkELTGSYKIKYHgIEIDFT------PPFRrismisLVEEATGIDFPA 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 318 AL--AMLREAGVEMGDEDDLSTPN--------EKLLGHLVKEKYDTDFYILDkYPLAVRPFyTMPDPRNPKQSNSYDMFM 387
Cdd:PLN02502 389 DLksDEANAYLIAACEKFDVKCPPpqttgrllNELFEEFLEETLVQPTFVLD-HPVEMSPL-AKPHRSKPGLTERFELFI 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 388 RGEEILSGAQRIHDP----QLLTERALHHGIDLEKIKAYIDSF----RFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMF 459
Cdd:PLN02502 467 NGRELANAFSELTDPvdqrERFEEQVKQHNAGDDEAMALDEDFctalEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAF 546
|
.
gi 1622849660 460 P 460
Cdd:PLN02502 547 P 547
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
202-461 |
1.39e-19 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 91.47 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 202 FTVSYFKNNAYLAQSPQLYKQMCICAdFEKVFCIGPVFRAEDSNTHRHLTEFVGLDIEMAFNyHYHEVMEEIADTMVQIF 281
Cdd:PLN02532 363 FSKDFFSRPTYLTVSGRLHLESYACA-LGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFS-ELEDAMNCAEDYFKFLC 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 282 KGLQERFQTEIQTVNKQFPCEPFKFLE-----PTLRLEYCEALAMLREA---GVEMGDEDDLSTPNEKLlGHLVKEKYDT 353
Cdd:PLN02532 441 KWVLENCSEDMKFVSKRIDKTISTRLEaiissSLQRISYTEAVDLLKQAtdkKFETKPEWGIALTTEHL-SYLADEIYKK 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 354 DFYILDkYPLAVRPFYTMPDpRNPKQSNSYDMFM-RGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPP 432
Cdd:PLN02532 520 PVIIYN-YPKELKPFYVRLN-DDGKTVAAFDLVVpKVGTVITGSQNEERMDILNARIEELGLPREQYEWYLDLRRHGTVK 597
|
250 260
....*....|....*....|....*....
gi 1622849660 433 HAGGGIGLERVTMLFLGLHNVRQTSMFPR 461
Cdd:PLN02532 598 HSGFSLGFELMVLFATGLPDVRDAIPFPR 626
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
142-460 |
3.20e-18 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 87.37 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 142 NQDTRLDNRVIDLRTS-TSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAAseGGANVFTVSYFKN----NAYLAQS 216
Cdd:PTZ00417 231 DTEIRYRQRYLDLMINeSTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVA--GGANARPFITHHNdldlDLYLRIA 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 217 PQLYKQMCICADFEKVFCIGPVFRAED-SNTHRhlTEFVGLDIEMAFNyHYHEVMEEIADTMVQIFKGLqerFQTEIQTV 295
Cdd:PTZ00417 309 TELPLKMLIVGGIDKVYEIGKVFRNEGiDNTHN--PEFTSCEFYWAYA-DFYDLIKWSEDFFSQLVMHL---FGTYKILY 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 296 NKQFP-CEPFK--FLEPTLRLEYCEALAMLREAGVE--------------MGDEDDLSTPN--------EKLLGHLVKEK 350
Cdd:PTZ00417 383 NKDGPeKDPIEidFTPPYPKVSIVEELEKLTNTKLEqpfdspetinkminLIKENKIEMPNpptaakllDQLASHFIENK 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 351 Y-DTDFYILDkYPLAVRPFYTMPDPRnPKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGIDLEKIKA-------- 421
Cdd:PTZ00417 463 YpNKPFFIIE-HPQIMSPLAKYHRSK-PGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAeafqfdaa 540
|
330 340 350
....*....|....*....|....*....|....*....
gi 1622849660 422 YIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 460
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 ... |
27-113 |
2.93e-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: 2.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 27 VWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASkqMVKFAANINKESIVDVEGVVRKVnqKIGSCTQQDVELHV 106
Cdd:cd04100 2 VTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELGE--FFEEAEKLRTESVVGVTGTVVKR--PEGNLATGEIELQA 77
|
....*..
gi 1622849660 107 QKIYVIS 113
Cdd:cd04100 78 EELEVLS 84
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
142-460 |
5.69e-16 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 80.78 E-value: 5.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 142 NQDTRLDNRVIDLRTST-SQAVFRLQSGICHLFRETLINKGFVEIQTPkiISAASEGGANV--FTVSYfknNAY-----L 213
Cdd:PRK02983 748 DPEARVRQRYLDLAVNPeARDLLRARSAVVRAVRETLVARGFLEVETP--ILQQVHGGANArpFVTHI---NAYdmdlyL 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 214 AQSPQLY-KQMCIcADFEKVFCIGPVFRAE--------------------DSNTHRHLTEfvGLDIEMAFNYH------- 265
Cdd:PRK02983 823 RIAPELYlKRLCV-GGVERVFELGRNFRNEgvdathnpeftlleayqahaDYDTMRDLTR--ELIQNAAQAAHgapvvmr 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 266 -YHEVMEEIAD-----TMVQIFKGLQERFQTEIQtvnkqfPCEPFkflePTLRlEYCEAlamlreAGVEMGDEDDLSTPN 339
Cdd:PRK02983 900 pDGDGVLEPVDisgpwPVVTVHDAVSEALGEEID------PDTPL----AELR-KLCDA------AGIPYRTDWDAGAVV 962
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 340 EKLLGHLVkEKYDTD--FYIldKYPLAVRPFyTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDP----QLLTERAL-HH 412
Cdd:PRK02983 963 LELYEHLV-EDRTTFptFYT--DFPTSVSPL-TRPHRSDPGLAERWDLVAWGVELGTAYSELTDPveqrRRLTEQSLlAA 1038
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1622849660 413 GIDLEKI---KAYIDSFRFGAPPHAGGGIGLERVTMLFLGLhNVRQTSMFP 460
Cdd:PRK02983 1039 GGDPEAMeldEDFLQALEYAMPPTGGLGMGVDRLVMLLTGR-SIRETLPFP 1088
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
32-460 |
4.46e-15 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 77.05 E-value: 4.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 32 RVHTSRAKGKQCFLVLRQQQFNVQALVAVgDHASKQMVKFAANINKESIVDVEGVVRKvnqkigscTQQDvEL--HVQKI 109
Cdd:PRK00484 62 RVMLKRVMGKASFATLQDGSGRIQLYVSK-DDVGEEALEAFKKLDLGDIIGVEGTLFK--------TKTG-ELsvKATEL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 110 YVISLAEPRLP-----LQlddavrpeaegeeegratvNQDTRLDNRVIDLRTS-TSQAVFRLQSGICHLFRETLINKGFV 183
Cdd:PRK00484 132 TLLTKSLRPLPdkfhgLT-------------------DVETRYRQRYVDLIVNpESRETFRKRSKIISAIRRFLDNRGFL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 184 EIQTPKIISAAseGGANV--FTVSYfknNA-----YLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNThRHLTEFVGL 256
Cdd:PRK00484 193 EVETPMLQPIA--GGAAArpFITHH---NAldidlYLRIAPELYLKRLIVGGFERVYEIGRNFRNEGIDT-RHNPEFTML 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 257 DIEMAfnYH-YHEVM---EE-IADTMVQIFKGLQERFQ-TEIqTVNKQFPCEPFK----------FLEPTLRleycEALA 320
Cdd:PRK00484 267 EFYQA--YAdYNDMMdltEElIRHLAQAVLGTTKVTYQgTEI-DFGPPFKRLTMVdaikeytgvdFDDMTDE----EARA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 321 MLREAGVEMGDEDDLSTPNEKLLGHLVKEKYDTDFYILDkYPLAVRPFyTMPDPRNPKQSNSYDMFMRGEEILSG----- 395
Cdd:PRK00484 340 LAKELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITD-YPVEISPL-AKRHREDPGLTERFELFIGGREIANAfseln 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622849660 396 -----AQRIHDpQLLtERAL----HHGIDLEkikaYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFP 460
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 ... |
17-155 |
2.50e-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: 61.00 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 17 DLTIQKADEVV----WVrarvHTSRAKGKQCFLVLRQQQFNVQALVavgDHASKQMVKFAANINKESIVDVEGVVRK--- 89
Cdd:cd04317 7 ELRESHVGQEVtlcgWV----QRRRDHGGLIFIDLRDRYGIVQVVF---DPEEAPEFELAEKLRNESVIQVTGKVRArpe 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622849660 90 --VNQKIGSctqQDVELHVQKIYVISLAEPrLPLQLDDAVRpeaegeeegratVNQDTRLDNRVIDLR 155
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 ... |
24-121 |
5.92e-10 |
|
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the homodimeric non-discriminating (ND) Pyrococcus kodakaraensis aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. P. kodakaraensis AspRS is a class 2b aaRS. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. P. kodakaraensis ND-AspRS can charge both tRNAAsp and tRNAAsn. Some of the enzymes in this group may be discriminating, based on the presence of homologs of asparaginyl-tRNA synthetase (AsnRS) in their completed genomes.
Pssm-ID: 239811 [Multi-domain] Cd Length: 108 Bit Score: 56.55 E-value: 5.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 24 DEVVWVrARVHTSRAKGKQCFLVLRQQQFNVQaLVAVGDHASKQMVKFAANINKESIVDVEGVVRKVNQKIGsctqqDVE 103
Cdd:cd04316 13 EEVTVA-GWVHEIRDLGGIKFVILRDREGIVQ-VTAPKKKVDKELFKTVRKLSRESVISVTGTVKAEPKAPN-----GVE 85
|
90
....*....|....*...
gi 1622849660 104 LHVQKIYVISLAEPRLPL 121
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 ... |
173-275 |
4.34e-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: 56.36 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 173 FRETLINKGFVEIQTPKIISAASEGGAN------VFTVSYFKNNAYLAQSPQLYKQM----CICADFEKVFCIGPVFRAE 242
Cdd:cd00768 9 LRRFMAELGFQEVETPIVEREPLLEKAGhepkdlLPVGAENEEDLYLRPTLEPGLVRlfvsHIRKLPLRLAEIGPAFRNE 88
|
90 100 110
....*....|....*....|....*....|....*....
gi 1622849660 243 DSNTH-RHLTEFVGLDIEMAF-----NYHYHEVMEEIAD 275
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 ... |
27-112 |
3.21e-07 |
|
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic acids. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See pfam00152). Aminoacyl-tRNA synthetases catalyze the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a hetero-trimeric complex, that contains a subunit in this family. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain.
Pssm-ID: 460164 [Multi-domain] Cd Length: 75 Bit Score: 47.61 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 27 VWVRARVHT-SRAKGKQCFLVLRQQQFNVQALVAvgdhaSKQMVKFAANINKESIVDVEGVVRKVNQKigsctqqDVELH 105
Cdd:pfam01336 1 VTVAGRVTSiRRSGGKLLFLTLRDGTGSIQVVVF-----KEEAEKLAKKLKEGDVVRVTGKVKKRKGG-------ELELV 68
|
....*..
gi 1622849660 106 VQKIYVI 112
Cdd:pfam01336 69 VEEIELL 75
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
27-117 |
1.01e-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: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 27 VWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAvgDHASKQMVKFAANINKESIVDVEGVVRKVNQKIGSctqqdVELHV 106
Cdd:cd04319 2 VTLAGWVYRKREVGKKAFIVLRDSTGIVQAVFS--KDLNEEAYREAKKVGIESSVIVEGAVKADPRAPGG-----AEVHG 74
|
90
....*....|.
gi 1622849660 107 QKIYVISLAEP 117
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 ... |
27-113 |
5.04e-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: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849660 27 VWVRARVHTSRAKGKQCFLVLRQQQFNVQAlVAVGDHASKQMVkfAANINKESIVDVEGVVRKVNQkiGSCTQQDVELHV 106
Cdd:cd04323 2 VKVFGWVHRLRSQKKLMFLVLRDGTGFLQC-VLSKKLVTEFYD--AKSLTQESSVEVTGEVKEDPR--AKQAPGGYELQV 76
|
....*..
gi 1622849660 107 QKIYVIS 113
Cdd:cd04323 77 DYLEIIG 83
|
|
| |
