|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
4-531 |
0e+00 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 705.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 4 AAEGEQPKLSKKELNKLARKAKKDEKagEKGGNQQQAAAMDQEDASKDFYGSYGLVNSKEKKVLN-FLKVKEINVSNATK 82
Cdd:PLN02850 5 AVEESGEKISKKAAKKAAAKAEKLRR--EATAKAAAASLEDEDDPLASNYGDVPLEELQSKVTGReWTDVSDLGEELAGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 83 DVWVRGRIHTTRSKGKNCFLVLRQGVYTVQVAMFM-NEKISKQMLKFVSSISKESIVDVYATINKVDNPIESCTQkDVEL 161
Cdd:PLN02850 83 EVLIRGRVHTIRGKGKSAFLVLRQSGFTVQCVVFVsEVTVSKGMVKYAKQLSRESVVDVEGVVSVPKKPVKGTTQ-QVEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 162 LAQQVFVVSTSAPKLPLQIEDASRrAPTDEEKASEQENQLAVVNLDTRLDNRVIDLRTPTSHAIFRIQAGICNQFRNILD 241
Cdd:PLN02850 162 QVRKIYCVSKALATLPFNVEDAAR-SESEIEKALQTGEQLVRVGQDTRLNNRVLDLRTPANQAIFRIQSQVCNLFREFLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 242 VRGFVEIMAPKIISAPSEGGANVFEVSYFKGSAYLAQSPQLYKQMAIAGDFEKVYTIGPVFRAEDSNTHRHMTEFVGLDL 321
Cdd:PLN02850 241 SKGFVEIHTPKLIAGASEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGDFRRVFEIGPVFRAEDSFTHRHLCEFTGLDL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 322 EMAFNFHYHEVMETIAEVLTQMFKGLQQNYQDEIAAVGNQYPAEPFQFCEPPLILKYPDAITLLRENGIEIGDEDDLSTP 401
Cdd:PLN02850 321 EMEIKEHYSEVLDVVDELFVAIFDGLNERCKKELEAIREQYPFEPLKYLPKTLRLTFAEGIQMLKEAGVEVDPLGDLNTE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 402 VEKFLGKLVKEKYSTDFYVLDKFPLSVRPFYTMPDAHDERYSNSYDMFMRGEEILSGAQRIHDADMLVERAKHHQVDLAK 481
Cdd:PLN02850 401 SERKLGQLVKEKYGTDFYILHRYPLAVRPFYTMPCPDDPKYSNSFDVFIRGEEIISGAQRVHDPELLEKRAEECGIDVKT 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 17551876 482 IQSYIDSFKYGCPPHAGGGIGLERVTMLFLGLHNIRLASLFPRDPKRLTP 531
Cdd:PLN02850 481 ISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQRLAP 530
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
2-531 |
0e+00 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 542.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 2 ADAAEGEQPKLSKKELNKLARKAKKDEKAGEKggnqqqAAAMDQedaSKDFYGSYGLVNSKEKKVLNFLKVKEINVSN-A 80
Cdd:PTZ00401 7 DAGAPAVEKKQSDKEARKAARLAEEKARAAEK------AALVEK---YKDVFGAAPMVQSTTYKSRTFIPVAVLSKPElV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 81 TKDVWVRGRIHTTRSKGKNCFLVLRQGVYTVQVAMFMNEKISKQMLKFVSSISKESIVDVYATINKVDNPIESCTQKDVE 160
Cdd:PTZ00401 78 DKTVLIRARVSTTRKKGKMAFMVLRDGSDSVQAMAAVEGDVPKEMIDFIGQIPTESIVDVEATVCKVEQPITSTSHSDIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 161 LLAQQVFVVSTSAPKLPLQIEDASRRAptDEEKASeqenqlavVNLDTRLDNRVIDLRTPTSHAIFRIQAGICNQFRNIL 240
Cdd:PTZ00401 158 LKVKKIHTVTESLRTLPFTLEDASRKE--SDEGAK--------VNFDTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 241 DVRGFVEIMAPKIISAPSEGGANVFEVSYFKGSAYLAQSPQLYKQMAIAGDFEKVYTIGPVFRAEDSNTHRHMTEFVGLD 320
Cdd:PTZ00401 228 IDSDFCEIHSPKIINAPSEGGANVFKLEYFNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHLTEFVGLD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 321 LEMAFNFHYHEVMETIAEVLTQMFKGLqQNYQDEIAAVGNQYPAEPFQF------------------CEPP--------- 373
Cdd:PTZ00401 308 VEMRINEHYYEVLDLAESLFNYIFERL-ATHTKELKAVCQQYPFEPLVWkltpermkelgvgvisegVEPTdkyqarvhn 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 374 -----LILKYPDAITLLreNGI---EIGDEDDLSTPVEKFLGKLVKEKYSTDFYVLDKFPLSVRPFYTMPDAHDERYSNS 445
Cdd:PTZ00401 387 mdsrmLRINYMHCIELL--NTVleeKMAPTDDINTTNEKLLGKLVKERYGTDFFISDRFPSSARPFYTMECKDDERFTNS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 446 YDMFMRGEEILSGAQRIHDADMLVERAKHHQVDLAKIQSYIDSFKYGCPPHAGGGIGLERVTMLFLGLHNIRLASLFPRD 525
Cdd:PTZ00401 465 YDMFIRGEEISSGAQRIHDPDLLLARAKMLNVDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPRD 544
|
....*.
gi 17551876 526 PKRLTP 531
Cdd:PTZ00401 545 PQRTTP 550
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
204-527 |
3.75e-178 |
|
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: 504.02 E-value: 3.75e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 204 VNLDTRLDNRVIDLRTPTSHAIFRIQAGICNQFRNILDVRGFVEIMAPKIISAPSEGGANVFEVSYFKGSAYLAQSPQLY 283
Cdd:cd00776 2 ANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 284 KQMAIAGdFEKVYTIGPVFRAEDSNTHRHMTEFVGLDLEMAFNFHYHEVMETIAEVLTQMFKGLQQNYQDEIAAVgNQYP 363
Cdd:cd00776 82 KEMLIAA-LERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRVLERCAKELELV-NQLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 364 AEPFQFCEPPLILKYPDAITLLRENGI--EIGDEDDLSTPVEKFLGKLVKekysTDFYVLDKFPLSVRPFYTMPDAHDER 441
Cdd:cd00776 160 RELLKPLEPFPRITYDEAIELLREKGVeeEVKWGEDLSTEHERLLGEIVK----GDPVFVTDYPKEIKPFYMKPDDDNPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 442 YSNSYDMFMRG-EEILSGAQRIHDADMLVERAKHHQVDLAKIQSYIDSFKYGCPPHAGGGIGLERVTMLFLGLHNIRLAS 520
Cdd:cd00776 236 TVESFDLLMPGvGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAI 315
|
....*..
gi 17551876 521 LFPRDPK 527
Cdd:cd00776 316 LFPRDPK 322
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
72-531 |
5.93e-157 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 454.26 E-value: 5.93e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 72 VKEINVSNATKDVWVRGRIHTTRSKGKNCFLVLRQGVYTVQVAMfmNEKISKQMLKFVSSISKESIVDVYATINKvdNPI 151
Cdd:PRK05159 7 TSELTPELDGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVV--KKKVDEELFETIKKLKRESVVSVTGTVKA--NPK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 152 escTQKDVELLAQQVFVVSTSAPKLPLQIedasrrapTDEEKASeqenqlavvnLDTRLDNRVIDLRTPTSHAIFRIQAG 231
Cdd:PRK05159 83 ---APGGVEVIPEEIEVLNKAEEPLPLDI--------SGKVLAE----------LDTRLDNRFLDLRRPRVRAIFKIRSE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 232 ICNQFRNILDVRGFVEIMAPKIISAPSEGGANVFEVSYFKGSAYLAQSPQLYKQMAIAGDFEKVYTIGPVFRAEDSNTHR 311
Cdd:PRK05159 142 VLRAFREFLYENGFTEIFTPKIVASGTEGGAELFPIDYFEKEAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 312 HMTEFVGLDLEMAFNFHYHEVMETIAEVLTQMFKGLQQNYQDEIAAVGNQYPAEPFQFceppLILKYPDAITLLRENGIE 391
Cdd:PRK05159 222 HLNEYTSIDVEMGFIDDHEDVMDLLENLLRYMYEDVAENCEKELELLGIELPVPETPI----PRITYDEAIEILKSKGNE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 392 IGDEDDLSTPVEKFLGKLVKEKYSTDFYVLDKFPLSVRPFYTMPDAHDERYSNSYDMFMRGEEILSGAQRIHDADMLVER 471
Cdd:PRK05159 298 ISWGDDLDTEGERLLGEYVKEEYGSDFYFITDYPSEKRPFYTMPDEDDPEISKSFDLLFRGLEITSGGQRIHRYDMLVES 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 472 AKHHQVDLAKIQSYIDSFKYGCPPHAGGGIGLERVTMLFLGLHNIRLASLFPRDPKRLTP 531
Cdd:PRK05159 378 IKEKGLNPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPRDRHRLTP 437
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
82-531 |
1.50e-155 |
|
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: 450.43 E-value: 1.50e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 82 KDVWVRGRIHTTRSKGKNCFLVLRQGVYTVQVAMFMNeKISKQMLKFVSSISKESIVDVYATINkvdnpIESCTQKDVEL 161
Cdd:TIGR00458 13 QEVTFMGWVHEIRDLGGLIFVLLRDREGLIQITAPAK-KVSKNLFKWAKKLNLESVVAVRGIVK-----IKEKAPGGFEI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 162 LAQQVFVVSTSAPKLPLQiedasrraPTDEEKASeqenqlavvnLDTRLDNRVIDLRTPTSHAIFRIQAGICNQFRNILD 241
Cdd:TIGR00458 87 IPTKIEVINEAKEPLPLD--------PTEKVPAE----------LDTRLDYRFLDLRRPTVQAIFRIRSGVLESVREFLA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 242 VRGFVEIMAPKIISAPSEGGANVFEVSYFKGSAYLAQSPQLYKQMAIAGDFEKVYTIGPVFRAEDSNTHRHMTEFVGLDL 321
Cdd:TIGR00458 149 EEGFIEVHTPKLVASATEGGTELFPITYFEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHRHLNEATSIDI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 322 EMAFNFHyHEVMETIAEVLTQMFKGLQQNYQDEIAAVGNQYPAEPFQFCEppliLKYPDAITLLRENGIEIGDEDDLSTP 401
Cdd:TIGR00458 229 EMAFEDH-HDVMDILEELVVRVFEDVPERCAHQLETLEFKLEKPEGKFVR----LTYDEAIEMANAKGVEIGWGEDLSTE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 402 VEKFLGklvkEKYSTDFYVLDkFPLSVRPFYTMPDAHDERYSNSYDMFMRGEEILSGAQRIHDADMLVERAKHHQVDLAK 481
Cdd:TIGR00458 304 AEKALG----EEMDGLYFITD-WPTEIRPFYTMPDEDNPEISKSFDLMYRDLEISSGAQRIHLHDLLVERIKAKGLNPEG 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 17551876 482 IQSYIDSFKYGCPPHAGGGIGLERVTMLFLGLHNIRLASLFPRDPKRLTP 531
Cdd:TIGR00458 379 FKDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRKRLTP 428
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
71-531 |
3.73e-149 |
|
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: 434.09 E-value: 3.73e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 71 KVKEINVSNATKDVWVRGRIHTTRSKGKNCFLVLRQGVYTVQVAMFMNEKISKQMLKfvsSISKESIVDVYATInkVDNP 150
Cdd:COG0017 4 YIKDLLPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKLENFEEAK---KLTTESSVEVTGTV--VESP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 151 IescTQKDVELLAQQVFVVSTSAPKLPLQIEDASrraptdeekaseqenqlavvnLDTRLDNRVIDLRTPTSHAIFRIQA 230
Cdd:COG0017 79 R---APQGVELQAEEIEVLGEADEPYPLQPKRHS---------------------LEFLLDNRHLRLRTNRFGAIFRIRS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 231 GICNQFRNILDVRGFVEIMAPKIISAPSEGGANVFEVSYFKGSAYLAQSPQLYKQMAIAGdFEKVYTIGPVFRAEDSNTH 310
Cdd:COG0017 135 ELARAIREFFQERGFVEVHTPIITASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMA-LEKVYTFGPTFRAEKSNTR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 311 RHMTEFVGLDLEMAFnFHYHEVMETIAEVLTQMFKGLQQNYQDEIAAVG------NQYPAEPFQfcepplILKYPDAITL 384
Cdd:COG0017 214 RHLAEFWMIEPEMAF-ADLEDVMDLAEEMLKYIIKYVLENCPEELEFLGrdverlEKVPESPFP------RITYTEAIEI 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 385 LRENGIEIGDEDDLSTPVEKFLGklvkEKYSTDFYVLDKFPLSVRPFYTMPDAHDERYSNSYDMFMRG-EEILSGAQRIH 463
Cdd:COG0017 287 LKKSGEKVEWGDDLGTEHERYLG----EEFFKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGiGEIIGGSQREH 362
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17551876 464 DADMLVERAKHHQVDLAKIQSYIDSFKYGCPPHAGGGIGLERVTMLFLGLHNIRLASLFPRDPKRLTP 531
Cdd:COG0017 363 RYDVLVERIKEKGLDPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
205-526 |
2.26e-98 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 300.25 E-value: 2.26e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 205 NLDTRLDNRVIDLRTPTSHAIFRIQAGICNQFRNILDVRGFVEIMAPKIISAPSEGGANVFEV------SYFkgsaYLAQ 278
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVpsralgKFY----ALPQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 279 SPQLYKQMAIAGDFEKVYTIGPVFRAEDSNTHRHMtEFVGLDLEMAFNfHYHEVMETIAEVLTQMFKGLQqNYQDEIAAV 358
Cdd:pfam00152 77 SPQLYKQLLMVAGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFV-DYEDVMDLTEELIKEIFKEVE-GIAKELEGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 359 GNQYPAEPFQfcepplILKYPDAITLLRENGIEIGDEDdLSTPVEKFLGKLVKEKYSTDFYVLDKFPLSVRPFYTMPDAH 438
Cdd:pfam00152 154 TLLDLKKPFP------RITYAEAIEKLNGKDVEELGYG-SDKPDLRFLLELVIDKNKFNPLWVTDFPAEHHPFTMPKDED 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 439 DERYSNSYDMFMRGEEILSGAQRIHDADMLVERAKHHQVD----LAKIQSYIDSFKYGCPPHAGGGIGLERVTMLFLGLH 514
Cdd:pfam00152 227 DPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDpeeaEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLE 306
|
330
....*....|..
gi 17551876 515 NIRLASLFPRDP 526
Cdd:pfam00152 307 SIREVIAFPKTR 318
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
68-531 |
8.95e-70 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 230.38 E-value: 8.95e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 68 NFLKVKEINVSN-ATKDVWVRGRIHTTRSKGKNCFLVLRQGVYTVQVAMFMNEKISKQmlKFVSSISKESIVDVYATInk 146
Cdd:PRK03932 2 MRVSIKDILKGKyVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDNGEEYF--EEIKKLTTGSSVIVTGTV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 147 vdnpIESCTQK-DVELLAQQVFVVSTSAPKLPLQIEDASrraptdeekaseqenqlavvnLDTRLDNRVIDLRTPTSHAI 225
Cdd:PRK03932 78 ----VESPRAGqGYELQATKIEVIGEDPEDYPIQKKRHS---------------------IEFLREIAHLRPRTNKFGAV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 226 FRIQAGICNQFRNILDVRGFVEIMAPKIISAPSEGGANVFEVS---------YFKGSAYLAQSPQLYKQMAIAGdFEKVY 296
Cdd:PRK03932 133 MRIRNTLAQAIHEFFNENGFVWVDTPIITASDCEGAGELFRVTtldldfskdFFGKEAYLTVSGQLYAEAYAMA-LGKVY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 297 TIGPVFRAEDSNTHRHMTEFVGLDLEMAFnFHYHEVMETIAEVLTQMFKGLQQNYQDEIAAVGNQYPAEPF----QFCEP 372
Cdd:PRK03932 212 TFGPTFRAENSNTRRHLAEFWMIEPEMAF-ADLEDNMDLAEEMLKYVVKYVLENCPDDLEFLNRRVDKGDIerleNFIES 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 373 PLI-LKYPDAITLLRENG------IEIGDedDLSTPVEKFLgklVKEKYSTDFYVLDkFPLSVRPFYTMPDAHDERYSnS 445
Cdd:PRK03932 291 PFPrITYTEAIEILQKSGkkfefpVEWGD--DLGSEHERYL---AEEHFKKPVFVTN-YPKDIKAFYMRLNPDGKTVA-A 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 446 YDMFMRG-EEILSGAQRIHDADMLVERAKHHQVDLAKIQSYIDSFKYGCPPHAGGGIGLERVTMLFLGLHNIRLASLFPR 524
Cdd:PRK03932 364 MDLLAPGiGEIIGGSQREERLDVLEARIKELGLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPR 443
|
....*..
gi 17551876 525 DPKRLTP 531
Cdd:PRK03932 444 TPGRAEF 450
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
82-531 |
4.30e-68 |
|
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: 226.11 E-value: 4.30e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 82 KDVWVRGRIHTTRSKGKNCFLVLRQGVYTVQVAMFMNEKISKQMLKFVSSISKESIVDVYATInkvdnpIESCTQKD-VE 160
Cdd:TIGR00457 17 DEVTVSGWVRTKRSSKKIIFLELNDGSSLGPIQAVINGEDNPYLFQLLKSLTTGSSVSVTGKV------VESPGKGQpVE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 161 LLAQQVFVVSTSAPK-LPLQIEDASrraptdeekaseqenqlavvnLDTRLDNRVIDLRTPTSHAIFRIQAGICNQFRNI 239
Cdd:TIGR00457 91 LQVKKIEVVGEAEPDdYPLQKKEHS---------------------LEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 240 LDVRGFVEIMAPKIISAPSEGGANVFEVS---------YFKGSAYLAQSPQLYKQmAIAGDFEKVYTIGPVFRAEDSNTH 310
Cdd:TIGR00457 150 FQENGFTWVSPPILTSNDCEGAGELFRVStgnidfsqdFFGKEAYLTVSGQLYLE-TYALALSKVYTFGPTFRAEKSNTS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 311 RHMTEFVGLDLEMAF-NFhyHEVMETIAEVLTQMFKGLQQNYQDEIAAVGNQYPAEPFQFCEPPLI-----LKYPDAITL 384
Cdd:TIGR00457 229 RHLSEFWMIEPEMAFaNL--NDLLQLAETLIKYIIKAVLENCSQELKFLEKNFDKDLIKRLENIINnkfarITYTDAIEI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 385 LRENGIEIGDED----DLSTPVEKFLGklvkEKYSTDFYVLDKFPLSVRPFYtMPDAHDERYSNSYDMFMRG-EEILSGA 459
Cdd:TIGR00457 307 LKESDKNFEYEDfwgdDLQTEHERFLA----EEYFKPPVFVTNYPKDIKAFY-MKLNDDGKTVAAMDLLAPGiGEIIGGS 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17551876 460 QRIHDADMLVERAKHHQVDLAKIQSYIDSFKYGCPPHAGGGIGLERVTMLFLGLHNIRLASLFPRDPKRLTP 531
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 ... |
226-525 |
1.72e-53 |
|
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: 181.91 E-value: 1.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 226 FRIQAGICNQFRNILDVRGFVEIMAPKIISAPSEGGANVFEVSYFKGS--AYLAQSPQLYKQMAIAGDFEKVYTIGPVFR 303
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGldYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 304 AEDSNThRHMTEFVGLDLEMAFnFHYHEVMEtiaeVLTQMFKGLQQNYQDEIAAVGNQYPAEpfqFCEPPLILKYPDAIt 383
Cdd:cd00669 81 NEDLRA-RHQPEFTMMDLEMAF-ADYEDVIE----LTERLVRHLAREVLGVTAVTYGFELED---FGLPFPRLTYREAL- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 384 llrengieigdeddlstpvekflgklvkEKYSTDFYVLDkFPLSVRPFYTMPDAHDERYSNSYDMFMRGEEILSGAQRIH 463
Cdd:cd00669 151 ----------------------------ERYGQPLFLTD-YPAEMHSPLASPHDVNPEIADAFDLFINGVEVGNGSSRLH 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17551876 464 DADMLVERAKHHQVDLA----KIQSYIDSFKYGCPPHAGGGIGLERVTMLFLGLHNIRLASLFPRD 525
Cdd:cd00669 202 DPDIQAEVFQEQGINKEagmeYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKM 267
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
217-526 |
3.26e-49 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 172.90 E-value: 3.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 217 LRTPTSHAIFRIQAGICNQFRNILDVRGFVEIMAPkIISA--------PSEGGANVFEVSYFKGSAYLAQSPQLYKQMAI 288
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPP-IISPstdplmglGSDLPVKQISIDFYGVEYYLADSMILHKQLAL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 289 AGdFEKVYTIGPVFRAE--DSNTHRHMTEFVGLDLEMAfNFHYHEVMETIAEVLTQMFKGLQQNYQDEIAAVGNQYP--A 364
Cdd:PRK06462 100 RM-LGKIFYLSPNFRLEpvDKDTGRHLYEFTQLDIEIE-GADLDEVMDLIEDLIKYLVKELLEEHEDELEFFGRDLPhlK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 365 EPFQfcepplILKYPDAITLLRENGIEIGDEDDLSTPVEKFLGKLVKEKystdFYVLDkFPLSVRPFYTMPDAHDERYSN 444
Cdd:PRK06462 178 RPFK------RITHKEAVEILNEEGCRGIDLEELGSEGEKSLSEHFEEP----FWIID-IPKGSREFYDREDPERPGVLR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 445 SYDMFMR---GEeILSGAQRIHDADMLVERAKHHQVDLAKIQSYIDSFKYGCPPHAGGGIGLERVTMLFLGLHNIRLASL 521
Cdd:PRK06462 247 NYDLLLPegyGE-AVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQP 325
|
....*
gi 17551876 522 FPRDP 526
Cdd:PRK06462 326 FPRVP 330
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
84-182 |
2.03e-45 |
|
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: 154.64 E-value: 2.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 84 VWVRGRIHTTRSKG-KNCFLVLRQGVYTVQ-VAMFMNEKISKQMLKFVSSISKESIVDVYATINKVDNPIESCTQKDVEL 161
Cdd:cd04320 2 VLIRARVHTSRAQGaKLAFLVLRQQGYTIQgVLAASAEGVSKQMVKWAGSLSKESIVDVEGTVKKPEEPIKSCTQQDVEL 81
|
90 100
....*....|....*....|.
gi 17551876 162 LAQQVFVVSTSAPKLPLQIED 182
Cdd:cd04320 82 HIEKIYVVSEAAEPLPFQLED 102
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
74-523 |
3.72e-35 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 139.05 E-value: 3.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 74 EINVSNATKDVWVRGRIHTTRSKGKNCFLVLR--QGVytVQVamFMNEkiSKQMLKFVSSISKESIVDVYATINKVD--- 148
Cdd:PRK00476 10 ELRESHVGQTVTLCGWVHRRRDHGGLIFIDLRdrEGI--VQV--VFDP--DAEAFEVAESLRSEYVIQVTGTVRARPegt 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 149 -NP-IESctqKDVELLAQQVFVVSTSAPkLPLQIEDasrraptdEEKASEqenqlavvnlDTRLDNRVIDLRTPTSHAIF 226
Cdd:PRK00476 84 vNPnLPT---GEIEVLASELEVLNKSKT-LPFPIDD--------EEDVSE----------ELRLKYRYLDLRRPEMQKNL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 227 RIQAGICNQFRNILDVRGFVEIMAPkIISAPSEGGANVFEV-S-YFKGSAY-LAQSPQLYKQ--MaIAGdFEKVYTIGPV 301
Cdd:PRK00476 142 KLRSKVTSAIRNFLDDNGFLEIETP-ILTKSTPEGARDYLVpSrVHPGKFYaLPQSPQLFKQllM-VAG-FDRYYQIARC 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 302 FRAEDSNTHRHMtEFVGLDLEMAFnFHYHEVMETIAEVLTQMFKglqqnyqdeiaAVGNQYPAEPFQfcepplILKYPDA 381
Cdd:PRK00476 219 FRDEDLRADRQP-EFTQIDIEMSF-VTQEDVMALMEGLIRHVFK-----------EVLGVDLPTPFP------RMTYAEA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 382 ITL-------LReNGIEIGD------------------------------------------------------------ 394
Cdd:PRK00476 280 MRRygsdkpdLR-FGLELVDvtdlfkdsgfkvfagaandggrvkairvpggaaqlsrkqideltefakiygakglayikv 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 395 -EDDLSTPVEKFLGKLVKEKYSTD---------FYVLDK----------------------------------FPL---- 426
Cdd:PRK00476 359 nEDGLKGPIAKFLSEEELAALLERtgakdgdliFFGADKakvvndalgalrlklgkelglidedkfaflwvvdFPMfeyd 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 427 --SVR------PFyTMPDAHDERY----------SNSYDMFMRGEEILSGAQRIHDADMLV----------ERAKhhqvd 478
Cdd:PRK00476 439 eeEGRwvaahhPF-TMPKDEDLDElettdpgkarAYAYDLVLNGYELGGGSIRIHRPEIQEkvfeilgiseEEAE----- 512
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 17551876 479 lAKIQSYIDSFKYGCPPHAGGGIGLERVTMLFLGLHNIRLASLFP 523
Cdd:PRK00476 513 -EKFGFLLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
225-523 |
5.14e-35 |
|
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: 132.70 E-value: 5.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 225 IFRIQagICNQFRNILDVRGFVEIMAPkIISAPSEGGANVFEVSY--FKGSAY-LAQSPQLYKQMAIAGDFEKVYTIGPV 301
Cdd:cd00777 2 RLRSR--VIKAIRNFLDEQGFVEIETP-ILTKSTPEGARDFLVPSrlHPGKFYaLPQSPQLFKQLLMVSGFDRYFQIARC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 302 FRAEDSNTHRHmTEFVGLDLEMAFnFHYHEVMETIAEVLTQMFKglqqnyqdeiaAVGNQYPAEPFQfcepplILKYPDA 381
Cdd:cd00777 79 FRDEDLRADRQ-PEFTQIDIEMSF-VDQEDIMSLIEGLLKYVFK-----------EVLGVELTTPFP------RMTYAEA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 382 ItllrengieigdeddlstpvekflgklvkEKYSTDF-YVLDkFPL------------SVRPFyTMPDAHDERY------ 442
Cdd:cd00777 140 M-----------------------------ERYGFKFlWIVD-FPLfewdeeegrlvsAHHPF-TAPKEEDLDLlekdpe 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 443 ---SNSYDMFMRGEEILSGAQRIHDADMLV----------ERAKhhqvdlAKIQSYIDSFKYGCPPHAGGGIGLERVTML 509
Cdd:cd00777 189 darAQAYDLVLNGVELGGGSIRIHDPDIQEkvfeilglseEEAE------EKFGFLLEAFKYGAPPHGGIALGLDRLVML 262
|
330
....*....|....
gi 17551876 510 FLGLHNIRLASLFP 523
Cdd:cd00777 263 LTGSESIRDVIAFP 276
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
74-517 |
3.29e-31 |
|
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: 127.42 E-value: 3.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 74 EINVSNATKDV----WVrgriHTTRSKGKNCFLVLR--QGVytVQVamFMNEKISKQMLKFVSSISKESIVDV------- 140
Cdd:COG0173 9 ELRESDVGQEVtlsgWV----HRRRDHGGLIFIDLRdrYGI--TQV--VFDPDDSAEAFEKAEKLRSEYVIAVtgkvrar 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 141 -YATINKvdnpiesctqK----DVELLAQQVFVVSTSAPkLPLQIEDasrraptdEEKASEqenqlavvnlDTRLDNRVI 215
Cdd:COG0173 81 pEGTVNP----------KlptgEIEVLASELEILNKAKT-PPFQIDD--------DTDVSE----------ELRLKYRYL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 216 DLRTPTSHAIFRIQAGICNQFRNILDVRGFVEIMAPkIISAPSEGGANVFEV-S-YFKGSAY-LAQSPQLYKQ--MaIAG 290
Cdd:COG0173 132 DLRRPEMQKNLILRHKVTKAIRNYLDENGFLEIETP-ILTKSTPEGARDYLVpSrVHPGKFYaLPQSPQLFKQllM-VSG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 291 dFEKVYTIGPVFRAEDSNTHRHMtEFVGLDLEMAF---NfhyhEVMETIAEVLTQMFKglqqnyqdeiaAVGNQYPAEPF 367
Cdd:COG0173 210 -FDRYFQIARCFRDEDLRADRQP-EFTQLDIEMSFvdqE----DVFELMEGLIRHLFK-----------EVLGVELPTPF 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 368 QfcepplILKYPDAITL-------LReNGIEIGD---------------------------------------------- 394
Cdd:COG0173 273 P------RMTYAEAMERygsdkpdLR-FGLELVDvtdifkdsgfkvfagaaenggrvkainvpggaslsrkqideltefa 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 395 --------------EDDLSTPVEKFLGKLVKEKYST-------D--FYVLDK---------------------------- 423
Cdd:COG0173 346 kqygakglayikvnEDGLKSPIAKFLSEEELAAILErlgakpgDliFFVADKpkvvnkalgalrlklgkelglidedefa 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 424 ------FPL------SVR------PFyTMPDAHDERY---------SNSYDMFMRGEEILSGAQRIHDADMLV------- 469
Cdd:COG0173 426 flwvvdFPLfeydeeEGRwvamhhPF-TMPKDEDLDLletdpgkvrAKAYDLVLNGYELGGGSIRIHDPELQEkvfellg 504
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 17551876 470 ---ERAKhhqvdlAKIQSYIDSFKYGCPPHAGGGIGLERVTMLFLGLHNIR 517
Cdd:COG0173 505 iseEEAE------EKFGFLLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIR 549
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
82-526 |
8.60e-26 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 111.22 E-value: 8.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 82 KDVWVRGRIHTTRSKGKNCFLVLRQG--VYTVQVAMFMNEKISKQMLKfvSSISKESIVDVYATINKVDNpiescTQKDV 159
Cdd:PLN02603 108 KTLNVMGWVRTLRAQSSVTFIEVNDGscLSNMQCVMTPDAEGYDQVES--GLITTGASVLVQGTVVSSQG-----GKQKV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 160 ELLAQQVFVVSTSAPKLPLQIEDASRRAptdeekaseqenqlavvnLDTRLDNRVidlRTPTSHAIFRIQAGICNQFRNI 239
Cdd:PLN02603 181 ELKVSKIVVVGKSDPSYPIQKKRVSREF------------------LRTKAHLRP---RTNTFGAVARVRNALAYATHKF 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 240 LDVRGFVEIMAPKIISAPSEGGANVFEVS------------------------------YFKGSAYLAQSPQLYKQmAIA 289
Cdd:PLN02603 240 FQENGFVWVSSPIITASDCEGAGEQFCVTtlipnsaenggslvddipktkdglidwsqdFFGKPAFLTVSGQLNGE-TYA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 290 GDFEKVYTIGPVFRAEDSNTHRHMTEFVGLDLEMAFNfHYHEVMETIAEVLTQMFKGLQQNYQDEIaavgnqypaEPFQ- 368
Cdd:PLN02603 319 TALSDVYTFGPTFRAENSNTSRHLAEFWMIEPELAFA-DLNDDMACATAYLQYVVKYILENCKEDM---------EFFNt 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 369 FCEPPLI-------------LKYPDAITLLrengieIGDEDDLSTPVEKFLG-KLVKEKYSTDF------YVLDKFPLSV 428
Cdd:PLN02603 389 WIEKGIIdrlsdvveknfvqLSYTDAIELL------LKAKKKFEFPVKWGLDlQSEHERYITEEafggrpVIIRDYPKEI 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 429 RPFYtMPDAHDERYSNSYDMFM-RGEEILSGAQRIHDADMLVERAKHHQVDLAKIQSYIDSFKYGCPPHAGGGIGLERVT 507
Cdd:PLN02603 463 KAFY-MRENDDGKTVAAMDMLVpRVGELIGGSQREERLEYLEARLDELKLNKESYWWYLDLRRYGSVPHAGFGLGFERLV 541
|
490
....*....|....*....
gi 17551876 508 MLFLGLHNIRLASLFPRDP 526
Cdd:PLN02603 542 QFATGIDNIRDAIPFPRVP 560
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
75-531 |
1.49e-24 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 107.76 E-value: 1.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 75 INVSNATKDVWVRGRIHTTRSKGKNCFLVLRQGVYTVQvAMFMNEKISKQMLKFVSSISKESIVDVYATINK----VDNP 150
Cdd:PRK12820 12 LSLDDTGREVCLAGWVDAFRDHGELLFIHLRDRNGFIQ-AVFSPEAAPADVYELAASLRAEFCVALQGEVQKrleeTENP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 151 -IESctqKDVELLAQQVFVVSTSApKLPLQIEDASRRAPTDEEKASEqenqlavVNLDTRLDNRVIDLRTPTSHAIFRIQ 229
Cdd:PRK12820 91 hIET---GDIEVFVRELSILAASE-ALPFAISDKAMTAGAGSAGADA-------VNEDLRLQYRYLDIRRPAMQDHLAKR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 230 AGICNQFRNILDVRGFVEIMAPKIISAPSEGGANVFEVSYFKGSAY--LAQSPQLYKQMAIAGDFEKVYTIGPVFRAEDS 307
Cdd:PRK12820 160 HRIIKCARDFLDSRGFLEIETPILTKSTPEGARDYLVPSRIHPKEFyaLPQSPQLFKQLLMIAGFERYFQLARCFRDEDL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 308 NTHRHmTEFVGLDLEMAFnFHYHEVMETIAEVLTQMFK--GL-------QQNYQDEIAAVGNQYPAEPFQfceppliLKY 378
Cdd:PRK12820 240 RPNRQ-PEFTQLDIEASF-IDEEFIFELIEELTARMFAigGIalprpfpRMPYAEAMDTTGSDRPDLRFD-------LKF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 379 PDAITLL----------------RENGIEI-GDEDDLSTPV-------------------------------------EK 404
Cdd:PRK12820 311 ADATDIFentrygifkqilqrggRIKGINIkGQSEKLSKNVlqneyakeiapsfgakgmtwmraeaggldsnivqffsAD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 405 FLGKLVKEKYSTD-------------------------------------FYVL--DKFPL-----------SVRPFyTM 434
Cdd:PRK12820 391 EKEALKRRFHAEDgdviimiadascaivlsalgqlrlhladrlglipegvFHPLwiTDFPLfeatddggvtsSHHPF-TA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 435 PDAHD----------ERYSNSYDMFMRGEEILSGAQRIHDADmlVERAKHHQVDLA------KIQSYIDSFKYGCPPHAG 498
Cdd:PRK12820 470 PDREDfdpgdieellDLRSRAYDLVVNGEELGGGSIRINDKD--IQLRIFAALGLSeediedKFGFFLRAFDFAAPPHGG 547
|
570 580 590
....*....|....*....|....*....|...
gi 17551876 499 GGIGLERVTMLFLGLHNIRLASLFPRDPKRLTP 531
Cdd:PRK12820 548 IALGLDRVVSMILQTPSIREVIAFPKNRSAACP 580
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
1-523 |
2.05e-24 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 107.00 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 1 MADAAEGEQPKLSKKELNKLARKAKKDEKAGEK-GGNQQQAAAMDQEDASKDFYgsyglVNSKEKKVLNfLKVKEIN--- 76
Cdd:PLN02502 8 LSKNALKKRLKAKQAEEEKAAKEEAKAAAAAAAaKGRSRKSAAADDETMDPTQY-----RANRLKKVEA-LRAKGVEpyp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 77 ------------------VSNATKD----VWVRGRIHTTRSKGKNCFLVLRQGVYTVQVaMFMNEKISKQ---MLKFVSS 131
Cdd:PLN02502 82 ykfdvthtapelqekygsLENGEELedvsVSVAGRIMAKRAFGKLAFYDLRDDGGKIQL-YADKKRLDLDeeeFEKLHSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 132 ISKESIVDVYATINKVDNPIESCTQKDVELLaqqvfvvSTSAPKLPlqiedasrraptdeEKASEQENQlavvnlDTRLD 211
Cdd:PLN02502 161 VDRGDIVGVTGTPGKTKKGELSIFPTSFEVL-------TKCLLMLP--------------DKYHGLTDQ------ETRYR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 212 NRVIDL-RTPTSHAIFRIQAGICNQFRNILDVRGFVEIMAPKIISAPseGGANVFEVSYFKGSA----YLAQSPQLYKQM 286
Cdd:PLN02502 214 QRYLDLiANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPMLNMIA--GGAAARPFVTHHNDLnmdlYLRIATELHLKR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 287 AIAGDFEKVYTIGPVFRAEDSNThRHMTEFVGLDLEMAFNfHYHEVMETIAEVLTQMFKGLQQNYQdeIaavgnQYPAEP 366
Cdd:PLN02502 292 LVVGGFERVYEIGRQFRNEGIST-RHNPEFTTCEFYQAYA-DYNDMMELTEEMVSGMVKELTGSYK--I-----KYHGIE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 367 FQFcEPPliLKYPDAITLLREnGIEIGDEDDLSTPVEKFLGKLVKEKY-------STDFYVLDKF------PLSVRPFYT 433
Cdd:PLN02502 363 IDF-TPP--FRRISMISLVEE-ATGIDFPADLKSDEANAYLIAACEKFdvkcpppQTTGRLLNELfeefleETLVQPTFV 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 434 M-------PDA--H------DERysnsYDMFMRGEEILSGAQRIHDA----DMLVERAKHHQVD----LAKIQSYIDSFK 490
Cdd:PLN02502 439 LdhpvemsPLAkpHrskpglTER----FELFINGRELANAFSELTDPvdqrERFEEQVKQHNAGddeaMALDEDFCTALE 514
|
570 580 590
....*....|....*....|....*....|...
gi 17551876 491 YGCPPHAGGGIGLERVTMLFLGLHNIRLASLFP 523
Cdd:PLN02502 515 YGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFP 547
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
74-524 |
3.99e-24 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 106.41 E-value: 3.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 74 EINVSNATKDVWVRGRIHTTRSKGKNCFLVLRQGVYTVQVAMFMNEkiSKQMLKFVSSISKESIVDVYATINKvdNPIES 153
Cdd:PLN02903 65 ALSVNDVGSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDE--FPEAHRTANRLRNEYVVAVEGTVRS--RPQES 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 154 CTQK----DVELLAQQVFVVSTSAPKLPLQIEDAsrraptDEEKASEQEnqlavvnlDTRLDNRVIDLRTPTSHAIFRIQ 229
Cdd:PLN02903 141 PNKKmktgSVEVVAESVDILNVVTKSLPFLVTTA------DEQKDSIKE--------EVRLRYRVLDLRRPQMNANLRLR 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 230 AGICNQFRNIL-DVRGFVEIMAPkIISAPSEGGANVFEV-SYFK-GSAY-LAQSPQLYKQMAIAGDFEKVYTIGPVFRAE 305
Cdd:PLN02903 207 HRVVKLIRRYLeDVHGFVEIETP-ILSRSTPEGARDYLVpSRVQpGTFYaLPQSPQLFKQMLMVSGFDRYYQIARCFRDE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 306 DSNTHRHmTEFVGLDLEMAF-------------------------------NFHYHEVME----------------TIAE 338
Cdd:PLN02903 286 DLRADRQ-PEFTQLDMELAFtpledmlklnedlirqvfkeikgvqlpnpfpRLTYAEAMSkygsdkpdlryglelvDVSD 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 339 VLT----QMFKGLQQN--------------------------YQDEIAAVGNQYP----AEPFQFCEPPLI---LKYPDA 381
Cdd:PLN02903 365 VFAessfKVFAGALESggvvkaicvpdgkkisnntalkkgdiYNEAIKSGAKGLAflkvLDDGELEGIKALvesLSPEQA 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 382 ITLLRENGIEIGD---------------EDDLSTPVEKFLGKLVKEKYS----TDFYVLDKFPLSVR------PFyTMPD 436
Cdd:PLN02903 445 EQLLAACGAGPGDlilfaagptssvnktLDRLRQFIAKTLDLIDPSRHSilwvTDFPMFEWNEDEQRlealhhPF-TAPN 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 437 AHD-ERYSN----SYDMFMRGEEILSGAQRIHDADmlVERAKHHQVDLAKIQS------YIDSFKYGCPPHAGGGIGLER 505
Cdd:PLN02903 524 PEDmGDLSSaralAYDMVYNGVEIGGGSLRIYRRD--VQQKVLEAIGLSPEEAeskfgyLLEALDMGAPPHGGIAYGLDR 601
|
570
....*....|....*....
gi 17551876 506 VTMLFLGLHNIRLASLFPR 524
Cdd:PLN02903 602 LVMLLAGAKSIRDVIAFPK 620
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
226-523 |
2.07e-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: 98.04 E-value: 2.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 226 FRIQAGICNQFRNILDVRGFVEIMAPkiISAPSEGGANV--FEVSY--FKGSAYLAQSPQLYKQMAIAGDFEKVYTIGPV 301
Cdd:cd00775 8 FIVRSKIISYIRKFLDDRGFLEVETP--MLQPIAGGAAArpFITHHnaLDMDLYLRIAPELYLKRLIVGGFERVYEIGRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 302 FRAEDSNThRHMTEFVGLDLEMAFNfHYHEVMETIAEVLTQMFKGLQQNYQDEiaavgnqYPAEPFQFCEPPLILKYPDA 381
Cdd:cd00775 86 FRNEGIDL-THNPEFTMIEFYEAYA-DYNDMMDLTEDLFSGLVKKINGKTKIE-------YGGKELDFTPPFKRVTMVDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 382 ITllRENGIEIGDEDDLSTP-VEKFLGKLVKEKYS---TDFYVLDK------------------FPLSVRPFyTMPDAHD 439
Cdd:cd00775 157 LK--EKTGIDFPELDLEQPEeLAKLLAKLIKEKIEkprTLGKLLDKlfeefveptliqptfiidHPVEISPL-AKRHRSN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 440 ERYSNSYDMFMRGEEILSGAQRIHDADMLVER------AKHHQVDLAKI--QSYIDSFKYGCPPHAGGGIGLERVTMLFL 511
Cdd:cd00775 234 PGLTERFELFICGKEIANAYTELNDPFDQRERfeeqakQKEAGDDEAMMmdEDFVTALEYGMPPTGGLGIGIDRLVMLLT 313
|
330
....*....|..
gi 17551876 512 GLHNIRLASLFP 523
Cdd:cd00775 314 DSNSIRDVILFP 325
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
207-523 |
3.70e-22 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 99.75 E-value: 3.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 207 DTRLDNRVIDL-RTPTSHAIFRIQAGICNQFRNILDVRGFVEIMAPKIISAPSEGGANVFEVSY--FKGSAYLAQSPQLY 283
Cdd:PRK12445 164 EVRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHnaLDLDMYLRIAPELY 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 284 KQMAIAGDFEKVYTIGPVFRAEDSNThRHMTEFVGLDLEMAFNfHYHEVMEtiaeVLTQMFKGLQQNYqdeIAAVGNQYP 363
Cdd:PRK12445 244 LKRLVVGGFERVFEINRNFRNEGISV-RHNPEFTMMELYMAYA-DYHDLIE----LTESLFRTLAQEV---LGTTKVTYG 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 364 AEPFQFCEPPLILKYPDAITLLRENgIEIGDEDD----------LSTPVEKF--LGKLVKEKYS-------TDFYVLDKF 424
Cdd:PRK12445 315 EHVFDFGKPFEKLTMREAIKKYRPE-TDMADLDNfdaakalaesIGITVEKSwgLGRIVTEIFDevaeahlIQPTFITEY 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 425 PLSVRPFYTMPDAHDErYSNSYDMFMRGEEILSGAQRIHDADMLVER------AKHHQVDLAKI--QSYIDSFKYGCPPH 496
Cdd:PRK12445 394 PAEVSPLARRNDVNPE-ITDRFEFFIGGREIGNGFSELNDAEDQAERfqeqvnAKAAGDDEAMFydEDYVTALEYGLPPT 472
|
330 340
....*....|....*....|....*..
gi 17551876 497 AGGGIGLERVTMLFLGLHNIRLASLFP 523
Cdd:PRK12445 473 AGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
80-523 |
5.34e-21 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 96.64 E-value: 5.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 80 ATKDVWVRGRIHTTRSKGKNCFLVLRQGVYTVQVAMFMNEKISKQMLK-FVSSISKESIVDVYATINKVDNPIESCTQKD 158
Cdd:PTZ00385 106 AQATVRVAGRVTSVRDIGKIIFVTIRSNGNELQVVGQVGEHFTREDLKkLKVSLRVGDIIGADGVPCRMQRGELSVAASR 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 159 VELLAQQVFVVSTSAPKLplqiedasrraptdEEKASEQENqlavvnlDTRLDNRVIDLRT-PTSHAIFRIQAGICNQFR 237
Cdd:PTZ00385 186 MLILSPYVCTDQVVCPNL--------------RGFTVLQDN-------DVKYRYRFTDMMTnPCVIETIKKRHVMLQALR 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 238 NILDVRGFVEIMAPKIISAPSEGGANVFeVSYFKGSA---YLAQSPQLYKQMAIAGDFEKVYTIGPVFRAEDSNtHRHMT 314
Cdd:PTZ00385 245 DYFNERNFVEVETPVLHTVASGANAKSF-VTHHNANAmdlFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDAD-RSHNP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 315 EFVGLDLEMAFNfHYHEVMETIAEVLTQMFKGLQQNYQDEIA---AVGNQYPAE---PFQfceppLILKYpDAITllREN 388
Cdd:PTZ00385 323 EFTSCEFYAAYH-TYEDLMPMTEDIFRQLAMRVNGTTVVQIYpenAHGNPVTVDlgkPFR-----RVSVY-DEIQ--RMS 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 389 GIEIGDEDDLSTP----------------------VEKFLGKLVkekystDFYVLDKF--PLSV--RPFYTMPDA--HDE 440
Cdd:PTZ00385 394 GVEFPPPNELNTPkgiaymsvvmlryniplppvrtAAKMFEKLI------DFFITDRVvePTFVmdHPLFMSPLAkeQVS 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 441 R--YSNSYDMFMRGEEILSGAQRIHDADMLVERAKHHQVD--------LAKIQSYIDSFKYGCPPHAGGGIGLERVTMLF 510
Cdd:PTZ00385 468 RpgLAERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLVDrqggdeeaMPLDETFLKSLQVGLPPTAGWGMGIDRALMLL 547
|
490
....*....|...
gi 17551876 511 LGLHNIRLASLFP 523
Cdd:PTZ00385 548 TNSSNIRDGIIFP 560
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
257-528 |
7.93e-21 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 95.83 E-value: 7.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 257 PSEGGANVFEVSYFKGSAYLAQSPQLYKQmAIAGDFEKVYTIGPVFRAEDSNTHRHMTEFVGLDLEMAFNfHYHEVMETI 336
Cdd:PLN02221 292 PKKDGKIDYSKDFFGRQAFLTVSGQLQVE-TYACALSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFA-DLEDDMNCA 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 337 AEVLTQMFKGLQQNYQDEIAAVGNQY-----------PAEPFQFceppliLKYPDAITLLRE---------NGIEIGDed 396
Cdd:PLN02221 370 EAYVKYMCKWLLDKCFDDMELMAKNFdsgcidrlrmvASTPFGR------ITYTEAIELLEEavakgkefdNNVEWGI-- 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 397 DLSTPVEKFLGKLVKEKYstdfYVLDKFPLSVRPFYtMPDAHDERYSNSYDMFM-RGEEILSGAQRIHDADMLVERAKHH 475
Cdd:PLN02221 442 DLASEHERYLTEVLFQKP----LIVYNYPKGIKAFY-MRLNDDEKTVAAMDVLVpKVGELIGGSQREERYDVIKQRIEEM 516
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 17551876 476 QVDLAKIQSYIDSFKYGCPPHAGGGIGLERVTMLFLGLHNIRLASLFPRDPKR 528
Cdd:PLN02221 517 GLPIEPYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRYPGK 569
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
265-526 |
1.32e-19 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 92.01 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 265 FEVSYFKGSAYLAQSPQLYKQmAIAGDFEKVYTIGPVFRAEDSNTHRHMTEFVGLDLEMAFNFHYH--EVMET-----IA 337
Cdd:PTZ00425 317 YKKDFFSKQAFLTVSGQLSLE-NLCSSMGDVYTFGPTFRAENSHTSRHLAEFWMIEPEIAFADLYDnmELAESyikycIG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 338 EVLTQMFKGL---QQNYQDEIAAVGNQYPAEPFQfcepplILKYPDAITLLR--ENGIEIGDE--DDLSTPVEKFlgklV 410
Cdd:PTZ00425 396 YVLNNNFDDIyyfEENVETGLISRLKNILDEDFA------KITYTNVIDLLQpySDSFEVPVKwgMDLQSEHERF----V 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 411 KEKYSTDFYVLDKFPLSVRPFYtMPDAHDERYSNSYDMFM-RGEEILSGAQRIHDADMLVERAKHHQVDLAKIQSYIDSF 489
Cdd:PTZ00425 466 AEQIFKKPVIVYNYPKDLKAFY-MKLNEDQKTVAAMDVLVpKIGEVIGGSQREDNLERLDKMIKEKKLNMESYWWYRQLR 544
|
250 260 270
....*....|....*....|....*....|....*..
gi 17551876 490 KYGCPPHAGGGIGLERVTMLFLGLHNIRLASLFPRDP 526
Cdd:PTZ00425 545 KFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPRYP 581
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
207-523 |
2.96e-18 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 88.14 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 207 DTRLDNRVIDLR-TPTSHAIFRIQAGICNQFRNILDVRGFVEIMAPKIISAPSEGGANVFEVSY--FKGSAYLAQSPQLY 283
Cdd:PTZ00417 233 EIRYRQRYLDLMiNESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHndLDLDLYLRIATELP 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 284 KQMAIAGDFEKVYTIGPVFRAED-SNTHRhmTEFVGLDLEMAFNfHYHEVMETIAEVLTQMFKGLQQNYQ---------- 352
Cdd:PTZ00417 313 LKMLIVGGIDKVYEIGKVFRNEGiDNTHN--PEFTSCEFYWAYA-DFYDLIKWSEDFFSQLVMHLFGTYKilynkdgpek 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 353 -----------------DEIAAVGNQYPAEPFQfcEPPLILKypdAITLLRENGIEIGDEDDLSTPVEKFLGKLVKEKYS 415
Cdd:PTZ00417 390 dpieidftppypkvsivEELEKLTNTKLEQPFD--SPETINK---MINLIKENKIEMPNPPTAAKLLDQLASHFIENKYP 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 416 TDFYVLDKFPLSVRPfytMPDAHDER--YSNSYDMFMRGEEILSGAQRIHDADMLVERAKHHQVDLAK--------IQSY 485
Cdd:PTZ00417 465 NKPFFIIEHPQIMSP---LAKYHRSKpgLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKgdaeafqfDAAF 541
|
330 340 350
....*....|....*....|....*....|....*...
gi 17551876 486 IDSFKYGCPPHAGGGIGLERVTMLFLGLHNIRLASLFP 523
Cdd:PTZ00417 542 CTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFP 579
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
70-523 |
1.52e-16 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 82.06 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 70 LKVKEINVSNAtkdvwvrGRIHTTRSKGKNCFLVLRQGVYTVQVaMFMNEKISKQMLKFVSSISKESIVDVYATINKvdn 149
Cdd:PRK00484 50 LEELEIEVSVA-------GRVMLKRVMGKASFATLQDGSGRIQL-YVSKDDVGEEALEAFKKLDLGDIIGVEGTLFK--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 150 piescTQKDvEL--LAQQVFVVSTSApkLPLqiedasrraP------TDEEkaseqenqlavvnldTRLDNRVIDLRT-P 220
Cdd:PRK00484 119 -----TKTG-ELsvKATELTLLTKSL--RPL---------PdkfhglTDVE---------------TRYRQRYVDLIVnP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 221 TSHAIFRIQAGICNQFRNILDVRGFVEIMAPKIISAPseGGA---------NVFEVSYfkgsaYLAQSPQLYKQMAIAGD 291
Cdd:PRK00484 167 ESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIA--GGAaarpfithhNALDIDL-----YLRIAPELYLKRLIVGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 292 FEKVYTIGPVFRAEDSNThRHMTEFVGLDLEMAFnFHYHEVM----ETIAEVLTQMFKGLQQNYQD-EI----------- 355
Cdd:PRK00484 240 FERVYEIGRNFRNEGIDT-RHNPEFTMLEFYQAY-ADYNDMMdlteELIRHLAQAVLGTTKVTYQGtEIdfgppfkrltm 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 356 -AAVgNQYPAEPFqfceppLILKYPDAITLLRENGIEIGDEDDLSTPVEKFLGKLVKEKYSTDFYVLDkFPLSVRPFyTM 434
Cdd:PRK00484 318 vDAI-KEYTGVDF------DDMTDEEARALAKELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITD-YPVEISPL-AK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 435 PDAHDERYSNSYDMFMRGEEILSG----------AQRIHdaDMLVERAK----HHQVDlakiQSYIDSFKYGCPPHAGGG 500
Cdd:PRK00484 389 RHREDPGLTERFELFIGGREIANAfselndpidqRERFE--AQVEAKEAgddeAMFMD----EDFLRALEYGMPPTGGLG 462
|
490 500
....*....|....*....|...
gi 17551876 501 IGLERVTMLFLGLHNIRLASLFP 523
Cdd:PRK00484 463 IGIDRLVMLLTDSPSIRDVILFP 485
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
84-171 |
9.70e-16 |
|
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: 72.21 E-value: 9.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 84 VWVRGRIHTTRSKGKNCFLVLRQGVYTVQVamFMNEKISKQMLKFVSSISKESIVDVYATINKVdnPIESCTQKDVELLA 163
Cdd:cd04100 2 VTLAGWVHSRRDHGGLIFIDLRDGSGIVQV--VVNKEELGEFFEEAEKLRTESVVGVTGTVVKR--PEGNLATGEIELQA 77
|
....*...
gi 17551876 164 QQVFVVST 171
Cdd:cd04100 78 EELEVLSK 85
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
207-523 |
1.36e-15 |
|
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA synthetase (class II) is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440803 [Multi-domain] Cd Length: 495 Bit Score: 79.31 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 207 DTRLDNRVIDLRT-PTSHAIFRIQAGICNQFRNILDVRGFVEIMAPKIISAPseGGANvfevsyfkgsA----------- 274
Cdd:COG1190 154 ETRYRQRYVDLIVnPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIA--GGAA----------Arpfithhnald 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 275 ---YLAQSPQLYKQMAIAGDFEKVYTIGPVFRAEDSNThRHMTEFVGLDLEMAF-NfhYHEVM----ETIAEVLTQMFKG 346
Cdd:COG1190 222 mdlYLRIAPELYLKRLIVGGFERVFEIGRNFRNEGIDT-THNPEFTMLELYQAYaD--YNDMMdlteELIREAAEAVLGT 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 347 LQQNYQdeiaavGNQYP-AEPFQ---FCEppLILKY-----------PDAITLLRENGIEIGDEDDLSTPVEKFLGKLVK 411
Cdd:COG1190 299 TKVTYQ------GQEIDlSPPWRritMVE--AIKEAtgidvtpltddEELRALAKELGIEVDPGWGRGKLIDELFEELVE 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 412 EKYSTDFYVLDkFPLSVRPFyTMPDAHDERYSNSYDMFMRGEEIlsgA-----------QRIHDADMLVERAK----HHQ 476
Cdd:COG1190 371 PKLIQPTFVTD-YPVEVSPL-AKRHRDDPGLTERFELFIAGREI---AnafselndpidQRERFEEQLELKAAgddeAMP 445
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 17551876 477 VDlakiQSYIDSFKYGCPPHAGGGIGLERVTMLFLGLHNIRLASLFP 523
Cdd:COG1190 446 MD----EDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 488
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
265-524 |
4.42e-15 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 77.99 E-value: 4.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 265 FEVSYFKGSAYLAQSPQLYKQmAIAGDFEKVYTIGPVFRAEDSNTHRHMTEFVGLDLEMAFNfHYHEVMETIAEVLTQMF 344
Cdd:PLN02532 363 FSKDFFSRPTYLTVSGRLHLE-SYACALGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFS-ELEDAMNCAEDYFKFLC 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 345 KGLQQNYQDEIAAVGNQYPAEPFQFCE-----PPLILKYPDAITLLRE---NGIEIGDEddLSTPV-EKFLGKLVKEKYS 415
Cdd:PLN02532 441 KWVLENCSEDMKFVSKRIDKTISTRLEaiissSLQRISYTEAVDLLKQatdKKFETKPE--WGIALtTEHLSYLADEIYK 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 416 TDFYVLDkFPLSVRPFYTMPDaHDERYSNSYDMFM-RGEEILSGAQRIHDADMLVERAKHHQVDLAKIQSYIDSFKYGCP 494
Cdd:PLN02532 519 KPVIIYN-YPKELKPFYVRLN-DDGKTVAAFDLVVpKVGTVITGSQNEERMDILNARIEELGLPREQYEWYLDLRRHGTV 596
|
250 260 270
....*....|....*....|....*....|
gi 17551876 495 PHAGGGIGLERVTMLFLGLHNIRLASLFPR 524
Cdd:PLN02532 597 KHSGFSLGFELMVLFATGLPDVRDAIPFPR 626
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
236-505 |
4.13e-13 |
|
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: 68.30 E-value: 4.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 236 FRNILDVRGFVEIMAPKIISAPSEGGANVFEV------SYFKGSAYLAQSPQLYK-QMAIAGD---FEKVYTIGPVFRAE 305
Cdd:cd00768 9 LRRFMAELGFQEVETPIVEREPLLEKAGHEPKdllpvgAENEEDLYLRPTLEPGLvRLFVSHIrklPLRLAEIGPAFRNE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 306 DSNTH-RHMTEFVGLDLEMAFnfhyhevmETIAEVLTqmFKGLQQNYQDeiaavgnqypaepfqfcepplilkypdaitL 384
Cdd:cd00768 89 GGRRGlRRVREFTQLEGEVFG--------EDGEEASE--FEELIELTEE------------------------------L 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 385 LRENGIEIgdeddlstpvekflgklvkekystDFYVLDKFPLSVRPFYtmpdahderYSNSYDMFM-----RGEEILSGA 459
Cdd:cd00768 129 LRALGIKL------------------------DIVFVEKTPGEFSPGG---------AGPGFEIEVdhpegRGLEIGSGG 175
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 17551876 460 QRIHDADMLVERAKhhqvdlakiqsYIDSFKYGCPPHAGGGIGLER 505
Cdd:cd00768 176 YRQDEQARAADLYF-----------LDEALEYRYPPTIGFGLGLER 210
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
84-169 |
3.92e-09 |
|
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: 53.39 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 84 VWVRGRIHT-TRSKGKNCFLVLRQGVYTVQVAMFmnekiSKQMLKFVSSISKESIVDVYATINKVDNpiesctqKDVELL 162
Cdd:pfam01336 1 VTVAGRVTSiRRSGGKLLFLTLRDGTGSIQVVVF-----KEEAEKLAKKLKEGDVVRVTGKVKKRKG-------GELELV 68
|
....*..
gi 17551876 163 AQQVFVV 169
Cdd:pfam01336 69 VEEIELL 75
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
72-523 |
2.01e-07 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 53.81 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 72 VKEINVSNATKDVWVRGRIHTTRSKGKNCFLVLRQGVYTVQVAMFMNEKISKQMLKFVSSISKESIVDVYATINKVDNPI 151
Cdd:PRK02983 642 VAEALDAPTGEEVSVSGRVLRIRDYGGVLFADLRDWSGELQVLLDASRLEQGSLADFRAAVDLGDLVEVTGTMGTSRNGT 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 152 ESctqkdveLLAQQVFVVSTSAPKLPlqiedASRRAPTDEEkaseqenqlavvnldTRLDNRVIDLRT-PTSHAIFRIQA 230
Cdd:PRK02983 722 LS-------LLVTSWRLAGKCLRPLP-----DKWKGLTDPE---------------ARVRQRYLDLAVnPEARDLLRARS 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 231 GICNQFRNILDVRGFVEIMAPkiISAPSEGGAN----VFEVSYFKGSAYLAQSPQLY-KQMAIAGdFEKVYTIGPVFRAE 305
Cdd:PRK02983 775 AVVRAVRETLVARGFLEVETP--ILQQVHGGANarpfVTHINAYDMDLYLRIAPELYlKRLCVGG-VERVFELGRNFRNE 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 306 DSNtHRHMTEFVGLDlemAFNFH--YHEVMEtiaevLTQ-MFKGLQQNYQDE--IAAVGNQYPAEPFQFCEP-PLILKYp 379
Cdd:PRK02983 852 GVD-ATHNPEFTLLE---AYQAHadYDTMRD-----LTReLIQNAAQAAHGApvVMRPDGDGVLEPVDISGPwPVVTVH- 921
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 380 DAITllRENGIEIgdedDLSTPVEKFL----------------GKLVKEKY------STD---FYVldKFPLSVRPFyTM 434
Cdd:PRK02983 922 DAVS--EALGEEI----DPDTPLAELRklcdaagipyrtdwdaGAVVLELYehlvedRTTfptFYT--DFPTSVSPL-TR 992
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 435 PDAHDERYSNSYDMFMRGEEIlsGAQRIHDADMLVERAKHHQvdlakiQS----------------YIDSFKYGCPPHAG 498
Cdd:PRK02983 993 PHRSDPGLAERWDLVAWGVEL--GTAYSELTDPVEQRRRLTE------QSllaaggdpeameldedFLQALEYAMPPTGG 1064
|
490 500
....*....|....*....|....*
gi 17551876 499 GGIGLERVTMLFLGLhNIRLASLFP 523
Cdd:PRK02983 1065 LGMGVDRLVMLLTGR-SIRETLPFP 1088
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
73-178 |
2.59e-07 |
|
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: 49.24 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 73 KEINVSNATKDVWVRGRIHTTRSKGKNCFLVLRQGVYTVQVAmFMNEKISKQMLKFVSSISKESIVDVYATINKvdnpiE 152
Cdd:cd04316 4 AEITPELDGEEVTVAGWVHEIRDLGGIKFVILRDREGIVQVT-APKKKVDKELFKTVRKLSRESVISVTGTVKA-----E 77
|
90 100
....*....|....*....|....*.
gi 17551876 153 SCTQKDVELLAQQVFVVSTSAPKLPL 178
Cdd:cd04316 78 PKAPNGVEIIPEEIEVLSEAKTPLPL 103
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
74-220 |
1.92e-06 |
|
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: 47.13 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551876 74 EINVSNATKDVWVRGRIHTTRSKGKNCFLVLRQGVYTVQVaMFmnEKISKQMLKFVSSISKESIVDVYATINKvdNPIES 153
Cdd:cd04317 7 ELRESHVGQEVTLCGWVQRRRDHGGLIFIDLRDRYGIVQV-VF--DPEEAPEFELAEKLRNESVIQVTGKVRA--RPEGT 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17551876 154 CTQK----DVELLAQQVFVVSTSAPkLPLQIEdasrraptDEEKASEqenqlavvnlDTRLDNRVIDLRTP 220
Cdd:cd04317 82 VNPKlptgEIEVVASELEVLNKAKT-LPFEID--------DDVNVSE----------ELRLKYRYLDLRRP 133
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
84-147 |
1.08e-04 |
|
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: 41.07 E-value: 1.08e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17551876 84 VWVRGRIHTTRSKGKNCFLVLRQGVYTVQVAMFmnEKISKQMLKfVSSISKESIVDVYATINKV 147
Cdd:cd04323 2 VKVFGWVHRLRSQKKLMFLVLRDGTGFLQCVLS--KKLVTEFYD-AKSLTQESSVEVTGEVKED 62
|
|
| |
