|
Name |
Accession |
Description |
Interval |
E-value |
| aspS_bact |
TIGR00459 |
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be ... |
35-658 |
0e+00 |
|
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be discriminating (6.1.1.12) or nondiscriminating (6.1.1.23). 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_bact, represents aspartyl-tRNA synthetases from the Bacteria and from mitochondria. In some species, this enzyme aminoacylates tRNA for both Asp and Asn; Asp-tRNA(asn) is subsequently transamidated to Asn-tRNA(asn). This model generates very low scores for the archaeal type of aspS and for asnS; scores between the trusted and noise cutoffs represent fragmentary sequences. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 211576 [Multi-domain] Cd Length: 583 Bit Score: 794.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 35 TSTIKQLKGLSSGQKIVLNGWIEqKPKRVGKnLIFGLLRDSNGdIIQLVDNKS-----LLKGFTLEDVVQAVGILSLKR- 108
Cdd:TIGR00459 3 THYCGQLRTEHLGQTVTLAGWVN-RRRDLGG-LIFIDLRDRSG-IVQVVCDPDadalkLAKGLRNEDVVQVKGKVSARPe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 109 --KLSNEDADEYEVQLEDITVLNASNKKPAQMQdfKLSAIYP--PEFRYLQLRNPKYQDFLKKRSSISKEIRNSFNNFDF 184
Cdd:TIGR00459 80 gnINRNLDTGEIEILAESITLLNKSKTPPLIIE--KTDAEEEvrLKYRYLDLRRPEMQQRLKLRHKVTKAVRNFLDQQGF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 185 TEVETPMLFKATPEGAREFLVPTRTKrsdgKPSFYALDQSPQQYKQLLMASGVNKYYQMARCFRDEDLRADRQPEFTQVD 264
Cdd:TIGR00459 158 LEIETPMLTKSTPEGARDYLVPSRVH----KGEFYALPQSPQLFKQLLMVSGVDRYYQIARCFRDEDLRADRQPEFTQID 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 265 MEMAFANSEDVMKIIEKTVSGVWSKFSKkrglLTLDSKgtlVPakkengtvsifRMTYEQAMTSYGIDKPDLRAPDLKII 344
Cdd:TIGR00459 234 MEMSFMTQEDVMELIEKLVSHVFLEVKG----IDLKKP---FP-----------VMTYAEAMERYGSDKPDLRFPLELID 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 345 NLGEFNafshlNKKFPVFEVIILRSAFSNMEEYKERWSFLTNNSNYNYRvpiVLPIENDEQANSNWFENFHAIatfenPH 424
Cdd:TIGR00459 296 VTDLFK-----DSEFKVFSNLINDGGRVKAIRVPGGWAELSRKSIKELR---KFAKEYGAKGLAYLKVNEDGI-----NS 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 425 LITKFLKLKKGDIVCGCTREPNHSIFEnpTPLGRlRQLVLQSEHgkNIYHAVNKDVAswIVDFPLFSPVIIEDksgkkek 504
Cdd:TIGR00459 363 PIKKFLDEKKGKILLERTDAQNGDILL--FGAGS-KKIVLDALG--ALRLKLGKDLG--LVDPDLFSFLWVVD------- 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 505 laYPEYEKD---RLCSTHHPFTMVKLKDYEKLEKTPEKCLGRHYDLVVNGVELGGGSTRIHDPRLQDYIFEdILKIDNAY 581
Cdd:TIGR00459 429 --FPMFEKDkegRLCAAHHPFTMPKDEDLENLEAAPEEALAEAYDLVLNGVELGGGSIRIHDPEVQKKVFE-ILGIDPEE 505
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6325153 582 --ELFGHLLNAFDMGTPPHAGFAIGFDRMCAMICETESIRDVIAFPKSITGADLVVKSPSVIPESILEPYNIKYsNSKK 658
Cdd:TIGR00459 506 arEKFGFLLEAFKYGTPPHAGFALGLDRLMMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFIDEKQLEELSIKY-VVKK 583
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
47-652 |
8.10e-171 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 500.36 E-value: 8.10e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 47 GQKIVLNGWIeQKpKRVGKNLIFGLLRDSNGdIIQLV-----DNKSLLKGFTLEDVVQAVGILSlKRKLSNEDAD----E 117
Cdd:PRK00476 17 GQTVTLCGWV-HR-RRDHGGLIFIDLRDREG-IVQVVfdpdaEAFEVAESLRSEYVIQVTGTVR-ARPEGTVNPNlptgE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 118 YEVQLEDITVLNASNKKPAQMQDfklSAIYPPE----FRYLQLRNPKYQDFLKKRSSISKEIRNSFNNFDFTEVETPMLF 193
Cdd:PRK00476 93 IEVLASELEVLNKSKTLPFPIDD---EEDVSEElrlkYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDNGFLEIETPILT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 194 KATPEGAREFLVPTRTKrsDGKpsFYALDQSPQQYKQLLMASGVNKYYQMARCFRDEDLRADRQPEFTQVDMEMAFANSE 273
Cdd:PRK00476 170 KSTPEGARDYLVPSRVH--PGK--FYALPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEFTQIDIEMSFVTQE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 274 DVMKIIEKTVSGVWSKFSKKRglltldskgtlVPAKkengtvsiF-RMTYEQAMTSYGIDKPDLRAPdLKIINLGE---- 348
Cdd:PRK00476 246 DVMALMEGLIRHVFKEVLGVD-----------LPTP--------FpRMTYAEAMRRYGSDKPDLRFG-LELVDVTDlfkd 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 349 --FNAFSHLNKKFPVFEVIIL--------RSAFSNMEEY-KER------WSFLTNNSnynYRVPIVLPIENDEQANsnwf 411
Cdd:PRK00476 306 sgFKVFAGAANDGGRVKAIRVpggaaqlsRKQIDELTEFaKIYgakglaYIKVNEDG---LKGPIAKFLSEEELAA---- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 412 enfhaiatfenphlITKFLKLKKGDIV---CGCTREPNHSifenptpLGRLRqLVLQSEHG---KNIYHAVnkdvasWIV 485
Cdd:PRK00476 379 --------------LLERTGAKDGDLIffgADKAKVVNDA-------LGALR-LKLGKELGlidEDKFAFL------WVV 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 486 DFPLFspviiedksgkkeklaypEYEKD--RLCSTHHPFTMVKLKDYEKLEKT-PEKCLGRHYDLVVNGVELGGGSTRIH 562
Cdd:PRK00476 431 DFPMF------------------EYDEEegRWVAAHHPFTMPKDEDLDELETTdPGKARAYAYDLVLNGYELGGGSIRIH 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 563 DPRLQDYIFEdILKIDN--AYELFGHLLNAFDMGTPPHAGFAIGFDRMCAMICETESIRDVIAFPKSITGADLVVKSPSV 640
Cdd:PRK00476 493 RPEIQEKVFE-ILGISEeeAEEKFGFLLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFPKTQSAQDLLTGAPSP 571
|
650
....*....|..
gi 6325153 641 IPESILEPYNIK 652
Cdd:PRK00476 572 VDEKQLRELGIR 583
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
47-652 |
2.86e-168 |
|
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: 493.75 E-value: 2.86e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 47 GQKIVLNGWIeQKpKR-VGkNLIFGLLRDSNGdIIQLV----DNKSLLK---GFTLEDVVQAVGILSlKRKLSNEDAD-- 116
Cdd:COG0173 16 GQEVTLSGWV-HR-RRdHG-GLIFIDLRDRYG-ITQVVfdpdDSAEAFEkaeKLRSEYVIAVTGKVR-ARPEGTVNPKlp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 117 --EYEVQLEDITVLNASNKKPAQMQDfklsAIYPPE-----FRYLQLRNPKYQDFLKKRSSISKEIRNSFNNFDFTEVET 189
Cdd:COG0173 91 tgEIEVLASELEILNKAKTPPFQIDD----DTDVSEelrlkYRYLDLRRPEMQKNLILRHKVTKAIRNYLDENGFLEIET 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 190 PMLFKATPEGAREFLVPTRTkrSDGKpsFYALDQSPQQYKQLLMASGVNKYYQMARCFRDEDLRADRQPEFTQVDMEMAF 269
Cdd:COG0173 167 PILTKSTPEGARDYLVPSRV--HPGK--FYALPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADRQPEFTQLDIEMSF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 270 ANSEDVMKIIEKTVSGVWSKFSKKRglltldskgtlVPAKkengtvsiF-RMTYEQAMTSYGIDKPDLRAPdLKIINLGE 348
Cdd:COG0173 243 VDQEDVFELMEGLIRHLFKEVLGVE-----------LPTP--------FpRMTYAEAMERYGSDKPDLRFG-LELVDVTD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 349 ------FNAFSHLNKKFPVFEVIIL-------RSAFSNMEEY-KER------WSFLTNNsnyNYRVPIVLPIENDEQANs 408
Cdd:COG0173 303 ifkdsgFKVFAGAAENGGRVKAINVpggaslsRKQIDELTEFaKQYgakglaYIKVNED---GLKSPIAKFLSEEELAA- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 409 nwfenfhaiatfenphlITKFLKLKKGDI---VCGCTREPNHSifenptpLGRLRqLVLQSEHG---KNIYHAVnkdvas 482
Cdd:COG0173 379 -----------------ILERLGAKPGDLiffVADKPKVVNKA-------LGALR-LKLGKELGlidEDEFAFL------ 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 483 WIVDFPLFspviiedksgkkeklaypEY--EKDRLCSTHHPFTMVKLKDYEKLEKTPEKCLGRHYDLVVNGVELGGGSTR 560
Cdd:COG0173 428 WVVDFPLF------------------EYdeEEGRWVAMHHPFTMPKDEDLDLLETDPGKVRAKAYDLVLNGYELGGGSIR 489
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 561 IHDPRLQDYIFEdILKIDN--AYELFGHLLNAFDMGTPPHAGFAIGFDRMCAMICETESIRDVIAFPKSITGADLVVKSP 638
Cdd:COG0173 490 IHDPELQEKVFE-LLGISEeeAEEKFGFLLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFPKTQSAQDLMTGAP 568
|
650
....*....|....
gi 6325153 639 SVIPESILEPYNIK 652
Cdd:COG0173 569 SEVDEKQLKELHIR 582
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
165-627 |
1.05e-134 |
|
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: 396.18 E-value: 1.05e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 165 LKKRSSISKEIRNSFNNFDFTEVETPMLFKATPEGAREFLVPTRTKrsdgKPSFYALDQSPQQYKQLLMASGVNKYYQMA 244
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGARDFLVPSRLH----PGKFYALPQSPQLFKQLLMVSGFDRYFQIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 245 RCFRDEDLRADRQPEFTQVDMEMAFANSEDVMKIIEKTVSGVWSKFskkrglltldskgtlvpaKKENGTVSIFRMTYEQ 324
Cdd:cd00777 77 RCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEV------------------LGVELTTPFPRMTYAE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 325 AMTSYGidkpdlrapdlkiinlgefnafshlnkkfpvfeviilrsafsnmeeykerWSFLtnnsnynyrvpivlpiende 404
Cdd:cd00777 139 AMERYG--------------------------------------------------FKFL-------------------- 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 405 qansnwfenfhaiatfenphlitkflklkkgdivcgctrepnhsifenptplgrlrqlvlqsehgkniyhavnkdvasWI 484
Cdd:cd00777 149 ------------------------------------------------------------------------------WI 150
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 485 VDFPLFSPVIiedksgkkeklaypeyEKDRLCSTHHPFTMVKLKDYEKLEKTPEKCLGRHYDLVVNGVELGGGSTRIHDP 564
Cdd:cd00777 151 VDFPLFEWDE----------------EEGRLVSAHHPFTAPKEEDLDLLEKDPEDARAQAYDLVLNGVELGGGSIRIHDP 214
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6325153 565 RLQDYIFEDILKID-NAYELFGHLLNAFDMGTPPHAGFAIGFDRMCAMICETESIRDVIAFPKS 627
Cdd:cd00777 215 DIQEKVFEILGLSEeEAEEKFGFLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVIAFPKT 278
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
150-626 |
3.09e-113 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 342.62 E-value: 3.09e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 150 EFRYLQLRNPKYQDFLKKRSSISKEIRNSFNNFDFTEVETPMLFK-ATPEGAREFLVPTRTKRSdgkpsFYALDQSPQQY 228
Cdd:pfam00152 7 KYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKsATPEGARDFLVPSRALGK-----FYALPQSPQLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 229 KQLLMASGVNKYYQMARCFRDEDLRADRQPEFTQVDMEMAFANSEDVMKIIEKTVSGVWSKFSKKRGLLTLDSKGTLvpa 308
Cdd:pfam00152 82 KQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDL--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 309 kkengTVSIFRMTYEQAM----------TSYGIDKPDLRAPDLKIINlgefnafshlnkkfpvfeviilrsafsnmeeyK 378
Cdd:pfam00152 159 -----KKPFPRITYAEAIeklngkdveeLGYGSDKPDLRFLLELVID--------------------------------K 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 379 ERWSFLtnnsnynyrvpivlpiendeqansnwfenfhaiatfenphlitkflklkkgdivcgctrepnhsifenptplgr 458
Cdd:pfam00152 202 NKFNPL-------------------------------------------------------------------------- 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 459 lrqlvlqsehgkniyhavnkdvasWIVDFPlfspviiedksgkkeklaypeyekdrlcSTHHPFTMVKLKDYeklektpe 538
Cdd:pfam00152 208 ------------------------WVTDFP----------------------------AEHHPFTMPKDEDD-------- 227
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 539 KCLGRHYDLVVNGVELGGGSTRIHDPRLQDYIFEDI-LKIDNAYELFGHLLNAFDMGTPPHAGFAIGFDRMCAMICETES 617
Cdd:pfam00152 228 PALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQgLDPEEAEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLES 307
|
....*....
gi 6325153 618 IRDVIAFPK 626
Cdd:pfam00152 308 IREVIAFPK 316
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
47-639 |
1.69e-99 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 318.27 E-value: 1.69e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 47 GQKIVLNGWIEQKpkRVGKNLIFGLLRDSNGdIIQLV-------DNKSLLKGFTLEDVVQAVGILslkRKLSNEDADE-- 117
Cdd:PLN02903 72 GSRVTLCGWVDLH--RDMGGLTFLDVRDHTG-IVQVVtlpdefpEAHRTANRLRNEYVVAVEGTV---RSRPQESPNKkm 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 118 ----YEVQLEDITVLNASNKK------PAQMQDFKLSAIYPPEFRYLQLRNPKYQDFLKKRSSISKEIRNSFNN-FDFTE 186
Cdd:PLN02903 146 ktgsVEVVAESVDILNVVTKSlpflvtTADEQKDSIKEEVRLRYRVLDLRRPQMNANLRLRHRVVKLIRRYLEDvHGFVE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 187 VETPMLFKATPEGAREFLVPTRTKRSDgkpsFYALDQSPQQYKQLLMASGVNKYYQMARCFRDEDLRADRQPEFTQVDME 266
Cdd:PLN02903 226 IETPILSRSTPEGARDYLVPSRVQPGT----FYALPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDME 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 267 MAFANSEDVMKIIEKTVSGVWskfskkrglltLDSKGTLVPAkkengtvSIFRMTYEQAMTSYGIDKPDLRApDLKIINL 346
Cdd:PLN02903 302 LAFTPLEDMLKLNEDLIRQVF-----------KEIKGVQLPN-------PFPRLTYAEAMSKYGSDKPDLRY-GLELVDV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 347 GE------FNAFSHLNKKFPVFEVIIL---RSAFSNmeeykerwSFLTNNSNYNYRV-------PIVLPIENDEqansnw 410
Cdd:PLN02903 363 SDvfaessFKVFAGALESGGVVKAICVpdgKKISNN--------TALKKGDIYNEAIksgakglAFLKVLDDGE------ 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 411 FENFHAIATFENPHLITKFLKL---KKGDIV---CGCTREPNHSifenptpLGRLRQLVLQS----EHGKniyHAVnkdv 480
Cdd:PLN02903 429 LEGIKALVESLSPEQAEQLLAAcgaGPGDLIlfaAGPTSSVNKT-------LDRLRQFIAKTldliDPSR---HSI---- 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 481 aSWIVDFPLFspviiedksgkkeklaypEY--EKDRLCSTHHPFTMVKLKDYEKLEKTpeKCLGrhYDLVVNGVELGGGS 558
Cdd:PLN02903 495 -LWVTDFPMF------------------EWneDEQRLEALHHPFTAPNPEDMGDLSSA--RALA--YDMVYNGVEIGGGS 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 559 TRIHDPRLQDYIFEDI-LKIDNAYELFGHLLNAFDMGTPPHAGFAIGFDRMCAMICETESIRDVIAFPKSITGADLVVKS 637
Cdd:PLN02903 552 LRIYRRDVQQKVLEAIgLSPEEAESKFGYLLEALDMGAPPHGGIAYGLDRLVMLLAGAKSIRDVIAFPKTTTAQCALTRA 631
|
..
gi 6325153 638 PS 639
Cdd:PLN02903 632 PS 633
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
46-646 |
5.70e-91 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 297.28 E-value: 5.70e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 46 SGQKIVLNGWIEQKpkRVGKNLIFGLLRDSNGdIIQLV--------DNKSLLKGFTLEDVVQAVGilSLKRKLSNED--- 114
Cdd:PRK12820 17 TGREVCLAGWVDAF--RDHGELLFIHLRDRNG-FIQAVfspeaapaDVYELAASLRAEFCVALQG--EVQKRLEETEnph 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 115 --ADEYEVQLEDITVLNASNKKPAQMQDFKLSAIYPP------------EFRYLQLRNPKYQDFLKKRSSISKEIRNSFN 180
Cdd:PRK12820 92 ieTGDIEVFVRELSILAASEALPFAISDKAMTAGAGSagadavnedlrlQYRYLDIRRPAMQDHLAKRHRIIKCARDFLD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 181 NFDFTEVETPMLFKATPEGAREFLVPTRTKrsdgKPSFYALDQSPQQYKQLLMASGVNKYYQMARCFRDEDLRADRQPEF 260
Cdd:PRK12820 172 SRGFLEIETPILTKSTPEGARDYLVPSRIH----PKEFYALPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 261 TQVDMEMAFANSEDVMKIIEKTVSGVWSkfskkrglltldSKGTLVPAkkengtvSIFRMTYEQAMTSYGIDKPDLRApD 340
Cdd:PRK12820 248 TQLDIEASFIDEEFIFELIEELTARMFA------------IGGIALPR-------PFPRMPYAEAMDTTGSDRPDLRF-D 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 341 LKIINLGefNAFShlNKKFPVFEVIILRSAFSNMEEYKERWSFLTNNSNYNYRVPIVLPI----------ENDEQANSNW 410
Cdd:PRK12820 308 LKFADAT--DIFE--NTRYGIFKQILQRGGRIKGINIKGQSEKLSKNVLQNEYAKEIAPSfgakgmtwmrAEAGGLDSNI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 411 FENFHAiatfENPHLITKFLKLKKGDIVCgCTREPNHSIFEnpTPLGRLRqLVLQSEHG---KNIYHAVnkdvasWIVDF 487
Cdd:PRK12820 384 VQFFSA----DEKEALKRRFHAEDGDVII-MIADASCAIVL--SALGQLR-LHLADRLGlipEGVFHPL------WITDF 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 488 PLFSPViiedksgkkeklaypeyEKDRLCSTHHPFTMVKLKDYEKLEKTPEKCL-GRHYDLVVNGVELGGGSTRIHDPRL 566
Cdd:PRK12820 450 PLFEAT-----------------DDGGVTSSHHPFTAPDREDFDPGDIEELLDLrSRAYDLVVNGEELGGGSIRINDKDI 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 567 QDYIFEDI-LKIDNAYELFGHLLNAFDMGTPPHAGFAIGFDRMCAMICETESIRDVIAFPKSITGADLVVKSPSVIPESI 645
Cdd:PRK12820 513 QLRIFAALgLSEEDIEDKFGFFLRAFDFAAPPHGGIALGLDRVVSMILQTPSIREVIAFPKNRSAACPLTGAPSEVAQEQ 592
|
.
gi 6325153 646 L 646
Cdd:PRK12820 593 L 593
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
165-626 |
6.31e-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: 183.06 E-value: 6.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 165 LKKRSSISKEIRNSFNNFDFTEVETPMLFKATP-EGAREFLVPTRTKRSDgkpsfYALDQSPQQYKQLLMASGVNKYYQM 243
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGgAGARPFLVKYNALGLD-----YYLRISPQLFKKRLMVGGLDRVFEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 244 ARCFRDEDLRADRQPEFTQVDMEMAFANSEDVMKIIEKTVSGVWS----KFSKKRGLLTLDSKGTLVpakkengtvsifR 319
Cdd:cd00669 76 NRNFRNEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLARevlgVTAVTYGFELEDFGLPFP------------R 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 320 MTYEQAMTSYGidkpdlrapdlkiinlgefnafshlnkkfpvfeviilrsafsnmeeykerwsfltnnsnynyrvpivlp 399
Cdd:cd00669 144 LTYREALERYG--------------------------------------------------------------------- 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 400 iendeqansnwfenfhaiatfenphlitkflklkkgdivcgctrepnhsifeNPTplgrlrqlvlqsehgkniyhavnkd 479
Cdd:cd00669 155 ----------------------------------------------------QPL------------------------- 157
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 480 vasWIVDFPLFSpviiedksgkkeklaypeyekdrlcstHHPFTMvklkdyeKLEKTPEKClgRHYDLVVNGVELGGGST 559
Cdd:cd00669 158 ---FLTDYPAEM---------------------------HSPLAS-------PHDVNPEIA--DAFDLFINGVEVGNGSS 198
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6325153 560 RIHDPRLQDYIFED-ILKIDNAYELFGHLLNAFDMGTPPHAGFAIGFDRMCAMICETESIRDVIAFPK 626
Cdd:cd00669 199 RLHDPDIQAEVFQEqGINKEAGMEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPK 266
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
34-625 |
1.30e-46 |
|
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: 170.62 E-value: 1.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 34 DTSTIKQLKGLSSGQKIVLNGWIEQKpkRVGKNLIFGLLRDSNGdIIQLV------DNKSLLKGFTLEDVVQAVGIL--S 105
Cdd:COG0017 1 KRTYIKDLLPEHVGQEVTVAGWVRTK--RDSGGISFLILRDGSG-FIQVVvkkdklENFEEAKKLTTESSVEVTGTVveS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 106 LKRKLSnedadeYEVQLEDITVLNASN------KKPAQMqDFKLsaiyppEFRYLQLRNPKYQDFLKKRSSISKEIRNSF 179
Cdd:COG0017 78 PRAPQG------VELQAEEIEVLGEADepyplqPKRHSL-EFLL------DNRHLRLRTNRFGAIFRIRSELARAIREFF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 180 NNFDFTEVETPMLFKATPEGARE-FLVptrtkrsD--GKPSFyaLDQSPQQYKQLLMASgVNKYYQMARCFRDEDLRADR 256
Cdd:COG0017 145 QERGFVEVHTPIITASATEGGGElFPV-------DyfGKEAY--LTQSGQLYKEALAMA-LEKVYTFGPTFRAEKSNTRR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 257 Q-PEFTQVDMEMAFANSEDVMKIIEKTVSGVWSKFSKKRG--LLTLDSKGTLVPAKKENgtvSIFRMTYEQAmtsygidk 333
Cdd:COG0017 215 HlAEFWMIEPEMAFADLEDVMDLAEEMLKYIIKYVLENCPeeLEFLGRDVERLEKVPES---PFPRITYTEA-------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 334 pdlrapdLKIinlgefnafshLNKKfpvfeviilrsafsnmeEYKERWsfltnnsnynyrvpivlpiENDeqansnwfen 413
Cdd:COG0017 284 -------IEI-----------LKKS-----------------GEKVEW-------------------GDD---------- 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 414 fhaiatfenphlitkflklkkgdivcgctrepnhsifenptplgrlrqlvLQSEHGKNIYHAVNKDvaswivdfplfsPV 493
Cdd:COG0017 300 --------------------------------------------------LGTEHERYLGEEFFKK------------PV 317
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 494 IIEDksgkkeklaYPEYEKdrlcsthhPF-TMVKLKDyeklektPEKCLGrhYDLVVNGV-ELGGGSTRIHDP-RLQDYI 570
Cdd:COG0017 318 FVTD---------YPKEIK--------AFyMKPNPDD-------PKTVAA--FDLLAPGIgEIIGGSQREHRYdVLVERI 371
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 6325153 571 FEDILKIDNayelFGHLLNAFDMGTPPHAGFAIGFDRMCAMICETESIRDVIAFP 625
Cdd:COG0017 372 KEKGLDPED----YEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFP 422
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
38-625 |
4.86e-42 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 158.04 E-value: 4.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 38 IKQLKGLSSGQKIVLNGWIEQKpkRVGKNLIFGLLRDSNGdIIQLV-------DNKSLLKGFTLEDVVQAVGILSlkrkl 110
Cdd:PRK05159 7 TSELTPELDGEEVTLAGWVHEI--RDLGGIAFLILRDRSG-IIQVVvkkkvdeELFETIKKLKRESVVSVTGTVK----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 111 SNEDADE-YEVQLEDITVLNA---------SNKKPAQMqDFKLsaiyppEFRYLQLRNPKYQDFLKKRSSISKEIRNSFN 180
Cdd:PRK05159 79 ANPKAPGgVEVIPEEIEVLNKaeeplpldiSGKVLAEL-DTRL------DNRFLDLRRPRVRAIFKIRSEVLRAFREFLY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 181 NFDFTEVETPMLFKATPEGARE------FlvptrtkrsdGKPSFyaLDQSPQQYKQLLMASGVNKYYQMARCFRDEDLRA 254
Cdd:PRK05159 152 ENGFTEIFTPKIVASGTEGGAElfpidyF----------EKEAY--LAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 255 DRQ-PEFTQVDMEMAFANS-EDVMKIIEKTVSGVWSKFSKKRG--LLTLDSKGTLVPAKkengtvsIFRMTYEQAmtsyg 330
Cdd:PRK05159 220 SRHlNEYTSIDVEMGFIDDhEDVMDLLENLLRYMYEDVAENCEkeLELLGIELPVPETP-------IPRITYDEA----- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 331 idkpdlrapdLKIINlgefnafshlnkkfpvfeviilrsafsnmEEYKERwsfltnnsnynyrvpivlpiendeqansNW 410
Cdd:PRK05159 288 ----------IEILK-----------------------------SKGNEI----------------------------SW 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 411 FENFHAiatfENPHLITKFLKlkkgdivcgctrepnhsifenptplgrlrqlvlqSEHGKNIYhavnkdvasWIVDFPlf 490
Cdd:PRK05159 301 GDDLDT----EGERLLGEYVK----------------------------------EEYGSDFY---------FITDYP-- 331
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 491 spviiedkSGKKeklaypeyekdrlcsthhPF-TMvklkdyeKLEKTPEKCLGrhYDLVVNGVELGGGSTRIHDPrlqDY 569
Cdd:PRK05159 332 --------SEKR------------------PFyTM-------PDEDDPEISKS--FDLLFRGLEITSGGQRIHRY---DM 373
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 6325153 570 IFEDILKIDNAYELFGHLLNAFDMGTPPHAGFAIGFDRMCAMICETESIRDVIAFP 625
Cdd:PRK05159 374 LVESIKEKGLNPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
49-130 |
1.15e-29 |
|
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae mitochondrial (mt) 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 fungal 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. Mutations in the gene for S. cerevisiae mtAspRS result in a "petite" phenotype typical for a mutation in a nuclear gene that results in a non-functioning mitochondrial protein synthesis system.
Pssm-ID: 239816 [Multi-domain] Cd Length: 86 Bit Score: 112.41 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 49 KIVLNGWIEQKPKRVgKNLIFGLLRDSNGDIIQLVDNK-----SLLKGFTLEDVVQAVGILSLKRKLSNEDADEYEVQLE 123
Cdd:cd04321 1 KVTLNGWIDRKPRIV-KKLSFADLRDPNGDIIQLVSTAkkdafSLLKSITAESPVQVRGKLQLKEAKSSEKNDEWELVVD 79
|
....*..
gi 6325153 124 DITVLNA 130
Cdd:cd04321 80 DIQTLNA 86
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
47-326 |
2.64e-29 |
|
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: 121.08 E-value: 2.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 47 GQKIVLNGWIEQKpKRVGKnLIFGLLRDSNGdIIQLVDNK--------SLLKGFTLEDVVQAVGILSLKRKLSNEdadeY 118
Cdd:TIGR00458 12 GQEVTFMGWVHEI-RDLGG-LIFVLLRDREG-LIQITAPAkkvsknlfKWAKKLNLESVVAVRGIVKIKEKAPGG----F 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 119 EVQLEDITVLNAS---------NKKPAQMqDFKLsaiyppEFRYLQLRNPKYQDFLKKRSSISKEIRNSFNNFDFTEVET 189
Cdd:TIGR00458 85 EIIPTKIEVINEAkeplpldptEKVPAEL-DTRL------DYRFLDLRRPTVQAIFRIRSGVLESVREFLAEEGFIEVHT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 190 PMLFKATPEGAREFLVPTRTKRSdgkpSFyaLDQSPQQYKQLLMASGVNKYYQMARCFRDEDLRADRQ-PEFTQVDMEMA 268
Cdd:TIGR00458 158 PKLVASATEGGTELFPITYFERE----AF--LGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHRHlNEATSIDIEMA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 269 FANSEDVMKIIEKTVSGVWSKFSKK--RGLLTLDSKGTLVPAKKEngtvsifRMTYEQAM 326
Cdd:TIGR00458 232 FEDHHDVMDILEELVVRVFEDVPERcaHQLETLEFKLEKPEGKFV-------RLTYDEAI 284
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
152-626 |
4.78e-28 |
|
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: 114.97 E-value: 4.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 152 RYLQLRNPKYQDFLKKRSSISKEIRNSFNNFDFTEVETPMLFKATPEGAREFLvptrTKRSDGKPSFyaLDQSPQQYKQL 231
Cdd:cd00776 11 RHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELF----KVSYFGKPAY--LAQSPQLYKEM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 232 LMASgVNKYYQMARCFRDEDLRADRQ-PEFTQVDMEMAFANS-EDVMKIIEKTVsgvwskfskkrglltldskgtlvpak 309
Cdd:cd00776 85 LIAA-LERVYEIGPVFRAEKSNTRRHlSEFWMLEAEMAFIEDyNEVMDLIEELI-------------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 310 kengtVSIFRMTYEQamtsygidkpdlRAPDLKIINLGEFNAFShLNKKFPVFeviilrsafsnmeEYKErwsfltnnsn 389
Cdd:cd00776 138 -----KYIFKRVLER------------CAKELELVNQLNRELLK-PLEPFPRI-------------TYDE---------- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 390 ynyrvpivlpiendeqansnwfenfhAIatfenphlitKFLKLKKGdivcgctrEPNHSIFENptplgrlrqlvLQSEHG 469
Cdd:cd00776 177 --------------------------AI----------ELLREKGV--------EEEVKWGED-----------LSTEHE 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 470 KNIYHAVNKDvaswivdfplfsPVIIEDksgkkeklaYPEYEKdrlcsthhPFTMvKLKDyekleKTPEKCLGrhYDLVV 549
Cdd:cd00776 202 RLLGEIVKGD------------PVFVTD---------YPKEIK--------PFYM-KPDD-----DNPETVES--FDLLM 244
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6325153 550 NGV-ELGGGSTRIHDP-RLQDYIFEDILKIdnayELFGHLLNAFDMGTPPHAGFAIGFDRMCAMICETESIRDVIAFPK 626
Cdd:cd00776 245 PGVgEIVGGSQRIHDYdELEERIKEHGLDP----ESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFPR 319
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
33-625 |
2.08e-22 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 100.57 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 33 KDTSTIKQ-LKGLSSGQKIVLNGWIeqKPKRVGKNLIFGLLRDSNGdIIQLV-------DNKSLLKGFTLEDVVQAVGIL 104
Cdd:PRK03932 1 MMRVSIKDiLKGKYVGQEVTVRGWV--RTKRDSGKIAFLQLRDGSC-FKQLQvvkdngeEYFEEIKKLTTGSSVIVTGTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 105 slkrKLSNEDADEYEVQLEDITVLNASNKKpaqmqdfklsaiYP-------PEF----RYLQLRNPKYQDFLKKRSSISK 173
Cdd:PRK03932 78 ----VESPRAGQGYELQATKIEVIGEDPED------------YPiqkkrhsIEFlreiAHLRPRTNKFGAVMRIRNTLAQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 174 EIRNSFNNFDFTEVETPMLFKATPEGARE-FLVPTRTKRSD----GKPSFyaLDQSPQQYKQlLMASGVNKYYQMARCFR 248
Cdd:PRK03932 142 AIHEFFNENGFVWVDTPIITASDCEGAGElFRVTTLDLDFSkdffGKEAY--LTVSGQLYAE-AYAMALGKVYTFGPTFR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 249 DEDLRADRQ-PEFTQVDMEMAFANSEDVMKIIEKTVSgvwskfskkrglltldskgtlvpakkengtvsifrmtyeqAMT 327
Cdd:PRK03932 219 AENSNTRRHlAEFWMIEPEMAFADLEDNMDLAEEMLK----------------------------------------YVV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 328 SYGIDKpdlRAPDLKIIN-LGEFNAFSHLNKkfpvfeviILRSAFSNMeEYKErwsfltnnsnynyrvpivlpiendeqa 406
Cdd:PRK03932 259 KYVLEN---CPDDLEFLNrRVDKGDIERLEN--------FIESPFPRI-TYTE--------------------------- 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 407 nsnwfenfhAIatfenphlitKFLKLKKGDivcgctrepnhsiFENPTPLGrlrqLVLQSEHGKNIYHAVNKdvaswivd 486
Cdd:PRK03932 300 ---------AI----------EILQKSGKK-------------FEFPVEWG----DDLGSEHERYLAEEHFK-------- 335
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 487 fplfSPVIIEDksgkkeklaYPEYEKdrlcsthhPFTMvKLKDYEKLEktpekclgRHYDLVVNGV-ELGGGSTRIHDPr 565
Cdd:PRK03932 336 ----KPVFVTN---------YPKDIK--------AFYM-RLNPDGKTV--------AAMDLLAPGIgEIIGGSQREERL- 384
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6325153 566 lqdyifeDILkiDNAYELFGhlLNAFDM---------GTPPHAGFAIGFDRMCAMICETESIRDVIAFP 625
Cdd:PRK03932 385 -------DVL--EARIKELG--LNKEDYwwyldlrryGSVPHSGFGLGFERLVAYITGLDNIRDVIPFP 442
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
158-625 |
6.13e-20 |
|
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: 91.49 E-value: 6.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 158 NPKYQDFLKKRSSISKEIRNSFNNFDFTEVETPMLfKATPEG--AREFLvptrTKRSDGKPSFYaLDQSPQQYKQLLMAS 235
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPML-QPIAGGaaARPFI----THHNALDMDLY-LRIAPELYLKRLIVG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 236 GVNKYYQMARCFRDEDLRADRQPEFTQVDMEMAFANSEDVMKIIEKTVSGVwskfskkrglltldskgtlvpAKKENGTV 315
Cdd:cd00775 75 GFERVYEIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGL---------------------VKKINGKT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 316 SIfrmtyeqamtsygidkpdlrapdlkiinlgEFNAFsHLNKKFPvFEVIILRSAfsnMEEYkerwsfltnnsnynyrVP 395
Cdd:cd00775 134 KI------------------------------EYGGK-ELDFTPP-FKRVTMVDA---LKEK----------------TG 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 396 IVLPIENDEQA-NSNWFENFHAIATFENPHLITKFLKLKKGDIVcgctrEPNHSifeNPTplgrlrqlvlqsehgkniyh 474
Cdd:cd00775 163 IDFPELDLEQPeELAKLLAKLIKEKIEKPRTLGKLLDKLFEEFV-----EPTLI---QPT-------------------- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 475 avnkdvasWIVDFPL-FSPviiedksgkkekLAYPEYEKDRLCsthhpftmvklkdyEKLEktpekclgrhydLVVNGVE 553
Cdd:cd00775 215 --------FIIDHPVeISP------------LAKRHRSNPGLT--------------ERFE------------LFICGKE 248
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6325153 554 LGGGSTRIHDPRLQDYIFEDILKI-----DNAYELFGHLLNAFDMGTPPHAGFAIGFDRMCAMICETESIRDVIAFP 625
Cdd:cd00775 249 IANAYTELNDPFDQRERFEEQAKQkeagdDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRDVILFP 325
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
152-285 |
1.20e-16 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 83.50 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 152 RYLQL-RNPKYQDFLKKRSSISKEIRNSFNNFDFTEVETPMLfKATPEGA--REFlvptRTKRSDGKPSFYaLDQSPQQY 228
Cdd:PLN02502 215 RYLDLiANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPML-NMIAGGAaaRPF----VTHHNDLNMDLY-LRIATELH 288
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 6325153 229 KQLLMASGVNKYYQMARCFRDEDLRADRQPEFTQVDMEMAFANSEDVMKIIEKTVSG 285
Cdd:PLN02502 289 LKRLVVGGFERVYEIGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSG 345
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
149-286 |
4.96e-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: 78.15 E-value: 4.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 149 PEFRYLQlR------NPKYQDFLKKRSSISKEIRNSFNNFDFTEVETPMLfKATPEGA--REFlvptRTKrsdgkpsFYA 220
Cdd:COG1190 153 PETRYRQ-RyvdlivNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPML-QPIAGGAaaRPF----ITH-------HNA 219
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6325153 221 LDQ------SPQQY-KQLLMAsGVNKYYQMARCFRDEDLRADRQPEFTQvdME--MAFANSEDVMKIIEKTVSGV 286
Cdd:COG1190 220 LDMdlylriAPELYlKRLIVG-GFERVFEIGRNFRNEGIDTTHNPEFTM--LElyQAYADYNDMMDLTEELIREA 291
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
61-625 |
5.53e-14 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 75.45 E-value: 5.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 61 KRVGKnLIFGLLRdSNGDIIQLV----------DNKSLLKGFTLEDVVQAVGI-LSLKRKLSNEDADEYEVQLEDI---T 126
Cdd:PTZ00385 120 RDIGK-IIFVTIR-SNGNELQVVgqvgehftreDLKKLKVSLRVGDIIGADGVpCRMQRGELSVAASRMLILSPYVctdQ 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 127 VLNASNKKPAQMQDFKLsaiyppEFRYL---QLRNPKYQDFLKKRSSISKEIRNSFNNFDFTEVETPMLFK-ATPEGARE 202
Cdd:PTZ00385 198 VVCPNLRGFTVLQDNDV------KYRYRftdMMTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPVLHTvASGANAKS 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 203 FLVPTRTKRSDgkpsfYALDQSPQQYKQLLMASGVNKYYQMARCFRDEDLRADRQPEFTQVDMEMAFANSEDVMKIIEKT 282
Cdd:PTZ00385 272 FVTHHNANAMD-----LFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDLMPMTEDI 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 283 vsgvwskFSKkrglLTLDSKGTLV----PAKKENGTVSI-----FRM--TYEQAMTSYGIDKPdlrAPDlkiinlgEFNA 351
Cdd:PTZ00385 347 -------FRQ----LAMRVNGTTVvqiyPENAHGNPVTVdlgkpFRRvsVYDEIQRMSGVEFP---PPN-------ELNT 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 352 fshlNKKFPVFEVIILRsafsnmeeykerwsfltnnsnYNYRVPIVlpiendeQANSNWFENFhaIATFENPHLItkflk 431
Cdd:PTZ00385 406 ----PKGIAYMSVVMLR---------------------YNIPLPPV-------RTAAKMFEKL--IDFFITDRVV----- 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 432 lkkgdivcgctrEPnhsifenptplgrlrqlvlqsehgkniyhavnkdvaSWIVDFPLF-SPViiedksgKKEKLAYPEy 510
Cdd:PTZ00385 447 ------------EP------------------------------------TFVMDHPLFmSPL-------AKEQVSRPG- 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 511 ekdrlcsthhpftmvklkdyeklektpekcLGRHYDLVVNGVELGGGSTRIHDPRLQDYIFEDILkID------NAYELF 584
Cdd:PTZ00385 471 ------------------------------LAERFELFVNGIEYCNAYSELNDPHEQYHRFQQQL-VDrqggdeEAMPLD 519
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 6325153 585 GHLLNAFDMGTPPHAGFAIGFDRMCAMICETESIRDVIAFP 625
Cdd:PTZ00385 520 ETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFP 560
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
49-129 |
2.70e-13 |
|
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: 65.66 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 49 KIVLNGWIEQKpkRVGKNLIFGLLRDSNGdIIQLVDNKSLL-------KGFTLEDVVQAVGILSlKRKLSNEDADEYEVQ 121
Cdd:cd04100 1 EVTLAGWVHSR--RDHGGLIFIDLRDGSG-IVQVVVNKEELgeffeeaEKLRTESVVGVTGTVV-KRPEGNLATGEIELQ 76
|
....*...
gi 6325153 122 LEDITVLN 129
Cdd:cd04100 77 AEELEVLS 84
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
61-286 |
3.36e-13 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 72.43 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 61 KRVGKNLIFGLLRDSNGDIiQL--------VDNKSLLKGFTLEDVVQAVGILSLKRKlsnedaDEYEVQLEDITVLNASn 132
Cdd:PRK00484 66 KRVMGKASFATLQDGSGRI-QLyvskddvgEEALEAFKKLDLGDIIGVEGTLFKTKT------GELSVKATELTLLTKS- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 133 KKPaqMQDfKLSAIYPPEFRYLQlR------NPKYQDFLKKRSSISKEIRNSFNNFDFTEVETPMLfKATPEGAreflvp 206
Cdd:PRK00484 138 LRP--LPD-KFHGLTDVETRYRQ-RyvdlivNPESRETFRKRSKIISAIRRFLDNRGFLEVETPML-QPIAGGA------ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 207 trtkrsDGKPsFY----ALDQ------SPQQY-KQLLMAsGVNKYYQMARCFRDEDLraDRQ--PEFTQVDMEMAFANSE 273
Cdd:PRK00484 207 ------AARP-FIthhnALDIdlylriAPELYlKRLIVG-GFERVYEIGRNFRNEGI--DTRhnPEFTMLEFYQAYADYN 276
|
250
....*....|...
gi 6325153 274 DVMKIIEKTVSGV 286
Cdd:PRK00484 277 DMMDLTEELIRHL 289
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
168-292 |
7.12e-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: 7.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 168 RSSISKEIRNSFNNFDFTEVETPMLFKATP-EGAREFLVPTRTKRsDGKPSFYALDQSPQQYKQLLMASGV----NKYYQ 242
Cdd:cd00768 2 RSKIEQKLRRFMAELGFQEVETPIVEREPLlEKAGHEPKDLLPVG-AENEEDLYLRPTLEPGLVRLFVSHIrklpLRLAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 6325153 243 MARCFRDEDLRAD--RQPEFTQVDMEMAFANSEDvMKIIEKTVSGVWSKFSK 292
Cdd:cd00768 81 IGPAFRNEGGRRGlrRVREFTQLEGEVFGEDGEE-ASEFEELIELTEELLRA 131
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
38-281 |
2.27e-12 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 69.74 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 38 IKQLKGLSSGQKIVLNGWIeQKPKRVGKnLIFGLLRDSNGDIIQLV--DNKSL-------LKGFTLEDVVQAVGILSLKR 108
Cdd:PLN02850 72 VSDLGEELAGSEVLIRGRV-HTIRGKGK-SAFLVLRQSGFTVQCVVfvSEVTVskgmvkyAKQLSRESVVDVEGVVSVPK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 109 KLSNEDADEYEVQLEDI-TVLNASNKKPAQMQD-------FKLSAIYPPEF-----------RYLQLRNPKYQDFLKKRS 169
Cdd:PLN02850 150 KPVKGTTQQVEIQVRKIyCVSKALATLPFNVEDaarseseIEKALQTGEQLvrvgqdtrlnnRVLDLRTPANQAIFRIQS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 170 SISKEIRNSFNNFDFTEVETPMLFKATPE-GAREFlvptrtkRSD--GKPSfyALDQSPQQYKQLLMASGVNKYYQMARC 246
Cdd:PLN02850 230 QVCNLFREFLLSKGFVEIHTPKLIAGASEgGSAVF-------RLDykGQPA--CLAQSPQLHKQMAICGDFRRVFEIGPV 300
|
250 260 270
....*....|....*....|....*....|....*..
gi 6325153 247 FRDEDLRADRQ-PEFTQVDMEMAFANSED-VMKIIEK 281
Cdd:PLN02850 301 FRAEDSFTHRHlCEFTGLDLEMEIKEHYSeVLDVVDE 337
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
47-160 |
2.50e-12 |
|
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: 64.46 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 47 GQKIVLNGWIEQkpKRVGKNLIFGLLRDSNGdIIQLV------DNKSLLKGFTLEDVVQAVGILSlKRKLSNEDAD---- 116
Cdd:cd04317 14 GQEVTLCGWVQR--RRDHGGLIFIDLRDRYG-IVQVVfdpeeaPEFELAEKLRNESVIQVTGKVR-ARPEGTVNPKlptg 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 6325153 117 EYEVQLEDITVLNASNKKPAQMQDF-------KLsaiyppEFRYLQLRNPK 160
Cdd:cd04317 90 EIEVVASELEVLNKAKTLPFEIDDDvnvseelRL------KYRYLDLRRPK 134
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
148-327 |
2.22e-11 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 65.81 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 148 PPEFRYLQLRNPKYQDFLKKRSSISKEIRNSFNNFDFTEVETPMLFKATPEGARE-FLVPTRTKRSDGKPSFYALDQSPQ 226
Cdd:PRK06462 13 FLRMSWKHISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPSTDPLMGLgSDLPVKQISIDFYGVEYYLADSMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 227 QYKQLLMASgVNKYYQMARCFRDEDLRADRQP---EFTQVDMEMAFANSEDVMKIIEKTVSGVWSKFSKKRGlLTLDSKG 303
Cdd:PRK06462 93 LHKQLALRM-LGKIFYLSPNFRLEPVDKDTGRhlyEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHE-DELEFFG 170
|
170 180
....*....|....*....|....
gi 6325153 304 TLVPAKKENgtvsIFRMTYEQAMT 327
Cdd:PRK06462 171 RDLPHLKRP----FKRITHKEAVE 190
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
67-271 |
1.18e-09 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 61.52 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 67 LIFGLLRDSNGDIIQLVDNKSLLKGFT--------LEDVVQAVGILSLKRKlsnedaDEYEVQLEDITvLNASNKKPaqM 138
Cdd:PRK02983 669 VLFADLRDWSGELQVLLDASRLEQGSLadfraavdLGDLVEVTGTMGTSRN------GTLSLLVTSWR-LAGKCLRP--L 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 139 QDfKLSAIYPPE----FRYLQLR-NPKYQDFLKKRSSISKEIRNSFNNFDFTEVETPMLfkATPEG---AREFLVPTRTk 210
Cdd:PRK02983 740 PD-KWKGLTDPEarvrQRYLDLAvNPEARDLLRARSAVVRAVRETLVARGFLEVETPIL--QQVHGganARPFVTHINA- 815
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6325153 211 rsdgkpsfYALDQ----SPQQYKQLLMASGVNKYYQMARCFRDEDLRADRQPEFTQVDMEMAFAN 271
Cdd:PRK02983 816 --------YDMDLylriAPELYLKRLCVGGVERVFELGRNFRNEGVDATHNPEFTLLEAYQAHAD 872
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
152-625 |
1.58e-09 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 60.79 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 152 RYLQLR-NPKYQDFLKKRSSISKEIRNSFNNFDFTEVETPML-FKATPEGAREFLvptrTKRSDGKPSFYaLDQSPQQYK 229
Cdd:PTZ00417 239 RYLDLMiNESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMnLVAGGANARPFI----THHNDLDLDLY-LRIATELPL 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 230 QLLMASGVNKYYQMARCFRDEDLRADRQPEFTQVDMEMAFANSEDVMKiiektvsgvWSKfskkrglltlDSKGTLVpak 309
Cdd:PTZ00417 314 KMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIK---------WSE----------DFFSQLV--- 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 310 kengtVSIFRmTYEqamTSYGIDKPDlrapdlkiinlgefnafshlnkKFPVfEViilrsafsnmeeykerwsfltnnsN 389
Cdd:PTZ00417 372 -----MHLFG-TYK---ILYNKDGPE----------------------KDPI-EI------------------------D 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 390 YNYRVPIVLPIENDEQANSNWFENfhaiaTFENPHLITKFLKLKKGDIVcgctREPNhsifeNPTPLGRLRQLVlqSEHG 469
Cdd:PTZ00417 396 FTPPYPKVSIVEELEKLTNTKLEQ-----PFDSPETINKMINLIKENKI----EMPN-----PPTAAKLLDQLA--SHFI 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 470 KNIYHavnkdvaswivDFPLFspvIIEdksgkkeklaypeyekdrlcsthHPFTMVKLKDYEKlektPEKCLGRHYDLVV 549
Cdd:PTZ00417 460 ENKYP-----------NKPFF---IIE-----------------------HPQIMSPLAKYHR----SKPGLTERLEMFI 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 550 NGVELGGGSTRIHDPRLQDYIF----EDILKID-NAYELFGHLLNAFDMGTPPHAGFAIGFDRMCAMICETESIRDVIAF 624
Cdd:PTZ00417 499 CGKEVLNAYTELNDPFKQKECFsaqqKDREKGDaEAFQFDAAFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILF 578
|
.
gi 6325153 625 P 625
Cdd:PTZ00417 579 P 579
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
61-280 |
1.16e-08 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 58.15 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 61 KRVGKNLIFGLLRDSNGDIIQLVDNKSLLKG--------FTLEDVVQAVGilslkrKLSNEDADEYEVQLEDITVLNasn 132
Cdd:PRK12445 77 RRIMGKASFVTLQDVGGRIQLYVARDSLPEGvyndqfkkWDLGDIIGARG------TLFKTQTGELSIHCTELRLLT--- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 133 KKPAQMQDfKLSAIYPPEFRYLQ-----LRNPKYQDFLKKRSSISKEIRNSFNNFDFTEVETPMLfKATPEGA--REFLV 205
Cdd:PRK12445 148 KALRPLPD-KFHGLQDQEVRYRQryldlIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMM-QVIPGGAsaRPFIT 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6325153 206 PTRTKRSDgkpsfYALDQSPQQYKQLLMASGVNKYYQMARCFRDEDLRADRQPEFTQVDMEMAFANSEDVMKIIE 280
Cdd:PRK12445 226 HHNALDLD-----MYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTE 295
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
50-128 |
5.55e-08 |
|
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: 50.31 E-value: 5.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 50 IVLNGWIEQKpKRVGKNLIFGLLRDSNGdIIQLV----DNKSLLKGFTLEDVVQAVGilslkrKLSNEDADEYEVQLEDI 125
Cdd:pfam01336 1 VTVAGRVTSI-RRSGGKLLFLTLRDGTG-SIQVVvfkeEAEKLAKKLKEGDVVRVTG------KVKKRKGGELELVVEEI 72
|
...
gi 6325153 126 TVL 128
Cdd:pfam01336 73 ELL 75
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
152-267 |
8.53e-08 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 55.38 E-value: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 152 RYLQLRNPKYQDFLKKRSSISKEIRNSFNNFDFTEVETPMLFKATPEGAREFLVPTRTKRsdgkpsFYALDQSPQQYKQL 231
Cdd:PTZ00401 200 RWMDLRTPASGAIFRLQSRVCQYFRQFLIDSDFCEIHSPKIINAPSEGGANVFKLEYFNR------FAYLAQSPQLYKQM 273
|
90 100 110
....*....|....*....|....*....|....*..
gi 6325153 232 LMASGVNKYYQMARCFRDEDLRADRQ-PEFTQVDMEM 267
Cdd:PTZ00401 274 VLQGDVPRVFEVGPVFRSENSNTHRHlTEFVGLDVEM 310
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
164-261 |
1.61e-07 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 53.39 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 164 FLKKRSSISKEIRNSFNNFDFTEVETPMLFKATPEGAREFLVPTRTK---RSDGKPSFyaLDQSPQQYKQLLMASGVNKY 240
Cdd:PRK09350 4 NLLKRAKIIAEIRRFFADRGVLEVETPILSQATVTDIHLVPFETRFVgpgASQGKTLW--LMTSPEYHMKRLLAAGSGPI 81
|
90 100
....*....|....*....|.
gi 6325153 241 YQMARCFRDEDLRADRQPEFT 261
Cdd:PRK09350 82 FQICKSFRNEEAGRYHNPEFT 102
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
502-626 |
1.24e-06 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 51.53 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 502 KEKLAYPEYEKDRLCSTHHPFTMVKLKDYEKLEKTpekclgrhYDLVVNGVELGGGSTRIHDPRLQdYIFEDILKIDnaY 581
Cdd:PTZ00401 430 KERYGTDFFISDRFPSSARPFYTMECKDDERFTNS--------YDMFIRGEEISSGAQRIHDPDLL-LARAKMLNVD--L 498
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 6325153 582 ELFGHLLNAFDMGTPPHAGFAIGFDRMCAMICETESIRDVIAFPK 626
Cdd:PTZ00401 499 TPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPR 543
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
546-626 |
3.19e-06 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 50.36 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 546 DLVVNGV-ELGGGSTRihDPRLqDYIFEDILKIDNAYELFGHLLNAFDMGTPPHAGFAIGFDRMCAMICETESIRDVIAF 624
Cdd:PLN02603 480 DMLVPRVgELIGGSQR--EERL-EYLEARLDELKLNKESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPF 556
|
..
gi 6325153 625 PK 626
Cdd:PLN02603 557 PR 558
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
545-625 |
8.43e-06 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 49.19 E-value: 8.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 545 YDLVVNGVELGGGSTRIHDP-----RLQDyifEDILKID---NAYELFGHLLNAFDMGTPPHAGFAIGFDRMCAMICETe 616
Cdd:PRK02983 1004 WDLVAWGVELGTAYSELTDPveqrrRLTE---QSLLAAGgdpEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLTGR- 1079
|
....*....
gi 6325153 617 SIRDVIAFP 625
Cdd:PRK02983 1080 SIRETLPFP 1088
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
553-626 |
1.93e-05 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 47.71 E-value: 1.93e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6325153 553 ELGGGSTRIHD-PRLQDYIFEDILKIDnAYELFGHLLNafdMGTPPHAGFAIGFDRMCAMICETESIRDVIAFPK 626
Cdd:PTZ00425 509 EVIGGSQREDNlERLDKMIKEKKLNME-SYWWYRQLRK---FGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPR 579
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
165-272 |
1.95e-05 |
|
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA. This domain 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. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.
Pssm-ID: 238396 [Multi-domain] Cd Length: 261 Bit Score: 46.83 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 165 LKKRSSISKEIRNSFNNFDFTEVETPMLfkatpegarEFL-VPTRTKRSDGKPSFYAL-DQSPQQY-------------- 228
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVF---------EYTeLFLRKSGDEVSKEMYRFkDKGGRDLalrpdltapvarav 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 6325153 229 -KQLLMASGVNKYYQMARCFRDEDLRADRQPEFTQVDMEMAFANS 272
Cdd:cd00773 73 aENLLSLPLPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDS 117
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
546-633 |
2.31e-05 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 47.68 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 546 DLVVNGV-ELGGGSTRihDPRLqDYIFEDILKIDNAYELFGHLLNAFDMGTPPHAGFAIGFDRMCAMICETESIRDVIAF 624
Cdd:PLN02221 487 DVLVPKVgELIGGSQR--EERY-DVIKQRIEEMGLPIEPYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPF 563
|
....*....
gi 6325153 625 PKSITGADL 633
Cdd:PLN02221 564 PRYPGKADL 572
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
49-128 |
6.64e-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: 39.14 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 49 KIVLNGWIEQKpkRVGKNLIFGLLRDSNGdIIQLVDNKSLLKGF------TLEDVVQAVGILSLKRKlSNEDADEYEVQL 122
Cdd:cd04323 1 RVKVFGWVHRL--RSQKKLMFLVLRDGTG-FLQCVLSKKLVTEFydakslTQESSVEVTGEVKEDPR-AKQAPGGYELQV 76
|
....*.
gi 6325153 123 EDITVL 128
Cdd:cd04323 77 DYLEII 82
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
550-621 |
1.10e-03 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 41.45 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325153 550 NGVELGGGSTRIHDPRLQDYIFE-DILK----------IDNayelfgHLLNAFDMGTPPHAGFAIGFDRMCAMICETESI 618
Cdd:PRK09350 230 KGIELANGFHELTDAREQRQRFEqDNRKraarglpqqpIDE------NLIAALEAGLPDCSGVALGVDRLIMLALGAESI 303
|
...
gi 6325153 619 RDV 621
Cdd:PRK09350 304 SEV 306
|
|
| |
