|
Name |
Accession |
Description |
Interval |
E-value |
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
1-577 |
0e+00 |
|
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439789 [Multi-domain] Cd Length: 574 Bit Score: 745.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 1 MNIQALLSEKVRQAMIAAGA-PADCEPQIRQSAKVQFGDYQANGMMAVAKKLGMAPRQLAEQVLTHLDLNGIASKVEIAG 79
Cdd:COG0018 1 MNIKEELAEAIAAALAALGAgLEEPDILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDADPLVEKVEIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 80 PGFINIFLDPAFLAEHVQQALAS-DRLGVATPEK-QTIVVDYSAPNVAKEMHVGHLRSTIIGDTAVRTLEFLGHKVIRAN 157
Cdd:COG0018 81 PGFINFFLSPAALAAVLKEILADgEDYGRSDAGKgKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYDVTREN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 158 HVGDWGTQFGMLIAWLEKQQQENA--GEMELADLEGFYRDAKKHYDEDEEFAERARNYVVKLQSGDEYFREMWRKLVDIT 235
Cdd:COG0018 161 YINDAGTQIGKLALSLERYGEEEIepESKPDGYLGDLYVKFHKEYEEDPELEDIARELLAKLEPGDEEALELWKKAVDWS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 236 MTQNQITYDRLNVTLtrDDVMGESLYNPM--LPGIVADLKAKGLAVESEGATVVFLDvfknKEGEPMGVIIQKKDGGYLY 313
Cdd:COG0018 241 LEEIKEDLKRLGVEF--DVWFSESSLYDSgaVEEVVEELKEKGLLYESDGALWVRLT----EFGDDKDRVLVKSDGTYTY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 314 TTTDIACAKYRYETLHADRVLYYIDSRQHQHLMQAWAIVRKAGYVPESvPLEHHMFGMMLGKDGKPFKTRAGGTVKLADL 393
Cdd:COG0018 315 FTTDIAYHLYKFERYGFDRVIYVVGADQHGHFKRLFAALKALGYDPAK-DLEHLLFGMVNLRDGEKMSTRAGTVVTLDDL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 394 LDEALERARRLVAEKNPDmpadELEKLANAVGIGAVKYADLSKNRTTDYIFDWDNMLAFEGNTAPYMQYAYTRVLSVFRK 473
Cdd:COG0018 394 LDEAVERAREIIEEKSEE----EKEEIAEQVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNTNPYVQYAHARICSILRK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 474 AEINEEQLAAA-PVIIREDREAQLAARLLQFEETLTVVAREGTPHVMCAYLYDLAGLFSGFYEHCPILSAENEEVRNSRL 552
Cdd:COG0018 470 AGEELDGLAEAdLSLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRILKAEDEELRAARL 549
|
570 580
....*....|....*....|....*
gi 24113254 553 KLAQLTAKTLKLGLDTLGIETVERM 577
Cdd:COG0018 550 ALVAATAQVLKNGLGLLGISAPERM 574
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
3-577 |
0e+00 |
|
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed genome to date. An interesting feature of the alignment of all arginyl-tRNA synthetases is a fairly deep split between two families. One family includes archaeal, eukaryotic and organellar, spirochete, E. coli, and Synechocystis sp. The second, sharing a deletion of about 25 residues in the central region relative to the first, includes Bacillus subtilis, Aquifex aeolicus, the Mycoplasmas and Mycobacteria, and the Gram-negative bacterium Helicobacter pylori. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273085 [Multi-domain] Cd Length: 563 Bit Score: 731.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 3 IQALLSEKVRQAMIAAGAPADCEPQIRQSAKVQFGDYQANGMMAVAKKLGMAPRQLAEQVLTHLDLNGIASKVEIAGPgF 82
Cdd:TIGR00456 1 IKTLLKEEISQALLKAGLSKESEILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKLKTGEIIEKVEAAGP-F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 83 INIFLDPAFLAEHVQQALASDR--LGVATPEKQTIVVDYSAPNVAKEMHVGHLRSTIIGDTAVRTLEFLGHKVIRANHVG 160
Cdd:TIGR00456 80 INFFLSPQKLLERLIQKILTQKekYGSKKLKNKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 161 DWGTQFGMLIAWLEKQQQE---NAGEMELADLEGFYRDAKKHYDEDEEFAERARNYVVKLQSGDEYFREMWRKLVDITMT 237
Cdd:TIGR00456 160 DWGRQFGLLALGVEKFGNEalnIAVKKPDHGLEGFYVEINKRLEENEELEEEARELFVKLESGDEETIKLWKRLVEYSLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 238 QNQITYDRLNVTLTRDDVMGESLYNPMLPGIVADLKAKGLAVEsEGATVVFLDVFKNKegepMGVIIQKKDGGYLYTTTD 317
Cdd:TIGR00456 240 GIKETYDRLNIHFDSFVWEGESVKNGMLPKVLEDLKEKGLVVE-DGALWLDLTLFGDK----KDRVLQKSDGTYLYLTTD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 318 IACAKYRYETlHADRVLYYIDSRQHQHLMQAWAIVRKAGYvpESVPLEHHMFGMMLGKDgkpFKTRAGGTVKLADLLDEA 397
Cdd:TIGR00456 315 IAYHLDKLER-GFDKMIYVWGSDHHLHIAQMFAILEKLGY--KKKELEHLNFGMVPLYS---MKTRRGNVISLDNLLDEA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 398 LERARRLVAEKNpdmpADELEKLANAVGIGAVKYADLSKNRTTDYIFDWDNMLAFEGNTAPYMQYAYTRVLSVFRKAEIN 477
Cdd:TIGR00456 389 SKRAGNVITIKN----DLEEEKVADAVGIGAVRYFDLSKNRTTDYVFDWDAMLSFEGNTAPYIQYAHARICSILRKAEID 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 478 EEQLAAAPVIIREDREAQLAARLLQFEETLTVVAREGTPHVMCAYLYDLAGLFSGFYEHCPILSAENeEVRNSRLKLAQL 557
Cdd:TIGR00456 465 GEKLIADDFELLEEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACPVLDAEN-ELAAARLALLKA 543
|
570 580
....*....|....*....|
gi 24113254 558 TAKTLKLGLDTLGIETVERM 577
Cdd:TIGR00456 544 TRQTLKNGLDLLGIEPPERM 563
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
1-577 |
0e+00 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 646.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 1 MNIQALLSEKVRQAMIAAGAPADCEPQIRQSAKVQFGDYQANGMMAVAKKLGMAPRQLAEQVLTHLdlngiaSKVEIAGP 80
Cdd:PRK01611 3 MDIKELLAEALAAALEAGGLPELPAVLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIVEAI------EKVEIAGP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 81 GFINIFLDPAFLAEHVQQAL-ASDRLGVATPEK-QTIVVDYSAPNVAKEMHVGHLRSTIIGDTAVRTLEFLGHKVIRANH 158
Cdd:PRK01611 77 GFINFFLDPAALAELVLAILeAGERYGRSDIGKgKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDVTREYY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 159 VGDWGTQFGMLIAwlekqqqenagemeladlegfyrdakkhydedeefaerarnyvvklqsgdeYFREMWRKLVDITMTQ 238
Cdd:PRK01611 157 VNDAGTQIGMLIA---------------------------------------------------SLELLWRKAVDISLDE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 239 NQITYDRLNVTLTRDDVMGESLYNPMLPGIVADLKAKGLAV-ESEGATVVFLDVFknkeGEPMGVIIQKKDGGYLYTTTD 317
Cdd:PRK01611 186 IKEDLDRLGVHFDVWFSESELYYNGKVDEVVEDLKEKGLLYvESDGALWVRLTEF----GDDKDRVLIKSDGTYTYFTRD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 318 IACAKYRYETLhaDRVLYYIDSRQHQHLMQAWAIVRKAGYVPESVP-LEHHMFGMMLGKDGKPFKTRAGGTVKLADLLDE 396
Cdd:PRK01611 262 IAYHLYKFERF--DRVIYVVGADHHGHFKRLKAALKALGYDPDALEvLLHQMVGLVRGGEGVKMSTRAGNVVTLDDLLDE 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 397 ALERARRLVAEKnpdmpadeleKLANAVGIGAVKYADLSKNRTTDYIFDWDNMLAFEGNTAPYMQYAYTRVLSVFRKAEi 476
Cdd:PRK01611 340 AVGRARELIEEK----------EIAEAVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPPYVQYAHARICSILRKAA- 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 477 nEEQLAAAPVIIREDREAQLAARLLQFEETLTVVAREGTPHVMCAYLYDLAGLFSGFYEHCPiLSAENEEVRNSRLKLAQ 556
Cdd:PRK01611 409 -EAGIDLLLALLTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYNRVL-LKDEEEELRNARLALVK 486
|
570 580
....*....|....*....|.
gi 24113254 557 LTAKTLKLGLDTLGIETVERM 577
Cdd:PRK01611 487 ATAQVLKNGLDLLGISAPERM 507
|
|
| tRNA-synt_1d |
pfam00750 |
tRNA synthetases class I (R); Other tRNA synthetase sub-families are too dissimilar to be ... |
95-446 |
0e+00 |
|
tRNA synthetases class I (R); Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only arginyl tRNA synthetase.
Pssm-ID: 395607 [Multi-domain] Cd Length: 348 Bit Score: 620.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 95 HVQQALASDRLGVATPEKQTIVVDYSAPNVAKEMHVGHLRSTIIGDTAVRTLEFLGHKVIRANHVGDWGTQFGMLIAWLE 174
Cdd:pfam00750 1 TVPNALLQKGLGKASREKKKVVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQFGMLIAGLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 175 KQQQEN-AGEMELADLEGFYRDAKKHYDEDEEFAERARNYVVKLQSGDEYFREMWRKLVDITMTQNQITYDRLNVTLTRd 253
Cdd:pfam00750 81 KYQDEKtLQEMPIQDLEDFYREAKKHYDEEEEFAERARNYVVKLQSGDEYWRRMWKLIVDITMTQNQRLYDRLDVTLTE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 254 dvMGESLYNPMLPGIVADLKAKGLAVESEGATVVFLDVFknkeGEPMGVIIQKKDGGYLYTTTDIACAKYRYETLHADRV 333
Cdd:pfam00750 160 --MGESLYNPMMNEIVKDFKKNGLVVEIDGALVVFLDEF----GKPMGVIVQKSDGGYLYTTTDIAAAKYRYETLHADRM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 334 LYYIDSRQHQHLMQAWAIVRKAGYVPESVPLEHHMFGMMLGKDGKPFKTRAGGTVKLADLLDEALERARRLVAEKNPD-- 411
Cdd:pfam00750 234 LYVIDSRQSQHMQQAFAILRKAGYVPESKDLEHINFGMVLGKDGKPFKTRKGGTVKLADLLDEALERALQLIMEKNKDki 313
|
330 340 350
....*....|....*....|....*....|....*
gi 24113254 412 MPADELEKLANAVGIGAVKYADLSKNRTTDYIFDW 446
Cdd:pfam00750 314 LQADELEAVADAVGIGAIKYADLSKNRTNDYIFDW 348
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
114-385 |
2.31e-80 |
|
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. There are at least three subgroups of ArgRS. One type contains both characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The second subtype lacks the KMSKS motif; however, it has a lysine N-terminal to the HIGH motif, which serves as the functional counterpart to the second lysine of the KMSKS motif. A third group, which is found primarily in archaea and a few bacteria, lacks both the KMSKS motif and the HIGH loop lysine.
Pssm-ID: 185675 [Multi-domain] Cd Length: 212 Bit Score: 251.33 E-value: 2.31e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 114 TIVVDYSAPNVAKEMHVGHLRSTIIGDTAVRTLEFLGHKVIRANHVGDWGTQFGMLIAWLEKqqqenagemeladlegfy 193
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSLEK------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 194 rdakkhydedeefaerarnyvvklqsgdeyfremWRKLVDITMTQNQITYDRLNVTltRDDVMGESLYNPMLPGIVADLK 273
Cdd:cd00671 63 ----------------------------------WRKLVEESIKADLETYGRLDVR--FDVWFGESSYLGLMGKVVELLE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 274 AKGLAVESEGATVVFLDVFknkeGEPMGVIIQKKDGGYLYTTTDIACAKYRYEtLHADRVLYYIDSRQHQHLMQAWAIVR 353
Cdd:cd00671 107 ELGLLYEEDGALWLDLTEF----GDDKDRVLVRSDGTYTYFTRDIAYHLDKFE-RGADKIIYVVGADHHGHFKRLFAALE 181
|
250 260 270
....*....|....*....|....*....|..
gi 24113254 354 KAGYvPESVPLEHHMFGMMLGKDGKPFKTRAG 385
Cdd:cd00671 182 LLGY-DEAKKLEHLLYGMVNLPKEGKMSTRAG 212
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
461-577 |
1.49e-34 |
|
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain of Arginyl tRNA synthetase. This domain is known as the DALR domain after characteristic conserved amino acids.
Pssm-ID: 214846 [Multi-domain] Cd Length: 122 Bit Score: 126.54 E-value: 1.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 461 QYAYTRVLSVFRKAEINEEQLAAAPVI----IREDREAQLAARLLQFEETLTVVAREGTPHVMCAYLYDLAGLFSGFYEH 536
Cdd:smart00836 2 QYAHARICSILRKAGEAGETLPDIADAdlslLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYNR 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 24113254 537 CPILSAENEEVRNSRLKLAQLTAKTLKLGLDTLGIETVERM 577
Cdd:smart00836 82 VRVLGEENPELRKARLALLKAVRQVLANGLRLLGISAPERM 122
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
1-577 |
0e+00 |
|
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439789 [Multi-domain] Cd Length: 574 Bit Score: 745.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 1 MNIQALLSEKVRQAMIAAGA-PADCEPQIRQSAKVQFGDYQANGMMAVAKKLGMAPRQLAEQVLTHLDLNGIASKVEIAG 79
Cdd:COG0018 1 MNIKEELAEAIAAALAALGAgLEEPDILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDADPLVEKVEIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 80 PGFINIFLDPAFLAEHVQQALAS-DRLGVATPEK-QTIVVDYSAPNVAKEMHVGHLRSTIIGDTAVRTLEFLGHKVIRAN 157
Cdd:COG0018 81 PGFINFFLSPAALAAVLKEILADgEDYGRSDAGKgKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYDVTREN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 158 HVGDWGTQFGMLIAWLEKQQQENA--GEMELADLEGFYRDAKKHYDEDEEFAERARNYVVKLQSGDEYFREMWRKLVDIT 235
Cdd:COG0018 161 YINDAGTQIGKLALSLERYGEEEIepESKPDGYLGDLYVKFHKEYEEDPELEDIARELLAKLEPGDEEALELWKKAVDWS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 236 MTQNQITYDRLNVTLtrDDVMGESLYNPM--LPGIVADLKAKGLAVESEGATVVFLDvfknKEGEPMGVIIQKKDGGYLY 313
Cdd:COG0018 241 LEEIKEDLKRLGVEF--DVWFSESSLYDSgaVEEVVEELKEKGLLYESDGALWVRLT----EFGDDKDRVLVKSDGTYTY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 314 TTTDIACAKYRYETLHADRVLYYIDSRQHQHLMQAWAIVRKAGYVPESvPLEHHMFGMMLGKDGKPFKTRAGGTVKLADL 393
Cdd:COG0018 315 FTTDIAYHLYKFERYGFDRVIYVVGADQHGHFKRLFAALKALGYDPAK-DLEHLLFGMVNLRDGEKMSTRAGTVVTLDDL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 394 LDEALERARRLVAEKNPDmpadELEKLANAVGIGAVKYADLSKNRTTDYIFDWDNMLAFEGNTAPYMQYAYTRVLSVFRK 473
Cdd:COG0018 394 LDEAVERAREIIEEKSEE----EKEEIAEQVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNTNPYVQYAHARICSILRK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 474 AEINEEQLAAA-PVIIREDREAQLAARLLQFEETLTVVAREGTPHVMCAYLYDLAGLFSGFYEHCPILSAENEEVRNSRL 552
Cdd:COG0018 470 AGEELDGLAEAdLSLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRILKAEDEELRAARL 549
|
570 580
....*....|....*....|....*
gi 24113254 553 KLAQLTAKTLKLGLDTLGIETVERM 577
Cdd:COG0018 550 ALVAATAQVLKNGLGLLGISAPERM 574
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
3-577 |
0e+00 |
|
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed genome to date. An interesting feature of the alignment of all arginyl-tRNA synthetases is a fairly deep split between two families. One family includes archaeal, eukaryotic and organellar, spirochete, E. coli, and Synechocystis sp. The second, sharing a deletion of about 25 residues in the central region relative to the first, includes Bacillus subtilis, Aquifex aeolicus, the Mycoplasmas and Mycobacteria, and the Gram-negative bacterium Helicobacter pylori. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273085 [Multi-domain] Cd Length: 563 Bit Score: 731.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 3 IQALLSEKVRQAMIAAGAPADCEPQIRQSAKVQFGDYQANGMMAVAKKLGMAPRQLAEQVLTHLDLNGIASKVEIAGPgF 82
Cdd:TIGR00456 1 IKTLLKEEISQALLKAGLSKESEILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKLKTGEIIEKVEAAGP-F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 83 INIFLDPAFLAEHVQQALASDR--LGVATPEKQTIVVDYSAPNVAKEMHVGHLRSTIIGDTAVRTLEFLGHKVIRANHVG 160
Cdd:TIGR00456 80 INFFLSPQKLLERLIQKILTQKekYGSKKLKNKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 161 DWGTQFGMLIAWLEKQQQE---NAGEMELADLEGFYRDAKKHYDEDEEFAERARNYVVKLQSGDEYFREMWRKLVDITMT 237
Cdd:TIGR00456 160 DWGRQFGLLALGVEKFGNEalnIAVKKPDHGLEGFYVEINKRLEENEELEEEARELFVKLESGDEETIKLWKRLVEYSLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 238 QNQITYDRLNVTLTRDDVMGESLYNPMLPGIVADLKAKGLAVEsEGATVVFLDVFKNKegepMGVIIQKKDGGYLYTTTD 317
Cdd:TIGR00456 240 GIKETYDRLNIHFDSFVWEGESVKNGMLPKVLEDLKEKGLVVE-DGALWLDLTLFGDK----KDRVLQKSDGTYLYLTTD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 318 IACAKYRYETlHADRVLYYIDSRQHQHLMQAWAIVRKAGYvpESVPLEHHMFGMMLGKDgkpFKTRAGGTVKLADLLDEA 397
Cdd:TIGR00456 315 IAYHLDKLER-GFDKMIYVWGSDHHLHIAQMFAILEKLGY--KKKELEHLNFGMVPLYS---MKTRRGNVISLDNLLDEA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 398 LERARRLVAEKNpdmpADELEKLANAVGIGAVKYADLSKNRTTDYIFDWDNMLAFEGNTAPYMQYAYTRVLSVFRKAEIN 477
Cdd:TIGR00456 389 SKRAGNVITIKN----DLEEEKVADAVGIGAVRYFDLSKNRTTDYVFDWDAMLSFEGNTAPYIQYAHARICSILRKAEID 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 478 EEQLAAAPVIIREDREAQLAARLLQFEETLTVVAREGTPHVMCAYLYDLAGLFSGFYEHCPILSAENeEVRNSRLKLAQL 557
Cdd:TIGR00456 465 GEKLIADDFELLEEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACPVLDAEN-ELAAARLALLKA 543
|
570 580
....*....|....*....|
gi 24113254 558 TAKTLKLGLDTLGIETVERM 577
Cdd:TIGR00456 544 TRQTLKNGLDLLGIEPPERM 563
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
1-577 |
0e+00 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 646.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 1 MNIQALLSEKVRQAMIAAGAPADCEPQIRQSAKVQFGDYQANGMMAVAKKLGMAPRQLAEQVLTHLdlngiaSKVEIAGP 80
Cdd:PRK01611 3 MDIKELLAEALAAALEAGGLPELPAVLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIVEAI------EKVEIAGP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 81 GFINIFLDPAFLAEHVQQAL-ASDRLGVATPEK-QTIVVDYSAPNVAKEMHVGHLRSTIIGDTAVRTLEFLGHKVIRANH 158
Cdd:PRK01611 77 GFINFFLDPAALAELVLAILeAGERYGRSDIGKgKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDVTREYY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 159 VGDWGTQFGMLIAwlekqqqenagemeladlegfyrdakkhydedeefaerarnyvvklqsgdeYFREMWRKLVDITMTQ 238
Cdd:PRK01611 157 VNDAGTQIGMLIA---------------------------------------------------SLELLWRKAVDISLDE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 239 NQITYDRLNVTLTRDDVMGESLYNPMLPGIVADLKAKGLAV-ESEGATVVFLDVFknkeGEPMGVIIQKKDGGYLYTTTD 317
Cdd:PRK01611 186 IKEDLDRLGVHFDVWFSESELYYNGKVDEVVEDLKEKGLLYvESDGALWVRLTEF----GDDKDRVLIKSDGTYTYFTRD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 318 IACAKYRYETLhaDRVLYYIDSRQHQHLMQAWAIVRKAGYVPESVP-LEHHMFGMMLGKDGKPFKTRAGGTVKLADLLDE 396
Cdd:PRK01611 262 IAYHLYKFERF--DRVIYVVGADHHGHFKRLKAALKALGYDPDALEvLLHQMVGLVRGGEGVKMSTRAGNVVTLDDLLDE 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 397 ALERARRLVAEKnpdmpadeleKLANAVGIGAVKYADLSKNRTTDYIFDWDNMLAFEGNTAPYMQYAYTRVLSVFRKAEi 476
Cdd:PRK01611 340 AVGRARELIEEK----------EIAEAVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPPYVQYAHARICSILRKAA- 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 477 nEEQLAAAPVIIREDREAQLAARLLQFEETLTVVAREGTPHVMCAYLYDLAGLFSGFYEHCPiLSAENEEVRNSRLKLAQ 556
Cdd:PRK01611 409 -EAGIDLLLALLTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYNRVL-LKDEEEELRNARLALVK 486
|
570 580
....*....|....*....|.
gi 24113254 557 LTAKTLKLGLDTLGIETVERM 577
Cdd:PRK01611 487 ATAQVLKNGLDLLGISAPERM 507
|
|
| tRNA-synt_1d |
pfam00750 |
tRNA synthetases class I (R); Other tRNA synthetase sub-families are too dissimilar to be ... |
95-446 |
0e+00 |
|
tRNA synthetases class I (R); Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only arginyl tRNA synthetase.
Pssm-ID: 395607 [Multi-domain] Cd Length: 348 Bit Score: 620.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 95 HVQQALASDRLGVATPEKQTIVVDYSAPNVAKEMHVGHLRSTIIGDTAVRTLEFLGHKVIRANHVGDWGTQFGMLIAWLE 174
Cdd:pfam00750 1 TVPNALLQKGLGKASREKKKVVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQFGMLIAGLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 175 KQQQEN-AGEMELADLEGFYRDAKKHYDEDEEFAERARNYVVKLQSGDEYFREMWRKLVDITMTQNQITYDRLNVTLTRd 253
Cdd:pfam00750 81 KYQDEKtLQEMPIQDLEDFYREAKKHYDEEEEFAERARNYVVKLQSGDEYWRRMWKLIVDITMTQNQRLYDRLDVTLTE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 254 dvMGESLYNPMLPGIVADLKAKGLAVESEGATVVFLDVFknkeGEPMGVIIQKKDGGYLYTTTDIACAKYRYETLHADRV 333
Cdd:pfam00750 160 --MGESLYNPMMNEIVKDFKKNGLVVEIDGALVVFLDEF----GKPMGVIVQKSDGGYLYTTTDIAAAKYRYETLHADRM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 334 LYYIDSRQHQHLMQAWAIVRKAGYVPESVPLEHHMFGMMLGKDGKPFKTRAGGTVKLADLLDEALERARRLVAEKNPD-- 411
Cdd:pfam00750 234 LYVIDSRQSQHMQQAFAILRKAGYVPESKDLEHINFGMVLGKDGKPFKTRKGGTVKLADLLDEALERALQLIMEKNKDki 313
|
330 340 350
....*....|....*....|....*....|....*
gi 24113254 412 MPADELEKLANAVGIGAVKYADLSKNRTTDYIFDW 446
Cdd:pfam00750 314 LQADELEAVADAVGIGAIKYADLSKNRTNDYIFDW 348
|
|
| PLN02286 |
PLN02286 |
arginine-tRNA ligase |
23-577 |
0e+00 |
|
arginine-tRNA ligase
Pssm-ID: 215160 [Multi-domain] Cd Length: 576 Bit Score: 588.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 23 DCEPQIRQSAKVQFGDYQANGMMAVAKKLG------MAPRQLAEQVLTHLDLNGIASKVEIAGPGFINIFLDPAFLAEHV 96
Cdd:PLN02286 20 SVEPLVAACTNPKFGDYQCNNAMGLWSKLKgkgtsfKNPRAVAQAIVKNLPASEMIESTSVAGPGFVNVRLSASWLAKRI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 97 QQAL--ASDRLGVATPeKQTIVVDYSAPNVAKEMHVGHLRSTIIGDTAVRTLEFLGHKVIRANHVGDWGTQFGMLIAWL- 173
Cdd:PLN02286 100 ERMLvdGIDTWAPTLP-VKRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEFSGVEVLRRNHVGDWGTQFGMLIEHLf 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 174 -EKQQQENAGEMELADLEGFYRDAKKHYDEDEEFAERARNYVVKLQSGDEYFREMWRKLVDITMTQNQITYDRLNVTLTR 252
Cdd:PLN02286 179 eKFPNWESVSDQAIGDLQEFYKAAKKRFDEDEEFKARAQQAVVRLQGGDPEYRAAWAKICEISRREFEKVYQRLRVELEE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 253 DdvmGESLYNPMLPGIVADLKAKGLAVESEGATVVFLDVFKNkegePMgvIIQKKDGGYLYTTTDIACAKYRYETLHADR 332
Cdd:PLN02286 259 K---GESFYNPYIPGVIEELESKGLVVESDGARVIFVEGFDI----PL--IVVKSDGGFNYASTDLAALWYRLNEEKAEW 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 333 VLYYIDSRQHQHLMQAWAIVRKAGYVPESVP--LEHHMFGMMLGKDGKPFKTRAGGTVKLADLLDEALERARRLVAEKNP 410
Cdd:PLN02286 330 IIYVTDVGQQQHFDMVFKAAKRAGWLPEDTYprLEHVGFGLVLGEDGKRFRTRSGEVVRLVDLLDEAKSRSKAALIERGK 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 411 D--MPADELEKLANAVGIGAVKYADLSKNRTTDYIFDWDNMLAFEGNTAPYMQYAYTRVLSVFRKAEINEEQLAAA-PVI 487
Cdd:PLN02286 410 DseWTPEELEQAAEAVGYGAVKYADLKNNRLTNYTFSFDQMLDLKGNTAVYLLYAHARICSIIRKSGKDIDELKKTgKIV 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 488 IREDREAQLAARLLQFEETLTVVAREGTPHVMCAYLYDLAGLFSGFYEHCPILSAENEEvrnSRLKLAQLTAKTLKLGLD 567
Cdd:PLN02286 490 LDHPDERALGLHLLQFPEVVEEACTDLLPNRLCEYLYNLSEKFTKFYSNCKVNGSEEET---SRLLLCEATAIVMRKCFH 566
|
570
....*....|
gi 24113254 568 TLGIETVERM 577
Cdd:PLN02286 567 LLGITPLYRL 576
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
114-385 |
2.31e-80 |
|
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. There are at least three subgroups of ArgRS. One type contains both characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The second subtype lacks the KMSKS motif; however, it has a lysine N-terminal to the HIGH motif, which serves as the functional counterpart to the second lysine of the KMSKS motif. A third group, which is found primarily in archaea and a few bacteria, lacks both the KMSKS motif and the HIGH loop lysine.
Pssm-ID: 185675 [Multi-domain] Cd Length: 212 Bit Score: 251.33 E-value: 2.31e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 114 TIVVDYSAPNVAKEMHVGHLRSTIIGDTAVRTLEFLGHKVIRANHVGDWGTQFGMLIAWLEKqqqenagemeladlegfy 193
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSLEK------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 194 rdakkhydedeefaerarnyvvklqsgdeyfremWRKLVDITMTQNQITYDRLNVTltRDDVMGESLYNPMLPGIVADLK 273
Cdd:cd00671 63 ----------------------------------WRKLVEESIKADLETYGRLDVR--FDVWFGESSYLGLMGKVVELLE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 274 AKGLAVESEGATVVFLDVFknkeGEPMGVIIQKKDGGYLYTTTDIACAKYRYEtLHADRVLYYIDSRQHQHLMQAWAIVR 353
Cdd:cd00671 107 ELGLLYEEDGALWLDLTEF----GDDKDRVLVRSDGTYTYFTRDIAYHLDKFE-RGADKIIYVVGADHHGHFKRLFAALE 181
|
250 260 270
....*....|....*....|....*....|..
gi 24113254 354 KAGYvPESVPLEHHMFGMMLGKDGKPFKTRAG 385
Cdd:cd00671 182 LLGY-DEAKKLEHLLYGMVNLPKEGKMSTRAG 212
|
|
| Anticodon_Ia_Arg |
cd07956 |
Anticodon-binding domain of arginyl tRNA synthetases; This domain is found in arginyl tRNA ... |
423-577 |
2.47e-61 |
|
Anticodon-binding domain of arginyl tRNA synthetases; This domain is found in arginyl tRNA synthetases (ArgRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. ArgRS catalyzes the transfer of arginine to the 3'-end of its tRNA.
Pssm-ID: 153410 [Multi-domain] Cd Length: 156 Bit Score: 199.75 E-value: 2.47e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 423 AVGIGAVKYADLSKNRTTDYIFDWDNMLAFEGNTAPYMQYAYTRVLSVFRKAEINEEQLA-AAPVIIREDREAQLAARLL 501
Cdd:cd07956 2 EVGVGAVKYQDLSNKRIKDYTFDWERMLSFEGDTGPYLQYAHARLCSILRKAGETIEAEAdADLSLLPEPDERDLILLLA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24113254 502 QFEETLTVVAREGTPHVMCAYLYDLAGLFSGFYEHCPILSAEnEEVRNSRLKLAQLTAKTLKLGLDTLGIETVERM 577
Cdd:cd07956 82 KFPEVVKNAAETLEPHTIATYLFDLAHAFSKFYNACPVLGAE-EELRNARLALVAAARQVLANGLDLLGIEAPERM 156
|
|
| DALR_1 |
pfam05746 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
460-577 |
6.13e-43 |
|
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain in Arginyl and glycyl tRNA synthetase. This domain is known as the DALR domain after characteriztic conserved amino acids.
Pssm-ID: 399042 [Multi-domain] Cd Length: 117 Bit Score: 149.34 E-value: 6.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 460 MQYAYTRVLSVFRKAEINEEQLAAAPVIIREDREAQLAARLLQFEETLTVVAREGTPHVMCAYLYDLAGLFSGFYEHCPI 539
Cdd:pfam05746 1 LQYAHARICSILRKAGELGINLDIDADLLTEEEEKELLKALLQFPEVLEEAAEELEPHRLANYLYELASAFHSFYNNCRV 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 24113254 540 LSAENEEvRNSRLKLAQLTAKTLKLGLDTLGIETVERM 577
Cdd:pfam05746 81 LDEDNEE-RNARLALLKAVRQVLKNGLDLLGIEAPEKM 117
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
461-577 |
1.49e-34 |
|
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain of Arginyl tRNA synthetase. This domain is known as the DALR domain after characteristic conserved amino acids.
Pssm-ID: 214846 [Multi-domain] Cd Length: 122 Bit Score: 126.54 E-value: 1.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 461 QYAYTRVLSVFRKAEINEEQLAAAPVI----IREDREAQLAARLLQFEETLTVVAREGTPHVMCAYLYDLAGLFSGFYEH 536
Cdd:smart00836 2 QYAHARICSILRKAGEAGETLPDIADAdlslLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYNR 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 24113254 537 CPILSAENEEVRNSRLKLAQLTAKTLKLGLDTLGIETVERM 577
Cdd:smart00836 82 VRVLGEENPELRKARLALLKAVRQVLANGLRLLGISAPERM 122
|
|
| Arg_tRNA_synt_N |
smart01016 |
Arginyl tRNA synthetase N terminal dom; This domain is found at the amino terminus of Arginyl ... |
1-87 |
1.29e-25 |
|
Arginyl tRNA synthetase N terminal dom; This domain is found at the amino terminus of Arginyl tRNA synthetase, also called additional domain 1 (Add-1). It is about 140 residues long and it has been suggested that this domain will be involved in tRNA recognition.
Pssm-ID: 214975 [Multi-domain] Cd Length: 85 Bit Score: 100.35 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 1 MNIQALLSEKVRQAMIAAGAPADcePQIRQSAKVQFGDYQANGMMAVAKKLGMAPRQLAEQVLTHLDLNGIASKVEIAGP 80
Cdd:smart01016 1 DLLKEAIAEALKKALGVEGEPID--IALERPKDPDHGDYATNVAFRLAKKLKKNPRELAEEIAEKLPKSDLVEKVEIAGP 78
|
....*..
gi 24113254 81 GFINIFL 87
Cdd:smart01016 79 GFINFFL 85
|
|
| Arg_tRNA_synt_N |
pfam03485 |
Arginyl tRNA synthetase N terminal domain; This domain is found at the amino terminus of ... |
7-87 |
6.77e-23 |
|
Arginyl tRNA synthetase N terminal domain; This domain is found at the amino terminus of Arginyl tRNA synthetase, also called additional domain 1 (Add-1). It is about 140 residues long and it has been suggested that this domain will be involved in tRNA recognition.
Pssm-ID: 460943 [Multi-domain] Cd Length: 83 Bit Score: 92.68 E-value: 6.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24113254 7 LSEKVRQAMIAAGA--PADCEPQIRQSAKVQFGDYQANGMMAVAKKLGMAPRQLAEQVLTHLDLNGIASKVEIAGPGFIN 84
Cdd:pfam03485 1 LKKAIAKALSKLGGpdLELIDIVIETPKNPKFGDYATNVAMQLAKKLKKNPREIAEEIAEKLEKSDIIEKVEVAGPGFIN 80
|
...
gi 24113254 85 IFL 87
Cdd:pfam03485 81 FFL 83
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
117-167 |
1.59e-07 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 50.94 E-value: 1.59e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 24113254 117 VDYSAPNVAKEMHVGHLRSTIIGDTAVRTLEFLGHKVIRANHVGDWGTQFG 167
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIG 51
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
122-198 |
7.71e-04 |
|
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173899 [Multi-domain] Cd Length: 213 Bit Score: 41.03 E-value: 7.71e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24113254 122 PNVAKEMHVGHLRSTIIGDTAVRTLEFLGHKVIRANHVgdwgTQFGMLIawLEKQQQENAGEMELAD--LEGFYRDAKK 198
Cdd:cd00672 28 PTVYDYAHIGHARTYVVFDVLRRYLEDLGYKVRYVQNI----TDIDDKI--IKRAREEGLSWKEVADyyTKEFFEDMKA 100
|
|
| |
