|
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: 743.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 1 MNIQALLSEKVSQALIAAGA-PADCEPQVRQSAKVQFGDYQANGVMAVAKKLGMPPRQLAEQVLTHLDLTGIASKTEIAG 79
Cdd:COG0018 1 MNIKEELAEAIAAALAALGAgLEEPDILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDADPLVEKVEIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 80 PGFINIFLEPAFLASHVDAALKS-DRLGVSRP-QAQTVVIDYSAPNVAKEMHVGHLRSTIIGDAAVRTLEFLGHKVIRAN 157
Cdd:COG0018 81 PGFINFFLSPAALAAVLKEILADgEDYGRSDAgKGKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYDVTREN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 158 HVGDWGTQFGMLIAYLEKQQQENA--GEMALADLEGFYREAKKHYDEDEAFAERARSYVVKLQGGDQYFLEMWRKLVDIT 235
Cdd:COG0018 161 YINDAGTQIGKLALSLERYGEEEIepESKPDGYLGDLYVKFHKEYEEDPELEDIARELLAKLEPGDEEALELWKKAVDWS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 236 MSQNQLTYNRLNVTLtrDDVMGESLYNPM--LPGIVADLKAKNLAVESEGATVVFLDEYknkeGEPMGVIIQKKDGGYLY 313
Cdd:COG0018 241 LEEIKEDLKRLGVEF--DVWFSESSLYDSgaVEEVVEELKEKGLLYESDGALWVRLTEF----GDDKDRVLVKSDGTYTY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 314 TTTDIACAKYRYETLHADRVLYYIDSRQHQHLMQAWTIVRKAGYVPDcVPLEHHMFGMMLGKDGKPFKTRAGGTVKLSDL 393
Cdd:COG0018 315 FTTDIAYHLYKFERYGFDRVIYVVGADQHGHFKRLFAALKALGYDPA-KDLEHLLFGMVNLRDGEKMSTRAGTVVTLDDL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 394 LDEALERARRLVAEKNPDmpadELEKLANAVGIGAVKYADLSKNRTTDYIFDWDNMLAFEGNTAPYMQYAYTRVLSVFRK 473
Cdd:COG0018 394 LDEAVERAREIIEEKSEE----EKEEIAEQVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNTNPYVQYAHARICSILRK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 474 ANIDENVLANATVT-ITEDREAQLAARLLQFEETLTVVARDGTPHVMCAYLYDLAGLFSGFYEHCPILSAENESVRNSRL 552
Cdd:COG0018 470 AGEELDGLAEADLSlLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRILKAEDEELRAARL 549
|
570 580
....*....|....*....|....*
gi 504697228 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: 703.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 3 IQALLSEKVSQALIAAGAPADCEPQVRQSAKVQFGDYQANGVMAVAKKLGMPPRQLAEQVLTHLDLTGIASKTEIAGPgF 82
Cdd:TIGR00456 1 IKTLLKEEISQALLKAGLSKESEILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKLKTGEIIEKVEAAGP-F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 83 INIFLEPAFLASHV--DAALKSDRLGVSRPQAQTVVIDYSAPNVAKEMHVGHLRSTIIGDAAVRTLEFLGHKVIRANHVG 160
Cdd:TIGR00456 80 INFFLSPQKLLERLiqKILTQKEKYGSKKLKNKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 161 DWGTQFGMLIAYLEKQQQE---NAGEMALADLEGFYREAKKHYDEDEAFAERARSYVVKLQGGDQYFLEMWRKLVDITMS 237
Cdd:TIGR00456 160 DWGRQFGLLALGVEKFGNEalnIAVKKPDHGLEGFYVEINKRLEENEELEEEARELFVKLESGDEETIKLWKRLVEYSLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 238 QNQLTYNRLNVTLTRDDVMGESLYNPMLPGIVADLKAKNLAVEsEGATVVFLDEYKNKegepMGVIIQKKDGGYLYTTTD 317
Cdd:TIGR00456 240 GIKETYDRLNIHFDSFVWEGESVKNGMLPKVLEDLKEKGLVVE-DGALWLDLTLFGDK----KDRVLQKSDGTYLYLTTD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 318 IACAKYRYETlHADRVLYYIDSRQHQHLMQAWTIVRKAGYvpDCVPLEHHMFGMMLGKDgkpFKTRAGGTVKLSDLLDEA 397
Cdd:TIGR00456 315 IAYHLDKLER-GFDKMIYVWGSDHHLHIAQMFAILEKLGY--KKKELEHLNFGMVPLYS---MKTRRGNVISLDNLLDEA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 398 LERARRLVAEKNpdmpADELEKLANAVGIGAVKYADLSKNRTTDYIFDWDNMLAFEGNTAPYMQYAYTRVLSVFRKANID 477
Cdd:TIGR00456 389 SKRAGNVITIKN----DLEEEKVADAVGIGAVRYFDLSKNRTTDYVFDWDAMLSFEGNTAPYIQYAHARICSILRKAEID 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 478 ENVLANATVTITEDREAQLAARLLQFEETLTVVARDGTPHVMCAYLYDLAGLFSGFYEHCPILSAENEsVRNSRLKLAQL 557
Cdd:TIGR00456 465 GEKLIADDFELLEEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACPVLDAENE-LAAARLALLKA 543
|
570 580
....*....|....*....|
gi 504697228 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: 642.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 1 MNIQALLSEKVSQALIAAGAPADCEPQVRQSAKVQFGDYQANGVMAVAKKLGMPPRQLAEQVLTHLdltgiaSKTEIAGP 80
Cdd:PRK01611 3 MDIKELLAEALAAALEAGGLPELPAVLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIVEAI------EKVEIAGP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 81 GFINIFLEPAFLASHVDAALK-SDRLGVSRP-QAQTVVIDYSAPNVAKEMHVGHLRSTIIGDAAVRTLEFLGHKVIRANH 158
Cdd:PRK01611 77 GFINFFLDPAALAELVLAILEaGERYGRSDIgKGKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDVTREYY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 159 VGDWGTQFGMLIAYLEKqqqenagemaladlegfyreakkhydedeafaerarsyvvklqggdqyfleMWRKLVDITMSQ 238
Cdd:PRK01611 157 VNDAGTQIGMLIASLEL---------------------------------------------------LWRKAVDISLDE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 239 NQLTYNRLNVTLTRDDVMGESLYNPMLPGIVADLKAKNLAV-ESEGATVVFLDEYknkeGEPMGVIIQKKDGGYLYTTTD 317
Cdd:PRK01611 186 IKEDLDRLGVHFDVWFSESELYYNGKVDEVVEDLKEKGLLYvESDGALWVRLTEF----GDDKDRVLIKSDGTYTYFTRD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 318 IACAKYRYETLhaDRVLYYIDSRQHQHLMQAWTIVRKAGYVPDCVP-LEHHMFGMMLGKDGKPFKTRAGGTVKLSDLLDE 396
Cdd:PRK01611 262 IAYHLYKFERF--DRVIYVVGADHHGHFKRLKAALKALGYDPDALEvLLHQMVGLVRGGEGVKMSTRAGNVVTLDDLLDE 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 397 ALERARRLVAEKnpdmpadeleKLANAVGIGAVKYADLSKNRTTDYIFDWDNMLAFEGNTAPYMQYAYTRVLSVFRKANi 476
Cdd:PRK01611 340 AVGRARELIEEK----------EIAEAVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPPYVQYAHARICSILRKAA- 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 477 dENVLANATVTITEDREAQLAARLLQFEETLTVVARDGTPHVMCAYLYDLAGLFSGFYEHCPiLSAENESVRNSRLKLAQ 556
Cdd:PRK01611 409 -EAGIDLLLALLTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYNRVL-LKDEEEELRNARLALVK 486
|
570 580
....*....|....*....|.
gi 504697228 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: 594.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 95 HVDAALKSDRLGVSRPQAQTVVIDYSAPNVAKEMHVGHLRSTIIGDAAVRTLEFLGHKVIRANHVGDWGTQFGMLIAYLE 174
Cdd:pfam00750 1 TVPNALLQKGLGKASREKKKVVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQFGMLIAGLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 175 KQQQEN-AGEMALADLEGFYREAKKHYDEDEAFAERARSYVVKLQGGDQYFLEMWRKLVDITMSQNQLTYNRLNVTLTRd 253
Cdd:pfam00750 81 KYQDEKtLQEMPIQDLEDFYREAKKHYDEEEEFAERARNYVVKLQSGDEYWRRMWKLIVDITMTQNQRLYDRLDVTLTE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 254 dvMGESLYNPMLPGIVADLKAKNLAVESEGATVVFLDEYknkeGEPMGVIIQKKDGGYLYTTTDIACAKYRYETLHADRV 333
Cdd:pfam00750 160 --MGESLYNPMMNEIVKDFKKNGLVVEIDGALVVFLDEF----GKPMGVIVQKSDGGYLYTTTDIAAAKYRYETLHADRM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 334 LYYIDSRQHQHLMQAWTIVRKAGYVPDCVPLEHHMFGMMLGKDGKPFKTRAGGTVKLSDLLDEALERARRLVAEKNPD-- 411
Cdd:pfam00750 234 LYVIDSRQSQHMQQAFAILRKAGYVPESKDLEHINFGMVLGKDGKPFKTRKGGTVKLADLLDEALERALQLIMEKNKDki 313
|
330 340 350
....*....|....*....|....*....|....*
gi 504697228 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 |
8.56e-78 |
|
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: 244.78 E-value: 8.56e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 114 TVVIDYSAPNVAKEMHVGHLRSTIIGDAAVRTLEFLGHKVIRANHVGDWGTQFGMLIAYLEKqqqenagemaladlegfy 193
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSLEK------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 194 reakkhydedeafaerarsyvvklqggdqyflemWRKLVDITMSQNQLTYNRLNVTltRDDVMGESLYNPMLPGIVADLK 273
Cdd:cd00671 63 ----------------------------------WRKLVEESIKADLETYGRLDVR--FDVWFGESSYLGLMGKVVELLE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 274 AKNLAVESEGATVVFLDEYknkeGEPMGVIIQKKDGGYLYTTTDIACAKYRYEtLHADRVLYYIDSRQHQHLMQAWTIVR 353
Cdd:cd00671 107 ELGLLYEEDGALWLDLTEF----GDDKDRVLVRSDGTYTYFTRDIAYHLDKFE-RGADKIIYVVGADHHGHFKRLFAALE 181
|
250 260 270
....*....|....*....|....*....|..
gi 504697228 354 KAGYvPDCVPLEHHMFGMMLGKDGKPFKTRAG 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 |
6.00e-33 |
|
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: 122.30 E-value: 6.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 461 QYAYTRVLSVFRKANIDENVLANATVT----ITEDREAQLAARLLQFEETLTVVARDGTPHVMCAYLYDLAGLFSGFYEH 536
Cdd:smart00836 2 QYAHARICSILRKAGEAGETLPDIADAdlslLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYNR 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 504697228 537 CPILSAENESVRNSRLKLAQLTAKTLKLGLDTLGIETVERM 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: 743.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 1 MNIQALLSEKVSQALIAAGA-PADCEPQVRQSAKVQFGDYQANGVMAVAKKLGMPPRQLAEQVLTHLDLTGIASKTEIAG 79
Cdd:COG0018 1 MNIKEELAEAIAAALAALGAgLEEPDILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDADPLVEKVEIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 80 PGFINIFLEPAFLASHVDAALKS-DRLGVSRP-QAQTVVIDYSAPNVAKEMHVGHLRSTIIGDAAVRTLEFLGHKVIRAN 157
Cdd:COG0018 81 PGFINFFLSPAALAAVLKEILADgEDYGRSDAgKGKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYDVTREN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 158 HVGDWGTQFGMLIAYLEKQQQENA--GEMALADLEGFYREAKKHYDEDEAFAERARSYVVKLQGGDQYFLEMWRKLVDIT 235
Cdd:COG0018 161 YINDAGTQIGKLALSLERYGEEEIepESKPDGYLGDLYVKFHKEYEEDPELEDIARELLAKLEPGDEEALELWKKAVDWS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 236 MSQNQLTYNRLNVTLtrDDVMGESLYNPM--LPGIVADLKAKNLAVESEGATVVFLDEYknkeGEPMGVIIQKKDGGYLY 313
Cdd:COG0018 241 LEEIKEDLKRLGVEF--DVWFSESSLYDSgaVEEVVEELKEKGLLYESDGALWVRLTEF----GDDKDRVLVKSDGTYTY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 314 TTTDIACAKYRYETLHADRVLYYIDSRQHQHLMQAWTIVRKAGYVPDcVPLEHHMFGMMLGKDGKPFKTRAGGTVKLSDL 393
Cdd:COG0018 315 FTTDIAYHLYKFERYGFDRVIYVVGADQHGHFKRLFAALKALGYDPA-KDLEHLLFGMVNLRDGEKMSTRAGTVVTLDDL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 394 LDEALERARRLVAEKNPDmpadELEKLANAVGIGAVKYADLSKNRTTDYIFDWDNMLAFEGNTAPYMQYAYTRVLSVFRK 473
Cdd:COG0018 394 LDEAVERAREIIEEKSEE----EKEEIAEQVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNTNPYVQYAHARICSILRK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 474 ANIDENVLANATVT-ITEDREAQLAARLLQFEETLTVVARDGTPHVMCAYLYDLAGLFSGFYEHCPILSAENESVRNSRL 552
Cdd:COG0018 470 AGEELDGLAEADLSlLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRILKAEDEELRAARL 549
|
570 580
....*....|....*....|....*
gi 504697228 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: 703.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 3 IQALLSEKVSQALIAAGAPADCEPQVRQSAKVQFGDYQANGVMAVAKKLGMPPRQLAEQVLTHLDLTGIASKTEIAGPgF 82
Cdd:TIGR00456 1 IKTLLKEEISQALLKAGLSKESEILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKLKTGEIIEKVEAAGP-F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 83 INIFLEPAFLASHV--DAALKSDRLGVSRPQAQTVVIDYSAPNVAKEMHVGHLRSTIIGDAAVRTLEFLGHKVIRANHVG 160
Cdd:TIGR00456 80 INFFLSPQKLLERLiqKILTQKEKYGSKKLKNKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 161 DWGTQFGMLIAYLEKQQQE---NAGEMALADLEGFYREAKKHYDEDEAFAERARSYVVKLQGGDQYFLEMWRKLVDITMS 237
Cdd:TIGR00456 160 DWGRQFGLLALGVEKFGNEalnIAVKKPDHGLEGFYVEINKRLEENEELEEEARELFVKLESGDEETIKLWKRLVEYSLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 238 QNQLTYNRLNVTLTRDDVMGESLYNPMLPGIVADLKAKNLAVEsEGATVVFLDEYKNKegepMGVIIQKKDGGYLYTTTD 317
Cdd:TIGR00456 240 GIKETYDRLNIHFDSFVWEGESVKNGMLPKVLEDLKEKGLVVE-DGALWLDLTLFGDK----KDRVLQKSDGTYLYLTTD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 318 IACAKYRYETlHADRVLYYIDSRQHQHLMQAWTIVRKAGYvpDCVPLEHHMFGMMLGKDgkpFKTRAGGTVKLSDLLDEA 397
Cdd:TIGR00456 315 IAYHLDKLER-GFDKMIYVWGSDHHLHIAQMFAILEKLGY--KKKELEHLNFGMVPLYS---MKTRRGNVISLDNLLDEA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 398 LERARRLVAEKNpdmpADELEKLANAVGIGAVKYADLSKNRTTDYIFDWDNMLAFEGNTAPYMQYAYTRVLSVFRKANID 477
Cdd:TIGR00456 389 SKRAGNVITIKN----DLEEEKVADAVGIGAVRYFDLSKNRTTDYVFDWDAMLSFEGNTAPYIQYAHARICSILRKAEID 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 478 ENVLANATVTITEDREAQLAARLLQFEETLTVVARDGTPHVMCAYLYDLAGLFSGFYEHCPILSAENEsVRNSRLKLAQL 557
Cdd:TIGR00456 465 GEKLIADDFELLEEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACPVLDAENE-LAAARLALLKA 543
|
570 580
....*....|....*....|
gi 504697228 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: 642.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 1 MNIQALLSEKVSQALIAAGAPADCEPQVRQSAKVQFGDYQANGVMAVAKKLGMPPRQLAEQVLTHLdltgiaSKTEIAGP 80
Cdd:PRK01611 3 MDIKELLAEALAAALEAGGLPELPAVLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIVEAI------EKVEIAGP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 81 GFINIFLEPAFLASHVDAALK-SDRLGVSRP-QAQTVVIDYSAPNVAKEMHVGHLRSTIIGDAAVRTLEFLGHKVIRANH 158
Cdd:PRK01611 77 GFINFFLDPAALAELVLAILEaGERYGRSDIgKGKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDVTREYY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 159 VGDWGTQFGMLIAYLEKqqqenagemaladlegfyreakkhydedeafaerarsyvvklqggdqyfleMWRKLVDITMSQ 238
Cdd:PRK01611 157 VNDAGTQIGMLIASLEL---------------------------------------------------LWRKAVDISLDE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 239 NQLTYNRLNVTLTRDDVMGESLYNPMLPGIVADLKAKNLAV-ESEGATVVFLDEYknkeGEPMGVIIQKKDGGYLYTTTD 317
Cdd:PRK01611 186 IKEDLDRLGVHFDVWFSESELYYNGKVDEVVEDLKEKGLLYvESDGALWVRLTEF----GDDKDRVLIKSDGTYTYFTRD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 318 IACAKYRYETLhaDRVLYYIDSRQHQHLMQAWTIVRKAGYVPDCVP-LEHHMFGMMLGKDGKPFKTRAGGTVKLSDLLDE 396
Cdd:PRK01611 262 IAYHLYKFERF--DRVIYVVGADHHGHFKRLKAALKALGYDPDALEvLLHQMVGLVRGGEGVKMSTRAGNVVTLDDLLDE 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 397 ALERARRLVAEKnpdmpadeleKLANAVGIGAVKYADLSKNRTTDYIFDWDNMLAFEGNTAPYMQYAYTRVLSVFRKANi 476
Cdd:PRK01611 340 AVGRARELIEEK----------EIAEAVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPPYVQYAHARICSILRKAA- 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 477 dENVLANATVTITEDREAQLAARLLQFEETLTVVARDGTPHVMCAYLYDLAGLFSGFYEHCPiLSAENESVRNSRLKLAQ 556
Cdd:PRK01611 409 -EAGIDLLLALLTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYNRVL-LKDEEEELRNARLALVK 486
|
570 580
....*....|....*....|.
gi 504697228 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: 594.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 95 HVDAALKSDRLGVSRPQAQTVVIDYSAPNVAKEMHVGHLRSTIIGDAAVRTLEFLGHKVIRANHVGDWGTQFGMLIAYLE 174
Cdd:pfam00750 1 TVPNALLQKGLGKASREKKKVVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQFGMLIAGLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 175 KQQQEN-AGEMALADLEGFYREAKKHYDEDEAFAERARSYVVKLQGGDQYFLEMWRKLVDITMSQNQLTYNRLNVTLTRd 253
Cdd:pfam00750 81 KYQDEKtLQEMPIQDLEDFYREAKKHYDEEEEFAERARNYVVKLQSGDEYWRRMWKLIVDITMTQNQRLYDRLDVTLTE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 254 dvMGESLYNPMLPGIVADLKAKNLAVESEGATVVFLDEYknkeGEPMGVIIQKKDGGYLYTTTDIACAKYRYETLHADRV 333
Cdd:pfam00750 160 --MGESLYNPMMNEIVKDFKKNGLVVEIDGALVVFLDEF----GKPMGVIVQKSDGGYLYTTTDIAAAKYRYETLHADRM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 334 LYYIDSRQHQHLMQAWTIVRKAGYVPDCVPLEHHMFGMMLGKDGKPFKTRAGGTVKLSDLLDEALERARRLVAEKNPD-- 411
Cdd:pfam00750 234 LYVIDSRQSQHMQQAFAILRKAGYVPESKDLEHINFGMVLGKDGKPFKTRKGGTVKLADLLDEALERALQLIMEKNKDki 313
|
330 340 350
....*....|....*....|....*....|....*
gi 504697228 412 MPADELEKLANAVGIGAVKYADLSKNRTTDYIFDW 446
Cdd:pfam00750 314 LQADELEAVADAVGIGAIKYADLSKNRTNDYIFDW 348
|
|
| PLN02286 |
PLN02286 |
arginine-tRNA ligase |
7-577 |
0e+00 |
|
arginine-tRNA ligase
Pssm-ID: 215160 [Multi-domain] Cd Length: 576 Bit Score: 584.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 7 LSEKVSQAL-IAAGAPADCEPQVRQSAKVQFGDYQANGVMAVAKKL-GMP-----PRQLAEQVLTHLDLTGIASKTEIAG 79
Cdd:PLN02286 3 LAKLFEASLrLTVPDEPSVEPLVAACTNPKFGDYQCNNAMGLWSKLkGKGtsfknPRAVAQAIVKNLPASEMIESTSVAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 80 PGFINIFLEPAFLASHVDAALKS--DRLGVSRPqAQTVVIDYSAPNVAKEMHVGHLRSTIIGDAAVRTLEFLGHKVIRAN 157
Cdd:PLN02286 83 PGFVNVRLSASWLAKRIERMLVDgiDTWAPTLP-VKRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEFSGVEVLRRN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 158 HVGDWGTQFGMLIAYL--EKQQQENAGEMALADLEGFYREAKKHYDEDEAFAERARSYVVKLQGGDQYFLEMWRKLVDIT 235
Cdd:PLN02286 162 HVGDWGTQFGMLIEHLfeKFPNWESVSDQAIGDLQEFYKAAKKRFDEDEEFKARAQQAVVRLQGGDPEYRAAWAKICEIS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 236 MSQNQLTYNRLNVTLTRDdvmGESLYNPMLPGIVADLKAKNLAVESEGATVVFLDEYKNkegePMgvIIQKKDGGYLYTT 315
Cdd:PLN02286 242 RREFEKVYQRLRVELEEK---GESFYNPYIPGVIEELESKGLVVESDGARVIFVEGFDI----PL--IVVKSDGGFNYAS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 316 TDIACAKYRYETLHADRVLYYIDSRQHQHLMQAWTIVRKAGYVPDCVP--LEHHMFGMMLGKDGKPFKTRAGGTVKLSDL 393
Cdd:PLN02286 313 TDLAALWYRLNEEKAEWIIYVTDVGQQQHFDMVFKAAKRAGWLPEDTYprLEHVGFGLVLGEDGKRFRTRSGEVVRLVDL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 394 LDEALERARRLVAEKNPD--MPADELEKLANAVGIGAVKYADLSKNRTTDYIFDWDNMLAFEGNTAPYMQYAYTRVLSVF 471
Cdd:PLN02286 393 LDEAKSRSKAALIERGKDseWTPEELEQAAEAVGYGAVKYADLKNNRLTNYTFSFDQMLDLKGNTAVYLLYAHARICSII 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 472 RKANIDENVLANAT-VTITEDREAQLAARLLQFEETLTVVARDGTPHVMCAYLYDLAGLFSGFYEHCPILSAENESvrnS 550
Cdd:PLN02286 473 RKSGKDIDELKKTGkIVLDHPDERALGLHLLQFPEVVEEACTDLLPNRLCEYLYNLSEKFTKFYSNCKVNGSEEET---S 549
|
570 580
....*....|....*....|....*..
gi 504697228 551 RLKLAQLTAKTLKLGLDTLGIETVERM 577
Cdd:PLN02286 550 RLLLCEATAIVMRKCFHLLGITPLYRL 576
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
114-385 |
8.56e-78 |
|
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: 244.78 E-value: 8.56e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 114 TVVIDYSAPNVAKEMHVGHLRSTIIGDAAVRTLEFLGHKVIRANHVGDWGTQFGMLIAYLEKqqqenagemaladlegfy 193
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSLEK------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 194 reakkhydedeafaerarsyvvklqggdqyflemWRKLVDITMSQNQLTYNRLNVTltRDDVMGESLYNPMLPGIVADLK 273
Cdd:cd00671 63 ----------------------------------WRKLVEESIKADLETYGRLDVR--FDVWFGESSYLGLMGKVVELLE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 274 AKNLAVESEGATVVFLDEYknkeGEPMGVIIQKKDGGYLYTTTDIACAKYRYEtLHADRVLYYIDSRQHQHLMQAWTIVR 353
Cdd:cd00671 107 ELGLLYEEDGALWLDLTEF----GDDKDRVLVRSDGTYTYFTRDIAYHLDKFE-RGADKIIYVVGADHHGHFKRLFAALE 181
|
250 260 270
....*....|....*....|....*....|..
gi 504697228 354 KAGYvPDCVPLEHHMFGMMLGKDGKPFKTRAG 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 |
9.92e-63 |
|
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: 203.21 E-value: 9.92e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 423 AVGIGAVKYADLSKNRTTDYIFDWDNMLAFEGNTAPYMQYAYTRVLSVFRKANIDENVLANATV-TITEDREAQLAARLL 501
Cdd:cd07956 2 EVGVGAVKYQDLSNKRIKDYTFDWERMLSFEGDTGPYLQYAHARLCSILRKAGETIEAEADADLsLLPEPDERDLILLLA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504697228 502 QFEETLTVVARDGTPHVMCAYLYDLAGLFSGFYEHCPILSAEnESVRNSRLKLAQLTAKTLKLGLDTLGIETVERM 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 |
1.42e-42 |
|
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: 148.57 E-value: 1.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 460 MQYAYTRVLSVFRKANIDENVLANATVTITEDREAQLAARLLQFEETLTVVARDGTPHVMCAYLYDLAGLFSGFYEHCPI 539
Cdd:pfam05746 1 LQYAHARICSILRKAGELGINLDIDADLLTEEEEKELLKALLQFPEVLEEAAEELEPHRLANYLYELASAFHSFYNNCRV 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 504697228 540 LSAENEsVRNSRLKLAQLTAKTLKLGLDTLGIETVERM 577
Cdd:pfam05746 81 LDEDNE-ERNARLALLKAVRQVLKNGLDLLGIEAPEKM 117
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
461-577 |
6.00e-33 |
|
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: 122.30 E-value: 6.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 461 QYAYTRVLSVFRKANIDENVLANATVT----ITEDREAQLAARLLQFEETLTVVARDGTPHVMCAYLYDLAGLFSGFYEH 536
Cdd:smart00836 2 QYAHARICSILRKAGEAGETLPDIADAdlslLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYNR 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 504697228 537 CPILSAENESVRNSRLKLAQLTAKTLKLGLDTLGIETVERM 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 |
4.63e-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: 98.81 E-value: 4.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 1 MNIQALLSEKVSQALIAAGAPADcePQVRQSAKVQFGDYQANGVMAVAKKLGMPPRQLAEQVLTHLDLTGIASKTEIAGP 80
Cdd:smart01016 1 DLLKEAIAEALKKALGVEGEPID--IALERPKDPDHGDYATNVAFRLAKKLKKNPRELAEEIAEKLPKSDLVEKVEIAGP 78
|
....*..
gi 504697228 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 |
1.23e-22 |
|
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: 91.91 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 7 LSEKVSQALIAAGA--PADCEPQVRQSAKVQFGDYQANGVMAVAKKLGMPPRQLAEQVLTHLDLTGIASKTEIAGPGFIN 84
Cdd:pfam03485 1 LKKAIAKALSKLGGpdLELIDIVIETPKNPKFGDYATNVAMQLAKKLKKNPREIAEEIAEKLEKSDIIEKVEVAGPGFIN 80
|
...
gi 504697228 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 ... |
119-260 |
2.58e-08 |
|
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: 52.87 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697228 119 YSAPNVAKEMHVGHLRSTIIGDAAVRTLEFLGHKVIRANHVGDWGTQFGmliayleKQQQENaGEMALADLEGFYREAKK 198
Cdd:cd00802 3 FSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIG-------DPANKK-GENAKAFVERWIERIKE 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504697228 199 HYDEDEAFAERARSYVVK-----LQGGDQYF-LEMWRKLVD---ITMSQNQLTYNRLNVTLTRddVMGESL 260
Cdd:cd00802 75 DVEYMFLQAADFLLLYETecdihLGGSDQLGhIELGLELLKkagGPARPFGLTFGRVMGADGT--KMSKSK 143
|
|
| |
