|
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: 730.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 1 MNIQALINDKVSQALEA-AGAPAGSPAAVRQSAKPQFGDYQANGVMGVAKRLGTNPREFAQKVLDVLNLDGIASKVEIAG 79
Cdd:COG0018 1 MNIKEELAEAIAAALAAlGAGLEEPDILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDADPLVEKVEIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 80 PGFLNIFLDEAFLAKQADAALAD-SRLGVA-VAETQTIVADYSAPNVAKEMHVGHLRSTIIGDAVVRTLEFLGHNVIRAN 157
Cdd:COG0018 81 PGFINFFLSPAALAAVLKEILADgEDYGRSdAGKGKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYDVTREN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 158 HIGDWGTQFGMLIANLERVQAESGEV-SMELADLEGFYRESKKLYDEDEEFAVKARGYVVKLQSGDEFCAEMWKKLVDVT 236
Cdd:COG0018 161 YINDAGTQIGKLALSLERYGEEEIEPeSKPDGYLGDLYVKFHKEYEEDPELEDIARELLAKLEPGDEEALELWKKAVDWS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 237 MIQNQRNYDRLNVSLtrDDVMGESMYNHM--LPTIVADLKEQGLAKEDDGAQVVFLEEYknkdGDPMGVIIQKRDGGFLY 314
Cdd:COG0018 241 LEEIKEDLKRLGVEF--DVWFSESSLYDSgaVEEVVEELKEKGLLYESDGALWVRLTEF----GDDKDRVLVKSDGTYTY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 315 TTTDIACAKYRFEELGADRVLYFIDSRQHQHLMQAWTIVRKAGYIPESvSLEHHAFGMMLGKDGKPFKTRAGGTVRLADL 394
Cdd:COG0018 315 FTTDIAYHLYKFERYGFDRVIYVVGADQHGHFKRLFAALKALGYDPAK-DLEHLLFGMVNLRDGEKMSTRAGTVVTLDDL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 395 LDEAEVRAAQLIESKNpelaEDEKKVIANTVAMAAVKYADLSKHRTTDYVFDWDNMLAFEGNTAPYMQYAYTRVASIFAK 474
Cdd:COG0018 394 LDEAVERAREIIEEKS----EEEKEEIAEQVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNTNPYVQYAHARICSILRK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 475 AGISMDSLEGE--IKITEEKEKALIAKLLQFEEAVQSVAREGQPHIMCSYLFELAGQFSSFYEACPILVAEDETVKQSRL 552
Cdd:COG0018 470 AGEELDGLAEAdlSLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRILKAEDEELRAARL 549
|
570 580
....*....|....*....|....*
gi 1519401526 553 KLAALTAKTIKQGLSLLGIDTLERM 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: 626.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 3 IQALINDKVSQALEAAGAPAGSPAAVRQSAKPQFGDYQANGVMGVAKRLGTNPREFAQKVLDVLNLDGIASKVEIAGPgF 82
Cdd:TIGR00456 1 IKTLLKEEISQALLKAGLSKESEILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKLKTGEIIEKVEAAGP-F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 83 LNIFLDEAFLAKQ--ADAALADSRLGVAVAETQTIVADYSAPNVAKEMHVGHLRSTIIGDAVVRTLEFLGHNVIRANHIG 160
Cdd:TIGR00456 80 INFFLSPQKLLERliQKILTQKEKYGSKKLKNKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 161 DWGTQFGMLIANLERVQAESG--EVSMELADLEGFYRESKKLYDEDEEFAVKARGYVVKLQSGDEFCAEMWKKLVDVTMI 238
Cdd:TIGR00456 160 DWGRQFGLLALGVEKFGNEALniAVKKPDHGLEGFYVEINKRLEENEELEEEARELFVKLESGDEETIKLWKRLVEYSLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 239 QNQRNYDRLNVSLTRDDVMGESMYNHMLPTIVADLKEQGLAKEdDGAQVVFLEEYKNKdgdpMGVIIQKRDGGFLYTTTD 318
Cdd:TIGR00456 240 GIKETYDRLNIHFDSFVWEGESVKNGMLPKVLEDLKEKGLVVE-DGALWLDLTLFGDK----KDRVLQKSDGTYLYLTTD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 319 IACAKYRFEElGADRVLYFIDSRQHQHLMQAWTIVRKAGYipESVSLEHHAFGMMLGKDgkpFKTRAGGTVRLADLLDEA 398
Cdd:TIGR00456 315 IAYHLDKLER-GFDKMIYVWGSDHHLHIAQMFAILEKLGY--KKKELEHLNFGMVPLYS---MKTRRGNVISLDNLLDEA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 399 EVRAAQLIESKNPELAEDekkvIANTVAMAAVKYADLSKHRTTDYVFDWDNMLAFEGNTAPYMQYAYTRVASIFAKAGIS 478
Cdd:TIGR00456 389 SKRAGNVITIKNDLEEEK----VADAVGIGAVRYFDLSKNRTTDYVFDWDAMLSFEGNTAPYIQYAHARICSILRKAEID 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 479 -MDSLEGEIKITEEKEKALIAKLLQFEEAVQSVAREGQPHIMCSYLFELAGQFSSFYEACPILVAEDEtVKQSRLKLAAL 557
Cdd:TIGR00456 465 gEKLIADDFELLEEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACPVLDAENE-LAAARLALLKA 543
|
570 580
....*....|....*....|
gi 1519401526 558 TAKTIKQGLSLLGIDTLERM 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: 626.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 1 MNIQALINDKVSQALEAAGAPAGSPAAVRQSAKPQFGDYQANGVMGVAKRLGTNPREFAQKVLDVLnldgiaSKVEIAGP 80
Cdd:PRK01611 3 MDIKELLAEALAAALEAGGLPELPAVLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIVEAI------EKVEIAGP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 81 GFLNIFLDEAFLAKQADAAL-ADSRLGV-AVAETQTIVADYSAPNVAKEMHVGHLRSTIIGDAVVRTLEFLGHNVIRANH 158
Cdd:PRK01611 77 GFINFFLDPAALAELVLAILeAGERYGRsDIGKGKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDVTREYY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 159 IGDWGTQFGMLIANLErvqaesgevsmeladlegfyreskklydedeefavkargyvvklqsgdefcaEMWKKLVDVTMI 238
Cdd:PRK01611 157 VNDAGTQIGMLIASLE----------------------------------------------------LLWRKAVDISLD 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 239 QNQRNYDRLNVSLTRDDVMGESMYNHMLPTIVADLKEQGLA-KEDDGAQVVFLEEYknkdGDPMGVIIQKRDGGFLYTTT 317
Cdd:PRK01611 185 EIKEDLDRLGVHFDVWFSESELYYNGKVDEVVEDLKEKGLLyVESDGALWVRLTEF----GDDKDRVLIKSDGTYTYFTR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 318 DIACAKYRFEELgaDRVLYFIDSRQHQHLMQAWTIVRKAGYIPESVS-LEHHAFGMMLGKDGKPFKTRAGGTVRLADLLD 396
Cdd:PRK01611 261 DIAYHLYKFERF--DRVIYVVGADHHGHFKRLKAALKALGYDPDALEvLLHQMVGLVRGGEGVKMSTRAGNVVTLDDLLD 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 397 EAEVRAAQLIEsknpelaedeKKVIANTVAMAAVKYADLSKHRTTDYVFDWDNMLAFEGNTAPYMQYAYTRVASIFAKAG 476
Cdd:PRK01611 339 EAVGRARELIE----------EKEIAEAVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPPYVQYAHARICSILRKAA 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 477 ISMDSLEGEIkITEEKEKALIAKLLQFEEAVQSVAREGQPHIMCSYLFELAGQFSSFYEACPiLVAEDETVKQSRLKLAA 556
Cdd:PRK01611 409 EAGIDLLLAL-LTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYNRVL-LKDEEEELRNARLALVK 486
|
570 580
....*....|....*....|.
gi 1519401526 557 LTAKTIKQGLSLLGIDTLERM 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 ... |
95-447 |
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: 531.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 95 QADAALADSRLGVAVAETQTIVADYSAPNVAKEMHVGHLRSTIIGDAVVRTLEFLGHNVIRANHIGDWGTQFGMLIANLE 174
Cdd:pfam00750 1 TVPNALLQKGLGKASREKKKVVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQFGMLIAGLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 175 RVQAESGEVSMELADLEGFYRESKKLYDEDEEFAVKARGYVVKLQSGDEFCAEMWKKLVDVTMIQNQRNYDRLNVSLTRd 254
Cdd:pfam00750 81 KYQDEKTLQEMPIQDLEDFYREAKKHYDEEEEFAERARNYVVKLQSGDEYWRRMWKLIVDITMTQNQRLYDRLDVTLTE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 255 dvMGESMYNHMLPTIVADLKEQGLAKEDDGAQVVFLEEYknkdGDPMGVIIQKRDGGFLYTTTDIACAKYRFEELGADRV 334
Cdd:pfam00750 160 --MGESLYNPMMNEIVKDFKKNGLVVEIDGALVVFLDEF----GKPMGVIVQKSDGGYLYTTTDIAAAKYRYETLHADRM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 335 LYFIDSRQHQHLMQAWTIVRKAGYIPESVSLEHHAFGMMLGKDGKPFKTRAGGTVRLADLLDEAEVRAAQLIESKNPE-- 412
Cdd:pfam00750 234 LYVIDSRQSQHMQQAFAILRKAGYVPESKDLEHINFGMVLGKDGKPFKTRKGGTVKLADLLDEALERALQLIMEKNKDki 313
|
330 340 350
....*....|....*....|....*....|....*
gi 1519401526 413 LAEDEKKVIANTVAMAAVKYADLSKHRTTDYVFDW 447
Cdd:pfam00750 314 LQADELEAVADAVGIGAIKYADLSKNRTNDYIFDW 348
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
114-386 |
2.03e-75 |
|
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: 238.62 E-value: 2.03e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 114 TIVADYSAPNVAKEMHVGHLRSTIIGDAVVRTLEFLGHNVIRANHIGDWGTQFGMLIANLERvqaesgevsmeladlegf 193
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSLEK------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 194 yreskklydedeefavkargyvvklqsgdefcaemWKKLVDVTMIQNQRNYDRLNVSltRDDVMGESMYNHMLPTIVADL 273
Cdd:cd00671 63 -----------------------------------WRKLVEESIKADLETYGRLDVR--FDVWFGESSYLGLMGKVVELL 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 274 KEQGLAKEDDGAQVVFLEEYknkdGDPMGVIIQKRDGGFLYTTTDIACAKYRFEElGADRVLYFIDSRQHQHLMQAWTIV 353
Cdd:cd00671 106 EELGLLYEEDGALWLDLTEF----GDDKDRVLVRSDGTYTYFTRDIAYHLDKFER-GADKIIYVVGADHHGHFKRLFAAL 180
|
250 260 270
....*....|....*....|....*....|...
gi 1519401526 354 RKAGYiPESVSLEHHAFGMMLGKDGKPFKTRAG 386
Cdd:cd00671 181 ELLGY-DEAKKLEHLLYGMVNLPKEGKMSTRAG 212
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
462-577 |
1.81e-37 |
|
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: 134.63 E-value: 1.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 462 QYAYTRVASIFAKAGISMDSLEGEIKI-----TEEKEKALIAKLLQFEEAVQSVAREGQPHIMCSYLFELAGQFSSFYEA 536
Cdd:smart00836 2 QYAHARICSILRKAGEAGETLPDIADAdlsllTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYNR 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1519401526 537 CPILVAEDETVKQSRLKLAALTAKTIKQGLSLLGIDTLERM 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: 730.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 1 MNIQALINDKVSQALEA-AGAPAGSPAAVRQSAKPQFGDYQANGVMGVAKRLGTNPREFAQKVLDVLNLDGIASKVEIAG 79
Cdd:COG0018 1 MNIKEELAEAIAAALAAlGAGLEEPDILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDADPLVEKVEIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 80 PGFLNIFLDEAFLAKQADAALAD-SRLGVA-VAETQTIVADYSAPNVAKEMHVGHLRSTIIGDAVVRTLEFLGHNVIRAN 157
Cdd:COG0018 81 PGFINFFLSPAALAAVLKEILADgEDYGRSdAGKGKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYDVTREN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 158 HIGDWGTQFGMLIANLERVQAESGEV-SMELADLEGFYRESKKLYDEDEEFAVKARGYVVKLQSGDEFCAEMWKKLVDVT 236
Cdd:COG0018 161 YINDAGTQIGKLALSLERYGEEEIEPeSKPDGYLGDLYVKFHKEYEEDPELEDIARELLAKLEPGDEEALELWKKAVDWS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 237 MIQNQRNYDRLNVSLtrDDVMGESMYNHM--LPTIVADLKEQGLAKEDDGAQVVFLEEYknkdGDPMGVIIQKRDGGFLY 314
Cdd:COG0018 241 LEEIKEDLKRLGVEF--DVWFSESSLYDSgaVEEVVEELKEKGLLYESDGALWVRLTEF----GDDKDRVLVKSDGTYTY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 315 TTTDIACAKYRFEELGADRVLYFIDSRQHQHLMQAWTIVRKAGYIPESvSLEHHAFGMMLGKDGKPFKTRAGGTVRLADL 394
Cdd:COG0018 315 FTTDIAYHLYKFERYGFDRVIYVVGADQHGHFKRLFAALKALGYDPAK-DLEHLLFGMVNLRDGEKMSTRAGTVVTLDDL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 395 LDEAEVRAAQLIESKNpelaEDEKKVIANTVAMAAVKYADLSKHRTTDYVFDWDNMLAFEGNTAPYMQYAYTRVASIFAK 474
Cdd:COG0018 394 LDEAVERAREIIEEKS----EEEKEEIAEQVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNTNPYVQYAHARICSILRK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 475 AGISMDSLEGE--IKITEEKEKALIAKLLQFEEAVQSVAREGQPHIMCSYLFELAGQFSSFYEACPILVAEDETVKQSRL 552
Cdd:COG0018 470 AGEELDGLAEAdlSLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRILKAEDEELRAARL 549
|
570 580
....*....|....*....|....*
gi 1519401526 553 KLAALTAKTIKQGLSLLGIDTLERM 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: 626.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 3 IQALINDKVSQALEAAGAPAGSPAAVRQSAKPQFGDYQANGVMGVAKRLGTNPREFAQKVLDVLNLDGIASKVEIAGPgF 82
Cdd:TIGR00456 1 IKTLLKEEISQALLKAGLSKESEILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKLKTGEIIEKVEAAGP-F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 83 LNIFLDEAFLAKQ--ADAALADSRLGVAVAETQTIVADYSAPNVAKEMHVGHLRSTIIGDAVVRTLEFLGHNVIRANHIG 160
Cdd:TIGR00456 80 INFFLSPQKLLERliQKILTQKEKYGSKKLKNKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 161 DWGTQFGMLIANLERVQAESG--EVSMELADLEGFYRESKKLYDEDEEFAVKARGYVVKLQSGDEFCAEMWKKLVDVTMI 238
Cdd:TIGR00456 160 DWGRQFGLLALGVEKFGNEALniAVKKPDHGLEGFYVEINKRLEENEELEEEARELFVKLESGDEETIKLWKRLVEYSLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 239 QNQRNYDRLNVSLTRDDVMGESMYNHMLPTIVADLKEQGLAKEdDGAQVVFLEEYKNKdgdpMGVIIQKRDGGFLYTTTD 318
Cdd:TIGR00456 240 GIKETYDRLNIHFDSFVWEGESVKNGMLPKVLEDLKEKGLVVE-DGALWLDLTLFGDK----KDRVLQKSDGTYLYLTTD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 319 IACAKYRFEElGADRVLYFIDSRQHQHLMQAWTIVRKAGYipESVSLEHHAFGMMLGKDgkpFKTRAGGTVRLADLLDEA 398
Cdd:TIGR00456 315 IAYHLDKLER-GFDKMIYVWGSDHHLHIAQMFAILEKLGY--KKKELEHLNFGMVPLYS---MKTRRGNVISLDNLLDEA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 399 EVRAAQLIESKNPELAEDekkvIANTVAMAAVKYADLSKHRTTDYVFDWDNMLAFEGNTAPYMQYAYTRVASIFAKAGIS 478
Cdd:TIGR00456 389 SKRAGNVITIKNDLEEEK----VADAVGIGAVRYFDLSKNRTTDYVFDWDAMLSFEGNTAPYIQYAHARICSILRKAEID 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 479 -MDSLEGEIKITEEKEKALIAKLLQFEEAVQSVAREGQPHIMCSYLFELAGQFSSFYEACPILVAEDEtVKQSRLKLAAL 557
Cdd:TIGR00456 465 gEKLIADDFELLEEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACPVLDAENE-LAAARLALLKA 543
|
570 580
....*....|....*....|
gi 1519401526 558 TAKTIKQGLSLLGIDTLERM 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: 626.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 1 MNIQALINDKVSQALEAAGAPAGSPAAVRQSAKPQFGDYQANGVMGVAKRLGTNPREFAQKVLDVLnldgiaSKVEIAGP 80
Cdd:PRK01611 3 MDIKELLAEALAAALEAGGLPELPAVLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIVEAI------EKVEIAGP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 81 GFLNIFLDEAFLAKQADAAL-ADSRLGV-AVAETQTIVADYSAPNVAKEMHVGHLRSTIIGDAVVRTLEFLGHNVIRANH 158
Cdd:PRK01611 77 GFINFFLDPAALAELVLAILeAGERYGRsDIGKGKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDVTREYY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 159 IGDWGTQFGMLIANLErvqaesgevsmeladlegfyreskklydedeefavkargyvvklqsgdefcaEMWKKLVDVTMI 238
Cdd:PRK01611 157 VNDAGTQIGMLIASLE----------------------------------------------------LLWRKAVDISLD 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 239 QNQRNYDRLNVSLTRDDVMGESMYNHMLPTIVADLKEQGLA-KEDDGAQVVFLEEYknkdGDPMGVIIQKRDGGFLYTTT 317
Cdd:PRK01611 185 EIKEDLDRLGVHFDVWFSESELYYNGKVDEVVEDLKEKGLLyVESDGALWVRLTEF----GDDKDRVLIKSDGTYTYFTR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 318 DIACAKYRFEELgaDRVLYFIDSRQHQHLMQAWTIVRKAGYIPESVS-LEHHAFGMMLGKDGKPFKTRAGGTVRLADLLD 396
Cdd:PRK01611 261 DIAYHLYKFERF--DRVIYVVGADHHGHFKRLKAALKALGYDPDALEvLLHQMVGLVRGGEGVKMSTRAGNVVTLDDLLD 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 397 EAEVRAAQLIEsknpelaedeKKVIANTVAMAAVKYADLSKHRTTDYVFDWDNMLAFEGNTAPYMQYAYTRVASIFAKAG 476
Cdd:PRK01611 339 EAVGRARELIE----------EKEIAEAVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPPYVQYAHARICSILRKAA 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 477 ISMDSLEGEIkITEEKEKALIAKLLQFEEAVQSVAREGQPHIMCSYLFELAGQFSSFYEACPiLVAEDETVKQSRLKLAA 556
Cdd:PRK01611 409 EAGIDLLLAL-LTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYNRVL-LKDEEEELRNARLALVK 486
|
570 580
....*....|....*....|.
gi 1519401526 557 LTAKTIKQGLSLLGIDTLERM 577
Cdd:PRK01611 487 ATAQVLKNGLDLLGISAPERM 507
|
|
| PLN02286 |
PLN02286 |
arginine-tRNA ligase |
28-577 |
0e+00 |
|
arginine-tRNA ligase
Pssm-ID: 215160 [Multi-domain] Cd Length: 576 Bit Score: 573.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 28 VRQSAKPQFGDYQANGVMGVAKRLG------TNPREFAQKVLDVLNLDGIASKVEIAGPGFLNIFLDEAFLAKQADAALA 101
Cdd:PLN02286 25 VAACTNPKFGDYQCNNAMGLWSKLKgkgtsfKNPRAVAQAIVKNLPASEMIESTSVAGPGFVNVRLSASWLAKRIERMLV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 102 DSRLGVAVAET-QTIVADYSAPNVAKEMHVGHLRSTIIGDAVVRTLEFLGHNVIRANHIGDWGTQFGMLIANLERVQAES 180
Cdd:PLN02286 105 DGIDTWAPTLPvKRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEFSGVEVLRRNHVGDWGTQFGMLIEHLFEKFPNW 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 181 GEVS-MELADLEGFYRESKKLYDEDEEFAVKARGYVVKLQSGDEFCAEMWKKLVDVTMIQNQRNYDRLNVSLTRDdvmGE 259
Cdd:PLN02286 185 ESVSdQAIGDLQEFYKAAKKRFDEDEEFKARAQQAVVRLQGGDPEYRAAWAKICEISRREFEKVYQRLRVELEEK---GE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 260 SMYNHMLPTIVADLKEQGLAKEDDGAQVVFLEEYKNkdgdPMgvIIQKRDGGFLYTTTDIACAKYRFEELGADRVLYFID 339
Cdd:PLN02286 262 SFYNPYIPGVIEELESKGLVVESDGARVIFVEGFDI----PL--IVVKSDGGFNYASTDLAALWYRLNEEKAEWIIYVTD 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 340 SRQHQHLMQAWTIVRKAGYIPES--VSLEHHAFGMMLGKDGKPFKTRAGGTVRLADLLDEAEVRA-AQLIESKNP-ELAE 415
Cdd:PLN02286 336 VGQQQHFDMVFKAAKRAGWLPEDtyPRLEHVGFGLVLGEDGKRFRTRSGEVVRLVDLLDEAKSRSkAALIERGKDsEWTP 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 416 DEKKVIANTVAMAAVKYADLSKHRTTDYVFDWDNMLAFEGNTAPYMQYAYTRVASIFAKAGISMDSLE--GEIKITEEKE 493
Cdd:PLN02286 416 EELEQAAEAVGYGAVKYADLKNNRLTNYTFSFDQMLDLKGNTAVYLLYAHARICSIIRKSGKDIDELKktGKIVLDHPDE 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 494 KALIAKLLQFEEAVQSVAREGQPHIMCSYLFELAGQFSSFYEACPILVAEDETvkqSRLKLAALTAKTIKQGLSLLGIDT 573
Cdd:PLN02286 496 RALGLHLLQFPEVVEEACTDLLPNRLCEYLYNLSEKFTKFYSNCKVNGSEEET---SRLLLCEATAIVMRKCFHLLGITP 572
|
....
gi 1519401526 574 LERM 577
Cdd:PLN02286 573 LYRL 576
|
|
| tRNA-synt_1d |
pfam00750 |
tRNA synthetases class I (R); Other tRNA synthetase sub-families are too dissimilar to be ... |
95-447 |
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: 531.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 95 QADAALADSRLGVAVAETQTIVADYSAPNVAKEMHVGHLRSTIIGDAVVRTLEFLGHNVIRANHIGDWGTQFGMLIANLE 174
Cdd:pfam00750 1 TVPNALLQKGLGKASREKKKVVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQFGMLIAGLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 175 RVQAESGEVSMELADLEGFYRESKKLYDEDEEFAVKARGYVVKLQSGDEFCAEMWKKLVDVTMIQNQRNYDRLNVSLTRd 254
Cdd:pfam00750 81 KYQDEKTLQEMPIQDLEDFYREAKKHYDEEEEFAERARNYVVKLQSGDEYWRRMWKLIVDITMTQNQRLYDRLDVTLTE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 255 dvMGESMYNHMLPTIVADLKEQGLAKEDDGAQVVFLEEYknkdGDPMGVIIQKRDGGFLYTTTDIACAKYRFEELGADRV 334
Cdd:pfam00750 160 --MGESLYNPMMNEIVKDFKKNGLVVEIDGALVVFLDEF----GKPMGVIVQKSDGGYLYTTTDIAAAKYRYETLHADRM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 335 LYFIDSRQHQHLMQAWTIVRKAGYIPESVSLEHHAFGMMLGKDGKPFKTRAGGTVRLADLLDEAEVRAAQLIESKNPE-- 412
Cdd:pfam00750 234 LYVIDSRQSQHMQQAFAILRKAGYVPESKDLEHINFGMVLGKDGKPFKTRKGGTVKLADLLDEALERALQLIMEKNKDki 313
|
330 340 350
....*....|....*....|....*....|....*
gi 1519401526 413 LAEDEKKVIANTVAMAAVKYADLSKHRTTDYVFDW 447
Cdd:pfam00750 314 LQADELEAVADAVGIGAIKYADLSKNRTNDYIFDW 348
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
114-386 |
2.03e-75 |
|
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: 238.62 E-value: 2.03e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 114 TIVADYSAPNVAKEMHVGHLRSTIIGDAVVRTLEFLGHNVIRANHIGDWGTQFGMLIANLERvqaesgevsmeladlegf 193
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSLEK------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 194 yreskklydedeefavkargyvvklqsgdefcaemWKKLVDVTMIQNQRNYDRLNVSltRDDVMGESMYNHMLPTIVADL 273
Cdd:cd00671 63 -----------------------------------WRKLVEESIKADLETYGRLDVR--FDVWFGESSYLGLMGKVVELL 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 274 KEQGLAKEDDGAQVVFLEEYknkdGDPMGVIIQKRDGGFLYTTTDIACAKYRFEElGADRVLYFIDSRQHQHLMQAWTIV 353
Cdd:cd00671 106 EELGLLYEEDGALWLDLTEF----GDDKDRVLVRSDGTYTYFTRDIAYHLDKFER-GADKIIYVVGADHHGHFKRLFAAL 180
|
250 260 270
....*....|....*....|....*....|...
gi 1519401526 354 RKAGYiPESVSLEHHAFGMMLGKDGKPFKTRAG 386
Cdd:cd00671 181 ELLGY-DEAKKLEHLLYGMVNLPKEGKMSTRAG 212
|
|
| Anticodon_Ia_Arg |
cd07956 |
Anticodon-binding domain of arginyl tRNA synthetases; This domain is found in arginyl tRNA ... |
425-577 |
1.15e-64 |
|
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: 208.22 E-value: 1.15e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 425 VAMAAVKYADLSKHRTTDYVFDWDNMLAFEGNTAPYMQYAYTRVASIFAKAGISMDSLEGE--IKITEEKEKALIAKLLQ 502
Cdd:cd07956 3 VGVGAVKYQDLSNKRIKDYTFDWERMLSFEGDTGPYLQYAHARLCSILRKAGETIEAEADAdlSLLPEPDERDLILLLAK 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519401526 503 FEEAVQSVAREGQPHIMCSYLFELAGQFSSFYEACPILVAEDEtVKQSRLKLAALTAKTIKQGLSLLGIDTLERM 577
Cdd:cd07956 83 FPEVVKNAAETLEPHTIATYLFDLAHAFSKFYNACPVLGAEEE-LRNARLALVAAARQVLANGLDLLGIEAPERM 156
|
|
| DALR_1 |
pfam05746 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
461-577 |
3.34e-44 |
|
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: 152.80 E-value: 3.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 461 MQYAYTRVASIFAKAGISMDSLE-GEIKITEEKEKALIAKLLQFEEAVQSVAREGQPHIMCSYLFELAGQFSSFYEACPI 539
Cdd:pfam05746 1 LQYAHARICSILRKAGELGINLDiDADLLTEEEEKELLKALLQFPEVLEEAAEELEPHRLANYLYELASAFHSFYNNCRV 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1519401526 540 LVAEDEtVKQSRLKLAALTAKTIKQGLSLLGIDTLERM 577
Cdd:pfam05746 81 LDEDNE-ERNARLALLKAVRQVLKNGLDLLGIEAPEKM 117
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
462-577 |
1.81e-37 |
|
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: 134.63 E-value: 1.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 462 QYAYTRVASIFAKAGISMDSLEGEIKI-----TEEKEKALIAKLLQFEEAVQSVAREGQPHIMCSYLFELAGQFSSFYEA 536
Cdd:smart00836 2 QYAHARICSILRKAGEAGETLPDIADAdlsllTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYNR 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1519401526 537 CPILVAEDETVKQSRLKLAALTAKTIKQGLSLLGIDTLERM 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 |
1.33e-22 |
|
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: 91.88 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 1 MNIQALINDKVSQALEAAGAPAGSPaaVRQSAKPQFGDYQANGVMGVAKRLGTNPREFAQKVLDVLNLDGIASKVEIAGP 80
Cdd:smart01016 1 DLLKEAIAEALKKALGVEGEPIDIA--LERPKDPDHGDYATNVAFRLAKKLKKNPRELAEEIAEKLPKSDLVEKVEIAGP 78
|
....*..
gi 1519401526 81 GFLNIFL 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 ... |
3-87 |
1.81e-19 |
|
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: 83.05 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 3 IQALINDKVSQALEAAGAPAGSPaaVRQSAKPQFGDYQANGVMGVAKRLGTNPREFAQKVLDVLNLDGIASKVEIAGPGF 82
Cdd:pfam03485 1 LKKAIAKALSKLGGPDLELIDIV--IETPKNPKFGDYATNVAMQLAKKLKKNPREIAEEIAEKLEKSDIIEKVEVAGPGF 78
|
....*
gi 1519401526 83 LNIFL 87
Cdd:pfam03485 79 INFFL 83
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
119-167 |
5.16e-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: 52.10 E-value: 5.16e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1519401526 119 YSAPNVAKEMHVGHLRSTIIGDAVVRTLEFLGHNVIRANHIGDWGTQFG 167
Cdd:cd00802 3 FSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIG 51
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
122-200 |
7.86e-04 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 42.15 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519401526 122 PNVAKEMHVGHLRSTIIGDAVVRTLEFLGHNVIRANHIGDWGTQFGMLIANLERVQAESGEVSMELADL-----EGFYRE 196
Cdd:PRK14534 29 PTVYNYAHIGNFRTYIFEDLLIKSLRLLKYNVNYAMNITDIGHLTGDFDDGEDKVVKAARERGLTVYEIsrfftEAFFDD 108
|
....
gi 1519401526 197 SKKL 200
Cdd:PRK14534 109 CKKL 112
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
122-161 |
2.38e-03 |
|
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: 39.48 E-value: 2.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1519401526 122 PNVAKEMHVGHLRSTIIGDAVVRTLEFLGHNVIRANHIGD 161
Cdd:cd00672 28 PTVYDYAHIGHARTYVVFDVLRRYLEDLGYKVRYVQNITD 67
|
|
| |
