|
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: 725.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 1 MNIQSILSDKIKQAMMAAGAD-ESCDALVRQSGKPQFGDYQANGIMAAAKKLNLSPREFAQSVLAHTDLSDIAEKLEIAG 79
Cdd:COG0018 1 MNIKEELAEAIAAALAALGAGlEEPDILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDADPLVEKVEIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 80 PGFINIFLNSNWITEQVSHTLSQ-PNLGIQAEDK-QTVVIDYSSPNVAKEMHVGHLRSTIIGDAVARTLEFLGHKVIRAN 157
Cdd:COG0018 81 PGFINFFLSPAALAAVLKEILADgEDYGRSDAGKgKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYDVTREN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 158 HVGDWGTQFGMLIAYLEKMQNEHT--SEMELQDLETFYREAKKHYDEDEKFAEKARNYVVKLQSGDEYCRAMWKRLVDIT 235
Cdd:COG0018 161 YINDAGTQIGKLALSLERYGEEEIepESKPDGYLGDLYVKFHKEYEEDPELEDIARELLAKLEPGDEEALELWKKAVDWS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 236 MQQNQHNYDRLNVTLteKDVMGESLYNSM--LPGIVEDLKKQGLAVEDDGALVVYLEEFknkeGEAMGVIVQKKDGGFLY 313
Cdd:COG0018 241 LEEIKEDLKRLGVEF--DVWFSESSLYDSgaVEEVVEELKEKGLLYESDGALWVRLTEF----GDDKDRVLVKSDGTYTY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 314 TTTDIAAAKYRYETLKANRALVFSDTRQSQHMQQAWLITRKAGYVPDNfSLEHKNFGMMLGKDGKPFKTRTGGTVKLADL 393
Cdd:COG0018 315 FTTDIAYHLYKFERYGFDRVIYVVGADQHGHFKRLFAALKALGYDPAK-DLEHLLFGMVNLRDGEKMSTRAGTVVTLDDL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 394 LDEAIDRAAILINEKSnnlsDTEKVAVAEAVGIGSVKYADLSKNRTTDYVFDWDNMLSFEGNTAPYMQYAYTRIRSIFNK 473
Cdd:COG0018 394 LDEAVERAREIIEEKS----EEEKEEIAEQVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNTNPYVQYAHARICSILRK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 474 TQVDLTALSTAPL-MLVDEKERSLAIKLLQFEEAVQTVGREGMPHVLCAYLYELAGVFSSFYEHCPILNAEDEKLMLSRL 552
Cdd:COG0018 470 AGEELDGLAEADLsLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRILKAEDEELRAARL 549
|
570 580
....*....|....*....|....*
gi 517167954 553 KLALLTEKTLKQGLDLLGIKTVDKM 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: 688.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 3 IQSILSDKIKQAMMAAGADESCDALVRQSGKPQFGDYQANGIMAAAKKLNLSPREFAQSVLAHTDLSDIAEKLEIAGPgF 82
Cdd:TIGR00456 1 IKTLLKEEISQALLKAGLSKESEILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKLKTGEIIEKVEAAGP-F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 83 INIFLNSNWITEQVSHTLS--QPNLGIQAEDKQTVVIDYSSPNVAKEMHVGHLRSTIIGDAVARTLEFLGHKVIRANHVG 160
Cdd:TIGR00456 80 INFFLSPQKLLERLIQKILtqKEKYGSKKLKNKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 161 DWGTQFGMLIAYLEKMQNEHT---SEMELQDLETFYREAKKHYDEDEKFAEKARNYVVKLQSGDEYCRAMWKRLVDITMQ 237
Cdd:TIGR00456 160 DWGRQFGLLALGVEKFGNEALniaVKKPDHGLEGFYVEINKRLEENEELEEEARELFVKLESGDEETIKLWKRLVEYSLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 238 QNQHNYDRLNVTLTEKDVMGESLYNSMLPGIVEDLKKQGLAVEDdGALVVYLEEFKNKegeaMGVIVQKKDGGFLYTTTD 317
Cdd:TIGR00456 240 GIKETYDRLNIHFDSFVWEGESVKNGMLPKVLEDLKEKGLVVED-GALWLDLTLFGDK----KDRVLQKSDGTYLYLTTD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 318 IAAAKYRYETlKANRALVFSDTRQSQHMQQAWLITRKAGYvpDNFSLEHKNFGMMLGKDgkpFKTRTGGTVKLADLLDEA 397
Cdd:TIGR00456 315 IAYHLDKLER-GFDKMIYVWGSDHHLHIAQMFAILEKLGY--KKKELEHLNFGMVPLYS---MKTRRGNVISLDNLLDEA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 398 IDRAAILINEKsNNLSDTEkvaVAEAVGIGSVKYADLSKNRTTDYVFDWDNMLSFEGNTAPYMQYAYTRIRSIFNKTQVD 477
Cdd:TIGR00456 389 SKRAGNVITIK-NDLEEEK---VADAVGIGAVRYFDLSKNRTTDYVFDWDAMLSFEGNTAPYIQYAHARICSILRKAEID 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 478 LTALSTAPLMLVDEKERSLAIKLLQFEEAVQTVGREGMPHVLCAYLYELAGVFSSFYEHCPILNAEDEKLMlSRLKLALL 557
Cdd:TIGR00456 465 GEKLIADDFELLEEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACPVLDAENELAA-ARLALLKA 543
|
570 580
....*....|....*....|
gi 517167954 558 TEKTLKQGLDLLGIKTVDKM 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: 618.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 1 MNIQSILSDKIKQAMMAAGADESCDALVRQSGKPQFGDYQANGIMAAAKKLNLSPREFAQSVLAHtdlsdiAEKLEIAGP 80
Cdd:PRK01611 3 MDIKELLAEALAAALEAGGLPELPAVLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIVEA------IEKVEIAGP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 81 GFINIFLNSNWITEQVSHTLSQ-PNLGIQAEDK-QTVVIDYSSPNVAKEMHVGHLRSTIIGDAVARTLEFLGHKVIRANH 158
Cdd:PRK01611 77 GFINFFLDPAALAELVLAILEAgERYGRSDIGKgKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDVTREYY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 159 VGDWGTQFGMLIAYLEKMqnehtsemelqdletfyreakkhydedekfaekarnyvvklqsgdeycramWKRLVDITMQQ 238
Cdd:PRK01611 157 VNDAGTQIGMLIASLELL---------------------------------------------------WRKAVDISLDE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 239 NQHNYDRLNVTLTEKDVMGESLYNSMLPGIVEDLKKQGLAV-EDDGALVVYLEEFknkeGEAMGVIVQKKDGGFLYTTTD 317
Cdd:PRK01611 186 IKEDLDRLGVHFDVWFSESELYYNGKVDEVVEDLKEKGLLYvESDGALWVRLTEF----GDDKDRVLIKSDGTYTYFTRD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 318 IAAAKYRYETLkaNRALVFSDTRQSQHMQQAWLITRKAGYVPDNFS-LEHKNFGMMLGKDGKPFKTRTGGTVKLADLLDE 396
Cdd:PRK01611 262 IAYHLYKFERF--DRVIYVVGADHHGHFKRLKAALKALGYDPDALEvLLHQMVGLVRGGEGVKMSTRAGNVVTLDDLLDE 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 397 AIDRAAILINEKsnnlsdtekvAVAEAVGIGSVKYADLSKNRTTDYVFDWDNMLSFEGNTAPYMQYAYTRIRSIFNKTQV 476
Cdd:PRK01611 340 AVGRARELIEEK----------EIAEAVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPPYVQYAHARICSILRKAAE 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 477 DltALSTAPLMLVDEKERSLAIKLLQFEEAVQTVGREGMPHVLCAYLYELAGVFSSFYEHCPiLNAEDEKLMLSRLKLAL 556
Cdd:PRK01611 410 A--GIDLLLALLTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYNRVL-LKDEEEELRNARLALVK 486
|
570 580
....*....|....*....|.
gi 517167954 557 LTEKTLKQGLDLLGIKTVDKM 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: 577.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 95 QVSHTLSQPNLGIQAEDKQTVVIDYSSPNVAKEMHVGHLRSTIIGDAVARTLEFLGHKVIRANHVGDWGTQFGMLIAYLE 174
Cdd:pfam00750 1 TVPNALLQKGLGKASREKKKVVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQFGMLIAGLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 175 KMQNEHTS-EMELQDLETFYREAKKHYDEDEKFAEKARNYVVKLQSGDEYCRAMWKRLVDITMQQNQHNYDRLNVTLTEk 253
Cdd:pfam00750 81 KYQDEKTLqEMPIQDLEDFYREAKKHYDEEEEFAERARNYVVKLQSGDEYWRRMWKLIVDITMTQNQRLYDRLDVTLTE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 254 dvMGESLYNSMLPGIVEDLKKQGLAVEDDGALVVYLEEFknkeGEAMGVIVQKKDGGFLYTTTDIAAAKYRYETLKANRA 333
Cdd:pfam00750 160 --MGESLYNPMMNEIVKDFKKNGLVVEIDGALVVFLDEF----GKPMGVIVQKSDGGYLYTTTDIAAAKYRYETLHADRM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 334 LVFSDTRQSQHMQQAWLITRKAGYVPDNFSLEHKNFGMMLGKDGKPFKTRTGGTVKLADLLDEAIDRAAILINEKSNN-- 411
Cdd:pfam00750 234 LYVIDSRQSQHMQQAFAILRKAGYVPESKDLEHINFGMVLGKDGKPFKTRKGGTVKLADLLDEALERALQLIMEKNKDki 313
|
330 340 350
....*....|....*....|....*....|....*
gi 517167954 412 LSDTEKVAVAEAVGIGSVKYADLSKNRTTDYVFDW 446
Cdd:pfam00750 314 LQADELEAVADAVGIGAIKYADLSKNRTNDYIFDW 348
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
114-385 |
1.92e-69 |
|
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: 222.82 E-value: 1.92e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 114 TVVIDYSSPNVAKEMHVGHLRSTIIGDAVARTLEFLGHKVIRANHVGDWGTQFGMLIAYLEKmqnehtsemelqdletfy 193
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSLEK------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 194 reakkhydedekfaekarnyvvklqsgdeycramWKRLVDITMQQNQHNYDRLNVtltEKDV-MGESLYNSMLPGIVEDL 272
Cdd:cd00671 63 ----------------------------------WRKLVEESIKADLETYGRLDV---RFDVwFGESSYLGLMGKVVELL 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 273 KKQGLAVEDDGALVVYLEEFknkeGEAMGVIVQKKDGGFLYTTTDIAAAKYRYEtLKANRALVFSDTRQSQHMQQAWLIT 352
Cdd:cd00671 106 EELGLLYEEDGALWLDLTEF----GDDKDRVLVRSDGTYTYFTRDIAYHLDKFE-RGADKIIYVVGADHHGHFKRLFAAL 180
|
250 260 270
....*....|....*....|....*....|...
gi 517167954 353 RKAGYVPDNfSLEHKNFGMMLGKDGKPFKTRTG 385
Cdd:cd00671 181 ELLGYDEAK-KLEHLLYGMVNLPKEGKMSTRAG 212
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
461-577 |
2.17e-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: 126.15 E-value: 2.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 461 QYAYTRIRSIFNK---TQVDLTALSTAPL-MLVDEKERSLAIKLLQFEEAVQTVGREGMPHVLCAYLYELAGVFSSFYEH 536
Cdd:smart00836 2 QYAHARICSILRKageAGETLPDIADADLsLLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYNR 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 517167954 537 CPILNAEDEKLMLSRLKLALLTEKTLKQGLDLLGIKTVDKM 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: 725.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 1 MNIQSILSDKIKQAMMAAGAD-ESCDALVRQSGKPQFGDYQANGIMAAAKKLNLSPREFAQSVLAHTDLSDIAEKLEIAG 79
Cdd:COG0018 1 MNIKEELAEAIAAALAALGAGlEEPDILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDADPLVEKVEIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 80 PGFINIFLNSNWITEQVSHTLSQ-PNLGIQAEDK-QTVVIDYSSPNVAKEMHVGHLRSTIIGDAVARTLEFLGHKVIRAN 157
Cdd:COG0018 81 PGFINFFLSPAALAAVLKEILADgEDYGRSDAGKgKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYDVTREN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 158 HVGDWGTQFGMLIAYLEKMQNEHT--SEMELQDLETFYREAKKHYDEDEKFAEKARNYVVKLQSGDEYCRAMWKRLVDIT 235
Cdd:COG0018 161 YINDAGTQIGKLALSLERYGEEEIepESKPDGYLGDLYVKFHKEYEEDPELEDIARELLAKLEPGDEEALELWKKAVDWS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 236 MQQNQHNYDRLNVTLteKDVMGESLYNSM--LPGIVEDLKKQGLAVEDDGALVVYLEEFknkeGEAMGVIVQKKDGGFLY 313
Cdd:COG0018 241 LEEIKEDLKRLGVEF--DVWFSESSLYDSgaVEEVVEELKEKGLLYESDGALWVRLTEF----GDDKDRVLVKSDGTYTY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 314 TTTDIAAAKYRYETLKANRALVFSDTRQSQHMQQAWLITRKAGYVPDNfSLEHKNFGMMLGKDGKPFKTRTGGTVKLADL 393
Cdd:COG0018 315 FTTDIAYHLYKFERYGFDRVIYVVGADQHGHFKRLFAALKALGYDPAK-DLEHLLFGMVNLRDGEKMSTRAGTVVTLDDL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 394 LDEAIDRAAILINEKSnnlsDTEKVAVAEAVGIGSVKYADLSKNRTTDYVFDWDNMLSFEGNTAPYMQYAYTRIRSIFNK 473
Cdd:COG0018 394 LDEAVERAREIIEEKS----EEEKEEIAEQVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNTNPYVQYAHARICSILRK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 474 TQVDLTALSTAPL-MLVDEKERSLAIKLLQFEEAVQTVGREGMPHVLCAYLYELAGVFSSFYEHCPILNAEDEKLMLSRL 552
Cdd:COG0018 470 AGEELDGLAEADLsLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRILKAEDEELRAARL 549
|
570 580
....*....|....*....|....*
gi 517167954 553 KLALLTEKTLKQGLDLLGIKTVDKM 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: 688.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 3 IQSILSDKIKQAMMAAGADESCDALVRQSGKPQFGDYQANGIMAAAKKLNLSPREFAQSVLAHTDLSDIAEKLEIAGPgF 82
Cdd:TIGR00456 1 IKTLLKEEISQALLKAGLSKESEILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKLKTGEIIEKVEAAGP-F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 83 INIFLNSNWITEQVSHTLS--QPNLGIQAEDKQTVVIDYSSPNVAKEMHVGHLRSTIIGDAVARTLEFLGHKVIRANHVG 160
Cdd:TIGR00456 80 INFFLSPQKLLERLIQKILtqKEKYGSKKLKNKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 161 DWGTQFGMLIAYLEKMQNEHT---SEMELQDLETFYREAKKHYDEDEKFAEKARNYVVKLQSGDEYCRAMWKRLVDITMQ 237
Cdd:TIGR00456 160 DWGRQFGLLALGVEKFGNEALniaVKKPDHGLEGFYVEINKRLEENEELEEEARELFVKLESGDEETIKLWKRLVEYSLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 238 QNQHNYDRLNVTLTEKDVMGESLYNSMLPGIVEDLKKQGLAVEDdGALVVYLEEFKNKegeaMGVIVQKKDGGFLYTTTD 317
Cdd:TIGR00456 240 GIKETYDRLNIHFDSFVWEGESVKNGMLPKVLEDLKEKGLVVED-GALWLDLTLFGDK----KDRVLQKSDGTYLYLTTD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 318 IAAAKYRYETlKANRALVFSDTRQSQHMQQAWLITRKAGYvpDNFSLEHKNFGMMLGKDgkpFKTRTGGTVKLADLLDEA 397
Cdd:TIGR00456 315 IAYHLDKLER-GFDKMIYVWGSDHHLHIAQMFAILEKLGY--KKKELEHLNFGMVPLYS---MKTRRGNVISLDNLLDEA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 398 IDRAAILINEKsNNLSDTEkvaVAEAVGIGSVKYADLSKNRTTDYVFDWDNMLSFEGNTAPYMQYAYTRIRSIFNKTQVD 477
Cdd:TIGR00456 389 SKRAGNVITIK-NDLEEEK---VADAVGIGAVRYFDLSKNRTTDYVFDWDAMLSFEGNTAPYIQYAHARICSILRKAEID 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 478 LTALSTAPLMLVDEKERSLAIKLLQFEEAVQTVGREGMPHVLCAYLYELAGVFSSFYEHCPILNAEDEKLMlSRLKLALL 557
Cdd:TIGR00456 465 GEKLIADDFELLEEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACPVLDAENELAA-ARLALLKA 543
|
570 580
....*....|....*....|
gi 517167954 558 TEKTLKQGLDLLGIKTVDKM 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: 618.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 1 MNIQSILSDKIKQAMMAAGADESCDALVRQSGKPQFGDYQANGIMAAAKKLNLSPREFAQSVLAHtdlsdiAEKLEIAGP 80
Cdd:PRK01611 3 MDIKELLAEALAAALEAGGLPELPAVLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIVEA------IEKVEIAGP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 81 GFINIFLNSNWITEQVSHTLSQ-PNLGIQAEDK-QTVVIDYSSPNVAKEMHVGHLRSTIIGDAVARTLEFLGHKVIRANH 158
Cdd:PRK01611 77 GFINFFLDPAALAELVLAILEAgERYGRSDIGKgKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDVTREYY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 159 VGDWGTQFGMLIAYLEKMqnehtsemelqdletfyreakkhydedekfaekarnyvvklqsgdeycramWKRLVDITMQQ 238
Cdd:PRK01611 157 VNDAGTQIGMLIASLELL---------------------------------------------------WRKAVDISLDE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 239 NQHNYDRLNVTLTEKDVMGESLYNSMLPGIVEDLKKQGLAV-EDDGALVVYLEEFknkeGEAMGVIVQKKDGGFLYTTTD 317
Cdd:PRK01611 186 IKEDLDRLGVHFDVWFSESELYYNGKVDEVVEDLKEKGLLYvESDGALWVRLTEF----GDDKDRVLIKSDGTYTYFTRD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 318 IAAAKYRYETLkaNRALVFSDTRQSQHMQQAWLITRKAGYVPDNFS-LEHKNFGMMLGKDGKPFKTRTGGTVKLADLLDE 396
Cdd:PRK01611 262 IAYHLYKFERF--DRVIYVVGADHHGHFKRLKAALKALGYDPDALEvLLHQMVGLVRGGEGVKMSTRAGNVVTLDDLLDE 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 397 AIDRAAILINEKsnnlsdtekvAVAEAVGIGSVKYADLSKNRTTDYVFDWDNMLSFEGNTAPYMQYAYTRIRSIFNKTQV 476
Cdd:PRK01611 340 AVGRARELIEEK----------EIAEAVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPPYVQYAHARICSILRKAAE 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 477 DltALSTAPLMLVDEKERSLAIKLLQFEEAVQTVGREGMPHVLCAYLYELAGVFSSFYEHCPiLNAEDEKLMLSRLKLAL 556
Cdd:PRK01611 410 A--GIDLLLALLTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYNRVL-LKDEEEELRNARLALVK 486
|
570 580
....*....|....*....|.
gi 517167954 557 LTEKTLKQGLDLLGIKTVDKM 577
Cdd:PRK01611 487 ATAQVLKNGLDLLGISAPERM 507
|
|
| PLN02286 |
PLN02286 |
arginine-tRNA ligase |
7-577 |
0e+00 |
|
arginine-tRNA ligase
Pssm-ID: 215160 [Multi-domain] Cd Length: 576 Bit Score: 611.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 7 LSDKIKQAMMAAGADE-SCDALVRQSGKPQFGDYQANGIMAAAKKLN------LSPREFAQSVLAHTDLSDIAEKLEIAG 79
Cdd:PLN02286 3 LAKLFEASLRLTVPDEpSVEPLVAACTNPKFGDYQCNNAMGLWSKLKgkgtsfKNPRAVAQAIVKNLPASEMIESTSVAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 80 PGFINIFLNSNWITEQVSHTLsqpnlgIQAED-------KQTVVIDYSSPNVAKEMHVGHLRSTIIGDAVARTLEFLGHK 152
Cdd:PLN02286 83 PGFVNVRLSASWLAKRIERML------VDGIDtwaptlpVKRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEFSGVE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 153 VIRANHVGDWGTQFGMLIAYLEKM--QNEHTSEMELQDLETFYREAKKHYDEDEKFAEKARNYVVKLQSGDEYCRAMWKR 230
Cdd:PLN02286 157 VLRRNHVGDWGTQFGMLIEHLFEKfpNWESVSDQAIGDLQEFYKAAKKRFDEDEEFKARAQQAVVRLQGGDPEYRAAWAK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 231 LVDITMQQNQHNYDRLNVTLTEKdvmGESLYNSMLPGIVEDLKKQGLAVEDDGALVVYLEEFKNKegeamgVIVQKKDGG 310
Cdd:PLN02286 237 ICEISRREFEKVYQRLRVELEEK---GESFYNPYIPGVIEELESKGLVVESDGARVIFVEGFDIP------LIVVKSDGG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 311 FLYTTTDIAAAKYRYETLKANRALVFSDTRQSQHMQQAWLITRKAGYVPDNF--SLEHKNFGMMLGKDGKPFKTRTGGTV 388
Cdd:PLN02286 308 FNYASTDLAALWYRLNEEKAEWIIYVTDVGQQQHFDMVFKAAKRAGWLPEDTypRLEHVGFGLVLGEDGKRFRTRSGEVV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 389 KLADLLDEAIDRAAILINEKSN--NLSDTEKVAVAEAVGIGSVKYADLSKNRTTDYVFDWDNMLSFEGNTAPYMQYAYTR 466
Cdd:PLN02286 388 RLVDLLDEAKSRSKAALIERGKdsEWTPEELEQAAEAVGYGAVKYADLKNNRLTNYTFSFDQMLDLKGNTAVYLLYAHAR 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 467 IRSIFNKTQVDLTAL-STAPLMLVDEKERSLAIKLLQFEEAVQTVGREGMPHVLCAYLYELAGVFSSFYEHCPILNAEDE 545
Cdd:PLN02286 468 ICSIIRKSGKDIDELkKTGKIVLDHPDERALGLHLLQFPEVVEEACTDLLPNRLCEYLYNLSEKFTKFYSNCKVNGSEEE 547
|
570 580 590
....*....|....*....|....*....|..
gi 517167954 546 KlmlSRLKLALLTEKTLKQGLDLLGIKTVDKM 577
Cdd:PLN02286 548 T---SRLLLCEATAIVMRKCFHLLGITPLYRL 576
|
|
| 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: 577.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 95 QVSHTLSQPNLGIQAEDKQTVVIDYSSPNVAKEMHVGHLRSTIIGDAVARTLEFLGHKVIRANHVGDWGTQFGMLIAYLE 174
Cdd:pfam00750 1 TVPNALLQKGLGKASREKKKVVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQFGMLIAGLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 175 KMQNEHTS-EMELQDLETFYREAKKHYDEDEKFAEKARNYVVKLQSGDEYCRAMWKRLVDITMQQNQHNYDRLNVTLTEk 253
Cdd:pfam00750 81 KYQDEKTLqEMPIQDLEDFYREAKKHYDEEEEFAERARNYVVKLQSGDEYWRRMWKLIVDITMTQNQRLYDRLDVTLTE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 254 dvMGESLYNSMLPGIVEDLKKQGLAVEDDGALVVYLEEFknkeGEAMGVIVQKKDGGFLYTTTDIAAAKYRYETLKANRA 333
Cdd:pfam00750 160 --MGESLYNPMMNEIVKDFKKNGLVVEIDGALVVFLDEF----GKPMGVIVQKSDGGYLYTTTDIAAAKYRYETLHADRM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 334 LVFSDTRQSQHMQQAWLITRKAGYVPDNFSLEHKNFGMMLGKDGKPFKTRTGGTVKLADLLDEAIDRAAILINEKSNN-- 411
Cdd:pfam00750 234 LYVIDSRQSQHMQQAFAILRKAGYVPESKDLEHINFGMVLGKDGKPFKTRKGGTVKLADLLDEALERALQLIMEKNKDki 313
|
330 340 350
....*....|....*....|....*....|....*
gi 517167954 412 LSDTEKVAVAEAVGIGSVKYADLSKNRTTDYVFDW 446
Cdd:pfam00750 314 LQADELEAVADAVGIGAIKYADLSKNRTNDYIFDW 348
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
114-385 |
1.92e-69 |
|
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: 222.82 E-value: 1.92e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 114 TVVIDYSSPNVAKEMHVGHLRSTIIGDAVARTLEFLGHKVIRANHVGDWGTQFGMLIAYLEKmqnehtsemelqdletfy 193
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSLEK------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 194 reakkhydedekfaekarnyvvklqsgdeycramWKRLVDITMQQNQHNYDRLNVtltEKDV-MGESLYNSMLPGIVEDL 272
Cdd:cd00671 63 ----------------------------------WRKLVEESIKADLETYGRLDV---RFDVwFGESSYLGLMGKVVELL 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 273 KKQGLAVEDDGALVVYLEEFknkeGEAMGVIVQKKDGGFLYTTTDIAAAKYRYEtLKANRALVFSDTRQSQHMQQAWLIT 352
Cdd:cd00671 106 EELGLLYEEDGALWLDLTEF----GDDKDRVLVRSDGTYTYFTRDIAYHLDKFE-RGADKIIYVVGADHHGHFKRLFAAL 180
|
250 260 270
....*....|....*....|....*....|...
gi 517167954 353 RKAGYVPDNfSLEHKNFGMMLGKDGKPFKTRTG 385
Cdd:cd00671 181 ELLGYDEAK-KLEHLLYGMVNLPKEGKMSTRAG 212
|
|
| Anticodon_Ia_Arg |
cd07956 |
Anticodon-binding domain of arginyl tRNA synthetases; This domain is found in arginyl tRNA ... |
422-577 |
1.90e-65 |
|
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: 210.53 E-value: 1.90e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 422 EAVGIGSVKYADLSKNRTTDYVFDWDNMLSFEGNTAPYMQYAYTRIRSIFNKTQVDLTALSTAPLM-LVDEKERSLAIKL 500
Cdd:cd07956 1 EEVGVGAVKYQDLSNKRIKDYTFDWERMLSFEGDTGPYLQYAHARLCSILRKAGETIEAEADADLSlLPEPDERDLILLL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517167954 501 LQFEEAVQTVGREGMPHVLCAYLYELAGVFSSFYEHCPILNAEDEkLMLSRLKLALLTEKTLKQGLDLLGIKTVDKM 577
Cdd:cd07956 81 AKFPEVVKNAAETLEPHTIATYLFDLAHAFSKFYNACPVLGAEEE-LRNARLALVAAARQVLANGLDLLGIEAPERM 156
|
|
| DALR_1 |
pfam05746 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
460-577 |
6.12e-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: 152.03 E-value: 6.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 460 MQYAYTRIRSIFNKTQVDLTALSTAPLMLVDEKERSLAIKLLQFEEAVQTVGREGMPHVLCAYLYELAGVFSSFYEHCPI 539
Cdd:pfam05746 1 LQYAHARICSILRKAGELGINLDIDADLLTEEEEKELLKALLQFPEVLEEAAEELEPHRLANYLYELASAFHSFYNNCRV 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 517167954 540 LNAEDEKLMlSRLKLALLTEKTLKQGLDLLGIKTVDKM 577
Cdd:pfam05746 81 LDEDNEERN-ARLALLKAVRQVLKNGLDLLGIEAPEKM 117
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
461-577 |
2.17e-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: 126.15 E-value: 2.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 461 QYAYTRIRSIFNK---TQVDLTALSTAPL-MLVDEKERSLAIKLLQFEEAVQTVGREGMPHVLCAYLYELAGVFSSFYEH 536
Cdd:smart00836 2 QYAHARICSILRKageAGETLPDIADADLsLLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYNR 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 517167954 537 CPILNAEDEKLMLSRLKLALLTEKTLKQGLDLLGIKTVDKM 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 |
1.17e-23 |
|
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: 94.96 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 1 MNIQSILSDKIKQAMMAAGADEscDALVRQSGKPQFGDYQANGIMAAAKKLNLSPREFAQSVLAHTDLSDIAEKLEIAGP 80
Cdd:smart01016 1 DLLKEAIAEALKKALGVEGEPI--DIALERPKDPDHGDYATNVAFRLAKKLKKNPRELAEEIAEKLPKSDLVEKVEIAGP 78
|
....*..
gi 517167954 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 ... |
3-87 |
4.87e-20 |
|
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: 84.59 E-value: 4.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517167954 3 IQSILSDKIKQAmmAAGADESCDALVRQSGKPQFGDYQANGIMAAAKKLNLSPREFAQSVLAHTDLSDIAEKLEIAGPGF 82
Cdd:pfam03485 1 LKKAIAKALSKL--GGPDLELIDIVIETPKNPKFGDYATNVAMQLAKKLKKNPREIAEEIAEKLEKSDIIEKVEVAGPGF 78
|
....*
gi 517167954 83 INIFL 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 ... |
119-179 |
2.93e-10 |
|
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: 58.65 E-value: 2.93e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517167954 119 YSSPNVAKEMHVGHLRSTIIGDAVARTLEFLGHKVIRANHVGDWGTQFG------------MLIAYLEKMQNE 179
Cdd:cd00802 3 FSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGdpankkgenakaFVERWIERIKED 75
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
122-153 |
3.89e-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: 39.10 E-value: 3.89e-03
10 20 30
....*....|....*....|....*....|..
gi 517167954 122 PNVAKEMHVGHLRSTIIGDAVARTLEFLGHKV 153
Cdd:cd00672 28 PTVYDYAHIGHARTYVVFDVLRRYLEDLGYKV 59
|
|
| |
