|
Name |
Accession |
Description |
Interval |
E-value |
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
1-576 |
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: 759.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 1 MNIQVLLSDKVSQALIAAGA-PADCEAQVRPSAKAQFGDYQANGVMSVAKKLGMPPRQLAEKVVQLLDLGDVASKVEIAG 79
Cdd:COG0018 1 MNIKEELAEAIAAALAALGAgLEEPDILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDADPLVEKVEIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 80 PGFINIFLNSDWVARQADQVLNA-PKLGIAPV-EPQTIVIDYSAPNVAKEMHVGHLRSTIIGDAAARTQEFLGHKVIRAN 157
Cdd:COG0018 81 PGFINFFLSPAALAAVLKEILADgEDYGRSDAgKGKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYDVTREN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 158 HVGDWGTQFGMLIAYLEKMQNENA--SDMGLSDLEQFYREAKKHYDEDAEFAERARAYVVKLQGGDQYCLKMWRKLVDIT 235
Cdd:COG0018 161 YINDAGTQIGKLALSLERYGEEEIepESKPDGYLGDLYVKFHKEYEEDPELEDIARELLAKLEPGDEEALELWKKAVDWS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 236 MAQNQLTYNRLNVTLteDDVMGESLYNAM--LPGIVADLKAKGLAVESEGATVVFLDEYqnkdGDPMGVIIQKKDGGYLY 313
Cdd:COG0018 241 LEEIKEDLKRLGVEF--DVWFSESSLYDSgaVEEVVEELKEKGLLYESDGALWVRLTEF----GDDKDRVLVKSDGTYTY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 314 TTTDIACAKYRYETLGANRVLYYIDSRQHQHLMQAWTIVRKAGYVPESvSLEHHMFGMMLGKDGKPFKTRSGGTVKLSDL 393
Cdd:COG0018 315 FTTDIAYHLYKFERYGFDRVIYVVGADQHGHFKRLFAALKALGYDPAK-DLEHLLFGMVNLRDGEKMSTRAGTVVTLDDL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 394 LDEAIERAEQLIAGKNpdmpEDEMKTIARVVGIGAVKYADLSKSRTTDYVFDWDNMLAFEGNTAPYMQYAYTRVASVFKR 473
Cdd:COG0018 394 LDEAVERAREIIEEKS----EEEKEEIAEQVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNTNPYVQYAHARICSILRK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 474 AGIDESSLTL--PLILTEEREIALATRLLQFEEVLTAVAREGTPHVMCSYLYDLAGLFSGFYEHCQILNADSEEARQSRL 551
Cdd:COG0018 470 AGEELDGLAEadLSLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRILKAEDEELRAARL 549
|
570 580
....*....|....*....|....*
gi 727180893 552 KLALLTAKTLKTGLDTLGIETVERM 576
Cdd:COG0018 550 ALVAATAQVLKNGLGLLGISAPERM 574
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
3-576 |
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: 666.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 3 IQVLLSDKVSQALIAAGAPADCEAQVRPSAKAQFGDYQANGVMSVAKKLGMPPRQLAEKVVQLLDLGDVASKVEIAGPgF 82
Cdd:TIGR00456 1 IKTLLKEEISQALLKAGLSKESEILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKLKTGEIIEKVEAAGP-F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 83 INIFLNSDWVARQADQVLNAPK--LGIAPVEPQTIVIDYSAPNVAKEMHVGHLRSTIIGDAAARTQEFLGHKVIRANHVG 160
Cdd:TIGR00456 80 INFFLSPQKLLERLIQKILTQKekYGSKKLKNKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 161 DWGTQFGMLIAYLEKMQNE---NASDMGLSDLEQFYREAKKHYDEDAEFAERARAYVVKLQGGDQYCLKMWRKLVDITMA 237
Cdd:TIGR00456 160 DWGRQFGLLALGVEKFGNEalnIAVKKPDHGLEGFYVEINKRLEENEELEEEARELFVKLESGDEETIKLWKRLVEYSLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 238 QNQLTYNRLNVTLTEDDVMGESLYNAMLPGIVADLKAKGLAVEsEGATVVFLDEYQNKdgdpMGVIIQKKDGGYLYTTTD 317
Cdd:TIGR00456 240 GIKETYDRLNIHFDSFVWEGESVKNGMLPKVLEDLKEKGLVVE-DGALWLDLTLFGDK----KDRVLQKSDGTYLYLTTD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 318 IACAKYRYETlGANRVLYYIDSRQHQHLMQAWTIVRKAGYvpESVSLEHHMFGMMLGKDgkpFKTRSGGTVKLSDLLDEA 397
Cdd:TIGR00456 315 IAYHLDKLER-GFDKMIYVWGSDHHLHIAQMFAILEKLGY--KKKELEHLNFGMVPLYS---MKTRRGNVISLDNLLDEA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 398 IERAEQLIAgKNPDMPEDEMktiARVVGIGAVKYADLSKSRTTDYVFDWDNMLAFEGNTAPYMQYAYTRVASVFKRAGID 477
Cdd:TIGR00456 389 SKRAGNVIT-IKNDLEEEKV---ADAVGIGAVRYFDLSKNRTTDYVFDWDAMLSFEGNTAPYIQYAHARICSILRKAEID 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 478 -ESSLTLPLILTEEREIALATRLLQFEEVLTAVAREGTPHVMCSYLYDLAGLFSGFYEHCQILNADsEEARQSRLKLALL 556
Cdd:TIGR00456 465 gEKLIADDFELLEEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACPVLDAE-NELAAARLALLKA 543
|
570 580
....*....|....*....|
gi 727180893 557 TAKTLKTGLDTLGIETVERM 576
Cdd:TIGR00456 544 TRQTLKNGLDLLGIEPPERM 563
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
1-576 |
0e+00 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 655.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 1 MNIQVLLSDKVSQALIAAGAPADCEAQVRPSAKAQFGDYQANGVMSVAKKLGMPPRQLAEKVVQLLdlgdvaSKVEIAGP 80
Cdd:PRK01611 3 MDIKELLAEALAAALEAGGLPELPAVLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIVEAI------EKVEIAGP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 81 GFINIFLNSDWVARQADQVLNA-PKLGIAPV-EPQTIVIDYSAPNVAKEMHVGHLRSTIIGDAAARTQEFLGHKVIRANH 158
Cdd:PRK01611 77 GFINFFLDPAALAELVLAILEAgERYGRSDIgKGKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDVTREYY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 159 VGDWGTQFGMLIAYLEKMqnenasdmglsdleqfyreakkhydedaefaerarayvvklqggdqyclkmWRKLVDITMAQ 238
Cdd:PRK01611 157 VNDAGTQIGMLIASLELL---------------------------------------------------WRKAVDISLDE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 239 NQLTYNRLNVTLTEDDVMGESLYNAMLPGIVADLKAKGLAV-ESEGATVVFLDEYqnkdGDPMGVIIQKKDGGYLYTTTD 317
Cdd:PRK01611 186 IKEDLDRLGVHFDVWFSESELYYNGKVDEVVEDLKEKGLLYvESDGALWVRLTEF----GDDKDRVLIKSDGTYTYFTRD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 318 IACAKYRYETLgaNRVLYYIDSRQHQHLMQAWTIVRKAGYVPESVS-LEHHMFGMMLGKDGKPFKTRSGGTVKLSDLLDE 396
Cdd:PRK01611 262 IAYHLYKFERF--DRVIYVVGADHHGHFKRLKAALKALGYDPDALEvLLHQMVGLVRGGEGVKMSTRAGNVVTLDDLLDE 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 397 AIERAEQLIAGKNpdmpedemktIARVVGIGAVKYADLSKSRTTDYVFDWDNMLAFEGNTAPYMQYAYTRVASVFKRAGI 476
Cdd:PRK01611 340 AVGRARELIEEKE----------IAEAVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPPYVQYAHARICSILRKAAE 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 477 DESSLTLPLiLTEEREIALATRLLQFEEVLTAVAREGTPHVMCSYLYDLAGLFSGFYEHCqILNADSEEARQSRLKLALL 556
Cdd:PRK01611 410 AGIDLLLAL-LTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYNRV-LLKDEEEELRNARLALVKA 487
|
570 580
....*....|....*....|
gi 727180893 557 TAKTLKTGLDTLGIETVERM 576
Cdd:PRK01611 488 TAQVLKNGLDLLGISAPERM 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: 554.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 95 QADQVLNAPKLGIAPVEPQTIVIDYSAPNVAKEMHVGHLRSTIIGDAAARTQEFLGHKVIRANHVGDWGTQFGMLIAYLE 174
Cdd:pfam00750 1 TVPNALLQKGLGKASREKKKVVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQFGMLIAGLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 175 KMQNENAS-DMGLSDLEQFYREAKKHYDEDAEFAERARAYVVKLQGGDQYCLKMWRKLVDITMAQNQLTYNRLNVTLTEd 253
Cdd:pfam00750 81 KYQDEKTLqEMPIQDLEDFYREAKKHYDEEEEFAERARNYVVKLQSGDEYWRRMWKLIVDITMTQNQRLYDRLDVTLTE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 254 dvMGESLYNAMLPGIVADLKAKGLAVESEGATVVFLDEYqnkdGDPMGVIIQKKDGGYLYTTTDIACAKYRYETLGANRV 333
Cdd:pfam00750 160 --MGESLYNPMMNEIVKDFKKNGLVVEIDGALVVFLDEF----GKPMGVIVQKSDGGYLYTTTDIAAAKYRYETLHADRM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 334 LYYIDSRQHQHLMQAWTIVRKAGYVPESVSLEHHMFGMMLGKDGKPFKTRSGGTVKLSDLLDEAIERAEQLIAGKNPD-- 411
Cdd:pfam00750 234 LYVIDSRQSQHMQQAFAILRKAGYVPESKDLEHINFGMVLGKDGKPFKTRKGGTVKLADLLDEALERALQLIMEKNKDki 313
|
330 340 350
....*....|....*....|....*....|....*
gi 727180893 412 MPEDEMKTIARVVGIGAVKYADLSKSRTTDYVFDW 446
Cdd:pfam00750 314 LQADELEAVADAVGIGAIKYADLSKNRTNDYIFDW 348
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
114-385 |
7.51e-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: 7.51e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 114 TIVIDYSAPNVAKEMHVGHLRSTIIGDAAARTQEFLGHKVIRANHVGDWGTQFGMLIAYLEKmqnenasdmglsdleqfy 193
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSLEK------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 194 reakkhydedaefaerarayvvklqggdqyclkmWRKLVDITMAQNQLTYNRLNVTLteDDVMGESLYNAMLPGIVADLK 273
Cdd:cd00671 63 ----------------------------------WRKLVEESIKADLETYGRLDVRF--DVWFGESSYLGLMGKVVELLE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 274 AKGLAVESEGATVVFLDEYqnkdGDPMGVIIQKKDGGYLYTTTDIACAKYRYEtLGANRVLYYIDSRQHQHLMQAWTIVR 353
Cdd:cd00671 107 ELGLLYEEDGALWLDLTEF----GDDKDRVLVRSDGTYTYFTRDIAYHLDKFE-RGADKIIYVVGADHHGHFKRLFAALE 181
|
250 260 270
....*....|....*....|....*....|..
gi 727180893 354 KAGYvPESVSLEHHMFGMMLGKDGKPFKTRSG 385
Cdd:cd00671 182 LLGY-DEAKKLEHLLYGMVNLPKEGKMSTRAG 212
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
461-576 |
6.45e-36 |
|
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: 130.39 E-value: 6.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 461 QYAYTRVASVFKRAG-----IDESSLTLPLILTEEREIALATRLLQFEEVLTAVAREGTPHVMCSYLYDLAGLFSGFYEH 535
Cdd:smart00836 2 QYAHARICSILRKAGeagetLPDIADADLSLLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYNR 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 727180893 536 CQILNADSEEARQSRLKLALLTAKTLKTGLDTLGIETVERM 576
Cdd:smart00836 82 VRVLGEENPELRKARLALLKAVRQVLANGLRLLGISAPERM 122
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
1-576 |
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: 759.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 1 MNIQVLLSDKVSQALIAAGA-PADCEAQVRPSAKAQFGDYQANGVMSVAKKLGMPPRQLAEKVVQLLDLGDVASKVEIAG 79
Cdd:COG0018 1 MNIKEELAEAIAAALAALGAgLEEPDILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDADPLVEKVEIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 80 PGFINIFLNSDWVARQADQVLNA-PKLGIAPV-EPQTIVIDYSAPNVAKEMHVGHLRSTIIGDAAARTQEFLGHKVIRAN 157
Cdd:COG0018 81 PGFINFFLSPAALAAVLKEILADgEDYGRSDAgKGKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYDVTREN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 158 HVGDWGTQFGMLIAYLEKMQNENA--SDMGLSDLEQFYREAKKHYDEDAEFAERARAYVVKLQGGDQYCLKMWRKLVDIT 235
Cdd:COG0018 161 YINDAGTQIGKLALSLERYGEEEIepESKPDGYLGDLYVKFHKEYEEDPELEDIARELLAKLEPGDEEALELWKKAVDWS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 236 MAQNQLTYNRLNVTLteDDVMGESLYNAM--LPGIVADLKAKGLAVESEGATVVFLDEYqnkdGDPMGVIIQKKDGGYLY 313
Cdd:COG0018 241 LEEIKEDLKRLGVEF--DVWFSESSLYDSgaVEEVVEELKEKGLLYESDGALWVRLTEF----GDDKDRVLVKSDGTYTY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 314 TTTDIACAKYRYETLGANRVLYYIDSRQHQHLMQAWTIVRKAGYVPESvSLEHHMFGMMLGKDGKPFKTRSGGTVKLSDL 393
Cdd:COG0018 315 FTTDIAYHLYKFERYGFDRVIYVVGADQHGHFKRLFAALKALGYDPAK-DLEHLLFGMVNLRDGEKMSTRAGTVVTLDDL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 394 LDEAIERAEQLIAGKNpdmpEDEMKTIARVVGIGAVKYADLSKSRTTDYVFDWDNMLAFEGNTAPYMQYAYTRVASVFKR 473
Cdd:COG0018 394 LDEAVERAREIIEEKS----EEEKEEIAEQVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNTNPYVQYAHARICSILRK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 474 AGIDESSLTL--PLILTEEREIALATRLLQFEEVLTAVAREGTPHVMCSYLYDLAGLFSGFYEHCQILNADSEEARQSRL 551
Cdd:COG0018 470 AGEELDGLAEadLSLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRILKAEDEELRAARL 549
|
570 580
....*....|....*....|....*
gi 727180893 552 KLALLTAKTLKTGLDTLGIETVERM 576
Cdd:COG0018 550 ALVAATAQVLKNGLGLLGISAPERM 574
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
3-576 |
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: 666.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 3 IQVLLSDKVSQALIAAGAPADCEAQVRPSAKAQFGDYQANGVMSVAKKLGMPPRQLAEKVVQLLDLGDVASKVEIAGPgF 82
Cdd:TIGR00456 1 IKTLLKEEISQALLKAGLSKESEILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKLKTGEIIEKVEAAGP-F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 83 INIFLNSDWVARQADQVLNAPK--LGIAPVEPQTIVIDYSAPNVAKEMHVGHLRSTIIGDAAARTQEFLGHKVIRANHVG 160
Cdd:TIGR00456 80 INFFLSPQKLLERLIQKILTQKekYGSKKLKNKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 161 DWGTQFGMLIAYLEKMQNE---NASDMGLSDLEQFYREAKKHYDEDAEFAERARAYVVKLQGGDQYCLKMWRKLVDITMA 237
Cdd:TIGR00456 160 DWGRQFGLLALGVEKFGNEalnIAVKKPDHGLEGFYVEINKRLEENEELEEEARELFVKLESGDEETIKLWKRLVEYSLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 238 QNQLTYNRLNVTLTEDDVMGESLYNAMLPGIVADLKAKGLAVEsEGATVVFLDEYQNKdgdpMGVIIQKKDGGYLYTTTD 317
Cdd:TIGR00456 240 GIKETYDRLNIHFDSFVWEGESVKNGMLPKVLEDLKEKGLVVE-DGALWLDLTLFGDK----KDRVLQKSDGTYLYLTTD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 318 IACAKYRYETlGANRVLYYIDSRQHQHLMQAWTIVRKAGYvpESVSLEHHMFGMMLGKDgkpFKTRSGGTVKLSDLLDEA 397
Cdd:TIGR00456 315 IAYHLDKLER-GFDKMIYVWGSDHHLHIAQMFAILEKLGY--KKKELEHLNFGMVPLYS---MKTRRGNVISLDNLLDEA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 398 IERAEQLIAgKNPDMPEDEMktiARVVGIGAVKYADLSKSRTTDYVFDWDNMLAFEGNTAPYMQYAYTRVASVFKRAGID 477
Cdd:TIGR00456 389 SKRAGNVIT-IKNDLEEEKV---ADAVGIGAVRYFDLSKNRTTDYVFDWDAMLSFEGNTAPYIQYAHARICSILRKAEID 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 478 -ESSLTLPLILTEEREIALATRLLQFEEVLTAVAREGTPHVMCSYLYDLAGLFSGFYEHCQILNADsEEARQSRLKLALL 556
Cdd:TIGR00456 465 gEKLIADDFELLEEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACPVLDAE-NELAAARLALLKA 543
|
570 580
....*....|....*....|
gi 727180893 557 TAKTLKTGLDTLGIETVERM 576
Cdd:TIGR00456 544 TRQTLKNGLDLLGIEPPERM 563
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
1-576 |
0e+00 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 655.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 1 MNIQVLLSDKVSQALIAAGAPADCEAQVRPSAKAQFGDYQANGVMSVAKKLGMPPRQLAEKVVQLLdlgdvaSKVEIAGP 80
Cdd:PRK01611 3 MDIKELLAEALAAALEAGGLPELPAVLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIVEAI------EKVEIAGP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 81 GFINIFLNSDWVARQADQVLNA-PKLGIAPV-EPQTIVIDYSAPNVAKEMHVGHLRSTIIGDAAARTQEFLGHKVIRANH 158
Cdd:PRK01611 77 GFINFFLDPAALAELVLAILEAgERYGRSDIgKGKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDVTREYY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 159 VGDWGTQFGMLIAYLEKMqnenasdmglsdleqfyreakkhydedaefaerarayvvklqggdqyclkmWRKLVDITMAQ 238
Cdd:PRK01611 157 VNDAGTQIGMLIASLELL---------------------------------------------------WRKAVDISLDE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 239 NQLTYNRLNVTLTEDDVMGESLYNAMLPGIVADLKAKGLAV-ESEGATVVFLDEYqnkdGDPMGVIIQKKDGGYLYTTTD 317
Cdd:PRK01611 186 IKEDLDRLGVHFDVWFSESELYYNGKVDEVVEDLKEKGLLYvESDGALWVRLTEF----GDDKDRVLIKSDGTYTYFTRD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 318 IACAKYRYETLgaNRVLYYIDSRQHQHLMQAWTIVRKAGYVPESVS-LEHHMFGMMLGKDGKPFKTRSGGTVKLSDLLDE 396
Cdd:PRK01611 262 IAYHLYKFERF--DRVIYVVGADHHGHFKRLKAALKALGYDPDALEvLLHQMVGLVRGGEGVKMSTRAGNVVTLDDLLDE 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 397 AIERAEQLIAGKNpdmpedemktIARVVGIGAVKYADLSKSRTTDYVFDWDNMLAFEGNTAPYMQYAYTRVASVFKRAGI 476
Cdd:PRK01611 340 AVGRARELIEEKE----------IAEAVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPPYVQYAHARICSILRKAAE 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 477 DESSLTLPLiLTEEREIALATRLLQFEEVLTAVAREGTPHVMCSYLYDLAGLFSGFYEHCqILNADSEEARQSRLKLALL 556
Cdd:PRK01611 410 AGIDLLLAL-LTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYNRV-LLKDEEEELRNARLALVKA 487
|
570 580
....*....|....*....|
gi 727180893 557 TAKTLKTGLDTLGIETVERM 576
Cdd:PRK01611 488 TAQVLKNGLDLLGISAPERM 507
|
|
| PLN02286 |
PLN02286 |
arginine-tRNA ligase |
7-576 |
0e+00 |
|
arginine-tRNA ligase
Pssm-ID: 215160 [Multi-domain] Cd Length: 576 Bit Score: 595.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 7 LSDKVSQAL-IAAGAPADCEAQVRPSAKAQFGDYQANGVMSVAKKL-GMP-----PRQLAEKVVQLLDLGDVASKVEIAG 79
Cdd:PLN02286 3 LAKLFEASLrLTVPDEPSVEPLVAACTNPKFGDYQCNNAMGLWSKLkGKGtsfknPRAVAQAIVKNLPASEMIESTSVAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 80 PGFINIFLNSDWVARQADQVLNAPKLGIAPVEP-QTIVIDYSAPNVAKEMHVGHLRSTIIGDAAARTQEFLGHKVIRANH 158
Cdd:PLN02286 83 PGFVNVRLSASWLAKRIERMLVDGIDTWAPTLPvKRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEFSGVEVLRRNH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 159 VGDWGTQFGMLIAYLEKM--QNENASDMGLSDLEQFYREAKKHYDEDAEFAERARAYVVKLQGGDQYCLKMWRKLVDITM 236
Cdd:PLN02286 163 VGDWGTQFGMLIEHLFEKfpNWESVSDQAIGDLQEFYKAAKKRFDEDEEFKARAQQAVVRLQGGDPEYRAAWAKICEISR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 237 AQNQLTYNRLNVTLTEDdvmGESLYNAMLPGIVADLKAKGLAVESEGATVVFLDEYQNkdgdPMgvIIQKKDGGYLYTTT 316
Cdd:PLN02286 243 REFEKVYQRLRVELEEK---GESFYNPYIPGVIEELESKGLVVESDGARVIFVEGFDI----PL--IVVKSDGGFNYAST 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 317 DIACAKYRYETLGANRVLYYIDSRQHQHLMQAWTIVRKAGYVPES--VSLEHHMFGMMLGKDGKPFKTRSGGTVKLSDLL 394
Cdd:PLN02286 314 DLAALWYRLNEEKAEWIIYVTDVGQQQHFDMVFKAAKRAGWLPEDtyPRLEHVGFGLVLGEDGKRFRTRSGEVVRLVDLL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 395 DEAIERAEQ-LIA-GKNPDMPEDEMKTIARVVGIGAVKYADLSKSRTTDYVFDWDNMLAFEGNTAPYMQYAYTRVASVFK 472
Cdd:PLN02286 394 DEAKSRSKAaLIErGKDSEWTPEELEQAAEAVGYGAVKYADLKNNRLTNYTFSFDQMLDLKGNTAVYLLYAHARICSIIR 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 473 RAG--IDESSLTLPLILTEEREIALATRLLQFEEVLTAVAREGTPHVMCSYLYDLAGLFSGFYEHCQILNADSEEarqSR 550
Cdd:PLN02286 474 KSGkdIDELKKTGKIVLDHPDERALGLHLLQFPEVVEEACTDLLPNRLCEYLYNLSEKFTKFYSNCKVNGSEEET---SR 550
|
570 580
....*....|....*....|....*.
gi 727180893 551 LKLALLTAKTLKTGLDTLGIETVERM 576
Cdd:PLN02286 551 LLLCEATAIVMRKCFHLLGITPLYRL 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: 554.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 95 QADQVLNAPKLGIAPVEPQTIVIDYSAPNVAKEMHVGHLRSTIIGDAAARTQEFLGHKVIRANHVGDWGTQFGMLIAYLE 174
Cdd:pfam00750 1 TVPNALLQKGLGKASREKKKVVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQFGMLIAGLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 175 KMQNENAS-DMGLSDLEQFYREAKKHYDEDAEFAERARAYVVKLQGGDQYCLKMWRKLVDITMAQNQLTYNRLNVTLTEd 253
Cdd:pfam00750 81 KYQDEKTLqEMPIQDLEDFYREAKKHYDEEEEFAERARNYVVKLQSGDEYWRRMWKLIVDITMTQNQRLYDRLDVTLTE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 254 dvMGESLYNAMLPGIVADLKAKGLAVESEGATVVFLDEYqnkdGDPMGVIIQKKDGGYLYTTTDIACAKYRYETLGANRV 333
Cdd:pfam00750 160 --MGESLYNPMMNEIVKDFKKNGLVVEIDGALVVFLDEF----GKPMGVIVQKSDGGYLYTTTDIAAAKYRYETLHADRM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 334 LYYIDSRQHQHLMQAWTIVRKAGYVPESVSLEHHMFGMMLGKDGKPFKTRSGGTVKLSDLLDEAIERAEQLIAGKNPD-- 411
Cdd:pfam00750 234 LYVIDSRQSQHMQQAFAILRKAGYVPESKDLEHINFGMVLGKDGKPFKTRKGGTVKLADLLDEALERALQLIMEKNKDki 313
|
330 340 350
....*....|....*....|....*....|....*
gi 727180893 412 MPEDEMKTIARVVGIGAVKYADLSKSRTTDYVFDW 446
Cdd:pfam00750 314 LQADELEAVADAVGIGAIKYADLSKNRTNDYIFDW 348
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
114-385 |
7.51e-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: 7.51e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 114 TIVIDYSAPNVAKEMHVGHLRSTIIGDAAARTQEFLGHKVIRANHVGDWGTQFGMLIAYLEKmqnenasdmglsdleqfy 193
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSLEK------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 194 reakkhydedaefaerarayvvklqggdqyclkmWRKLVDITMAQNQLTYNRLNVTLteDDVMGESLYNAMLPGIVADLK 273
Cdd:cd00671 63 ----------------------------------WRKLVEESIKADLETYGRLDVRF--DVWFGESSYLGLMGKVVELLE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 274 AKGLAVESEGATVVFLDEYqnkdGDPMGVIIQKKDGGYLYTTTDIACAKYRYEtLGANRVLYYIDSRQHQHLMQAWTIVR 353
Cdd:cd00671 107 ELGLLYEEDGALWLDLTEF----GDDKDRVLVRSDGTYTYFTRDIAYHLDKFE-RGADKIIYVVGADHHGHFKRLFAALE 181
|
250 260 270
....*....|....*....|....*....|..
gi 727180893 354 KAGYvPESVSLEHHMFGMMLGKDGKPFKTRSG 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 ... |
422-576 |
7.38e-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: 203.60 E-value: 7.38e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 422 RVVGIGAVKYADLSKSRTTDYVFDWDNMLAFEGNTAPYMQYAYTRVASVFKRAGIDESSLT---LPLiLTEEREIALATR 498
Cdd:cd07956 1 EEVGVGAVKYQDLSNKRIKDYTFDWERMLSFEGDTGPYLQYAHARLCSILRKAGETIEAEAdadLSL-LPEPDERDLILL 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727180893 499 LLQFEEVLTAVAREGTPHVMCSYLYDLAGLFSGFYEHCQILNADsEEARQSRLKLALLTAKTLKTGLDTLGIETVERM 576
Cdd:cd07956 80 LAKFPEVVKNAAETLEPHTIATYLFDLAHAFSKFYNACPVLGAE-EELRNARLALVAAARQVLANGLDLLGIEAPERM 156
|
|
| DALR_1 |
pfam05746 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
460-576 |
1.53e-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: 148.18 E-value: 1.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 460 MQYAYTRVASVFKRAGIDESSLTL-PLILTEEREIALATRLLQFEEVLTAVAREGTPHVMCSYLYDLAGLFSGFYEHCQI 538
Cdd:pfam05746 1 LQYAHARICSILRKAGELGINLDIdADLLTEEEEKELLKALLQFPEVLEEAAEELEPHRLANYLYELASAFHSFYNNCRV 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 727180893 539 LNADSEEaRQSRLKLALLTAKTLKTGLDTLGIETVERM 576
Cdd:pfam05746 81 LDEDNEE-RNARLALLKAVRQVLKNGLDLLGIEAPEKM 117
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
461-576 |
6.45e-36 |
|
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: 130.39 E-value: 6.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 461 QYAYTRVASVFKRAG-----IDESSLTLPLILTEEREIALATRLLQFEEVLTAVAREGTPHVMCSYLYDLAGLFSGFYEH 535
Cdd:smart00836 2 QYAHARICSILRKAGeagetLPDIADADLSLLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYNR 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 727180893 536 CQILNADSEEARQSRLKLALLTAKTLKTGLDTLGIETVERM 576
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 |
7.44e-26 |
|
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: 101.12 E-value: 7.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 1 MNIQVLLSDKVSQALIAAGAPADceAQVRPSAKAQFGDYQANGVMSVAKKLGMPPRQLAEKVVQLLDLGDVASKVEIAGP 80
Cdd:smart01016 1 DLLKEAIAEALKKALGVEGEPID--IALERPKDPDHGDYATNVAFRLAKKLKKNPRELAEEIAEKLPKSDLVEKVEIAGP 78
|
....*..
gi 727180893 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 |
7.55e-24 |
|
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: 95.38 E-value: 7.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180893 7 LSDKVSQALIAAGA--PADCEAQVRPSAKAQFGDYQANGVMSVAKKLGMPPRQLAEKVVQLLDLGDVASKVEIAGPGFIN 84
Cdd:pfam03485 1 LKKAIAKALSKLGGpdLELIDIVIETPKNPKFGDYATNVAMQLAKKLKKNPREIAEEIAEKLEKSDIIEKVEVAGPGFIN 80
|
...
gi 727180893 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 ... |
119-179 |
1.67e-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: 53.64 E-value: 1.67e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727180893 119 YSAPNVAKEMHVGHLRSTIIGDAAARTQEFLGHKVIRANHVGDWGTQFG------------MLIAYLEKMQNE 179
Cdd:cd00802 3 FSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGdpankkgenakaFVERWIERIKED 75
|
|
| |
