|
Name |
Accession |
Description |
Interval |
E-value |
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
1-581 |
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: 729.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 1 MKEHIHHLLEQTVANLKsagilPADLEARVQVDRCKEKAHGDLATNLAMLLAKPARKNPRELAAAIIEHLPASDLIAKVE 80
Cdd:COG0018 3 IKEELAEAIAAALAALG-----AGLEEPDILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDADPLVEKVE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 81 IAGPGFINFFFDPSWLAGQVEAMVTSANA--NVKLPTPQTVVVDYSAPNVAKEMAVHHIRSTVLGDVAARALEFLGHKVV 158
Cdd:COG0018 78 IAGPGFINFFLSPAALAAVLKEILADGEDygRSDAGKGKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYDVT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 159 RANHIGDWGTQFGMLIAYLEKMANEHA--SDMELRDLEAFYTQAKRHYDEDEAFAERARNYVVKLQGGDEYCRTMWKKLV 236
Cdd:COG0018 158 RENYINDAGTQIGKLALSLERYGEEEIepESKPDGYLGDLYVKFHKEYEEDPELEDIARELLAKLEPGDEEALELWKKAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 237 DMTMEQNQRNYDRLNVSLtnKDIMGESMYNDM--LPEIVADLKARGLAVESEGATVVFLDEFknkdGEPMGVIIQKSDGG 314
Cdd:COG0018 238 DWSLEEIKEDLKRLGVEF--DVWFSESSLYDSgaVEEVVEELKEKGLLYESDGALWVRLTEF----GDDKDRVLVKSDGT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 315 FLYTTTDIACAKYRYETLGADRVMYFIDSRQHQHLMQAWTITRKAGYVPESvPLEHHAFGMMLGKDGRPYKTRSGGTVKL 394
Cdd:COG0018 312 YTYFTTDIAYHLYKFERYGFDRVIYVVGADQHGHFKRLFAALKALGYDPAK-DLEHLLFGMVNLRDGEKMSTRAGTVVTL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 395 VDLLNEAEERAAALLESRNsdlsAEEKAQVVHAIAMGAVKYADLSKNRTTDYIFDWDLMLSFEGNTAPYLQYAYTRIQSI 474
Cdd:COG0018 391 DDLLDEAVERAREIIEEKS----EEEKEEIAEQVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNTNPYVQYAHARICSI 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 475 FRKAGVDADTLG--GKVVLNEEAEETLAQKLIQFSDAVNGVADKGMPHLLCTYLYELSGNFMTFYEACPINKDGvDEATR 552
Cdd:COG0018 467 LRKAGEELDGLAeaDLSLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRILKAE-DEELR 545
|
570 580
....*....|....*....|....*....
gi 516374808 553 QSRLLLCAATAKVLKLGLGVLGIHTLERM 581
Cdd:COG0018 546 AARLALVAATAQVLKNGLGLLGISAPERM 574
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
1-581 |
0e+00 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 621.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 1 MKEHIHHLLEQTVANLKSAGILPAdlEARVQVDRCKEKAHGDLATNLAMLLAKPARKNPRELAAAIIEHlpasdlIAKVE 80
Cdd:PRK01611 1 MMMDIKELLAEALAAALEAGGLPE--LPAVLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIVEA------IEKVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 81 IAGPGFINFFFDPSWLAGQVEAMVTSANA--NVKLPTPQTVVVDYSAPNVAKEMAVHHIRSTVLGDVAARALEFLGHKVV 158
Cdd:PRK01611 73 IAGPGFINFFLDPAALAELVLAILEAGERygRSDIGKGKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDVT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 159 RANHIGDWGTQFGMLIAYLEKManehasdmelrdleafytqakrhydedeafaerarnyvvklqggdeycrtmWKKLVDM 238
Cdd:PRK01611 153 REYYVNDAGTQIGMLIASLELL---------------------------------------------------WRKAVDI 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 239 TMEQNQRNYDRLNVSLTNKDIMGESMYNDMLPEIVADLKARGLAV-ESEGATVVFLDEFknkdGEPMGVIIQKSDGGFLY 317
Cdd:PRK01611 182 SLDEIKEDLDRLGVHFDVWFSESELYYNGKVDEVVEDLKEKGLLYvESDGALWVRLTEF----GDDKDRVLIKSDGTYTY 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 318 TTTDIACAKYRYETLgaDRVMYFIDSRQHQHLMQAWTITRKAGYVPESVP-LEHHAFGMMLGKDGRPYKTRSGGTVKLVD 396
Cdd:PRK01611 258 FTRDIAYHLYKFERF--DRVIYVVGADHHGHFKRLKAALKALGYDPDALEvLLHQMVGLVRGGEGVKMSTRAGNVVTLDD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 397 LLNEAEERAAALLESRnsdlsaeekaQVVHAIAMGAVKYADLSKNRTTDYIFDWDLMLSFEGNTAPYLQYAYTRIQSIFR 476
Cdd:PRK01611 336 LLDEAVGRARELIEEK----------EIAEAVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPPYVQYAHARICSILR 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 477 KAGvDADTLGGKVVLNEEAEETLAQKLIQFSDAVNGVADKGMPHLLCTYLYELSGNFMTFYEACPINKDgvDEATRQSRL 556
Cdd:PRK01611 406 KAA-EAGIDLLLALLTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYNRVLLKDE--EEELRNARL 482
|
570 580
....*....|....*....|....*
gi 516374808 557 LLCAATAKVLKLGLGVLGIHTLERM 581
Cdd:PRK01611 483 ALVKATAQVLKNGLDLLGISAPERM 507
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
1-581 |
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: 585.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 1 MKEHIhhlleqTVANLKSAGILPADlearVQVDRCKEKAHGDLATNLAMLLAKPARKNPRELAAAIIEHLPASDLIAKVE 80
Cdd:TIGR00456 5 LKEEI------SQALLKAGLSKESE----ILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKLKTGEIIEKVE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 81 IAGPgFINFFFDPSWLAGQVEAMVTSANAN--VKLPTPQTVVVDYSAPNVAKEMAVHHIRSTVLGDVAARALEFLGHKVV 158
Cdd:TIGR00456 75 AAGP-FINFFLSPQKLLERLIQKILTQKEKygSKKLKNKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 159 RANHIGDWGTQFGMLIAYLEKMANEH---ASDMELRDLEAFYTQAKRHYDEDEAFAERARNYVVKLQGGDEYCRTMWKKL 235
Cdd:TIGR00456 154 REYYVNDWGRQFGLLALGVEKFGNEAlniAVKKPDHGLEGFYVEINKRLEENEELEEEARELFVKLESGDEETIKLWKRL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 236 VDMTMEQNQRNYDRLNVSLTNKDIMGESMYNDMLPEIVADLKARGLAVEsEGATVVFLDEFKNKdgepMGVIIQKSDGGF 315
Cdd:TIGR00456 234 VEYSLEGIKETYDRLNIHFDSFVWEGESVKNGMLPKVLEDLKEKGLVVE-DGALWLDLTLFGDK----KDRVLQKSDGTY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 316 LYTTTDIACAKYRYETlGADRVMYFIDSRQHQHLMQAWTITRKAGYvpESVPLEHHAFGMMLGKDgrpYKTRSGGTVKLV 395
Cdd:TIGR00456 309 LYLTTDIAYHLDKLER-GFDKMIYVWGSDHHLHIAQMFAILEKLGY--KKKELEHLNFGMVPLYS---MKTRRGNVISLD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 396 DLLNEAEERAAALLESRNsdlsAEEKAQVVHAIAMGAVKYADLSKNRTTDYIFDWDLMLSFEGNTAPYLQYAYTRIQSIF 475
Cdd:TIGR00456 383 NLLDEASKRAGNVITIKN----DLEEEKVADAVGIGAVRYFDLSKNRTTDYVFDWDAMLSFEGNTAPYIQYAHARICSIL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 476 RKAGVDADT-LGGKVVLNEEAEETLAQKLIQFSDAVNGVADKGMPHLLCTYLYELSGNFMTFYEACPINKDgvDEATRQS 554
Cdd:TIGR00456 459 RKAEIDGEKlIADDFELLEEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACPVLDA--ENELAAA 536
|
570 580
....*....|....*....|....*..
gi 516374808 555 RLLLCAATAKVLKLGLGVLGIHTLERM 581
Cdd:TIGR00456 537 RLALLKATRQTLKNGLDLLGIEPPERM 563
|
|
| tRNA-synt_1d |
pfam00750 |
tRNA synthetases class I (R); Other tRNA synthetase sub-families are too dissimilar to be ... |
99-450 |
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: 535.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 99 QVEAMVTSANANVKLPTPQTVVVDYSAPNVAKEMAVHHIRSTVLGDVAARALEFLGHKVVRANHIGDWGTQFGMLIAYLE 178
Cdd:pfam00750 1 TVPNALLQKGLGKASREKKKVVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQFGMLIAGLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 179 KMANEHAS-DMELRDLEAFYTQAKRHYDEDEAFAERARNYVVKLQGGDEYCRTMWKKLVDMTMEQNQRNYDRLNVSLTNk 257
Cdd:pfam00750 81 KYQDEKTLqEMPIQDLEDFYREAKKHYDEEEEFAERARNYVVKLQSGDEYWRRMWKLIVDITMTQNQRLYDRLDVTLTE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 258 diMGESMYNDMLPEIVADLKARGLAVESEGATVVFLDEFknkdGEPMGVIIQKSDGGFLYTTTDIACAKYRYETLGADRV 337
Cdd:pfam00750 160 --MGESLYNPMMNEIVKDFKKNGLVVEIDGALVVFLDEF----GKPMGVIVQKSDGGYLYTTTDIAAAKYRYETLHADRM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 338 MYFIDSRQHQHLMQAWTITRKAGYVPESVPLEHHAFGMMLGKDGRPYKTRSGGTVKLVDLLNEAEERAAALLESRNSD-- 415
Cdd:pfam00750 234 LYVIDSRQSQHMQQAFAILRKAGYVPESKDLEHINFGMVLGKDGKPFKTRKGGTVKLADLLDEALERALQLIMEKNKDki 313
|
330 340 350
....*....|....*....|....*....|....*
gi 516374808 416 LSAEEKAQVVHAIAMGAVKYADLSKNRTTDYIFDW 450
Cdd:pfam00750 314 LQADELEAVADAVGIGAIKYADLSKNRTNDYIFDW 348
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
118-389 |
5.69e-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: 221.67 E-value: 5.69e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 118 TVVVDYSAPNVAKEMAVHHIRSTVLGDVAARALEFLGHKVVRANHIGDWGTQFGMLIAYLEKmanehasdmelrdleafy 197
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSLEK------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 198 tqakrhydedeafaerarnyvvklqggdeycrtmWKKLVDMTMEQNQRNYDRLNVSLtnKDIMGESMYNDMLPEIVADLK 277
Cdd:cd00671 63 ----------------------------------WRKLVEESIKADLETYGRLDVRF--DVWFGESSYLGLMGKVVELLE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 278 ARGLAVESEGATVVFLDEFknkdGEPMGVIIQKSDGGFLYTTTDIACAKYRYEtLGADRVMYFIDSRQHQHLMQAWTITR 357
Cdd:cd00671 107 ELGLLYEEDGALWLDLTEF----GDDKDRVLVRSDGTYTYFTRDIAYHLDKFE-RGADKIIYVVGADHHGHFKRLFAALE 181
|
250 260 270
....*....|....*....|....*....|..
gi 516374808 358 KAGYvPESVPLEHHAFGMMLGKDGRPYKTRSG 389
Cdd:cd00671 182 LLGY-DEAKKLEHLLYGMVNLPKEGKMSTRAG 212
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
464-581 |
3.06e-33 |
|
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain of Arginyl tRNA synthetase. This domain is known as the DALR domain after characteristic conserved amino acids.
Pssm-ID: 214846 [Multi-domain] Cd Length: 122 Bit Score: 123.07 E-value: 3.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 464 LQYAYTRIQSIFRKAGVDADTLGGKVV-----LNEEAEETLAQKLIQFSDAVNGVADKGMPHLLCTYLYELSGNFMTFYE 538
Cdd:smart00836 1 VQYAHARICSILRKAGEAGETLPDIADadlslLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYN 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 516374808 539 ACPInKDGVDEATRQSRLLLCAATAKVLKLGLGVLGIHTLERM 581
Cdd:smart00836 81 RVRV-LGEENPELRKARLALLKAVRQVLANGLRLLGISAPERM 122
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
1-581 |
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: 729.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 1 MKEHIHHLLEQTVANLKsagilPADLEARVQVDRCKEKAHGDLATNLAMLLAKPARKNPRELAAAIIEHLPASDLIAKVE 80
Cdd:COG0018 3 IKEELAEAIAAALAALG-----AGLEEPDILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDADPLVEKVE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 81 IAGPGFINFFFDPSWLAGQVEAMVTSANA--NVKLPTPQTVVVDYSAPNVAKEMAVHHIRSTVLGDVAARALEFLGHKVV 158
Cdd:COG0018 78 IAGPGFINFFLSPAALAAVLKEILADGEDygRSDAGKGKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYDVT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 159 RANHIGDWGTQFGMLIAYLEKMANEHA--SDMELRDLEAFYTQAKRHYDEDEAFAERARNYVVKLQGGDEYCRTMWKKLV 236
Cdd:COG0018 158 RENYINDAGTQIGKLALSLERYGEEEIepESKPDGYLGDLYVKFHKEYEEDPELEDIARELLAKLEPGDEEALELWKKAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 237 DMTMEQNQRNYDRLNVSLtnKDIMGESMYNDM--LPEIVADLKARGLAVESEGATVVFLDEFknkdGEPMGVIIQKSDGG 314
Cdd:COG0018 238 DWSLEEIKEDLKRLGVEF--DVWFSESSLYDSgaVEEVVEELKEKGLLYESDGALWVRLTEF----GDDKDRVLVKSDGT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 315 FLYTTTDIACAKYRYETLGADRVMYFIDSRQHQHLMQAWTITRKAGYVPESvPLEHHAFGMMLGKDGRPYKTRSGGTVKL 394
Cdd:COG0018 312 YTYFTTDIAYHLYKFERYGFDRVIYVVGADQHGHFKRLFAALKALGYDPAK-DLEHLLFGMVNLRDGEKMSTRAGTVVTL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 395 VDLLNEAEERAAALLESRNsdlsAEEKAQVVHAIAMGAVKYADLSKNRTTDYIFDWDLMLSFEGNTAPYLQYAYTRIQSI 474
Cdd:COG0018 391 DDLLDEAVERAREIIEEKS----EEEKEEIAEQVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNTNPYVQYAHARICSI 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 475 FRKAGVDADTLG--GKVVLNEEAEETLAQKLIQFSDAVNGVADKGMPHLLCTYLYELSGNFMTFYEACPINKDGvDEATR 552
Cdd:COG0018 467 LRKAGEELDGLAeaDLSLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRILKAE-DEELR 545
|
570 580
....*....|....*....|....*....
gi 516374808 553 QSRLLLCAATAKVLKLGLGVLGIHTLERM 581
Cdd:COG0018 546 AARLALVAATAQVLKNGLGLLGISAPERM 574
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
1-581 |
0e+00 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 621.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 1 MKEHIHHLLEQTVANLKSAGILPAdlEARVQVDRCKEKAHGDLATNLAMLLAKPARKNPRELAAAIIEHlpasdlIAKVE 80
Cdd:PRK01611 1 MMMDIKELLAEALAAALEAGGLPE--LPAVLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIVEA------IEKVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 81 IAGPGFINFFFDPSWLAGQVEAMVTSANA--NVKLPTPQTVVVDYSAPNVAKEMAVHHIRSTVLGDVAARALEFLGHKVV 158
Cdd:PRK01611 73 IAGPGFINFFLDPAALAELVLAILEAGERygRSDIGKGKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDVT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 159 RANHIGDWGTQFGMLIAYLEKManehasdmelrdleafytqakrhydedeafaerarnyvvklqggdeycrtmWKKLVDM 238
Cdd:PRK01611 153 REYYVNDAGTQIGMLIASLELL---------------------------------------------------WRKAVDI 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 239 TMEQNQRNYDRLNVSLTNKDIMGESMYNDMLPEIVADLKARGLAV-ESEGATVVFLDEFknkdGEPMGVIIQKSDGGFLY 317
Cdd:PRK01611 182 SLDEIKEDLDRLGVHFDVWFSESELYYNGKVDEVVEDLKEKGLLYvESDGALWVRLTEF----GDDKDRVLIKSDGTYTY 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 318 TTTDIACAKYRYETLgaDRVMYFIDSRQHQHLMQAWTITRKAGYVPESVP-LEHHAFGMMLGKDGRPYKTRSGGTVKLVD 396
Cdd:PRK01611 258 FTRDIAYHLYKFERF--DRVIYVVGADHHGHFKRLKAALKALGYDPDALEvLLHQMVGLVRGGEGVKMSTRAGNVVTLDD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 397 LLNEAEERAAALLESRnsdlsaeekaQVVHAIAMGAVKYADLSKNRTTDYIFDWDLMLSFEGNTAPYLQYAYTRIQSIFR 476
Cdd:PRK01611 336 LLDEAVGRARELIEEK----------EIAEAVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPPYVQYAHARICSILR 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 477 KAGvDADTLGGKVVLNEEAEETLAQKLIQFSDAVNGVADKGMPHLLCTYLYELSGNFMTFYEACPINKDgvDEATRQSRL 556
Cdd:PRK01611 406 KAA-EAGIDLLLALLTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYNRVLLKDE--EEELRNARL 482
|
570 580
....*....|....*....|....*
gi 516374808 557 LLCAATAKVLKLGLGVLGIHTLERM 581
Cdd:PRK01611 483 ALVKATAQVLKNGLDLLGISAPERM 507
|
|
| PLN02286 |
PLN02286 |
arginine-tRNA ligase |
22-581 |
0e+00 |
|
arginine-tRNA ligase
Pssm-ID: 215160 [Multi-domain] Cd Length: 576 Bit Score: 594.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 22 LPADLEARVQVDRCKEKAHGDLATNLAMLLAKPAR------KNPRELAAAIIEHLPASDLIAKVEIAGPGFINFFFDPSW 95
Cdd:PLN02286 15 VPDEPSVEPLVAACTNPKFGDYQCNNAMGLWSKLKgkgtsfKNPRAVAQAIVKNLPASEMIESTSVAGPGFVNVRLSASW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 96 LAGQVEAMVTSANANVKLPTP-QTVVVDYSAPNVAKEMAVHHIRSTVLGDVAARALEFLGHKVVRANHIGDWGTQFGMLI 174
Cdd:PLN02286 95 LAKRIERMLVDGIDTWAPTLPvKRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEFSGVEVLRRNHVGDWGTQFGMLI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 175 AYLEKM--ANEHASDMELRDLEAFYTQAKRHYDEDEAFAERARNYVVKLQGGDEYCRTMWKKLVDMTMEQNQRNYDRLNV 252
Cdd:PLN02286 175 EHLFEKfpNWESVSDQAIGDLQEFYKAAKKRFDEDEEFKARAQQAVVRLQGGDPEYRAAWAKICEISRREFEKVYQRLRV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 253 SLTNKdimGESMYNDMLPEIVADLKARGLAVESEGATVVFLDEFKNkdgePMgvIIQKSDGGFLYTTTDIACAKYRYETL 332
Cdd:PLN02286 255 ELEEK---GESFYNPYIPGVIEELESKGLVVESDGARVIFVEGFDI----PL--IVVKSDGGFNYASTDLAALWYRLNEE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 333 GADRVMYFIDSRQHQHLMQAWTITRKAGYVPESVP--LEHHAFGMMLGKDGRPYKTRSGGTVKLVDLLNEAEERAAALLE 410
Cdd:PLN02286 326 KAEWIIYVTDVGQQQHFDMVFKAAKRAGWLPEDTYprLEHVGFGLVLGEDGKRFRTRSGEVVRLVDLLDEAKSRSKAALI 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 411 SRN--SDLSAEEKAQVVHAIAMGAVKYADLSKNRTTDYIFDWDLMLSFEGNTAPYLQYAYTRIQSIFRKAGVDADTL--G 486
Cdd:PLN02286 406 ERGkdSEWTPEELEQAAEAVGYGAVKYADLKNNRLTNYTFSFDQMLDLKGNTAVYLLYAHARICSIIRKSGKDIDELkkT 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 487 GKVVLNEEAEETLAQKLIQFSDAVNGVADKGMPHLLCTYLYELSGNFMTFYEACPINkdGVDEATrqSRLLLCAATAKVL 566
Cdd:PLN02286 486 GKIVLDHPDERALGLHLLQFPEVVEEACTDLLPNRLCEYLYNLSEKFTKFYSNCKVN--GSEEET--SRLLLCEATAIVM 561
|
570
....*....|....*
gi 516374808 567 KLGLGVLGIHTLERM 581
Cdd:PLN02286 562 RKCFHLLGITPLYRL 576
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
1-581 |
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: 585.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 1 MKEHIhhlleqTVANLKSAGILPADlearVQVDRCKEKAHGDLATNLAMLLAKPARKNPRELAAAIIEHLPASDLIAKVE 80
Cdd:TIGR00456 5 LKEEI------SQALLKAGLSKESE----ILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKLKTGEIIEKVE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 81 IAGPgFINFFFDPSWLAGQVEAMVTSANAN--VKLPTPQTVVVDYSAPNVAKEMAVHHIRSTVLGDVAARALEFLGHKVV 158
Cdd:TIGR00456 75 AAGP-FINFFLSPQKLLERLIQKILTQKEKygSKKLKNKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 159 RANHIGDWGTQFGMLIAYLEKMANEH---ASDMELRDLEAFYTQAKRHYDEDEAFAERARNYVVKLQGGDEYCRTMWKKL 235
Cdd:TIGR00456 154 REYYVNDWGRQFGLLALGVEKFGNEAlniAVKKPDHGLEGFYVEINKRLEENEELEEEARELFVKLESGDEETIKLWKRL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 236 VDMTMEQNQRNYDRLNVSLTNKDIMGESMYNDMLPEIVADLKARGLAVEsEGATVVFLDEFKNKdgepMGVIIQKSDGGF 315
Cdd:TIGR00456 234 VEYSLEGIKETYDRLNIHFDSFVWEGESVKNGMLPKVLEDLKEKGLVVE-DGALWLDLTLFGDK----KDRVLQKSDGTY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 316 LYTTTDIACAKYRYETlGADRVMYFIDSRQHQHLMQAWTITRKAGYvpESVPLEHHAFGMMLGKDgrpYKTRSGGTVKLV 395
Cdd:TIGR00456 309 LYLTTDIAYHLDKLER-GFDKMIYVWGSDHHLHIAQMFAILEKLGY--KKKELEHLNFGMVPLYS---MKTRRGNVISLD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 396 DLLNEAEERAAALLESRNsdlsAEEKAQVVHAIAMGAVKYADLSKNRTTDYIFDWDLMLSFEGNTAPYLQYAYTRIQSIF 475
Cdd:TIGR00456 383 NLLDEASKRAGNVITIKN----DLEEEKVADAVGIGAVRYFDLSKNRTTDYVFDWDAMLSFEGNTAPYIQYAHARICSIL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 476 RKAGVDADT-LGGKVVLNEEAEETLAQKLIQFSDAVNGVADKGMPHLLCTYLYELSGNFMTFYEACPINKDgvDEATRQS 554
Cdd:TIGR00456 459 RKAEIDGEKlIADDFELLEEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACPVLDA--ENELAAA 536
|
570 580
....*....|....*....|....*..
gi 516374808 555 RLLLCAATAKVLKLGLGVLGIHTLERM 581
Cdd:TIGR00456 537 RLALLKATRQTLKNGLDLLGIEPPERM 563
|
|
| tRNA-synt_1d |
pfam00750 |
tRNA synthetases class I (R); Other tRNA synthetase sub-families are too dissimilar to be ... |
99-450 |
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: 535.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 99 QVEAMVTSANANVKLPTPQTVVVDYSAPNVAKEMAVHHIRSTVLGDVAARALEFLGHKVVRANHIGDWGTQFGMLIAYLE 178
Cdd:pfam00750 1 TVPNALLQKGLGKASREKKKVVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQFGMLIAGLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 179 KMANEHAS-DMELRDLEAFYTQAKRHYDEDEAFAERARNYVVKLQGGDEYCRTMWKKLVDMTMEQNQRNYDRLNVSLTNk 257
Cdd:pfam00750 81 KYQDEKTLqEMPIQDLEDFYREAKKHYDEEEEFAERARNYVVKLQSGDEYWRRMWKLIVDITMTQNQRLYDRLDVTLTE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 258 diMGESMYNDMLPEIVADLKARGLAVESEGATVVFLDEFknkdGEPMGVIIQKSDGGFLYTTTDIACAKYRYETLGADRV 337
Cdd:pfam00750 160 --MGESLYNPMMNEIVKDFKKNGLVVEIDGALVVFLDEF----GKPMGVIVQKSDGGYLYTTTDIAAAKYRYETLHADRM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 338 MYFIDSRQHQHLMQAWTITRKAGYVPESVPLEHHAFGMMLGKDGRPYKTRSGGTVKLVDLLNEAEERAAALLESRNSD-- 415
Cdd:pfam00750 234 LYVIDSRQSQHMQQAFAILRKAGYVPESKDLEHINFGMVLGKDGKPFKTRKGGTVKLADLLDEALERALQLIMEKNKDki 313
|
330 340 350
....*....|....*....|....*....|....*
gi 516374808 416 LSAEEKAQVVHAIAMGAVKYADLSKNRTTDYIFDW 450
Cdd:pfam00750 314 LQADELEAVADAVGIGAIKYADLSKNRTNDYIFDW 348
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
118-389 |
5.69e-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: 221.67 E-value: 5.69e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 118 TVVVDYSAPNVAKEMAVHHIRSTVLGDVAARALEFLGHKVVRANHIGDWGTQFGMLIAYLEKmanehasdmelrdleafy 197
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSLEK------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 198 tqakrhydedeafaerarnyvvklqggdeycrtmWKKLVDMTMEQNQRNYDRLNVSLtnKDIMGESMYNDMLPEIVADLK 277
Cdd:cd00671 63 ----------------------------------WRKLVEESIKADLETYGRLDVRF--DVWFGESSYLGLMGKVVELLE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 278 ARGLAVESEGATVVFLDEFknkdGEPMGVIIQKSDGGFLYTTTDIACAKYRYEtLGADRVMYFIDSRQHQHLMQAWTITR 357
Cdd:cd00671 107 ELGLLYEEDGALWLDLTEF----GDDKDRVLVRSDGTYTYFTRDIAYHLDKFE-RGADKIIYVVGADHHGHFKRLFAALE 181
|
250 260 270
....*....|....*....|....*....|..
gi 516374808 358 KAGYvPESVPLEHHAFGMMLGKDGRPYKTRSG 389
Cdd:cd00671 182 LLGY-DEAKKLEHLLYGMVNLPKEGKMSTRAG 212
|
|
| Anticodon_Ia_Arg |
cd07956 |
Anticodon-binding domain of arginyl tRNA synthetases; This domain is found in arginyl tRNA ... |
426-581 |
4.53e-62 |
|
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: 201.67 E-value: 4.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 426 HAIAMGAVKYADLSKNRTTDYIFDWDLMLSFEGNTAPYLQYAYTRIQSIFRKAGVDADTLGGKVV--LNEEAEETLAQKL 503
Cdd:cd07956 1 EEVGVGAVKYQDLSNKRIKDYTFDWERMLSFEGDTGPYLQYAHARLCSILRKAGETIEAEADADLslLPEPDERDLILLL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516374808 504 IQFSDAVNGVADKGMPHLLCTYLYELSGNFMTFYEACPINKDgvDEATRQSRLLLCAATAKVLKLGLGVLGIHTLERM 581
Cdd:cd07956 81 AKFPEVVKNAAETLEPHTIATYLFDLAHAFSKFYNACPVLGA--EEELRNARLALVAAARQVLANGLDLLGIEAPERM 156
|
|
| DALR_1 |
pfam05746 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
464-581 |
1.86e-38 |
|
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: 137.40 E-value: 1.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 464 LQYAYTRIQSIFRKAGVD-ADTLGGKVVLNEEAEETLAQKLIQFSDAVNGVADKGMPHLLCTYLYELSGNFMTFYEACPI 542
Cdd:pfam05746 1 LQYAHARICSILRKAGELgINLDIDADLLTEEEEKELLKALLQFPEVLEEAAEELEPHRLANYLYELASAFHSFYNNCRV 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 516374808 543 NKDgvDEATRQSRLLLCAATAKVLKLGLGVLGIHTLERM 581
Cdd:pfam05746 81 LDE--DNEERNARLALLKAVRQVLKNGLDLLGIEAPEKM 117
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
464-581 |
3.06e-33 |
|
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain of Arginyl tRNA synthetase. This domain is known as the DALR domain after characteristic conserved amino acids.
Pssm-ID: 214846 [Multi-domain] Cd Length: 122 Bit Score: 123.07 E-value: 3.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 464 LQYAYTRIQSIFRKAGVDADTLGGKVV-----LNEEAEETLAQKLIQFSDAVNGVADKGMPHLLCTYLYELSGNFMTFYE 538
Cdd:smart00836 1 VQYAHARICSILRKAGEAGETLPDIADadlslLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYN 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 516374808 539 ACPInKDGVDEATRQSRLLLCAATAKVLKLGLGVLGIHTLERM 581
Cdd:smart00836 81 RVRV-LGEENPELRKARLALLKAVRQVLANGLRLLGISAPERM 122
|
|
| Arg_tRNA_synt_N |
smart01016 |
Arginyl tRNA synthetase N terminal dom; This domain is found at the amino terminus of Arginyl ... |
3-91 |
7.82e-31 |
|
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: 114.99 E-value: 7.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 3 EHIHHLLEQTVAnlksAGILPADLEARVQVDRCKEKAHGDLATNLAMLLAKPARKNPRELAAAIIEHLPASDLIAKVEIA 82
Cdd:smart01016 1 DLLKEAIAEALK----KALGVEGEPIDIALERPKDPDHGDYATNVAFRLAKKLKKNPRELAEEIAEKLPKSDLVEKVEIA 76
|
....*....
gi 516374808 83 GPGFINFFF 91
Cdd:smart01016 77 GPGFINFFL 85
|
|
| Arg_tRNA_synt_N |
pfam03485 |
Arginyl tRNA synthetase N terminal domain; This domain is found at the amino terminus of ... |
5-91 |
1.41e-28 |
|
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: 108.86 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 5 IHHLLEQTVANLKSAGILPADLEarvqVDRCKEKAHGDLATNLAMLLAKPARKNPRELAAAIIEHLPASDLIAKVEIAGP 84
Cdd:pfam03485 1 LKKAIAKALSKLGGPDLELIDIV----IETPKNPKFGDYATNVAMQLAKKLKKNPREIAEEIAEKLEKSDIIEKVEVAGP 76
|
....*..
gi 516374808 85 GFINFFF 91
Cdd:pfam03485 77 GFINFFL 83
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
121-204 |
5.53e-07 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 49.02 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516374808 121 VDYSAPNVAKEMAVHHIRSTVLGDVAARALEFLGHKVVRANHIGDWGTQFG------------MLIAYLEKMANEHASDM 188
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGdpankkgenakaFVERWIERIKEDVEYMF 80
|
90
....*....|....*...
gi 516374808 189 E--LRDLEaFYTQAKRHY 204
Cdd:cd00802 81 LqaADFLL-LYETECDIH 97
|
|
| |
