|
Name |
Accession |
Description |
Interval |
E-value |
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
1-558 |
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: 673.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 1 MDFKQKVVDLVSE---QVDLPKEKISMLIERPKNPKMGDYA-FPAFALAKIEHKNPALIAKDIAEKIS-DDNFTSIQAVG 75
Cdd:COG0018 1 MNIKEELAEAIAAalaALGAGLEEPDILVERPKDPEHGDYAtNVAMQLAKPLKKNPREIAEEIAEALDaDPLVEKVEIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 76 P-YVNFAIDHAKLVnATLNDVLTEKEHFGDQKLGEG-NVPIDMSSPNIAKPMSMGHLRSTVIGNSIAKTLEKVGYTPIKI 153
Cdd:COG0018 81 PgFINFFLSPAALA-AVLKEILADGEDYGRSDAGKGkKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYDVTRE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 154 NYLGDYGTQFGKLITAYRLWGNEE-DVKKDPITNLFHYYVKFHEEAEKDPKLEDEGRAAFKKLENGDEEEIKLWKWFREV 232
Cdd:COG0018 160 NYINDAGTQIGKLALSLERYGEEEiEPESKPDGYLGDLYVKFHKEYEEDPELEDIARELLAKLEPGDEEALELWKKAVDW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 233 SLQEFNRIYKELGVTFDSYNGEAFFNDK--MQPVVDELREKGLLEESRGAQVVNLGE--DENPALILKSDGSSLYMTRDL 308
Cdd:COG0018 240 SLEEIKEDLKRLGVEFDVWFSESSLYDSgaVEEVVEELKEKGLLYESDGALWVRLTEfgDDKDRVLVKSDGTYTYFTTDI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 309 AAALYRKKEYDFVMSLYVAGGEQTGHFKQLKQVLKKMGYDWSDNIHHIPFGLIT-QGGKKLSTRKGNVVFLDQVLKDAVS 387
Cdd:COG0018 320 AYHLYKFERYGFDRVIYVVGADQHGHFKRLFAALKALGYDPAKDLEHLLFGMVNlRDGEKMSTRAGTVVTLDDLLDEAVE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 388 LAEQQIEEKnpNLSNKKQVAHDVGVGAVVFHDLKNDRMDNFDFDLEEVVRFEGDTGPYVQYTNARAQSILRKANKEISM- 466
Cdd:COG0018 400 RAREIIEEK--SEEEKEEIAEQVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNTNPYVQYAHARICSILRKAGEELDGl 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 467 ---DNLSLNDDWSFAVAKALADFPAIVEKASEKFEPSIIAKYALDLSKKFNKYYANVRILDEDN--QLNARLALVQATSI 541
Cdd:COG0018 478 aeaDLSLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRILKAEDeeLRAARLALVAATAQ 557
|
570
....*....|....*..
gi 560182726 542 VLTEALRLLGVNAPKEM 558
Cdd:COG0018 558 VLKNGLGLLGISAPERM 574
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
1-558 |
0e+00 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 543.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 1 MDFKQKVVDLVSEQVD--LPKEKISMLIERPKNPKMGDYAFP-AFALAKIEHKNPALIAKDIAEKISddnftSIQAVGP- 76
Cdd:PRK01611 3 MDIKELLAEALAAALEagGLPELPAVLIERPKDPEHGDYATNvAMQLAKKLKKNPREIAEEIVEAIE-----KVEIAGPg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 77 YVNFAIDHAKLvNATLNDVLTEKEHFGDQKLGEG-NVPIDMSSPNIAKPMSMGHLRSTVIGNSIAKTLEKVGYTPIKINY 155
Cdd:PRK01611 78 FINFFLDPAAL-AELVLAILEAGERYGRSDIGKGkKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDVTREYY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 156 LGDYGTQFGKLITAYRlwgneedvkkdpitnlfhyyvkfheeaekdpkledegraafkklengdeeeiKLWKWFREVSLQ 235
Cdd:PRK01611 157 VNDAGTQIGMLIASLE----------------------------------------------------LLWRKAVDISLD 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 236 EFNRIYKELGVTFDSY--NGEAFFNDKMQPVVDELREKGLL-EESRGAQVVNLGE--DENPALILKSDGSSLYMTRDLAA 310
Cdd:PRK01611 185 EIKEDLDRLGVHFDVWfsESELYYNGKVDEVVEDLKEKGLLyVESDGALWVRLTEfgDDKDRVLIKSDGTYTYFTRDIAY 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 311 ALYRKKEYDFVmsLYVAGGEQTGHFKQLKQVLKKMGYDWS--DNIHHIPFGLITQG-GKKLSTRKGNVVFLDQVLKDAVS 387
Cdd:PRK01611 265 HLYKFERFDRV--IYVVGADHHGHFKRLKAALKALGYDPDalEVLLHQMVGLVRGGeGVKMSTRAGNVVTLDDLLDEAVG 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 388 LAEQQIEEKnpnlsnkkQVAHDVGVGAVVFHDLKNDRMDNFDFDLEEVVRFEGDTGPYVQYTNARAQSILRKANKE-ISM 466
Cdd:PRK01611 343 RARELIEEK--------EIAEAVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPPYVQYAHARICSILRKAAEAgIDL 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 467 DNLSLNDDWSFAVAKALADFPAIVEKASEKFEPSIIAKYALDLSKKFNKYYANVRILDEDNQL-NARLALVQATSIVLTE 545
Cdd:PRK01611 415 LLALLTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYNRVLLKDEEEELrNARLALVKATAQVLKN 494
|
570
....*....|...
gi 560182726 546 ALRLLGVNAPKEM 558
Cdd:PRK01611 495 GLDLLGISAPERM 507
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
18-558 |
1.65e-146 |
|
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: 433.31 E-value: 1.65e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 18 PKEKISMLIERPKNPKMGDYAFP-AFALAKIEHKNPALIAKDIAEKISDDNFT-SIQAVGPYVNFAIDHAKLVNATLNDV 95
Cdd:TIGR00456 18 LSKESEILVEETPNPEFGDYASNiAFPLAKVLKKAPRQIAEEIVLKLKTGEIIeKVEAAGPFINFFLSPQKLLERLIQKI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 96 LTEKEHFGDQKLGEGNVPIDMSSPNIAKPMSMGHLRSTVIGNSIAKTLEKVGYTPIKINYLGDYGTQFGKLITAYRLWGN 175
Cdd:TIGR00456 98 LTQKEKYGSKKLKNKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYVNDWGRQFGLLALGVEKFGN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 176 EEDVK--KDPITNLFHYYVKFHEEAEKDPKLEDEGRAAFKKLENGDEEEIKLWKWFREVSLQEFNRIYKELGVTFDSY-- 251
Cdd:TIGR00456 178 EALNIavKKPDHGLEGFYVEINKRLEENEELEEEARELFVKLESGDEETIKLWKRLVEYSLEGIKETYDRLNIHFDSFvw 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 252 NGEAFFNDKMQPVVDELREKGLLEESrGAQVVNLGE--DENPALILKSDGSSLYMTRDLAAALYRKKEyDFVMSLYVAGG 329
Cdd:TIGR00456 258 EGESVKNGMLPKVLEDLKEKGLVVED-GALWLDLTLfgDKKDRVLQKSDGTYLYLTTDIAYHLDKLER-GFDKMIYVWGS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 330 EQTGHFKQLKQVLKKMGYdWSDNIHHIPFGLITqgGKKLSTRKGNVVFLDQVLKDAVSLAEQQIEEKNpNLSNKKqVAHD 409
Cdd:TIGR00456 336 DHHLHIAQMFAILEKLGY-KKKELEHLNFGMVP--LYSMKTRRGNVISLDNLLDEASKRAGNVITIKN-DLEEEK-VADA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 410 VGVGAVVFHDLKNDRMDNFDFDLEEVVRFEGDTGPYVQYTNARAQSILRKAN----KEISMDNLSLNDDwSFAVAKALAD 485
Cdd:TIGR00456 411 VGIGAVRYFDLSKNRTTDYVFDWDAMLSFEGNTAPYIQYAHARICSILRKAEidgeKLIADDFELLEEK-EKELLKLLLQ 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 560182726 486 FPAIVEKASEKFEPSIIAKYALDLSKKFNKYYANVRILDEDNQL-NARLALVQATSIVLTEALRLLGVNAPKEM 558
Cdd:TIGR00456 490 FPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACPVLDAENELaAARLALLKATRQTLKNGLDLLGIEPPERM 563
|
|
| tRNA-synt_1d |
pfam00750 |
tRNA synthetases class I (R); Other tRNA synthetase sub-families are too dissimilar to be ... |
112-431 |
2.59e-87 |
|
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: 273.68 E-value: 2.59e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 112 VPIDMSSPNIAKPMSMGHLRSTVIGNSIAKTLEKVGYTPIKINYLGDYGTQFGKLITAYRLWGNEEDVKKDPITNLFHYY 191
Cdd:pfam00750 21 VVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQFGMLIAGLEKYQDEKTLQEMPIQDLEDFY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 192 VKFHEEAEKDPKLEDEGRAAFKKLENGDEEEIKLWKWFREVSLQEFNRIYKELGVTFdSYNGEAFFNDKMQPVVDELREK 271
Cdd:pfam00750 101 REAKKHYDEEEEFAERARNYVVKLQSGDEYWRRMWKLIVDITMTQNQRLYDRLDVTL-TEMGESLYNPMMNEIVKDFKKN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 272 GLLEESRGAQVVNLGE--DENPALILKSDGSSLYMTRDLAAALYRKKEYDFVMSLYVAGGEQTGHFKQLKQVLKKMGYDW 349
Cdd:pfam00750 180 GLVVEIDGALVVFLDEfgKPMGVIVQKSDGGYLYTTTDIAAAKYRYETLHADRMLYVIDSRQSQHMQQAFAILRKAGYVP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 350 -SDNIHHIPFGLI-TQGGKKLSTRKGNVVFLDQVLKDAVSLAEQQIEEKNPN----LSNKKQVAHDVGVGAVVFHDLKND 423
Cdd:pfam00750 260 eSKDLEHINFGMVlGKDGKPFKTRKGGTVKLADLLDEALERALQLIMEKNKDkilqADELEAVADAVGIGAIKYADLSKN 339
|
....*...
gi 560182726 424 RMDNFDFD 431
Cdd:pfam00750 340 RTNDYIFD 347
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
114-373 |
4.18e-63 |
|
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: 205.88 E-value: 4.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 114 IDMSSPNIAKPMSMGHLRSTVIGNSIAKTLEKVGYTPIKINYLGDYGTQFGKLITAYrlwgneedvkkdpitnlfhyyvk 193
Cdd:cd00671 4 VEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSL----------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 194 fheeaekdpkledegraafkklengdeeeiKLWKWFREVSLQEFNRIYKELGVTFDSYNGEAFFNDKMQPVVDELREKGL 273
Cdd:cd00671 61 ------------------------------EKWRKLVEESIKADLETYGRLDVRFDVWFGESSYLGLMGKVVELLEELGL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 274 LEESRGAQVVNLGE--DENPALILKSDGSSLYMTRDLAAALYrKKEYDFVMSLYVAGGEQTGHFKQLKQVLKKMGYDWSD 351
Cdd:cd00671 111 LYEEDGALWLDLTEfgDDKDRVLVRSDGTYTYFTRDIAYHLD-KFERGADKIIYVVGADHHGHFKRLFAALELLGYDEAK 189
|
250 260
....*....|....*....|...
gi 560182726 352 NIHHIPFGLIT-QGGKKLSTRKG 373
Cdd:cd00671 190 KLEHLLYGMVNlPKEGKMSTRAG 212
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
446-558 |
3.73e-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: 130.78 E-value: 3.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 446 VQYTNARAQSILRKAN------KEISMDNLS-LNDDWSFAVAKALADFPAIVEKASEKFEPSIIAKYALDLSKKFNKYYA 518
Cdd:smart00836 1 VQYAHARICSILRKAGeagetlPDIADADLSlLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYN 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 560182726 519 NVRILDEDN--QLNARLALVQATSIVLTEALRLLGVNAPKEM 558
Cdd:smart00836 81 RVRVLGEENpeLRKARLALLKAVRQVLANGLRLLGISAPERM 122
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
1-558 |
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: 673.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 1 MDFKQKVVDLVSE---QVDLPKEKISMLIERPKNPKMGDYA-FPAFALAKIEHKNPALIAKDIAEKIS-DDNFTSIQAVG 75
Cdd:COG0018 1 MNIKEELAEAIAAalaALGAGLEEPDILVERPKDPEHGDYAtNVAMQLAKPLKKNPREIAEEIAEALDaDPLVEKVEIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 76 P-YVNFAIDHAKLVnATLNDVLTEKEHFGDQKLGEG-NVPIDMSSPNIAKPMSMGHLRSTVIGNSIAKTLEKVGYTPIKI 153
Cdd:COG0018 81 PgFINFFLSPAALA-AVLKEILADGEDYGRSDAGKGkKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYDVTRE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 154 NYLGDYGTQFGKLITAYRLWGNEE-DVKKDPITNLFHYYVKFHEEAEKDPKLEDEGRAAFKKLENGDEEEIKLWKWFREV 232
Cdd:COG0018 160 NYINDAGTQIGKLALSLERYGEEEiEPESKPDGYLGDLYVKFHKEYEEDPELEDIARELLAKLEPGDEEALELWKKAVDW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 233 SLQEFNRIYKELGVTFDSYNGEAFFNDK--MQPVVDELREKGLLEESRGAQVVNLGE--DENPALILKSDGSSLYMTRDL 308
Cdd:COG0018 240 SLEEIKEDLKRLGVEFDVWFSESSLYDSgaVEEVVEELKEKGLLYESDGALWVRLTEfgDDKDRVLVKSDGTYTYFTTDI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 309 AAALYRKKEYDFVMSLYVAGGEQTGHFKQLKQVLKKMGYDWSDNIHHIPFGLIT-QGGKKLSTRKGNVVFLDQVLKDAVS 387
Cdd:COG0018 320 AYHLYKFERYGFDRVIYVVGADQHGHFKRLFAALKALGYDPAKDLEHLLFGMVNlRDGEKMSTRAGTVVTLDDLLDEAVE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 388 LAEQQIEEKnpNLSNKKQVAHDVGVGAVVFHDLKNDRMDNFDFDLEEVVRFEGDTGPYVQYTNARAQSILRKANKEISM- 466
Cdd:COG0018 400 RAREIIEEK--SEEEKEEIAEQVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNTNPYVQYAHARICSILRKAGEELDGl 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 467 ---DNLSLNDDWSFAVAKALADFPAIVEKASEKFEPSIIAKYALDLSKKFNKYYANVRILDEDN--QLNARLALVQATSI 541
Cdd:COG0018 478 aeaDLSLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRILKAEDeeLRAARLALVAATAQ 557
|
570
....*....|....*..
gi 560182726 542 VLTEALRLLGVNAPKEM 558
Cdd:COG0018 558 VLKNGLGLLGISAPERM 574
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
1-558 |
0e+00 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 543.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 1 MDFKQKVVDLVSEQVD--LPKEKISMLIERPKNPKMGDYAFP-AFALAKIEHKNPALIAKDIAEKISddnftSIQAVGP- 76
Cdd:PRK01611 3 MDIKELLAEALAAALEagGLPELPAVLIERPKDPEHGDYATNvAMQLAKKLKKNPREIAEEIVEAIE-----KVEIAGPg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 77 YVNFAIDHAKLvNATLNDVLTEKEHFGDQKLGEG-NVPIDMSSPNIAKPMSMGHLRSTVIGNSIAKTLEKVGYTPIKINY 155
Cdd:PRK01611 78 FINFFLDPAAL-AELVLAILEAGERYGRSDIGKGkKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDVTREYY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 156 LGDYGTQFGKLITAYRlwgneedvkkdpitnlfhyyvkfheeaekdpkledegraafkklengdeeeiKLWKWFREVSLQ 235
Cdd:PRK01611 157 VNDAGTQIGMLIASLE----------------------------------------------------LLWRKAVDISLD 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 236 EFNRIYKELGVTFDSY--NGEAFFNDKMQPVVDELREKGLL-EESRGAQVVNLGE--DENPALILKSDGSSLYMTRDLAA 310
Cdd:PRK01611 185 EIKEDLDRLGVHFDVWfsESELYYNGKVDEVVEDLKEKGLLyVESDGALWVRLTEfgDDKDRVLIKSDGTYTYFTRDIAY 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 311 ALYRKKEYDFVmsLYVAGGEQTGHFKQLKQVLKKMGYDWS--DNIHHIPFGLITQG-GKKLSTRKGNVVFLDQVLKDAVS 387
Cdd:PRK01611 265 HLYKFERFDRV--IYVVGADHHGHFKRLKAALKALGYDPDalEVLLHQMVGLVRGGeGVKMSTRAGNVVTLDDLLDEAVG 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 388 LAEQQIEEKnpnlsnkkQVAHDVGVGAVVFHDLKNDRMDNFDFDLEEVVRFEGDTGPYVQYTNARAQSILRKANKE-ISM 466
Cdd:PRK01611 343 RARELIEEK--------EIAEAVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPPYVQYAHARICSILRKAAEAgIDL 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 467 DNLSLNDDWSFAVAKALADFPAIVEKASEKFEPSIIAKYALDLSKKFNKYYANVRILDEDNQL-NARLALVQATSIVLTE 545
Cdd:PRK01611 415 LLALLTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYNRVLLKDEEEELrNARLALVKATAQVLKN 494
|
570
....*....|...
gi 560182726 546 ALRLLGVNAPKEM 558
Cdd:PRK01611 495 GLDLLGISAPERM 507
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
18-558 |
1.65e-146 |
|
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: 433.31 E-value: 1.65e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 18 PKEKISMLIERPKNPKMGDYAFP-AFALAKIEHKNPALIAKDIAEKISDDNFT-SIQAVGPYVNFAIDHAKLVNATLNDV 95
Cdd:TIGR00456 18 LSKESEILVEETPNPEFGDYASNiAFPLAKVLKKAPRQIAEEIVLKLKTGEIIeKVEAAGPFINFFLSPQKLLERLIQKI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 96 LTEKEHFGDQKLGEGNVPIDMSSPNIAKPMSMGHLRSTVIGNSIAKTLEKVGYTPIKINYLGDYGTQFGKLITAYRLWGN 175
Cdd:TIGR00456 98 LTQKEKYGSKKLKNKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYVNDWGRQFGLLALGVEKFGN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 176 EEDVK--KDPITNLFHYYVKFHEEAEKDPKLEDEGRAAFKKLENGDEEEIKLWKWFREVSLQEFNRIYKELGVTFDSY-- 251
Cdd:TIGR00456 178 EALNIavKKPDHGLEGFYVEINKRLEENEELEEEARELFVKLESGDEETIKLWKRLVEYSLEGIKETYDRLNIHFDSFvw 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 252 NGEAFFNDKMQPVVDELREKGLLEESrGAQVVNLGE--DENPALILKSDGSSLYMTRDLAAALYRKKEyDFVMSLYVAGG 329
Cdd:TIGR00456 258 EGESVKNGMLPKVLEDLKEKGLVVED-GALWLDLTLfgDKKDRVLQKSDGTYLYLTTDIAYHLDKLER-GFDKMIYVWGS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 330 EQTGHFKQLKQVLKKMGYdWSDNIHHIPFGLITqgGKKLSTRKGNVVFLDQVLKDAVSLAEQQIEEKNpNLSNKKqVAHD 409
Cdd:TIGR00456 336 DHHLHIAQMFAILEKLGY-KKKELEHLNFGMVP--LYSMKTRRGNVISLDNLLDEASKRAGNVITIKN-DLEEEK-VADA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 410 VGVGAVVFHDLKNDRMDNFDFDLEEVVRFEGDTGPYVQYTNARAQSILRKAN----KEISMDNLSLNDDwSFAVAKALAD 485
Cdd:TIGR00456 411 VGIGAVRYFDLSKNRTTDYVFDWDAMLSFEGNTAPYIQYAHARICSILRKAEidgeKLIADDFELLEEK-EKELLKLLLQ 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 560182726 486 FPAIVEKASEKFEPSIIAKYALDLSKKFNKYYANVRILDEDNQL-NARLALVQATSIVLTEALRLLGVNAPKEM 558
Cdd:TIGR00456 490 FPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACPVLDAENELaAARLALLKATRQTLKNGLDLLGIEPPERM 563
|
|
| PLN02286 |
PLN02286 |
arginine-tRNA ligase |
5-552 |
4.66e-107 |
|
arginine-tRNA ligase
Pssm-ID: 215160 [Multi-domain] Cd Length: 576 Bit Score: 332.38 E-value: 4.66e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 5 QKVVDLVSE--QVDLPKE-KISMLIERPKNPKMGDY----AFPAFALAK---IEHKNPALIAKDIAEKISDDNFT-SIQA 73
Cdd:PLN02286 1 RELAKLFEAslRLTVPDEpSVEPLVAACTNPKFGDYqcnnAMGLWSKLKgkgTSFKNPRAVAQAIVKNLPASEMIeSTSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 74 VGP-YVNFAIDhAKLVNATLNDVLTEKEHFGDQKLGEGNVPIDMSSPNIAKPMSMGHLRSTVIGNSIAKTLEKVGYTPIK 152
Cdd:PLN02286 81 AGPgFVNVRLS-ASWLAKRIERMLVDGIDTWAPTLPVKRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEFSGVEVLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 153 INYLGDYGTQFGKLITAYR-LWGNEEDVKKDPITNLFHYYVKFHEEAEKDPKLEDEGRAAFKKLENGDEEEIKLWKWFRE 231
Cdd:PLN02286 160 RNHVGDWGTQFGMLIEHLFeKFPNWESVSDQAIGDLQEFYKAAKKRFDEDEEFKARAQQAVVRLQGGDPEYRAAWAKICE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 232 VSLQEFNRIYKELGVTFDSyNGEAFFNDKMQPVVDELREKGLLEESRGAQVVNLGEDENPALILKSDGSSLYMTRDLAAA 311
Cdd:PLN02286 240 ISRREFEKVYQRLRVELEE-KGESFYNPYIPGVIEELESKGLVVESDGARVIFVEGFDIPLIVVKSDGGFNYASTDLAAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 312 LYRKKEYDFVMSLYVAGGEQTGHFKQLKQVLKKMGydWSDN-----IHHIPFGLItQG--GKKLSTRKGNVVFLDQVLKD 384
Cdd:PLN02286 319 WYRLNEEKAEWIIYVTDVGQQQHFDMVFKAAKRAG--WLPEdtyprLEHVGFGLV-LGedGKRFRTRSGEVVRLVDLLDE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 385 AVSLAEQQIEEKNP--NLSNK--KQVAHDVGVGAVVFHDLKNDRMDNFDFDLEEVVRFEGDTGPYVQYTNARAQSILRKA 460
Cdd:PLN02286 396 AKSRSKAALIERGKdsEWTPEelEQAAEAVGYGAVKYADLKNNRLTNYTFSFDQMLDLKGNTAVYLLYAHARICSIIRKS 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 461 NKEI----SMDNLSLNDDWSFAVAKALADFPAIVEKASEKFEPSIIAKYALDLSKKFNKYYANVRILDEDNQlNARLALV 536
Cdd:PLN02286 476 GKDIdelkKTGKIVLDHPDERALGLHLLQFPEVVEEACTDLLPNRLCEYLYNLSEKFTKFYSNCKVNGSEEE-TSRLLLC 554
|
570
....*....|....*.
gi 560182726 537 QATSIVLTEALRLLGV 552
Cdd:PLN02286 555 EATAIVMRKCFHLLGI 570
|
|
| tRNA-synt_1d |
pfam00750 |
tRNA synthetases class I (R); Other tRNA synthetase sub-families are too dissimilar to be ... |
112-431 |
2.59e-87 |
|
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: 273.68 E-value: 2.59e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 112 VPIDMSSPNIAKPMSMGHLRSTVIGNSIAKTLEKVGYTPIKINYLGDYGTQFGKLITAYRLWGNEEDVKKDPITNLFHYY 191
Cdd:pfam00750 21 VVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQFGMLIAGLEKYQDEKTLQEMPIQDLEDFY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 192 VKFHEEAEKDPKLEDEGRAAFKKLENGDEEEIKLWKWFREVSLQEFNRIYKELGVTFdSYNGEAFFNDKMQPVVDELREK 271
Cdd:pfam00750 101 REAKKHYDEEEEFAERARNYVVKLQSGDEYWRRMWKLIVDITMTQNQRLYDRLDVTL-TEMGESLYNPMMNEIVKDFKKN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 272 GLLEESRGAQVVNLGE--DENPALILKSDGSSLYMTRDLAAALYRKKEYDFVMSLYVAGGEQTGHFKQLKQVLKKMGYDW 349
Cdd:pfam00750 180 GLVVEIDGALVVFLDEfgKPMGVIVQKSDGGYLYTTTDIAAAKYRYETLHADRMLYVIDSRQSQHMQQAFAILRKAGYVP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 350 -SDNIHHIPFGLI-TQGGKKLSTRKGNVVFLDQVLKDAVSLAEQQIEEKNPN----LSNKKQVAHDVGVGAVVFHDLKND 423
Cdd:pfam00750 260 eSKDLEHINFGMVlGKDGKPFKTRKGGTVKLADLLDEALERALQLIMEKNKDkilqADELEAVADAVGIGAIKYADLSKN 339
|
....*...
gi 560182726 424 RMDNFDFD 431
Cdd:pfam00750 340 RTNDYIFD 347
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
114-373 |
4.18e-63 |
|
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: 205.88 E-value: 4.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 114 IDMSSPNIAKPMSMGHLRSTVIGNSIAKTLEKVGYTPIKINYLGDYGTQFGKLITAYrlwgneedvkkdpitnlfhyyvk 193
Cdd:cd00671 4 VEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSL----------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 194 fheeaekdpkledegraafkklengdeeeiKLWKWFREVSLQEFNRIYKELGVTFDSYNGEAFFNDKMQPVVDELREKGL 273
Cdd:cd00671 61 ------------------------------EKWRKLVEESIKADLETYGRLDVRFDVWFGESSYLGLMGKVVELLEELGL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 274 LEESRGAQVVNLGE--DENPALILKSDGSSLYMTRDLAAALYrKKEYDFVMSLYVAGGEQTGHFKQLKQVLKKMGYDWSD 351
Cdd:cd00671 111 LYEEDGALWLDLTEfgDDKDRVLVRSDGTYTYFTRDIAYHLD-KFERGADKIIYVVGADHHGHFKRLFAALELLGYDEAK 189
|
250 260
....*....|....*....|...
gi 560182726 352 NIHHIPFGLIT-QGGKKLSTRKG 373
Cdd:cd00671 190 KLEHLLYGMVNlPKEGKMSTRAG 212
|
|
| Anticodon_Ia_Arg |
cd07956 |
Anticodon-binding domain of arginyl tRNA synthetases; This domain is found in arginyl tRNA ... |
410-558 |
1.84e-56 |
|
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: 186.27 E-value: 1.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 410 VGVGAVVFHDLKNDRMDNFDFDLEEVVRFEGDTGPYVQYTNARAQSILRKANKEIS----MDNLSLNDDWSFAVAKALAD 485
Cdd:cd07956 3 VGVGAVKYQDLSNKRIKDYTFDWERMLSFEGDTGPYLQYAHARLCSILRKAGETIEaeadADLSLLPEPDERDLILLLAK 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 560182726 486 FPAIVEKASEKFEPSIIAKYALDLSKKFNKYYANVRILDEDNQL-NARLALVQATSIVLTEALRLLGVNAPKEM 558
Cdd:cd07956 83 FPEVVKNAAETLEPHTIATYLFDLAHAFSKFYNACPVLGAEEELrNARLALVAAARQVLANGLDLLGIEAPERM 156
|
|
| DALR_1 |
pfam05746 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
446-558 |
5.47e-37 |
|
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: 133.16 E-value: 5.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 446 VQYTNARAQSILRKANK---EISMDNLSLNDDWSFAVAKALADFPAIVEKASEKFEPSIIAKYALDLSKKFNKYYANVRI 522
Cdd:pfam05746 1 LQYAHARICSILRKAGElgiNLDIDADLLTEEEEKELLKALLQFPEVLEEAAEELEPHRLANYLYELASAFHSFYNNCRV 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 560182726 523 LDEDNQ-LNARLALVQATSIVLTEALRLLGVNAPKEM 558
Cdd:pfam05746 81 LDEDNEeRNARLALLKAVRQVLKNGLDLLGIEAPEKM 117
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
446-558 |
3.73e-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: 130.78 E-value: 3.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 446 VQYTNARAQSILRKAN------KEISMDNLS-LNDDWSFAVAKALADFPAIVEKASEKFEPSIIAKYALDLSKKFNKYYA 518
Cdd:smart00836 1 VQYAHARICSILRKAGeagetlPDIADADLSlLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYN 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 560182726 519 NVRILDEDN--QLNARLALVQATSIVLTEALRLLGVNAPKEM 558
Cdd:smart00836 81 RVRVLGEENpeLRKARLALLKAVRQVLANGLRLLGISAPERM 122
|
|
| Arg_tRNA_synt_N |
pfam03485 |
Arginyl tRNA synthetase N terminal domain; This domain is found at the amino terminus of ... |
3-80 |
8.21e-18 |
|
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: 78.04 E-value: 8.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 3 FKQKVVDLVSEQVDLPKEKISMLIERPKNPKMGDYAFP-AFALAKIEHKNPALIAKDIAEKIS-DDNFTSIQAVGP-YVN 79
Cdd:pfam03485 1 LKKAIAKALSKLGGPDLELIDIVIETPKNPKFGDYATNvAMQLAKKLKKNPREIAEEIAEKLEkSDIIEKVEVAGPgFIN 80
|
.
gi 560182726 80 F 80
Cdd:pfam03485 81 F 81
|
|
| Arg_tRNA_synt_N |
smart01016 |
Arginyl tRNA synthetase N terminal dom; This domain is found at the amino terminus of Arginyl ... |
1-80 |
1.51e-16 |
|
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: 74.54 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560182726 1 MDFKQKVVDLVSEQVDLPKEKISMLIERPKNPKMGDYAFP-AFALAKIEHKNPALIAKDIAEKIS-DDNFTSIQAVGP-Y 77
Cdd:smart01016 1 DLLKEAIAEALKKALGVEGEPIDIALERPKDPDHGDYATNvAFRLAKKLKKNPRELAEEIAEKLPkSDLVEKVEIAGPgF 80
|
...
gi 560182726 78 VNF 80
Cdd:smart01016 81 INF 83
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
117-166 |
1.47e-05 |
|
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: 45.16 E-value: 1.47e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 560182726 117 SSPNIAKPMSMGHLRSTVIGNSIAKTLEKVGYTPIKINYLGDYGTQFGKL 166
Cdd:cd00802 4 SGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDP 53
|
|
| |
