|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02286 |
PLN02286 |
arginine-tRNA ligase |
80-660 |
0e+00 |
|
arginine-tRNA ligase
Pssm-ID: 215160 [Multi-domain] Cd Length: 576 Bit Score: 744.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 80 LQEVFGHAIKAAYPDLENPPLLVTPSQQAKFGDYQCNSAMGISQMLKTKE-QKVNPREIAENITKHLPDNECIEKVEIAG 158
Cdd:PLN02286 3 LAKLFEASLRLTVPDEPSVEPLVAACTNPKFGDYQCNNAMGLWSKLKGKGtSFKNPRAVAQAIVKNLPASEMIESTSVAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 159 PGFINVHLRKDFVSEQLTSLLVNGVQLPA-LGENKKVIVDFSSPNIAKEMHVGHLRSTIIGESISRLFEFAGYDVLRLNH 237
Cdd:PLN02286 83 PGFVNVRLSASWLAKRIERMLVDGIDTWApTLPVKRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEFSGVEVLRRNH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 238 VGDWGTQFGMLIAHLQDKFPDYLTVSP-PIGDLQVFYKESKKRFDTEEEFKKRAYQCVVLLQGKNPDITKAWKLICDVSR 316
Cdd:PLN02286 163 VGDWGTQFGMLIEHLFEKFPNWESVSDqAIGDLQEFYKAAKKRFDEDEEFKARAQQAVVRLQGGDPEYRAAWAKICEISR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 317 QELNKIYDALDVSLIERGESFYQDRMNDIVKEFEDRGFVQVDDGRKIVFVPGCSIPLTIVKSDGGYTYDTSDLAAIKQRL 396
Cdd:PLN02286 243 REFEKVYQRLRVELEEKGESFYNPYIPGVIEELESKGLVVESDGARVIFVEGFDIPLIVVKSDGGFNYASTDLAALWYRL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 397 FEEKADMIIYVVDNGQSVHFQTIFAAAQMIGWY-DPKVTRVFHAGFGVVLGEDKKKFKTRSGETVRLMDLLGEGLKRSMD 475
Cdd:PLN02286 323 NEEKAEWIIYVTDVGQQQHFDMVFKAAKRAGWLpEDTYPRLEHVGFGLVLGEDGKRFRTRSGEVVRLVDLLDEAKSRSKA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 476 KLKEKERDKVLTAEELNAAQTSVAYGCIKYADLSHNRLNDYIFSFDKMLDDRGNTAAYLLYAFTRIRSIARLANIDEEML 555
Cdd:PLN02286 403 ALIERGKDSEWTPEELEQAAEAVGYGAVKYADLKNNRLTNYTFSFDQMLDLKGNTAVYLLYAHARICSIIRKSGKDIDEL 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 556 QKAareTKILLDHEKEWKLGRCILRFPEILQKILDDLFLHTLCDYIYELATAFTEFYDSCYCVEKDRQTGkilkvnmwRM 635
Cdd:PLN02286 483 KKT---GKIVLDHPDERALGLHLLQFPEVVEEACTDLLPNRLCEYLYNLSEKFTKFYSNCKVNGSEEETS--------RL 551
|
570 580
....*....|....*....|....*
gi 15149476 636 LLCEAVAAVMAKGFDILGIKPVQRM 660
Cdd:PLN02286 552 LLCEATAIVMRKCFHLLGITPLYRL 576
|
|
| tRNA-synt_1d |
pfam00750 |
tRNA synthetases class I (R); Other tRNA synthetase sub-families are too dissimilar to be ... |
174-520 |
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: 593.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 174 QLTSLLVNGVQLPALGENKKVIVDFSSPNIAKEMHVGHLRSTIIGESISRLFEFAGYDVLRLNHVGDWGTQFGMLIAHLQ 253
Cdd:pfam00750 1 TVPNALLQKGLGKASREKKKVVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQFGMLIAGLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 254 DKFPDYLTVSPPIGDLQVFYKESKKRFDTEEEFKKRAYQCVVLLQGKNPDITKAWKLICDVSRQELNKIYDALDVSLIER 333
Cdd:pfam00750 81 KYQDEKTLQEMPIQDLEDFYREAKKHYDEEEEFAERARNYVVKLQSGDEYWRRMWKLIVDITMTQNQRLYDRLDVTLTEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 334 GESFYQDRMNDIVKEFEDRGFVQVDDGRKIVFVP--GCSIPLTIVKSDGGYTYDTSDLAAIKQRLFEEKADMIIYVVDNG 411
Cdd:pfam00750 161 GESLYNPMMNEIVKDFKKNGLVVEIDGALVVFLDefGKPMGVIVQKSDGGYLYTTTDIAAAKYRYETLHADRMLYVIDSR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 412 QSVHFQTIFAAAQMIGwYDPKVTRVFHAGFGVVLGEDKKKFKTRSGETVRLMDLLGEGLKRSMDKLKEKERDKVLTAEEL 491
Cdd:pfam00750 241 QSQHMQQAFAILRKAG-YVPESKDLEHINFGMVLGKDGKPFKTRKGGTVKLADLLDEALERALQLIMEKNKDKILQADEL 319
|
330 340
....*....|....*....|....*....
gi 15149476 492 NAAQTSVAYGCIKYADLSHNRLNDYIFSF 520
Cdd:pfam00750 320 EAVADAVGIGAIKYADLSKNRTNDYIFDW 348
|
|
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
75-660 |
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: 565.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 75 NIISRLQEVFGHAIKAAYPDLENPPLLVTPSQQAKFGDYQCNSAMGISqmlktKEQKVNPREIAENITKHLPDNECIEKV 154
Cdd:COG0018 2 NIKEELAEAIAAALAALGAGLEEPDILVERPKDPEHGDYATNVAMQLA-----KPLKKNPREIAEEIAEALDADPLVEKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 155 EIAGPGFINVHLRKDFVSEQLTSLLVNGVQL--PALGENKKVIVDFSSPNIAKEMHVGHLRSTIIGESISRLFEFAGYDV 232
Cdd:COG0018 77 EIAGPGFINFFLSPAALAAVLKEILADGEDYgrSDAGKGKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYDV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 233 LRLNHVGDWGTQFGMLIAHLQDKFPDYLTV-SPPIGDLQVFYKESKKRFDTEEEFKKRAYQCVVLLQGKNPDITKAWKLI 311
Cdd:COG0018 157 TRENYINDAGTQIGKLALSLERYGEEEIEPeSKPDGYLGDLYVKFHKEYEEDPELEDIARELLAKLEPGDEEALELWKKA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 312 CDVSRQELNKIYDALDVSL-IERGESFYQD--RMNDIVKEFEDRGFVQVDDGRKIVFVP--GCSIPLTIVKSDGGYTYDT 386
Cdd:COG0018 237 VDWSLEEIKEDLKRLGVEFdVWFSESSLYDsgAVEEVVEELKEKGLLYESDGALWVRLTefGDDKDRVLVKSDGTYTYFT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 387 SDLAAIKQRLFEEKADMIIYVVDNGQSVHFQTIFAAAQMIGWydPKVTRVFHAGFGVVLGEDKKKFKTRSGETVRLMDLL 466
Cdd:COG0018 317 TDIAYHLYKFERYGFDRVIYVVGADQHGHFKRLFAALKALGY--DPAKDLEHLLFGMVNLRDGEKMSTRAGTVVTLDDLL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 467 GEGLKRSMDKLKEKerdkvlTAEELNAAQTSVAYGCIKYADLSHNRLNDYIFSFDKMLDDRGNTAAYLLYAFTRIRSIAR 546
Cdd:COG0018 395 DEAVERAREIIEEK------SEEEKEEIAEQVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNTNPYVQYAHARICSILR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 547 LAnidEEMLQKAARETKILLDHEKEWKLGRCILRFPEILQKILDDLFLHTLCDYIYELATAFTEFYDSCycvekdrqtgK 626
Cdd:COG0018 469 KA---GEELDGLAEADLSLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNAC----------R 535
|
570 580 590
....*....|....*....|....*....|....*....
gi 15149476 627 ILKVN-----MWRMLLCEAVAAVMAKGFDILGIKPVQRM 660
Cdd:COG0018 536 ILKAEdeelrAARLALVAATAQVLKNGLGLLGISAPERM 574
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
76-660 |
9.31e-137 |
|
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: 412.12 E-value: 9.31e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 76 IISRLQEVFGHA-IKAAYPDLENPPLLVTPSQQakFGDYQCNSAMGISqmlktKEQKVNPREIAENITKHLPDNECIEKV 154
Cdd:TIGR00456 1 IKTLLKEEISQAlLKAGLSKESEILVEETPNPE--FGDYASNIAFPLA-----KVLKKAPRQIAEEIVLKLKTGEIIEKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 155 EIAGPgFINVHLRKDFVSEQLTSLLVN-----GVQLPalgENKKVIVDFSSPNIAKEMHVGHLRSTIIGESISRLFEFAG 229
Cdd:TIGR00456 74 EAAGP-FINFFLSPQKLLERLIQKILTqkekyGSKKL---KNKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 230 YDVLRLNHVGDWGTQFGMLIAHLQDKFPDYLT--VSPPIGDLQVFYKESKKRFDTEEEFKKRAYQCVVLLQGKNPDITKA 307
Cdd:TIGR00456 150 YDVIREYYVNDWGRQFGLLALGVEKFGNEALNiaVKKPDHGLEGFYVEINKRLEENEELEEEARELFVKLESGDEETIKL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 308 WKLICDVSRQELNKIYDALDVSLIER---GESFYQDRMNDIVKEFEDRGFVqVDDGRKIVFVPGCSI--PLTIVKSDGGY 382
Cdd:TIGR00456 230 WKRLVEYSLEGIKETYDRLNIHFDSFvweGESVKNGMLPKVLEDLKEKGLV-VEDGALWLDLTLFGDkkDRVLQKSDGTY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 383 TYDTSDLAAIKQRLfEEKADMIIYVVDNGQSVHFQTIFAAAQMIGwydPKVTRVFHAGFGVVLGedkKKFKTRSGETVRL 462
Cdd:TIGR00456 309 LYLTTDIAYHLDKL-ERGFDKMIYVWGSDHHLHIAQMFAILEKLG---YKKKELEHLNFGMVPL---YSMKTRRGNVISL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 463 MDLLGEGLKRSMDKLKEKERdkvltAEELNAAQtSVAYGCIKYADLSHNRLNDYIFSFDKMLDDRGNTAAYLLYAFTRIR 542
Cdd:TIGR00456 382 DNLLDEASKRAGNVITIKND-----LEEEKVAD-AVGIGAVRYFDLSKNRTTDYVFDWDAMLSFEGNTAPYIQYAHARIC 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 543 SIARLANIDEEMLQKAaretKILLDHEKEWKLGRCILRFPEILQKILDDLFLHTLCDYIYELATAFTEFYDSCycvekdr 622
Cdd:TIGR00456 456 SILRKAEIDGEKLIAD----DFELLEEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKAC------- 524
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 15149476 623 qtgKILK----VNMWRMLLCEAVAAVMAKGFDILGIKPVQRM 660
Cdd:TIGR00456 525 ---PVLDaeneLAAARLALLKATRQTLKNGLDLLGIEPPERM 563
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
193-457 |
2.89e-84 |
|
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: 263.66 E-value: 2.89e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 193 KVIVDFSSPNIAKEMHVGHLRSTIIGESISRLFEFAGYDVLRLNHVGDWGTQFGMLIAHLQDkfpdyltvsppigdlqvf 272
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSLEK------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 273 ykeskkrfdteeefkkrayqcvvllqgknpditkaWKLICDVSRQELNKIYDALDVSLIE-RGESFYQDRMNDIVKEFED 351
Cdd:cd00671 63 -----------------------------------WRKLVEESIKADLETYGRLDVRFDVwFGESSYLGLMGKVVELLEE 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 352 RGFVQVDDGRKIVFVP--GCSIPLTIVKSDGGYTYDTSDLAAIKQRlFEEKADMIIYVVDNGQSVHFQTIFAAAQMIGWY 429
Cdd:cd00671 108 LGLLYEEDGALWLDLTefGDDKDRVLVRSDGTYTYFTRDIAYHLDK-FERGADKIIYVVGADHHGHFKRLFAALELLGYD 186
|
250 260
....*....|....*....|....*...
gi 15149476 430 DPKvtRVFHAGFGVVLGEDKKKFKTRSG 457
Cdd:cd00671 187 EAK--KLEHLLYGMVNLPKEGKMSTRAG 212
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
534-660 |
2.23e-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: 123.84 E-value: 2.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 534 LLYAFTRIRSIARLANIDEEMLQKAARETKILLDHEKEWKLGRCILRFPEILQKILDDLFLHTLCDYIYELATAFTEFYD 613
Cdd:smart00836 1 VQYAHARICSILRKAGEAGETLPDIADADLSLLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYN 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15149476 614 SCYCVEKDRqtgKILKVNmwRMLLCEAVAAVMAKGFDILGIKPVQRM 660
Cdd:smart00836 81 RVRVLGEEN---PELRKA--RLALLKAVRQVLANGLRLLGISAPERM 122
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02286 |
PLN02286 |
arginine-tRNA ligase |
80-660 |
0e+00 |
|
arginine-tRNA ligase
Pssm-ID: 215160 [Multi-domain] Cd Length: 576 Bit Score: 744.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 80 LQEVFGHAIKAAYPDLENPPLLVTPSQQAKFGDYQCNSAMGISQMLKTKE-QKVNPREIAENITKHLPDNECIEKVEIAG 158
Cdd:PLN02286 3 LAKLFEASLRLTVPDEPSVEPLVAACTNPKFGDYQCNNAMGLWSKLKGKGtSFKNPRAVAQAIVKNLPASEMIESTSVAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 159 PGFINVHLRKDFVSEQLTSLLVNGVQLPA-LGENKKVIVDFSSPNIAKEMHVGHLRSTIIGESISRLFEFAGYDVLRLNH 237
Cdd:PLN02286 83 PGFVNVRLSASWLAKRIERMLVDGIDTWApTLPVKRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEFSGVEVLRRNH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 238 VGDWGTQFGMLIAHLQDKFPDYLTVSP-PIGDLQVFYKESKKRFDTEEEFKKRAYQCVVLLQGKNPDITKAWKLICDVSR 316
Cdd:PLN02286 163 VGDWGTQFGMLIEHLFEKFPNWESVSDqAIGDLQEFYKAAKKRFDEDEEFKARAQQAVVRLQGGDPEYRAAWAKICEISR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 317 QELNKIYDALDVSLIERGESFYQDRMNDIVKEFEDRGFVQVDDGRKIVFVPGCSIPLTIVKSDGGYTYDTSDLAAIKQRL 396
Cdd:PLN02286 243 REFEKVYQRLRVELEEKGESFYNPYIPGVIEELESKGLVVESDGARVIFVEGFDIPLIVVKSDGGFNYASTDLAALWYRL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 397 FEEKADMIIYVVDNGQSVHFQTIFAAAQMIGWY-DPKVTRVFHAGFGVVLGEDKKKFKTRSGETVRLMDLLGEGLKRSMD 475
Cdd:PLN02286 323 NEEKAEWIIYVTDVGQQQHFDMVFKAAKRAGWLpEDTYPRLEHVGFGLVLGEDGKRFRTRSGEVVRLVDLLDEAKSRSKA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 476 KLKEKERDKVLTAEELNAAQTSVAYGCIKYADLSHNRLNDYIFSFDKMLDDRGNTAAYLLYAFTRIRSIARLANIDEEML 555
Cdd:PLN02286 403 ALIERGKDSEWTPEELEQAAEAVGYGAVKYADLKNNRLTNYTFSFDQMLDLKGNTAVYLLYAHARICSIIRKSGKDIDEL 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 556 QKAareTKILLDHEKEWKLGRCILRFPEILQKILDDLFLHTLCDYIYELATAFTEFYDSCYCVEKDRQTGkilkvnmwRM 635
Cdd:PLN02286 483 KKT---GKIVLDHPDERALGLHLLQFPEVVEEACTDLLPNRLCEYLYNLSEKFTKFYSNCKVNGSEEETS--------RL 551
|
570 580
....*....|....*....|....*
gi 15149476 636 LLCEAVAAVMAKGFDILGIKPVQRM 660
Cdd:PLN02286 552 LLCEATAIVMRKCFHLLGITPLYRL 576
|
|
| tRNA-synt_1d |
pfam00750 |
tRNA synthetases class I (R); Other tRNA synthetase sub-families are too dissimilar to be ... |
174-520 |
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: 593.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 174 QLTSLLVNGVQLPALGENKKVIVDFSSPNIAKEMHVGHLRSTIIGESISRLFEFAGYDVLRLNHVGDWGTQFGMLIAHLQ 253
Cdd:pfam00750 1 TVPNALLQKGLGKASREKKKVVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQFGMLIAGLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 254 DKFPDYLTVSPPIGDLQVFYKESKKRFDTEEEFKKRAYQCVVLLQGKNPDITKAWKLICDVSRQELNKIYDALDVSLIER 333
Cdd:pfam00750 81 KYQDEKTLQEMPIQDLEDFYREAKKHYDEEEEFAERARNYVVKLQSGDEYWRRMWKLIVDITMTQNQRLYDRLDVTLTEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 334 GESFYQDRMNDIVKEFEDRGFVQVDDGRKIVFVP--GCSIPLTIVKSDGGYTYDTSDLAAIKQRLFEEKADMIIYVVDNG 411
Cdd:pfam00750 161 GESLYNPMMNEIVKDFKKNGLVVEIDGALVVFLDefGKPMGVIVQKSDGGYLYTTTDIAAAKYRYETLHADRMLYVIDSR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 412 QSVHFQTIFAAAQMIGwYDPKVTRVFHAGFGVVLGEDKKKFKTRSGETVRLMDLLGEGLKRSMDKLKEKERDKVLTAEEL 491
Cdd:pfam00750 241 QSQHMQQAFAILRKAG-YVPESKDLEHINFGMVLGKDGKPFKTRKGGTVKLADLLDEALERALQLIMEKNKDKILQADEL 319
|
330 340
....*....|....*....|....*....
gi 15149476 492 NAAQTSVAYGCIKYADLSHNRLNDYIFSF 520
Cdd:pfam00750 320 EAVADAVGIGAIKYADLSKNRTNDYIFDW 348
|
|
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
75-660 |
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: 565.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 75 NIISRLQEVFGHAIKAAYPDLENPPLLVTPSQQAKFGDYQCNSAMGISqmlktKEQKVNPREIAENITKHLPDNECIEKV 154
Cdd:COG0018 2 NIKEELAEAIAAALAALGAGLEEPDILVERPKDPEHGDYATNVAMQLA-----KPLKKNPREIAEEIAEALDADPLVEKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 155 EIAGPGFINVHLRKDFVSEQLTSLLVNGVQL--PALGENKKVIVDFSSPNIAKEMHVGHLRSTIIGESISRLFEFAGYDV 232
Cdd:COG0018 77 EIAGPGFINFFLSPAALAAVLKEILADGEDYgrSDAGKGKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYDV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 233 LRLNHVGDWGTQFGMLIAHLQDKFPDYLTV-SPPIGDLQVFYKESKKRFDTEEEFKKRAYQCVVLLQGKNPDITKAWKLI 311
Cdd:COG0018 157 TRENYINDAGTQIGKLALSLERYGEEEIEPeSKPDGYLGDLYVKFHKEYEEDPELEDIARELLAKLEPGDEEALELWKKA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 312 CDVSRQELNKIYDALDVSL-IERGESFYQD--RMNDIVKEFEDRGFVQVDDGRKIVFVP--GCSIPLTIVKSDGGYTYDT 386
Cdd:COG0018 237 VDWSLEEIKEDLKRLGVEFdVWFSESSLYDsgAVEEVVEELKEKGLLYESDGALWVRLTefGDDKDRVLVKSDGTYTYFT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 387 SDLAAIKQRLFEEKADMIIYVVDNGQSVHFQTIFAAAQMIGWydPKVTRVFHAGFGVVLGEDKKKFKTRSGETVRLMDLL 466
Cdd:COG0018 317 TDIAYHLYKFERYGFDRVIYVVGADQHGHFKRLFAALKALGY--DPAKDLEHLLFGMVNLRDGEKMSTRAGTVVTLDDLL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 467 GEGLKRSMDKLKEKerdkvlTAEELNAAQTSVAYGCIKYADLSHNRLNDYIFSFDKMLDDRGNTAAYLLYAFTRIRSIAR 546
Cdd:COG0018 395 DEAVERAREIIEEK------SEEEKEEIAEQVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNTNPYVQYAHARICSILR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 547 LAnidEEMLQKAARETKILLDHEKEWKLGRCILRFPEILQKILDDLFLHTLCDYIYELATAFTEFYDSCycvekdrqtgK 626
Cdd:COG0018 469 KA---GEELDGLAEADLSLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNAC----------R 535
|
570 580 590
....*....|....*....|....*....|....*....
gi 15149476 627 ILKVN-----MWRMLLCEAVAAVMAKGFDILGIKPVQRM 660
Cdd:COG0018 536 ILKAEdeelrAARLALVAATAQVLKNGLGLLGISAPERM 574
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
73-660 |
2.92e-163 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 478.11 E-value: 2.92e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 73 MINIISRLQEVFGHAIKAAYPDlENPPLLVTPSQQAKFGDYQCNSAMGISqmlktKEQKVNPREIAENITKHlpdnecIE 152
Cdd:PRK01611 2 MMDIKELLAEALAAALEAGGLP-ELPAVLIERPKDPEHGDYATNVAMQLA-----KKLKKNPREIAEEIVEA------IE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 153 KVEIAGPGFINVHLRKDFVSEQLTSLLVNGVQL--PALGENKKVIVDFSSPNIAKEMHVGHLRSTIIGESISRLFEFAGY 230
Cdd:PRK01611 70 KVEIAGPGFINFFLDPAALAELVLAILEAGERYgrSDIGKGKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 231 DVLRLNHVGDWGTQFGMLIAHLQdkfpdyltvsppigdlqvfykeskkrfdteeefkkrayqcvvllqgknpditKAWKL 310
Cdd:PRK01611 150 DVTREYYVNDAGTQIGMLIASLE----------------------------------------------------LLWRK 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 311 ICDVSRQELNKIYDALDVSLIE---RGESFYQDRMNDIVKEFEDRG-FVQVDDGRKIVFVP--GCSIPLTIVKSDGGYTY 384
Cdd:PRK01611 178 AVDISLDEIKEDLDRLGVHFDVwfsESELYYNGKVDEVVEDLKEKGlLYVESDGALWVRLTefGDDKDRVLIKSDGTYTY 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 385 DTSDLAAIKQRLfeEKADMIIYVVDNGQSVHFQTIFAAAQMIGWYDPKVTRVFHAGFGVVLGEDKKKFKTRSGETVRLMD 464
Cdd:PRK01611 258 FTRDIAYHLYKF--ERFDRVIYVVGADHHGHFKRLKAALKALGYDPDALEVLLHQMVGLVRGGEGVKMSTRAGNVVTLDD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 465 LLGEGLKRSMDKLKEKERDKVltaeelnaaqtsVAYGCIKYADLSHNRLNDYIFSFDKMLDDRGNTAAYLLYAFTRIRSI 544
Cdd:PRK01611 336 LLDEAVGRARELIEEKEIAEA------------VGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPPYVQYAHARICSI 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 545 ARLANIDEEMLQKAaretkiLLDHEKEWKLGRCILRFPEILQKILDDLFLHTLCDYIYELATAFTEFYDSCYCVEKDRqt 624
Cdd:PRK01611 404 LRKAAEAGIDLLLA------LLTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYNRVLLKDEEE-- 475
|
570 580 590
....*....|....*....|....*....|....*.
gi 15149476 625 gkilKVNMWRMLLCEAVAAVMAKGFDILGIKPVQRM 660
Cdd:PRK01611 476 ----ELRNARLALVKATAQVLKNGLDLLGISAPERM 507
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
76-660 |
9.31e-137 |
|
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: 412.12 E-value: 9.31e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 76 IISRLQEVFGHA-IKAAYPDLENPPLLVTPSQQakFGDYQCNSAMGISqmlktKEQKVNPREIAENITKHLPDNECIEKV 154
Cdd:TIGR00456 1 IKTLLKEEISQAlLKAGLSKESEILVEETPNPE--FGDYASNIAFPLA-----KVLKKAPRQIAEEIVLKLKTGEIIEKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 155 EIAGPgFINVHLRKDFVSEQLTSLLVN-----GVQLPalgENKKVIVDFSSPNIAKEMHVGHLRSTIIGESISRLFEFAG 229
Cdd:TIGR00456 74 EAAGP-FINFFLSPQKLLERLIQKILTqkekyGSKKL---KNKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 230 YDVLRLNHVGDWGTQFGMLIAHLQDKFPDYLT--VSPPIGDLQVFYKESKKRFDTEEEFKKRAYQCVVLLQGKNPDITKA 307
Cdd:TIGR00456 150 YDVIREYYVNDWGRQFGLLALGVEKFGNEALNiaVKKPDHGLEGFYVEINKRLEENEELEEEARELFVKLESGDEETIKL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 308 WKLICDVSRQELNKIYDALDVSLIER---GESFYQDRMNDIVKEFEDRGFVqVDDGRKIVFVPGCSI--PLTIVKSDGGY 382
Cdd:TIGR00456 230 WKRLVEYSLEGIKETYDRLNIHFDSFvweGESVKNGMLPKVLEDLKEKGLV-VEDGALWLDLTLFGDkkDRVLQKSDGTY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 383 TYDTSDLAAIKQRLfEEKADMIIYVVDNGQSVHFQTIFAAAQMIGwydPKVTRVFHAGFGVVLGedkKKFKTRSGETVRL 462
Cdd:TIGR00456 309 LYLTTDIAYHLDKL-ERGFDKMIYVWGSDHHLHIAQMFAILEKLG---YKKKELEHLNFGMVPL---YSMKTRRGNVISL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 463 MDLLGEGLKRSMDKLKEKERdkvltAEELNAAQtSVAYGCIKYADLSHNRLNDYIFSFDKMLDDRGNTAAYLLYAFTRIR 542
Cdd:TIGR00456 382 DNLLDEASKRAGNVITIKND-----LEEEKVAD-AVGIGAVRYFDLSKNRTTDYVFDWDAMLSFEGNTAPYIQYAHARIC 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 543 SIARLANIDEEMLQKAaretKILLDHEKEWKLGRCILRFPEILQKILDDLFLHTLCDYIYELATAFTEFYDSCycvekdr 622
Cdd:TIGR00456 456 SILRKAEIDGEKLIAD----DFELLEEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKAC------- 524
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 15149476 623 qtgKILK----VNMWRMLLCEAVAAVMAKGFDILGIKPVQRM 660
Cdd:TIGR00456 525 ---PVLDaeneLAAARLALLKATRQTLKNGLDLLGIEPPERM 563
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
193-457 |
2.89e-84 |
|
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: 263.66 E-value: 2.89e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 193 KVIVDFSSPNIAKEMHVGHLRSTIIGESISRLFEFAGYDVLRLNHVGDWGTQFGMLIAHLQDkfpdyltvsppigdlqvf 272
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSLEK------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 273 ykeskkrfdteeefkkrayqcvvllqgknpditkaWKLICDVSRQELNKIYDALDVSLIE-RGESFYQDRMNDIVKEFED 351
Cdd:cd00671 63 -----------------------------------WRKLVEESIKADLETYGRLDVRFDVwFGESSYLGLMGKVVELLEE 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 352 RGFVQVDDGRKIVFVP--GCSIPLTIVKSDGGYTYDTSDLAAIKQRlFEEKADMIIYVVDNGQSVHFQTIFAAAQMIGWY 429
Cdd:cd00671 108 LGLLYEEDGALWLDLTefGDDKDRVLVRSDGTYTYFTRDIAYHLDK-FERGADKIIYVVGADHHGHFKRLFAALELLGYD 186
|
250 260
....*....|....*....|....*...
gi 15149476 430 DPKvtRVFHAGFGVVLGEDKKKFKTRSG 457
Cdd:cd00671 187 EAK--KLEHLLYGMVNLPKEGKMSTRAG 212
|
|
| Anticodon_Ia_Arg |
cd07956 |
Anticodon-binding domain of arginyl tRNA synthetases; This domain is found in arginyl tRNA ... |
498-660 |
3.35e-37 |
|
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: 135.80 E-value: 3.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 498 VAYGCIKYADLSHNRLNDYIFSFDKMLDDRGNTAAYLLYAFTRIRSIARLANIDEEMLQKAAREtkiLLDHEKEWKLGRC 577
Cdd:cd07956 3 VGVGAVKYQDLSNKRIKDYTFDWERMLSFEGDTGPYLQYAHARLCSILRKAGETIEAEADADLS---LLPEPDERDLILL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 578 ILRFPEILQKILDDLFLHTLCDYIYELATAFTEFYDSCycvekdrqtgKILK----VNMWRMLLCEAVAAVMAKGFDILG 653
Cdd:cd07956 80 LAKFPEVVKNAAETLEPHTIATYLFDLAHAFSKFYNAC----------PVLGaeeeLRNARLALVAAARQVLANGLDLLG 149
|
....*..
gi 15149476 654 IKPVQRM 660
Cdd:cd07956 150 IEAPERM 156
|
|
| DALR_1 |
pfam05746 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
534-660 |
4.11e-34 |
|
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: 125.84 E-value: 4.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 534 LLYAFTRIRSIARLANIDEEmlqkAARETKILLDHEKEWKLGRCILRFPEILQKILDDLFLHTLCDYIYELATAFTEFYD 613
Cdd:pfam05746 1 LQYAHARICSILRKAGELGI----NLDIDADLLTEEEEKELLKALLQFPEVLEEAAEELEPHRLANYLYELASAFHSFYN 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15149476 614 SCYCVEKDRqtgkilKVNMWRMLLCEAVAAVMAKGFDILGIKPVQRM 660
Cdd:pfam05746 77 NCRVLDEDN------EERNARLALLKAVRQVLKNGLDLLGIEAPEKM 117
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
534-660 |
2.23e-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: 123.84 E-value: 2.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 534 LLYAFTRIRSIARLANIDEEMLQKAARETKILLDHEKEWKLGRCILRFPEILQKILDDLFLHTLCDYIYELATAFTEFYD 613
Cdd:smart00836 1 VQYAHARICSILRKAGEAGETLPDIADADLSLLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYN 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15149476 614 SCYCVEKDRqtgKILKVNmwRMLLCEAVAAVMAKGFDILGIKPVQRM 660
Cdd:smart00836 81 RVRVLGEEN---PELRKA--RLALLKAVRQVLANGLRLLGISAPERM 122
|
|
| Arg_tRNA_synt_N |
smart01016 |
Arginyl tRNA synthetase N terminal dom; This domain is found at the amino terminus of Arginyl ... |
79-166 |
4.36e-25 |
|
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: 99.20 E-value: 4.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 79 RLQEVFGHAIKAAYPDLENPP-LLVTPSQQAKFGDYQCNSAMGISqmlktKEQKVNPREIAENITKHLPDNECIEKVEIA 157
Cdd:smart01016 2 LLKEAIAEALKKALGVEGEPIdIALERPKDPDHGDYATNVAFRLA-----KKLKKNPRELAEEIAEKLPKSDLVEKVEIA 76
|
....*....
gi 15149476 158 GPGFINVHL 166
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 ... |
80-166 |
2.91e-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: 96.92 E-value: 2.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149476 80 LQEVFGHAI-KAAYPDLENPPLLVTPSQQAKFGDYQCNSAMGISqmlktKEQKVNPREIAENITKHLPDNECIEKVEIAG 158
Cdd:pfam03485 1 LKKAIAKALsKLGGPDLELIDIVIETPKNPKFGDYATNVAMQLA-----KKLKKNPREIAEEIAEKLEKSDIIEKVEVAG 75
|
....*...
gi 15149476 159 PGFINVHL 166
Cdd:pfam03485 76 PGFINFFL 83
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
196-246 |
3.72e-08 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 52.87 E-value: 3.72e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 15149476 196 VDFSSPNIAKEMHVGHLRSTIIGESISRLFEFAGYDVLRLNHVGDWGTQFG 246
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIG 51
|
|
| |
