|
Name |
Accession |
Description |
Interval |
E-value |
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
4-554 |
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: 595.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 4 EELSEAIALALEEtissgqltLVEGAELPAVRVERPKSREHGDWATNVALQLAKKVGKNPREAAALLAEKISAIPGVASV 83
Cdd:COG0018 5 EELAEAIAAALAA--------LGAGLEEPDILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDADPLVEKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 84 DIAGPGFLNITLDAAAAGELAATIVEAGEAYGRSDKFAGKTINLEFVSANPTGPIHLGGTRWAAVGDALARVLEAEGANV 163
Cdd:COG0018 77 EIAGPGFINFFLSPAALAAVLKEILADGEDYGRSDAGKGKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYDV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 164 VREYYFNDHGTQIDRFVRSLIAAARGEETPE---DGYAGAYIVDIKDQILAQRP---------DALEAENPEEI-FREIG 230
Cdd:COG0018 157 TRENYINDAGTQIGKLALSLERYGEEEIEPEskpDGYLGDLYVKFHKEYEEDPElediarellAKLEPGDEEALeLWKKA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 231 THLMFDQIKESLAAFGTHFDVFFHENSVFEGGKVDALLDAMRENGQLFEADGAWWMRTTDYGDDKDRVVIKSDGNHAYVA 310
Cdd:COG0018 237 VDWSLEEIKEDLKRLGVEFDVWFSESSLYDSGAVEEVVEELKEKGLLYESDGALWVRLTEFGDDKDRVLVKSDGTYTYFT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 311 GDIAYYQDKMTRaeNPADVAIYMLGADHNGYVGRLKAIAQILGY-RADQIEVMIGQLVNLvKDGKPvrMSKRAGTVVTLE 389
Cdd:COG0018 317 TDIAYHLYKFER--YGFDRVIYVVGADQHGHFKRLFAALKALGYdPAKDLEHLLFGMVNL-RDGEK--MSTRAGTVVTLD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 390 DLVE-----------------------AVGVDAARYELTRYSVDTPIDIDLGLLTS-KSNENPvyYVQYAHARTAAVARN 445
Cdd:COG0018 392 DLLDeaverareiieekseeekeeiaeQVGIDAVRYFDLSRSRDKDLDFDLDLALSfEGNTNP--YVQYAHARICSILRK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 446 AAEAgVKVEDGVDTSLLDSAADGELLAVLGQFPAAVRDAAKFYEPHRVNRYLEQLASAYHSWYGVSRVapkADEEVTDLH 525
Cdd:COG0018 470 AGEE-LDGLAEADLSLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRI---LKAEDEELR 545
|
570 580
....*....|....*....|....*....
gi 1080203726 526 RTRLLLNNAAQQVLANGLNLLGVSAPERM 554
Cdd:COG0018 546 AARLALVAATAQVLKNGLGLLGISAPERM 574
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
1-554 |
0e+00 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 578.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 1 MTPEELSEAIALALEEtissgqltlVEGAELPAVRVERPKSREHGDWATNVALQLAKKVGKNPREAAALLAEKIsaipgv 80
Cdd:PRK01611 4 DIKELLAEALAAALEA---------GGLPELPAVLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIVEAI------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 81 ASVDIAGPGFLNITLDAAAAGELAATIVEAGEAYGRSDKFAGKTINLEFVSANPTGPIHLGGTRWAAVGDALARVLEAEG 160
Cdd:PRK01611 69 EKVEIAGPGFINFFLDPAALAELVLAILEAGERYGRSDIGKGKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 161 ANVVREYYFNDHGTQIDRFVRSLIAaargeetpedgyagayivdikdqilaqrpdaleaenpeeiFREIGTHLMFDQIKE 240
Cdd:PRK01611 149 YDVTREYYVNDAGTQIGMLIASLEL----------------------------------------LWRKAVDISLDEIKE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 241 SLAAFGTHFDVFFHENSVFEGGKVDALLDAMRENGQLF-EADGAWWMRTTDYGDDKDRVVIKSDGNHAYVAGDIAYYQDK 319
Cdd:PRK01611 189 DLDRLGVHFDVWFSESELYYNGKVDEVVEDLKEKGLLYvESDGALWVRLTEFGDDKDRVLIKSDGTYTYFTRDIAYHLYK 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 320 MTRAenpaDVAIYMLGADHNGYVGRLKAIAQILGYRADQIEVMIGQLVNLVKDGKPVRMSKRAGTVVTLEDLVE------ 393
Cdd:PRK01611 269 FERF----DRVIYVVGADHHGHFKRLKAALKALGYDPDALEVLLHQMVGLVRGGEGVKMSTRAGNVVTLDDLLDeavgra 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 394 -----------AVGVDAARYELTRYSVDTPIDIDLGLLTSKSNENPVyYVQYAHARTAAVARNAAEAGVKvedgVDTSLL 462
Cdd:PRK01611 345 relieekeiaeAVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPP-YVQYAHARICSILRKAAEAGID----LLLALL 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 463 DSAADGELLAVLGQFPAAVRDAAKFYEPHRVNRYLEQLASAYHSWYgvSRVAPKADEEvtDLHRTRLLLNNAAQQVLANG 542
Cdd:PRK01611 420 TEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFY--NRVLLKDEEE--ELRNARLALVKATAQVLKNG 495
|
570
....*....|..
gi 1080203726 543 LNLLGVSAPERM 554
Cdd:PRK01611 496 LDLLGISAPERM 507
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
4-554 |
5.48e-128 |
|
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: 385.93 E-value: 5.48e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 4 EELSEAIALALEEtissgqltlVEGAELPAVRVERPKSREHGDWATNVALQLAKKVGKNPREAAALLAEKISAIPGVASV 83
Cdd:TIGR00456 3 TLLKEEISQALLK---------AGLSKESEILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKLKTGEIIEKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 84 DIAGPgFLNITLDAAA-AGELAATIVEAGEAYGRSDKfAGKTINLEFVSANPTGPIHLGGTRWAAVGDALARVLEAEGAN 162
Cdd:TIGR00456 74 EAAGP-FINFFLSPQKlLERLIQKILTQKEKYGSKKL-KNKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 163 VVREYYFNDHGTQIDRFVRSLIAAARGEET-----PEDGYAGAYIVDIKDqiLAQRPDALEA--------ENPEEIFREI 229
Cdd:TIGR00456 152 VIREYYVNDWGRQFGLLALGVEKFGNEALNiavkkPDHGLEGFYVEINKR--LEENEELEEEarelfvklESGDEETIKL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 230 ---GTHLMFDQIKESLAAFGTHFDVFFHENSVFEGGKVDALLDAMRENGqLFEADGAWWMRTTDYGDDKDRVVIKSDGNH 306
Cdd:TIGR00456 230 wkrLVEYSLEGIKETYDRLNIHFDSFVWEGESVKNGMLPKVLEDLKEKG-LVVEDGALWLDLTLFGDKKDRVLQKSDGTY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 307 AYVAGDIAYYQDkmtRAENPADVAIYMLGADHNGYVGRLKAIAQILGYRADQIEVMIGQLVNLVK-----------DGKP 375
Cdd:TIGR00456 309 LYLTTDIAYHLD---KLERGFDKMIYVWGSDHHLHIAQMFAILEKLGYKKKELEHLNFGMVPLYSmktrrgnvislDNLL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 376 VRMSKRAGTVVT------LEDLVEAVGVDAARYELTRYSVDTPIDIDLGLLTSkSNENPVYYVQYAHARTAAVARNAAEA 449
Cdd:TIGR00456 386 DEASKRAGNVITikndleEEKVADAVGIGAVRYFDLSKNRTTDYVFDWDAMLS-FEGNTAPYIQYAHARICSILRKAEID 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 450 GVKVEDgvDTSLLDSAADGELLAVLGQFPAAVRDAAKFYEPHRVNRYLEQLASAYHSWYGVSRVApKADEEVTdlhRTRL 529
Cdd:TIGR00456 465 GEKLIA--DDFELLEEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACPVL-DAENELA---AARL 538
|
570 580
....*....|....*....|....*
gi 1080203726 530 LLNNAAQQVLANGLNLLGVSAPERM 554
Cdd:TIGR00456 539 ALLKATRQTLKNGLDLLGIEPPERM 563
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
124-383 |
4.17e-71 |
|
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: 226.68 E-value: 4.17e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 124 TINLEFVSANPTGPIHLGGTRWAAVGDALARVLEAEGANVVREYYFNDHGTQIDRFVRSLIAAargeetpedgyagayiv 203
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSLEKW----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 204 dikdqilaqrpdaleaenpeeifreigTHLMFDQIKESLAAFGT---HFDVFFHENSVFegGKVDALLDAMRENGQLFEA 280
Cdd:cd00671 64 ---------------------------RKLVEESIKADLETYGRldvRFDVWFGESSYL--GLMGKVVELLEELGLLYEE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 281 DGAWWMRTTDYGDDKDRVVIKSDGNHAYVAGDIAYYQDKMTRaenPADVAIYMLGADHNGYVGRLKAIAQILGYR-ADQI 359
Cdd:cd00671 115 DGALWLDLTEFGDDKDRVLVRSDGTYTYFTRDIAYHLDKFER---GADKIIYVVGADHHGHFKRLFAALELLGYDeAKKL 191
|
250 260
....*....|....*....|....
gi 1080203726 360 EVMIGQLVNLVKDGKpvrMSKRAG 383
Cdd:cd00671 192 EHLLYGMVNLPKEGK---MSTRAG 212
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
432-554 |
3.32e-34 |
|
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain of Arginyl tRNA synthetase. This domain is known as the DALR domain after characteristic conserved amino acids.
Pssm-ID: 214846 [Multi-domain] Cd Length: 122 Bit Score: 125.38 E-value: 3.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 432 VQYAHARTAAVARNAAEAGVKVED--GVDTSLLDSAADGELLAVLGQFPAAVRDAAKFYEPHRVNRYLEQLASAYHSWYG 509
Cdd:smart00836 1 VQYAHARICSILRKAGEAGETLPDiaDADLSLLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYN 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1080203726 510 VSRVapkADEEVTDLHRTRLLLNNAAQQVLANGLNLLGVSAPERM 554
Cdd:smart00836 81 RVRV---LGEENPELRKARLALLKAVRQVLANGLRLLGISAPERM 122
|
|
| DALR_1 |
pfam05746 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
432-554 |
2.74e-27 |
|
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: 106.20 E-value: 2.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 432 VQYAHARTAAVARNAAEAGVKVEdgVDTSLLDSAADGELLAVLGQFPAAVRDAAKFYEPHRVNRYLEQLASAYHSWYGVS 511
Cdd:pfam05746 1 LQYAHARICSILRKAGELGINLD--IDADLLTEEEEKELLKALLQFPEVLEEAAEELEPHRLANYLYELASAFHSFYNNC 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1080203726 512 RVAPKADEEVTDlhrtRLLLNNAAQQVLANGLNLLGVSAPERM 554
Cdd:pfam05746 79 RVLDEDNEERNA----RLALLKAVRQVLKNGLDLLGIEAPEKM 117
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
4-554 |
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: 595.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 4 EELSEAIALALEEtissgqltLVEGAELPAVRVERPKSREHGDWATNVALQLAKKVGKNPREAAALLAEKISAIPGVASV 83
Cdd:COG0018 5 EELAEAIAAALAA--------LGAGLEEPDILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDADPLVEKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 84 DIAGPGFLNITLDAAAAGELAATIVEAGEAYGRSDKFAGKTINLEFVSANPTGPIHLGGTRWAAVGDALARVLEAEGANV 163
Cdd:COG0018 77 EIAGPGFINFFLSPAALAAVLKEILADGEDYGRSDAGKGKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYDV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 164 VREYYFNDHGTQIDRFVRSLIAAARGEETPE---DGYAGAYIVDIKDQILAQRP---------DALEAENPEEI-FREIG 230
Cdd:COG0018 157 TRENYINDAGTQIGKLALSLERYGEEEIEPEskpDGYLGDLYVKFHKEYEEDPElediarellAKLEPGDEEALeLWKKA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 231 THLMFDQIKESLAAFGTHFDVFFHENSVFEGGKVDALLDAMRENGQLFEADGAWWMRTTDYGDDKDRVVIKSDGNHAYVA 310
Cdd:COG0018 237 VDWSLEEIKEDLKRLGVEFDVWFSESSLYDSGAVEEVVEELKEKGLLYESDGALWVRLTEFGDDKDRVLVKSDGTYTYFT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 311 GDIAYYQDKMTRaeNPADVAIYMLGADHNGYVGRLKAIAQILGY-RADQIEVMIGQLVNLvKDGKPvrMSKRAGTVVTLE 389
Cdd:COG0018 317 TDIAYHLYKFER--YGFDRVIYVVGADQHGHFKRLFAALKALGYdPAKDLEHLLFGMVNL-RDGEK--MSTRAGTVVTLD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 390 DLVE-----------------------AVGVDAARYELTRYSVDTPIDIDLGLLTS-KSNENPvyYVQYAHARTAAVARN 445
Cdd:COG0018 392 DLLDeaverareiieekseeekeeiaeQVGIDAVRYFDLSRSRDKDLDFDLDLALSfEGNTNP--YVQYAHARICSILRK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 446 AAEAgVKVEDGVDTSLLDSAADGELLAVLGQFPAAVRDAAKFYEPHRVNRYLEQLASAYHSWYGVSRVapkADEEVTDLH 525
Cdd:COG0018 470 AGEE-LDGLAEADLSLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRI---LKAEDEELR 545
|
570 580
....*....|....*....|....*....
gi 1080203726 526 RTRLLLNNAAQQVLANGLNLLGVSAPERM 554
Cdd:COG0018 546 AARLALVAATAQVLKNGLGLLGISAPERM 574
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
1-554 |
0e+00 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 578.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 1 MTPEELSEAIALALEEtissgqltlVEGAELPAVRVERPKSREHGDWATNVALQLAKKVGKNPREAAALLAEKIsaipgv 80
Cdd:PRK01611 4 DIKELLAEALAAALEA---------GGLPELPAVLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIVEAI------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 81 ASVDIAGPGFLNITLDAAAAGELAATIVEAGEAYGRSDKFAGKTINLEFVSANPTGPIHLGGTRWAAVGDALARVLEAEG 160
Cdd:PRK01611 69 EKVEIAGPGFINFFLDPAALAELVLAILEAGERYGRSDIGKGKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 161 ANVVREYYFNDHGTQIDRFVRSLIAaargeetpedgyagayivdikdqilaqrpdaleaenpeeiFREIGTHLMFDQIKE 240
Cdd:PRK01611 149 YDVTREYYVNDAGTQIGMLIASLEL----------------------------------------LWRKAVDISLDEIKE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 241 SLAAFGTHFDVFFHENSVFEGGKVDALLDAMRENGQLF-EADGAWWMRTTDYGDDKDRVVIKSDGNHAYVAGDIAYYQDK 319
Cdd:PRK01611 189 DLDRLGVHFDVWFSESELYYNGKVDEVVEDLKEKGLLYvESDGALWVRLTEFGDDKDRVLIKSDGTYTYFTRDIAYHLYK 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 320 MTRAenpaDVAIYMLGADHNGYVGRLKAIAQILGYRADQIEVMIGQLVNLVKDGKPVRMSKRAGTVVTLEDLVE------ 393
Cdd:PRK01611 269 FERF----DRVIYVVGADHHGHFKRLKAALKALGYDPDALEVLLHQMVGLVRGGEGVKMSTRAGNVVTLDDLLDeavgra 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 394 -----------AVGVDAARYELTRYSVDTPIDIDLGLLTSKSNENPVyYVQYAHARTAAVARNAAEAGVKvedgVDTSLL 462
Cdd:PRK01611 345 relieekeiaeAVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPP-YVQYAHARICSILRKAAEAGID----LLLALL 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 463 DSAADGELLAVLGQFPAAVRDAAKFYEPHRVNRYLEQLASAYHSWYgvSRVAPKADEEvtDLHRTRLLLNNAAQQVLANG 542
Cdd:PRK01611 420 TEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFY--NRVLLKDEEE--ELRNARLALVKATAQVLKNG 495
|
570
....*....|..
gi 1080203726 543 LNLLGVSAPERM 554
Cdd:PRK01611 496 LDLLGISAPERM 507
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
4-554 |
5.48e-128 |
|
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: 385.93 E-value: 5.48e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 4 EELSEAIALALEEtissgqltlVEGAELPAVRVERPKSREHGDWATNVALQLAKKVGKNPREAAALLAEKISAIPGVASV 83
Cdd:TIGR00456 3 TLLKEEISQALLK---------AGLSKESEILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKLKTGEIIEKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 84 DIAGPgFLNITLDAAA-AGELAATIVEAGEAYGRSDKfAGKTINLEFVSANPTGPIHLGGTRWAAVGDALARVLEAEGAN 162
Cdd:TIGR00456 74 EAAGP-FINFFLSPQKlLERLIQKILTQKEKYGSKKL-KNKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 163 VVREYYFNDHGTQIDRFVRSLIAAARGEET-----PEDGYAGAYIVDIKDqiLAQRPDALEA--------ENPEEIFREI 229
Cdd:TIGR00456 152 VIREYYVNDWGRQFGLLALGVEKFGNEALNiavkkPDHGLEGFYVEINKR--LEENEELEEEarelfvklESGDEETIKL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 230 ---GTHLMFDQIKESLAAFGTHFDVFFHENSVFEGGKVDALLDAMRENGqLFEADGAWWMRTTDYGDDKDRVVIKSDGNH 306
Cdd:TIGR00456 230 wkrLVEYSLEGIKETYDRLNIHFDSFVWEGESVKNGMLPKVLEDLKEKG-LVVEDGALWLDLTLFGDKKDRVLQKSDGTY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 307 AYVAGDIAYYQDkmtRAENPADVAIYMLGADHNGYVGRLKAIAQILGYRADQIEVMIGQLVNLVK-----------DGKP 375
Cdd:TIGR00456 309 LYLTTDIAYHLD---KLERGFDKMIYVWGSDHHLHIAQMFAILEKLGYKKKELEHLNFGMVPLYSmktrrgnvislDNLL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 376 VRMSKRAGTVVT------LEDLVEAVGVDAARYELTRYSVDTPIDIDLGLLTSkSNENPVYYVQYAHARTAAVARNAAEA 449
Cdd:TIGR00456 386 DEASKRAGNVITikndleEEKVADAVGIGAVRYFDLSKNRTTDYVFDWDAMLS-FEGNTAPYIQYAHARICSILRKAEID 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 450 GVKVEDgvDTSLLDSAADGELLAVLGQFPAAVRDAAKFYEPHRVNRYLEQLASAYHSWYGVSRVApKADEEVTdlhRTRL 529
Cdd:TIGR00456 465 GEKLIA--DDFELLEEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACPVL-DAENELA---AARL 538
|
570 580
....*....|....*....|....*
gi 1080203726 530 LLNNAAQQVLANGLNLLGVSAPERM 554
Cdd:TIGR00456 539 ALLKATRQTLKNGLDLLGIEPPERM 563
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
124-383 |
4.17e-71 |
|
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: 226.68 E-value: 4.17e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 124 TINLEFVSANPTGPIHLGGTRWAAVGDALARVLEAEGANVVREYYFNDHGTQIDRFVRSLIAAargeetpedgyagayiv 203
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSLEKW----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 204 dikdqilaqrpdaleaenpeeifreigTHLMFDQIKESLAAFGT---HFDVFFHENSVFegGKVDALLDAMRENGQLFEA 280
Cdd:cd00671 64 ---------------------------RKLVEESIKADLETYGRldvRFDVWFGESSYL--GLMGKVVELLEELGLLYEE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 281 DGAWWMRTTDYGDDKDRVVIKSDGNHAYVAGDIAYYQDKMTRaenPADVAIYMLGADHNGYVGRLKAIAQILGYR-ADQI 359
Cdd:cd00671 115 DGALWLDLTEFGDDKDRVLVRSDGTYTYFTRDIAYHLDKFER---GADKIIYVVGADHHGHFKRLFAALELLGYDeAKKL 191
|
250 260
....*....|....*....|....
gi 1080203726 360 EVMIGQLVNLVKDGKpvrMSKRAG 383
Cdd:cd00671 192 EHLLYGMVNLPKEGK---MSTRAG 212
|
|
| Anticodon_Ia_Arg |
cd07956 |
Anticodon-binding domain of arginyl tRNA synthetases; This domain is found in arginyl tRNA ... |
393-554 |
9.15e-38 |
|
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: 136.58 E-value: 9.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 393 EAVGVDAARYELTRYSVDTPIDIDLGLLTSKSNeNPVYYVQYAHARtaaVARNAAEAGVKVED--GVDTSLLDSAADGEL 470
Cdd:cd07956 1 EEVGVGAVKYQDLSNKRIKDYTFDWERMLSFEG-DTGPYLQYAHAR---LCSILRKAGETIEAeaDADLSLLPEPDERDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 471 LAVLGQFPAAVRDAAKFYEPHRVNRYLEQLASAYHSWYGVSRVApKADEEVTdlhRTRLLLNNAAQQVLANGLNLLGVSA 550
Cdd:cd07956 77 ILLLAKFPEVVKNAAETLEPHTIATYLFDLAHAFSKFYNACPVL-GAEEELR---NARLALVAAARQVLANGLDLLGIEA 152
|
....
gi 1080203726 551 PERM 554
Cdd:cd07956 153 PERM 156
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
432-554 |
3.32e-34 |
|
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain of Arginyl tRNA synthetase. This domain is known as the DALR domain after characteristic conserved amino acids.
Pssm-ID: 214846 [Multi-domain] Cd Length: 122 Bit Score: 125.38 E-value: 3.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 432 VQYAHARTAAVARNAAEAGVKVED--GVDTSLLDSAADGELLAVLGQFPAAVRDAAKFYEPHRVNRYLEQLASAYHSWYG 509
Cdd:smart00836 1 VQYAHARICSILRKAGEAGETLPDiaDADLSLLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYN 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1080203726 510 VSRVapkADEEVTDLHRTRLLLNNAAQQVLANGLNLLGVSAPERM 554
Cdd:smart00836 81 RVRV---LGEENPELRKARLALLKAVRQVLANGLRLLGISAPERM 122
|
|
| DALR_1 |
pfam05746 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
432-554 |
2.74e-27 |
|
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: 106.20 E-value: 2.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 432 VQYAHARTAAVARNAAEAGVKVEdgVDTSLLDSAADGELLAVLGQFPAAVRDAAKFYEPHRVNRYLEQLASAYHSWYGVS 511
Cdd:pfam05746 1 LQYAHARICSILRKAGELGINLD--IDADLLTEEEEKELLKALLQFPEVLEEAAEELEPHRLANYLYELASAFHSFYNNC 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1080203726 512 RVAPKADEEVTDlhrtRLLLNNAAQQVLANGLNLLGVSAPERM 554
Cdd:pfam05746 79 RVLDEDNEERNA----RLALLKAVRQVLKNGLDLLGIEAPEKM 117
|
|
| Arg_tRNA_synt_N |
smart01016 |
Arginyl tRNA synthetase N terminal dom; This domain is found at the amino terminus of Arginyl ... |
4-95 |
9.41e-26 |
|
Arginyl tRNA synthetase N terminal dom; This domain is found at the amino terminus of Arginyl tRNA synthetase, also called additional domain 1 (Add-1). It is about 140 residues long and it has been suggested that this domain will be involved in tRNA recognition.
Pssm-ID: 214975 [Multi-domain] Cd Length: 85 Bit Score: 100.74 E-value: 9.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 4 EELSEAIALALEETissgqltLVEGAELPAVRVERPKSREHGDWATNVALQLAKKVGKNPREAAALLAEKISAIPGVASV 83
Cdd:smart01016 1 DLLKEAIAEALKKA-------LGVEGEPIDIALERPKDPDHGDYATNVAFRLAKKLKKNPRELAEEIAEKLPKSDLVEKV 73
|
90
....*....|..
gi 1080203726 84 DIAGPGFLNITL 95
Cdd:smart01016 74 EIAGPGFINFFL 85
|
|
| Arg_tRNA_synt_N |
pfam03485 |
Arginyl tRNA synthetase N terminal domain; This domain is found at the amino terminus of ... |
6-95 |
1.29e-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: 97.30 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 6 LSEAIALALEETissgqltLVEGAELPAVRVERPKSREHGDWATNVALQLAKKVGKNPREAAALLAEKISAIPGVASVDI 85
Cdd:pfam03485 1 LKKAIAKALSKL-------GGPDLELIDIVIETPKNPKFGDYATNVAMQLAKKLKKNPREIAEEIAEKLEKSDIIEKVEV 73
|
90
....*....|
gi 1080203726 86 AGPGFLNITL 95
Cdd:pfam03485 74 AGPGFINFFL 83
|
|
| PLN02286 |
PLN02286 |
arginine-tRNA ligase |
5-554 |
1.17e-21 |
|
arginine-tRNA ligase
Pssm-ID: 215160 [Multi-domain] Cd Length: 576 Bit Score: 98.56 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 5 ELSEAIALALEETISSGqlTLVEgaelpaVRVERPKSREHGDWATNVALQLAKKVG------KNPREAAALLAEKISAIP 78
Cdd:PLN02286 2 ELAKLFEASLRLTVPDE--PSVE------PLVAACTNPKFGDYQCNNAMGLWSKLKgkgtsfKNPRAVAQAIVKNLPASE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 79 GVASVDIAGPGFLNITLDAAAAGELAATIVEAGEAyGRSDKFAGKTINLEFVSANPTGPIHLGGTRWAAVGDALARVLEA 158
Cdd:PLN02286 74 MIESTSVAGPGFVNVRLSASWLAKRIERMLVDGID-TWAPTLPVKRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 159 EGANVVREYYFNDHGTQIDRFVRSLIAAARGEETPEDgyagayiVDIKD-QIL----AQRPDA--------------LEA 219
Cdd:PLN02286 153 SGVEVLRRNHVGDWGTQFGMLIEHLFEKFPNWESVSD-------QAIGDlQEFykaaKKRFDEdeefkaraqqavvrLQG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 220 ENPEeifreigTHLMFDQIKE-SLAAFGTHFD---VFFHEN-SVFEGGKVDALLDAMRENGQLFEADGAWWMRTTdyGDD 294
Cdd:PLN02286 226 GDPE-------YRAAWAKICEiSRREFEKVYQrlrVELEEKgESFYNPYIPGVIEELESKGLVVESDGARVIFVE--GFD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 295 KDRVVIKSDGNHAYVAGDIAYYQDKMTraENPADVAIYMLGADHNGYVGRLKAIAQILGYRADQIEVM---IGQLVNLVK 371
Cdd:PLN02286 297 IPLIVVKSDGGFNYASTDLAALWYRLN--EEKAEWIIYVTDVGQQQHFDMVFKAAKRAGWLPEDTYPRlehVGFGLVLGE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 372 DGKpvRMSKRAGTVVTLEDLV-----------------------------EAVGVDAARY------ELTRY--SVDTPID 414
Cdd:PLN02286 375 DGK--RFRTRSGEVVRLVDLLdeaksrskaaliergkdsewtpeeleqaaEAVGYGAVKYadlknnRLTNYtfSFDQMLD 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 415 IdlglltsksNENPVYYVQYAHARTaavARNAAEAGVKVEDGVDTS--LLDSAADGELLAVLGQFPAAVRDAAKFYEPHR 492
Cdd:PLN02286 453 L---------KGNTAVYLLYAHARI---CSIIRKSGKDIDELKKTGkiVLDHPDERALGLHLLQFPEVVEEACTDLLPNR 520
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080203726 493 VNRYLEQLASAYHSWYGVSRVApKADEEvtdlhRTRLLLNNAAQQVLANGLNLLGVSAPERM 554
Cdd:PLN02286 521 LCEYLYNLSEKFTKFYSNCKVN-GSEEE-----TSRLLLCEATAIVMRKCFHLLGITPLYRL 576
|
|
| tRNA-synt_1d |
pfam00750 |
tRNA synthetases class I (R); Other tRNA synthetase sub-families are too dissimilar to be ... |
123-393 |
1.34e-19 |
|
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: 90.32 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 123 KTINLEFVSANPTGPIHLGGTRWAAVGDALARVLEAEGANVVREYYFNDHGTQIDRFVRSLiaAARGEE----TPEDGYA 198
Cdd:pfam00750 19 KKVVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQFGMLIAGL--EKYQDEktlqEMPIQDL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 199 GAYIVDIK-----DQILAQRPDA--LEAENPEEIFREIGThLMFDQIKESLAAFGTHFDVFFHE--NSVFEgGKVDALLD 269
Cdd:pfam00750 97 EDFYREAKkhydeEEEFAERARNyvVKLQSGDEYWRRMWK-LIVDITMTQNQRLYDRLDVTLTEmgESLYN-PMMNEIVK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080203726 270 AMRENGQLFEADGAWWMRTTDYGDDKDRVVIKSDGNHAYVAGDIAyyQDKMTRAENPADVAIYMLGADHNGYVGRLKAIA 349
Cdd:pfam00750 175 DFKKNGLVVEIDGALVVFLDEFGKPMGVIVQKSDGGYLYTTTDIA--AAKYRYETLHADRMLYVIDSRQSQHMQQAFAIL 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1080203726 350 QILGYRADQIEVM-IGQLVNLVKDGKPvrMSKRAGTVVTLEDLVE 393
Cdd:pfam00750 253 RKAGYVPESKDLEhINFGMVLGKDGKP--FKTRKGGTVKLADLLD 295
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
369-406 |
7.26e-04 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 42.48 E-value: 7.26e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1080203726 369 LVKDGKpvrMSKRAGTVVTLEDLVEAVGVDAARYELTR 406
Cdd:PRK12267 294 LMKDGK---MSKSKGNVVDPEELVDRYGLDALRYYLLR 328
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
360-408 |
5.43e-03 |
|
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) catalytic core domain. This enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. ValRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 185677 [Multi-domain] Cd Length: 382 Bit Score: 39.15 E-value: 5.43e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1080203726 360 EVMIGQLVnLVKDGKpvRMSKRAGTVVTLEDLVEAVGVDAARYELTRYS 408
Cdd:cd00817 329 EVYLHGLV-RDEDGR--KMSKSLGNVIDPLDVIDGYGADALRFTLASAA 374
|
|
| |
