|
Name |
Accession |
Description |
Interval |
E-value |
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
4-555 |
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: 588.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 4 DALAEALLSVVAPLAEarrpgssdGLTAADFVFERPKNRDHGDWASNAAMKLAKRVGTNPREFAAEIAAALAETPGVASV 83
Cdd:COG0018 5 EELAEAIAAALAALGA--------GLEEPDILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDADPLVEKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 84 EVAGPGFINIRLDAAAAGALAREIVEAGAAFGRNDSQAGNSINLEFVSANPTGPMHIGHTRWAALGDAIARLLLASGAEL 163
Cdd:COG0018 77 EIAGPGFINFFLSPAALAAVLKEILADGEDYGRSDAGKGKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYDV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 164 VREFYINDAGAQMQRFGRSVLASAKGEPTPE---DGYPGAY-------------IDDLARRVLSArpdlltLAPEEQEQV 227
Cdd:COG0018 157 TRENYINDAGTQIGKLALSLERYGEEEIEPEskpDGYLGDLyvkfhkeyeedpeLEDIARELLAK------LEPGDEEAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 228 AL-DLGYELQMADLKDSLEKFNVHFDVFFSERLLHATPAdggpslVDQAVDRLRAQGHVFDQDDAVWVRTTDFGDDKDRV 306
Cdd:COG0018 231 ELwKKAVDWSLEEIKEDLKRLGVEFDVWFSESSLYDSGA------VEEVVEELKEKGLLYESDGALWVRLTEFGDDKDRV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 307 IRRSNGEYTYFAADAAYYLNK-GDRGFAHKIYLLGADHHGYVHRLKALAGAAGDDPEKDIEVLIGQLVSV-NGARLSKRA 384
Cdd:COG0018 305 LVKSDGTYTYFTTDIAYHLYKfERYGFDRVIYVVGADQHGHFKRLFAALKALGYDPAKDLEHLLFGMVNLrDGEKMSTRA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 385 GNIIELDDLRDWL-----------------------GTDALRYSLARYPADSPLTLDPE-ILQKRTNDNPvfYVQYAHAR 440
Cdd:COG0018 385 GTVVTLDDLLDEAverareiieekseeekeeiaeqvGIDAVRYFDLSRSRDKDLDFDLDlALSFEGNTNP--YVQYAHAR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 441 THNVARNAADSGVTRDAFAPEMLDHETESALLGALQEFPRIVAFAAELREPHRVARYLEELASLYHRWYDTCRVTplgDE 520
Cdd:COG0018 463 ICSILRKAGEELDGLAEADLSLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRIL---KA 539
|
570 580 590
....*....|....*....|....*....|....*
gi 1654126220 521 EVTDLHRTRLWLNDATGQVLRNGLDLLGVSAPERM 555
Cdd:COG0018 540 EDEELRAARLALVAATAQVLKNGLGLLGISAPERM 574
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
4-555 |
0e+00 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 540.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 4 DALAEALLSVVAPLAEarrpgssdgltaaDFVFERPKNRDHGDWASNAAMKLAKRVGTNPREFAAEIAAalaetpGVASV 83
Cdd:PRK01611 11 EALAAALEAGGLPELP-------------AVLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIVE------AIEKV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 84 EVAGPGFINIRLDAAAAGALAREIVEAGAAFGRNDSQAGNSINLEFVSANPTGPMHIGHTRWAALGDAIARLLLASGAEL 163
Cdd:PRK01611 72 EIAGPGFINFFLDPAALAELVLAILEAGERYGRSDIGKGKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 164 VREFYINDAGAQMQRFGRSVLAsakgeptpedgypgayiddlarrvlsarpdlltlapeeqeqvALDLGYELQMADLKDS 243
Cdd:PRK01611 152 TREYYVNDAGTQIGMLIASLEL------------------------------------------LWRKAVDISLDEIKED 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 244 LEKFNVHFDVFFSERLLHATPAdggpslVDQAVDRLRAQGHVFDQDD-AVWVRTTDFGDDKDRVIRRSNGEYTYFAADAA 322
Cdd:PRK01611 190 LDRLGVHFDVWFSESELYYNGK------VDEVVEDLKEKGLLYVESDgALWVRLTEFGDDKDRVLIKSDGTYTYFTRDIA 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 323 YYLNKGDRgFAHKIYLLGADHHGYVHRLKALAGAAGDDPEKdIEVLIGQLVSV----NGARLSKRAGNIIELDDLRDWL- 397
Cdd:PRK01611 264 YHLYKFER-FDRVIYVVGADHHGHFKRLKAALKALGYDPDA-LEVLLHQMVGLvrggEGVKMSTRAGNVVTLDDLLDEAv 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 398 ----------------GTDALRYSLARYPADSPLTLDPEILQKRTNDNPVfYVQYAHARTHNVARNAADSGVTRDafaPE 461
Cdd:PRK01611 342 grarelieekeiaeavGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPP-YVQYAHARICSILRKAAEAGIDLL---LA 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 462 MLDHETESALLGALQEFPRIVAFAAELREPHRVARYLEELASLYHRWYDTCrvtpLGDEEVTDLHRTRLWLNDATGQVLR 541
Cdd:PRK01611 418 LLTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYNRV----LLKDEEEELRNARLALVKATAQVLK 493
|
570
....*....|....
gi 1654126220 542 NGLDLLGVSAPERM 555
Cdd:PRK01611 494 NGLDLLGISAPERM 507
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
33-555 |
1.63e-107 |
|
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: 333.15 E-value: 1.63e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 33 DFVFERPKNRDHGDWASNAAMKLAKRVGTNPREFAAEIAAALAETPGVASVEVAGPgFINIRLDAAA-AGALAREIVEAG 111
Cdd:TIGR00456 23 EILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKLKTGEIIEKVEAAGP-FINFFLSPQKlLERLIQKILTQK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 112 AAFGRNDSQaGNSINLEFVSANPTGPMHIGHTRWAALGDAIARLLLASGAELVREFYINDAGAQMQRFGRSV-----LAS 186
Cdd:TIGR00456 102 EKYGSKKLK-NKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYVNDWGRQFGLLALGVekfgnEAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 187 AKGEPTPEDGYPGAYIDDLARrvLSARPDLLTLApeEQEQVALDLGYE-----------LQMADLKDSLEKFNVHFDVFF 255
Cdd:TIGR00456 181 NIAVKKPDHGLEGFYVEINKR--LEENEELEEEA--RELFVKLESGDEetiklwkrlveYSLEGIKETYDRLNIHFDSFV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 256 SErllhatpadgGPSLVDQAVDR----LRAQGHVFdQDDAVWVRTTDFGDDKDRVIRRSNGEYTYFAADAAYYLNKGDRG 331
Cdd:TIGR00456 257 WE----------GESVKNGMLPKvledLKEKGLVV-EDGALWLDLTLFGDKKDRVLQKSDGTYLYLTTDIAYHLDKLERG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 332 FAHKIYLLGADHHGYVHRLKALAGAAGDDPeKDIEVLIGQLV-------------SVNG--ARLSKRAGNII------EL 390
Cdd:TIGR00456 326 FDKMIYVWGSDHHLHIAQMFAILEKLGYKK-KELEHLNFGMVplysmktrrgnviSLDNllDEASKRAGNVItikndlEE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 391 DDLRDWLGTDALRYSLARYPADSPLTLD-PEILQkrTNDNPVFYVQYAHARTHNVARNAADSGVTRDAfAPEMLDHETES 469
Cdd:TIGR00456 405 EKVADAVGIGAVRYFDLSKNRTTDYVFDwDAMLS--FEGNTAPYIQYAHARICSILRKAEIDGEKLIA-DDFELLEEKEK 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 470 ALLGALQEFPRIVAFAAELREPHRVARYLEELASLYHRWYDTCRVtpLGDEEvtDLHRTRLWLNDATGQVLRNGLDLLGV 549
Cdd:TIGR00456 482 ELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACPV--LDAEN--ELAAARLALLKATRQTLKNGLDLLGI 557
|
....*.
gi 1654126220 550 SAPERM 555
Cdd:TIGR00456 558 EPPERM 563
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
125-385 |
1.20e-69 |
|
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. There are at least three subgroups of ArgRS. One type contains both characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The second subtype lacks the KMSKS motif; however, it has a lysine N-terminal to the HIGH motif, which serves as the functional counterpart to the second lysine of the KMSKS motif. A third group, which is found primarily in archaea and a few bacteria, lacks both the KMSKS motif and the HIGH loop lysine.
Pssm-ID: 185675 [Multi-domain] Cd Length: 212 Bit Score: 222.82 E-value: 1.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 125 INLEFVSANPTGPMHIGHTRWAALGDAIARLLLASGAELVREFYINDAGAQMQRFGRSVLASAKgeptpedgypgayIDD 204
Cdd:cd00671 2 ILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSLEKWRK-------------LVE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 205 LARRvlsarpdlltlapeeqeqvaldlgyelqmaDLKDSLEKFNVHFDVFFSERLLHatpadggpSLVDQAVDRLRAQGH 284
Cdd:cd00671 69 ESIK------------------------------ADLETYGRLDVRFDVWFGESSYL--------GLMGKVVELLEELGL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 285 VFDQDDAVWVRTTDFGDDKDRVIRRSNGEYTYFAADAAYYLNKGDRGFAHKIYLLGADHHGYVHRLKALAGAAGDDPEKD 364
Cdd:cd00671 111 LYEEDGALWLDLTEFGDDKDRVLVRSDGTYTYFTRDIAYHLDKFERGADKIIYVVGADHHGHFKRLFAALELLGYDEAKK 190
|
250 260
....*....|....*....|..
gi 1654126220 365 IEVLIGQLVS-VNGARLSKRAG 385
Cdd:cd00671 191 LEHLLYGMVNlPKEGKMSTRAG 212
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
434-555 |
7.66e-43 |
|
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: 148.88 E-value: 7.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 434 VQYAHARTHNVARNAADSGVTRDAFA---PEMLDHETESALLGALQEFPRIVAFAAELREPHRVARYLEELASLYHRWYD 510
Cdd:smart00836 1 VQYAHARICSILRKAGEAGETLPDIAdadLSLLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYN 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1654126220 511 TCRVTplgDEEVTDLHRTRLWLNDATGQVLRNGLDLLGVSAPERM 555
Cdd:smart00836 81 RVRVL---GEENPELRKARLALLKAVRQVLANGLRLLGISAPERM 122
|
|
| DALR_1 |
pfam05746 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
434-555 |
1.33e-36 |
|
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: 132.00 E-value: 1.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 434 VQYAHARTHNVARNAADSGVTRDAfAPEMLDHETESALLGALQEFPRIVAFAAELREPHRVARYLEELASLYHRWYDTCR 513
Cdd:pfam05746 1 LQYAHARICSILRKAGELGINLDI-DADLLTEEEEKELLKALLQFPEVLEEAAEELEPHRLANYLYELASAFHSFYNNCR 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1654126220 514 VtpLGDEEvtDLHRTRLWLNDATGQVLRNGLDLLGVSAPERM 555
Cdd:pfam05746 80 V--LDEDN--EERNARLALLKAVRQVLKNGLDLLGIEAPEKM 117
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
4-555 |
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: 588.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 4 DALAEALLSVVAPLAEarrpgssdGLTAADFVFERPKNRDHGDWASNAAMKLAKRVGTNPREFAAEIAAALAETPGVASV 83
Cdd:COG0018 5 EELAEAIAAALAALGA--------GLEEPDILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDADPLVEKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 84 EVAGPGFINIRLDAAAAGALAREIVEAGAAFGRNDSQAGNSINLEFVSANPTGPMHIGHTRWAALGDAIARLLLASGAEL 163
Cdd:COG0018 77 EIAGPGFINFFLSPAALAAVLKEILADGEDYGRSDAGKGKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYDV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 164 VREFYINDAGAQMQRFGRSVLASAKGEPTPE---DGYPGAY-------------IDDLARRVLSArpdlltLAPEEQEQV 227
Cdd:COG0018 157 TRENYINDAGTQIGKLALSLERYGEEEIEPEskpDGYLGDLyvkfhkeyeedpeLEDIARELLAK------LEPGDEEAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 228 AL-DLGYELQMADLKDSLEKFNVHFDVFFSERLLHATPAdggpslVDQAVDRLRAQGHVFDQDDAVWVRTTDFGDDKDRV 306
Cdd:COG0018 231 ELwKKAVDWSLEEIKEDLKRLGVEFDVWFSESSLYDSGA------VEEVVEELKEKGLLYESDGALWVRLTEFGDDKDRV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 307 IRRSNGEYTYFAADAAYYLNK-GDRGFAHKIYLLGADHHGYVHRLKALAGAAGDDPEKDIEVLIGQLVSV-NGARLSKRA 384
Cdd:COG0018 305 LVKSDGTYTYFTTDIAYHLYKfERYGFDRVIYVVGADQHGHFKRLFAALKALGYDPAKDLEHLLFGMVNLrDGEKMSTRA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 385 GNIIELDDLRDWL-----------------------GTDALRYSLARYPADSPLTLDPE-ILQKRTNDNPvfYVQYAHAR 440
Cdd:COG0018 385 GTVVTLDDLLDEAverareiieekseeekeeiaeqvGIDAVRYFDLSRSRDKDLDFDLDlALSFEGNTNP--YVQYAHAR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 441 THNVARNAADSGVTRDAFAPEMLDHETESALLGALQEFPRIVAFAAELREPHRVARYLEELASLYHRWYDTCRVTplgDE 520
Cdd:COG0018 463 ICSILRKAGEELDGLAEADLSLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRIL---KA 539
|
570 580 590
....*....|....*....|....*....|....*
gi 1654126220 521 EVTDLHRTRLWLNDATGQVLRNGLDLLGVSAPERM 555
Cdd:COG0018 540 EDEELRAARLALVAATAQVLKNGLGLLGISAPERM 574
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
4-555 |
0e+00 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 540.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 4 DALAEALLSVVAPLAEarrpgssdgltaaDFVFERPKNRDHGDWASNAAMKLAKRVGTNPREFAAEIAAalaetpGVASV 83
Cdd:PRK01611 11 EALAAALEAGGLPELP-------------AVLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIVE------AIEKV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 84 EVAGPGFINIRLDAAAAGALAREIVEAGAAFGRNDSQAGNSINLEFVSANPTGPMHIGHTRWAALGDAIARLLLASGAEL 163
Cdd:PRK01611 72 EIAGPGFINFFLDPAALAELVLAILEAGERYGRSDIGKGKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 164 VREFYINDAGAQMQRFGRSVLAsakgeptpedgypgayiddlarrvlsarpdlltlapeeqeqvALDLGYELQMADLKDS 243
Cdd:PRK01611 152 TREYYVNDAGTQIGMLIASLEL------------------------------------------LWRKAVDISLDEIKED 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 244 LEKFNVHFDVFFSERLLHATPAdggpslVDQAVDRLRAQGHVFDQDD-AVWVRTTDFGDDKDRVIRRSNGEYTYFAADAA 322
Cdd:PRK01611 190 LDRLGVHFDVWFSESELYYNGK------VDEVVEDLKEKGLLYVESDgALWVRLTEFGDDKDRVLIKSDGTYTYFTRDIA 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 323 YYLNKGDRgFAHKIYLLGADHHGYVHRLKALAGAAGDDPEKdIEVLIGQLVSV----NGARLSKRAGNIIELDDLRDWL- 397
Cdd:PRK01611 264 YHLYKFER-FDRVIYVVGADHHGHFKRLKAALKALGYDPDA-LEVLLHQMVGLvrggEGVKMSTRAGNVVTLDDLLDEAv 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 398 ----------------GTDALRYSLARYPADSPLTLDPEILQKRTNDNPVfYVQYAHARTHNVARNAADSGVTRDafaPE 461
Cdd:PRK01611 342 grarelieekeiaeavGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPP-YVQYAHARICSILRKAAEAGIDLL---LA 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 462 MLDHETESALLGALQEFPRIVAFAAELREPHRVARYLEELASLYHRWYDTCrvtpLGDEEVTDLHRTRLWLNDATGQVLR 541
Cdd:PRK01611 418 LLTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYNRV----LLKDEEEELRNARLALVKATAQVLK 493
|
570
....*....|....
gi 1654126220 542 NGLDLLGVSAPERM 555
Cdd:PRK01611 494 NGLDLLGISAPERM 507
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
33-555 |
1.63e-107 |
|
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: 333.15 E-value: 1.63e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 33 DFVFERPKNRDHGDWASNAAMKLAKRVGTNPREFAAEIAAALAETPGVASVEVAGPgFINIRLDAAA-AGALAREIVEAG 111
Cdd:TIGR00456 23 EILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKLKTGEIIEKVEAAGP-FINFFLSPQKlLERLIQKILTQK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 112 AAFGRNDSQaGNSINLEFVSANPTGPMHIGHTRWAALGDAIARLLLASGAELVREFYINDAGAQMQRFGRSV-----LAS 186
Cdd:TIGR00456 102 EKYGSKKLK-NKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYVNDWGRQFGLLALGVekfgnEAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 187 AKGEPTPEDGYPGAYIDDLARrvLSARPDLLTLApeEQEQVALDLGYE-----------LQMADLKDSLEKFNVHFDVFF 255
Cdd:TIGR00456 181 NIAVKKPDHGLEGFYVEINKR--LEENEELEEEA--RELFVKLESGDEetiklwkrlveYSLEGIKETYDRLNIHFDSFV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 256 SErllhatpadgGPSLVDQAVDR----LRAQGHVFdQDDAVWVRTTDFGDDKDRVIRRSNGEYTYFAADAAYYLNKGDRG 331
Cdd:TIGR00456 257 WE----------GESVKNGMLPKvledLKEKGLVV-EDGALWLDLTLFGDKKDRVLQKSDGTYLYLTTDIAYHLDKLERG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 332 FAHKIYLLGADHHGYVHRLKALAGAAGDDPeKDIEVLIGQLV-------------SVNG--ARLSKRAGNII------EL 390
Cdd:TIGR00456 326 FDKMIYVWGSDHHLHIAQMFAILEKLGYKK-KELEHLNFGMVplysmktrrgnviSLDNllDEASKRAGNVItikndlEE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 391 DDLRDWLGTDALRYSLARYPADSPLTLD-PEILQkrTNDNPVFYVQYAHARTHNVARNAADSGVTRDAfAPEMLDHETES 469
Cdd:TIGR00456 405 EKVADAVGIGAVRYFDLSKNRTTDYVFDwDAMLS--FEGNTAPYIQYAHARICSILRKAEIDGEKLIA-DDFELLEEKEK 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 470 ALLGALQEFPRIVAFAAELREPHRVARYLEELASLYHRWYDTCRVtpLGDEEvtDLHRTRLWLNDATGQVLRNGLDLLGV 549
Cdd:TIGR00456 482 ELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACPV--LDAEN--ELAAARLALLKATRQTLKNGLDLLGI 557
|
....*.
gi 1654126220 550 SAPERM 555
Cdd:TIGR00456 558 EPPERM 563
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
125-385 |
1.20e-69 |
|
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. There are at least three subgroups of ArgRS. One type contains both characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The second subtype lacks the KMSKS motif; however, it has a lysine N-terminal to the HIGH motif, which serves as the functional counterpart to the second lysine of the KMSKS motif. A third group, which is found primarily in archaea and a few bacteria, lacks both the KMSKS motif and the HIGH loop lysine.
Pssm-ID: 185675 [Multi-domain] Cd Length: 212 Bit Score: 222.82 E-value: 1.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 125 INLEFVSANPTGPMHIGHTRWAALGDAIARLLLASGAELVREFYINDAGAQMQRFGRSVLASAKgeptpedgypgayIDD 204
Cdd:cd00671 2 ILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSLEKWRK-------------LVE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 205 LARRvlsarpdlltlapeeqeqvaldlgyelqmaDLKDSLEKFNVHFDVFFSERLLHatpadggpSLVDQAVDRLRAQGH 284
Cdd:cd00671 69 ESIK------------------------------ADLETYGRLDVRFDVWFGESSYL--------GLMGKVVELLEELGL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 285 VFDQDDAVWVRTTDFGDDKDRVIRRSNGEYTYFAADAAYYLNKGDRGFAHKIYLLGADHHGYVHRLKALAGAAGDDPEKD 364
Cdd:cd00671 111 LYEEDGALWLDLTEFGDDKDRVLVRSDGTYTYFTRDIAYHLDKFERGADKIIYVVGADHHGHFKRLFAALELLGYDEAKK 190
|
250 260
....*....|....*....|..
gi 1654126220 365 IEVLIGQLVS-VNGARLSKRAG 385
Cdd:cd00671 191 LEHLLYGMVNlPKEGKMSTRAG 212
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
434-555 |
7.66e-43 |
|
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: 148.88 E-value: 7.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 434 VQYAHARTHNVARNAADSGVTRDAFA---PEMLDHETESALLGALQEFPRIVAFAAELREPHRVARYLEELASLYHRWYD 510
Cdd:smart00836 1 VQYAHARICSILRKAGEAGETLPDIAdadLSLLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYN 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1654126220 511 TCRVTplgDEEVTDLHRTRLWLNDATGQVLRNGLDLLGVSAPERM 555
Cdd:smart00836 81 RVRVL---GEENPELRKARLALLKAVRQVLANGLRLLGISAPERM 122
|
|
| Anticodon_Ia_Arg |
cd07956 |
Anticodon-binding domain of arginyl tRNA synthetases; This domain is found in arginyl tRNA ... |
395-555 |
5.23e-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: 136.96 E-value: 5.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 395 DWLGTDALRYSLARYPADSPLTLDPEILQKRTNDnPVFYVQYAHARTHNVARNAadsGVTRDAFAPEMLD---HETESAL 471
Cdd:cd07956 1 EEVGVGAVKYQDLSNKRIKDYTFDWERMLSFEGD-TGPYLQYAHARLCSILRKA---GETIEAEADADLSllpEPDERDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 472 LGALQEFPRIVAFAAELREPHRVARYLEELASLYHRWYDTCRVtpLGDEEvtDLHRTRLWLNDATGQVLRNGLDLLGVSA 551
Cdd:cd07956 77 ILLLAKFPEVVKNAAETLEPHTIATYLFDLAHAFSKFYNACPV--LGAEE--ELRNARLALVAAARQVLANGLDLLGIEA 152
|
....
gi 1654126220 552 PERM 555
Cdd:cd07956 153 PERM 156
|
|
| DALR_1 |
pfam05746 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
434-555 |
1.33e-36 |
|
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: 132.00 E-value: 1.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 434 VQYAHARTHNVARNAADSGVTRDAfAPEMLDHETESALLGALQEFPRIVAFAAELREPHRVARYLEELASLYHRWYDTCR 513
Cdd:pfam05746 1 LQYAHARICSILRKAGELGINLDI-DADLLTEEEEKELLKALLQFPEVLEEAAEELEPHRLANYLYELASAFHSFYNNCR 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1654126220 514 VtpLGDEEvtDLHRTRLWLNDATGQVLRNGLDLLGVSAPERM 555
Cdd:pfam05746 80 V--LDEDN--EERNARLALLKAVRQVLKNGLDLLGIEAPEKM 117
|
|
| PLN02286 |
PLN02286 |
arginine-tRNA ligase |
41-555 |
1.03e-28 |
|
arginine-tRNA ligase
Pssm-ID: 215160 [Multi-domain] Cd Length: 576 Bit Score: 120.13 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 41 NRDHGDWASNAAMKLAKRVG------TNPREFAAEIAAALAETPGVASVEVAGPGFINIRL-DAAAAGALAREIVEAGAA 113
Cdd:PLN02286 30 NPKFGDYQCNNAMGLWSKLKgkgtsfKNPRAVAQAIVKNLPASEMIESTSVAGPGFVNVRLsASWLAKRIERMLVDGIDT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 114 FGRNDSQagNSINLEFVSANPTGPMHIGHTRWAALGDAIARLLLASGAELVREFYINDAGAQmqrFGRSVLASAKGEPTP 193
Cdd:PLN02286 110 WAPTLPV--KRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEFSGVEVLRRNHVGDWGTQ---FGMLIEHLFEKFPNW 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 194 EDGYPGAyIDDL------ARRVLSARPDLLTLApeEQEQVALDLGYELQMADLKDSLEKFNVHFDVFFseRLLHATPADG 267
Cdd:PLN02286 185 ESVSDQA-IGDLqefykaAKKRFDEDEEFKARA--QQAVVRLQGGDPEYRAAWAKICEISRREFEKVY--QRLRVELEEK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 268 GPS----LVDQAVDRLRAQGHVFDQDDAVWVRTTdfGDDKDRVIRRSNGEYTYFAADAA---YYLN--KGDRgfahKIYL 338
Cdd:PLN02286 260 GESfynpYIPGVIEELESKGLVVESDGARVIFVE--GFDIPLIVVKSDGGFNYASTDLAalwYRLNeeKAEW----IIYV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 339 LGADHHGYVHRLKALAGAAG----DDPEKDIEVLIGQLVSVNGARLSKRAGNIIELDDLRD------------------W 396
Cdd:PLN02286 334 TDVGQQQHFDMVFKAAKRAGwlpeDTYPRLEHVGFGLVLGEDGKRFRTRSGEVVRLVDLLDeaksrskaaliergkdseW 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 397 LGTD------ALRYSLARYpAD---SPLT---------LDpeilqkrTNDNPVFYVQYAHARTHNVARNAADSGVTRDAF 458
Cdd:PLN02286 414 TPEEleqaaeAVGYGAVKY-ADlknNRLTnytfsfdqmLD-------LKGNTAVYLLYAHARICSIIRKSGKDIDELKKT 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 459 APEMLDHETESALLGALQEFPRIVAFAAELREPHRVARYLEELASLYHRWYDTCRVtpLGDEEVTdlhrTRLWLNDATGQ 538
Cdd:PLN02286 486 GKIVLDHPDERALGLHLLQFPEVVEEACTDLLPNRLCEYLYNLSEKFTKFYSNCKV--NGSEEET----SRLLLCEATAI 559
|
570
....*....|....*..
gi 1654126220 539 VLRNGLDLLGVSAPERM 555
Cdd:PLN02286 560 VMRKCFHLLGITPLYRL 576
|
|
| Arg_tRNA_synt_N |
smart01016 |
Arginyl tRNA synthetase N terminal dom; This domain is found at the amino terminus of Arginyl ... |
17-95 |
9.63e-19 |
|
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: 80.71 E-value: 9.63e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654126220 17 LAEARRPGSSDGLTAADFVFERPKNRDHGDWASNAAMKLAKRVGTNPREFAAEIAAALAETPGVASVEVAGPGFINIRL 95
Cdd:smart01016 7 IAEALKKALGVEGEPIDIALERPKDPDHGDYATNVAFRLAKKLKKNPRELAEEIAEKLPKSDLVEKVEIAGPGFINFFL 85
|
|
| tRNA-synt_1d |
pfam00750 |
tRNA synthetases class I (R); Other tRNA synthetase sub-families are too dissimilar to be ... |
127-395 |
1.31e-17 |
|
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: 84.54 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 127 LEFVSANPTGPMHIGHTRWAALGDAIARLLLASGAELVREFYINDAGAQmqrFGrsVLASAKGEPTPEDGYPGAYIDDLA 206
Cdd:pfam00750 23 VDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQ---FG--MLIAGLEKYQDEKTLQEMPIQDLE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 207 RRVLSARPDLLTlaPEEQEQVALDLGYELQMAD-------------LKDSLEKFNVHFDVFFSERllhatpadgGPSL-- 271
Cdd:pfam00750 98 DFYREAKKHYDE--EEEFAERARNYVVKLQSGDeywrrmwklivdiTMTQNQRLYDRLDVTLTEM---------GESLyn 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 272 --VDQAVDRLRAQGHVFDQDDAVWVRTTDFGDDKDRVIRRSNGEYTYFAADAA-----YYLNKGDRgfahKIYLLGADHH 344
Cdd:pfam00750 167 pmMNEIVKDFKKNGLVVEIDGALVVFLDEFGKPMGVIVQKSDGGYLYTTTDIAaakyrYETLHADR----MLYVIDSRQS 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1654126220 345 GYVHRLKALAGAAGDDPE-KDIE-VLIGQLVSVNGARLSKRAGNIIELDDLRD 395
Cdd:pfam00750 243 QHMQQAFAILRKAGYVPEsKDLEhINFGMVLGKDGKPFKTRKGGTVKLADLLD 295
|
|
| Arg_tRNA_synt_N |
pfam03485 |
Arginyl tRNA synthetase N terminal domain; This domain is found at the amino terminus of ... |
4-95 |
1.38e-17 |
|
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: 77.66 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 4 DALAEALLSVVAPLAEArrpgssdgltaADFVFERPKNRDHGDWASNAAMKLAKRVGTNPREFAAEIAAALAETPGVASV 83
Cdd:pfam03485 3 KAIAKALSKLGGPDLEL-----------IDIVIETPKNPKFGDYATNVAMQLAKKLKKNPREIAEEIAEKLEKSDIIEKV 71
|
90
....*....|..
gi 1654126220 84 EVAGPGFINIRL 95
Cdd:pfam03485 72 EVAGPGFINFFL 83
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
128-217 |
3.85e-04 |
|
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: 40.93 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 128 EFVSANPTGPMHIGHTRWAALGDAIARLLLASGAELVREFYINDAGAQmqrfgRSVLASAKGEPTPE--DGYPGAYIDDL 205
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGL-----IGDPANKKGENAKAfvERWIERIKEDV 76
|
90
....*....|..
gi 1654126220 206 ARRVLSARPDLL 217
Cdd:cd00802 77 EYMFLQAADFLL 88
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
373-429 |
1.57e-03 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 41.12 E-value: 1.57e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1654126220 373 VSVNGARLSKRAGNIIELDDLRDWLGTDALRYSLARY-PADSPLTLDPEILQKRTNDN 429
Cdd:pfam09334 318 LTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARNrPETKDTDFSWEDFVERVNSE 375
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
366-411 |
2.25e-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: 40.31 E-value: 2.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1654126220 366 EVLIGQLV-SVNGARLSKRAGNIIELDDLRDWLGTDALRYSLARYPA 411
Cdd:cd00817 329 EVYLHGLVrDEDGRKMSKSLGNVIDPLDVIDGYGADALRFTLASAAT 375
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
329-407 |
2.58e-03 |
|
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.
Pssm-ID: 459685 [Multi-domain] Cd Length: 602 Bit Score: 40.47 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654126220 329 DRGFAHKIYLLGADHH-GYVHRLKALAGA-AGDDPEKdiEVLIGQLV-SVNGARLSKRAGNIIELDDLRDWLGTDALRYS 405
Cdd:pfam00133 512 KKFFPADMLLEGSDQTrGWFYRMIMLSTAlTGSVPFK--NVLVHGLVrDEQGRKMSKSLGNVIDPLDVIDKYGADALRLW 589
|
..
gi 1654126220 406 LA 407
Cdd:pfam00133 590 LA 591
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
366-409 |
3.29e-03 |
|
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase and is particularly closely related to the isoleucyl tRNA synthetase. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273070 [Multi-domain] Cd Length: 861 Bit Score: 40.43 E-value: 3.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1654126220 366 EVLIGQLV-SVNGARLSKRAGNIIELDDLRDWLGTDALRYSLARY 409
Cdd:TIGR00422 511 EVYIHGLVrDEQGRKMSKSLGNVIDPLDVIEKYGADALRFTLASL 555
|
|
| |
