|
Name |
Accession |
Description |
Interval |
E-value |
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
21-550 |
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: 641.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 21 HDADVSIVPENPTVERPRNPEHGDYATNIAMQLGKRVGMVPRDLATEIATALGASEGIDEATIAGPGFINIRLASDAQGK 100
Cdd:COG0018 16 AALGAGLEEPDILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDADPLVEKVEIAGPGFINFFLSPAALAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 101 IVEDVLAAGEKWGHADFNSNLDVNLEFVSANPTGPIHLGGTRWAAVGDALGRVLSATGAKVTREYYFNDHGRQIDRFSDS 180
Cdd:COG0018 96 VLKEILADGEDYGRSDAGKGKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYDVTRENYINDAGTQIGKLALS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 181 LVAAARNEPTPE---DGYGGE-YIQ------------DIAAAVLEKnpqaLEGSEEEVQEhFRAIGVDMMFEHIKKSLHE 244
Cdd:COG0018 176 LERYGEEEIEPEskpDGYLGDlYVKfhkeyeedpeleDIARELLAK----LEPGDEEALE-LWKKAVDWSLEEIKEDLKR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 245 FGTDFDVYFHENSLFESGQVEAAVNSLKENGKLYEADGAWWLKSTDYGDDKDRVVIKSDGDAAYIAGDIAYVKNKFDRGH 324
Cdd:COG0018 251 LGVEFDVWFSESSLYDSGAVEEVVEELKEKGLLYESDGALWVRLTEFGDDKDRVLVKSDGTYTYFTTDIAYHLYKFERYG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 325 -NLCIYMLGADHHGYIARLRAAAAALGYN-ADGVEVLIGQMVNlLRDGKavRMSKRAGTVVTLDDLVE------------ 390
Cdd:COG0018 331 fDRVIYVVGADQHGHFKRLFAALKALGYDpAKDLEHLLFGMVN-LRDGE--KMSTRAGTVVTLDDLLDeaverareiiee 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 391 -----------AIGVDAARYSLIRSSVDSSLDIDLGLWAS-QSSDNPvyYVQYGHARLCSIGRRAEEAGVTSEGADFSLL 458
Cdd:COG0018 408 kseeekeeiaeQVGIDAVRYFDLSRSRDKDLDFDLDLALSfEGNTNP--YVQYAHARICSILRKAGEELDGLAEADLSLL 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 459 VEDREGELIRTIGEFPAIIKSAADLREPHRIARYAEQLAGVFHRFYDTCQILpkaDEEVSELHRARLGLAEATRQTLANA 538
Cdd:COG0018 486 TEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRIL---KAEDEELRAARLALVAATAQVLKNG 562
|
570
....*....|..
gi 1063218703 539 LQLLGVTAPERM 550
Cdd:COG0018 563 LGLLGISAPERM 574
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
20-550 |
0e+00 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 606.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 20 AHDADVSIVPENPTVERPRNPEHGDYATNIAMQLGKRVGMVPRDLATEIAtalgasEGIDEATIAGPGFINIRLASDAQG 99
Cdd:PRK01611 16 ALEAGGLPELPAVLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIV------EAIEKVEIAGPGFINFFLDPAALA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 100 KIVEDVLAAGEKWGHADFNSNLDVNLEFVSANPTGPIHLGGTRWAAVGDALGRVLSATGAKVTREYYFNDHGRQIDRFSD 179
Cdd:PRK01611 90 ELVLAILEAGERYGRSDIGKGKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDVTREYYVNDAGTQIGMLIA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 180 SLvaaarneptpedgyggeyiqdiaaavleknpqalegseeevqEHFRAIGVDMMFEHIKKSLHEFGTDFDVYFHENSLF 259
Cdd:PRK01611 170 SL------------------------------------------ELLWRKAVDISLDEIKEDLDRLGVHFDVWFSESELY 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 260 ESGQVEAAVNSLKENGKLY-EADGAWWLKSTDYGDDKDRVVIKSDGDAAYIAGDIAYVKNKFDRgHNLCIYMLGADHHGY 338
Cdd:PRK01611 208 YNGKVDEVVEDLKEKGLLYvESDGALWVRLTEFGDDKDRVLIKSDGTYTYFTRDIAYHLYKFER-FDRVIYVVGADHHGH 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 339 IARLRAAAAALGYNADGVEVLIGQMVNLLRDGKAVRMSKRAGTVVTLDDLVE-----------------AIGVDAARYSL 401
Cdd:PRK01611 287 FKRLKAALKALGYDPDALEVLLHQMVGLVRGGEGVKMSTRAGNVVTLDDLLDeavgrarelieekeiaeAVGIDAVRYFD 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 402 IRSSVDSSLDIDLGLWASQSSDNPVyYVQYGHARLCSIGRRAEEAGVTsegADFSLLVEDREGELIRTIGEFPAIIKSAA 481
Cdd:PRK01611 367 LSRSRDKDLDFDLDLALSFEGNNPP-YVQYAHARICSILRKAAEAGID---LLLALLTEEEEKELIKKLAEFPEVVESAA 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063218703 482 DLREPHRIARYAEQLAGVFHRFYDtcQILPKADEEvsELHRARLGLAEATRQTLANALQLLGVTAPERM 550
Cdd:PRK01611 443 EELEPHRIANYLYELAGAFHSFYN--RVLLKDEEE--ELRNARLALVKATAQVLKNGLDLLGISAPERM 507
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
6-550 |
2.56e-141 |
|
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: 419.82 E-value: 2.56e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 6 LAVLVRKVTVEVLTAHDADVSivpeNPTVERPRNPEHGDYATNIAMQLGKRVGMVPRDLATEIATALGASEGIDEATIAG 85
Cdd:TIGR00456 2 KTLLKEEISQALLKAGLSKES----EILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKLKTGEIIEKVEAAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 86 PgFINIRLASDAQGK-IVEDVLAAGEKWGHADFNsNLDVNLEFVSANPTGPIHLGGTRWAAVGDALGRVLSATGAKVTRE 164
Cdd:TIGR00456 78 P-FINFFLSPQKLLErLIQKILTQKEKYGSKKLK-NKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIRE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 165 YYFNDHGRQIDRFSDSLVAAARNE-----PTPEDGYGGEYIQdiAAAVLEKNPQALEGSEEEVQE---------HFRAIG 230
Cdd:TIGR00456 156 YYVNDWGRQFGLLALGVEKFGNEAlniavKKPDHGLEGFYVE--INKRLEENEELEEEARELFVKlesgdeetiKLWKRL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 231 VDMMFEHIKKSLHEFGTDFDVYFHENSLFESGQVEAAVNSLKENGKLYEaDGAWWLKSTDYGDDKDRVVIKSDGDAAYIA 310
Cdd:TIGR00456 234 VEYSLEGIKETYDRLNIHFDSFVWEGESVKNGMLPKVLEDLKEKGLVVE-DGALWLDLTLFGDKKDRVLQKSDGTYLYLT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 311 GDIAYVKNKFDRGHNLCIYMLGADHHGYIARLRAAAAALGYNADGVEVLIGQMVNLL----RDGKAV-------RMSKRA 379
Cdd:TIGR00456 313 TDIAYHLDKLERGFDKMIYVWGSDHHLHIAQMFAILEKLGYKKKELEHLNFGMVPLYsmktRRGNVIsldnlldEASKRA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 380 GTVVT------LDDLVEAIGVDAARYSLIRSSVDSSLDIDLGLwASQSSDNPVYYVQYGHARLCSIGRRAEEAGVTSEGA 453
Cdd:TIGR00456 393 GNVITikndleEEKVADAVGIGAVRYFDLSKNRTTDYVFDWDA-MLSFEGNTAPYIQYAHARICSILRKAEIDGEKLIAD 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 454 DFSLLvEDREGELIRTIGEFPAIIKSAADLREPHRIARYAEQLAGVFHRFYDTCQILpKADEEVSelhRARLGLAEATRQ 533
Cdd:TIGR00456 472 DFELL-EEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACPVL-DAENELA---AARLALLKATRQ 546
|
570
....*....|....*..
gi 1063218703 534 TLANALQLLGVTAPERM 550
Cdd:TIGR00456 547 TLKNGLDLLGIEPPERM 563
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
123-380 |
3.33e-72 |
|
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: 229.37 E-value: 3.33e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 123 VNLEFVSANPTGPIHLGGTRWAAVGDALGRVLSATGAKVTREYYFNDHGRQIDRFSDSLvaaarneptpedgyggeyiqd 202
Cdd:cd00671 2 ILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSL--------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 203 iaaavleknpqalegseeevqEHFRaigvDMMFEHIKKSLHEFGT---DFDVYFHENSLfeSGQVEAAVNSLKENGKLYE 279
Cdd:cd00671 61 ---------------------EKWR----KLVEESIKADLETYGRldvRFDVWFGESSY--LGLMGKVVELLEELGLLYE 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 280 ADGAWWLKSTDYGDDKDRVVIKSDGDAAYIAGDIAYVKNKFDRGHNLCIYMLGADHHGYIARLRAAAAALGYN-ADGVEV 358
Cdd:cd00671 114 EDGALWLDLTEFGDDKDRVLVRSDGTYTYFTRDIAYHLDKFERGADKIIYVVGADHHGHFKRLFAALELLGYDeAKKLEH 193
|
250 260
....*....|....*....|..
gi 1063218703 359 LIGQMVNLLRDGKavrMSKRAG 380
Cdd:cd00671 194 LLYGMVNLPKEGK---MSTRAG 212
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
429-550 |
1.01e-48 |
|
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: 164.67 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 429 VQYGHARLCSIGRRAEEAGVT---SEGADFSLLVEDREGELIRTIGEFPAIIKSAADLREPHRIARYAEQLAGVFHRFYD 505
Cdd:smart00836 1 VQYAHARICSILRKAGEAGETlpdIADADLSLLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYN 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1063218703 506 TCQILpkaDEEVSELHRARLGLAEATRQTLANALQLLGVTAPERM 550
Cdd:smart00836 81 RVRVL---GEENPELRKARLALLKAVRQVLANGLRLLGISAPERM 122
|
|
| DALR_1 |
pfam05746 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
429-550 |
1.04e-42 |
|
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: 148.18 E-value: 1.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 429 VQYGHARLCSIGRRAEEAGVTSEgADFSLLVEDREGELIRTIGEFPAIIKSAADLREPHRIARYAEQLAGVFHRFYDTCQ 508
Cdd:pfam05746 1 LQYAHARICSILRKAGELGINLD-IDADLLTEEEEKELLKALLQFPEVLEEAAEELEPHRLANYLYELASAFHSFYNNCR 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1063218703 509 ILPKADEEVselhRARLGLAEATRQTLANALQLLGVTAPERM 550
Cdd:pfam05746 80 VLDEDNEER----NARLALLKAVRQVLKNGLDLLGIEAPEKM 117
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
21-550 |
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: 641.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 21 HDADVSIVPENPTVERPRNPEHGDYATNIAMQLGKRVGMVPRDLATEIATALGASEGIDEATIAGPGFINIRLASDAQGK 100
Cdd:COG0018 16 AALGAGLEEPDILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDADPLVEKVEIAGPGFINFFLSPAALAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 101 IVEDVLAAGEKWGHADFNSNLDVNLEFVSANPTGPIHLGGTRWAAVGDALGRVLSATGAKVTREYYFNDHGRQIDRFSDS 180
Cdd:COG0018 96 VLKEILADGEDYGRSDAGKGKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYDVTRENYINDAGTQIGKLALS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 181 LVAAARNEPTPE---DGYGGE-YIQ------------DIAAAVLEKnpqaLEGSEEEVQEhFRAIGVDMMFEHIKKSLHE 244
Cdd:COG0018 176 LERYGEEEIEPEskpDGYLGDlYVKfhkeyeedpeleDIARELLAK----LEPGDEEALE-LWKKAVDWSLEEIKEDLKR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 245 FGTDFDVYFHENSLFESGQVEAAVNSLKENGKLYEADGAWWLKSTDYGDDKDRVVIKSDGDAAYIAGDIAYVKNKFDRGH 324
Cdd:COG0018 251 LGVEFDVWFSESSLYDSGAVEEVVEELKEKGLLYESDGALWVRLTEFGDDKDRVLVKSDGTYTYFTTDIAYHLYKFERYG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 325 -NLCIYMLGADHHGYIARLRAAAAALGYN-ADGVEVLIGQMVNlLRDGKavRMSKRAGTVVTLDDLVE------------ 390
Cdd:COG0018 331 fDRVIYVVGADQHGHFKRLFAALKALGYDpAKDLEHLLFGMVN-LRDGE--KMSTRAGTVVTLDDLLDeaverareiiee 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 391 -----------AIGVDAARYSLIRSSVDSSLDIDLGLWAS-QSSDNPvyYVQYGHARLCSIGRRAEEAGVTSEGADFSLL 458
Cdd:COG0018 408 kseeekeeiaeQVGIDAVRYFDLSRSRDKDLDFDLDLALSfEGNTNP--YVQYAHARICSILRKAGEELDGLAEADLSLL 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 459 VEDREGELIRTIGEFPAIIKSAADLREPHRIARYAEQLAGVFHRFYDTCQILpkaDEEVSELHRARLGLAEATRQTLANA 538
Cdd:COG0018 486 TEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRIL---KAEDEELRAARLALVAATAQVLKNG 562
|
570
....*....|..
gi 1063218703 539 LQLLGVTAPERM 550
Cdd:COG0018 563 LGLLGISAPERM 574
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
20-550 |
0e+00 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 606.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 20 AHDADVSIVPENPTVERPRNPEHGDYATNIAMQLGKRVGMVPRDLATEIAtalgasEGIDEATIAGPGFINIRLASDAQG 99
Cdd:PRK01611 16 ALEAGGLPELPAVLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIV------EAIEKVEIAGPGFINFFLDPAALA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 100 KIVEDVLAAGEKWGHADFNSNLDVNLEFVSANPTGPIHLGGTRWAAVGDALGRVLSATGAKVTREYYFNDHGRQIDRFSD 179
Cdd:PRK01611 90 ELVLAILEAGERYGRSDIGKGKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDVTREYYVNDAGTQIGMLIA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 180 SLvaaarneptpedgyggeyiqdiaaavleknpqalegseeevqEHFRAIGVDMMFEHIKKSLHEFGTDFDVYFHENSLF 259
Cdd:PRK01611 170 SL------------------------------------------ELLWRKAVDISLDEIKEDLDRLGVHFDVWFSESELY 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 260 ESGQVEAAVNSLKENGKLY-EADGAWWLKSTDYGDDKDRVVIKSDGDAAYIAGDIAYVKNKFDRgHNLCIYMLGADHHGY 338
Cdd:PRK01611 208 YNGKVDEVVEDLKEKGLLYvESDGALWVRLTEFGDDKDRVLIKSDGTYTYFTRDIAYHLYKFER-FDRVIYVVGADHHGH 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 339 IARLRAAAAALGYNADGVEVLIGQMVNLLRDGKAVRMSKRAGTVVTLDDLVE-----------------AIGVDAARYSL 401
Cdd:PRK01611 287 FKRLKAALKALGYDPDALEVLLHQMVGLVRGGEGVKMSTRAGNVVTLDDLLDeavgrarelieekeiaeAVGIDAVRYFD 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 402 IRSSVDSSLDIDLGLWASQSSDNPVyYVQYGHARLCSIGRRAEEAGVTsegADFSLLVEDREGELIRTIGEFPAIIKSAA 481
Cdd:PRK01611 367 LSRSRDKDLDFDLDLALSFEGNNPP-YVQYAHARICSILRKAAEAGID---LLLALLTEEEEKELIKKLAEFPEVVESAA 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063218703 482 DLREPHRIARYAEQLAGVFHRFYDtcQILPKADEEvsELHRARLGLAEATRQTLANALQLLGVTAPERM 550
Cdd:PRK01611 443 EELEPHRIANYLYELAGAFHSFYN--RVLLKDEEE--ELRNARLALVKATAQVLKNGLDLLGISAPERM 507
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
6-550 |
2.56e-141 |
|
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: 419.82 E-value: 2.56e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 6 LAVLVRKVTVEVLTAHDADVSivpeNPTVERPRNPEHGDYATNIAMQLGKRVGMVPRDLATEIATALGASEGIDEATIAG 85
Cdd:TIGR00456 2 KTLLKEEISQALLKAGLSKES----EILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKLKTGEIIEKVEAAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 86 PgFINIRLASDAQGK-IVEDVLAAGEKWGHADFNsNLDVNLEFVSANPTGPIHLGGTRWAAVGDALGRVLSATGAKVTRE 164
Cdd:TIGR00456 78 P-FINFFLSPQKLLErLIQKILTQKEKYGSKKLK-NKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIRE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 165 YYFNDHGRQIDRFSDSLVAAARNE-----PTPEDGYGGEYIQdiAAAVLEKNPQALEGSEEEVQE---------HFRAIG 230
Cdd:TIGR00456 156 YYVNDWGRQFGLLALGVEKFGNEAlniavKKPDHGLEGFYVE--INKRLEENEELEEEARELFVKlesgdeetiKLWKRL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 231 VDMMFEHIKKSLHEFGTDFDVYFHENSLFESGQVEAAVNSLKENGKLYEaDGAWWLKSTDYGDDKDRVVIKSDGDAAYIA 310
Cdd:TIGR00456 234 VEYSLEGIKETYDRLNIHFDSFVWEGESVKNGMLPKVLEDLKEKGLVVE-DGALWLDLTLFGDKKDRVLQKSDGTYLYLT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 311 GDIAYVKNKFDRGHNLCIYMLGADHHGYIARLRAAAAALGYNADGVEVLIGQMVNLL----RDGKAV-------RMSKRA 379
Cdd:TIGR00456 313 TDIAYHLDKLERGFDKMIYVWGSDHHLHIAQMFAILEKLGYKKKELEHLNFGMVPLYsmktRRGNVIsldnlldEASKRA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 380 GTVVT------LDDLVEAIGVDAARYSLIRSSVDSSLDIDLGLwASQSSDNPVYYVQYGHARLCSIGRRAEEAGVTSEGA 453
Cdd:TIGR00456 393 GNVITikndleEEKVADAVGIGAVRYFDLSKNRTTDYVFDWDA-MLSFEGNTAPYIQYAHARICSILRKAEIDGEKLIAD 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 454 DFSLLvEDREGELIRTIGEFPAIIKSAADLREPHRIARYAEQLAGVFHRFYDTCQILpKADEEVSelhRARLGLAEATRQ 533
Cdd:TIGR00456 472 DFELL-EEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACPVL-DAENELA---AARLALLKATRQ 546
|
570
....*....|....*..
gi 1063218703 534 TLANALQLLGVTAPERM 550
Cdd:TIGR00456 547 TLKNGLDLLGIEPPERM 563
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
123-380 |
3.33e-72 |
|
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: 229.37 E-value: 3.33e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 123 VNLEFVSANPTGPIHLGGTRWAAVGDALGRVLSATGAKVTREYYFNDHGRQIDRFSDSLvaaarneptpedgyggeyiqd 202
Cdd:cd00671 2 ILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSL--------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 203 iaaavleknpqalegseeevqEHFRaigvDMMFEHIKKSLHEFGT---DFDVYFHENSLfeSGQVEAAVNSLKENGKLYE 279
Cdd:cd00671 61 ---------------------EKWR----KLVEESIKADLETYGRldvRFDVWFGESSY--LGLMGKVVELLEELGLLYE 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 280 ADGAWWLKSTDYGDDKDRVVIKSDGDAAYIAGDIAYVKNKFDRGHNLCIYMLGADHHGYIARLRAAAAALGYN-ADGVEV 358
Cdd:cd00671 114 EDGALWLDLTEFGDDKDRVLVRSDGTYTYFTRDIAYHLDKFERGADKIIYVVGADHHGHFKRLFAALELLGYDeAKKLEH 193
|
250 260
....*....|....*....|..
gi 1063218703 359 LIGQMVNLLRDGKavrMSKRAG 380
Cdd:cd00671 194 LLYGMVNLPKEGK---MSTRAG 212
|
|
| Anticodon_Ia_Arg |
cd07956 |
Anticodon-binding domain of arginyl tRNA synthetases; This domain is found in arginyl tRNA ... |
390-550 |
3.23e-52 |
|
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: 175.10 E-value: 3.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 390 EAIGVDAARYSLIRSSVDSSLDIDLGLWASQSSDnPVYYVQYGHARLCSIGRRAEEAGVTSEGADFSLLVEDREGELIRT 469
Cdd:cd07956 1 EEVGVGAVKYQDLSNKRIKDYTFDWERMLSFEGD-TGPYLQYAHARLCSILRKAGETIEAEADADLSLLPEPDERDLILL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 470 IGEFPAIIKSAADLREPHRIARYAEQLAGVFHRFYDTCQILpKADEEVSElhrARLGLAEATRQTLANALQLLGVTAPER 549
Cdd:cd07956 80 LAKFPEVVKNAAETLEPHTIATYLFDLAHAFSKFYNACPVL-GAEEELRN---ARLALVAAARQVLANGLDLLGIEAPER 155
|
.
gi 1063218703 550 M 550
Cdd:cd07956 156 M 156
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
429-550 |
1.01e-48 |
|
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: 164.67 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 429 VQYGHARLCSIGRRAEEAGVT---SEGADFSLLVEDREGELIRTIGEFPAIIKSAADLREPHRIARYAEQLAGVFHRFYD 505
Cdd:smart00836 1 VQYAHARICSILRKAGEAGETlpdIADADLSLLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYN 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1063218703 506 TCQILpkaDEEVSELHRARLGLAEATRQTLANALQLLGVTAPERM 550
Cdd:smart00836 81 RVRVL---GEENPELRKARLALLKAVRQVLANGLRLLGISAPERM 122
|
|
| DALR_1 |
pfam05746 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
429-550 |
1.04e-42 |
|
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: 148.18 E-value: 1.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 429 VQYGHARLCSIGRRAEEAGVTSEgADFSLLVEDREGELIRTIGEFPAIIKSAADLREPHRIARYAEQLAGVFHRFYDTCQ 508
Cdd:pfam05746 1 LQYAHARICSILRKAGELGINLD-IDADLLTEEEEKELLKALLQFPEVLEEAAEELEPHRLANYLYELASAFHSFYNNCR 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1063218703 509 ILPKADEEVselhRARLGLAEATRQTLANALQLLGVTAPERM 550
Cdd:pfam05746 80 VLDEDNEER----NARLALLKAVRQVLKNGLDLLGIEAPEKM 117
|
|
| PLN02286 |
PLN02286 |
arginine-tRNA ligase |
32-550 |
8.41e-34 |
|
arginine-tRNA ligase
Pssm-ID: 215160 [Multi-domain] Cd Length: 576 Bit Score: 135.15 E-value: 8.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 32 PTVERPRNPEHGDYATNIAMQLGKRVGMV------PRDLATEIATALGASEGIDEATIAGPGFINIRLASDAQGKIVEDV 105
Cdd:PLN02286 23 PLVAACTNPKFGDYQCNNAMGLWSKLKGKgtsfknPRAVAQAIVKNLPASEMIESTSVAGPGFVNVRLSASWLAKRIERM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 106 LAAG-EKWghADFNSNLDVNLEFVSANPTGPIHLGGTRWAAVGDALGRVLSATGAKVTREYYFNDHGRQIDRFSDSLVAA 184
Cdd:PLN02286 103 LVDGiDTW--APTLPVKRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEFSGVEVLRRNHVGDWGTQFGMLIEHLFEK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 185 ARNEPTPEDGYGGEYIQ---------DIAAAVLEKNPQA---LEGSEEEVQEHFRAI------GVDMMFEHIKKSLHEFG 246
Cdd:PLN02286 181 FPNWESVSDQAIGDLQEfykaakkrfDEDEEFKARAQQAvvrLQGGDPEYRAAWAKIceisrrEFEKVYQRLRVELEEKG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 247 TDFDVYFhenslfesgqVEAAVNSLKENGKLYEADGAWWLKSTdyGDDKDRVVIKSDGDAAYIAGDIAYVKNkfdRGHNL 326
Cdd:PLN02286 261 ESFYNPY----------IPGVIEELESKGLVVESDGARVIFVE--GFDIPLIVVKSDGGFNYASTDLAALWY---RLNEE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 327 C----IYMLGADHHGYIARLRAAAAALGYNADGVEVL---IGQMVNLLRDGKavRMSKRAGTVVTLDDLV---------- 389
Cdd:PLN02286 326 KaewiIYVTDVGQQQHFDMVFKAAKRAGWLPEDTYPRlehVGFGLVLGEDGK--RFRTRSGEVVRLVDLLdeaksrskaa 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 390 -------------------EAIGVDAARYSLIRS--------SVDSSLDIdlglwasqsSDNPVYYVQYGHARLCSIGRR 442
Cdd:PLN02286 404 liergkdsewtpeeleqaaEAVGYGAVKYADLKNnrltnytfSFDQMLDL---------KGNTAVYLLYAHARICSIIRK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 443 AE-EAGVTSEGADFSLLVEDrEGELIRTIGEFPAIIKSAADLREPHRIARYAEQLAGVFHRFYDTCQILpKADEEVSelh 521
Cdd:PLN02286 475 SGkDIDELKKTGKIVLDHPD-ERALGLHLLQFPEVVEEACTDLLPNRLCEYLYNLSEKFTKFYSNCKVN-GSEEETS--- 549
|
570 580
....*....|....*....|....*....
gi 1063218703 522 raRLGLAEATRQTLANALQLLGVTAPERM 550
Cdd:PLN02286 550 --RLLLCEATAIVMRKCFHLLGITPLYRL 576
|
|
| Arg_tRNA_synt_N |
smart01016 |
Arginyl tRNA synthetase N terminal dom; This domain is found at the amino terminus of Arginyl ... |
24-93 |
2.02e-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: 99.97 E-value: 2.02e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 24 DVSIVPENPTVERPRNPEHGDYATNIAMQLGKRVGMVPRDLATEIATALGASEGIDEATIAGPGFINIRL 93
Cdd:smart01016 16 GVEGEPIDIALERPKDPDHGDYATNVAFRLAKKLKKNPRELAEEIAEKLPKSDLVEKVEIAGPGFINFFL 85
|
|
| Arg_tRNA_synt_N |
pfam03485 |
Arginyl tRNA synthetase N terminal domain; This domain is found at the amino terminus of ... |
23-93 |
3.68e-25 |
|
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: 98.84 E-value: 3.68e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063218703 23 ADVSIVPENPTVERPRNPEHGDYATNIAMQLGKRVGMVPRDLATEIATALGASEGIDEATIAGPGFINIRL 93
Cdd:pfam03485 13 GGPDLELIDIVIETPKNPKFGDYATNVAMQLAKKLKKNPREIAEEIAEKLEKSDIIEKVEVAGPGFINFFL 83
|
|
| tRNA-synt_1d |
pfam00750 |
tRNA synthetases class I (R); Other tRNA synthetase sub-families are too dissimilar to be ... |
123-413 |
9.69e-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: 81.85 E-value: 9.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 123 VNLEFVSANPTGPIHLGGTRWAAVGDALGRVLSATGAKVTREYYFNDHGRQIdrfsdSLVAAARNEPTPEDGYGGEYIQD 202
Cdd:pfam00750 21 VVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQF-----GMLIAGLEKYQDEKTLQEMPIQD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 203 IAAAVLEKNPQALEgsEEEVQEHFRAIGV-----DMMFEHIKKSLHEFG--------TDFDVYFHE--NSLFESgQVEAA 267
Cdd:pfam00750 96 LEDFYREAKKHYDE--EEEFAERARNYVVklqsgDEYWRRMWKLIVDITmtqnqrlyDRLDVTLTEmgESLYNP-MMNEI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218703 268 VNSLKENGKLYEADGAWWLKSTDYGDDKDRVVIKSDGDAAYIAGDIAYVKNKFDRGH-NLCIYMLGADHHGYIARLRAAA 346
Cdd:pfam00750 173 VKDFKKNGLVVEIDGALVVFLDEFGKPMGVIVQKSDGGYLYTTTDIAAAKYRYETLHaDRMLYVIDSRQSQHMQQAFAIL 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063218703 347 AALGYNADGVEVL-IGQMVNLLRDGKavRMSKRAGTVVTLDDLVEAiGVDAARYSLIRSSVDSSLDID 413
Cdd:pfam00750 253 RKAGYVPESKDLEhINFGMVLGKDGK--PFKTRKGGTVKLADLLDE-ALERALQLIMEKNKDKILQAD 317
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
357-405 |
6.97e-04 |
|
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: 42.23 E-value: 6.97e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1063218703 357 EVLIGQMVnllRDGKAVRMSKRAGTVVTLDDLVEAIGVDAARYSLIRSS 405
Cdd:cd00817 329 EVYLHGLV---RDEDGRKMSKSLGNVIDPLDVIDGYGADALRFTLASAA 374
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
366-413 |
1.00e-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: 42.01 E-value: 1.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1063218703 366 LLRDGKAVRMSKRAGTVVTLDDLVEAIGVDAARYSLIRSSVDSSLDID 413
Cdd:pfam00133 555 LVRDEQGRKMSKSLGNVIDPLDVIDKYGADALRLWLANSDYGRDINLS 602
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
357-406 |
1.71e-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: 41.20 E-value: 1.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1063218703 357 EVLIGQMVnllRDGKAVRMSKRAGTVVTLDDLVEAIGVDAARYSLIRSSV 406
Cdd:TIGR00422 511 EVYIHGLV---RDEQGRKMSKSLGNVIDPLDVIEKYGADALRFTLASLVT 557
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
366-414 |
6.53e-03 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 39.20 E-value: 6.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1063218703 366 LLRDGKavrMSKRAGTVVTLDDLVEAIGVDAARYSLIRSSVDSSlDIDL 414
Cdd:pfam09334 319 TYEGGK---MSKSRGNVVWPSEALDRFPPDALRYYLARNRPETK-DTDF 363
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
366-404 |
7.21e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 39.01 E-value: 7.21e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1063218703 366 LLRDGKavrMSKRAGTVVTLDDLVEAIGVDAARYSLIRS 404
Cdd:PRK12267 294 LMKDGK---MSKSKGNVVDPEELVDRYGLDALRYYLLRE 329
|
|
| |
