|
Name |
Accession |
Description |
Interval |
E-value |
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
5-556 |
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: 604.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 5 DLSALLSAVLTDAVdagdlpAALREEITPARVKVERPRSREHGDWATNVALQLGKKAGMAPRDLAGLVAERLTDKPGIAA 84
Cdd:COG0018 2 NIKEELAEAIAAAL------AALGAGLEEPDILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDADPLVEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 85 VDVAGPGFLNVTLDAASAGALAREIVEAGPEYGRNDALAGHTVNMEFVSANPTGPLHIGHTRWAALGDAIARLLRASGAD 164
Cdd:COG0018 76 VEIAGPGFINFFLSPAALAAVLKEILADGEDYGRSDAGKGKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 165 VTAEYYVNDAGNQMNVFADSVLARLHGRDVPA---GGYPGA-YVQ--ELADAVALEHPDVRELT------DEAARPvVRE 232
Cdd:COG0018 156 VTRENYINDAGTQIGKLALSLERYGEEEIEPEskpDGYLGDlYVKfhKEYEEDPELEDIARELLaklepgDEEALE-LWK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 233 AAYRLQMQDIKNTLAAFDVHFDVFTSEQTLHDSGAIEQAVQRLRAQGHVEDREGAVWLKTTDFGDDKDRVLIRANGEPTY 312
Cdd:COG0018 235 KAVDWSLEEIKEDLKRLGVEFDVWFSESSLYDSGAVEEVVEELKEKGLLYESDGALWVRLTEFGDDKDRVLVKSDGTYTY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 313 FAADAAYYLHKRDR-GFEEKVYLLGADHHGYVNRLKAIAAAAGDDPATNIEILIGQLISV-NGAKLSKRAGNIIELKDLV 390
Cdd:COG0018 315 FTTDIAYHLYKFERyGFDRVIYVVGADQHGHFKRLFAALKALGYDPAKDLEHLLFGMVNLrDGEKMSTRAGTVVTLDDLL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 391 EWL-----------------------GRDALRYDLARYPADSPLTIDPELLRST-TNDNPvyYVQYAHARASGAARTAQA 446
Cdd:COG0018 395 DEAverareiieekseeekeeiaeqvGIDAVRYFDLSRSRDKDLDFDLDLALSFeGNTNP--YVQYAHARICSILRKAGE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 447 HGVDRSEFDAALLTHATESELLAQLAEFPAVVGAAARLREPHRVARHLEVIAGAYHSWYAACRIVPMPTddgtprpvETL 526
Cdd:COG0018 473 ELDGLAEADLSLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRILKAED--------EEL 544
|
570 580 590
....*....|....*....|....*....|
gi 1072319979 527 NRTRLWLNDATAQVLANGLGLLGVTAPEKM 556
Cdd:COG0018 545 RAARLALVAATAQVLKNGLGLLGISAPERM 574
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
4-556 |
0e+00 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 570.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 4 EDLSALLSAVLTDAVDAGDLPAalreeitPARVKVERPRSREHGDWATNVALQLGKKAGMAPRDLAGLVAERltdkpgIA 83
Cdd:PRK01611 3 MDIKELLAEALAAALEAGGLPE-------LPAVLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIVEA------IE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 84 AVDVAGPGFLNVTLDAASAGALAREIVEAGPEYGRNDALAGHTVNMEFVSANPTGPLHIGHTRWAALGDAIARLLRASGA 163
Cdd:PRK01611 70 KVEIAGPGFINFFLDPAALAELVLAILEAGERYGRSDIGKGKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 164 DVTAEYYVNDAGNQMNVFADSVLArlhgrdvpaggypgayvqeladavalehpdvreltdeaarpvVREAAYRLQMQDIK 243
Cdd:PRK01611 150 DVTREYYVNDAGTQIGMLIASLEL------------------------------------------LWRKAVDISLDEIK 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 244 NTLAAFDVHFDVFTSEQTLHDSGAIEQAVQRLRAQGH-VEDREGAVWLKTTDFGDDKDRVLIRANGEPTYFAADAAYYLH 322
Cdd:PRK01611 188 EDLDRLGVHFDVWFSESELYYNGKVDEVVEDLKEKGLlYVESDGALWVRLTEFGDDKDRVLIKSDGTYTYFTRDIAYHLY 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 323 KRDRgFEEKVYLLGADHHGYVNRLKAIAAAAGDDPAtNIEILIGQLISV----NGAKLSKRAGNIIELKDLVEWL----- 393
Cdd:PRK01611 268 KFER-FDRVIYVVGADHHGHFKRLKAALKALGYDPD-ALEVLLHQMVGLvrggEGVKMSTRAGNVVTLDDLLDEAvgrar 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 394 ------------GRDALRYDLARYPADSPLTIDPELLRSTTNDNPVYyVQYAHARASGAARTAQAHGVDrseFDAALLTH 461
Cdd:PRK01611 346 elieekeiaeavGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPPY-VQYAHARICSILRKAAEAGID---LLLALLTE 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 462 ATESELLAQLAEFPAVVGAAARLREPHRVARHLEVIAGAYHSWYAACRIVPmptddgtprPVETLNRTRLWLNDATAQVL 541
Cdd:PRK01611 422 EEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYNRVLLKD---------EEEELRNARLALVKATAQVL 492
|
570
....*....|....*
gi 1072319979 542 ANGLGLLGVTAPEKM 556
Cdd:PRK01611 493 KNGLDLLGISAPERM 507
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
36-556 |
4.78e-119 |
|
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: 362.81 E-value: 4.78e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 36 VKVERPRSREHGDWATNVALQLGKKAGMAPRDLAGLVAERLtDKPGIA-AVDVAGPgFLNVTLDAAS-AGALAREIVEAG 113
Cdd:TIGR00456 24 ILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKL-KTGEIIeKVEAAGP-FINFFLSPQKlLERLIQKILTQK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 114 PEYGRNDaLAGHTVNMEFVSANPTGPLHIGHTRWAALGDAIARLLRASGADVTAEYYVNDAGNQMNVFADSVLARLHGRD 193
Cdd:TIGR00456 102 EKYGSKK-LKNKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYVNDWGRQFGLLALGVEKFGNEAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 194 V-----PAGGYPGAYVQelADAVALEHPDVRELTDEAARPV---------VREAAYRLQMQDIKNTLAAFDVHFDVFTSE 259
Cdd:TIGR00456 181 NiavkkPDHGLEGFYVE--INKRLEENEELEEEARELFVKLesgdeetikLWKRLVEYSLEGIKETYDRLNIHFDSFVWE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 260 QTLHDSGAIEQAVQRLRAQGHVEdREGAVWLKTTDFGDDKDRVLIRANGEPTYFAADAAYYLHKRDRGFEEKVYLLGADH 339
Cdd:TIGR00456 259 GESVKNGMLPKVLEDLKEKGLVV-EDGALWLDLTLFGDKKDRVLQKSDGTYLYLTTDIAYHLDKLERGFDKMIYVWGSDH 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 340 HGYVNRLKAIAAAAGDDPaTNIEILI-------------GQLISVNG--AKLSKRAGNIIELK------DLVEWLGRDAL 398
Cdd:TIGR00456 338 HLHIAQMFAILEKLGYKK-KELEHLNfgmvplysmktrrGNVISLDNllDEASKRAGNVITIKndleeeKVADAVGIGAV 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 399 RYDLARYPADSPLTIDPELLRSTTNdNPVYYVQYAHARASGAARTAQAHGVDRSEFDaALLTHATESELLAQLAEFPAVV 478
Cdd:TIGR00456 417 RYFDLSKNRTTDYVFDWDAMLSFEG-NTAPYIQYAHARICSILRKAEIDGEKLIADD-FELLEEKEKELLKLLLQFPEVL 494
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1072319979 479 GAAARLREPHRVARHLEVIAGAYHSWYAACRIVpmptddGTPRPVEtlnRTRLWLNDATAQVLANGLGLLGVTAPEKM 556
Cdd:TIGR00456 495 EEAAEELEPHVLTNYLYELASLFSSFYKACPVL------DAENELA---AARLALLKATRQTLKNGLDLLGIEPPERM 563
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
126-381 |
6.34e-75 |
|
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: 236.69 E-value: 6.34e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 126 TVNMEFVSANPTGPLHIGHTRWAALGDAIARLLRASGADVTAEYYVNDAGNQMNVFADSVlarlhgrdvpaggypgayvq 205
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSL-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 206 eladavalehpdvreltdEAARPVVREAayrlqMQDIKNTLAAFDVHFDVFTSEQTLhdSGAIEQAVQRLRAQGHVEDRE 285
Cdd:cd00671 61 ------------------EKWRKLVEES-----IKADLETYGRLDVRFDVWFGESSY--LGLMGKVVELLEELGLLYEED 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 286 GAVWLKTTDFGDDKDRVLIRANGEPTYFAADAAYYLHKRDRGFEEKVYLLGADHHGYVNRLKAIAAAAGDDPATNIEILI 365
Cdd:cd00671 116 GALWLDLTEFGDDKDRVLVRSDGTYTYFTRDIAYHLDKFERGADKIIYVVGADHHGHFKRLFAALELLGYDEAKKLEHLL 195
|
250
....*....|....*..
gi 1072319979 366 GQLIS-VNGAKLSKRAG 381
Cdd:cd00671 196 YGMVNlPKEGKMSTRAG 212
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
430-556 |
2.70e-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: 125.77 E-value: 2.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 430 VQYAHARASGAARTAQAHGVDRSEF---DAALLTHATESELLAQLAEFPAVVGAAARLREPHRVARHLEVIAGAYHSWYA 506
Cdd:smart00836 1 VQYAHARICSILRKAGEAGETLPDIadaDLSLLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYN 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1072319979 507 ACRIVpmptddGTPRPVETLNrtRLWLNDATAQVLANGLGLLGVTAPEKM 556
Cdd:smart00836 81 RVRVL------GEENPELRKA--RLALLKAVRQVLANGLRLLGISAPERM 122
|
|
| DALR_1 |
pfam05746 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
430-556 |
8.33e-30 |
|
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: 113.13 E-value: 8.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 430 VQYAHARASGAARTAQaHGVDRSEFDAALLTHATESELLAQLAEFPAVVGAAARLREPHRVARHLEVIAGAYHSWYAACR 509
Cdd:pfam05746 1 LQYAHARICSILRKAG-ELGINLDIDADLLTEEEEKELLKALLQFPEVLEEAAEELEPHRLANYLYELASAFHSFYNNCR 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1072319979 510 IvpMPTDDgtprpvETLNRtRLWLNDATAQVLANGLGLLGVTAPEKM 556
Cdd:pfam05746 80 V--LDEDN------EERNA-RLALLKAVRQVLKNGLDLLGIEAPEKM 117
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
5-556 |
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: 604.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 5 DLSALLSAVLTDAVdagdlpAALREEITPARVKVERPRSREHGDWATNVALQLGKKAGMAPRDLAGLVAERLTDKPGIAA 84
Cdd:COG0018 2 NIKEELAEAIAAAL------AALGAGLEEPDILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDADPLVEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 85 VDVAGPGFLNVTLDAASAGALAREIVEAGPEYGRNDALAGHTVNMEFVSANPTGPLHIGHTRWAALGDAIARLLRASGAD 164
Cdd:COG0018 76 VEIAGPGFINFFLSPAALAAVLKEILADGEDYGRSDAGKGKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 165 VTAEYYVNDAGNQMNVFADSVLARLHGRDVPA---GGYPGA-YVQ--ELADAVALEHPDVRELT------DEAARPvVRE 232
Cdd:COG0018 156 VTRENYINDAGTQIGKLALSLERYGEEEIEPEskpDGYLGDlYVKfhKEYEEDPELEDIARELLaklepgDEEALE-LWK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 233 AAYRLQMQDIKNTLAAFDVHFDVFTSEQTLHDSGAIEQAVQRLRAQGHVEDREGAVWLKTTDFGDDKDRVLIRANGEPTY 312
Cdd:COG0018 235 KAVDWSLEEIKEDLKRLGVEFDVWFSESSLYDSGAVEEVVEELKEKGLLYESDGALWVRLTEFGDDKDRVLVKSDGTYTY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 313 FAADAAYYLHKRDR-GFEEKVYLLGADHHGYVNRLKAIAAAAGDDPATNIEILIGQLISV-NGAKLSKRAGNIIELKDLV 390
Cdd:COG0018 315 FTTDIAYHLYKFERyGFDRVIYVVGADQHGHFKRLFAALKALGYDPAKDLEHLLFGMVNLrDGEKMSTRAGTVVTLDDLL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 391 EWL-----------------------GRDALRYDLARYPADSPLTIDPELLRST-TNDNPvyYVQYAHARASGAARTAQA 446
Cdd:COG0018 395 DEAverareiieekseeekeeiaeqvGIDAVRYFDLSRSRDKDLDFDLDLALSFeGNTNP--YVQYAHARICSILRKAGE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 447 HGVDRSEFDAALLTHATESELLAQLAEFPAVVGAAARLREPHRVARHLEVIAGAYHSWYAACRIVPMPTddgtprpvETL 526
Cdd:COG0018 473 ELDGLAEADLSLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRILKAED--------EEL 544
|
570 580 590
....*....|....*....|....*....|
gi 1072319979 527 NRTRLWLNDATAQVLANGLGLLGVTAPEKM 556
Cdd:COG0018 545 RAARLALVAATAQVLKNGLGLLGISAPERM 574
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
4-556 |
0e+00 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 570.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 4 EDLSALLSAVLTDAVDAGDLPAalreeitPARVKVERPRSREHGDWATNVALQLGKKAGMAPRDLAGLVAERltdkpgIA 83
Cdd:PRK01611 3 MDIKELLAEALAAALEAGGLPE-------LPAVLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIVEA------IE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 84 AVDVAGPGFLNVTLDAASAGALAREIVEAGPEYGRNDALAGHTVNMEFVSANPTGPLHIGHTRWAALGDAIARLLRASGA 163
Cdd:PRK01611 70 KVEIAGPGFINFFLDPAALAELVLAILEAGERYGRSDIGKGKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 164 DVTAEYYVNDAGNQMNVFADSVLArlhgrdvpaggypgayvqeladavalehpdvreltdeaarpvVREAAYRLQMQDIK 243
Cdd:PRK01611 150 DVTREYYVNDAGTQIGMLIASLEL------------------------------------------LWRKAVDISLDEIK 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 244 NTLAAFDVHFDVFTSEQTLHDSGAIEQAVQRLRAQGH-VEDREGAVWLKTTDFGDDKDRVLIRANGEPTYFAADAAYYLH 322
Cdd:PRK01611 188 EDLDRLGVHFDVWFSESELYYNGKVDEVVEDLKEKGLlYVESDGALWVRLTEFGDDKDRVLIKSDGTYTYFTRDIAYHLY 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 323 KRDRgFEEKVYLLGADHHGYVNRLKAIAAAAGDDPAtNIEILIGQLISV----NGAKLSKRAGNIIELKDLVEWL----- 393
Cdd:PRK01611 268 KFER-FDRVIYVVGADHHGHFKRLKAALKALGYDPD-ALEVLLHQMVGLvrggEGVKMSTRAGNVVTLDDLLDEAvgrar 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 394 ------------GRDALRYDLARYPADSPLTIDPELLRSTTNDNPVYyVQYAHARASGAARTAQAHGVDrseFDAALLTH 461
Cdd:PRK01611 346 elieekeiaeavGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPPY-VQYAHARICSILRKAAEAGID---LLLALLTE 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 462 ATESELLAQLAEFPAVVGAAARLREPHRVARHLEVIAGAYHSWYAACRIVPmptddgtprPVETLNRTRLWLNDATAQVL 541
Cdd:PRK01611 422 EEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYNRVLLKD---------EEEELRNARLALVKATAQVL 492
|
570
....*....|....*
gi 1072319979 542 ANGLGLLGVTAPEKM 556
Cdd:PRK01611 493 KNGLDLLGISAPERM 507
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
36-556 |
4.78e-119 |
|
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: 362.81 E-value: 4.78e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 36 VKVERPRSREHGDWATNVALQLGKKAGMAPRDLAGLVAERLtDKPGIA-AVDVAGPgFLNVTLDAAS-AGALAREIVEAG 113
Cdd:TIGR00456 24 ILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKL-KTGEIIeKVEAAGP-FINFFLSPQKlLERLIQKILTQK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 114 PEYGRNDaLAGHTVNMEFVSANPTGPLHIGHTRWAALGDAIARLLRASGADVTAEYYVNDAGNQMNVFADSVLARLHGRD 193
Cdd:TIGR00456 102 EKYGSKK-LKNKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYVNDWGRQFGLLALGVEKFGNEAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 194 V-----PAGGYPGAYVQelADAVALEHPDVRELTDEAARPV---------VREAAYRLQMQDIKNTLAAFDVHFDVFTSE 259
Cdd:TIGR00456 181 NiavkkPDHGLEGFYVE--INKRLEENEELEEEARELFVKLesgdeetikLWKRLVEYSLEGIKETYDRLNIHFDSFVWE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 260 QTLHDSGAIEQAVQRLRAQGHVEdREGAVWLKTTDFGDDKDRVLIRANGEPTYFAADAAYYLHKRDRGFEEKVYLLGADH 339
Cdd:TIGR00456 259 GESVKNGMLPKVLEDLKEKGLVV-EDGALWLDLTLFGDKKDRVLQKSDGTYLYLTTDIAYHLDKLERGFDKMIYVWGSDH 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 340 HGYVNRLKAIAAAAGDDPaTNIEILI-------------GQLISVNG--AKLSKRAGNIIELK------DLVEWLGRDAL 398
Cdd:TIGR00456 338 HLHIAQMFAILEKLGYKK-KELEHLNfgmvplysmktrrGNVISLDNllDEASKRAGNVITIKndleeeKVADAVGIGAV 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 399 RYDLARYPADSPLTIDPELLRSTTNdNPVYYVQYAHARASGAARTAQAHGVDRSEFDaALLTHATESELLAQLAEFPAVV 478
Cdd:TIGR00456 417 RYFDLSKNRTTDYVFDWDAMLSFEG-NTAPYIQYAHARICSILRKAEIDGEKLIADD-FELLEEKEKELLKLLLQFPEVL 494
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1072319979 479 GAAARLREPHRVARHLEVIAGAYHSWYAACRIVpmptddGTPRPVEtlnRTRLWLNDATAQVLANGLGLLGVTAPEKM 556
Cdd:TIGR00456 495 EEAAEELEPHVLTNYLYELASLFSSFYKACPVL------DAENELA---AARLALLKATRQTLKNGLDLLGIEPPERM 563
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
126-381 |
6.34e-75 |
|
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: 236.69 E-value: 6.34e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 126 TVNMEFVSANPTGPLHIGHTRWAALGDAIARLLRASGADVTAEYYVNDAGNQMNVFADSVlarlhgrdvpaggypgayvq 205
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSL-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 206 eladavalehpdvreltdEAARPVVREAayrlqMQDIKNTLAAFDVHFDVFTSEQTLhdSGAIEQAVQRLRAQGHVEDRE 285
Cdd:cd00671 61 ------------------EKWRKLVEES-----IKADLETYGRLDVRFDVWFGESSY--LGLMGKVVELLEELGLLYEED 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 286 GAVWLKTTDFGDDKDRVLIRANGEPTYFAADAAYYLHKRDRGFEEKVYLLGADHHGYVNRLKAIAAAAGDDPATNIEILI 365
Cdd:cd00671 116 GALWLDLTEFGDDKDRVLVRSDGTYTYFTRDIAYHLDKFERGADKIIYVVGADHHGHFKRLFAALELLGYDEAKKLEHLL 195
|
250
....*....|....*..
gi 1072319979 366 GQLIS-VNGAKLSKRAG 381
Cdd:cd00671 196 YGMVNlPKEGKMSTRAG 212
|
|
| Anticodon_Ia_Arg |
cd07956 |
Anticodon-binding domain of arginyl tRNA synthetases; This domain is found in arginyl tRNA ... |
391-556 |
1.18e-36 |
|
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: 133.49 E-value: 1.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 391 EWLGRDALRY-DLARYPaDSPLTIDPELLRSTTNDnPVYYVQYAHARASGAARTAQAHGVDRSEFDAALLTHATESELLA 469
Cdd:cd07956 1 EEVGVGAVKYqDLSNKR-IKDYTFDWERMLSFEGD-TGPYLQYAHARLCSILRKAGETIEAEADADLSLLPEPDERDLIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 470 QLAEFPAVVGAAARLREPHRVARHLEVIAGAYHSWYAACRIVpmptddGTPRPVETLnrtRLWLNDATAQVLANGLGLLG 549
Cdd:cd07956 79 LLAKFPEVVKNAAETLEPHTIATYLFDLAHAFSKFYNACPVL------GAEEELRNA---RLALVAAARQVLANGLDLLG 149
|
....*..
gi 1072319979 550 VTAPEKM 556
Cdd:cd07956 150 IEAPERM 156
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
430-556 |
2.70e-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: 125.77 E-value: 2.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 430 VQYAHARASGAARTAQAHGVDRSEF---DAALLTHATESELLAQLAEFPAVVGAAARLREPHRVARHLEVIAGAYHSWYA 506
Cdd:smart00836 1 VQYAHARICSILRKAGEAGETLPDIadaDLSLLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYN 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1072319979 507 ACRIVpmptddGTPRPVETLNrtRLWLNDATAQVLANGLGLLGVTAPEKM 556
Cdd:smart00836 81 RVRVL------GEENPELRKA--RLALLKAVRQVLANGLRLLGISAPERM 122
|
|
| DALR_1 |
pfam05746 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
430-556 |
8.33e-30 |
|
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: 113.13 E-value: 8.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 430 VQYAHARASGAARTAQaHGVDRSEFDAALLTHATESELLAQLAEFPAVVGAAARLREPHRVARHLEVIAGAYHSWYAACR 509
Cdd:pfam05746 1 LQYAHARICSILRKAG-ELGINLDIDADLLTEEEEKELLKALLQFPEVLEEAAEELEPHRLANYLYELASAFHSFYNNCR 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1072319979 510 IvpMPTDDgtprpvETLNRtRLWLNDATAQVLANGLGLLGVTAPEKM 556
Cdd:pfam05746 80 V--LDEDN------EERNA-RLALLKAVRQVLKNGLDLLGIEAPEKM 117
|
|
| Arg_tRNA_synt_N |
smart01016 |
Arginyl tRNA synthetase N terminal dom; This domain is found at the amino terminus of Arginyl ... |
9-97 |
2.18e-23 |
|
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: 94.19 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 9 LLSAVLTDAVDAgdlpaALREEITPARVKVERPRSREHGDWATNVALQLGKKAGMAPRDLAGLVAERLTDKPGIAAVDVA 88
Cdd:smart01016 2 LLKEAIAEALKK-----ALGVEGEPIDIALERPKDPDHGDYATNVAFRLAKKLKKNPRELAEEIAEKLPKSDLVEKVEIA 76
|
....*....
gi 1072319979 89 GPGFLNVTL 97
Cdd:smart01016 77 GPGFINFFL 85
|
|
| PLN02286 |
PLN02286 |
arginine-tRNA ligase |
38-556 |
6.69e-23 |
|
arginine-tRNA ligase
Pssm-ID: 215160 [Multi-domain] Cd Length: 576 Bit Score: 102.41 E-value: 6.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 38 VERPRSREHGDWATNVALQLGKKAG------MAPRDLAGLVAERLTDKPGIAAVDVAGPGFLNVTLDAAS-AGALAREIV 110
Cdd:PLN02286 25 VAACTNPKFGDYQCNNAMGLWSKLKgkgtsfKNPRAVAQAIVKNLPASEMIESTSVAGPGFVNVRLSASWlAKRIERMLV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 111 EAGPEYGRndALAGHTVNMEFVSANPTGPLHIGHTRWAALGDAIARLLRASGADVTAEYYVNDAGNQMNVfadsVLARLH 190
Cdd:PLN02286 105 DGIDTWAP--TLPVKRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEFSGVEVLRRNHVGDWGTQFGM----LIEHLF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 191 GRdvpaggYP---GAYVQELADAVALEHP-DVRELTDEAARPVVREAAYRLQMQDIKnTLAAFDVHFDVFTSE------- 259
Cdd:PLN02286 179 EK------FPnweSVSDQAIGDLQEFYKAaKKRFDEDEEFKARAQQAVVRLQGGDPE-YRAAWAKICEISRREfekvyqr 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 260 --QTLHDSGA------IEQAVQRLRAQGHVEDREGAvwlkTTDFGDDKDRVLI--RANGEPTYFAADAAYYLHkrdRGFE 329
Cdd:PLN02286 252 lrVELEEKGEsfynpyIPGVIEELESKGLVVESDGA----RVIFVEGFDIPLIvvKSDGGFNYASTDLAALWY---RLNE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 330 EK----VYLLGADHHGYVNRLKAIAAAAG--DD---PATNiEILIGQLISVNGAKLSKRAGNIIELKDLV---------- 390
Cdd:PLN02286 325 EKaewiIYVTDVGQQQHFDMVFKAAKRAGwlPEdtyPRLE-HVGFGLVLGEDGKRFRTRSGEVVRLVDLLdeaksrskaa 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 391 --------EWLGRD------ALRYDLARYpAD---SPLT-----IDPELlrsTTNDNPVYYVQYAHARASGAARTAQAHG 448
Cdd:PLN02286 404 liergkdsEWTPEEleqaaeAVGYGAVKY-ADlknNRLTnytfsFDQML---DLKGNTAVYLLYAHARICSIIRKSGKDI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 449 VDRSEFDAALLTHATESELLAQLAEFPAVVGAAARLREPHRVARHLEVIAGAYHSWYAACRIVpmptddGTPRPvetlnR 528
Cdd:PLN02286 480 DELKKTGKIVLDHPDERALGLHLLQFPEVVEEACTDLLPNRLCEYLYNLSEKFTKFYSNCKVN------GSEEE-----T 548
|
570 580
....*....|....*....|....*...
gi 1072319979 529 TRLWLNDATAQVLANGLGLLGVTAPEKM 556
Cdd:PLN02286 549 SRLLLCEATAIVMRKCFHLLGITPLYRL 576
|
|
| Arg_tRNA_synt_N |
pfam03485 |
Arginyl tRNA synthetase N terminal domain; This domain is found at the amino terminus of ... |
6-97 |
1.36e-21 |
|
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: 88.83 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 6 LSALLSAVLTDAVDAGdlpaalreeITPARVKVERPRSREHGDWATNVALQLGKKAGMAPRDLAGLVAERLTDKPGIAAV 85
Cdd:pfam03485 1 LKKAIAKALSKLGGPD---------LELIDIVIETPKNPKFGDYATNVAMQLAKKLKKNPREIAEEIAEKLEKSDIIEKV 71
|
90
....*....|..
gi 1072319979 86 DVAGPGFLNVTL 97
Cdd:pfam03485 72 EVAGPGFINFFL 83
|
|
| tRNA-synt_1d |
pfam00750 |
tRNA synthetases class I (R); Other tRNA synthetase sub-families are too dissimilar to be ... |
126-414 |
2.25e-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: 83.77 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 126 TVNMEFVSANPTGPLHIGHTRWAALGDAIARLLRASGADVTAEYYVNDAGNQMNVFAdsVLARLHGRDVPAGGYPgayVQ 205
Cdd:pfam00750 20 KVVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQFGMLI--AGLEKYQDEKTLQEMP---IQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 206 ELADAV--ALEHPDVRELTDEAAR----------PVVREAAYRL---QMQDIKNTLAAFDVhFDVFTSEQTLHDSgaIEQ 270
Cdd:pfam00750 95 DLEDFYreAKKHYDEEEEFAERARnyvvklqsgdEYWRRMWKLIvdiTMTQNQRLYDRLDV-TLTEMGESLYNPM--MNE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 271 AVQRLRAQGHVEDREGAVWLKTTDFGDDKDRVLIRANGEPTYFAAD-AAYYLHKRDRGFEEKVYLLGADHHGYVNRLKAI 349
Cdd:pfam00750 172 IVKDFKKNGLVVEIDGALVVFLDEFGKPMGVIVQKSDGGYLYTTTDiAAAKYRYETLHADRMLYVIDSRQSQHMQQAFAI 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072319979 350 AAAAGDDP-ATNIE-ILIGQLISVNGAKLSKRAGNIIELKDLVEwLGRDALRYDLARYPADSPLTID 414
Cdd:pfam00750 252 LRKAGYVPeSKDLEhINFGMVLGKDGKPFKTRKGGTVKLADLLD-EALERALQLIMEKNKDKILQAD 317
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
136-405 |
3.88e-05 |
|
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. 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. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function.
Pssm-ID: 173907 [Multi-domain] Cd Length: 319 Bit Score: 45.99 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 136 PTGPLHIGHTRWAALGDAIARLLRASGADV-----TAEYyvndaGNqmnvfADSVLARLHGRDvpaggypgayVQELADA 210
Cdd:cd00814 11 VNGVPHLGHLYGTVLADVFARYQRLRGYDVlfvtgTDEH-----GT-----KIEQKAEEEGVT----------PQELCDK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 211 VALEHpdvreltdeaarpvvreaayrlqmqdiKNTLAAFDVHFDVF--TSEQTLHDsgAIEQAVQRLRAQGHVEDR--EG 286
Cdd:cd00814 71 YHEIF---------------------------KDLFKWLNISFDYFirTTSPRHKE--IVQEFFKKLYENGYIYEGeyEG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 287 ----------AVWLKTT----DFGDDKDRVL--IRANGE---PTYFAADAAYYLHK--RDR--------------GFEEK 331
Cdd:cd00814 122 lycvscerflPEWREEEhyffRLSKFQDRLLewLEKNPDfiwPENARNEVLSWLKEglKDLsitrdlfdwgipvpLDPGK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 332 V-Y-----LLgadhhGYVNRLKAIAAAAGDDP------------------------------ATNIE----ILIGQLISV 371
Cdd:cd00814 202 ViYvwfdaLI-----GYISATGYYNEEWGNSWwwkdgwpelvhfigkdiirfhaiywpamllGAGLPlptrIVAHGYLTV 276
|
330 340 350
....*....|....*....|....*....|....
gi 1072319979 372 NGAKLSKRAGNIIELKDLVEWLGRDALRYDLARY 405
Cdd:cd00814 277 EGKKMSKSRGNVVDPDDLLERYGADALRYYLLRE 310
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
330-414 |
1.31e-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: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 330 EKVYLLGAD---HHGYVnrLKAIAAAAGDDPATNIeiLIGQLISVNGAKLSKRAGNIIELKDLVEWLGRDALRYDLARYp 406
Cdd:pfam09334 280 ELVHFIGKDiiyFHTIF--WPAMLLGAGYRLPTTV--FAHGYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARN- 354
|
....*...
gi 1072319979 407 adSPLTID 414
Cdd:pfam09334 355 --RPETKD 360
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
323-403 |
2.41e-03 |
|
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases (IleRS) 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. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. IleRS 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: 173909 [Multi-domain] Cd Length: 338 Bit Score: 40.29 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319979 323 KRDRGFEEKVYLLGADHH-GYVNRLKAIAAAAGDDPATNIEILIGQLISVNGAKLSKRAGNIIELKDLVEWLGRDALRYD 401
Cdd:cd00818 246 DFEELFPADFILEGSDQTrGWFYSLLLLSTALFGKAPYKNVIVHGFVLDEDGRKMSKSLGNYVDPQEVVDKYGADALRLW 325
|
..
gi 1072319979 402 LA 403
Cdd:cd00818 326 VA 327
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
136-165 |
2.66e-03 |
|
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) 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. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173906 [Multi-domain] Cd Length: 314 Bit Score: 39.92 E-value: 2.66e-03
10 20 30
....*....|....*....|....*....|
gi 1072319979 136 PTGPLHIGHTRWAALGDAIARLLRASGADV 165
Cdd:cd00812 11 PSGALHVGHVRTYTIGDIIARYKRMQGYNV 40
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
362-407 |
2.86e-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: 2.86e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1072319979 362 EILI-GQLISVNGAKLSKRAGNIIELKDLVEWLGRDALRYDLARYPA 407
Cdd:cd00817 329 EVYLhGLVRDEDGRKMSKSLGNVIDPLDVIDGYGADALRFTLASAAT 375
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
363-399 |
3.11e-03 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 40.62 E-value: 3.11e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1072319979 363 ILIGQLISVNGAKLSKRAGNIIELKDLVEWLGRDALR 399
Cdd:PRK12300 565 IVVNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVR 601
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
371-404 |
4.56e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 39.78 E-value: 4.56e-03
10 20 30
....*....|....*....|....*....|....
gi 1072319979 371 VNGAKLSKRAGNIIELKDLVEWLGRDALRYDLAR 404
Cdd:PRK12267 295 MKDGKMSKSKGNVVDPEELVDRYGLDALRYYLLR 328
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
129-177 |
4.86e-03 |
|
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: 37.84 E-value: 4.86e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1072319979 129 MEFVSANPTGPLHIGHTRWAALGDAIARLLRASGADVTAEYYVNDAGNQ 177
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGL 49
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
362-405 |
5.80e-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: 39.66 E-value: 5.80e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1072319979 362 EILIGQLI-SVNGAKLSKRAGNIIELKDLVEWLGRDALRYDLARY 405
Cdd:TIGR00422 511 EVYIHGLVrDEQGRKMSKSLGNVIDPLDVIEKYGADALRFTLASL 555
|
|
| |
