|
Name |
Accession |
Description |
Interval |
E-value |
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
1-585 |
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: 638.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 1 MNLFRDFQKRINSAIEALDVVRENDaacnfdRLTVEPPRDSAHGDISTNAAMVLAKPLKSNPRALAEAIAAQFADDADVA 80
Cdd:COG0018 1 MNIKEELAEAIAAALAALGAGLEEP------DILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDADPLVE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 81 ETSVAGPGFLNFRLAPAYWQRLTAEVCRQGSDYGRSELGAGRKVNVEYVSANPTGPMHVGHCRGAVVGDALANLLAFAGY 160
Cdd:COG0018 75 KVEIAGPGFINFFLSPAALAAVLKEILADGEDYGRSDAGKGKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 161 KVDKEYYINDAGVQIDVLTRSVmLRYREalGETIGEIPSGLYPGDYLVPVGEALK--AEFGDR----LLSMDDDERDAI- 233
Cdd:COG0018 155 DVTRENYINDAGTQIGKLALSL-ERYGE--EEIEPESKPDGYLGDLYVKFHKEYEedPELEDIarelLAKLEPGDEEALe 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 234 LRDRTIAMMMAMIRSDLAALNVKHDIFFSEQLLHADGekAIRKAINELTYQGHVYkgklpppkgqlpedwEDRDQTLFRS 313
Cdd:COG0018 232 LWKKAVDWSLEEIKEDLKRLGVEFDVWFSESSLYDSG--AVEEVVEELKEKGLLY---------------ESDGALWVRL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 314 TEVGDDIDRPLIKSDGTYTYFAADVAYFYDKFAR-GYDEMIYVLGADHGGYVKRLEAVARAVSGDKV-QLTVLLCQLVKL 391
Cdd:COG0018 295 TEFGDDKDRVLVKSDGTYTYFTTDIAYHLYKFERyGFDRVIYVVGADQHGHFKRLFAALKALGYDPAkDLEHLLFGMVNL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 392 yRDGEPvrMSKRSGEFVTLREVVDE-----------------------VGSGSVRFMMLYRKSSEPLDFDFAKVTE-QSK 447
Cdd:COG0018 375 -RDGEK--MSTRAGTVVTLDDLLDEaverareiieekseeekeeiaeqVGIDAVRYFDLSRSRDKDLDFDLDLALSfEGN 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 448 DNPvfYVQYAHARCHSVFRQAKEMFPDLDlsgealaNADLTPLRDASELALIGKVAEFPRMIEAAAHGHEPHRVAFYLYE 527
Cdd:COG0018 452 TNP--YVQYAHARICSILRKAGEELDGLA-------EADLSLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYE 522
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 2073742946 528 LANALHSHWNKgrdvpeLRFVNDKNREFTIARMGLVYAVASVLKAGLQITGTDAPEEM 585
Cdd:COG0018 523 LAKAFHSFYNA------CRILKAEDEELRAARLALVAATAQVLKNGLGLLGISAPERM 574
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
3-585 |
0e+00 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 607.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 3 LFRDFQKRINSAIEALDvvrENDAACNFDRLTVEPPRDSAHGDISTNAAMVLAKPLKSNPRALAEAIAAQfaddadVAET 82
Cdd:PRK01611 1 MMMDIKELLAEALAAAL---EAGGLPELPAVLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIVEA------IEKV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 83 SVAGPGFLNFRLAPAYWQRLTAEVCRQGSDYGRSELGAGRKVNVEYVSANPTGPMHVGHCRGAVVGDALANLLAFAGYKV 162
Cdd:PRK01611 72 EIAGPGFINFFLDPAALAELVLAILEAGERYGRSDIGKGKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 163 DKEYYINDAGVQIDVLTRSVMLryrealgetigeipsglypgdylvpvgealkaefgdrllsmddderdaiLRDRTIAMM 242
Cdd:PRK01611 152 TREYYVNDAGTQIGMLIASLEL-------------------------------------------------LWRKAVDIS 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 243 MAMIRSDLAALNVKHDIFFSEQLLHADGEkaIRKAINELTYQGHVYKgklpppkgqlpedwEDRDQTLFRSTEVGDDIDR 322
Cdd:PRK01611 183 LDEIKEDLDRLGVHFDVWFSESELYYNGK--VDEVVEDLKEKGLLYV--------------ESDGALWVRLTEFGDDKDR 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 323 PLIKSDGTYTYFAADVAYFYDKFARgYDEMIYVLGADHGGYVKRLEAVARAVSGDKVQLTVLLCQLVKLYRDGEPVRMSK 402
Cdd:PRK01611 247 VLIKSDGTYTYFTRDIAYHLYKFER-FDRVIYVVGADHHGHFKRLKAALKALGYDPDALEVLLHQMVGLVRGGEGVKMST 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 403 RSGEFVTLREVVDE-----------------VGSGSVRFMMLYRKSSEPLDFDFAKVTEQSKDNPVfYVQYAHARCHSVF 465
Cdd:PRK01611 326 RAGNVVTLDDLLDEavgrarelieekeiaeaVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPP-YVQYAHARICSIL 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 466 RQAKEMFPDLDLSgealanadltPLRDASELALIGKVAEFPRMIEAAAHGHEPHRVAFYLYELANALHSHWNKgrdVPel 545
Cdd:PRK01611 405 RKAAEAGIDLLLA----------LLTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYNR---VL-- 469
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2073742946 546 rfVNDKNREFTIARMGLVYAVASVLKAGLQITGTDAPEEM 585
Cdd:PRK01611 470 --LKDEEEELRNARLALVKATAQVLKNGLDLLGISAPERM 507
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
11-585 |
2.19e-128 |
|
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed genome to date. An interesting feature of the alignment of all arginyl-tRNA synthetases is a fairly deep split between two families. One family includes archaeal, eukaryotic and organellar, spirochete, E. coli, and Synechocystis sp. The second, sharing a deletion of about 25 residues in the central region relative to the first, includes Bacillus subtilis, Aquifex aeolicus, the Mycoplasmas and Mycobacteria, and the Gram-negative bacterium Helicobacter pylori. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273085 [Multi-domain] Cd Length: 563 Bit Score: 387.85 E-value: 2.19e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 11 INSAIEALDVVRENDAACNFDRLTVEPPRDSAHGDISTNAAMVLAKPLKSNPRALAEAIAAQFaDDADVAETSVAGPGFL 90
Cdd:TIGR00456 2 KTLLKEEISQALLKAGLSKESEILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKL-KTGEIIEKVEAAGPFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 91 NFRLAPAYW-QRLTAEVCRQGSDYGRSELGaGRKVNVEYVSANPTGPMHVGHCRGAVVGDALANLLAFAGYKVDKEYYIN 169
Cdd:TIGR00456 81 NFFLSPQKLlERLIQKILTQKEKYGSKKLK-NKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 170 DAGVQIDVLTRSVMLRYREALGeTIGEIPSGLYPGDYlVPVGEALKAEFG------DRLLSMDD-DERDAILRDRTIAMM 242
Cdd:TIGR00456 160 DWGRQFGLLALGVEKFGNEALN-IAVKKPDHGLEGFY-VEINKRLEENEEleeearELFVKLESgDEETIKLWKRLVEYS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 243 MAMIRSDLAALNVKHDIFFSEQLLHADGEkaIRKAINELTYQGHVYKgklpppkgqlpedwedRDQTLFRSTEVGDDIDR 322
Cdd:TIGR00456 238 LEGIKETYDRLNIHFDSFVWEGESVKNGM--LPKVLEDLKEKGLVVE----------------DGALWLDLTLFGDKKDR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 323 PLIKSDGTYTYFAADVAYFYDKFARGYDEMIYVLGADHGGYVKRLEAVARAVSGDKVQLTVLLCQLVKLYR--------- 393
Cdd:TIGR00456 300 VLQKSDGTYLYLTTDIAYHLDKLERGFDKMIYVWGSDHHLHIAQMFAILEKLGYKKKELEHLNFGMVPLYSmktrrgnvi 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 394 --DGEPVRMSKRSGEFVTLR------EVVDEVGSGSVRFMMLYRKSSEPLDFDFAKVTeQSKDNPVFYVQYAHARCHSVF 465
Cdd:TIGR00456 380 slDNLLDEASKRAGNVITIKndleeeKVADAVGIGAVRYFDLSKNRTTDYVFDWDAML-SFEGNTAPYIQYAHARICSIL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 466 RQAkemfpdlDLSGEALANADLTpLRDASELALIGKVAEFPRMIEAAAHGHEPHRVAFYLYELANALHSHWNKGRdvpel 545
Cdd:TIGR00456 459 RKA-------EIDGEKLIADDFE-LLEEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACP----- 525
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2073742946 546 rfVNDKNREFTIARMGLVYAVASVLKAGLQITGTDAPEEM 585
Cdd:TIGR00456 526 --VLDAENELAAARLALLKATRQTLKNGLDLLGIEPPERM 563
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
123-405 |
1.19e-71 |
|
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. There are at least three subgroups of ArgRS. One type contains both characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The second subtype lacks the KMSKS motif; however, it has a lysine N-terminal to the HIGH motif, which serves as the functional counterpart to the second lysine of the KMSKS motif. A third group, which is found primarily in archaea and a few bacteria, lacks both the KMSKS motif and the HIGH loop lysine.
Pssm-ID: 185675 [Multi-domain] Cd Length: 212 Bit Score: 228.99 E-value: 1.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 123 KVNVEYVSANPTGPMHVGHCRGAVVGDALANLLAFAGYKVDKEYYINDAGVQIDVLTRSVMLryrealgetigeipsgly 202
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSLEK------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 203 pgdylvpvgealkaefgdrllsmddderdaiLRDrtiaMMMAMIRSDLAA---LNVKHDIFFSEQLLhADGEKAIRKAIN 279
Cdd:cd00671 63 -------------------------------WRK----LVEESIKADLETygrLDVRFDVWFGESSY-LGLMGKVVELLE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 280 ELtyqghvykgklpppkgqlPEDWEDRDQTLFRSTEVGDDIDRPLIKSDGTYTYFAADVAYFYDKFARGYDEMIYVLGAD 359
Cdd:cd00671 107 EL------------------GLLYEEDGALWLDLTEFGDDKDRVLVRSDGTYTYFTRDIAYHLDKFERGADKIIYVVGAD 168
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2073742946 360 HGGYVKRLEAVARAVSGD-KVQLTVLLCQLVKLYRdgePVRMSKRSG 405
Cdd:cd00671 169 HHGHFKRLFAALELLGYDeAKKLEHLLYGMVNLPK---EGKMSTRAG 212
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
454-585 |
1.19e-40 |
|
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: 143.49 E-value: 1.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 454 VQYAHARCHSVFRQAKEMFPDLDlsgeALANADLTPLRDASELALIGKVAEFPRMIEAAAHGHEPHRVAFYLYELANALH 533
Cdd:smart00836 1 VQYAHARICSILRKAGEAGETLP----DIADADLSLLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFH 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2073742946 534 SHWNKgrdvpeLRFVNDKNREFTIARMGLVYAVASVLKAGLQITGTDAPEEM 585
Cdd:smart00836 77 SFYNR------VRVLGEENPELRKARLALLKAVRQVLANGLRLLGISAPERM 122
|
|
| DALR_1 |
pfam05746 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
454-585 |
1.39e-34 |
|
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain in Arginyl and glycyl tRNA synthetase. This domain is known as the DALR domain after characteriztic conserved amino acids.
Pssm-ID: 399042 [Multi-domain] Cd Length: 117 Bit Score: 126.61 E-value: 1.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 454 VQYAHARCHSVFRQAKEMFPDLDlsgealanADLTPLRDASELALIGKVAEFPRMIEAAAHGHEPHRVAFYLYELANALH 533
Cdd:pfam05746 1 LQYAHARICSILRKAGELGINLD--------IDADLLTEEEEKELLKALLQFPEVLEEAAEELEPHRLANYLYELASAFH 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2073742946 534 SHWNKGRdvpelrfVNDKNREFTIARMGLVYAVASVLKAGLQITGTDAPEEM 585
Cdd:pfam05746 73 SFYNNCR-------VLDEDNEERNARLALLKAVRQVLKNGLDLLGIEAPEKM 117
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
1-585 |
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: 638.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 1 MNLFRDFQKRINSAIEALDVVRENDaacnfdRLTVEPPRDSAHGDISTNAAMVLAKPLKSNPRALAEAIAAQFADDADVA 80
Cdd:COG0018 1 MNIKEELAEAIAAALAALGAGLEEP------DILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDADPLVE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 81 ETSVAGPGFLNFRLAPAYWQRLTAEVCRQGSDYGRSELGAGRKVNVEYVSANPTGPMHVGHCRGAVVGDALANLLAFAGY 160
Cdd:COG0018 75 KVEIAGPGFINFFLSPAALAAVLKEILADGEDYGRSDAGKGKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 161 KVDKEYYINDAGVQIDVLTRSVmLRYREalGETIGEIPSGLYPGDYLVPVGEALK--AEFGDR----LLSMDDDERDAI- 233
Cdd:COG0018 155 DVTRENYINDAGTQIGKLALSL-ERYGE--EEIEPESKPDGYLGDLYVKFHKEYEedPELEDIarelLAKLEPGDEEALe 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 234 LRDRTIAMMMAMIRSDLAALNVKHDIFFSEQLLHADGekAIRKAINELTYQGHVYkgklpppkgqlpedwEDRDQTLFRS 313
Cdd:COG0018 232 LWKKAVDWSLEEIKEDLKRLGVEFDVWFSESSLYDSG--AVEEVVEELKEKGLLY---------------ESDGALWVRL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 314 TEVGDDIDRPLIKSDGTYTYFAADVAYFYDKFAR-GYDEMIYVLGADHGGYVKRLEAVARAVSGDKV-QLTVLLCQLVKL 391
Cdd:COG0018 295 TEFGDDKDRVLVKSDGTYTYFTTDIAYHLYKFERyGFDRVIYVVGADQHGHFKRLFAALKALGYDPAkDLEHLLFGMVNL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 392 yRDGEPvrMSKRSGEFVTLREVVDE-----------------------VGSGSVRFMMLYRKSSEPLDFDFAKVTE-QSK 447
Cdd:COG0018 375 -RDGEK--MSTRAGTVVTLDDLLDEaverareiieekseeekeeiaeqVGIDAVRYFDLSRSRDKDLDFDLDLALSfEGN 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 448 DNPvfYVQYAHARCHSVFRQAKEMFPDLDlsgealaNADLTPLRDASELALIGKVAEFPRMIEAAAHGHEPHRVAFYLYE 527
Cdd:COG0018 452 TNP--YVQYAHARICSILRKAGEELDGLA-------EADLSLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYE 522
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 2073742946 528 LANALHSHWNKgrdvpeLRFVNDKNREFTIARMGLVYAVASVLKAGLQITGTDAPEEM 585
Cdd:COG0018 523 LAKAFHSFYNA------CRILKAEDEELRAARLALVAATAQVLKNGLGLLGISAPERM 574
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
3-585 |
0e+00 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 607.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 3 LFRDFQKRINSAIEALDvvrENDAACNFDRLTVEPPRDSAHGDISTNAAMVLAKPLKSNPRALAEAIAAQfaddadVAET 82
Cdd:PRK01611 1 MMMDIKELLAEALAAAL---EAGGLPELPAVLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIVEA------IEKV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 83 SVAGPGFLNFRLAPAYWQRLTAEVCRQGSDYGRSELGAGRKVNVEYVSANPTGPMHVGHCRGAVVGDALANLLAFAGYKV 162
Cdd:PRK01611 72 EIAGPGFINFFLDPAALAELVLAILEAGERYGRSDIGKGKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 163 DKEYYINDAGVQIDVLTRSVMLryrealgetigeipsglypgdylvpvgealkaefgdrllsmddderdaiLRDRTIAMM 242
Cdd:PRK01611 152 TREYYVNDAGTQIGMLIASLEL-------------------------------------------------LWRKAVDIS 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 243 MAMIRSDLAALNVKHDIFFSEQLLHADGEkaIRKAINELTYQGHVYKgklpppkgqlpedwEDRDQTLFRSTEVGDDIDR 322
Cdd:PRK01611 183 LDEIKEDLDRLGVHFDVWFSESELYYNGK--VDEVVEDLKEKGLLYV--------------ESDGALWVRLTEFGDDKDR 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 323 PLIKSDGTYTYFAADVAYFYDKFARgYDEMIYVLGADHGGYVKRLEAVARAVSGDKVQLTVLLCQLVKLYRDGEPVRMSK 402
Cdd:PRK01611 247 VLIKSDGTYTYFTRDIAYHLYKFER-FDRVIYVVGADHHGHFKRLKAALKALGYDPDALEVLLHQMVGLVRGGEGVKMST 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 403 RSGEFVTLREVVDE-----------------VGSGSVRFMMLYRKSSEPLDFDFAKVTEQSKDNPVfYVQYAHARCHSVF 465
Cdd:PRK01611 326 RAGNVVTLDDLLDEavgrarelieekeiaeaVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPP-YVQYAHARICSIL 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 466 RQAKEMFPDLDLSgealanadltPLRDASELALIGKVAEFPRMIEAAAHGHEPHRVAFYLYELANALHSHWNKgrdVPel 545
Cdd:PRK01611 405 RKAAEAGIDLLLA----------LLTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYNR---VL-- 469
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2073742946 546 rfVNDKNREFTIARMGLVYAVASVLKAGLQITGTDAPEEM 585
Cdd:PRK01611 470 --LKDEEEELRNARLALVKATAQVLKNGLDLLGISAPERM 507
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
11-585 |
2.19e-128 |
|
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed genome to date. An interesting feature of the alignment of all arginyl-tRNA synthetases is a fairly deep split between two families. One family includes archaeal, eukaryotic and organellar, spirochete, E. coli, and Synechocystis sp. The second, sharing a deletion of about 25 residues in the central region relative to the first, includes Bacillus subtilis, Aquifex aeolicus, the Mycoplasmas and Mycobacteria, and the Gram-negative bacterium Helicobacter pylori. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273085 [Multi-domain] Cd Length: 563 Bit Score: 387.85 E-value: 2.19e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 11 INSAIEALDVVRENDAACNFDRLTVEPPRDSAHGDISTNAAMVLAKPLKSNPRALAEAIAAQFaDDADVAETSVAGPGFL 90
Cdd:TIGR00456 2 KTLLKEEISQALLKAGLSKESEILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKL-KTGEIIEKVEAAGPFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 91 NFRLAPAYW-QRLTAEVCRQGSDYGRSELGaGRKVNVEYVSANPTGPMHVGHCRGAVVGDALANLLAFAGYKVDKEYYIN 169
Cdd:TIGR00456 81 NFFLSPQKLlERLIQKILTQKEKYGSKKLK-NKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 170 DAGVQIDVLTRSVMLRYREALGeTIGEIPSGLYPGDYlVPVGEALKAEFG------DRLLSMDD-DERDAILRDRTIAMM 242
Cdd:TIGR00456 160 DWGRQFGLLALGVEKFGNEALN-IAVKKPDHGLEGFY-VEINKRLEENEEleeearELFVKLESgDEETIKLWKRLVEYS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 243 MAMIRSDLAALNVKHDIFFSEQLLHADGEkaIRKAINELTYQGHVYKgklpppkgqlpedwedRDQTLFRSTEVGDDIDR 322
Cdd:TIGR00456 238 LEGIKETYDRLNIHFDSFVWEGESVKNGM--LPKVLEDLKEKGLVVE----------------DGALWLDLTLFGDKKDR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 323 PLIKSDGTYTYFAADVAYFYDKFARGYDEMIYVLGADHGGYVKRLEAVARAVSGDKVQLTVLLCQLVKLYR--------- 393
Cdd:TIGR00456 300 VLQKSDGTYLYLTTDIAYHLDKLERGFDKMIYVWGSDHHLHIAQMFAILEKLGYKKKELEHLNFGMVPLYSmktrrgnvi 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 394 --DGEPVRMSKRSGEFVTLR------EVVDEVGSGSVRFMMLYRKSSEPLDFDFAKVTeQSKDNPVFYVQYAHARCHSVF 465
Cdd:TIGR00456 380 slDNLLDEASKRAGNVITIKndleeeKVADAVGIGAVRYFDLSKNRTTDYVFDWDAML-SFEGNTAPYIQYAHARICSIL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 466 RQAkemfpdlDLSGEALANADLTpLRDASELALIGKVAEFPRMIEAAAHGHEPHRVAFYLYELANALHSHWNKGRdvpel 545
Cdd:TIGR00456 459 RKA-------EIDGEKLIADDFE-LLEEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACP----- 525
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2073742946 546 rfVNDKNREFTIARMGLVYAVASVLKAGLQITGTDAPEEM 585
Cdd:TIGR00456 526 --VLDAENELAAARLALLKATRQTLKNGLDLLGIEPPERM 563
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
123-405 |
1.19e-71 |
|
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. There are at least three subgroups of ArgRS. One type contains both characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The second subtype lacks the KMSKS motif; however, it has a lysine N-terminal to the HIGH motif, which serves as the functional counterpart to the second lysine of the KMSKS motif. A third group, which is found primarily in archaea and a few bacteria, lacks both the KMSKS motif and the HIGH loop lysine.
Pssm-ID: 185675 [Multi-domain] Cd Length: 212 Bit Score: 228.99 E-value: 1.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 123 KVNVEYVSANPTGPMHVGHCRGAVVGDALANLLAFAGYKVDKEYYINDAGVQIDVLTRSVMLryrealgetigeipsgly 202
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSLEK------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 203 pgdylvpvgealkaefgdrllsmddderdaiLRDrtiaMMMAMIRSDLAA---LNVKHDIFFSEQLLhADGEKAIRKAIN 279
Cdd:cd00671 63 -------------------------------WRK----LVEESIKADLETygrLDVRFDVWFGESSY-LGLMGKVVELLE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 280 ELtyqghvykgklpppkgqlPEDWEDRDQTLFRSTEVGDDIDRPLIKSDGTYTYFAADVAYFYDKFARGYDEMIYVLGAD 359
Cdd:cd00671 107 EL------------------GLLYEEDGALWLDLTEFGDDKDRVLVRSDGTYTYFTRDIAYHLDKFERGADKIIYVVGAD 168
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2073742946 360 HGGYVKRLEAVARAVSGD-KVQLTVLLCQLVKLYRdgePVRMSKRSG 405
Cdd:cd00671 169 HHGHFKRLFAALELLGYDeAKKLEHLLYGMVNLPK---EGKMSTRAG 212
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
454-585 |
1.19e-40 |
|
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: 143.49 E-value: 1.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 454 VQYAHARCHSVFRQAKEMFPDLDlsgeALANADLTPLRDASELALIGKVAEFPRMIEAAAHGHEPHRVAFYLYELANALH 533
Cdd:smart00836 1 VQYAHARICSILRKAGEAGETLP----DIADADLSLLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFH 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2073742946 534 SHWNKgrdvpeLRFVNDKNREFTIARMGLVYAVASVLKAGLQITGTDAPEEM 585
Cdd:smart00836 77 SFYNR------VRVLGEENPELRKARLALLKAVRQVLANGLRLLGISAPERM 122
|
|
| Anticodon_Ia_Arg |
cd07956 |
Anticodon-binding domain of arginyl tRNA synthetases; This domain is found in arginyl tRNA ... |
415-585 |
8.36e-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: 8.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 415 DEVGSGSVRFMMLYRKSSEPLDFDFAKVTEQSKDnPVFYVQYAHARCHSVFRQAKEMFpdldlsgEALANADLTPLRDAS 494
Cdd:cd07956 1 EEVGVGAVKYQDLSNKRIKDYTFDWERMLSFEGD-TGPYLQYAHARLCSILRKAGETI-------EAEADADLSLLPEPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 495 ELALIGKVAEFPRMIEAAAHGHEPHRVAFYLYELANALHSHWNKGRdvpelrfVNDKNREFTIARMGLVYAVASVLKAGL 574
Cdd:cd07956 73 ERDLILLLAKFPEVVKNAAETLEPHTIATYLFDLAHAFSKFYNACP-------VLGAEEELRNARLALVAAARQVLANGL 145
|
170
....*....|.
gi 2073742946 575 QITGTDAPEEM 585
Cdd:cd07956 146 DLLGIEAPERM 156
|
|
| DALR_1 |
pfam05746 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
454-585 |
1.39e-34 |
|
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain in Arginyl and glycyl tRNA synthetase. This domain is known as the DALR domain after characteriztic conserved amino acids.
Pssm-ID: 399042 [Multi-domain] Cd Length: 117 Bit Score: 126.61 E-value: 1.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 454 VQYAHARCHSVFRQAKEMFPDLDlsgealanADLTPLRDASELALIGKVAEFPRMIEAAAHGHEPHRVAFYLYELANALH 533
Cdd:pfam05746 1 LQYAHARICSILRKAGELGINLD--------IDADLLTEEEEKELLKALLQFPEVLEEAAEELEPHRLANYLYELASAFH 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2073742946 534 SHWNKGRdvpelrfVNDKNREFTIARMGLVYAVASVLKAGLQITGTDAPEEM 585
Cdd:pfam05746 73 SFYNNCR-------VLDEDNEERNARLALLKAVRQVLKNGLDLLGIEAPEKM 117
|
|
| PLN02286 |
PLN02286 |
arginine-tRNA ligase |
35-529 |
1.59e-29 |
|
arginine-tRNA ligase
Pssm-ID: 215160 [Multi-domain] Cd Length: 576 Bit Score: 123.21 E-value: 1.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 35 VEPPRDSAHGDISTNAAMVLAKPLK------SNPRALAEAIAAQFADDADVAETSVAGPGFLNFRLAPAYWQRLTAEVCR 108
Cdd:PLN02286 25 VAACTNPKFGDYQCNNAMGLWSKLKgkgtsfKNPRAVAQAIVKNLPASEMIESTSVAGPGFVNVRLSASWLAKRIERMLV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 109 QGSDYGRSELGAGRKVnVEYVSANPTGPMHVGHCRGAVVGDALANLLAFAGYKVDKEYYINDAGVQIDVLTRSV--MLRY 186
Cdd:PLN02286 105 DGIDTWAPTLPVKRAV-VDFSSPNIAKEMHVGHLRSTIIGDTLARMLEFSGVEVLRRNHVGDWGTQFGMLIEHLfeKFPN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 187 REALGET-IGEIPSgLYpgdylvpvgEALKAEFgdrllsmDDDE------RDAILR----DRTIAMMMAMI----RSDLA 251
Cdd:PLN02286 184 WESVSDQaIGDLQE-FY---------KAAKKRF-------DEDEefkaraQQAVVRlqggDPEYRAAWAKIceisRREFE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 252 A----LNVKhdiffseqlLHADGEKA----IRKAINELTYQGHVykgklpppkgqlpedwEDRDQTLFRSTEvGDDIdrP 323
Cdd:PLN02286 247 KvyqrLRVE---------LEEKGESFynpyIPGVIEELESKGLV----------------VESDGARVIFVE-GFDI--P 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 324 LI--KSDGTYTYFAADVAyfydkfARGY-------DEMIYVLGADHGGYVKRLEAVARAV----SGDKVQLTVLLCQLVk 390
Cdd:PLN02286 299 LIvvKSDGGFNYASTDLA------ALWYrlneekaEWIIYVTDVGQQQHFDMVFKAAKRAgwlpEDTYPRLEHVGFGLV- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 391 LYRDGEpvRMSKRSGEFVTLREVVDE-----------------------------VGSGSVRFMMLYRKSSEPLDFDFAK 441
Cdd:PLN02286 372 LGEDGK--RFRTRSGEVVRLVDLLDEaksrskaaliergkdsewtpeeleqaaeaVGYGAVKYADLKNNRLTNYTFSFDQ 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 442 VTEqSKDNPVFYVQYAHARCHSVFRQAKemfPDLDlsgeALANADLTPLRDASELALIGKVAEFPRMIEAAAHGHEPHRV 521
Cdd:PLN02286 450 MLD-LKGNTAVYLLYAHARICSIIRKSG---KDID----ELKKTGKIVLDHPDERALGLHLLQFPEVVEEACTDLLPNRL 521
|
....*...
gi 2073742946 522 AFYLYELA 529
Cdd:PLN02286 522 CEYLYNLS 529
|
|
| Arg_tRNA_synt_N |
smart01016 |
Arginyl tRNA synthetase N terminal dom; This domain is found at the amino terminus of Arginyl ... |
5-94 |
1.04e-24 |
|
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: 98.04 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 5 RDFQKRINSAIEALdvvreNDAACNFDRLTVEPPRDSAHGDISTNAAMVLAKPLKSNPRALAEAIAAQFADDADVAETSV 84
Cdd:smart01016 1 DLLKEAIAEALKKA-----LGVEGEPIDIALERPKDPDHGDYATNVAFRLAKKLKKNPRELAEEIAEKLPKSDLVEKVEI 75
|
90
....*....|
gi 2073742946 85 AGPGFLNFRL 94
Cdd:smart01016 76 AGPGFINFFL 85
|
|
| Arg_tRNA_synt_N |
pfam03485 |
Arginyl tRNA synthetase N terminal domain; This domain is found at the amino terminus of ... |
7-94 |
1.70e-22 |
|
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: 91.52 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 7 FQKRINSAIEALDVVRENDAAcnfdrLTVEPPRDSAHGDISTNAAMVLAKPLKSNPRALAEAIAAQFADDADVAETSVAG 86
Cdd:pfam03485 1 LKKAIAKALSKLGGPDLELID-----IVIETPKNPKFGDYATNVAMQLAKKLKKNPREIAEEIAEKLEKSDIIEKVEVAG 75
|
....*...
gi 2073742946 87 PGFLNFRL 94
Cdd:pfam03485 76 PGFINFFL 83
|
|
| tRNA-synt_1d |
pfam00750 |
tRNA synthetases class I (R); Other tRNA synthetase sub-families are too dissimilar to be ... |
118-426 |
5.29e-16 |
|
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: 79.53 E-value: 5.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 118 LGAGRKVNVEYVSANPTGPMHVGHCRGAVVGDALANLLAFAGYKVDKEYYINDAGVQIDVLTRSVMLRYREalgETIGEI 197
Cdd:pfam00750 15 SREKKKVVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQFGMLIAGLEKYQDE---KTLQEM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 198 PSGLYPGDYLvpvgEALK-----AEFGDR-------LLSMDDDERdailrdRTIAMMMAMIRSDLAALNVKHDIFFSEQl 265
Cdd:pfam00750 92 PIQDLEDFYR----EAKKhydeeEEFAERarnyvvkLQSGDEYWR------RMWKLIVDITMTQNQRLYDRLDVTLTEM- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 266 lhadGEK----AIRKAINELTYQGHVYkgklpppkgqlpedwEDRDQTLFRSTEVGDDIDRPLIKSDGTYTYFAADV-AY 340
Cdd:pfam00750 161 ----GESlynpMMNEIVKDFKKNGLVV---------------EIDGALVVFLDEFGKPMGVIVQKSDGGYLYTTTDIaAA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073742946 341 FYDKFARGYDEMIYVLGADHGGYVKRLEAVARAVSGDKVQLTVLLCQL-VKLYRDGEPvrMSKRSGEFVTLREVVDEVGS 419
Cdd:pfam00750 222 KYRYETLHADRMLYVIDSRQSQHMQQAFAILRKAGYVPESKDLEHINFgMVLGKDGKP--FKTRKGGTVKLADLLDEALE 299
|
....*..
gi 2073742946 420 GSVRFMM 426
Cdd:pfam00750 300 RALQLIM 306
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
126-197 |
2.74e-05 |
|
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: 44.39 E-value: 2.74e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2073742946 126 VEYVSANPTGPMHVGHCRGAVVGDALANLLAFAGYKVDKEYYINDAGVQIDVLTRSVMLRYREALGETIGEI 197
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERI 72
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
394-444 |
4.82e-05 |
|
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439985 [Multi-domain] Cd Length: 465 Bit Score: 46.25 E-value: 4.82e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2073742946 394 DGEpvRMSKRSGEFVTLREVVDEVGSGSVRFMML---YRKssePLDFDFAKVTE 444
Cdd:COG0215 262 NGE--KMSKSLGNFFTVRDLLKKYDPEVLRFFLLsahYRS---PLDFSEEALEE 310
|
|
| |
