|
Name |
Accession |
Description |
Interval |
E-value |
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
1-584 |
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: 644.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 1 MNLFTDFEARIKTALEQIDLvrekrsELDFGRITVEPPRDASHGDVATNAAMVLAKVLGTNPRALADVIIAKLKEDADVA 80
Cdd:COG0018 1 MNIKEELAEAIAAALAALGA------GLEEPDILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDADPLVE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 81 DVSVAGPGFINIRLAVGYWQRLLASMIGAGTDYGRSSLGKGKKVNVEYVSANPTGPMHVGHCRGAVVGDALANLLAFAGY 160
Cdd:COG0018 75 KVEIAGPGFINFFLSPAALAAVLKEILADGEDYGRSDAGKGKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 161 GVEKEYYINDAGSQIDVLARSVFlRYREalGEKIGEIPSGLYPGDY---------LVPVGQSLAADYGVRLHNMPEDqWM 231
Cdd:COG0018 155 DVTRENYINDAGTQIGKLALSLE-RYGE--EEIEPESKPDGYLGDLyvkfhkeyeEDPELEDIARELLAKLEPGDEE-AL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 232 PIVKdRTIDAMMVMIRDDLAALNVHHDVFFSERTLHANGaaAIRTAINDLTFKGYVYkgtlpppkgqlpedwEDREQTLF 311
Cdd:COG0018 231 ELWK-KAVDWSLEEIKEDLKRLGVEFDVWFSESSLYDSG--AVEEVVEELKEKGLLY---------------ESDGALWV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 312 RSTEVGDDIDRPLIKSDGSYTYFAADVAYFKNKFDR-GFDEMIYVLGADHGGYVKRLEAVARGVSDGKAK-LTVLLCQLV 389
Cdd:COG0018 293 RLTEFGDDKDRVLVKSDGTYTYFTTDIAYHLYKFERyGFDRVIYVVGADQHGHFKRLFAALKALGYDPAKdLEHLLFGMV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 390 KLyRNGEpvKMSKRSGDFVTLRDVVEE-----------------------VGRDSVRFMMLYRKNSEPLDFDFAKVTE-Q 445
Cdd:COG0018 373 NL-RDGE--KMSTRAGTVVTLDDLLDEaverareiieekseeekeeiaeqVGIDAVRYFDLSRSRDKDLDFDLDLALSfE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 446 SKDNPvfYVQYAHARCMSVFRQAREAFADLD-VSPENLAktvagigDPAELQLVAKLAEFPRIVEAAAQSQEPHRVAFYL 524
Cdd:COG0018 450 GNTNP--YVQYAHARICSILRKAGEELDGLAeADLSLLT-------EEEELALIKKLAQFPEVVEEAAEDLEPHRIANYL 520
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 525 YDVASSFHAHWNKgkdqpeLRFVNDKNRESSIARLGLVYAVASVLKSGLAITGTAAPDEM 584
Cdd:COG0018 521 YELAKAFHSFYNA------CRILKAEDEELRAARLALVAATAQVLKNGLGLLGISAPERM 574
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
3-584 |
0e+00 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 620.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 3 LFTDFEARIKTALEQIDlvrEKRSELDFGRITVEPPRDASHGDVATNAAMVLAKVLGTNPRALADVIIAKlkedadVADV 82
Cdd:PRK01611 1 MMMDIKELLAEALAAAL---EAGGLPELPAVLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIVEA------IEKV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 83 SVAGPGFINIRLAVGYWQRLLASMIGAGTDYGRSSLGKGKKVNVEYVSANPTGPMHVGHCRGAVVGDALANLLAFAGYGV 162
Cdd:PRK01611 72 EIAGPGFINFFLDPAALAELVLAILEAGERYGRSDIGKGKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 163 EKEYYINDAGSQIDVLARSVFLRYREAlgekigeipsglypgdylvpvgqslaadygvrlhnmpedqwmpivkdrtIDAM 242
Cdd:PRK01611 152 TREYYVNDAGTQIGMLIASLELLWRKA-------------------------------------------------VDIS 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 243 MVMIRDDLAALNVHHDVFFSERTLHANGAaaIRTAINDLTFKGYVYKgtlpppkgqlpedwEDREQTLFRSTEVGDDIDR 322
Cdd:PRK01611 183 LDEIKEDLDRLGVHFDVWFSESELYYNGK--VDEVVEDLKEKGLLYV--------------ESDGALWVRLTEFGDDKDR 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 323 PLIKSDGSYTYFAADVAYFKNKFDRgFDEMIYVLGADHGGYVKRLEAVARGVSDGKAKLTVLLCQLVKLYRNGEPVKMSK 402
Cdd:PRK01611 247 VLIKSDGTYTYFTRDIAYHLYKFER-FDRVIYVVGADHHGHFKRLKAALKALGYDPDALEVLLHQMVGLVRGGEGVKMST 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 403 RSGDFVTLRDVVEE-----------------VGRDSVRFMMLYRKNSEPLDFDFAKVTEQSKDNPVfYVQYAHARCMSVF 465
Cdd:PRK01611 326 RAGNVVTLDDLLDEavgrarelieekeiaeaVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPP-YVQYAHARICSIL 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 466 RQAREAFADLDVSPenlaktvagIGDPAELQLVAKLAEFPRIVEAAAQSQEPHRVAFYLYDVASSFHAHWNkgkdqpelR 545
Cdd:PRK01611 405 RKAAEAGIDLLLAL---------LTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYN--------R 467
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1581859887 546 FVNDKNRES-SIARLGLVYAVASVLKSGLAITGTAAPDEM 584
Cdd:PRK01611 468 VLLKDEEEElRNARLALVKATAQVLKNGLDLLGISAPERM 507
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
11-584 |
8.20e-125 |
|
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: 378.61 E-value: 8.20e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 11 IKTAL-EQIDLVREKRSELDFGRITVEPPRDASHGDVATNAAMVLAKVLGTNPRALADVIIAKLKEDADVADVSVAGPgF 89
Cdd:TIGR00456 1 IKTLLkEEISQALLKAGLSKESEILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKLKTGEIIEKVEAAGP-F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 90 INIRLAVGYW-QRLLASMIGAGTDYGRSSLgKGKKVNVEYVSANPTGPMHVGHCRGAVVGDALANLLAFAGYGVEKEYYI 168
Cdd:TIGR00456 80 INFFLSPQKLlERLIQKILTQKEKYGSKKL-KNKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 169 NDAGSQIDVLARSVFLRYREALGEKiGEIPSGLYPGDYlVPVGQSLAADYGVR------LHNMPE-DQWMPIVKDRTIDA 241
Cdd:TIGR00456 159 NDWGRQFGLLALGVEKFGNEALNIA-VKKPDHGLEGFY-VEINKRLEENEELEeearelFVKLESgDEETIKLWKRLVEY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 242 MMVMIRDDLAALNVHHDVFFSERTLHANGaaAIRTAINDLTFKGYVYKgtlpppkgqlpedwedREQTLFRSTEVGDDID 321
Cdd:TIGR00456 237 SLEGIKETYDRLNIHFDSFVWEGESVKNG--MLPKVLEDLKEKGLVVE----------------DGALWLDLTLFGDKKD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 322 RPLIKSDGSYTYFAADVAYFKNKFDRGFDEMIYVLGADHGGYVKRLEAVARGVSDGKAKLTVLLCQLVKLYR-------- 393
Cdd:TIGR00456 299 RVLQKSDGTYLYLTTDIAYHLDKLERGFDKMIYVWGSDHHLHIAQMFAILEKLGYKKKELEHLNFGMVPLYSmktrrgnv 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 394 ---NGEPVKMSKRSGDFVTLR------DVVEEVGRDSVRFMMLYRKNSEPLDFDFAKVTeQSKDNPVFYVQYAHARCMSV 464
Cdd:TIGR00456 379 islDNLLDEASKRAGNVITIKndleeeKVADAVGIGAVRYFDLSKNRTTDYVFDWDAML-SFEGNTAPYIQYAHARICSI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 465 FRQAREAFADLDVSP-ENLaktvagigDPAELQLVAKLAEFPRIVEAAAQSQEPHRVAFYLYDVASSFHAHWNKGKdqpe 543
Cdd:TIGR00456 458 LRKAEIDGEKLIADDfELL--------EEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACP---- 525
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1581859887 544 lrfVNDKNRESSIARLGLVYAVASVLKSGLAITGTAAPDEM 584
Cdd:TIGR00456 526 ---VLDAENELAAARLALLKATRQTLKNGLDLLGIEPPERM 563
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
123-405 |
5.65e-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: 229.76 E-value: 5.65e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 123 KVNVEYVSANPTGPMHVGHCRGAVVGDALANLLAFAGYGVEKEYYINDAGSQIDVLARSVFLryrealgekigeipsgly 202
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSLEK------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 203 pgdylvpvgqslaadygvrlhnmpedqWmpivkdrtIDAMMVMIRDDLAA---LNVHHDVFFSERTLhangAAAIRTAIN 279
Cdd:cd00671 63 ---------------------------W--------RKLVEESIKADLETygrLDVRFDVWFGESSY----LGLMGKVVE 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 280 DLTFKGYVYkgtlpppkgqlpedwEDREQTLFRSTEVGDDIDRPLIKSDGSYTYFAADVAYFKNKFDRGFDEMIYVLGAD 359
Cdd:cd00671 104 LLEELGLLY---------------EEDGALWLDLTEFGDDKDRVLVRSDGTYTYFTRDIAYHLDKFERGADKIIYVVGAD 168
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1581859887 360 HGGYVKRLEAVARGVS-DGKAKLTVLLCQLVKLYRngePVKMSKRSG 405
Cdd:cd00671 169 HHGHFKRLFAALELLGyDEAKKLEHLLYGMVNLPK---EGKMSTRAG 212
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
454-584 |
2.58e-41 |
|
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: 145.41 E-value: 2.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 454 VQYAHARCMSVFRQAREAFADLdvsPENLAKTVAGIGDPAELQLVAKLAEFPRIVEAAAQSQEPHRVAFYLYDVASSFHA 533
Cdd:smart00836 1 VQYAHARICSILRKAGEAGETL---PDIADADLSLLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHS 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1581859887 534 HWNKgkdqpeLRFVNDKNRESSIARLGLVYAVASVLKSGLAITGTAAPDEM 584
Cdd:smart00836 78 FYNR------VRVLGEENPELRKARLALLKAVRQVLANGLRLLGISAPERM 122
|
|
| DALR_1 |
pfam05746 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
454-584 |
1.62e-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: 1.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 454 VQYAHARCMSVFRQAREAFADLDVSPENLAktvagigDPAELQLVAKLAEFPRIVEAAAQSQEPHRVAFYLYDVASSFHA 533
Cdd:pfam05746 1 LQYAHARICSILRKAGELGINLDIDADLLT-------EEEEKELLKALLQFPEVLEEAAEELEPHRLANYLYELASAFHS 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1581859887 534 HWNKGKdqpelrfVNDKNRESSIARLGLVYAVASVLKSGLAITGTAAPDEM 584
Cdd:pfam05746 74 FYNNCR-------VLDEDNEERNARLALLKAVRQVLKNGLDLLGIEAPEKM 117
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
1-584 |
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: 644.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 1 MNLFTDFEARIKTALEQIDLvrekrsELDFGRITVEPPRDASHGDVATNAAMVLAKVLGTNPRALADVIIAKLKEDADVA 80
Cdd:COG0018 1 MNIKEELAEAIAAALAALGA------GLEEPDILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDADPLVE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 81 DVSVAGPGFINIRLAVGYWQRLLASMIGAGTDYGRSSLGKGKKVNVEYVSANPTGPMHVGHCRGAVVGDALANLLAFAGY 160
Cdd:COG0018 75 KVEIAGPGFINFFLSPAALAAVLKEILADGEDYGRSDAGKGKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 161 GVEKEYYINDAGSQIDVLARSVFlRYREalGEKIGEIPSGLYPGDY---------LVPVGQSLAADYGVRLHNMPEDqWM 231
Cdd:COG0018 155 DVTRENYINDAGTQIGKLALSLE-RYGE--EEIEPESKPDGYLGDLyvkfhkeyeEDPELEDIARELLAKLEPGDEE-AL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 232 PIVKdRTIDAMMVMIRDDLAALNVHHDVFFSERTLHANGaaAIRTAINDLTFKGYVYkgtlpppkgqlpedwEDREQTLF 311
Cdd:COG0018 231 ELWK-KAVDWSLEEIKEDLKRLGVEFDVWFSESSLYDSG--AVEEVVEELKEKGLLY---------------ESDGALWV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 312 RSTEVGDDIDRPLIKSDGSYTYFAADVAYFKNKFDR-GFDEMIYVLGADHGGYVKRLEAVARGVSDGKAK-LTVLLCQLV 389
Cdd:COG0018 293 RLTEFGDDKDRVLVKSDGTYTYFTTDIAYHLYKFERyGFDRVIYVVGADQHGHFKRLFAALKALGYDPAKdLEHLLFGMV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 390 KLyRNGEpvKMSKRSGDFVTLRDVVEE-----------------------VGRDSVRFMMLYRKNSEPLDFDFAKVTE-Q 445
Cdd:COG0018 373 NL-RDGE--KMSTRAGTVVTLDDLLDEaverareiieekseeekeeiaeqVGIDAVRYFDLSRSRDKDLDFDLDLALSfE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 446 SKDNPvfYVQYAHARCMSVFRQAREAFADLD-VSPENLAktvagigDPAELQLVAKLAEFPRIVEAAAQSQEPHRVAFYL 524
Cdd:COG0018 450 GNTNP--YVQYAHARICSILRKAGEELDGLAeADLSLLT-------EEEELALIKKLAQFPEVVEEAAEDLEPHRIANYL 520
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 525 YDVASSFHAHWNKgkdqpeLRFVNDKNRESSIARLGLVYAVASVLKSGLAITGTAAPDEM 584
Cdd:COG0018 521 YELAKAFHSFYNA------CRILKAEDEELRAARLALVAATAQVLKNGLGLLGISAPERM 574
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
3-584 |
0e+00 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 620.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 3 LFTDFEARIKTALEQIDlvrEKRSELDFGRITVEPPRDASHGDVATNAAMVLAKVLGTNPRALADVIIAKlkedadVADV 82
Cdd:PRK01611 1 MMMDIKELLAEALAAAL---EAGGLPELPAVLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIVEA------IEKV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 83 SVAGPGFINIRLAVGYWQRLLASMIGAGTDYGRSSLGKGKKVNVEYVSANPTGPMHVGHCRGAVVGDALANLLAFAGYGV 162
Cdd:PRK01611 72 EIAGPGFINFFLDPAALAELVLAILEAGERYGRSDIGKGKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 163 EKEYYINDAGSQIDVLARSVFLRYREAlgekigeipsglypgdylvpvgqslaadygvrlhnmpedqwmpivkdrtIDAM 242
Cdd:PRK01611 152 TREYYVNDAGTQIGMLIASLELLWRKA-------------------------------------------------VDIS 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 243 MVMIRDDLAALNVHHDVFFSERTLHANGAaaIRTAINDLTFKGYVYKgtlpppkgqlpedwEDREQTLFRSTEVGDDIDR 322
Cdd:PRK01611 183 LDEIKEDLDRLGVHFDVWFSESELYYNGK--VDEVVEDLKEKGLLYV--------------ESDGALWVRLTEFGDDKDR 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 323 PLIKSDGSYTYFAADVAYFKNKFDRgFDEMIYVLGADHGGYVKRLEAVARGVSDGKAKLTVLLCQLVKLYRNGEPVKMSK 402
Cdd:PRK01611 247 VLIKSDGTYTYFTRDIAYHLYKFER-FDRVIYVVGADHHGHFKRLKAALKALGYDPDALEVLLHQMVGLVRGGEGVKMST 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 403 RSGDFVTLRDVVEE-----------------VGRDSVRFMMLYRKNSEPLDFDFAKVTEQSKDNPVfYVQYAHARCMSVF 465
Cdd:PRK01611 326 RAGNVVTLDDLLDEavgrarelieekeiaeaVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPP-YVQYAHARICSIL 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 466 RQAREAFADLDVSPenlaktvagIGDPAELQLVAKLAEFPRIVEAAAQSQEPHRVAFYLYDVASSFHAHWNkgkdqpelR 545
Cdd:PRK01611 405 RKAAEAGIDLLLAL---------LTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYN--------R 467
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1581859887 546 FVNDKNRES-SIARLGLVYAVASVLKSGLAITGTAAPDEM 584
Cdd:PRK01611 468 VLLKDEEEElRNARLALVKATAQVLKNGLDLLGISAPERM 507
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
11-584 |
8.20e-125 |
|
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: 378.61 E-value: 8.20e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 11 IKTAL-EQIDLVREKRSELDFGRITVEPPRDASHGDVATNAAMVLAKVLGTNPRALADVIIAKLKEDADVADVSVAGPgF 89
Cdd:TIGR00456 1 IKTLLkEEISQALLKAGLSKESEILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKLKTGEIIEKVEAAGP-F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 90 INIRLAVGYW-QRLLASMIGAGTDYGRSSLgKGKKVNVEYVSANPTGPMHVGHCRGAVVGDALANLLAFAGYGVEKEYYI 168
Cdd:TIGR00456 80 INFFLSPQKLlERLIQKILTQKEKYGSKKL-KNKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 169 NDAGSQIDVLARSVFLRYREALGEKiGEIPSGLYPGDYlVPVGQSLAADYGVR------LHNMPE-DQWMPIVKDRTIDA 241
Cdd:TIGR00456 159 NDWGRQFGLLALGVEKFGNEALNIA-VKKPDHGLEGFY-VEINKRLEENEELEeearelFVKLESgDEETIKLWKRLVEY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 242 MMVMIRDDLAALNVHHDVFFSERTLHANGaaAIRTAINDLTFKGYVYKgtlpppkgqlpedwedREQTLFRSTEVGDDID 321
Cdd:TIGR00456 237 SLEGIKETYDRLNIHFDSFVWEGESVKNG--MLPKVLEDLKEKGLVVE----------------DGALWLDLTLFGDKKD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 322 RPLIKSDGSYTYFAADVAYFKNKFDRGFDEMIYVLGADHGGYVKRLEAVARGVSDGKAKLTVLLCQLVKLYR-------- 393
Cdd:TIGR00456 299 RVLQKSDGTYLYLTTDIAYHLDKLERGFDKMIYVWGSDHHLHIAQMFAILEKLGYKKKELEHLNFGMVPLYSmktrrgnv 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 394 ---NGEPVKMSKRSGDFVTLR------DVVEEVGRDSVRFMMLYRKNSEPLDFDFAKVTeQSKDNPVFYVQYAHARCMSV 464
Cdd:TIGR00456 379 islDNLLDEASKRAGNVITIKndleeeKVADAVGIGAVRYFDLSKNRTTDYVFDWDAML-SFEGNTAPYIQYAHARICSI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 465 FRQAREAFADLDVSP-ENLaktvagigDPAELQLVAKLAEFPRIVEAAAQSQEPHRVAFYLYDVASSFHAHWNKGKdqpe 543
Cdd:TIGR00456 458 LRKAEIDGEKLIADDfELL--------EEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACP---- 525
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1581859887 544 lrfVNDKNRESSIARLGLVYAVASVLKSGLAITGTAAPDEM 584
Cdd:TIGR00456 526 ---VLDAENELAAARLALLKATRQTLKNGLDLLGIEPPERM 563
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
123-405 |
5.65e-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: 229.76 E-value: 5.65e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 123 KVNVEYVSANPTGPMHVGHCRGAVVGDALANLLAFAGYGVEKEYYINDAGSQIDVLARSVFLryrealgekigeipsgly 202
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSLEK------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 203 pgdylvpvgqslaadygvrlhnmpedqWmpivkdrtIDAMMVMIRDDLAA---LNVHHDVFFSERTLhangAAAIRTAIN 279
Cdd:cd00671 63 ---------------------------W--------RKLVEESIKADLETygrLDVRFDVWFGESSY----LGLMGKVVE 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 280 DLTFKGYVYkgtlpppkgqlpedwEDREQTLFRSTEVGDDIDRPLIKSDGSYTYFAADVAYFKNKFDRGFDEMIYVLGAD 359
Cdd:cd00671 104 LLEELGLLY---------------EEDGALWLDLTEFGDDKDRVLVRSDGTYTYFTRDIAYHLDKFERGADKIIYVVGAD 168
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1581859887 360 HGGYVKRLEAVARGVS-DGKAKLTVLLCQLVKLYRngePVKMSKRSG 405
Cdd:cd00671 169 HHGHFKRLFAALELLGyDEAKKLEHLLYGMVNLPK---EGKMSTRAG 212
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
454-584 |
2.58e-41 |
|
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: 145.41 E-value: 2.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 454 VQYAHARCMSVFRQAREAFADLdvsPENLAKTVAGIGDPAELQLVAKLAEFPRIVEAAAQSQEPHRVAFYLYDVASSFHA 533
Cdd:smart00836 1 VQYAHARICSILRKAGEAGETL---PDIADADLSLLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHS 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1581859887 534 HWNKgkdqpeLRFVNDKNRESSIARLGLVYAVASVLKSGLAITGTAAPDEM 584
Cdd:smart00836 78 FYNR------VRVLGEENPELRKARLALLKAVRQVLANGLRLLGISAPERM 122
|
|
| Anticodon_Ia_Arg |
cd07956 |
Anticodon-binding domain of arginyl tRNA synthetases; This domain is found in arginyl tRNA ... |
415-584 |
6.55e-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: 131.57 E-value: 6.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 415 EEVGRDSVRFMMLYRKNSEPLDFDFAKVTEQSKDnPVFYVQYAHARCMSVFRQA---REAFADLDVSPENlaktvagigD 491
Cdd:cd07956 1 EEVGVGAVKYQDLSNKRIKDYTFDWERMLSFEGD-TGPYLQYAHARLCSILRKAgetIEAEADADLSLLP---------E 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 492 PAELQLVAKLAEFPRIVEAAAQSQEPHRVAFYLYDVASSFHAHWNKGKdqpelrfVNDKNRESSIARLGLVYAVASVLKS 571
Cdd:cd07956 71 PDERDLILLLAKFPEVVKNAAETLEPHTIATYLFDLAHAFSKFYNACP-------VLGAEEELRNARLALVAAARQVLAN 143
|
170
....*....|...
gi 1581859887 572 GLAITGTAAPDEM 584
Cdd:cd07956 144 GLDLLGIEAPERM 156
|
|
| DALR_1 |
pfam05746 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
454-584 |
1.62e-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: 1.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 454 VQYAHARCMSVFRQAREAFADLDVSPENLAktvagigDPAELQLVAKLAEFPRIVEAAAQSQEPHRVAFYLYDVASSFHA 533
Cdd:pfam05746 1 LQYAHARICSILRKAGELGINLDIDADLLT-------EEEEKELLKALLQFPEVLEEAAEELEPHRLANYLYELASAFHS 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1581859887 534 HWNKGKdqpelrfVNDKNRESSIARLGLVYAVASVLKSGLAITGTAAPDEM 584
Cdd:pfam05746 74 FYNNCR-------VLDEDNEERNARLALLKAVRQVLKNGLDLLGIEAPEKM 117
|
|
| PLN02286 |
PLN02286 |
arginine-tRNA ligase |
35-577 |
9.62e-31 |
|
arginine-tRNA ligase
Pssm-ID: 215160 [Multi-domain] Cd Length: 576 Bit Score: 126.68 E-value: 9.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 35 VEPPRDASHGDVATNAAMVLAKVLG------TNPRALADVIIAKLKEDADVADVSVAGPGFINIRLAVGYWQRLLASMIG 108
Cdd:PLN02286 25 VAACTNPKFGDYQCNNAMGLWSKLKgkgtsfKNPRAVAQAIVKNLPASEMIESTSVAGPGFVNVRLSASWLAKRIERMLV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 109 AGTDYGRSSLGKgKKVNVEYVSANPTGPMHVGHCRGAVVGDALANLLAFAGYGVEKEYYINDAGSQIDVLARSVFLRYRE 188
Cdd:PLN02286 105 DGIDTWAPTLPV-KRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEFSGVEVLRRNHVGDWGTQFGMLIEHLFEKFPN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 189 ALGEKIGEIpsglypGDylvpvgqsLAADYGVRLHNMPEDqwmPIVKDRTIDAMMVMIRDD---LAALNVHHDVffSER- 264
Cdd:PLN02286 184 WESVSDQAI------GD--------LQEFYKAAKKRFDED---EEFKARAQQAVVRLQGGDpeyRAAWAKICEI--SRRe 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 265 ----------TLHANGAAA----IRTAINDLTFKGYVykgtlpppkgqlpedwEDREQTLFRSTEvGDDIdrPLI--KSD 328
Cdd:PLN02286 245 fekvyqrlrvELEEKGESFynpyIPGVIEELESKGLV----------------VESDGARVIFVE-GFDI--PLIvvKSD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 329 GSYTYFAADVAYFKNKF-DRGFDEMIYVLGADHGGYVKRLEAVAR----GVSDGKAKLTVLLCQLVKlyrnGEPVKMSK- 402
Cdd:PLN02286 306 GGFNYASTDLAALWYRLnEEKAEWIIYVTDVGQQQHFDMVFKAAKragwLPEDTYPRLEHVGFGLVL----GEDGKRFRt 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 403 RSGDFVTLRDVVEE-----------------------------VGRDSVRFMMLYRKNSEPLDFDFAKVTEqSKDNPVFY 453
Cdd:PLN02286 382 RSGEVVRLVDLLDEaksrskaaliergkdsewtpeeleqaaeaVGYGAVKYADLKNNRLTNYTFSFDQMLD-LKGNTAVY 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 454 VQYAHARCMSVFRQAREafadlDVspENLAKTVA-GIGDPAELQLVAKLAEFPRIVEAAAQSQEPHRVAFYLYDVASSFH 532
Cdd:PLN02286 461 LLYAHARICSIIRKSGK-----DI--DELKKTGKiVLDHPDERALGLHLLQFPEVVEEACTDLLPNRLCEYLYNLSEKFT 533
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1581859887 533 AHWNKGKdqpelrfVNDKNRESSiaRLGLVYAVASVLKSGLAITG 577
Cdd:PLN02286 534 KFYSNCK-------VNGSEEETS--RLLLCEATAIVMRKCFHLLG 569
|
|
| Arg_tRNA_synt_N |
smart01016 |
Arginyl tRNA synthetase N terminal dom; This domain is found at the amino terminus of Arginyl ... |
1-94 |
3.79e-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: 99.20 E-value: 3.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 1 MNLFTDFEARIKTALEQIDLVREkrseldfgrITVEPPRDASHGDVATNAAMVLAKVLGTNPRALADVIIAKLKEDADVA 80
Cdd:smart01016 1 DLLKEAIAEALKKALGVEGEPID---------IALERPKDPDHGDYATNVAFRLAKKLKKNPRELAEEIAEKLPKSDLVE 71
|
90
....*....|....
gi 1581859887 81 DVSVAGPGFINIRL 94
Cdd:smart01016 72 KVEIAGPGFINFFL 85
|
|
| Arg_tRNA_synt_N |
pfam03485 |
Arginyl tRNA synthetase N terminal domain; This domain is found at the amino terminus of ... |
7-94 |
6.84e-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: 89.98 E-value: 6.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 7 FEARIKTALEQIDLVrekrsELDFGRITVEPPRDASHGDVATNAAMVLAKVLGTNPRALADVIIAKLKEDADVADVSVAG 86
Cdd:pfam03485 1 LKKAIAKALSKLGGP-----DLELIDIVIETPKNPKFGDYATNVAMQLAKKLKKNPREIAEEIAEKLEKSDIIEKVEVAG 75
|
....*...
gi 1581859887 87 PGFINIRL 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 |
3.13e-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: 80.31 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 118 LGKGKKVNVEYVSANPTGPMHVGHCRGAVVGDALANLLAFAGYGVEKEYYINDAGSQIDVLARSVFLRYREALgekIGEI 197
Cdd:pfam00750 15 SREKKKVVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQFGMLIAGLEKYQDEKT---LQEM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 198 PSGLYPGDYlVPVGQSLAAD---------YGVRLHNMPED---QWMPIVKdrtidammvMIRDDLAALNVHHDVFFSERT 265
Cdd:pfam00750 92 PIQDLEDFY-REAKKHYDEEeefaerarnYVVKLQSGDEYwrrMWKLIVD---------ITMTQNQRLYDRLDVTLTEMG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 266 lHANGAAAIRTAINDLTFKGYVYkgtlpppkgqlpedwEDREQTLFRSTEVGDDIDRPLIKSDGSYTYFAADVAYFK-NK 344
Cdd:pfam00750 162 -ESLYNPMMNEIVKDFKKNGLVV---------------EIDGALVVFLDEFGKPMGVIVQKSDGGYLYTTTDIAAAKyRY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 345 FDRGFDEMIYVLGADHGGYVKRLEAVARGVS-DGKAKLTVLLCQLVKLYRNGEPvkMSKRSGDFVTLRDVVEEVGRDSVR 423
Cdd:pfam00750 226 ETLHADRMLYVIDSRQSQHMQQAFAILRKAGyVPESKDLEHINFGMVLGKDGKP--FKTRKGGTVKLADLLDEALERALQ 303
|
...
gi 1581859887 424 FMM 426
Cdd:pfam00750 304 LIM 306
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
126-239 |
7.63e-08 |
|
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: 51.71 E-value: 7.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859887 126 VEYVSANPTGPMHVGHCRGAVVGDALANLLAFAGYGVEKEYYINDAGSQIDVLARS---VFLRYREALGEKIGEipsgly 202
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKkgeNAKAFVERWIERIKE------ 74
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1581859887 203 pgDYLVPVGQSLAA----DYGVRLHNMPEDQWMPIVKDRTI 239
Cdd:cd00802 75 --DVEYMFLQAADFlllyETECDIHLGGSDQLGHIELGLEL 113
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
394-444 |
7.54e-07 |
|
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: 51.64 E-value: 7.54e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1581859887 394 NGEpvKMSKRSGDFVTLRDVVEEVGRDSVRFMML---YRKnsePLDFDFAKVTE 444
Cdd:COG0215 262 NGE--KMSKSLGNFFTVRDLLKKYDPEVLRFFLLsahYRS---PLDFSEEALEE 310
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
394-437 |
3.98e-05 |
|
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) 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.
Pssm-ID: 173899 [Multi-domain] Cd Length: 213 Bit Score: 44.88 E-value: 3.98e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1581859887 394 NGEpvKMSKRSGDFVTLRDVVEEVGRDSVRFMMLYRKNSEPLDF 437
Cdd:cd00672 171 DGE--KMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDF 212
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
393-439 |
1.82e-04 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 44.47 E-value: 1.82e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1581859887 393 RNGEpvKMSKRSGDFVTLRDVVEEVGRDSVRFMMLYrkNSEPL-DFDF 439
Cdd:PRK12300 573 LEGK--KMSKSKGNVIPLRKAIEEYGADVVRLYLTS--SAELLqDADW 616
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
394-424 |
4.80e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 40.05 E-value: 4.80e-03
10 20 30
....*....|....*....|....*....|.
gi 1581859887 394 NGEpvKMSKRSGDFVTLRDVVEEVGRDSVRF 424
Cdd:PLN02959 715 NSE--KMSKSTGNFLTLRQAIEEFSADATRF 743
|
|
| LysRS_core_class_I |
cd00674 |
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) ... |
399-438 |
4.99e-03 |
|
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) 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. The class I LysRS is found only in archaea and some bacteria and has evolved separately from class II LysRS, as the two do not share structural or sequence similarity.
Pssm-ID: 173900 [Multi-domain] Cd Length: 353 Bit Score: 39.61 E-value: 4.99e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1581859887 399 KMSKRSGDFVTLRDVVEEVGRDSVRFMMLYRKNSE-PLDFD 438
Cdd:cd00674 275 KMSSSKGNVITPSDWLEVAPPEVLRYLYARRKNPEkHIGFD 315
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