|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02286 |
PLN02286 |
arginine-tRNA ligase |
16-590 |
0e+00 |
|
arginine-tRNA ligase
Pssm-ID: 215160 [Multi-domain] Cd Length: 576 Bit Score: 1204.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 16 RQLAKLFDVSLKLTVPDEPNVEPLIEP---GKFGDYQCNNAMGLWSLIKGKGTQFRGPPAVGQALIQSLPTSEMVESCSI 92
Cdd:PLN02286 1 RELAKLFEASLRLTVPDEPSVEPLVAActnPKFGDYQCNNAMGLWSKLKGKGTSFKNPRAVAQAIVKNLPASEMIESTSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 93 AGPGFVNVVLSSKWMAKSIENMLVDGIDTWAPTLSVKRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEYSKVEVLRR 172
Cdd:PLN02286 81 AGPGFVNVRLSASWLAKRIERMLVDGIDTWAPTLPVKRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEFSGVEVLRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 173 NHVGDWGTQFGMLIEFLFEKFPDTESVTETAIGDLQVFYRESKLKFDLNPEFKEKAQQAVVRLQGGDPVYRQAWAKICEI 252
Cdd:PLN02286 161 NHVGDWGTQFGMLIEHLFEKFPNWESVSDQAIGDLQEFYKAAKKRFDEDEEFKARAQQAVVRLQGGDPEYRAAWAKICEI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 253 SRNEFAKVYKRLRIELEEKGESFYNPYIANVIEELSSKGLVEESKGARVIFIEGFKIPLIVVKSDGGFNYASTDLTALWY 332
Cdd:PLN02286 241 SRREFEKVYQRLRVELEEKGESFYNPYIPGVIEELESKGLVVESDGARVIFVEGFDIPLIVVKSDGGFNYASTDLAALWY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 333 RLNEEKAEWIIYVTDVGQQQHFDMFFKAARKAGWLPDDdkTYPRVSHVGFGLVLGDDNKRFRTRAAEVVRLADLLDEAKD 412
Cdd:PLN02286 321 RLNEEKAEWIIYVTDVGQQQHFDMVFKAAKRAGWLPED--TYPRLEHVGFGLVLGEDGKRFRTRSGEVVRLVDLLDEAKS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 413 RSKAALIERGKDKEWSPEELDQIAEAVGYGALKYADLKTNRITGYTFSFDQMLNDKGDTAVYLLYAHARICSIIRKSGKD 492
Cdd:PLN02286 399 RSKAALIERGKDSEWTPEELEQAAEAVGYGAVKYADLKNNRLTNYTFSFDQMLDLKGNTAVYLLYAHARICSIIRKSGKD 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 493 IDELKKTGKIALDHAAERALGLHLLQFAETVEEACTTLLPNVLCKYLYYLSEEFTKFYSNCQVNGSAEETSRLLLCEATA 572
Cdd:PLN02286 479 IDELKKTGKIVLDHPDERALGLHLLQFPEVVEEACTDLLPNRLCEYLYNLSEKFTKFYSNCKVNGSEEETSRLLLCEATA 558
|
570
....*....|....*...
gi 15219682 573 IVMRKCFHLLGITPVYKL 590
Cdd:PLN02286 559 IVMRKCFHLLGITPLYRL 576
|
|
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
13-587 |
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: 569.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 13 NPRRQLAKLFDVSLKLTVPDEPNVEPLIEP---GKFGDYQCNNAMGLwslikGKgtQFRGPP-AVGQALIQSLPTSEMVE 88
Cdd:COG0018 2 NIKEELAEAIAAALAALGAGLEEPDILVERpkdPEHGDYATNVAMQL-----AK--PLKKNPrEIAEEIAEALDADPLVE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 89 SCSIAGPGFVNVVLSSKWMAKSIENMLVDGIDTWAPTLSV-KRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEYSKV 167
Cdd:COG0018 75 KVEIAGPGFINFFLSPAALAAVLKEILADGEDYGRSDAGKgKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 168 EVLRRNHVGDWGTQFGMLIEFLFEKFPDTESVTETAIGDLQVFYRESKLKFDLNPEFKEKAQQAVVRLQGGDPVYRQAWA 247
Cdd:COG0018 155 DVTRENYINDAGTQIGKLALSLERYGEEEIEPESKPDGYLGDLYVKFHKEYEEDPELEDIARELLAKLEPGDEEALELWK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 248 KICEISRNEFAKVYKRLRIELEE-KGESFYNP--YIANVIEELSSKGLVEESKGARVIFIEGFKI--PLIVVKSDGGFNY 322
Cdd:COG0018 235 KAVDWSLEEIKEDLKRLGVEFDVwFSESSLYDsgAVEEVVEELKEKGLLYESDGALWVRLTEFGDdkDRVLVKSDGTYTY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 323 ASTDLTALWYRLNEEKAEWIIYVTDVGQQQHFDMFFKAARKAGWLPDDDktyprVSHVGFGLVLGDDNKRFRTRAAEVVR 402
Cdd:COG0018 315 FTTDIAYHLYKFERYGFDRVIYVVGADQHGHFKRLFAALKALGYDPAKD-----LEHLLFGMVNLRDGEKMSTRAGTVVT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 403 LADLLDEAKDRSKAALIERgkdkewSPEELDQIAEAVGYGALKYADLKTNRITGYTFSFDQMLNDKGDTAVYLLYAHARI 482
Cdd:COG0018 390 LDDLLDEAVERAREIIEEK------SEEEKEEIAEQVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNTNPYVQYAHARI 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 483 CSIIRKSGKDIDELKKTGKIALDHAAERALGLHLLQFAETVEEACTTLLPNVLCKYLYYLSEEFTKFYSNCQVNGSAEE- 561
Cdd:COG0018 464 CSILRKAGEELDGLAEADLSLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRILKAEDEe 543
|
570 580
....*....|....*....|....*...
gi 15219682 562 --TSRLLLCEATAIVMRKCFHLLGITPV 587
Cdd:COG0018 544 lrAARLALVAATAQVLKNGLGLLGISAP 571
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
30-590 |
7.69e-140 |
|
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: 417.51 E-value: 7.69e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 30 VPDEPNVEPLIEPgKFGDYQCNNAMGLwslikgKGTQFRGPPAVGQALIQSLPTSEMVESCSIAGPgFVNVVLSSKWMAK 109
Cdd:TIGR00456 20 KESEILVEETPNP-EFGDYASNIAFPL------AKVLKKAPRQIAEEIVLKLKTGEIIEKVEAAGP-FINFFLSPQKLLE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 110 SIENMLVDGIDTWAPTLSV-KRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEYSKVEVLRRNHVGDWGTQFGMLIeF 188
Cdd:TIGR00456 92 RLIQKILTQKEKYGSKKLKnKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYVNDWGRQFGLLA-L 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 189 LFEKFPDTESVTETA--IGDLQVFYRESKLKFDLNPEFKEKAQQAVVRLQGGDPVYRQAWAKICEISRNEFAKVYKRLRI 266
Cdd:TIGR00456 171 GVEKFGNEALNIAVKkpDHGLEGFYVEINKRLEENEELEEEARELFVKLESGDEETIKLWKRLVEYSLEGIKETYDRLNI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 267 ELEEK---GESFYNPYIANVIEELSSKGLVEESkGARVIFIEGF--KIPLIVVKSDGGFNYASTDLTALWYRLnEEKAEW 341
Cdd:TIGR00456 251 HFDSFvweGESVKNGMLPKVLEDLKEKGLVVED-GALWLDLTLFgdKKDRVLQKSDGTYLYLTTDIAYHLDKL-ERGFDK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 342 IIYVTDVGQQQHFDMFFKAARKAGWLPdddktyPRVSHVGFGLVLGDDNKrfrTRAAEVVRLADLLDEAKDRSKAALIER 421
Cdd:TIGR00456 329 MIYVWGSDHHLHIAQMFAILEKLGYKK------KELEHLNFGMVPLYSMK---TRRGNVISLDNLLDEASKRAGNVITIK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 422 GKdkewspEELDQIAEAVGYGALKYADLKTNRITGYTFSFDQMLNDKGDTAVYLLYAHARICSIIRKSGKDIDELKKTgK 501
Cdd:TIGR00456 400 ND------LEEEKVADAVGIGAVRYFDLSKNRTTDYVFDWDAMLSFEGNTAPYIQYAHARICSILRKAEIDGEKLIAD-D 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 502 IALDHAAERALGLHLLQFAETVEEACTTLLPNVLCKYLYYLSEEFTKFYSNCQVNGSAEE--TSRLLLCEATAIVMRKCF 579
Cdd:TIGR00456 473 FELLEEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACPVLDAENElaAARLALLKATRQTLKNGL 552
|
570
....*....|.
gi 15219682 580 HLLGITPVYKL 590
Cdd:TIGR00456 553 DLLGIEPPERM 563
|
|
| tRNA-synt_1d |
pfam00750 |
tRNA synthetases class I (R); Other tRNA synthetase sub-families are too dissimilar to be ... |
129-461 |
1.74e-133 |
|
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: 393.47 E-value: 1.74e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 129 KRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEYSKVEVLRRNHVGDWGTQFGMLIEFLFEKFPDTESVtETAIGDLQ 208
Cdd:pfam00750 19 KKVVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQFGMLIAGLEKYQDEKTLQ-EMPIQDLE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 209 VFYRESKLKFDLNPEFKEKAQQAVVRLQGGDPVYRQAWAKICEISRNEFAKVYKRLRIELEEKGESFYNPYIANVIEELS 288
Cdd:pfam00750 98 DFYREAKKHYDEEEEFAERARNYVVKLQSGDEYWRRMWKLIVDITMTQNQRLYDRLDVTLTEMGESLYNPMMNEIVKDFK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 289 SKGLVEESKGARVIFIEGF--KIPLIVVKSDGGFNYASTDLTALWYRLNEEKAEWIIYVTDVGQQQHFDMFFKAARKAGW 366
Cdd:pfam00750 178 KNGLVVEIDGALVVFLDEFgkPMGVIVQKSDGGYLYTTTDIAAAKYRYETLHADRMLYVIDSRQSQHMQQAFAILRKAGY 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 367 LPDDDktypRVSHVGFGLVLGDDNKRFRTRAAEVVRLADLLDEAKDRSKAALIERGKDKEWSPEELDQIAEAVGYGALKY 446
Cdd:pfam00750 258 VPESK----DLEHINFGMVLGKDGKPFKTRKGGTVKLADLLDEALERALQLIMEKNKDKILQADELEAVADAVGIGAIKY 333
|
330
....*....|....*
gi 15219682 447 ADLKTNRITGYTFSF 461
Cdd:pfam00750 334 ADLSKNRTNDYIFDW 348
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
130-397 |
1.55e-68 |
|
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: 220.90 E-value: 1.55e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 130 RAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEYSKVEVLRRNHVGDWGTQFGMLIEFLfekfpdtesvtetaigdlqv 209
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSL-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 210 fyresklkfdlnpefkekaqqavvrlqggdpvyrQAWAKICEISRNEFAKVYKRLRIEL-EEKGESFYNPYIANVIEELS 288
Cdd:cd00671 61 ----------------------------------EKWRKLVEESIKADLETYGRLDVRFdVWFGESSYLGLMGKVVELLE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 289 SKGLVEESKGARVIFIEGFK--IPLIVVKSDGGFNYASTDLTALWYRLnEEKAEWIIYVTDVGQQQHFDMFFKAARKAGW 366
Cdd:cd00671 107 ELGLLYEEDGALWLDLTEFGddKDRVLVRSDGTYTYFTRDIAYHLDKF-ERGADKIIYVVGADHHGHFKRLFAALELLGY 185
|
250 260 270
....*....|....*....|....*....|.
gi 15219682 367 LPDDdktypRVSHVGFGLVLGDDNKRFRTRA 397
Cdd:cd00671 186 DEAK-----KLEHLLYGMVNLPKEGKMSTRA 211
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
475-587 |
6.61e-33 |
|
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: 122.30 E-value: 6.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 475 LLYAHARICSIIRKS---GKDIDELKKTGKIALDHAAERALGLHLLQFAETVEEACTTLLPNVLCKYLYYLSEEFTKFYS 551
Cdd:smart00836 1 VQYAHARICSILRKAgeaGETLPDIADADLSLLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYN 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 15219682 552 NCQVNGSAEE---TSRLLLCEATAIVMRKCFHLLGITPV 587
Cdd:smart00836 81 RVRVLGEENPelrKARLALLKAVRQVLANGLRLLGISAP 119
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02286 |
PLN02286 |
arginine-tRNA ligase |
16-590 |
0e+00 |
|
arginine-tRNA ligase
Pssm-ID: 215160 [Multi-domain] Cd Length: 576 Bit Score: 1204.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 16 RQLAKLFDVSLKLTVPDEPNVEPLIEP---GKFGDYQCNNAMGLWSLIKGKGTQFRGPPAVGQALIQSLPTSEMVESCSI 92
Cdd:PLN02286 1 RELAKLFEASLRLTVPDEPSVEPLVAActnPKFGDYQCNNAMGLWSKLKGKGTSFKNPRAVAQAIVKNLPASEMIESTSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 93 AGPGFVNVVLSSKWMAKSIENMLVDGIDTWAPTLSVKRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEYSKVEVLRR 172
Cdd:PLN02286 81 AGPGFVNVRLSASWLAKRIERMLVDGIDTWAPTLPVKRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEFSGVEVLRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 173 NHVGDWGTQFGMLIEFLFEKFPDTESVTETAIGDLQVFYRESKLKFDLNPEFKEKAQQAVVRLQGGDPVYRQAWAKICEI 252
Cdd:PLN02286 161 NHVGDWGTQFGMLIEHLFEKFPNWESVSDQAIGDLQEFYKAAKKRFDEDEEFKARAQQAVVRLQGGDPEYRAAWAKICEI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 253 SRNEFAKVYKRLRIELEEKGESFYNPYIANVIEELSSKGLVEESKGARVIFIEGFKIPLIVVKSDGGFNYASTDLTALWY 332
Cdd:PLN02286 241 SRREFEKVYQRLRVELEEKGESFYNPYIPGVIEELESKGLVVESDGARVIFVEGFDIPLIVVKSDGGFNYASTDLAALWY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 333 RLNEEKAEWIIYVTDVGQQQHFDMFFKAARKAGWLPDDdkTYPRVSHVGFGLVLGDDNKRFRTRAAEVVRLADLLDEAKD 412
Cdd:PLN02286 321 RLNEEKAEWIIYVTDVGQQQHFDMVFKAAKRAGWLPED--TYPRLEHVGFGLVLGEDGKRFRTRSGEVVRLVDLLDEAKS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 413 RSKAALIERGKDKEWSPEELDQIAEAVGYGALKYADLKTNRITGYTFSFDQMLNDKGDTAVYLLYAHARICSIIRKSGKD 492
Cdd:PLN02286 399 RSKAALIERGKDSEWTPEELEQAAEAVGYGAVKYADLKNNRLTNYTFSFDQMLDLKGNTAVYLLYAHARICSIIRKSGKD 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 493 IDELKKTGKIALDHAAERALGLHLLQFAETVEEACTTLLPNVLCKYLYYLSEEFTKFYSNCQVNGSAEETSRLLLCEATA 572
Cdd:PLN02286 479 IDELKKTGKIVLDHPDERALGLHLLQFPEVVEEACTDLLPNRLCEYLYNLSEKFTKFYSNCKVNGSEEETSRLLLCEATA 558
|
570
....*....|....*...
gi 15219682 573 IVMRKCFHLLGITPVYKL 590
Cdd:PLN02286 559 IVMRKCFHLLGITPLYRL 576
|
|
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
13-587 |
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: 569.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 13 NPRRQLAKLFDVSLKLTVPDEPNVEPLIEP---GKFGDYQCNNAMGLwslikGKgtQFRGPP-AVGQALIQSLPTSEMVE 88
Cdd:COG0018 2 NIKEELAEAIAAALAALGAGLEEPDILVERpkdPEHGDYATNVAMQL-----AK--PLKKNPrEIAEEIAEALDADPLVE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 89 SCSIAGPGFVNVVLSSKWMAKSIENMLVDGIDTWAPTLSV-KRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEYSKV 167
Cdd:COG0018 75 KVEIAGPGFINFFLSPAALAAVLKEILADGEDYGRSDAGKgKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 168 EVLRRNHVGDWGTQFGMLIEFLFEKFPDTESVTETAIGDLQVFYRESKLKFDLNPEFKEKAQQAVVRLQGGDPVYRQAWA 247
Cdd:COG0018 155 DVTRENYINDAGTQIGKLALSLERYGEEEIEPESKPDGYLGDLYVKFHKEYEEDPELEDIARELLAKLEPGDEEALELWK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 248 KICEISRNEFAKVYKRLRIELEE-KGESFYNP--YIANVIEELSSKGLVEESKGARVIFIEGFKI--PLIVVKSDGGFNY 322
Cdd:COG0018 235 KAVDWSLEEIKEDLKRLGVEFDVwFSESSLYDsgAVEEVVEELKEKGLLYESDGALWVRLTEFGDdkDRVLVKSDGTYTY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 323 ASTDLTALWYRLNEEKAEWIIYVTDVGQQQHFDMFFKAARKAGWLPDDDktyprVSHVGFGLVLGDDNKRFRTRAAEVVR 402
Cdd:COG0018 315 FTTDIAYHLYKFERYGFDRVIYVVGADQHGHFKRLFAALKALGYDPAKD-----LEHLLFGMVNLRDGEKMSTRAGTVVT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 403 LADLLDEAKDRSKAALIERgkdkewSPEELDQIAEAVGYGALKYADLKTNRITGYTFSFDQMLNDKGDTAVYLLYAHARI 482
Cdd:COG0018 390 LDDLLDEAVERAREIIEEK------SEEEKEEIAEQVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNTNPYVQYAHARI 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 483 CSIIRKSGKDIDELKKTGKIALDHAAERALGLHLLQFAETVEEACTTLLPNVLCKYLYYLSEEFTKFYSNCQVNGSAEE- 561
Cdd:COG0018 464 CSILRKAGEELDGLAEADLSLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRILKAEDEe 543
|
570 580
....*....|....*....|....*...
gi 15219682 562 --TSRLLLCEATAIVMRKCFHLLGITPV 587
Cdd:COG0018 544 lrAARLALVAATAQVLKNGLGLLGISAP 571
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
13-587 |
2.90e-155 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 455.00 E-value: 2.90e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 13 NPRRQLAKLFDVSL-KLTVPDEPNVepLIEPGK---FGDYQCNNAMGLWSLIKGKgtqfrgPPAVGQALIqslptsEMVE 88
Cdd:PRK01611 4 DIKELLAEALAAALeAGGLPELPAV--LIERPKdpeHGDYATNVAMQLAKKLKKN------PREIAEEIV------EAIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 89 SCSIAGPGFVNVVLSSKWMAKSIENMLVDGiDTW--APTLSVKRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEYSK 166
Cdd:PRK01611 70 KVEIAGPGFINFFLDPAALAELVLAILEAG-ERYgrSDIGKGKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 167 VEVLRRNHVGDWGTQFGMLIEFLFEkfpdtesvtetaigdlqvfyresklkfdlnpefkekaqqavvrlqggdpvyrqAW 246
Cdd:PRK01611 149 YDVTREYYVNDAGTQIGMLIASLEL-----------------------------------------------------LW 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 247 AKICEISRNEFAKVYKRLRIELEE---KGESFYNPYIANVIEELSSKGL-VEESKGARVIFIEGF--KIPLIVVKSDGGF 320
Cdd:PRK01611 176 RKAVDISLDEIKEDLDRLGVHFDVwfsESELYYNGKVDEVVEDLKEKGLlYVESDGALWVRLTEFgdDKDRVLIKSDGTY 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 321 NYASTDLTALWYRLneEKAEWIIYVTDVGQQQHFDMFFKAARKAGWLPDDDKtypRVSHVGFGLVLGDDNKRFRTRAAEV 400
Cdd:PRK01611 256 TYFTRDIAYHLYKF--ERFDRVIYVVGADHHGHFKRLKAALKALGYDPDALE---VLLHQMVGLVRGGEGVKMSTRAGNV 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 401 VRLADLLDEAKDRSKAALIERgkdkewspeeldQIAEAVGYGALKYADLKTNRITGYTFSFDQMLNDKGDTAVYLLYAHA 480
Cdd:PRK01611 331 VTLDDLLDEAVGRARELIEEK------------EIAEAVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPPYVQYAHA 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 481 RICSIIRKSGkdiDELKKTGKIALDHAAERALGLHLLQFAETVEEACTTLLPNVLCKYLYYLSEEFTKFYSNCQVNGSAE 560
Cdd:PRK01611 399 RICSILRKAA---EAGIDLLLALLTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYNRVLLKDEEE 475
|
570 580
....*....|....*....|....*....
gi 15219682 561 E--TSRLLLCEATAIVMRKCFHLLGITPV 587
Cdd:PRK01611 476 ElrNARLALVKATAQVLKNGLDLLGISAP 504
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
30-590 |
7.69e-140 |
|
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: 417.51 E-value: 7.69e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 30 VPDEPNVEPLIEPgKFGDYQCNNAMGLwslikgKGTQFRGPPAVGQALIQSLPTSEMVESCSIAGPgFVNVVLSSKWMAK 109
Cdd:TIGR00456 20 KESEILVEETPNP-EFGDYASNIAFPL------AKVLKKAPRQIAEEIVLKLKTGEIIEKVEAAGP-FINFFLSPQKLLE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 110 SIENMLVDGIDTWAPTLSV-KRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEYSKVEVLRRNHVGDWGTQFGMLIeF 188
Cdd:TIGR00456 92 RLIQKILTQKEKYGSKKLKnKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYVNDWGRQFGLLA-L 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 189 LFEKFPDTESVTETA--IGDLQVFYRESKLKFDLNPEFKEKAQQAVVRLQGGDPVYRQAWAKICEISRNEFAKVYKRLRI 266
Cdd:TIGR00456 171 GVEKFGNEALNIAVKkpDHGLEGFYVEINKRLEENEELEEEARELFVKLESGDEETIKLWKRLVEYSLEGIKETYDRLNI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 267 ELEEK---GESFYNPYIANVIEELSSKGLVEESkGARVIFIEGF--KIPLIVVKSDGGFNYASTDLTALWYRLnEEKAEW 341
Cdd:TIGR00456 251 HFDSFvweGESVKNGMLPKVLEDLKEKGLVVED-GALWLDLTLFgdKKDRVLQKSDGTYLYLTTDIAYHLDKL-ERGFDK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 342 IIYVTDVGQQQHFDMFFKAARKAGWLPdddktyPRVSHVGFGLVLGDDNKrfrTRAAEVVRLADLLDEAKDRSKAALIER 421
Cdd:TIGR00456 329 MIYVWGSDHHLHIAQMFAILEKLGYKK------KELEHLNFGMVPLYSMK---TRRGNVISLDNLLDEASKRAGNVITIK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 422 GKdkewspEELDQIAEAVGYGALKYADLKTNRITGYTFSFDQMLNDKGDTAVYLLYAHARICSIIRKSGKDIDELKKTgK 501
Cdd:TIGR00456 400 ND------LEEEKVADAVGIGAVRYFDLSKNRTTDYVFDWDAMLSFEGNTAPYIQYAHARICSILRKAEIDGEKLIAD-D 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 502 IALDHAAERALGLHLLQFAETVEEACTTLLPNVLCKYLYYLSEEFTKFYSNCQVNGSAEE--TSRLLLCEATAIVMRKCF 579
Cdd:TIGR00456 473 FELLEEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACPVLDAENElaAARLALLKATRQTLKNGL 552
|
570
....*....|.
gi 15219682 580 HLLGITPVYKL 590
Cdd:TIGR00456 553 DLLGIEPPERM 563
|
|
| tRNA-synt_1d |
pfam00750 |
tRNA synthetases class I (R); Other tRNA synthetase sub-families are too dissimilar to be ... |
129-461 |
1.74e-133 |
|
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: 393.47 E-value: 1.74e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 129 KRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEYSKVEVLRRNHVGDWGTQFGMLIEFLFEKFPDTESVtETAIGDLQ 208
Cdd:pfam00750 19 KKVVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQFGMLIAGLEKYQDEKTLQ-EMPIQDLE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 209 VFYRESKLKFDLNPEFKEKAQQAVVRLQGGDPVYRQAWAKICEISRNEFAKVYKRLRIELEEKGESFYNPYIANVIEELS 288
Cdd:pfam00750 98 DFYREAKKHYDEEEEFAERARNYVVKLQSGDEYWRRMWKLIVDITMTQNQRLYDRLDVTLTEMGESLYNPMMNEIVKDFK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 289 SKGLVEESKGARVIFIEGF--KIPLIVVKSDGGFNYASTDLTALWYRLNEEKAEWIIYVTDVGQQQHFDMFFKAARKAGW 366
Cdd:pfam00750 178 KNGLVVEIDGALVVFLDEFgkPMGVIVQKSDGGYLYTTTDIAAAKYRYETLHADRMLYVIDSRQSQHMQQAFAILRKAGY 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 367 LPDDDktypRVSHVGFGLVLGDDNKRFRTRAAEVVRLADLLDEAKDRSKAALIERGKDKEWSPEELDQIAEAVGYGALKY 446
Cdd:pfam00750 258 VPESK----DLEHINFGMVLGKDGKPFKTRKGGTVKLADLLDEALERALQLIMEKNKDKILQADELEAVADAVGIGAIKY 333
|
330
....*....|....*
gi 15219682 447 ADLKTNRITGYTFSF 461
Cdd:pfam00750 334 ADLSKNRTNDYIFDW 348
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
130-397 |
1.55e-68 |
|
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: 220.90 E-value: 1.55e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 130 RAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEYSKVEVLRRNHVGDWGTQFGMLIEFLfekfpdtesvtetaigdlqv 209
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSL-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 210 fyresklkfdlnpefkekaqqavvrlqggdpvyrQAWAKICEISRNEFAKVYKRLRIEL-EEKGESFYNPYIANVIEELS 288
Cdd:cd00671 61 ----------------------------------EKWRKLVEESIKADLETYGRLDVRFdVWFGESSYLGLMGKVVELLE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 289 SKGLVEESKGARVIFIEGFK--IPLIVVKSDGGFNYASTDLTALWYRLnEEKAEWIIYVTDVGQQQHFDMFFKAARKAGW 366
Cdd:cd00671 107 ELGLLYEEDGALWLDLTEFGddKDRVLVRSDGTYTYFTRDIAYHLDKF-ERGADKIIYVVGADHHGHFKRLFAALELLGY 185
|
250 260 270
....*....|....*....|....*....|.
gi 15219682 367 LPDDdktypRVSHVGFGLVLGDDNKRFRTRA 397
Cdd:cd00671 186 DEAK-----KLEHLLYGMVNLPKEGKMSTRA 211
|
|
| Anticodon_Ia_Arg |
cd07956 |
Anticodon-binding domain of arginyl tRNA synthetases; This domain is found in arginyl tRNA ... |
437-587 |
4.33e-47 |
|
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: 162.00 E-value: 4.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 437 EAVGYGALKYADLKTNRITGYTFSFDQMLNDKGDTAVYLLYAHARICSIIRKSGKDIDELKKTGKIALDHAAERALGLHL 516
Cdd:cd07956 1 EEVGVGAVKYQDLSNKRIKDYTFDWERMLSFEGDTGPYLQYAHARLCSILRKAGETIEAEADADLSLLPEPDERDLILLL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15219682 517 LQFAETVEEACTTLLPNVLCKYLYYLSEEFTKFYSNCQVNGSAEE--TSRLLLCEATAIVMRKCFHLLGITPV 587
Cdd:cd07956 81 AKFPEVVKNAAETLEPHTIATYLFDLAHAFSKFYNACPVLGAEEElrNARLALVAAARQVLANGLDLLGIEAP 153
|
|
| DALR_1 |
pfam05746 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
475-590 |
3.85e-37 |
|
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: 133.93 E-value: 3.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 475 LLYAHARICSIIRKSGKDIDELKKTgKIALDHAAERALGLHLLQFAETVEEACTTLLPNVLCKYLYYLSEEFTKFYSNCQ 554
Cdd:pfam05746 1 LQYAHARICSILRKAGELGINLDID-ADLLTEEEEKELLKALLQFPEVLEEAAEELEPHRLANYLYELASAFHSFYNNCR 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 15219682 555 VNGSAEE--TSRLLLCEATAIVMRKCFHLLGITPVYKL 590
Cdd:pfam05746 80 VLDEDNEerNARLALLKAVRQVLKNGLDLLGIEAPEKM 117
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
475-587 |
6.61e-33 |
|
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: 122.30 E-value: 6.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 475 LLYAHARICSIIRKS---GKDIDELKKTGKIALDHAAERALGLHLLQFAETVEEACTTLLPNVLCKYLYYLSEEFTKFYS 551
Cdd:smart00836 1 VQYAHARICSILRKAgeaGETLPDIADADLSLLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYN 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 15219682 552 NCQVNGSAEE---TSRLLLCEATAIVMRKCFHLLGITPV 587
Cdd:smart00836 81 RVRVLGEENPelrKARLALLKAVRQVLANGLRLLGISAP 119
|
|
| Arg_tRNA_synt_N |
pfam03485 |
Arginyl tRNA synthetase N terminal domain; This domain is found at the amino terminus of ... |
18-102 |
7.60e-14 |
|
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: 66.87 E-value: 7.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 18 LAKLFDVSL-KLTVPDEPNVEPLIEP---GKFGDYQCNNAMGLWSLIKgkgtqfRGPPAVGQALIQSLPTSEMVESCSIA 93
Cdd:pfam03485 1 LKKAIAKALsKLGGPDLELIDIVIETpknPKFGDYATNVAMQLAKKLK------KNPREIAEEIAEKLEKSDIIEKVEVA 74
|
....*....
gi 15219682 94 GPGFVNVVL 102
Cdd:pfam03485 75 GPGFINFFL 83
|
|
| Arg_tRNA_synt_N |
smart01016 |
Arginyl tRNA synthetase N terminal dom; This domain is found at the amino terminus of Arginyl ... |
16-102 |
1.67e-13 |
|
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: 66.07 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219682 16 RQLAKLFDVSLKLTVPDEPN-VEPLIEP---GKFGDYQCNNAMGLWSLIKgkgtqfRGPPAVGQALIQSLPTSEMVESCS 91
Cdd:smart01016 1 DLLKEAIAEALKKALGVEGEpIDIALERpkdPDHGDYATNVAFRLAKKLK------KNPRELAEEIAEKLPKSDLVEKVE 74
|
90
....*....|.
gi 15219682 92 IAGPGFVNVVL 102
Cdd:smart01016 75 IAGPGFINFFL 85
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
133-183 |
2.54e-07 |
|
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: 50.17 E-value: 2.54e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 15219682 133 VDFSSPNIAKEMHVGHLRSTIIGDTLARMLEYSKVEVLRRNHVGDWGTQFG 183
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIG 51
|
|
| |
