|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
19-557 |
0e+00 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 691.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 19 QVILGEDGKPLSKKALKKLQKEQEKQRKKEERalqleaeREAREKKAAAEDTAKDNYGKLPLIQSRdSDRTGQKRVKFVD 98
Cdd:PLN02850 3 QEAVEESGEKISKKAAKKAAAKAEKLRREATA-------KAAAASLEDEDDPLASNYGDVPLEELQ-SKVTGREWTDVSD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 99 LDEAKDsDKEVLFRARVHNTRQQGaTLAFLTLRQQASLIQGLVKAnKEGTISKNMVKWAGSLNLESIVLVRGIVKKVDEP 178
Cdd:PLN02850 75 LGEELA-GSEVLIRGRVHTIRGKG-KSAFLVLRQSGFTVQCVVFV-SEVTVSKGMVKYAKQLSRESVVDVEGVVSVPKKP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 179 IKSATvQNLEIHITKIYTISETPEALPILLEDASRSEAEAEAAG-----LPVVNLDTRLDYRVIDLRTVTNQAIFRIQAG 253
Cdd:PLN02850 152 VKGTT-QQVEIQVRKIYCVSKALATLPFNVEDAARSESEIEKALqtgeqLVRVGQDTRLNNRVLDLRTPANQAIFRIQSQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 254 VCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQQLIVADFERVYEIGPVFRAENSNTHR 333
Cdd:PLN02850 231 VCNLFREFLLSKGFVEIHTPKLIAGASEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGDFRRVFEIGPVFRAEDSFTHR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 334 HMTEFTGLDMEMAFEEHYHEVLDTLSELFVFIFSELPKRFAHEIELVRKQYPVEEFK-LPkdgKMVRLTYKEGIEMLRAA 412
Cdd:PLN02850 311 HLCEFTGLDLEMEIKEHYSEVLDVVDELFVAIFDGLNERCKKELEAIREQYPFEPLKyLP---KTLRLTFAEGIQMLKEA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 413 GKEIGDFEDLSTENEKFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPDPANPKYSNSYDFFMRGEEILSGAQRIHDHALL 492
Cdd:PLN02850 388 GVEVDPLGDLNTESERKLGQLVKEKYGTDFYILHRYPLAVRPFYTMPCPDDPKYSNSFDVFIRGEEIISGAQRVHDPELL 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323011 493 QERMKAHGLSPEDpgLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDPKRLRP 557
Cdd:PLN02850 468 EKRAEECGIDVKT--ISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQRLAP 530
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
94-557 |
0e+00 |
|
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, aspS_arch, represents aspartyl-tRNA synthetases from the eukaryotic cytosol and from the Archaea. In some species, this enzyme aminoacylates tRNA for both Asp and Asn; Asp-tRNA(asn) is subsequently transamidated to Asn-tRNA(asn). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273087 [Multi-domain] Cd Length: 428 Bit Score: 664.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 94 VKFVDLDEAKDSdKEVLFRARVHNTRQQGAtLAFLTLRQQASLIQGLVKANKegtISKNMVKWAGSLNLESIVLVRGIVK 173
Cdd:TIGR00458 1 VYSADIKPEMDG-QEVTFMGWVHEIRDLGG-LIFVLLRDREGLIQITAPAKK---VSKNLFKWAKKLNLESVVAVRGIVK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 174 kvdepIKSATVQNLEIHITKIYTISETPEALPILLEDasRSEAEaeaaglpvvnLDTRLDYRVIDLRTVTNQAIFRIQAG 253
Cdd:TIGR00458 76 -----IKEKAPGGFEIIPTKIEVINEAKEPLPLDPTE--KVPAE----------LDTRLDYRFLDLRRPTVQAIFRIRSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 254 VCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQQLIVADFERVYEIGPVFRAENSNTHR 333
Cdd:TIGR00458 139 VLESVREFLAEEGFIEVHTPKLVASATEGGTELFPITYFEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 334 HMTEFTGLDMEMAFEEHyHEVLDTLSELFVFIFSELPKRFAHeielvrkQYPVEEFKLPK-DGKMVRLTYKEGIEMLRAA 412
Cdd:TIGR00458 219 HLNEATSIDIEMAFEDH-HDVMDILEELVVRVFEDVPERCAH-------QLETLEFKLEKpEGKFVRLTYDEAIEMANAK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 413 GKEIGDFEDLSTENEKFLGklvrDKYDTDFYILDkFPLEIRPFYTMPDPANPKYSNSYDFFMRGEEILSGAQRIHDHALL 492
Cdd:TIGR00458 291 GVEIGWGEDLSTEAEKALG----EEMDGLYFITD-WPTEIRPFYTMPDEDNPEISKSFDLMYRDLEISSGAQRIHLHDLL 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323011 493 QERMKAHGLSPEdpGLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDPKRLRP 557
Cdd:TIGR00458 366 VERIKAKGLNPE--GFKDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRKRLTP 428
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
226-553 |
3.67e-171 |
|
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs in the core domain. This family includes AsnRS as well as a subgroup of AspRS. AsnRS and AspRS are homodimers, which attach either asparagine or aspartate to the 3'OH group of ribose of the appropriate tRNA. While archaea lack asnRS, they possess a non-discriminating aspRS, which can mischarge Asp-tRNA with Asn. Subsequently, a tRNA-dependent aspartate amidotransferase converts the bound aspartate to asparagine. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.
Pssm-ID: 238399 [Multi-domain] Cd Length: 322 Bit Score: 487.07 E-value: 3.67e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 226 VNLDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFN 305
Cdd:cd00776 2 ANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 306 KQQLIVAdFERVYEIGPVFRAENSNTHRHMTEFTGLDMEMAFEEHYHEVLDTLSELFVFIFSELPKRFAHEIELVrKQYP 385
Cdd:cd00776 82 KEMLIAA-LERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRVLERCAKELELV-NQLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 386 VEEFKLPKdgKMVRLTYKEGIEMLRAAGK--EIGDFEDLSTENEKFLGKLVRdkydTDFYILDKFPLEIRPFYTMPDPAN 463
Cdd:cd00776 160 RELLKPLE--PFPRITYDEAIELLREKGVeeEVKWGEDLSTEHERLLGEIVK----GDPVFVTDYPKEIKPFYMKPDDDN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 464 PKYSNSYDFFMRG-EEILSGAQRIHDHALLQERMKAHGLSPEDpgLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNI 542
Cdd:cd00776 234 PETVESFDLLMPGvGEIVGGSQRIHDYDELEERIKEHGLDPES--FEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNI 311
|
330
....*....|.
gi 6323011 543 RRASLFPRDPK 553
Cdd:cd00776 312 REAILFPRDPK 322
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
30-557 |
2.61e-170 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 493.74 E-value: 2.61e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 30 SKKALKKLQKEQEKQRKKEERALQLEAEREAR-EKKAAAEDTAKDNYGKLPLIQSrdSDRTGQKRVKFVDLDEAKDSDKE 108
Cdd:PTZ00401 3 SNHADAGAPAVEKKQSDKEARKAARLAEEKARaAEKAALVEKYKDVFGAAPMVQS--TTYKSRTFIPVAVLSKPELVDKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 109 VLFRARVHNTRQQGaTLAFLTLRQQASLIQGLVKAnkEGTISKNMVKWAGSLNLESIVLVRGIVKKVDEPIKSATVQNLE 188
Cdd:PTZ00401 81 VLIRARVSTTRKKG-KMAFMVLRDGSDSVQAMAAV--EGDVPKEMIDFIGQIPTESIVDVEATVCKVEQPITSTSHSDIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 189 IHITKIYTISETPEALPILLEDASRSEAEAEAAglpvVNLDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREYLATKKFT 268
Cdd:PTZ00401 158 LKVKKIHTVTESLRTLPFTLEDASRKESDEGAK----VNFDTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDSDFC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 269 EVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQQLIVADFERVYEIGPVFRAENSNTHRHMTEFTGLDMEMAFE 348
Cdd:PTZ00401 234 EIHSPKIINAPSEGGANVFKLEYFNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHLTEFVGLDVEMRIN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 349 EHYHEVLDTLSELFVFIFSELPKRFAhEIELVRKQYP--------------------VEEFKLPKD----------GKMV 398
Cdd:PTZ00401 314 EHYYEVLDLAESLFNYIFERLATHTK-ELKAVCQQYPfeplvwkltpermkelgvgvISEGVEPTDkyqarvhnmdSRML 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 399 RLTYKEGIEMLRAAGKE-IGDFEDLSTENEKFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPDPANPKYSNSYDFFMRGE 477
Cdd:PTZ00401 393 RINYMHCIELLNTVLEEkMAPTDDINTTNEKLLGKLVKERYGTDFFISDRFPSSARPFYTMECKDDERFTNSYDMFIRGE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 478 EILSGAQRIHDHALLQERMKAHG--LSPedpgLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDPKRL 555
Cdd:PTZ00401 473 EISSGAQRIHDPDLLLARAKMLNvdLTP----IKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPRDPQRT 548
|
..
gi 6323011 556 RP 557
Cdd:PTZ00401 549 TP 550
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
92-557 |
5.63e-151 |
|
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl/asparaginyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439788 [Multi-domain] Cd Length: 430 Bit Score: 439.87 E-value: 5.63e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 92 KRVKFVDLDEAKDsDKEVLFRARVHNTRQQGAtLAFLTLRQQASLIQGLVKANKEGTISKnmvkwAGSLNLESIVLVRGI 171
Cdd:COG0017 1 KRTYIKDLLPEHV-GQEVTVAGWVRTKRDSGG-ISFLILRDGSGFIQVVVKKDKLENFEE-----AKKLTTESSVEVTGT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 172 VKKvdEPIKSatvQNLEIHITKIYTISETPEALPILLEDASrseaeaeaaglpvvnLDTRLDYRVIDLRTVTNQAIFRIQ 251
Cdd:COG0017 74 VVE--SPRAP---QGVELQAEEIEVLGEADEPYPLQPKRHS---------------LEFLLDNRHLRLRTNRFGAIFRIR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 252 AGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQQLIVAdFERVYEIGPVFRAENSNT 331
Cdd:COG0017 134 SELARAIREFFQERGFVEVHTPIITASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMA-LEKVYTFGPTFRAEKSNT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 332 HRHMTEFTGLDMEMAFEEHyHEVLDTLSELFVFIFSELPKRFAHEIELvrkqYPVEEFKLPK--DGKMVRLTYKEGIEML 409
Cdd:COG0017 213 RRHLAEFWMIEPEMAFADL-EDVMDLAEEMLKYIIKYVLENCPEELEF----LGRDVERLEKvpESPFPRITYTEAIEIL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 410 RAAGKEIGDFEDLSTENEKFLGklvrDKYDTDFYILDKFPLEIRPFYTMPDPANPKYSNSYDFFMRG-EEILSGAQRIHD 488
Cdd:COG0017 288 KKSGEKVEWGDDLGTEHERYLG----EEFFKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGiGEIIGGSQREHR 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323011 489 HALLQERMKAHGLSPEDpgLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDPKRLRP 557
Cdd:COG0017 364 YDVLVERIKEKGLDPED--YEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
91-557 |
7.90e-151 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 439.63 E-value: 7.90e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 91 QKRVKFVDLDEAKDSdKEVLFRARVHNTRQQGAtLAFLTLRQQASLIQGLVKANKegtiSKNMVKWAGSLNLESIVLVRG 170
Cdd:PRK05159 2 MKRHLTSELTPELDG-EEVTLAGWVHEIRDLGG-IAFLILRDRSGIIQVVVKKKV----DEELFETIKKLKRESVVSVTG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 171 IVKKVDepiKSATvqNLEIHITKIYTISETPEALPilLEDASRSEAEaeaaglpvvnLDTRLDYRVIDLRTVTNQAIFRI 250
Cdd:PRK05159 76 TVKANP---KAPG--GVEVIPEEIEVLNKAEEPLP--LDISGKVLAE----------LDTRLDNRFLDLRRPRVRAIFKI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 251 QAGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQQLIVADFERVYEIGPVFRAENSN 330
Cdd:PRK05159 139 RSEVLRAFREFLYENGFTEIFTPKIVASGTEGGAELFPIDYFEKEAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHN 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 331 THRHMTEFTGLDMEMAFEEHYHEVLDTLSELFVFIFSELPKRFAHEIELVRKQYPVEEFKLPkdgkmvRLTYKEGIEMLR 410
Cdd:PRK05159 219 TSRHLNEYTSIDVEMGFIDDHEDVMDLLENLLRYMYEDVAENCEKELELLGIELPVPETPIP------RITYDEAIEILK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 411 AAGKEIGDFEDLSTENEKFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPDPANPKYSNSYDFFMRGEEILSGAQRIHDHA 490
Cdd:PRK05159 293 SKGNEISWGDDLDTEGERLLGEYVKEEYGSDFYFITDYPSEKRPFYTMPDEDDPEISKSFDLLFRGLEITSGGQRIHRYD 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323011 491 LLQERMKAHGLSPEDpgLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDPKRLRP 557
Cdd:PRK05159 373 MLVESIKEKGLNPES--FEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPRDRHRLTP 437
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
227-552 |
1.79e-97 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 298.71 E-value: 1.79e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 227 NLDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEV------TYFkgkaYLAQ 300
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVpsralgKFY----ALPQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 301 SPQFNKQQLIVADFERVYEIGPVFRAENSNTHRHMtEFTGLDMEMAFEEhYHEVLDTLSELFVFIFSELpkrfaHEIELV 380
Cdd:pfam00152 77 SPQLYKQLLMVAGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVD-YEDVMDLTEELIKEIFKEV-----EGIAKE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 381 RKQYPVEEFKLPkdgkMVRLTYKEGIEMLRAAGKEIGDFeDLSTENEKFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPD 460
Cdd:pfam00152 150 LEGGTLLDLKKP----FPRITYAEAIEKLNGKDVEELGY-GSDKPDLRFLLELVIDKNKFNPLWVTDFPAEHHPFTMPKD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 461 PANPKYSNSYDFFMRGEEILSGAQRIHDHALLQERMKAHGLSPEDPGLKD--YCDGFSYGCPPHAGGGIGLERVVMFYLD 538
Cdd:pfam00152 225 EDDPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPEEAEEKFgfYLDALKYGAPPHGGLGIGLDRLVMLLTG 304
|
330
....*....|....
gi 6323011 539 LKNIRRASLFPRDP 552
Cdd:pfam00152 305 LESIREVIAFPKTR 318
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
92-557 |
2.23e-75 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 245.79 E-value: 2.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 92 KRVKFVDLDEAKDSDKEVLFRARVHNTRQQGAtLAFLTLRQQASLIQGLVKANKEGTISKNmvkwAGSLNLESIVLVRGI 171
Cdd:PRK03932 2 MRVSIKDILKGKYVGQEVTVRGWVRTKRDSGK-IAFLQLRDGSCFKQLQVVKDNGEEYFEE----IKKLTTGSSVIVTGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 172 VKKvdEPIKSatvQNLEIHITKIYTISETPEALPILLEDASrseaeaeaaglpvvnLDTRLDYRVIDLRTVTNQAIFRIQ 251
Cdd:PRK03932 77 VVE--SPRAG---QGYELQATKIEVIGEDPEDYPIQKKRHS---------------IEFLREIAHLRPRTNKFGAVMRIR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 252 AGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVT---------YFKGKAYLAQSPQFNKQQLIVAdFERVYEIGP 322
Cdd:PRK03932 137 NTLAQAIHEFFNENGFVWVDTPIITASDCEGAGELFRVTtldldfskdFFGKEAYLTVSGQLYAEAYAMA-LGKVYTFGP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 323 VFRAENSNTHRHMTEFTGLDMEMAFEEHYhEVLDtLSELFV-FIFSELPKRFAHEIELVRKQYP---VEEFKLPKDGKMV 398
Cdd:PRK03932 216 TFRAENSNTRRHLAEFWMIEPEMAFADLE-DNMD-LAEEMLkYVVKYVLENCPDDLEFLNRRVDkgdIERLENFIESPFP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 399 RLTYKEGIEMLRAAGKeigDFE-------DLSTENEKFLGKLVrdkYDTDFYILDkFPLEIRPFYTMPDPAN-------- 463
Cdd:PRK03932 294 RITYTEAIEILQKSGK---KFEfpvewgdDLGSEHERYLAEEH---FKKPVFVTN-YPKDIKAFYMRLNPDGktvaamdl 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 464 --PKYsnsydffmrGeEILSGAQRIHDHALLQERMKAHGLSPEDpgLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKN 541
Cdd:PRK03932 367 laPGI---------G-EIIGGSQREERLDVLEARIKELGLNKED--YWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDN 434
|
490
....*....|....*.
gi 6323011 542 IRRASLFPRDPKRLRP 557
Cdd:PRK03932 435 IRDVIPFPRTPGRAEF 450
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
93-557 |
1.99e-66 |
|
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, asnS, represents asparaginyl-tRNA synthetases from the three domains of life. Some species lack this enzyme and charge tRNA(asn) by misacylation with Asp, followed by transamidation of Asp to Asn. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273086 [Multi-domain] Cd Length: 453 Bit Score: 222.64 E-value: 1.99e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 93 RVKFVDLDEAKDSDKEVLFRARVHNTRQQgATLAFLTLRQQASL--IQGLVKankeGTISKNMVKWAGSLNLESIVLVRG 170
Cdd:TIGR00457 3 AIKDLLQQVYKFVGDEVTVSGWVRTKRSS-KKIIFLELNDGSSLgpIQAVIN----GEDNPYLFQLLKSLTTGSSVSVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 171 IVKKvdEPIKSatvQNLEIHITKIYTISE-TPEALPILLEDASrseaeaeaaglpvvnLDTRLDYRVIDLRTVTNQAIFR 249
Cdd:TIGR00457 78 KVVE--SPGKG---QPVELQVKKIEVVGEaEPDDYPLQKKEHS---------------LEFLRDIAHLRLRTNTLGAVMR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 250 IQAGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVT---------YFKGKAYLAQSPQFNKQQLIVAdFERVYEI 320
Cdd:TIGR00457 138 VRNALSQAIHRYFQENGFTWVSPPILTSNDCEGAGELFRVStgnidfsqdFFGKEAYLTVSGQLYLETYALA-LSKVYTF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 321 GPVFRAENSNTHRHMTEFTGLDMEMAFEEhYHEVLDTLSELFVFIFSELPKRFAHEIELVRKQYPVEEF-KLPKD--GKM 397
Cdd:TIGR00457 217 GPTFRAEKSNTSRHLSEFWMIEPEMAFAN-LNDLLQLAETLIKYIIKAVLENCSQELKFLEKNFDKDLIkRLENIinNKF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 398 VRLTYKEGIEMLRAAGK--EIGDF--EDLSTENEKFLGklvrDKYDTDFYILDKFPLEIRPFYtMPDPANPKYSNSYDFF 473
Cdd:TIGR00457 296 ARITYTDAIEILKESDKnfEYEDFwgDDLQTEHERFLA----EEYFKPPVFVTNYPKDIKAFY-MKLNDDGKTVAAMDLL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 474 MRG-EEILSGAQRIHDHALLQERMKAHGLSPEDpgLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDP 552
Cdd:TIGR00457 371 APGiGEIIGGSEREDDLDKLENRMKEMGLDTDA--LNWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTP 448
|
....*
gi 6323011 553 KRLRP 557
Cdd:TIGR00457 449 GNINF 453
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
248-551 |
3.97e-60 |
|
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of class II aminoacyl-tRNA synthetases of the subgroup containing aspartyl, lysyl, and asparaginyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. Nearly all class II tRNA synthetases are dimers and enzymes in this subgroup are homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238358 [Multi-domain] Cd Length: 269 Bit Score: 200.01 E-value: 3.97e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 248 FRIQAGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVTYF-KGK-AYLAQSPQFNKQQLIVADFERVYEIGPVFR 325
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNaLGLdYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 326 AEnSNTHRHMTEFTGLDMEMAFEEhYHEVLDTLSELFVFIFSELPKRFAHEIELVrkqypVEEFKLPkdgkMVRLTYKEG 405
Cdd:cd00669 81 NE-DLRARHQPEFTMMDLEMAFAD-YEDVIELTERLVRHLAREVLGVTAVTYGFE-----LEDFGLP----FPRLTYREA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 406 IEMLRAagkeigdfedlstenekflgklvrdkydtdFYILDKFPLEIRPFYTMPDPANPKYSNSYDFFMRGEEILSGAQR 485
Cdd:cd00669 150 LERYGQ------------------------------PLFLTDYPAEMHSPLASPHDVNPEIADAFDLFINGVEVGNGSSR 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323011 486 IHDHALLQERMKAHGLSPEDPGLK--DYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRD 551
Cdd:cd00669 200 LHDPDIQAEVFQEQGINKEAGMEYfeFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKM 267
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
108-210 |
3.38e-48 |
|
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae and human cytoplasmic aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis.
Pssm-ID: 239815 [Multi-domain] Cd Length: 102 Bit Score: 162.73 E-value: 3.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 108 EVLFRARVHNTRQQGATLAFLTLRQQASLIQGLVKANKEGtISKNMVKWAGSLNLESIVLVRGIVKKVDEPIKSATVQNL 187
Cdd:cd04320 1 EVLIRARVHTSRAQGAKLAFLVLRQQGYTIQGVLAASAEG-VSKQMVKWAGSLSKESIVDVEGTVKKPEEPIKSCTQQDV 79
|
90 100
....*....|....*....|...
gi 6323011 188 EIHITKIYTISETPEALPILLED 210
Cdd:cd04320 80 ELHIEKIYVVSEAAEPLPFQLED 102
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
247-552 |
5.22e-47 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 167.50 E-value: 5.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 247 IFRIQAGVCELFREYLATKKFTEVHTP-------KLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQqLIVADFERVYE 319
Cdd:PRK06462 29 VLKVQSSILRYTREFLDGRGFVEVLPPiispstdPLMGLGSDLPVKQISIDFYGVEYYLADSMILHKQ-LALRMLGKIFY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 320 IGPVFRAEN--SNTHRHMTEFTGLDMEMAfEEHYHEVLDTLSELFVFIFSELPKRFAHEIELVRKQYPveEFKLPKDgkm 397
Cdd:PRK06462 108 LSPNFRLEPvdKDTGRHLYEFTQLDIEIE-GADLDEVMDLIEDLIKYLVKELLEEHEDELEFFGRDLP--HLKRPFK--- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 398 vRLTYKEGIEMLRAAGKEIGDFEDLSTENEKFLGKlvrdKYDTDFYILDkFPLEIRPFYTMPDPANPKYSNSYDFFMRG- 476
Cdd:PRK06462 182 -RITHKEAVEILNEEGCRGIDLEELGSEGEKSLSE----HFEEPFWIID-IPKGSREFYDREDPERPGVLRNYDLLLPEg 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323011 477 -EEILSGAQRIHDHALLQERMKAHGLSPEDpgLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDP 552
Cdd:PRK06462 256 yGEAVSGGEREYEYEEIVERIREHGVDPEK--YKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFPRVP 330
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
257-549 |
5.50e-34 |
|
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. AspRS is a homodimer, which attaches a specific amino acid to the 3' OH group of ribose of the appropriate tRNA. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. AspRS in this family differ from those found in the AsxRS family by a GAD insert in the core domain.
Pssm-ID: 238400 [Multi-domain] Cd Length: 280 Bit Score: 130.00 E-value: 5.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 257 LFREYLATKKFTEVHTPkLLGAPSEGGSSVFEVTY--FKGKAY-LAQSPQFNKQQLIVADFERVYEIGPVFRAENSNTHR 333
Cdd:cd00777 10 AIRNFLDEQGFVEIETP-ILTKSTPEGARDFLVPSrlHPGKFYaLPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 334 HmTEFTGLDMEMAFEEHyHEVLDTLSELFVFIFSELpkrFAHEIELvrkqypveefKLPkdgkmvRLTYKEGIEMLRAAG 413
Cdd:cd00777 89 Q-PEFTQIDIEMSFVDQ-EDIMSLIEGLLKYVFKEV---LGVELTT----------PFP------RMTYAEAMERYGFKF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 414 KEIGDFEDLSTENEKflGKLV---------RDKYDTDfyiLDKFPLEIRpfytmpdpanpkySNSYDFFMRGEEILSGAQ 484
Cdd:cd00777 148 LWIVDFPLFEWDEEE--GRLVsahhpftapKEEDLDL---LEKDPEDAR-------------AQAYDLVLNGVELGGGSI 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323011 485 RIHDhALLQERM-KAHGLSPEDPGLKDYC--DGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFP 549
Cdd:cd00777 210 RIHD-PDIQEKVfEILGLSEEEAEEKFGFllEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVIAFP 276
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
115-549 |
1.22e-32 |
|
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439943 [Multi-domain] Cd Length: 589 Bit Score: 132.04 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 115 VHNTRQQGAtLAFLTLRQQASLIQglVKANKEgtISKNMVKWAGSLNLESIVLVRGIVKKVDE----P-IKSATVqnlEI 189
Cdd:COG0173 25 VHRRRDHGG-LIFIDLRDRYGITQ--VVFDPD--DSAEAFEKAEKLRSEYVIAVTGKVRARPEgtvnPkLPTGEI---EV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 190 HITKIYTISETpEALPILLEDASRseaeaeaaglpvVNLDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREYLATKKFTE 269
Cdd:COG0173 97 LASELEILNKA-KTPPFQIDDDTD------------VSEELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDENGFLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 270 VHTPkLLGAPS-EGG------SSVfevtyFKGKAY-LAQSPQFNKQQLIVADFERVYEIGPVFRAENSNTHRHMtEFTGL 341
Cdd:COG0173 164 IETP-ILTKSTpEGArdylvpSRV-----HPGKFYaLPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADRQP-EFTQL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 342 DMEMAF--EEhyhEVLDTLSELFVFIFSE-----LPK---------------------RFAHEI----ELVRKqypvEEF 389
Cdd:COG0173 237 DIEMSFvdQE---DVFELMEGLIRHLFKEvlgveLPTpfprmtyaeamerygsdkpdlRFGLELvdvtDIFKD----SGF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 390 KL----PKDGKMVR-LTYKEGIEMLRaagKEIGDFEDLS-------------TENE------KFLGKLVR---------- 435
Cdd:COG0173 310 KVfagaAENGGRVKaINVPGGASLSR---KQIDELTEFAkqygakglayikvNEDGlkspiaKFLSEEELaailerlgak 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 436 ---------DKYDT--------------DFYILDK----------FPL------EIR------PFyTMPDP-------AN 463
Cdd:COG0173 387 pgdliffvaDKPKVvnkalgalrlklgkELGLIDEdefaflwvvdFPLfeydeeEGRwvamhhPF-TMPKDedldlleTD 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 464 PK--YSNSYDFFMRGEEILSGAQRIHDHAlLQERM-KAHGLSPED-----PGLkdyCDGFSYGCPPHAGGGIGLERVVMF 535
Cdd:COG0173 466 PGkvRAKAYDLVLNGYELGGGSIRIHDPE-LQEKVfELLGISEEEaeekfGFL---LEAFKYGAPPHGGIAFGLDRLVML 541
|
570
....*....|....
gi 6323011 536 YLDLKNIRRASLFP 549
Cdd:COG0173 542 LAGEDSIRDVIAFP 555
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
115-549 |
1.43e-32 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 131.73 E-value: 1.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 115 VHNTRQQGAtLAFLTLRQQASLIQGLVKANKEgtisknMVKWAGSLNLESIVLVRGIVKKVDEP-----IKSATVqnlEI 189
Cdd:PRK00476 26 VHRRRDHGG-LIFIDLRDREGIVQVVFDPDAE------AFEVAESLRSEYVIQVTGTVRARPEGtvnpnLPTGEI---EV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 190 HITKIYTISEtPEALPILLEDAsrseaeaeaaglPVVNLDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREYLATKKFTE 269
Cdd:PRK00476 96 LASELEVLNK-SKTLPFPIDDE------------EDVSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDNGFLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 270 VHTPkLLGAPS-EGG------SSVfevtyFKGKAY-LAQSPQFNKQQLIVADFERVYEIGPVFRAENSNTHRHMtEFTGL 341
Cdd:PRK00476 163 IETP-ILTKSTpEGArdylvpSRV-----HPGKFYaLPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQP-EFTQI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 342 DMEMAF--EEhyhEVLDTLSELFVFIFSE-----LPK---------------------RFAHEI----ELVRKqypvEEF 389
Cdd:PRK00476 236 DIEMSFvtQE---DVMALMEGLIRHVFKEvlgvdLPTpfprmtyaeamrrygsdkpdlRFGLELvdvtDLFKD----SGF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 390 KL----PKDGKMVRltykeGIEMLRAAG----KEIGDFEDLSTENE-------------------KFLGK---------- 432
Cdd:PRK00476 309 KVfagaANDGGRVK-----AIRVPGGAAqlsrKQIDELTEFAKIYGakglayikvnedglkgpiaKFLSEeelaallert 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 433 ---------LVRDKYDT--------------DFYILDK----------FPL------EIR------PFyTMPDP------ 461
Cdd:PRK00476 384 gakdgdlifFGADKAKVvndalgalrlklgkELGLIDEdkfaflwvvdFPMfeydeeEGRwvaahhPF-TMPKDedldel 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 462 --ANPK--YSNSYDFFMRGEEILSGAQRIHDHAlLQERM-KAHGLSPEDP-----GLkdyCDGFSYGCPPHAGGGIGLER 531
Cdd:PRK00476 463 etTDPGkaRAYAYDLVLNGYELGGGSIRIHRPE-IQEKVfEILGISEEEAeekfgFL---LDALKYGAPPHGGIAFGLDR 538
|
570
....*....|....*...
gi 6323011 532 VVMFYLDLKNIRRASLFP 549
Cdd:PRK00476 539 LVMLLAGADSIRDVIAFP 556
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
47-552 |
1.27e-30 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 125.86 E-value: 1.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 47 KEERALQLEAEREAREKKAAAEDTAKDNYG-KLPLIQSRDSDRTGQ--KRVKFVDLDEAKDSD-----KEVLFRARVHNT 118
Cdd:PLN02603 40 TFHHLAALSGLPRRRRFCAAASASLQSPESaKVEAAKGAFGEAVGEfrKKLRIADVKGGEDEGlarvgKTLNVMGWVRTL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 119 RQQgATLAFLTLRQQASL--IQGLVKANKEGTiskNMVKwAGSLNLESIVLVRGIVKKvdepiKSATVQNLEIHITKIYT 196
Cdd:PLN02603 120 RAQ-SSVTFIEVNDGSCLsnMQCVMTPDAEGY---DQVE-SGLITTGASVLVQGTVVS-----SQGGKQKVELKVSKIVV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 197 ISETPEALPILLEDASRSEAEAEAAGLPvvnldtrldyrvidlRTVTNQAIFRIQAGVCELFREYLATKKFTEVHTPKLL 276
Cdd:PLN02603 190 VGKSDPSYPIQKKRVSREFLRTKAHLRP---------------RTNTFGAVARVRNALAYATHKFFQENGFVWVSSPIIT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 277 GAPSEGGSSVFEVT------------------------------YFKGKAYLAQSPQFNKQQLIVAdFERVYEIGPVFRA 326
Cdd:PLN02603 255 ASDCEGAGEQFCVTtlipnsaenggslvddipktkdglidwsqdFFGKPAFLTVSGQLNGETYATA-LSDVYTFGPTFRA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 327 ENSNTHRHMTEFTGLDMEMAFEEHYHE--------------VLDTLSELFVFIFSELPKRFAHEI-ELVRKQYpveefkl 391
Cdd:PLN02603 334 ENSNTSRHLAEFWMIEPELAFADLNDDmacataylqyvvkyILENCKEDMEFFNTWIEKGIIDRLsDVVEKNF------- 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 392 pkdgkmVRLTYKEGIEMLRAAGKEigdFE-------DLSTENEKFLGKLVrdkYDTDFYILDKFPLEIRPFYtMPDPANP 464
Cdd:PLN02603 407 ------VQLSYTDAIELLLKAKKK---FEfpvkwglDLQSEHERYITEEA---FGGRPVIIRDYPKEIKAFY-MRENDDG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 465 KYSNSYDFFM-RGEEILSGAQRIHDHALLQERMKAHGLSPEDPGLkdYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIR 543
Cdd:PLN02603 474 KTVAAMDMLVpRVGELIGGSQREERLEYLEARLDELKLNKESYWW--YLDLRRYGSVPHAGFGLGFERLVQFATGIDNIR 551
|
....*....
gi 6323011 544 RASLFPRDP 552
Cdd:PLN02603 552 DAIPFPRVP 560
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
104-551 |
9.27e-29 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 121.25 E-value: 9.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 104 DSDKEVLFRARVHNTRQQGATLaFLTLRQQASLIQGLVkaNKEGTiSKNMVKWAGSLNLESIVLVRGIVKKVDEPIKSAT 183
Cdd:PRK12820 16 DTGREVCLAGWVDAFRDHGELL-FIHLRDRNGFIQAVF--SPEAA-PADVYELAASLRAEFCVALQGEVQKRLEETENPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 184 VQ--NLEIHITKIYTISETpEALPILLEDASRSeAEAEAAGLPVVNLDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREY 261
Cdd:PRK12820 92 IEtgDIEVFVRELSILAAS-EALPFAISDKAMT-AGAGSAGADAVNEDLRLQYRYLDIRRPAMQDHLAKRHRIIKCARDF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 262 LATKKFTEVHTPKLLGAPSEGGSSVFEVTYFKGKAY--LAQSPQFNKQQLIVADFERVYEIGPVFRAENSNTHRHmTEFT 339
Cdd:PRK12820 170 LDSRGFLEIETPILTKSTPEGARDYLVPSRIHPKEFyaLPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQ-PEFT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 340 GLDMEMAF--EEHYHEVLDtlsELFVFIFS----ELPKRF-----AHEIE---------------------LVRKQYPVE 387
Cdd:PRK12820 249 QLDIEASFidEEFIFELIE---ELTARMFAiggiALPRPFprmpyAEAMDttgsdrpdlrfdlkfadatdiFENTRYGIF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 388 EFKLPKDGKMVRLTYK-------------------------EGIEMLRA-AGKEIGDFEDLSTENEKFLGKLVRDKYDTD 441
Cdd:PRK12820 326 KQILQRGGRIKGINIKgqseklsknvlqneyakeiapsfgaKGMTWMRAeAGGLDSNIVQFFSADEKEALKRRFHAEDGD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 442 FYIL---------------------DK---------FPLEIRPF-----------------YTMP-----DPANPK---- 465
Cdd:PRK12820 406 VIIMiadascaivlsalgqlrlhlaDRlglipegvfHPLWITDFplfeatddggvtsshhpFTAPdredfDPGDIEelld 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 466 -YSNSYDFFMRGEEILSGAQRIHDHALLQERMKAHGLSPEDpgLKD----YCDGFSYGCPPHAGGGIGLERVVMFYLDLK 540
Cdd:PRK12820 486 lRSRAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEED--IEDkfgfFLRAFDFAAPPHGGIALGLDRVVSMILQTP 563
|
570
....*....|.
gi 6323011 541 NIRRASLFPRD 551
Cdd:PRK12820 564 SIREVIAFPKN 574
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
197-554 |
3.67e-27 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 115.48 E-value: 3.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 197 ISETPEALPILLEDASRSEAEAEAAGLPVVNLDtrldyRVIDLRTVTNQAIFRIQAGVCELfreYLATKKFTEVHTPKLL 276
Cdd:PLN02221 216 INYTERLEQDLIDNPPPTEADVEAARLIVKERG-----EVVAQLKAAKASKEEITAAVAEL---KIAKESLAHIEERSKL 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 277 --GAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQQLIVAdFERVYEIGPVFRAENSNTHRHMTEFTGLDMEMAFEEhYHEV 354
Cdd:PLN02221 288 kpGLPKKDGKIDYSKDFFGRQAFLTVSGQLQVETYACA-LSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFAD-LEDD 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 355 LDTLSELFVFIFSELPKRFAHEIELVRKQYP---VEEFKLPKDGKMVRLTYKEGIEMLRAAGKEIGDFE-------DLST 424
Cdd:PLN02221 366 MNCAEAYVKYMCKWLLDKCFDDMELMAKNFDsgcIDRLRMVASTPFGRITYTEAIELLEEAVAKGKEFDnnvewgiDLAS 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 425 ENEKFLGKLVRDKYdtdfYILDKFPLEIRPFYtMPDPANPKYSNSYDFFM-RGEEILSGAQRIHDHALLQERMKAHGLsP 503
Cdd:PLN02221 446 EHERYLTEVLFQKP----LIVYNYPKGIKAFY-MRLNDDEKTVAAMDVLVpKVGELIGGSQREERYDVIKQRIEEMGL-P 519
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 6323011 504 EDPgLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDPKR 554
Cdd:PLN02221 520 IEP-YEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRYPGK 569
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
103-550 |
5.82e-27 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 115.27 E-value: 5.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 103 KDSDKEVLFRARVHNTRQQGAtLAFLTLRQQAsliqGLVKANKEGTISKNMVKWAGSLNLESIVLVRGIVKK--VDEPIK 180
Cdd:PLN02903 69 NDVGSRVTLCGWVDLHRDMGG-LTFLDVRDHT----GIVQVVTLPDEFPEAHRTANRLRNEYVVAVEGTVRSrpQESPNK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 181 SATVQNLEIHITKIYTISETPEALPILLEDASRSEaeaeaaglPVVNLDTRLDYRVIDLRTVTNQAIFRIQAGVCELFRE 260
Cdd:PLN02903 144 KMKTGSVEVVAESVDILNVVTKSLPFLVTTADEQK--------DSIKEEVRLRYRVLDLRRPQMNANLRLRHRVVKLIRR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 261 YLA-TKKFTEVHTPKLLGAPSEGGSSVFEVTYFK-GKAY-LAQSPQFNKQQLIVADFERVYEIGPVFRAENSNTHRHmTE 337
Cdd:PLN02903 216 YLEdVHGFVEIETPILSRSTPEGARDYLVPSRVQpGTFYaLPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQ-PE 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 338 FTGLDMEMAFEEhYHEVLDTLSELFVFIFSE-----LPK---------------------RFAHEIELVRKQYPVEEFKL 391
Cdd:PLN02903 295 FTQLDMELAFTP-LEDMLKLNEDLIRQVFKEikgvqLPNpfprltyaeamskygsdkpdlRYGLELVDVSDVFAESSFKV 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 392 ----------------PKDGKMVRLTYK----------------------------EGI-------------EMLRAAGK 414
Cdd:PLN02903 374 fagalesggvvkaicvPDGKKISNNTALkkgdiyneaiksgakglaflkvlddgelEGIkalveslspeqaeQLLAACGA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 415 EIGDFEDLSTENEKFLGK-------LVRDKYD------------TDFYILDKFPLEIR------PFyTMPDPANPK-YSN 468
Cdd:PLN02903 454 GPGDLILFAAGPTSSVNKtldrlrqFIAKTLDlidpsrhsilwvTDFPMFEWNEDEQRlealhhPF-TAPNPEDMGdLSS 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 469 ----SYDFFMRGEEILSGAQRIHDHALLQERMKAHGLSPEDPGLK-DYC-DGFSYGCPPHAGGGIGLERVVMFYLDLKNI 542
Cdd:PLN02903 533 aralAYDMVYNGVEIGGGSLRIYRRDVQQKVLEAIGLSPEEAESKfGYLlEALDMGAPPHGGIAYGLDRLVMLLAGAKSI 612
|
....*...
gi 6323011 543 RRASLFPR 550
Cdd:PLN02903 613 RDVIAFPK 620
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
42-549 |
8.89e-27 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 114.00 E-value: 8.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 42 EKQRKKEERALQLEAEREAREKKAAAedtAKDNYGKLPLIQSRDSDrTGQKRVKF--VDLDEAKDSDKEVLFRARVHNTR 119
Cdd:PRK12445 3 EQETRGANEAIDFNDELRNRREKLAA---LRQQGVAFPNDFRRDHT-SDQLHEEFdaKDNQELESLNIEVSVAGRMMTRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 120 QQGATlAFLTLRQQASLIQGLVKANK--EGTISKNMVKWagslNLESIVLVRGIVKKVDepiksatVQNLEIHITKIYTI 197
Cdd:PRK12445 79 IMGKA-SFVTLQDVGGRIQLYVARDSlpEGVYNDQFKKW----DLGDIIGARGTLFKTQ-------TGELSIHCTELRLL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 198 SETPEALPILLEDASRSEaeaeaaglpvvnldTRLDYRVIDL-RTVTNQAIFRIQAGVCELFREYLATKKFTEVHTPKLL 276
Cdd:PRK12445 147 TKALRPLPDKFHGLQDQE--------------VRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQ 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 277 GAPSEGGSSVFeVTYFKG---KAYLAQSPQFNKQQLIVADFERVYEIGPVFRAENSNThRHMTEFTGLDMEMAFEEhYHE 353
Cdd:PRK12445 213 VIPGGASARPF-ITHHNAldlDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISV-RHNPEFTMMELYMAYAD-YHD 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 354 VLDTLSELFvfifselpKRFAHEIeLVRKQYPVEEFKLPKDGKMVRLTYKEGIEMLRA-----------AGKEIGDFEDL 422
Cdd:PRK12445 290 LIELTESLF--------RTLAQEV-LGTTKVTYGEHVFDFGKPFEKLTMREAIKKYRPetdmadldnfdAAKALAESIGI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 423 STENEKFLGKLVRDKYD-------TDFYILDKFPLEIRPFYTMPDpANPKYSNSYDFFMRGEEILSGAQRIHDH----AL 491
Cdd:PRK12445 361 TVEKSWGLGRIVTEIFDevaeahlIQPTFITEYPAEVSPLARRND-VNPEITDRFEFFIGGREIGNGFSELNDAedqaER 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 492 LQERMKAHGLSPEDPGL--KDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFP 549
Cdd:PRK12445 440 FQEQVNAKAAGDDEAMFydEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
22-549 |
2.59e-25 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 109.70 E-value: 2.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 22 LGEDGKPLSKKALKKLQK----EQEKQRKKEERALQLEAEREAREKKAAAEDTA-------KDNygKLPLIQSRDS---- 86
Cdd:PLN02502 1 AESNGEPLSKNALKKRLKakqaEEEKAAKEEAKAAAAAAAAKGRSRKSAAADDEtmdptqyRAN--RLKKVEALRAkgve 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 87 ------DRT---GQKRVKFVDL-DEAKDSDKEVLFRARVHNTRQQGaTLAFLTLRQQASLIQGLVKANKEGTISKNMVKW 156
Cdd:PLN02502 79 pypykfDVThtaPELQEKYGSLeNGEELEDVSVSVAGRIMAKRAFG-KLAFYDLRDDGGKIQLYADKKRLDLDEEEFEKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 157 AGSLNLESIVLVRGIVKKVDEPIKSATVQNLEIHitkiytiseTPEALPilLEDAsrseaeaeAAGLPvvNLDTRLDYRV 236
Cdd:PLN02502 158 HSLVDRGDIVGVTGTPGKTKKGELSIFPTSFEVL---------TKCLLM--LPDK--------YHGLT--DQETRYRQRY 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 237 IDL---RTVTNqaIFRIQAGVCELFREYLATKKFTEVHTPKLLGAPseGGSSV--FeVTYFKG---KAYLAQSPQFNKQQ 308
Cdd:PLN02502 217 LDLianPEVRD--IFRTRAKIISYIRRFLDDRGFLEVETPMLNMIA--GGAAArpF-VTHHNDlnmDLYLRIATELHLKR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 309 LIVADFERVYEIGPVFRAENSNThRHMTEFTGLDMEMAFEEhYHEVLDTLSELF-----------------VFIFSELPK 371
Cdd:PLN02502 292 LVVGGFERVYEIGRQFRNEGIST-RHNPEFTTCEFYQAYAD-YNDMMELTEEMVsgmvkeltgsykikyhgIEIDFTPPF 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 372 RFAHEIELVRKQYPVeefKLPKDGKMvrltykegiEMLRAAGKEIGDFEDLSTENEKFLGKLVrDKYDTDF--------- 442
Cdd:PLN02502 370 RRISMISLVEEATGI---DFPADLKS---------DEANAYLIAACEKFDVKCPPPQTTGRLL-NELFEEFleetlvqpt 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 443 YILDkFPLEIRPFyTMPDPANPKYSNSYDFFMRGEEILSGAQRIHD----HALLQERMKAHGlSPEDPGL---KDYCDGF 515
Cdd:PLN02502 437 FVLD-HPVEMSPL-AKPHRSKPGLTERFELFINGRELANAFSELTDpvdqRERFEEQVKQHN-AGDDEAMaldEDFCTAL 513
|
570 580 590
....*....|....*....|....*....|....
gi 6323011 516 SYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFP 549
Cdd:PLN02502 514 EYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFP 547
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
248-549 |
5.24e-24 |
|
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a lysine to the 3' OH group of ribose of the appropriate tRNA. Its assignment to class II aaRS is based upon its structure and the presence of three characteristic sequence motifs in the core domain. It is found in eukaryotes as well as some prokaryotes and archaea. However, LysRS belongs to class I aaRS's in some prokaryotes and archaea. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.
Pssm-ID: 238398 [Multi-domain] Cd Length: 329 Bit Score: 103.05 E-value: 5.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 248 FRIQAGVCELFREYLATKKFTEVHTPKLLGAPseGGSSV--FeVTY---FKGKAYLAQSPQFNKQQLIVADFERVYEIGP 322
Cdd:cd00775 8 FIVRSKIISYIRKFLDDRGFLEVETPMLQPIA--GGAAArpF-ITHhnaLDMDLYLRIAPELYLKRLIVGGFERVYEIGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 323 VFRAENSNThRHMTEFTGLDMEMAFEEhYHEVLDTLSELFVF----IFSELPKRF-AHEIELVRKqypveeFKlpkdgkm 397
Cdd:cd00775 85 NFRNEGIDL-THNPEFTMIEFYEAYAD-YNDMMDLTEDLFSGlvkkINGKTKIEYgGKELDFTPP------FK------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 398 vRLTYKEGIEmlRAAGKEIGDFEDLSTEN-EKFLGKLVRDKYD---TDFYILDK------------------FPLEIRPF 455
Cdd:cd00775 150 -RVTMVDALK--EKTGIDFPELDLEQPEElAKLLAKLIKEKIEkprTLGKLLDKlfeefveptliqptfiidHPVEISPL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 456 yTMPDPANPKYSNSYDFFMRGEEILSG----------AQRIhdhaLLQERMKAHGLSPEDPGLKDYCDGFSYGCPPHAGG 525
Cdd:cd00775 227 -AKRHRSNPGLTERFELFICGKEIANAytelndpfdqRERF----EEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGL 301
|
330 340
....*....|....*....|....
gi 6323011 526 GIGLERVVMFYLDLKNIRRASLFP 549
Cdd:cd00775 302 GIGIDRLVMLLTDSNSIRDVILFP 325
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
229-549 |
2.86e-22 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 100.88 E-value: 2.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 229 DTRLDYRVIDLrtVTNQAIF---RIQAGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFeVTYFKGKA---YLAQSP 302
Cdd:PTZ00385 213 DVKYRYRFTDM--MTNPCVIetiKKRHVMLQALRDYFNERNFVEVETPVLHTVASGANAKSF-VTHHNANAmdlFLRVAP 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 303 QFNKQQLIVADFERVYEIGPVFRAENSNtHRHMTEFTGLDMEMAFeeHYHEVLDTLSElfvFIFSELPKRFAHEIELvrK 382
Cdd:PTZ00385 290 ELHLKQCIVGGMERIYEIGKVFRNEDAD-RSHNPEFTSCEFYAAY--HTYEDLMPMTE---DIFRQLAMRVNGTTVV--Q 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 383 QYPVEEFKLPKD---GKMVRL--TYKegiEMLRAAGKEIGDFEDLSTENEKFLGKLVRDKYD----------------TD 441
Cdd:PTZ00385 362 IYPENAHGNPVTvdlGKPFRRvsVYD---EIQRMSGVEFPPPNELNTPKGIAYMSVVMLRYNiplppvrtaakmfeklID 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 442 FYILDKFpleIRPFYTMPDP-----------ANPKYSNSYDFFMRGEEILSGAQRIHD-----HALLQERMKAHGLSPED 505
Cdd:PTZ00385 439 FFITDRV---VEPTFVMDHPlfmsplakeqvSRPGLAERFELFVNGIEYCNAYSELNDpheqyHRFQQQLVDRQGGDEEA 515
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 6323011 506 PGLKD-YCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFP 549
Cdd:PTZ00385 516 MPLDEtFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFP 560
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
291-552 |
3.70e-20 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 93.93 E-value: 3.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 291 YFKGKAYLAQSPQFNKQQLiVADFERVYEIGPVFRAENSNTHRHMTEFTGLDMEMAFEEHYHEVldTLSELFV-FIFSEL 369
Cdd:PTZ00425 321 FFSKQAFLTVSGQLSLENL-CSSMGDVYTFGPTFRAENSHTSRHLAEFWMIEPEIAFADLYDNM--ELAESYIkYCIGYV 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 370 PKRFAHEIELVRKQYP---VEEFKLPKDGKMVRLTYKEGIEMLRAAGKEigdFE-------DLSTENEKFLGKLVRDKYd 439
Cdd:PTZ00425 398 LNNNFDDIYYFEENVEtglISRLKNILDEDFAKITYTNVIDLLQPYSDS---FEvpvkwgmDLQSEHERFVAEQIFKKP- 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 440 tdfYILDKFPLEIRPFYtMPDPANPKYSNSYDFFM-RGEEILSGAQRIHDHALLQERMKAHGLSPEDPGLkdYCDGFSYG 518
Cdd:PTZ00425 474 ---VIVYNYPKDLKAFY-MKLNEDQKTVAAMDVLVpKIGEVIGGSQREDNLERLDKMIKEKKLNMESYWW--YRQLRKFG 547
|
250 260 270
....*....|....*....|....*....|....
gi 6323011 519 CPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDP 552
Cdd:PTZ00425 548 SHPHAGFGLGFERLIMLVTGVDNIKDTIPFPRYP 581
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
53-549 |
2.21e-17 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 85.14 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 53 QLEAEReaREKKAAAEDTAKDNYGKlpliqsrDSDRT---GQKRVKFVDLDEAKDSDKEVLFR--ARVHNTRQQGAtLAF 127
Cdd:PRK00484 5 EQIAVR--REKLAELREQGIDPYPN-------KFERThtaAELRAKYDDKEKEELEELEIEVSvaGRVMLKRVMGK-ASF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 128 LTLRQQASLIQGLVKANKEGTISKNMVKwagSLNLESIVLVRGIVkkvdepIKSATVQnLEIHITKIytisetpealpIL 207
Cdd:PRK00484 75 ATLQDGSGRIQLYVSKDDVGEEALEAFK---KLDLGDIIGVEGTL------FKTKTGE-LSVKATEL-----------TL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 208 LEDASRSeaeaeaagLPVV-----NLDTRLDYRVIDLrtVTNQA---IFRIQAGVCELFREYLATKKFTEVHTPKLLGAP 279
Cdd:PRK00484 134 LTKSLRP--------LPDKfhgltDVETRYRQRYVDL--IVNPEsreTFRKRSKIISAIRRFLDNRGFLEVETPMLQPIA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 280 seGGSSV--FeVTY---FKGKAYLAQSPQFNKQQLIVADFERVYEIGPVFRAENSNThRHMTEFTGLDMEMAFEEhYHEV 354
Cdd:PRK00484 204 --GGAAArpF-ITHhnaLDIDLYLRIAPELYLKRLIVGGFERVYEIGRNFRNEGIDT-RHNPEFTMLEFYQAYAD-YNDM 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 355 LDTLSELFVFIfselpkrfAHEIELVRK-QYPVEEFKLpkDGKMVRLTYKEGI-------------EMLRAAGKEIGdFE 420
Cdd:PRK00484 279 MDLTEELIRHL--------AQAVLGTTKvTYQGTEIDF--GPPFKRLTMVDAIkeytgvdfddmtdEEARALAKELG-IE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 421 DLSTEN-----EKFLGKLVRDKYDTDFYILDkFPLEIRPFyTMPDPANPKYSNSYDFFMRGEEILSG----------AQR 485
Cdd:PRK00484 348 VEKSWGlgkliNELFEEFVEPKLIQPTFITD-YPVEISPL-AKRHREDPGLTERFELFIGGREIANAfselndpidqRER 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323011 486 IHDHALLQER--MKAHGLspeDpglKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFP 549
Cdd:PRK00484 426 FEAQVEAKEAgdDEAMFM---D---EDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
247-549 |
1.25e-15 |
|
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA synthetase (class II) is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440803 [Multi-domain] Cd Length: 495 Bit Score: 79.69 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 247 IFRIQAGVCELFREYLATKKFTEVHTPKLlgAPSEGGSSV--FeVTYFKG---KAYLAQSPQFNKQQLIVADFERVYEIG 321
Cdd:COG1190 173 TFRKRSKIIRAIRRFLDERGFLEVETPML--QPIAGGAAArpF-ITHHNAldmDLYLRIAPELYLKRLIVGGFERVFEIG 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 322 PVFRAENSNThRHMTEFTGLDMEMAFEEhYHEVLDTLSELFVFIFSELPKrfAHEIELvrkqypveefklpkDGKMV--- 398
Cdd:COG1190 250 RNFRNEGIDT-THNPEFTMLELYQAYAD-YNDMMDLTEELIREAAEAVLG--TTKVTY--------------QGQEIdls 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 399 ----RLTYKEGIEmlRAAGKeigDFEDLSTENE-----------------------KFLGKLVRDKYDTDFYILDkFPLE 451
Cdd:COG1190 312 ppwrRITMVEAIK--EATGI---DVTPLTDDEElralakelgievdpgwgrgklidELFEELVEPKLIQPTFVTD-YPVE 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 452 IRPFyTMPDPANPKYSNSYDFFMRGEEILSG----------AQRIHDhallQERMKAHGlSPEDPGL-KDYCDGFSYGCP 520
Cdd:COG1190 386 VSPL-AKRHRDDPGLTERFELFIAGREIANAfselndpidqRERFEE----QLELKAAG-DDEAMPMdEDFLRALEYGMP 459
|
330 340
....*....|....*....|....*....
gi 6323011 521 PHAGGGIGLERVVMFYLDLKNIRRASLFP 549
Cdd:COG1190 460 PTGGLGIGIDRLVMLLTDSPSIRDVILFP 488
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
108-199 |
1.94e-15 |
|
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. Class 2b aaRSs include the homodimeric aspartyl-, asparaginyl-, and lysyl-tRNA synthetases (AspRS, AsnRS, and LysRS). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Included in this group are archeal and archeal-like AspRSs which are non-discriminating and can charge both tRNAAsp and tRNAAsn. E. coli cells have two isoforms of LysRSs (LysS and LysU) encoded by two distinct genes, which are differentially regulated. The cytoplasmic and the mitochondrial isoforms of human LysRS are encoded by a single gene. Yeast cytoplasmic and mitochondrial LysRSs participate in mitochondrial import of cytoplasmic tRNAlysCUU. In addition to their housekeeping role, human LysRS may function as a signaling molecule that activates immune cells. Tomato LysRS may participate in a process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging. AsnRS is immunodominant antigen of the filarial nematode Brugia malayai and is of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.
Pssm-ID: 239766 [Multi-domain] Cd Length: 85 Bit Score: 71.44 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 108 EVLFRARVHNTRQQGAtLAFLTLRQQASLIQGLVKANKEGtiskNMVKWAGSLNLESIVLVRGIVKKVDEPIksATVQNL 187
Cdd:cd04100 1 EVTLAGWVHSRRDHGG-LIFIDLRDGSGIVQVVVNKEELG----EFFEEAEKLRTESVVGVTGTVVKRPEGN--LATGEI 73
|
90
....*....|..
gi 6323011 188 EIHITKIYTISE 199
Cdd:cd04100 74 ELQAEELEVLSK 85
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
229-557 |
3.39e-15 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 78.51 E-value: 3.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 229 DTRLDYRVIDLRTVTNQA---IFRIQAGVCELFREYLATKKFTEVHTPkLLGAPSEGGSSVFEVTYFKG---KAYLAQSP 302
Cdd:PTZ00417 231 DTEIRYRQRYLDLMINEStrsTFITRTKIINYLRNFLNDRGFIEVETP-TMNLVAGGANARPFITHHNDldlDLYLRIAT 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 303 QFNKQQLIVADFERVYEIGPVFRAEN-SNTHRhmTEFTGLDMEMAFEEHYHEVL---DTLSELFVFIFSEL--------P 370
Cdd:PTZ00417 310 ELPLKMLIVGGIDKVYEIGKVFRNEGiDNTHN--PEFTSCEFYWAYADFYDLIKwseDFFSQLVMHLFGTYkilynkdgP 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 371 KRFAHEIELVrKQYP----VEE--------FKLPKDG-----KMVRLTYKEGIEMlraagkeigdfedlstENEKFLGKL 433
Cdd:PTZ00417 388 EKDPIEIDFT-PPYPkvsiVEElekltntkLEQPFDSpetinKMINLIKENKIEM----------------PNPPTAAKL 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 434 VrDKYDTDFyILDKFPleIRPFYTMPDP-----------ANPKYSNSYDFFMRGEEILSGAQRIHDHALLQERMKAHGLS 502
Cdd:PTZ00417 451 L-DQLASHF-IENKYP--NKPFFIIEHPqimsplakyhrSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKD 526
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323011 503 PEDPGLK------DYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPrdpkRLRP 557
Cdd:PTZ00417 527 REKGDAEafqfdaAFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFP----TMRP 583
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
274-550 |
1.03e-14 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 77.22 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 274 KLLGAPSEGGSSV-FEVTYFKGKAYLAQSPQFNKQQLIVAdFERVYEIGPVFRAENSNTHRHMTEFTGLDMEMAFEEhYH 352
Cdd:PLN02532 349 KLKTGTSVKADKLsFSKDFFSRPTYLTVSGRLHLESYACA-LGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFSE-LE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 353 EVLDTLSELFVFIFSELPKRFAHEIELVRKQYP---VEEFKLPKDGKMVRLTYKEGIEMLRAAGKEigDFED-------L 422
Cdd:PLN02532 427 DAMNCAEDYFKFLCKWVLENCSEDMKFVSKRIDktiSTRLEAIISSSLQRISYTEAVDLLKQATDK--KFETkpewgiaL 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 423 STENEKFLGKlvrdkydtDFY----ILDKFPLEIRPFYTMPDPaNPKYSNSYDFFM-RGEEILSGAQRIHDHALLQERMK 497
Cdd:PLN02532 505 TTEHLSYLAD--------EIYkkpvIIYNYPKELKPFYVRLND-DGKTVAAFDLVVpKVGTVITGSQNEERMDILNARIE 575
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 6323011 498 AHGLSPEDpgLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPR 550
Cdd:PLN02532 576 ELGLPREQ--YEWYLDLRRHGTVKHSGFSLGFELMVLFATGLPDVRDAIPFPR 626
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
230-549 |
1.55e-11 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 67.30 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 230 TRLDYRVIDLrtVTN---QAIFRIQAGVCELFREYLATKKFTEVHTPKLlgAPSEGGSSV--FeVTYFKgkAY-----LA 299
Cdd:PRK02983 751 ARVRQRYLDL--AVNpeaRDLLRARSAVVRAVRETLVARGFLEVETPIL--QQVHGGANArpF-VTHIN--AYdmdlyLR 823
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 300 QSPQFNKQQLIVADFERVYEIGPVFRAENSNtHRHMTEFTGLDmemAFEEH--YHEVLDTLSELF----VFIFSElpkrf 373
Cdd:PRK02983 824 IAPELYLKRLCVGGVERVFELGRNFRNEGVD-ATHNPEFTLLE---AYQAHadYDTMRDLTRELIqnaaQAAHGA----- 894
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 374 aHEIELVRKQYPVEEFKLPKDGKMVrlTYKEGIEmlRAAGKEIG---DFEDL---------STENEKFLGKLVRDKYD-- 439
Cdd:PRK02983 895 -PVVMRPDGDGVLEPVDISGPWPVV--TVHDAVS--EALGEEIDpdtPLAELrklcdaagiPYRTDWDAGAVVLELYEhl 969
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 440 ----TD---FYIldKFPLEIRPFyTMPDPANPKYSNSYDFFMRGEEiLSGA---------QRihdhALLQER-MKAHGLS 502
Cdd:PRK02983 970 vedrTTfptFYT--DFPTSVSPL-TRPHRSDPGLAERWDLVAWGVE-LGTAyseltdpveQR----RRLTEQsLLAAGGD 1041
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 6323011 503 PEDPGL-KDYCDGFSYGCPPHAGGGIGLERVVMFyLDLKNIRRASLFP 549
Cdd:PRK02983 1042 PEAMELdEDFLQALEYAMPPTGGLGMGVDRLVML-LTGRSIRETLPFP 1088
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
258-531 |
2.30e-11 |
|
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 63.29 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 258 FREYLATKKFTEVHTPKLLGAPSEGGSSVFEVT------YFKGKAYLAQSPQFNKQQL----IVADFERVYEIGPVFRAE 327
Cdd:cd00768 9 LRRFMAELGFQEVETPIVEREPLLEKAGHEPKDllpvgaENEEDLYLRPTLEPGLVRLfvshIRKLPLRLAEIGPAFRNE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 328 NSNTH-RHMTEFTGLDMEMAFEEhyhevldtlselfvfifSELPKRFAHEIELVRkqypveefklpkdgkmvrltykegi 406
Cdd:cd00768 89 GGRRGlRRVREFTQLEGEVFGED-----------------GEEASEFEELIELTE------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 407 EMLRAAGKEIgdfedlstenekflgklvrdkydtDFYILDKFPLEIRPFYtmpdpanpkYSNSYDFFM-----RGEEILS 481
Cdd:cd00768 127 ELLRALGIKL------------------------DIVFVEKTPGEFSPGG---------AGPGFEIEVdhpegRGLEIGS 173
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 6323011 482 GAQRIHDHALLQErmkahglspedpgLKDYCDGFSYGCPPHAGGGIGLER 531
Cdd:cd00768 174 GGYRQDEQARAAD-------------LYFLDEALEYRYPPTIGFGLGLER 210
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
115-240 |
2.53e-08 |
|
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli aspartyl-tRNA synthetase (AspRS), the human mitochondrial (mt) AspRS-2, the discriminating (D) Thermus thermophilus AspRS-1, and the nondiscriminating (ND) Helicobacter pylori AspRS. These homodimeric enzymes are class2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. Human mtAspRS participates in mitochondrial biosynthesis; this enzyme been shown to charge E.coli native tRNAsp in addition to in vitro transcribed human mitochondrial tRNAsp. T. thermophilus is rare among bacteria in having both a D_AspRS and a ND_AspRS. H.pylori ND-AspRS can charge both tRNAASp and tRNAAsn, it is fractionally more efficient at aminoacylating tRNAAsp over tRNAAsn. The H.pylori genome does not contain AsnRS.
Pssm-ID: 239812 [Multi-domain] Cd Length: 135 Bit Score: 52.91 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 115 VHNTRQQGAtLAFLTLRQQASLIQglVKANKEgtiSKNMVKWAGSLNLESIVLVRGIVKKVDEP---IKSATvQNLEIHI 191
Cdd:cd04317 23 VQRRRDHGG-LIFIDLRDRYGIVQ--VVFDPE---EAPEFELAEKLRNESVIQVTGKVRARPEGtvnPKLPT-GEIEVVA 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 6323011 192 TKIYTISETpEALPILLEDASrseaeaeaaglpVVNLDTRLDYRVIDLR 240
Cdd:cd04317 96 SELEVLNKA-KTLPFEIDDDV------------NVSEELRLKYRYLDLR 131
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
109-197 |
7.31e-08 |
|
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic acids. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See pfam00152). Aminoacyl-tRNA synthetases catalyze the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a hetero-trimeric complex, that contains a subunit in this family. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain.
Pssm-ID: 460164 [Multi-domain] Cd Length: 75 Bit Score: 49.54 E-value: 7.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 109 VLFRARVHNTRQQGATLAFLTLRQQASLIQglVKANKEgtiskNMVKWAGSLNLESIVLVRGIVKKVDEPiksatvqNLE 188
Cdd:pfam01336 1 VTVAGRVTSIRRSGGKLLFLTLRDGTGSIQ--VVVFKE-----EAEKLAKKLKEGDVVRVTGKVKKRKGG-------ELE 66
|
....*....
gi 6323011 189 IHITKIYTI 197
Cdd:pfam01336 67 LVVEEIELL 75
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
259-544 |
1.34e-05 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 47.23 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 259 REYLATKKFTEVHTPKLLGAP-SEGGSSVFEvTYFKG-------KAYLAQSPQFNKQQLIVADFERVYEIGPVFRAENSN 330
Cdd:PRK09350 16 RRFFADRGVLEVETPILSQATvTDIHLVPFE-TRFVGpgasqgkTLWLMTSPEYHMKRLLAAGSGPIFQICKSFRNEEAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 331 THrHMTEFTGLDMemaFEEHY--HEVLDTLSELFVFIFselpkrFAHEIELVRKQYPVEEF----KLPKDgkmvrltyke 404
Cdd:PRK09350 95 RY-HNPEFTMLEW---YRPHYdmYRLMNEVDDLLQQVL------DCEPAESLSYQQAFLRYlgidPLSAD---------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 405 gIEMLRAAGKEIGDFEDLSTEnekflgklvrDKYDTDFYILdkFPLEIRP---------FYTMP---------DPANPKY 466
Cdd:PRK09350 155 -KTQLREVAAKLGLSNIADEE----------EDRDTLLQLL--FTFGVEPnigkekptfVYHFPasqaalakiSTEDHRV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 467 SNSYDFFMRGEEILSGAQRIHDHALLQERMKAHGLSPEDPGLKDY------CDGFSYGCPPHAGGGIGLERVVMFYLDLK 540
Cdd:PRK09350 222 AERFEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQpidenlIAALEAGLPDCSGVALGVDRLIMLALGAE 301
|
....
gi 6323011 541 NIRR 544
Cdd:PRK09350 302 SISE 305
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
107-206 |
2.90e-05 |
|
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the homodimeric non-discriminating (ND) Pyrococcus kodakaraensis aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. P. kodakaraensis AspRS is a class 2b aaRS. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. P. kodakaraensis ND-AspRS can charge both tRNAAsp and tRNAAsn. Some of the enzymes in this group may be discriminating, based on the presence of homologs of asparaginyl-tRNA synthetase (AsnRS) in their completed genomes.
Pssm-ID: 239811 [Multi-domain] Cd Length: 108 Bit Score: 43.46 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011 107 KEVLFRARVHNTRQQGAtLAFLTLRQQASLIQglVKANKEgTISKNMVKWAGSLNLESIVLVRGIVKkvDEPIKSATVqn 186
Cdd:cd04316 13 EEVTVAGWVHEIRDLGG-IKFVILRDREGIVQ--VTAPKK-KVDKELFKTVRKLSRESVISVTGTVK--AEPKAPNGV-- 84
|
90 100
....*....|....*....|
gi 6323011 187 lEIHITKIYTISETPEALPI 206
Cdd:cd04316 85 -EIIPEEIEVLSEAKTPLPL 103
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
24-46 |
4.60e-03 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 40.01 E-value: 4.60e-03
10 20
....*....|....*....|...
gi 6323011 24 EDGKPLSKKALKKLQKEQEKQRK 46
Cdd:PTZ00399 617 ADGEEISKKERKKLSKEYDKQAK 639
|
|
| NatA_aux_su |
pfam12569 |
N-terminal acetyltransferase A, auxiliary subunit; This entry represents N-terminal ... |
31-102 |
9.77e-03 |
|
N-terminal acetyltransferase A, auxiliary subunit; This entry represents N-terminal acetyltransferase A (NatA) auxiliary subunit (also known as NMDA receptor-regulated protein 1), which is a non-catalytic component of the NatA N-terminal acetyltransferase that catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-terminal acetylation plays a role in normal eukaryotic translation and processing, protecting against proteolytic degradation and protein turnover. NAT1 anchors ARD1 and NAT5 to the ribosome, and may present the N terminus of nascent polypeptides for acetylation.
Pssm-ID: 463630 [Multi-domain] Cd Length: 514 Bit Score: 38.79 E-value: 9.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323011 31 KKALKKLQKEQekqrKKEERAlqlEAEREAREKKAAAEDTAKDNYGKlplIQSRDSDRTGQKRVKFVD-LDEA 102
Cdd:pfam12569 411 KKARKKQKKAE----KKAEKE---EAEKAAKKKKKKAEKKAKGEDGE---TKKEDPDPLGEKLAQTEDpLEEA 473
|
|
|