|
Name |
Accession |
Description |
Interval |
E-value |
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
9-439 |
2.27e-177 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 503.10 E-value: 2.27e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 9 TLKSLWHHPHNGELISINGWVRSIRKLKNVCFAMVSDGTCQQALQVVTSP-----EQSKKLSYGASVNIEGQLAVSKNAK 83
Cdd:PRK03932 5 SIKDILKGKYVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDNgeeyfEEIKKLTTGSSVIVTGTVVESPRAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 84 lglQQYELLAEKIKIYGQiNDDNYPIQKKHLTTEMLRQIPHLRLRTAKQGEIFRLRSDSLKALRQFFSSKDFTETNPPII 163
Cdd:PRK03932 85 ---QGYELQATKIEVIGE-DPEDYPIQKKRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 164 TSSDCEGAGEVFTLTpqethknkSFERDDQKHFFDRPAFLTVSTQLHLEALALGLSRVYTISPAFRAEQSHTSRHLAEFW 243
Cdd:PRK03932 161 TASDCEGAGELFRVT--------TLDLDFSKDFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEFW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 244 MLEAEVAFMTsLSQLTSLMEDMIKYTLNSLMEQNYH-----RDHWDQLL---------KPWKCMTYSEAIEELSAVKKTW 309
Cdd:PRK03932 233 MIEPEMAFAD-LEDNMDLAEEMLKYVVKYVLENCPDdleflNRRVDKGDierlenfieSPFPRITYTEAIEILQKSGKKF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 310 KYPPKWGNDLSSEHEKYLCEILHKTPVFVTDYPQKIKPFYMKSSgPD--TVAAVDLLVPQVGELAGGSLRKDHLD----- 382
Cdd:PRK03932 312 EFPVEWGDDLGSEHERYLAEEHFKKPVFVTNYPKDIKAFYMRLN-PDgkTVAAMDLLAPGIGEIIGGSQREERLDvlear 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 19111871 383 --EYKTYPPELQWYLDLMKYSNAPHGGFGLGIERLIAFLEGEnTNVKETIPFPRSVGSI 439
Cdd:PRK03932 391 ikELGLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGL-DNIRDVIPFPRTPGRA 448
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
16-439 |
1.08e-172 |
|
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: 490.72 E-value: 1.08e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 16 HPHNGELISINGWVRSIRKLKNVCFAMVSDGTCQqaLQVVTSP------EQSKKLSYGASVNIEGQLAVSKNAKLGlqqY 89
Cdd:COG0017 10 PEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGF--IQVVVKKdklenfEEAKKLTTESSVEVTGTVVESPRAPQG---V 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 90 ELLAEKIKIYGqINDDNYPIQKKHLTTEMLRQIPHLRLRTAKQGEIFRLRSDSLKALRQFFSSKDFTETNPPIITSSDCE 169
Cdd:COG0017 85 ELQAEEIEVLG-EADEPYPLQPKRHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEVHTPIITASATE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 170 GAGEVFTLTpqethknksferddqkhFFDRPAFLTVSTQLHLEALALGLSRVYTISPAFRAEQSHTSRHLAEFWMLEAEV 249
Cdd:COG0017 164 GGGELFPVD-----------------YFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 250 AFMTsLSQLTSLMEDMIKYTLNSLMEQ--------NYHRDHWDQLLK-PWKCMTYSEAIEELSAVKKtwkyPPKWGNDLS 320
Cdd:COG0017 227 AFAD-LEDVMDLAEEMLKYIIKYVLENcpeeleflGRDVERLEKVPEsPFPRITYTEAIEILKKSGE----KVEWGDDLG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 321 SEHEKYLCEILHKTPVFVTDYPQKIKPFYMK--SSGPDTVAAVDLLVPQVGELAGGSLRKDHLDEYKT------YPPE-L 391
Cdd:COG0017 302 TEHERYLGEEFFKKPVFVTDYPKEIKAFYMKpnPDDPKTVAAFDLLAPGIGEIIGGSQREHRYDVLVErikekgLDPEdY 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 19111871 392 QWYLDLMKYSNAPHGGFGLGIERLIAFLEGEnTNVKETIPFPRSVGSI 439
Cdd:COG0017 382 EWYLDLRRYGSVPHAGFGLGLERLVMWLTGL-ENIREVIPFPRDPGRL 428
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
16-439 |
6.35e-165 |
|
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: 471.86 E-value: 6.35e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 16 HPHNGELISINGWVRSIRKLKNVCFAMVSDGTCQQALQVVTSPE-------QSKKLSYGASVNIEGQLAVSKNAKlglQQ 88
Cdd:TIGR00457 12 YKFVGDEVTVSGWVRTKRSSKKIIFLELNDGSSLGPIQAVINGEdnpylfqLLKSLTTGSSVSVTGKVVESPGKG---QP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 89 YELLAEKIKIYGQINDDNYPIQKKHLTTEMLRQIPHLRLRTAKQGEIFRLRSDSLKALRQFFSSKDFTETNPPIITSSDC 168
Cdd:TIGR00457 89 VELQVKKIEVVGEAEPDDYPLQKKEHSLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWVSPPILTSNDC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 169 EGAGEVFTLTPQEThknksferDDQKHFFDRPAFLTVSTQLHLEALALGLSRVYTISPAFRAEQSHTSRHLAEFWMLEAE 248
Cdd:TIGR00457 169 EGAGELFRVSTGNI--------DFSQDFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 249 VAFMTsLSQLTSLMEDMIKYTLNSLME----------QNYHRD----HWDQLLKPWKCMTYSEAIEELSAVKKTWKYPPK 314
Cdd:TIGR00457 241 MAFAN-LNDLLQLAETLIKYIIKAVLEncsqelkfleKNFDKDlikrLENIINNKFARITYTDAIEILKESDKNFEYEDF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 315 WGNDLSSEHEKYLCEILHKTPVFVTDYPQKIKPFYMK-SSGPDTVAAVDLLVPQVGELAGGSLRKDHLDEYKTY------ 387
Cdd:TIGR00457 320 WGDDLQTEHERFLAEEYFKPPVFVTNYPKDIKAFYMKlNDDGKTVAAMDLLAPGIGEIIGGSEREDDLDKLENRmkemgl 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 19111871 388 -PPELQWYLDLMKYSNAPHGGFGLGIERLIAFLEGeNTNVKETIPFPRSVGSI 439
Cdd:TIGR00457 400 dTDALNWYLDLRKYGSVPHSGFGLGFERLLAYITG-LENIRDAIPFPRTPGNI 451
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
113-434 |
4.94e-151 |
|
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: 431.60 E-value: 4.94e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 113 HLTTEMLRQIPHLRLRTAKQGEIFRLRSDSLKALRQFFSSKDFTETNPPIITSSDCEGAGEVFTLtpqethknksferdd 192
Cdd:cd00776 1 DANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKV--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 193 qkHFFDRPAFLTVSTQLHLEALALGLSRVYTISPAFRAEQSHTSRHLAEFWMLEAEVAFMTSLSQLTSLMEDMIKYTLNS 272
Cdd:cd00776 66 --SYFGKPAYLAQSPQLYKEMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 273 LMEQNYHR--------DHWDQLLKPWKCMTYSEAIEELSAVKKtwKYPPKWGNDLSSEHEKYLCEILHKTPVFVTDYPQK 344
Cdd:cd00776 144 VLERCAKElelvnqlnRELLKPLEPFPRITYDEAIELLREKGV--EEEVKWGEDLSTEHERLLGEIVKGDPVFVTDYPKE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 345 IKPFYMKSSG--PDTVAAVDLLVPQVGELAGGSLRKDHLDEYKTYPPE-------LQWYLDLMKYSNAPHGGFGLGIERL 415
Cdd:cd00776 222 IKPFYMKPDDdnPETVESFDLLMPGVGEIVGGSQRIHDYDELEERIKEhgldpesFEWYLDLRKYGMPPHGGFGLGLERL 301
|
330
....*....|....*....
gi 19111871 416 IAFLEGENtNVKETIPFPR 434
Cdd:cd00776 302 VMWLLGLD-NIREAILFPR 319
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
20-438 |
1.69e-121 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 365.07 E-value: 1.69e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 20 GELISINGWVRSIRKLKNVCFAMVSDGTCQQALQVVTSPE-------QSKKLSYGASVNIEGQLAVSKNAKlglQQYELL 92
Cdd:PLN02603 107 GKTLNVMGWVRTLRAQSSVTFIEVNDGSCLSNMQCVMTPDaegydqvESGLITTGASVLVQGTVVSSQGGK---QKVELK 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 93 AEKIKIYGQiNDDNYPIQKKHLTTEMLRQIPHLRLRTAKQGEIFRLRSDSLKALRQFFSSKDFTETNPPIITSSDCEGAG 172
Cdd:PLN02603 184 VSKIVVVGK-SDPSYPIQKKRVSREFLRTKAHLRPRTNTFGAVARVRNALAYATHKFFQENGFVWVSSPIITASDCEGAG 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 173 EVF---TLTPQETH----------KNKSFERDDQKHFFDRPAFLTVSTQLHLEALALGLSRVYTISPAFRAEQSHTSRHL 239
Cdd:PLN02603 263 EQFcvtTLIPNSAEnggslvddipKTKDGLIDWSQDFFGKPAFLTVSGQLNGETYATALSDVYTFGPTFRAENSNTSRHL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 240 AEFWMLEAEVAFM---TSLSQLTSLMEDMIKYTLNSLMEQNYHRDHW----------DQLLKPWKCMTYSEAIEELSAVK 306
Cdd:PLN02603 343 AEFWMIEPELAFAdlnDDMACATAYLQYVVKYILENCKEDMEFFNTWiekgiidrlsDVVEKNFVQLSYTDAIELLLKAK 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 307 KTWKYPPKWGNDLSSEHEKYLCEI-LHKTPVFVTDYPQKIKPFYMKSSGP-DTVAAVDLLVPQVGELAGGSLR------- 377
Cdd:PLN02603 423 KKFEFPVKWGLDLQSEHERYITEEaFGGRPVIIRDYPKEIKAFYMRENDDgKTVAAMDMLVPRVGELIGGSQReerleyl 502
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19111871 378 KDHLDEYKTYPPELQWYLDLMKYSNAPHGGFGLGIERLIAFLEGENtNVKETIPFPRSVGS 438
Cdd:PLN02603 503 EARLDELKLNKESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGID-NIRDAIPFPRVPGS 562
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
20-437 |
1.41e-100 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 311.54 E-value: 1.41e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 20 GELISINGWVRSIRKLKNVCFAM--VSDGTCQQALQVVTSP---EQSKKLSYGASVNIEGQLAVSKNAKLGLQQYELLAE 94
Cdd:PLN02221 50 GQKVRIGGWVKTGREQGKGTFAFleVNDGSCPANLQVMVDSslyDLSTLVATGTCVTVDGVLKVPPEGKGTKQKIELSVE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 95 KIKIYGQINDDNYPIQKKHLTTEMLRQIPHLRLRTAKQGEIFRLRSDSLKALRQFFSSKDFTETNPPIITSSDCEGAGEV 174
Cdd:PLN02221 130 KVIDVGTVDPTKYPLPKTKLTLEFLRDVLHLRSRTNSISAVARIRNALAFATHSFFQEHSFLYIHTPIITTSDCEGAGEM 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 175 FTLT----------------PQETHKN---------------------------------------KSFER--------- 190
Cdd:PLN02221 210 FQVTtlinyterleqdlidnPPPTEADveaarlivkergevvaqlkaakaskeeitaavaelkiakESLAHieersklkp 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 191 ---------DDQKHFFDRPAFLTVSTQLHLEALALGLSRVYTISPAFRAEQSHTSRHLAEFWMLEAEVAFmTSLSQLTSL 261
Cdd:PLN02221 290 glpkkdgkiDYSKDFFGRQAFLTVSGQLQVETYACALSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAF-ADLEDDMNC 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 262 MEDMIKYTLN----------SLMEQNYHRDHWDQL----LKPWKCMTYSEAIEELS-AVKKTWKYPPK--WGNDLSSEHE 324
Cdd:PLN02221 369 AEAYVKYMCKwlldkcfddmELMAKNFDSGCIDRLrmvaSTPFGRITYTEAIELLEeAVAKGKEFDNNveWGIDLASEHE 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 325 KYLCEILHKTPVFVTDYPQKIKPFYMK-SSGPDTVAAVDLLVPQVGELAGGSLRKDHLDEYKTYPPEL-------QWYLD 396
Cdd:PLN02221 449 RYLTEVLFQKPLIVYNYPKGIKAFYMRlNDDEKTVAAMDVLVPKVGELIGGSQREERYDVIKQRIEEMglpiepyEWYLD 528
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 19111871 397 LMKYSNAPHGGFGLGIERLIAFLEGENtNVKETIPFPRSVG 437
Cdd:PLN02221 529 LRRYGTVKHCGFGLGFERMILFATGID-NIRDVIPFPRYPG 568
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
20-437 |
8.20e-100 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 310.03 E-value: 8.20e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 20 GELISINGWVRSIRKLKN--VCFAMVSDGTCQQALQVVTSP-----EQSKKLSYGASVNIEGQLAVS------------K 80
Cdd:PTZ00425 81 DQIITVCGWSKAVRKQGGgrFCFVNLNDGSCHLNLQIIVDQsienyEKLLKCGVGCCFRFTGKLIISpvqnenkkgllkE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 81 NAKLGLQQYELlaEKIKIYGQ-INDDNYPIQKKHLTTEMLRQIPHLRLRTAKQGEIFRLRSDSLKALRQFFSSKDFTETN 159
Cdd:PTZ00425 161 NVELALKDNSI--HNFEIYGEnLDPQKYPLSKKNHGKEFLREVAHLRPRSYFISSVIRIRNALAIATHLFFQSRGFLYIH 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 160 PPIITSSDCEGAGEVFTLT------------PQETHKNKSFER----------------------------------DDQ 193
Cdd:PTZ00425 239 TPLITTSDCEGGGEMFTVTtllgedadyraiPRVNKKNKKGEKredilntcnannnngnssssnavsspaypdqyliDYK 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 194 KHFFDRPAFLTVSTQLHLEALALGLSRVYTISPAFRAEQSHTSRHLAEFWMLEAEVAFmTSLSQLTSLMEDMIKYTLNSL 273
Cdd:PTZ00425 319 KDFFSKQAFLTVSGQLSLENLCSSMGDVYTFGPTFRAENSHTSRHLAEFWMIEPEIAF-ADLYDNMELAESYIKYCIGYV 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 274 MEQNYHRDHW--------------DQLLKPWKCMTYSEAIEELSAVKKTWKYPPKWGNDLSSEHEKYLCEILHKTPVFVT 339
Cdd:PTZ00425 398 LNNNFDDIYYfeenvetglisrlkNILDEDFAKITYTNVIDLLQPYSDSFEVPVKWGMDLQSEHERFVAEQIFKKPVIVY 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 340 DYPQKIKPFYMK-SSGPDTVAAVDLLVPQVGELAGGSLRKDHLD-------EYKTYPPELQWYLDLMKYSNAPHGGFGLG 411
Cdd:PTZ00425 478 NYPKDLKAFYMKlNEDQKTVAAMDVLVPKIGEVIGGSQREDNLErldkmikEKKLNMESYWWYRQLRKFGSHPHAGFGLG 557
|
490 500
....*....|....*....|....*.
gi 19111871 412 IERLIAFLEGENtNVKETIPFPRSVG 437
Cdd:PTZ00425 558 FERLIMLVTGVD-NIKDTIPFPRYPG 582
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
19-434 |
6.75e-86 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 269.37 E-value: 6.75e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 19 NGELISINGWVRSIRKLKNVCFAMVSD--GTcqqaLQVVTSP-------EQSKKLSYGASVNIEGQLAVSKNAKLGlqqY 89
Cdd:PRK05159 15 DGEEVTLAGWVHEIRDLGGIAFLILRDrsGI----IQVVVKKkvdeelfETIKKLKRESVVSVTGTVKANPKAPGG---V 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 90 ELLAEKIKIYGQiNDDNYPIQkkhLTTEMLRQIP------HLRLRTAKQGEIFRLRSDSLKALRQFFSSKDFTETNPPII 163
Cdd:PRK05159 88 EVIPEEIEVLNK-AEEPLPLD---ISGKVLAELDtrldnrFLDLRRPRVRAIFKIRSEVLRAFREFLYENGFTEIFTPKI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 164 TSSDCEGAGEVFTLTpqethknksferddqkhFFDRPAFLTVSTQLHLEAL-ALGLSRVYTISPAFRAEQSHTSRHLAEF 242
Cdd:PRK05159 164 VASGTEGGAELFPID-----------------YFEKEAYLAQSPQLYKQMMvGAGFERVFEIGPVFRAEEHNTSRHLNEY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 243 WMLEAEVAFMTSLSQLTSLMEDMIKYTLNSLMEqNYHRD------HWDQLLKPWKCMTYSEAIEELSAvkktwKY-PPKW 315
Cdd:PRK05159 227 TSIDVEMGFIDDHEDVMDLLENLLRYMYEDVAE-NCEKElellgiELPVPETPIPRITYDEAIEILKS-----KGnEISW 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 316 GNDLSSEHEKYLCEILHKT----PVFVTDYPQKIKPFYMK--SSGPDTVAAVDLLVPQVgELAGGSLR---KDHLDE--- 383
Cdd:PRK05159 301 GDDLDTEGERLLGEYVKEEygsdFYFITDYPSEKRPFYTMpdEDDPEISKSFDLLFRGL-EITSGGQRihrYDMLVEsik 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 19111871 384 YKTYPPEL-QWYLDLMKYSNAPHGGFGLGIERLIAFLEGENtNVKETIPFPR 434
Cdd:PRK05159 380 EKGLNPESfEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLE-NIREAVLFPR 430
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
117-434 |
1.04e-82 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 257.11 E-value: 1.04e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 117 EMLRQIPHLRLRTAKQGEIFRLRSDSLKALRQFFSSKDFTETNPPIITSSDCEGAGEVFtLTPQETHKNksferddqkhF 196
Cdd:pfam00152 3 ETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDF-LVPSRALGK----------F 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 197 FdrpaFLTVSTQLHLEALAL-GLSRVYTISPAFRAEQSHTSRHLaEFWMLEAEVAFMtSLSQLTSLMEDMIKYTLNSLME 275
Cdd:pfam00152 72 Y----ALPQSPQLYKQLLMVaGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFV-DYEDVMDLTEELIKEIFKEVEG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 276 --QNYHRDHWDQLLKPWKCMTYSEAIEELsavkkTWKYPPKWGNDLSSEHEKYLCEILHKT----PVFVTDYPQKIKPFY 349
Cdd:pfam00152 146 iaKELEGGTLLDLKKPFPRITYAEAIEKL-----NGKDVEELGYGSDKPDLRFLLELVIDKnkfnPLWVTDFPAEHHPFT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 350 MK--SSGPDTVAAVDLLVPQVgELAGGSLR-----------KDHLDEYKTYPPELQWYLDLMKYSNAPHGGFGLGIERLI 416
Cdd:pfam00152 221 MPkdEDDPALAEAFDLVLNGV-EIGGGSIRihdpelqeerfEEQGLDPEEAEEKFGFYLDALKYGAPPHGGLGIGLDRLV 299
|
330
....*....|....*...
gi 19111871 417 AFLEGENtNVKETIPFPR 434
Cdd:pfam00152 300 MLLTGLE-SIREVIAFPK 316
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
30-437 |
4.18e-82 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 265.19 E-value: 4.18e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 30 RSIRKLKNVCFAMVSDGTCQQALQVV-----TSPEQSkkLSYGASVNIEGQLAVSKNAkLGLQQYELLAEKIKIYGQIND 104
Cdd:PLN02532 127 KSAPPPPSVAYLLISDGSCVASLQVVvdsalAPLTQL--MATGTCILAEGVLKLPLPA-QGKHVIELEVEKILHIGTVDP 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 105 DNYPIQKKHLTTEMLRQIPHLRLRTAKQGEIFRLRSDSLKALRQFFSSKDFTETNPPIITSSDCEGAGEVFTLT------ 178
Cdd:PLN02532 204 EKYPLSKKRLPLDMLRDFSHFRPRTTTVASVTRVRSALTHATHTFFQDHGFLYVQVPIITTTDATGFGEMFRVTtllgks 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 179 --------PQETH-----------KNKS-----FERDD------------------------------------------ 192
Cdd:PLN02532 284 ddkeekkpVHETEgisleavkaaiKEKTnlveeLKRSEsnrealvaaeqdlrktnqlasqleakeklktgtsvkadklsf 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 193 QKHFFDRPAFLTVSTQLHLEALALGLSRVYTISPAFRAEQSHTSRHLAEFWMLEAEVAFmtslSQLTSLM---EDMIKYT 269
Cdd:PLN02532 364 SKDFFSRPTYLTVSGRLHLESYACALGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAF----SELEDAMncaEDYFKFL 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 270 LNSLMEQ-----NYHRDHWDQ---------LLKPWKCMTYSEAIEEL-SAVKKTWKYPPKWGNDLSSEHEKYLCEILHKT 334
Cdd:PLN02532 440 CKWVLENcsedmKFVSKRIDKtistrleaiISSSLQRISYTEAVDLLkQATDKKFETKPEWGIALTTEHLSYLADEIYKK 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 335 PVFVTDYPQKIKPFYMK-SSGPDTVAAVDLLVPQVGELAGGSLRKDHLD-------EYKTYPPELQWYLDLMKYSNAPHG 406
Cdd:PLN02532 520 PVIIYNYPKELKPFYVRlNDDGKTVAAFDLVVPKVGTVITGSQNEERMDilnarieELGLPREQYEWYLDLRRHGTVKHS 599
|
490 500 510
....*....|....*....|....*....|.
gi 19111871 407 GFGLGIERLIAFLEGEnTNVKETIPFPRSVG 437
Cdd:PLN02532 600 GFSLGFELMVLFATGL-PDVRDAIPFPRSWG 629
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
19-434 |
4.62e-50 |
|
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: 175.40 E-value: 4.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 19 NGELISINGWVRSIRKLKNVCFAMVSDgtcQQALQVVTSPEQ--SKKL-SYGASVNIEGQLAVSKNAKL---GLQQYELL 92
Cdd:TIGR00458 11 DGQEVTFMGWVHEIRDLGGLIFVLLRD---REGLIQITAPAKkvSKNLfKWAKKLNLESVVAVRGIVKIkekAPGGFEII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 93 AEKIKIYgQINDDNYPIQ-KKHLTTEMLRQIPH--LRLRTAKQGEIFRLRSDSLKALRQFFSSKDFTETNPPIITSSDCE 169
Cdd:TIGR00458 88 PTKIEVI-NEAKEPLPLDpTEKVPAELDTRLDYrfLDLRRPTVQAIFRIRSGVLESVREFLAEEGFIEVHTPKLVASATE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 170 GAGEVFTLTpqethknksferddqkhFFDRPAFLTVSTQLHLEAL-ALGLSRVYTISPAFRAEQSHTSRHLAEFWMLEAE 248
Cdd:TIGR00458 167 GGTELFPIT-----------------YFEREAFLGQSPQLYKQQLmAAGFERVYEIGPIFRAEEHNTHRHLNEATSIDIE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 249 VAFmTSLSQLTSLMEDMIKYTLNSLMEQNYHRDHWDQLL-----KPWKCMTYSEAIEELSAVKKtwkyPPKWGNDLSSEH 323
Cdd:TIGR00458 230 MAF-EDHHDVMDILEELVVRVFEDVPERCAHQLETLEFKlekpeGKFVRLTYDEAIEMANAKGV----EIGWGEDLSTEA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 324 EKYLCEILhKTPVFVTDYPQKIKPFYM--KSSGPDTVAAVDLLVPQVgELAGGSLR---KDHLDE---YKTYPPE-LQWY 394
Cdd:TIGR00458 305 EKALGEEM-DGLYFITDWPTEIRPFYTmpDEDNPEISKSFDLMYRDL-EISSGAQRihlHDLLVErikAKGLNPEgFKDY 382
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 19111871 395 LDLMKYSNAPHGGFGLGIERLIAFLEGENtNVKETIPFPR 434
Cdd:TIGR00458 383 LEAFSYGMPPHAGWGLGAERFVMFLLGLK-NIREAVLFPR 421
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
134-437 |
3.20e-47 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 165.19 E-value: 3.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 134 EIFRLRSDSLKALRQFFSSKDFTETNPPIITSSDCEGAGEVFTLTpqethknksfERDDQKHFFDRPAFLTVSTQLHLEA 213
Cdd:PRK06462 28 KVLKVQSSILRYTREFLDGRGFVEVLPPIISPSTDPLMGLGSDLP----------VKQISIDFYGVEYYLADSMILHKQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 214 LALGLSRVYTISPAFRAEQ--SHTSRHLAEFWMLEAEVAFmTSLSQLTSLMEDMIKYTLNSLMEQnyhrdHWDQLL---- 287
Cdd:PRK06462 98 ALRMLGKIFYLSPNFRLEPvdKDTGRHLYEFTQLDIEIEG-ADLDEVMDLIEDLIKYLVKELLEE-----HEDELEffgr 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 288 ------KPWKCMTYSEAIEELsavkktwKYPPKWGNDLS---SEHEKYLCEIlHKTPVFVTDYPQKIKPFYMKSSG--PD 356
Cdd:PRK06462 172 dlphlkRPFKRITHKEAVEIL-------NEEGCRGIDLEelgSEGEKSLSEH-FEEPFWIIDIPKGSREFYDREDPerPG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 357 TVAAVDLLVPQ-VGELAGGSLRK-------DHLDEYKTYPPELQWYLDLMKYSNAPHGGFGLGIERLIAFLEGENtNVKE 428
Cdd:PRK06462 244 VLRNYDLLLPEgYGEAVSGGEREyeyeeivERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLR-HIRE 322
|
....*....
gi 19111871 429 TIPFPRSVG 437
Cdd:PRK06462 323 VQPFPRVPG 331
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
136-434 |
5.76e-36 |
|
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: 133.37 E-value: 5.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 136 FRLRSDSLKALRQFFSSKDFTETNPPIITSSDCEGAGEVFTLtpqethknKSFERDdqkHFfdrpAFLTVSTQLHLEALA 215
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLV--------KYNALG---LD----YYLRISPQLFKKRLM 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 216 L-GLSRVYTISPAFRAEQShTSRHLAEFWMLEAEVAFMTsLSQLTSLMEDMIKYTLNSLMEQNYH--RDHWDQLLKPWKC 292
Cdd:cd00669 66 VgGLDRVFEINRNFRNEDL-RARHQPEFTMMDLEMAFAD-YEDVIELTERLVRHLAREVLGVTAVtyGFELEDFGLPFPR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 293 MTYSEAIEELSAvkktwkyppkwgndlssehekylceilhktPVFVTDYPQKIKPFYMK--SSGPDTVAAVDLLVPQVgE 370
Cdd:cd00669 144 LTYREALERYGQ------------------------------PLFLTDYPAEMHSPLASphDVNPEIADAFDLFINGV-E 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19111871 371 LAGGSLR-KDHLDEYKTY-----PPELQ-----WYLDLMKYSNAPHGGFGLGIERLIAFLEGeNTNVKETIPFPR 434
Cdd:cd00669 193 VGNGSSRlHDPDIQAEVFqeqgiNKEAGmeyfeFYLKALEYGLPPHGGLGIGIDRLIMLMTN-SPTIREVIAFPK 266
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
20-434 |
5.44e-32 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 127.52 E-value: 5.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 20 GELISINGWVRSIRKLKNVCFAMV--SDGTCQQALqVVTSPEQSK-------KLSYGASVNIEGQLAVSKNAKLGL-QQY 89
Cdd:PLN02850 81 GSEVLIRGRVHTIRGKGKSAFLVLrqSGFTVQCVV-FVSEVTVSKgmvkyakQLSRESVVDVEGVVSVPKKPVKGTtQQV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 90 ELLAEKI--------KIYGQINDDNYPIQKKHLTTEMLRQIPH-----------LRLRTAKQGEIFRLRSDSLKALRQFF 150
Cdd:PLN02850 160 EIQVRKIycvskalaTLPFNVEDAARSESEIEKALQTGEQLVRvgqdtrlnnrvLDLRTPANQAIFRIQSQVCNLFREFL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 151 SSKDFTETNPPIITSSDCEGAGEVFTLtpqethknksferddqkHFFDRPAFLTVSTQLHLE-ALALGLSRVYTISPAFR 229
Cdd:PLN02850 240 LSKGFVEIHTPKLIAGASEGGSAVFRL-----------------DYKGQPACLAQSPQLHKQmAICGDFRRVFEIGPVFR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 230 AEQSHTSRHLAEFWMLEAEVAFMTSLSQLTSLMEDMIKYTLNSLMEqnyhrdhwdqllkpwKCMTYSEAI------EELS 303
Cdd:PLN02850 303 AEDSFTHRHLCEFTGLDLEMEIKEHYSEVLDVVDELFVAIFDGLNE---------------RCKKELEAIreqypfEPLK 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 304 AVKKTWKYPPKWG--------------NDLSSEHEKYLCEIL---HKTPVFVTD-YPQKIKPFY-MKS------------ 352
Cdd:PLN02850 368 YLPKTLRLTFAEGiqmlkeagvevdplGDLNTESERKLGQLVkekYGTDFYILHrYPLAVRPFYtMPCpddpkysnsfdv 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 353 --------SGPDTVAAVDLLVPQVGELAggslrkdhLDeyktyPPELQWYLDLMKYSNAPHGGFGLGIERLIAFLEGENt 424
Cdd:PLN02850 448 firgeeiiSGAQRVHDPELLEKRAEECG--------ID-----VKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLN- 513
|
490
....*....|
gi 19111871 425 NVKETIPFPR 434
Cdd:PLN02850 514 NIRKTSLFPR 523
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
23-101 |
7.72e-26 |
|
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli asparaginyl-tRNA synthetase (AsnRS) and, in Arabidopsis thaliana and Saccharomyces cerevisiae mitochondrial (mt) AsnRS. 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. S. cerevisiae mtAsnRS can charge E.coli tRNA with asparagines. Mutations in the gene for S. cerevisiae mtAsnRS has been found to induce a "petite" phenotype typical for a mutation in a nuclear gene that results in a non-functioning mitochondrial protein synthesis system.
Pssm-ID: 239813 [Multi-domain] Cd Length: 82 Bit Score: 99.95 E-value: 7.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 23 ISINGWVRSIRKLKNVCFAMVSDGTCQQALQVV-----TSPEQSKKLSYGASVNIEGQLAVSKNAKlglQQYELLAEKIK 97
Cdd:cd04318 2 VTVNGWVRSVRDSKKISFIELNDGSCLKNLQVVvdkelTNFKEILKLSTGSSIRVEGVLVKSPGAK---QPFELQAEKIE 78
|
....
gi 19111871 98 IYGQ 101
Cdd:cd04318 79 VLGE 82
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
20-434 |
7.23e-25 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 107.00 E-value: 7.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 20 GELISINGWVRSIRKLKNVCFAMVSDGTCQQALQVVTSPEQSKKLsygasVNIEGQLAVSknAKLGLQQYELLAEKIKIY 99
Cdd:PTZ00401 78 DKTVLIRARVSTTRKKGKMAFMVLRDGSDSVQAMAAVEGDVPKEM-----IDFIGQIPTE--SIVDVEATVCKVEQPITS 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 100 GQINDDNYPIQKKHLTTEMLRQIPH--------------------------LRLRTAKQGEIFRLRSDSLKALRQFFSSK 153
Cdd:PTZ00401 151 TSHSDIELKVKKIHTVTESLRTLPFtledasrkesdegakvnfdtrlnsrwMDLRTPASGAIFRLQSRVCQYFRQFLIDS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 154 DFTETNPPIITSSDCEGAGEVFTLtpqethknksferddqkHFFDRPAFLTVSTQLHLE-ALALGLSRVYTISPAFRAEQ 232
Cdd:PTZ00401 231 DFCEIHSPKIINAPSEGGANVFKL-----------------EYFNRFAYLAQSPQLYKQmVLQGDVPRVFEVGPVFRSEN 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 233 SHTSRHLAEFWMLEAEVAFMTSLSQLTSLMEDMIKYTLNSLMEQNYHRDHWDQL--LKP--WKC---------------- 292
Cdd:PTZ00401 294 SNTHRHLTEFVGLDVEMRINEHYYEVLDLAESLFNYIFERLATHTKELKAVCQQypFEPlvWKLtpermkelgvgviseg 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 293 --------------------MTYSEAIEELSAVKKTwKYPPKwgNDLSSEHEKYLCEIL---HKTPVFVTD-YPQKIKPF 348
Cdd:PTZ00401 374 veptdkyqarvhnmdsrmlrINYMHCIELLNTVLEE-KMAPT--DDINTTNEKLLGKLVkerYGTDFFISDrFPSSARPF 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 349 YMKSSGPDT--VAAVDLLVpQVGELAGGSLRKDHLDEYKTYPPELQW-------YLDLMKYSNAPHGGFGLGIERLIAFL 419
Cdd:PTZ00401 451 YTMECKDDErfTNSYDMFI-RGEEISSGAQRIHDPDLLLARAKMLNVdltpikeYVDSFRLGAWPHGGFGVGLERVVMLY 529
|
490
....*....|....*
gi 19111871 420 EGENtNVKETIPFPR 434
Cdd:PTZ00401 530 LGLS-NVRLASLFPR 543
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
134-433 |
6.80e-18 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 85.53 E-value: 6.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 134 EIFRLRSDSLKALRQFFSSKDFTETNPPI---ITSsdceGAgevfTLTPQETHKNksferddqkhFFDRPAFLTVSTQLH 210
Cdd:PRK00484 170 ETFRKRSKIISAIRRFLDNRGFLEVETPMlqpIAG----GA----AARPFITHHN----------ALDIDLYLRIAPELY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 211 LEALAL-GLSRVYTISPAFRAEQSHTsRHLAEFWMLEAEVAFMT--SLSQLTslmEDMIKY---TLNSLMEQNYHRDHWD 284
Cdd:PRK00484 232 LKRLIVgGFERVYEIGRNFRNEGIDT-RHNPEFTMLEFYQAYADynDMMDLT---EELIRHlaqAVLGTTKVTYQGTEID 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 285 qLLKPWKCMTYSEAI-------------EELSAVKKTW--KYPPKWGndlsseHEKYLCEILHKT-------PVFVTDYP 342
Cdd:PRK00484 308 -FGPPFKRLTMVDAIkeytgvdfddmtdEEARALAKELgiEVEKSWG------LGKLINELFEEFvepkliqPTFITDYP 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 343 QKIKPFYMKS-SGPDTVAAVDLLV--------------P---------QVGELAGGSLRKDHLDEYktyppelqwYLDLM 398
Cdd:PRK00484 381 VEISPLAKRHrEDPGLTERFELFIggreianafselndPidqrerfeaQVEAKEAGDDEAMFMDED---------FLRAL 451
|
330 340 350
....*....|....*....|....*....|....*
gi 19111871 399 KYSNAPHGGFGLGIERLIAFLEGeNTNVKETIPFP 433
Cdd:PRK00484 452 EYGMPPTGGLGIGIDRLVMLLTD-SPSIRDVILFP 485
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
20-433 |
8.65e-18 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 86.17 E-value: 8.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 20 GELISINGWVRSIRKLKNVCFAMVSDGTCQqaLQVV---TSPEQSKKLSYGASVNI------EGQLAVSKNAKLglqqyE 90
Cdd:PRK02983 651 GEEVSVSGRVLRIRDYGGVLFADLRDWSGE--LQVLldaSRLEQGSLADFRAAVDLgdlvevTGTMGTSRNGTL-----S 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 91 LLAEKIKIYGQindDNYPIQKKH--LTTemlrqiPHLRLRT--------AKQGEIFRLRSDSLKALRQFFSSKDFTETNP 160
Cdd:PRK02983 724 LLVTSWRLAGK---CLRPLPDKWkgLTD------PEARVRQryldlavnPEARDLLRARSAVVRAVRETLVARGFLEVET 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 161 PIITSSDcEGAgevfTLTPQETHKNKsferddqkhfFDRPAFLTVSTQLHLEALAL-GLSRVYTISPAFRAE-QSHTsrH 238
Cdd:PRK02983 795 PILQQVH-GGA----NARPFVTHINA----------YDMDLYLRIAPELYLKRLCVgGVERVFELGRNFRNEgVDAT--H 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 239 LAEFWMLEAEVAF--MTSLSQLTslmEDMIKYTlnslmEQNYH------RDHWDQLLK------PWKCMTYSEAI----- 299
Cdd:PRK02983 858 NPEFTLLEAYQAHadYDTMRDLT---RELIQNA-----AQAAHgapvvmRPDGDGVLEpvdisgPWPVVTVHDAVsealg 929
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 300 ---------EELSAVKKTW--KYPPKWGN-DLSSEHEKYLCEILHKTPVFVTDYPQKIKPFYMK-SSGP------DTVA- 359
Cdd:PRK02983 930 eeidpdtplAELRKLCDAAgiPYRTDWDAgAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPhRSDPglaerwDLVAw 1009
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 360 AVDL----------------LVPQVGELAGGSLRKDHLDEYktyppelqwYLDLMKYSNAPHGGFGLGIERLIAFLEGen 423
Cdd:PRK02983 1010 GVELgtayseltdpveqrrrLTEQSLLAAGGDPEAMELDED---------FLQALEYAMPPTGGLGMGVDRLVMLLTG-- 1078
|
490
....*....|
gi 19111871 424 TNVKETIPFP 433
Cdd:PRK02983 1079 RSIRETLPFP 1088
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
138-415 |
1.81e-15 |
|
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: 74.85 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 138 LRSDSLKALRQFFSSKDFTETNPPIITSsdcEGAGEVFTLTPQETHKNKSFERDDqkhFFDRPAFLTVSTQLHLEALALG 217
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVER---EPLLEKAGHEPKDLLPVGAENEED---LYLRPTLEPGLVRLFVSHIRKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 218 LSRVYTISPAFRAEQSHTS-RHLAEFWMLEAEVAFMTSLSQltSLMEDMIkytlnslmeqnyhrdhwdqllkpwkcmtys 296
Cdd:cd00768 75 PLRLAEIGPAFRNEGGRRGlRRVREFTQLEGEVFGEDGEEA--SEFEELI------------------------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 297 EAIEELsavkktWKYppkWGNDLSsehekylceilhktPVFVTDYPQKIKPFYmksSGPDTVAAVDLLVPQVGELAGGSL 376
Cdd:cd00768 123 ELTEEL------LRA---LGIKLD--------------IVFVEKTPGEFSPGG---AGPGFEIEVDHPEGRGLEIGSGGY 176
|
250 260 270
....*....|....*....|....*....|....*....
gi 19111871 377 RkDHLDEYKTyppELQWYLDLMKYSNAPHGGFGLGIERL 415
Cdd:cd00768 177 R-QDEQARAA---DLYFLDEALEYRYPPTIGFGLGLERL 211
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
23-101 |
4.62e-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: 69.90 E-value: 4.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 23 ISINGWVRSIRKLKNVCFAMVSDGTcqQALQVVTSPEQS-------KKLSYGASVNIEGQLAVSKNAKLGLQQYELLAEK 95
Cdd:cd04100 2 VTLAGWVHSRRDHGGLIFIDLRDGS--GIVQVVVNKEELgeffeeaEKLRTESVVGVTGTVVKRPEGNLATGEIELQAEE 79
|
....*.
gi 19111871 96 IKIYGQ 101
Cdd:cd04100 80 LEVLSK 85
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
18-300 |
1.28e-12 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 69.71 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 18 HNGELISINGWVRSIRKLKNVCFAMVSD--GTCQqalqVVTSP-----EQSKKLSYGASVNIEGQL----AVSKNAKLGL 86
Cdd:PRK00476 15 HVGQTVTLCGWVHRRRDHGGLIFIDLRDreGIVQ----VVFDPdaeafEVAESLRSEYVIQVTGTVrarpEGTVNPNLPT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 87 QQYELLAEKIKIYG-------QINDD-NYPiqkkhlttEMLRqiphLR-----LRTAKQGEIFRLRSDSLKALRQFFSSK 153
Cdd:PRK00476 91 GEIEVLASELEVLNksktlpfPIDDEeDVS--------EELR----LKyryldLRRPEMQKNLKLRSKVTSAIRNFLDDN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 154 DFTETNPPIITSSDCEGAGEvFtLTPQETHKNKsferddqkhFFDRPA----F---LTVStqlhlealalGLSRVYTISP 226
Cdd:PRK00476 159 GFLEIETPILTKSTPEGARD-Y-LVPSRVHPGK---------FYALPQspqlFkqlLMVA----------GFDRYYQIAR 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19111871 227 AFRAEQSHTSRhLAEFWMLEAEVAFMTSlSQLTSLMEDMIKYtlnsLMEQNYHRDhwdqLLKPWKCMTYSEAIE 300
Cdd:PRK00476 218 CFRDEDLRADR-QPEFTQIDIEMSFVTQ-EDVMALMEGLIRH----VFKEVLGVD----LPTPFPRMTYAEAMR 281
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
18-300 |
4.02e-12 |
|
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: 68.10 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 18 HNGELISINGWVRSIRKLKNVCFAMVSD--GTcqqaLQVVTSPEQSKKLSYGAS-------VNIEGQLAV----SKNAKL 84
Cdd:COG0173 14 DVGQEVTLSGWVHRRRDHGGLIFIDLRDryGI----TQVVFDPDDSAEAFEKAEklrseyvIAVTGKVRArpegTVNPKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 85 GLQQYELLAEKIKIYG-------QINDDNypiqkkhLTTEMLRqiphLR-----LRTAKQGEIFRLRSDSLKALRQFFSS 152
Cdd:COG0173 90 PTGEIEVLASELEILNkaktppfQIDDDT-------DVSEELR----LKyryldLRRPEMQKNLILRHKVTKAIRNYLDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 153 KDFTETNPPIITSSDCEGAGEvFtLTPQETHKNKsferddqkhFFdrpA-------F---LTVStqlhlealalGLSRVY 222
Cdd:COG0173 159 NGFLEIETPILTKSTPEGARD-Y-LVPSRVHPGK---------FY---AlpqspqlFkqlLMVS----------GFDRYF 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19111871 223 TISPAFRAEQSHTSRHlAEFWMLEAEVAFMTSlSQLTSLMEDMIKYtlnsLMEQNYHRDhwdqLLKPWKCMTYSEAIE 300
Cdd:COG0173 215 QIARCFRDEDLRADRQ-PEFTQLDIEMSFVDQ-EDVFELMEGLIRH----LFKEVLGVE----LPTPFPRMTYAEAME 282
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
18-300 |
1.98e-11 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 66.16 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 18 HNGELISINGWVRSIRKLKNVCFAMVSDGTcqQALQVVTSPEQSKKLSYGASVNIEGQLAVS------------KNAKLG 85
Cdd:PRK12820 16 DTGREVCLAGWVDAFRDHGELLFIHLRDRN--GFIQAVFSPEAAPADVYELAASLRAEFCVAlqgevqkrleetENPHIE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 86 LQQYELLAEKIKIYGQINDDNYPIQKKHLT-----------TEMLR-QIPHLRLRTAKQGEIFRLRSDSLKALRQFFSSK 153
Cdd:PRK12820 94 TGDIEVFVRELSILAASEALPFAISDKAMTagagsagadavNEDLRlQYRYLDIRRPAMQDHLAKRHRIIKCARDFLDSR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 154 DFTETNPPIITSSDCEGAGEVftLTPQETHKnksferddqKHFFDRPAfltvSTQLHLEALAL-GLSRVYTISPAFRAEQ 232
Cdd:PRK12820 174 GFLEIETPILTKSTPEGARDY--LVPSRIHP---------KEFYALPQ----SPQLFKQLLMIaGFERYFQLARCFRDED 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 233 SHTSRHlAEFWMLEAEVAFMTSlSQLTSLMEDMI--KYTLNSLmeqnyhrdhwdQLLKPWKCMTYSEAIE 300
Cdd:PRK12820 239 LRPNRQ-PEFTQLDIEASFIDE-EFIFELIEELTarMFAIGGI-----------ALPRPFPRMPYAEAMD 295
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
23-433 |
1.65e-10 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 63.13 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 23 ISINGWVRSIRKLKNVCFAMV-SDGTcqqALQVVT------SPEQSKKLSygASVNI--------------EGQLAVSKN 81
Cdd:PTZ00385 110 VRVAGRVTSVRDIGKIIFVTIrSNGN---ELQVVGqvgehfTREDLKKLK--VSLRVgdiigadgvpcrmqRGELSVAAS 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 82 AKLGLQQY----ELLAEKIKIYGQINDDNypIQKKHLTTEMLRQIPHLrlrtakqgEIFRLRSDSLKALRQFFSSKDFTE 157
Cdd:PTZ00385 185 RMLILSPYvctdQVVCPNLRGFTVLQDND--VKYRYRFTDMMTNPCVI--------ETIKKRHVMLQALRDYFNERNFVE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 158 TNPPIITSSDCEGAGEVFTltpqeTHKNKSferddqkhffDRPAFLTVSTQLHL-EALALGLSRVYTISPAFRAEQSHTS 236
Cdd:PTZ00385 255 VETPVLHTVASGANAKSFV-----THHNAN----------AMDLFLRVAPELHLkQCIVGGMERIYEIGKVFRNEDADRS 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 237 rHLAEFWMLEAEVAFMTsLSQLTSLMEDMIKY--------TLNSLMEQNYHRDHWD-QLLKPWKCMTYSEAIEELSAVkk 307
Cdd:PTZ00385 320 -HNPEFTSCEFYAAYHT-YEDLMPMTEDIFRQlamrvngtTVVQIYPENAHGNPVTvDLGKPFRRVSVYDEIQRMSGV-- 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 308 twKYPPKwgNDLSSEHE-KYLCEILHK----------------------------TPVFVTDYPQKIKPFYMK-SSGPDT 357
Cdd:PTZ00385 396 --EFPPP--NELNTPKGiAYMSVVMLRyniplppvrtaakmfeklidffitdrvvEPTFVMDHPLFMSPLAKEqVSRPGL 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 358 VAAVDLLVPQVGELAGGSLRKDHLDEYKTYPPEL--------------QWYLDLMKYSNAPHGGFGLGIERLIAFLEGeN 423
Cdd:PTZ00385 472 AERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLvdrqggdeeampldETFLKSLQVGLPPTAGWGMGIDRALMLLTN-S 550
|
490
....*....|
gi 19111871 424 TNVKETIPFP 433
Cdd:PTZ00385 551 SNIRDGIIFP 560
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
23-98 |
2.99e-07 |
|
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: 47.61 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 23 ISINGWVRSI-RKLKNVCFAMVSDGTCQqaLQVVTSPE----QSKKLSYGASVNIEGQLAVSKNAKlglqqYELLAEKIK 97
Cdd:pfam01336 1 VTVAGRVTSIrRSGGKLLFLTLRDGTGS--IQVVVFKEeaekLAKKLKEGDVVRVTGKVKKRKGGE-----LELVVEEIE 73
|
.
gi 19111871 98 I 98
Cdd:pfam01336 74 L 74
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
19-98 |
1.37e-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: 43.84 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 19 NGELISINGWVRSIRKLKNVCFAMVSD--GTCQqalqvVTSP---------EQSKKLSYGASVNIEGQLAVSKNAKLGlq 87
Cdd:cd04316 11 DGEEVTVAGWVHEIRDLGGIKFVILRDreGIVQ-----VTAPkkkvdkelfKTVRKLSRESVISVTGTVKAEPKAPNG-- 83
|
90
....*....|.
gi 19111871 88 qYELLAEKIKI 98
Cdd:cd04316 84 -VEIIPEEIEV 93
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
23-100 |
1.63e-05 |
|
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and Saccharomyces cerevisiae cytoplasmic asparaginyl-tRNA synthetase (AsnRS), in Brugia malayai AsnRs and, in various putative bacterial AsnRSs. 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 synthesis, whereas the other exclusively with mitochondrial protein synthesis. AsnRS is immunodominant antigen of the filarial nematode B. malayai and 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: 239818 [Multi-domain] Cd Length: 84 Bit Score: 42.99 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 23 ISINGWVRSIRKLKNVCFAMVSDGT----CQQALQVVTSPEQSKKLSYGASVNIEGQL---AVSKNAKLGlqqYELLAEK 95
Cdd:cd04323 2 VKVFGWVHRLRSQKKLMFLVLRDGTgflqCVLSKKLVTEFYDAKSLTQESSVEVTGEVkedPRAKQAPGG---YELQVDY 78
|
....*
gi 19111871 96 IKIYG 100
Cdd:cd04323 79 LEIIG 83
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
18-128 |
8.20e-04 |
|
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: 39.43 E-value: 8.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 18 HNGELISINGWVRSIRKLKNVCFAMVSDGTcqQALQVVTSPEQSKKLSYGASVNIEGQLAV----------SKNAKLGLQ 87
Cdd:cd04317 12 HVGQEVTLCGWVQRRRDHGGLIFIDLRDRY--GIVQVVFDPEEAPEFELAEKLRNESVIQVtgkvrarpegTVNPKLPTG 89
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 19111871 88 QYELLAEKIKIYGQINDDNYPIQKKHLTTEMLR-QIPHLRLR 128
Cdd:cd04317 90 EIEVVASELEVLNKAKTLPFEIDDDVNVSEELRlKYRYLDLR 131
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
134-343 |
1.18e-03 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 40.68 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 134 EIFRLRSDSLKALRQFFSSKDFTETNPPII---TSSDCEgagevftLTPQETHKNkSFERDDQKHFFdrpafLTVSTQLH 210
Cdd:PRK09350 3 PNLLKRAKIIAEIRRFFADRGVLEVETPILsqaTVTDIH-------LVPFETRFV-GPGASQGKTLW-----LMTSPEYH 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111871 211 LEA-LALGLSRVYTISPAFRAEQShTSRHLAEFWMLE-AEVAFmtSLSQLTSLMEDMIKYTLNSlmeqnyhrdhwdqllK 288
Cdd:PRK09350 70 MKRlLAAGSGPIFQICKSFRNEEA-GRYHNPEFTMLEwYRPHY--DMYRLMNEVDDLLQQVLDC---------------E 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19111871 289 PWKCMTYSEA------IEELSAVKKTWKY-PPKWG-NDLSSEHEKY--LCEIL----------HKTPVFVTDYPQ 343
Cdd:PRK09350 132 PAESLSYQQAflrylgIDPLSADKTQLREvAAKLGlSNIADEEEDRdtLLQLLftfgvepnigKEKPTFVYHFPA 206
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