|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02853 |
PLN02853 |
Probable phenylalanyl-tRNA synthetase alpha chain |
4-496 |
0e+00 |
|
Probable phenylalanyl-tRNA synthetase alpha chain
Pssm-ID: 215458 [Multi-domain] Cd Length: 492 Bit Score: 764.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 4 DLTERILQHLETTDK-ADTLDLAALFAEDHQKIVGSLKSIQAHGeLVTAETVTHKSLGLTDEGRAVVENGSHEALVYDLV 82
Cdd:PLN02853 3 MAEEALLGALSNNEEiSDSGQFAASHGLDHNEVVGVIKSLHGFR-YVDAQDIKRETWVLTEEGKKYAAEGSPEVQLFAAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 83 PPEG-IAQAALMA-AGGANAKVGFSKAMSHGWILVDKSvtpPLVRRKVDTITDVVRNQLQQVALGKGdqLPAKEVADFKK 160
Cdd:PLN02853 82 PAEGsISKDELQKkLDPAVFDIGFKQAMKNKWLEMGGK---PQVSRKVQHVEDEVKELLLAIQEGKE--VDDKDIDALKK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 161 RK-LLQETTTKSFVLARGPEFATTLTKLETDLTVEMLANGLWDQLKFKAYNFDALGAPPTRGHLHPLLKVRTEFRQIFLE 239
Cdd:PLN02853 157 RRkLITLETWKGYSIKKGPNYAPERKKAATDLTREMLQSGDWKDLEFKEYNFNALGAPPEGGHLHPLLKVRQQFRKIFLQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 240 MGFSEMPTNNYVESSFWNFDALYQPQQHPARDAHDTFFVNHPAKSHKFPQDYLERVKKVHSVGGYGSKGYGYDWKLEEAQ 319
Cdd:PLN02853 237 MGFEEMPTNNFVESSFWNFDALFQPQQHPARDSHDTFFLKAPATTRQLPEDYVERVKTVHESGGYGSIGYGYDWKREEAN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 320 KNLLRTHTTAVSARMLYKLANqeGGFKAAKYFSIDKVFRNETLDATHLAEFHQVEGVIADVGLTLGDLIGTLYEFFRKLG 399
Cdd:PLN02853 317 KNLLRTHTTAVSSRMLYKLAQ--KGFKPKRYFSIDRVFRNEAVDRTHLAEFHQVEGLVCDRGLTLGDLIGVLEDFFSRLG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 400 ITQLEFKPAYNPYTEPSMEIFCYHPGLAKWIEVGNSGVFRPEMLLPMGLPENVNVIAWGLSLERPTMIKYGINNIRDLVG 479
Cdd:PLN02853 395 MTKLRFKPAYNPYTEPSMEIFSYHEGLKKWVEVGNSGMFRPEMLLPMGLPEDVNVIAWGLSLERPTMILYGIDNIRDLFG 474
|
490
....*....|....*..
gi 18858079 480 PKVDLKMVEEGPICRLD 496
Cdd:PLN02853 475 HKVDLGLIKRNPICRLG 491
|
|
| tRNA-synt_2d |
pfam01409 |
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ... |
209-489 |
6.95e-116 |
|
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only phenylalanyl-tRNA synthetases. This is the core catalytic domain.
Pssm-ID: 396130 [Multi-domain] Cd Length: 245 Bit Score: 341.10 E-value: 6.95e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 209 YNFDALGAPPTRGHLHPLLKVRTEFRQIFLEMGFSEMPtNNYVESSFWNFDALYQPQQHPARDAHDTFFVNHPAKShkfp 288
Cdd:pfam01409 2 YDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVE-GPEVESDFYNFDALNIPQDHPARDMQDTFYLKKPLKP---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 289 qdylervkkvhsvggygskgygydwkleEAQKNLLRTHTTAVSARMLYKlanqeGGFKAAKYFSIDKVFRNETLDATHLA 368
Cdd:pfam01409 77 ----------------------------VARRLLLRTHTTPVQARTLAK-----KPKPPIKIFSIGRVFRRDQVDATHLP 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 369 EFHQVEGVIADVGLTLGDLIGTLYEFFRKL-GIT-QLEFKPAYNPYTEPSMEIFCYHPGLAKWIEVGNSGVFRPEMLLPM 446
Cdd:pfam01409 124 EFHQVEGLVVDENVTFADLKGVLEEFLRKFfGFEvKVRFRPSYFPFTEPSAEVDVYVCKLGGWLEVGGAGMVHPNVLEAV 203
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 18858079 447 GLPENVNVIAWGLSLERPTMIKYGINNIRDLVGPkvDLKMVEE 489
Cdd:pfam01409 204 GIDEDYSGFAFGLGVERLAMLKYGIDDIRDLYEN--DLRFLRQ 244
|
|
| PheRS_alpha_core |
cd00496 |
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ... |
224-483 |
7.38e-115 |
|
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. While class II aaRSs generally aminoacylate the 3'-OH 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. PheRS is an alpha-2/ beta-2 tetramer.
Pssm-ID: 238277 [Multi-domain] Cd Length: 218 Bit Score: 337.60 E-value: 7.38e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 224 HPLLKVRTEFRQIFLEMGFSEMpTNNYVESSFWNFDALYQPQQHPARDAHDTFFVNHPAKshkfpqdylervkkvhsvgg 303
Cdd:cd00496 1 HPLNKVIEEIEDIFVSMGFTEV-EGPEVETDFYNFDALNIPQDHPARDMQDTFYINDPAR-------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 304 ygskgygydwkleeaqkNLLRTHTTAVSARMLYKLanqeggFKAAKYFSIDKVFRNETLDATHLAEFHQVEGVIADVGLT 383
Cdd:cd00496 60 -----------------LLLRTHTSAVQARALAKL------KPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKGLT 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 384 LGDLIGTLYEFFRKLG--ITQLEFKPAYNPYTEPSMEIFCYHPGLAKWIEVGNSGVFRPEMLLPMGLPENVNVIAWGLSL 461
Cdd:cd00496 117 FADLKGTLEEFAKELFgpITKVRFRPSYFPFTEPSFEVDVYCPGCLGWLEILGCGMVRPEVLENAGIDEEYSGFAFGIGL 196
|
250 260
....*....|....*....|..
gi 18858079 462 ERPTMIKYGINNIRDLVGPKVD 483
Cdd:cd00496 197 ERLAMLKYGIPDIRLFYSNDLR 218
|
|
| pheS |
TIGR00468 |
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ... |
157-491 |
1.82e-105 |
|
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are heterodimeric, with 2 alpha (pheS) and 2 beta (pheT) subunits. This model describes the alpha subunit, which shows some similarity to class II aminoacyl-tRNA ligases. Mitochondrial phenylalanyl-tRNA synthetase is a single polypeptide chain, active as a monomer, and similar to this chain rather than to the beta chain, but excluded from this model. An interesting feature of the alignment of all sequences captured by this model is a deep split between non-spirochete bacterial examples and all other examples; supporting this split is a relative deletion of about 50 residues in the former set between two motifs well conserved throughout the alignment. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273095 [Multi-domain] Cd Length: 293 Bit Score: 316.56 E-value: 1.82e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 157 DFKKRKLLQETTTKSFVLARGPEFATTLTKLETDLTVEMLANGLWDQLKFKAYNFDALGAPPTRGHLHPLLKVRTEFRQI 236
Cdd:TIGR00468 5 LLKQLGKLTKEETKPALGALINEVKIELQDELTKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDEIRDI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 237 FLEMGFSEMPtNNYVESSFWNFDALYQPQQHPARDAHDTFFVNhpakshkfpqdylervkkvhsvggygskgygydwkle 316
Cdd:TIGR00468 85 FLGLGFTEET-GPEVETDFWNFDALNIPQDHPARDMQDTFYIK------------------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 317 eaQKNLLRTHTTAVSARMLyklanQEGGFKAAKYFSIDKVFRNETLDATHLAEFHQVEGVIADVGLTLGDLIGTLYEFFR 396
Cdd:TIGR00468 127 --DRLLLRTHTTAVQLRTM-----EEQEKPPIRIFSPGRVFRNDTVDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLK 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 397 KL-GITQLEFKPAYNPYTEPSMEIFCYHPGLAKWIEVGNSGVFRPEMLLPMGLPENVNVIAWGLSLERPTMIKYGINNIR 475
Cdd:TIGR00468 200 KMfGETEIRFRPSYFPFTEPSAEIDVYCPEGKGWLEVLGAGMFRPEVLEPMGIDPTYPGFAWGIGIERLAMLKYGITDIR 279
|
330
....*....|....*.
gi 18858079 476 DLVGPkvDLKMVEEGP 491
Cdd:TIGR00468 280 DLYEN--DLRFLRQFK 293
|
|
| PheS |
COG0016 |
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ... |
215-478 |
7.22e-58 |
|
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; Phenylalanyl-tRNA synthetase alpha subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439787 [Multi-domain] Cd Length: 339 Bit Score: 194.89 E-value: 7.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 215 GAPPTRGHLHPLLKVRTEFRQIFLEMGFS--EMPtnnYVESSFWNFDALYQPQQHPARDAHDTFFVNhpakshkfpqdyl 292
Cdd:COG0016 98 GRPRPLGSLHPLTQVIEEIEDIFVGMGFEvaEGP---EIETDWYNFEALNIPPDHPARDMQDTFYID------------- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 293 ervkkvhsvggygskgygydwkleeaQKNLLRTHTTAVSAR-MLyklaNQEGGFKAAkyfSIDKVFRNETLDATHLAEFH 371
Cdd:COG0016 162 --------------------------DGLLLRTHTSPVQIRtME----KQKPPIRII---APGRVYRRDESDATHSPMFH 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 372 QVEGVIADVGLTLGDLIGTLYEFFRKL-GI-TQLEFKPAYNPYTEPSMEI-------------FCYHPGlakWIEVGNSG 436
Cdd:COG0016 209 QVEGLVVDKGISFADLKGTLEEFAKAFfGEdVKVRFRPSYFPFTEPSAEVdiscficggkgcrVCKGTG---WLEILGCG 285
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 18858079 437 VFRPEMLLPMGL-PENVNVIAWGLSLERPTMIKYGINNIRDLV 478
Cdd:COG0016 286 MVHPNVLRAVGIdPEEYSGFAFGMGIERLAMLKYGIDDIRLFF 328
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02853 |
PLN02853 |
Probable phenylalanyl-tRNA synthetase alpha chain |
4-496 |
0e+00 |
|
Probable phenylalanyl-tRNA synthetase alpha chain
Pssm-ID: 215458 [Multi-domain] Cd Length: 492 Bit Score: 764.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 4 DLTERILQHLETTDK-ADTLDLAALFAEDHQKIVGSLKSIQAHGeLVTAETVTHKSLGLTDEGRAVVENGSHEALVYDLV 82
Cdd:PLN02853 3 MAEEALLGALSNNEEiSDSGQFAASHGLDHNEVVGVIKSLHGFR-YVDAQDIKRETWVLTEEGKKYAAEGSPEVQLFAAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 83 PPEG-IAQAALMA-AGGANAKVGFSKAMSHGWILVDKSvtpPLVRRKVDTITDVVRNQLQQVALGKGdqLPAKEVADFKK 160
Cdd:PLN02853 82 PAEGsISKDELQKkLDPAVFDIGFKQAMKNKWLEMGGK---PQVSRKVQHVEDEVKELLLAIQEGKE--VDDKDIDALKK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 161 RK-LLQETTTKSFVLARGPEFATTLTKLETDLTVEMLANGLWDQLKFKAYNFDALGAPPTRGHLHPLLKVRTEFRQIFLE 239
Cdd:PLN02853 157 RRkLITLETWKGYSIKKGPNYAPERKKAATDLTREMLQSGDWKDLEFKEYNFNALGAPPEGGHLHPLLKVRQQFRKIFLQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 240 MGFSEMPTNNYVESSFWNFDALYQPQQHPARDAHDTFFVNHPAKSHKFPQDYLERVKKVHSVGGYGSKGYGYDWKLEEAQ 319
Cdd:PLN02853 237 MGFEEMPTNNFVESSFWNFDALFQPQQHPARDSHDTFFLKAPATTRQLPEDYVERVKTVHESGGYGSIGYGYDWKREEAN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 320 KNLLRTHTTAVSARMLYKLANqeGGFKAAKYFSIDKVFRNETLDATHLAEFHQVEGVIADVGLTLGDLIGTLYEFFRKLG 399
Cdd:PLN02853 317 KNLLRTHTTAVSSRMLYKLAQ--KGFKPKRYFSIDRVFRNEAVDRTHLAEFHQVEGLVCDRGLTLGDLIGVLEDFFSRLG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 400 ITQLEFKPAYNPYTEPSMEIFCYHPGLAKWIEVGNSGVFRPEMLLPMGLPENVNVIAWGLSLERPTMIKYGINNIRDLVG 479
Cdd:PLN02853 395 MTKLRFKPAYNPYTEPSMEIFSYHEGLKKWVEVGNSGMFRPEMLLPMGLPEDVNVIAWGLSLERPTMILYGIDNIRDLFG 474
|
490
....*....|....*..
gi 18858079 480 PKVDLKMVEEGPICRLD 496
Cdd:PLN02853 475 HKVDLGLIKRNPICRLG 491
|
|
| PTZ00326 |
PTZ00326 |
phenylalanyl-tRNA synthetase alpha chain; Provisional |
1-484 |
0e+00 |
|
phenylalanyl-tRNA synthetase alpha chain; Provisional
Pssm-ID: 240361 [Multi-domain] Cd Length: 494 Bit Score: 731.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 1 MHPDLTERILQHLETTDKA-DTLDLAALFAEDHQKIVGSLKSIQAhGELVTAETVTHKSLGLTDEGRAVVENGSHEALVY 79
Cdd:PTZ00326 3 QKELEENTILSKLESENEIvNSLALAESLNIDHQKVVGAIKSLES-ANYITTEMKKSNTWTLTEEGEDYLKNGSPEYRLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 80 DLVPPEGIAQAALMA-AGGANAKVGFSKAMSHGWILVDKSV-TPPLVRRKVDTITDVVRNQLQQVALG-KGDQLPAKEVA 156
Cdd:PTZ00326 82 QKLKEGGISKADDAKkLGGKVADIGLGNAMKKKWIKLNKGDkKVFLSRKLVDSVVDTVRLLLKIVAKGsQAEKIDSKELK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 157 DFKKRKLLQETTTKSFVLARGPEFATTLTKLETDLTVEMLANGLWDQLKFKAYNFDALGAPPTRGHLHPLLKVRTEFRQI 236
Cdd:PTZ00326 162 ELKKRKLATLEKIKYFVVTKGPKFAKEIKKQITDLTQEMLLNGSWKNAEFKEYNFNALGKKIGGGNLHPLLKVRREFREI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 237 FLEMGFSEMPTNNYVESSFWNFDALYQPQQHPARDAHDTFFVNHPAKSH--KFPQDYLERVKKVHSVGGYGSKGYGYDWK 314
Cdd:PTZ00326 242 LLEMGFEEMPTNRYVESSFWNFDALFQPQQHPARDAQDTFFLSKPETSKvnDLDDDYVERVKKVHEVGGYGSIGWRYDWK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 315 LEEAQKNLLRTHTTAVSARMLYKLANQ---EGGFKAAKYFSIDKVFRNETLDATHLAEFHQVEGVIADVGLTLGDLIGTL 391
Cdd:PTZ00326 322 LEEARKNILRTHTTAVSARMLYKLAQEykkTGPFKPKKYFSIDRVFRNETLDATHLAEFHQVEGFVIDRNLTLGDLIGTI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 392 YEFFRKLGITQLEFKPAYNPYTEPSMEIFCYHPGLAKWIEVGNSGVFRPEMLLPMGLPENVNVIAWGLSLERPTMIKYGI 471
Cdd:PTZ00326 402 REFFRRIGITKLRFKPAFNPYTEPSMEIFGYHPGLKKWVEVGNSGIFRPEMLRPMGFPEDVTVIAWGLSLERPTMIKYGI 481
|
490
....*....|...
gi 18858079 472 NNIRDLVGPKVDL 484
Cdd:PTZ00326 482 KNIRDLFGHKVDL 494
|
|
| pheS |
PRK04172 |
phenylalanine--tRNA ligase subunit alpha; |
8-491 |
4.47e-141 |
|
phenylalanine--tRNA ligase subunit alpha;
Pssm-ID: 235239 [Multi-domain] Cd Length: 489 Bit Score: 414.61 E-value: 4.47e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 8 RILQHLETTDKADTLDLAALFAEDHQKIVGSLKSIQAHGeLVTAETVTHKSLGLTDEGRAVVENGSHEALVYDLVPPEG- 86
Cdd:PRK04172 10 KVLKALKELKEATLEELAEKLGLPPEAVMRAAEWLEEKG-LVKVEERVEEVYVLTEEGKKYAEEGLPERRLLNALKDGGe 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 87 --IAQAALMAAGGANAKVGFSKAMSHGWILVDKSVtpplVRRKVDTITDVVRNQLQQVALGKGDQLP---AKEVADFKKR 161
Cdd:PRK04172 89 vsLDELKEALLDKKEVGIALGNLARKGWAKIEKGK----VILKPDAYEDPEEKALKALAEGDKEELSeedLKVLKELKKR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 162 KLLQ--ETTTKSFVLA-RGPEFATTLTKLE---TDLTVEMLANGLWDQLKFKAYNFDALGAPPTRGHLHPLLKVRTEFRQ 235
Cdd:PRK04172 165 KLVEekERTERSVELTdAGLELLKEGIELKeeiTQLTPELLKSGEWKEKEFRPYNVKAPPPKIYPGKKHPYREFIDEVRD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 236 IFLEMGFSEMpTNNYVESSFWNFDALYQPQQHPARDAHDTFFVNHPAKsHKFPQDYLERVKKVHSVGGYGSKGY-GYDWK 314
Cdd:PRK04172 245 ILVEMGFEEM-KGPLVETEFWNFDALFQPQDHPAREMQDTFYLKYPGI-GDLPEELVERVKEVHEHGGDTGSRGwGYKWD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 315 LEEAQKNLLRTHTTAVSARMLYKLANQEGgfkaaKYFSIDKVFRNETLDATHLAEFHQVEGVIADVGLTLGDLIGTLYEF 394
Cdd:PRK04172 323 EDIAKRLVLRTHTTALSARYLASRPEPPQ-----KYFSIGRVFRPDTIDATHLPEFYQLEGIVMGEDVSFRDLLGILKEF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 395 FRKLGITQLEFKPAYNPYTEPSMEIFCYHPGLaKWIEVGNSGVFRPEMLLPMGLpeNVNVIAWGLSLERPTMIKYGINNI 474
Cdd:PRK04172 398 YKRLGFEEVKFRPAYFPFTEPSVEVEVYHEGL-GWVELGGAGIFRPEVLEPLGI--DVPVLAWGLGIERLAMLRLGLDDI 474
|
490
....*....|....*..
gi 18858079 475 RDLVGPkvDLKMVEEGP 491
Cdd:PRK04172 475 RDLYSS--DIEWLRERP 489
|
|
| tRNA-synt_2d |
pfam01409 |
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ... |
209-489 |
6.95e-116 |
|
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only phenylalanyl-tRNA synthetases. This is the core catalytic domain.
Pssm-ID: 396130 [Multi-domain] Cd Length: 245 Bit Score: 341.10 E-value: 6.95e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 209 YNFDALGAPPTRGHLHPLLKVRTEFRQIFLEMGFSEMPtNNYVESSFWNFDALYQPQQHPARDAHDTFFVNHPAKShkfp 288
Cdd:pfam01409 2 YDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVE-GPEVESDFYNFDALNIPQDHPARDMQDTFYLKKPLKP---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 289 qdylervkkvhsvggygskgygydwkleEAQKNLLRTHTTAVSARMLYKlanqeGGFKAAKYFSIDKVFRNETLDATHLA 368
Cdd:pfam01409 77 ----------------------------VARRLLLRTHTTPVQARTLAK-----KPKPPIKIFSIGRVFRRDQVDATHLP 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 369 EFHQVEGVIADVGLTLGDLIGTLYEFFRKL-GIT-QLEFKPAYNPYTEPSMEIFCYHPGLAKWIEVGNSGVFRPEMLLPM 446
Cdd:pfam01409 124 EFHQVEGLVVDENVTFADLKGVLEEFLRKFfGFEvKVRFRPSYFPFTEPSAEVDVYVCKLGGWLEVGGAGMVHPNVLEAV 203
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 18858079 447 GLPENVNVIAWGLSLERPTMIKYGINNIRDLVGPkvDLKMVEE 489
Cdd:pfam01409 204 GIDEDYSGFAFGLGVERLAMLKYGIDDIRDLYEN--DLRFLRQ 244
|
|
| PheRS_alpha_core |
cd00496 |
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ... |
224-483 |
7.38e-115 |
|
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. While class II aaRSs generally aminoacylate the 3'-OH 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. PheRS is an alpha-2/ beta-2 tetramer.
Pssm-ID: 238277 [Multi-domain] Cd Length: 218 Bit Score: 337.60 E-value: 7.38e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 224 HPLLKVRTEFRQIFLEMGFSEMpTNNYVESSFWNFDALYQPQQHPARDAHDTFFVNHPAKshkfpqdylervkkvhsvgg 303
Cdd:cd00496 1 HPLNKVIEEIEDIFVSMGFTEV-EGPEVETDFYNFDALNIPQDHPARDMQDTFYINDPAR-------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 304 ygskgygydwkleeaqkNLLRTHTTAVSARMLYKLanqeggFKAAKYFSIDKVFRNETLDATHLAEFHQVEGVIADVGLT 383
Cdd:cd00496 60 -----------------LLLRTHTSAVQARALAKL------KPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKGLT 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 384 LGDLIGTLYEFFRKLG--ITQLEFKPAYNPYTEPSMEIFCYHPGLAKWIEVGNSGVFRPEMLLPMGLPENVNVIAWGLSL 461
Cdd:cd00496 117 FADLKGTLEEFAKELFgpITKVRFRPSYFPFTEPSFEVDVYCPGCLGWLEILGCGMVRPEVLENAGIDEEYSGFAFGIGL 196
|
250 260
....*....|....*....|..
gi 18858079 462 ERPTMIKYGINNIRDLVGPKVD 483
Cdd:cd00496 197 ERLAMLKYGIPDIRLFYSNDLR 218
|
|
| pheS |
TIGR00468 |
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ... |
157-491 |
1.82e-105 |
|
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are heterodimeric, with 2 alpha (pheS) and 2 beta (pheT) subunits. This model describes the alpha subunit, which shows some similarity to class II aminoacyl-tRNA ligases. Mitochondrial phenylalanyl-tRNA synthetase is a single polypeptide chain, active as a monomer, and similar to this chain rather than to the beta chain, but excluded from this model. An interesting feature of the alignment of all sequences captured by this model is a deep split between non-spirochete bacterial examples and all other examples; supporting this split is a relative deletion of about 50 residues in the former set between two motifs well conserved throughout the alignment. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273095 [Multi-domain] Cd Length: 293 Bit Score: 316.56 E-value: 1.82e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 157 DFKKRKLLQETTTKSFVLARGPEFATTLTKLETDLTVEMLANGLWDQLKFKAYNFDALGAPPTRGHLHPLLKVRTEFRQI 236
Cdd:TIGR00468 5 LLKQLGKLTKEETKPALGALINEVKIELQDELTKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDEIRDI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 237 FLEMGFSEMPtNNYVESSFWNFDALYQPQQHPARDAHDTFFVNhpakshkfpqdylervkkvhsvggygskgygydwkle 316
Cdd:TIGR00468 85 FLGLGFTEET-GPEVETDFWNFDALNIPQDHPARDMQDTFYIK------------------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 317 eaQKNLLRTHTTAVSARMLyklanQEGGFKAAKYFSIDKVFRNETLDATHLAEFHQVEGVIADVGLTLGDLIGTLYEFFR 396
Cdd:TIGR00468 127 --DRLLLRTHTTAVQLRTM-----EEQEKPPIRIFSPGRVFRNDTVDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLK 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 397 KL-GITQLEFKPAYNPYTEPSMEIFCYHPGLAKWIEVGNSGVFRPEMLLPMGLPENVNVIAWGLSLERPTMIKYGINNIR 475
Cdd:TIGR00468 200 KMfGETEIRFRPSYFPFTEPSAEIDVYCPEGKGWLEVLGAGMFRPEVLEPMGIDPTYPGFAWGIGIERLAMLKYGITDIR 279
|
330
....*....|....*.
gi 18858079 476 DLVGPkvDLKMVEEGP 491
Cdd:TIGR00468 280 DLYEN--DLRFLRQFK 293
|
|
| PheS |
COG0016 |
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ... |
215-478 |
7.22e-58 |
|
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; Phenylalanyl-tRNA synthetase alpha subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439787 [Multi-domain] Cd Length: 339 Bit Score: 194.89 E-value: 7.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 215 GAPPTRGHLHPLLKVRTEFRQIFLEMGFS--EMPtnnYVESSFWNFDALYQPQQHPARDAHDTFFVNhpakshkfpqdyl 292
Cdd:COG0016 98 GRPRPLGSLHPLTQVIEEIEDIFVGMGFEvaEGP---EIETDWYNFEALNIPPDHPARDMQDTFYID------------- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 293 ervkkvhsvggygskgygydwkleeaQKNLLRTHTTAVSAR-MLyklaNQEGGFKAAkyfSIDKVFRNETLDATHLAEFH 371
Cdd:COG0016 162 --------------------------DGLLLRTHTSPVQIRtME----KQKPPIRII---APGRVYRRDESDATHSPMFH 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 372 QVEGVIADVGLTLGDLIGTLYEFFRKL-GI-TQLEFKPAYNPYTEPSMEI-------------FCYHPGlakWIEVGNSG 436
Cdd:COG0016 209 QVEGLVVDKGISFADLKGTLEEFAKAFfGEdVKVRFRPSYFPFTEPSAEVdiscficggkgcrVCKGTG---WLEILGCG 285
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 18858079 437 VFRPEMLLPMGL-PENVNVIAWGLSLERPTMIKYGINNIRDLV 478
Cdd:COG0016 286 MVHPNVLRAVGIdPEEYSGFAFGMGIERLAMLKYGIDDIRLFF 328
|
|
| PheRS_DBD1 |
pfam18552 |
PheRS DNA binding domain 1; This is a DNA-binding fold domain found in Phenylalanyl-tRNA ... |
1-59 |
7.74e-25 |
|
PheRS DNA binding domain 1; This is a DNA-binding fold domain found in Phenylalanyl-tRNA Synthetase (EC:6.1.1.20) N-terminal region. This domain belongs to a superfamily of 'winged helix' DNA-biding domains. The topology of DBD-1 and DBD-3 closely resembles the topology of the Z-DNA-binding domain Zalpha of double-stranded RNA (dsRNA) adenosine deaminase and other domains from DNA-binding proteins. Mutational analysis indicate that DBD-1, 2 and 3 play critical roles in tRNA-Phe binding and recognition, i.e., from the drastic reduction of aminoacylation activity seen upon removal of the N-terminal domains.
Pssm-ID: 465796 [Multi-domain] Cd Length: 59 Bit Score: 96.87 E-value: 7.74e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 18858079 1 MHPDLTERILQHLETTDKADTLDLAALFAEDHQKIVGSLKSIQAHGELVTAETVTHKSL 59
Cdd:pfam18552 1 MDKDLEEQILQYLEKHGGVDSLDLAAELGVDHQKVVGAVKSLQALGDVITAEQRSSKHW 59
|
|
| PLN02788 |
PLN02788 |
phenylalanine-tRNA synthetase |
211-475 |
1.44e-21 |
|
phenylalanine-tRNA synthetase
Pssm-ID: 215422 [Multi-domain] Cd Length: 402 Bit Score: 96.76 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 211 FDALGAPPTRGHLHPLLKVRTEFRQIFlemgfSEMPTNNY--------VESSFWNFDALYQPQQHPARDAHDTFFVNhpa 282
Cdd:PLN02788 55 FSKIGMQLHRRPDHPLGILKNAIYDYF-----DENYSNKFkkfddlspIVSTKQNFDDVLVPPDHVSRSYNDTYYVD--- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 283 kshkfpqdylervkkvhsvggygskgygydwkleeaQKNLLRTHTTAVSARMLyklanQEGgfkAAKYFSIDKVFRNETL 362
Cdd:PLN02788 127 ------------------------------------AQTVLRCHTSAHQAELL-----RAG---HTHFLVTGDVYRRDSI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 363 DATHLAEFHQVEGV-------IADVGLT-----LGDLIGTLYEFFRKL-GITQLEFKPAYNPYTEPSMEIFCYHPGlaKW 429
Cdd:PLN02788 163 DATHYPVFHQMEGVrvfspeeWEASGLDgtdlaAEDLKKTLEGLARHLfGDVEMRWVDAYFPFTNPSFELEIFFKG--EW 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 18858079 430 IEVGNSGVFRPEMLLPMGLPENVnviAW--GLSLERPTMIKYGINNIR 475
Cdd:PLN02788 241 LEVLGCGVTEQEILKNNGRSDNV---AWafGLGLERLAMVLFDIPDIR 285
|
|
| sepS |
TIGR00470 |
O-phosphoserine--tRNA ligase; This family of archaeal proteins resembles known ... |
349-482 |
9.99e-18 |
|
O-phosphoserine--tRNA ligase; This family of archaeal proteins resembles known phenylalanyl-tRNA synthetase alpha chains. Recently, it was shown to act in a proposed pathway of tRNA(Cys) indirect aminoacylation, resulting in Cys biosynthesis from O-phosphoserine, in certain archaea. It charges tRNA(Cys) with O-phosphoserine. The pscS gene product converts the phosphoserine to Cys. [Amino acid biosynthesis, Serine family, Protein synthesis, tRNA aminoacylation]
Pssm-ID: 129562 [Multi-domain] Cd Length: 533 Bit Score: 85.70 E-value: 9.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 349 KYFSIDKVFRNETL-DATHLAEFHQVEGVIADVGLTLGDLIGTLYEFFRKLGITQLEFKPA------YNPYTEpsMEIFC 421
Cdd:TIGR00470 209 KLFSIDRCFRREQReDRSHLMTYHSASCVVVDEEVSVDDGKAVAEGLLAQFGFTKFRFRPDekkskyYIPETQ--TEVYA 286
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18858079 422 YHPGLAKWIEVGNSGVFRPEMLLPMGLPenVNVIAWGLSLERPTMIKYGINNIRDLVGPKV 482
Cdd:TIGR00470 287 YHPKLGEWIEVATFGVYSPIALAKYNID--VPVMNLGLGVERLAMILYGYEDVRAMVYPQI 345
|
|
| PheRS_DBD3 |
pfam18553 |
PheRS DNA binding domain 3; This is a DNA-binding fold domain found in Phenylalanyl-tRNA ... |
73-130 |
1.03e-16 |
|
PheRS DNA binding domain 3; This is a DNA-binding fold domain found in Phenylalanyl-tRNA Synthetase N-terminal region. This domain belongs to a superfamily of 'winged helix' DNA-biding domains. The topology of DBD-1 and DBD-3 closely resembles the topology of the Z-DNA-binding domain Zalpha of double-stranded RNA (dsRNA) adenosine deaminase and other domains from DNA-binding proteins. Mutational analysis indicate that DBD-1, 2 and 3 play critical roles in tRNAPhe binding and recognition, i.e., from the drastic reduction of aminoacylation activity seen upon removal of the N-terminal domains.
Pssm-ID: 465797 [Multi-domain] Cd Length: 57 Bit Score: 74.23 E-value: 1.03e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 18858079 73 SHEALVYDLVPP-EGIAQAALMAAGGANAKVGFSKAMSHGWILVDKSVTppLVRRKVDT 130
Cdd:pfam18553 1 SPEARVFNAVPPaGGISLKELMKLGDSVAKVGFGKAMKNKWIKKDKGDG--KVVRKVDS 57
|
|
| pheS_mito |
TIGR00469 |
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ... |
242-475 |
9.96e-12 |
|
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA synthetases, the mitochondrial form demonstrated from yeast is monomeric. It is similar to but longer than the alpha subunit (PheS) of the alpha 2 beta 2 form found in Bacteria, Archaea, and eukaryotes, and shares the characteristic motifs of class II aminoacyl-tRNA ligases. This model models the experimental example from Saccharomyces cerevisiae (designated MSF1) and its orthologs from other eukaryotic species. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 129561 [Multi-domain] Cd Length: 460 Bit Score: 67.02 E-value: 9.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 242 FSEMPTNNYVESSFWNFDALYQPQQHPARDAHDTFFVNhpakshkfpqdylervkkvhsvggygskgygydwkleeaQKN 321
Cdd:TIGR00469 68 FKIFDNFKPVVTTMENFDNLGFPADHPGRQKSDCYYIN---------------------------------------EQH 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 322 LLRTHTTAVSARMLYKLANQEGGFKAAKYFSIDkVFRNETLDATHLAEFHQVEGVI------ADVG-------------- 381
Cdd:TIGR00469 109 LLRAHTSAHELECFQGGLDDSDNIKSGFLISAD-VYRRDEIDKTHYPVFHQADGAAirkrtkADLFekepgyiekfeedi 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 382 -------------LTLGD------------------------------LIGTLYEFF---------RKLGITQLEFK--- 406
Cdd:TIGR00469 188 rgteadlnkenvkIILDDdsiplkennpkqeyasdlavdlcehelkhsIEGITKDLFgkkissmikNKANNTPKELKvrw 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18858079 407 -PAYNPYTEPSMEIFCYHPGlaKWIEVGNSGVFRPEMLLPMGLPENVNV-IAWGLSLERPTMIKYGINNIR 475
Cdd:TIGR00469 268 iDAYFPFTAPSWEIEIWFKD--EWLELCGCGIIRHDILLRAGVHPSETIgWAFGLGLDRIAMLLFDIPDIR 336
|
|
| PheRS_DBD2 |
pfam18554 |
PheRS DNA binding domain 2; This is a DNA-binding fold domain found in Phenylalanyl-tRNA ... |
133-165 |
1.74e-11 |
|
PheRS DNA binding domain 2; This is a DNA-binding fold domain found in Phenylalanyl-tRNA Synthetase N-terminal region. Mutational analysis indicate that DBD-1, 2 and 3 play critical roles in tRNA- Phe binding and recognition, i.e., from the drastic reduction of aminoacylation activity seen upon removal of the N-terminal domains. DBD-2 and DBD-3 constitute large insertions sequentially included between two neighboring antiparallel strands of the DBD-1 domain. Moreover, the DBD-3 pfam18553 is the domain insertion into DBD-2.
Pssm-ID: 465798 [Multi-domain] Cd Length: 33 Bit Score: 58.57 E-value: 1.74e-11
10 20 30
....*....|....*....|....*....|...
gi 18858079 133 DVVRNQLQQVALGKGDQLPAKEVADFKKRKLLQ 165
Cdd:pfam18554 1 DEVQEQLKLIQEGKGDSLSDKVKNELKKRKLLQ 33
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
323-464 |
2.07e-09 |
|
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: 57.51 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 323 LRTHTTAVSARMLYKLANQEGgfkaAKYFSIDKVFRNE--TLDATHLAEFHQVEGVIA--DVGLTLGD--LIGTLYEFFR 396
Cdd:cd00768 55 LRPTLEPGLVRLFVSHIRKLP----LRLAEIGPAFRNEggRRGLRRVREFTQLEGEVFgeDGEEASEFeeLIELTEELLR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 397 KLGI---------TQLEFKPAYNpytEPSMEIFCYHPgLAKWIEVGNSGVFRPE--------MLLPMGLPENVNVIAWGL 459
Cdd:cd00768 131 ALGIkldivfvekTPGEFSPGGA---GPGFEIEVDHP-EGRGLEIGSGGYRQDEqaraadlyFLDEALEYRYPPTIGFGL 206
|
....*
gi 18858079 460 SLERP 464
Cdd:cd00768 207 GLERL 211
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
343-422 |
6.57e-04 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 41.78 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 343 GGFKaaKYFSIDKVFRNETLDATHLAEFHQV----------------EGVIADV-----GLTLGDLIGTLYEFfrKLGIT 401
Cdd:pfam00152 88 AGFD--RVFQIARCFRDEDLRTDRQPEFTQLdlemsfvdyedvmdltEELIKEIfkeveGIAKELEGGTLLDL--KKPFP 163
|
90 100
....*....|....*....|.
gi 18858079 402 QLEFKPAYNPYTEPSMEIFCY 422
Cdd:pfam00152 164 RITYAEAIEKLNGKDVEELGY 184
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
327-406 |
4.06e-03 |
|
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA. This domain 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. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.
Pssm-ID: 238396 [Multi-domain] Cd Length: 261 Bit Score: 39.12 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858079 327 TTAVsARMLykLANQEGGFKAAKYFSIDKVFRNETLDATHLAEFHQV-------EGVIADVgltlgDLIGTLYEFFRKLG 399
Cdd:cd00773 65 TAPV-ARAV--AENLLSLPLPLKLYYIGPVFRYERPQKGRYREFYQVgveiigsDSPLADA-----EVIALAVEILEALG 136
|
....*..
gi 18858079 400 ITQLEFK 406
Cdd:cd00773 137 LKDFQIK 143
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
349-406 |
5.18e-03 |
|
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439894 [Multi-domain] Cd Length: 422 Bit Score: 39.33 E-value: 5.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18858079 349 KYFSIDKVFRNETLDATHLAEFHQV-------EGVIADVgltlgDLIGTLYEFFRKLGITQLEFK 406
Cdd:COG0124 101 KLYYIGPVFRYERPQKGRYRQFHQFgvevigsDSPLADA-----EVIALAADLLKALGLKDFTLE 160
|
|
| |
