NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|14318497|ref|NP_116631|]
View 

phenylalanine--tRNA ligase subunit alpha [Saccharomyces cerevisiae S288C]

Protein Classification

phenylalanine--tRNA ligase alpha subunit( domain architecture ID 1003922)

phenylalanine--tRNA ligase alpha subunit catalyzes a two-step reaction, first charging a phenylalanine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; forms a heterotetramer of alpha(2)beta(2); binds two magnesium ions per tetramer

EC:  6.1.1.20
Gene Ontology:  GO:0004826|GO:0006432|GO:0005524|GO:0000049
PubMed:  20223217

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PTZ00326 super family cl30525
phenylalanyl-tRNA synthetase alpha chain; Provisional
 1-486 0e+00

phenylalanyl-tRNA synthetase alpha chain; Provisional


The actual alignment was detected with superfamily member PTZ00326:

Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 685.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497    1 MSDFQLEILKKLDELDEIKSTLATFPQHGS--QDVLSALNSLKAHNKLEFSKVDTVTYDLTKEGAQILNEGSYEIKLVKL 78
Cdd:PTZ00326   4 KELEENTILSKLESENEIVNSLALAESLNIdhQKVVGAIKSLESANYITTEMKKSNTWTLTEEGEDYLKNGSPEYRLWQK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   79 IQELGQLQIkDVMSKLGPQVGKVGQARAFKNGWIAKNASN-ELELSAKLqntdLNELTDETQSILAQIKNNSHLDSIDAK 157
Cdd:PTZ00326  84 LKEGGISKA-DDAKKLGGKVADIGLGNAMKKKWIKLNKGDkKVFLSRKL----VDSVVDTVRLLLKIVAKGSQAEKIDSK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497  158 ILNDLKKRKLIAQGKITDFNVTKGPEFSTDLTKLETDLTSDMVSTNAYKDLKFKPYNFNSQGVQISSGALHPLNKVREEF 237
Cdd:PTZ00326 159 ELKELKKRKLATLEKIKYFVVTKGPKFAKEIKKQITDLTQEMLLNGSWKNAEFKEYNFNALGKKIGGGNLHPLLKVRREF 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497  238 RQIFFSMGFTEMPSNQYVETGFWNFDALYVPQQHPARDLQDTFYIKDPLTADLPD-DKTYMDNIKAVHEQGRFGSIGYRY 316
Cdd:PTZ00326 239 REILLEMGFEEMPTNRYVESSFWNFDALFQPQQHPARDAQDTFFLSKPETSKVNDlDDDYVERVKKVHEVGGYGSIGWRY 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497  317 NWKPEECQKLVLRTHSTAISARMLHDLAKDP------KPTRLFSIDRVFRNEAVDATHLAEFHQVEGVLADYNITLGDLI 390
Cdd:PTZ00326 319 DWKLEEARKNILRTHTTAVSARMLYKLAQEYkktgpfKPKKYFSIDRVFRNETLDATHLAEFHQVEGFVIDRNLTLGDLI 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497  391 KFMEEFFERMGVTGLRFKPTYNPYTEPSMEIFSWHEGLQKWVEIGNSGMFRPEMLESMGLPKDLRVLGWGLSLERPTMIK 470
Cdd:PTZ00326 399 GTIREFFRRIGITKLRFKPAFNPYTEPSMEIFGYHPGLKKWVEVGNSGIFRPEMLRPMGFPEDVTVIAWGLSLERPTMIK 478

                        490
                 ....*....|....*.
gi 14318497  471 YKVQNIRELLGHKVSL 486
Cdd:PTZ00326 479 YGIKNIRDLFGHKVDL 494
 
Name Accession Description Interval E-value
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 1-486 0e+00

phenylalanyl-tRNA synthetase alpha chain; Provisional


Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 685.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497    1 MSDFQLEILKKLDELDEIKSTLATFPQHGS--QDVLSALNSLKAHNKLEFSKVDTVTYDLTKEGAQILNEGSYEIKLVKL 78
Cdd:PTZ00326   4 KELEENTILSKLESENEIVNSLALAESLNIdhQKVVGAIKSLESANYITTEMKKSNTWTLTEEGEDYLKNGSPEYRLWQK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   79 IQELGQLQIkDVMSKLGPQVGKVGQARAFKNGWIAKNASN-ELELSAKLqntdLNELTDETQSILAQIKNNSHLDSIDAK 157
Cdd:PTZ00326  84 LKEGGISKA-DDAKKLGGKVADIGLGNAMKKKWIKLNKGDkKVFLSRKL----VDSVVDTVRLLLKIVAKGSQAEKIDSK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497  158 ILNDLKKRKLIAQGKITDFNVTKGPEFSTDLTKLETDLTSDMVSTNAYKDLKFKPYNFNSQGVQISSGALHPLNKVREEF 237
Cdd:PTZ00326 159 ELKELKKRKLATLEKIKYFVVTKGPKFAKEIKKQITDLTQEMLLNGSWKNAEFKEYNFNALGKKIGGGNLHPLLKVRREF 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497  238 RQIFFSMGFTEMPSNQYVETGFWNFDALYVPQQHPARDLQDTFYIKDPLTADLPD-DKTYMDNIKAVHEQGRFGSIGYRY 316
Cdd:PTZ00326 239 REILLEMGFEEMPTNRYVESSFWNFDALFQPQQHPARDAQDTFFLSKPETSKVNDlDDDYVERVKKVHEVGGYGSIGWRY 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497  317 NWKPEECQKLVLRTHSTAISARMLHDLAKDP------KPTRLFSIDRVFRNEAVDATHLAEFHQVEGVLADYNITLGDLI 390
Cdd:PTZ00326 319 DWKLEEARKNILRTHTTAVSARMLYKLAQEYkktgpfKPKKYFSIDRVFRNETLDATHLAEFHQVEGFVIDRNLTLGDLI 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497  391 KFMEEFFERMGVTGLRFKPTYNPYTEPSMEIFSWHEGLQKWVEIGNSGMFRPEMLESMGLPKDLRVLGWGLSLERPTMIK 470
Cdd:PTZ00326 399 GTIREFFRRIGITKLRFKPAFNPYTEPSMEIFGYHPGLKKWVEVGNSGIFRPEMLRPMGFPEDVTVIAWGLSLERPTMIK 478

                        490
                 ....*....|....*.
gi 14318497  471 YKVQNIRELLGHKVSL 486
Cdd:PTZ00326 479 YGIKNIRDLFGHKVDL 494
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 152-493 1.83e-130

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: 380.50  E-value: 1.83e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   152 DSIDAKILNDLKKRKlIAQGKITDFNVTKgPEFSTDLTKLETDLTSdmvsTNAYKDLKFKPYNFNSQGVQISSGALHPLN 231
Cdd:TIGR00468   2 LKDLLKQLGKLTKEE-TKPALGALINEVK-IELQDELTKLKPELES----AGLWSKLKFETYDVSLPGTKIYPGSLHPLT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   232 KVREEFRQIFFSMGFTEMPSNQyVETGFWNFDALYVPQQHPARDLQDTFYIKDpltadlpddktymdnikavheqgrfgs 311
Cdd:TIGR00468  76 RVIDEIRDIFLGLGFTEETGPE-VETDFWNFDALNIPQDHPARDMQDTFYIKD--------------------------- 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   312 igyrynwkpeecqKLVLRTHSTAisaRMLHDLAKDPKP-TRLFSIDRVFRNEAVDATHLAEFHQVEGVLADYNITLGDLI 390
Cdd:TIGR00468 128 -------------RLLLRTHTTA---VQLRTMEEQEKPpIRIFSPGRVFRNDTVDATHLPEFHQVEGLVIDKNISFTNLK 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   391 KFMEEFFERMGV-TGLRFKPTYNPYTEPSMEIFSWH-EGLQkWVEIGNSGMFRPEMLESMGLPKDLRVLGWGLSLERPTM 468
Cdd:TIGR00468 192 GFLEEFLKKMFGeTEIRFRPSYFPFTEPSAEIDVYCpEGKG-WLEVLGAGMFRPEVLEPMGIDPTYPGFAWGIGIERLAM 270

                         330       340
                  ....*....|....*....|....*
gi 14318497   469 IKYKVQNIRELLGHKvsLDFIETNP 493
Cdd:TIGR00468 271 LKYGITDIRDLYEND--LRFLRQFK 293
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 212-490 2.29e-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: 342.64  E-value: 2.29e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   212 PYNFNSQGVQISSGALHPLNKVREEFRQIFFSMGFTEMPsNQYVETGFWNFDALYVPQQHPARDLQDTFYIKDPLTAdlp 291
Cdd:pfam01409   1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVE-GPEVESDFYNFDALNIPQDHPARDMQDTFYLKKPLKP--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   292 ddktymdnikavheqgrfgsigyrynwkpeECQKLVLRTHSTAISARMLHDlaKDPKPTRLFSIDRVFRNEAVDATHLAE 371
Cdd:pfam01409  77 ------------------------------VARRLLLRTHTTPVQARTLAK--KPKPPIKIFSIGRVFRRDQVDATHLPE 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   372 FHQVEGVLADYNITLGDLIKFMEEFFERM-GVT-GLRFKPTYNPYTEPSMEIFSWHEGLQKWVEIGNSGMFRPEMLESMG 449
Cdd:pfam01409 125 FHQVEGLVVDENVTFADLKGVLEEFLRKFfGFEvKVRFRPSYFPFTEPSAEVDVYVCKLGGWLEVGGAGMVHPNVLEAVG 204

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 14318497   450 LPKDLRVLGWGLSLERPTMIKYKVQNIRELLGHkvSLDFIE 490
Cdd:pfam01409 205 IDEDYSGFAFGLGVERLAMLKYGIDDIRDLYEN--DLRFLR 243
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 228-484 8.97e-111

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: 327.20  E-value: 8.97e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497 228 HPLNKVREEFRQIFFSMGFTEMPSNqYVETGFWNFDALYVPQQHPARDLQDTFYIKDPltadlpddktymdnikavheqg 307
Cdd:cd00496   1 HPLNKVIEEIEDIFVSMGFTEVEGP-EVETDFYNFDALNIPQDHPARDMQDTFYINDP---------------------- 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497 308 rfgsigyrynwkpeecQKLVLRTHSTAISARMLHDLakdPKPTRLFSIDRVFRNEAVDATHLAEFHQVEGVLADYNITLG 387
Cdd:cd00496  58 ----------------ARLLLRTHTSAVQARALAKL---KPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKGLTFA 118

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497 388 DLIKFMEEFFERMG--VTGLRFKPTYNPYTEPSMEIFSWHEGLQKWVEIGNSGMFRPEMLESMGLPKDLRVLGWGLSLER 465
Cdd:cd00496 119 DLKGTLEEFAKELFgpITKVRFRPSYFPFTEPSFEVDVYCPGCLGWLEILGCGMVRPEVLENAGIDEEYSGFAFGIGLER 198

                       250
                ....*....|....*....
gi 14318497 466 PTMIKYKVQNIRELLGHKV 484
Cdd:cd00496 199 LAMLKYGIPDIRLFYSNDL 217
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 219-477 1.99e-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: 196.43  E-value: 1.99e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497 219 GVQISSGALHPLNKVREEFRQIFFSMGFT--EMPSnqyVETGFWNFDALYVPQQHPARDLQDTFYIKDpltadlpddkty 296
Cdd:COG0016  98 GRPRPLGSLHPLTQVIEEIEDIFVGMGFEvaEGPE---IETDWYNFEALNIPPDHPARDMQDTFYIDD------------ 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497 297 mdnikavheqgrfgsigyrynwkpeecqKLVLRTHSTAISARMLhdLAKDPkPTRLFSIDRVFRNEAVDATHLAEFHQVE 376
Cdd:COG0016 163 ----------------------------GLLLRTHTSPVQIRTM--EKQKP-PIRIIAPGRVYRRDESDATHSPMFHQVE 211

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497 377 GVLADYNITLGDLIKFMEEFFERM-GV-TGLRFKPTYNPYTEPSMEI-FSWH----EGLQ-----KWVEIGNSGMFRPEM 444
Cdd:COG0016 212 GLVVDKGISFADLKGTLEEFAKAFfGEdVKVRFRPSYFPFTEPSAEVdISCFicggKGCRvckgtGWLEILGCGMVHPNV 291

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 14318497 445 LESMGL-PKdlRVLG--WGLSLERPTMIKYKVQNIR 477
Cdd:COG0016 292 LRAVGIdPE--EYSGfaFGMGIERLAMLKYGIDDIR 325
 
Name Accession Description Interval E-value
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 1-486 0e+00

phenylalanyl-tRNA synthetase alpha chain; Provisional


Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 685.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497    1 MSDFQLEILKKLDELDEIKSTLATFPQHGS--QDVLSALNSLKAHNKLEFSKVDTVTYDLTKEGAQILNEGSYEIKLVKL 78
Cdd:PTZ00326   4 KELEENTILSKLESENEIVNSLALAESLNIdhQKVVGAIKSLESANYITTEMKKSNTWTLTEEGEDYLKNGSPEYRLWQK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   79 IQELGQLQIkDVMSKLGPQVGKVGQARAFKNGWIAKNASN-ELELSAKLqntdLNELTDETQSILAQIKNNSHLDSIDAK 157
Cdd:PTZ00326  84 LKEGGISKA-DDAKKLGGKVADIGLGNAMKKKWIKLNKGDkKVFLSRKL----VDSVVDTVRLLLKIVAKGSQAEKIDSK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497  158 ILNDLKKRKLIAQGKITDFNVTKGPEFSTDLTKLETDLTSDMVSTNAYKDLKFKPYNFNSQGVQISSGALHPLNKVREEF 237
Cdd:PTZ00326 159 ELKELKKRKLATLEKIKYFVVTKGPKFAKEIKKQITDLTQEMLLNGSWKNAEFKEYNFNALGKKIGGGNLHPLLKVRREF 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497  238 RQIFFSMGFTEMPSNQYVETGFWNFDALYVPQQHPARDLQDTFYIKDPLTADLPD-DKTYMDNIKAVHEQGRFGSIGYRY 316
Cdd:PTZ00326 239 REILLEMGFEEMPTNRYVESSFWNFDALFQPQQHPARDAQDTFFLSKPETSKVNDlDDDYVERVKKVHEVGGYGSIGWRY 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497  317 NWKPEECQKLVLRTHSTAISARMLHDLAKDP------KPTRLFSIDRVFRNEAVDATHLAEFHQVEGVLADYNITLGDLI 390
Cdd:PTZ00326 319 DWKLEEARKNILRTHTTAVSARMLYKLAQEYkktgpfKPKKYFSIDRVFRNETLDATHLAEFHQVEGFVIDRNLTLGDLI 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497  391 KFMEEFFERMGVTGLRFKPTYNPYTEPSMEIFSWHEGLQKWVEIGNSGMFRPEMLESMGLPKDLRVLGWGLSLERPTMIK 470
Cdd:PTZ00326 399 GTIREFFRRIGITKLRFKPAFNPYTEPSMEIFGYHPGLKKWVEVGNSGIFRPEMLRPMGFPEDVTVIAWGLSLERPTMIK 478

                        490
                 ....*....|....*.
gi 14318497  471 YKVQNIRELLGHKVSL 486
Cdd:PTZ00326 479 YGIKNIRDLFGHKVDL 494
PLN02853 PLN02853
Probable phenylalanyl-tRNA synthetase alpha chain
 1-498 0e+00

Probable phenylalanyl-tRNA synthetase alpha chain


Pssm-ID: 215458 [Multi-domain]  Cd Length: 492  Bit Score: 646.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497    1 MSDFQLEILKKLDELDEIKSTLATFPQHG--SQDVLSALNSLKAHNKLEFSKVDTVTYDLTKEGAQILNEGSYEIKLVKL 78
Cdd:PLN02853   1 AAMAEEALLGALSNNEEISDSGQFAASHGldHNEVVGVIKSLHGFRYVDAQDIKRETWVLTEEGKKYAAEGSPEVQLFAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   79 IQELGQLQIKDVMSKLGPQVGKVGQARAFKNGWIAKNasNELELSAKLQNTDlneltDETQSILAQIKNNshlDSIDAKI 158
Cdd:PLN02853  81 VPAEGSISKDELQKKLDPAVFDIGFKQAMKNKWLEMG--GKPQVSRKVQHVE-----DEVKELLLAIQEG---KEVDDKD 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497  159 LNDLKKRK-LIAQGKITDFNVTKGPEFSTDLTKLETDLTSDMVSTNAYKDLKFKPYNFNSQGVQISSGALHPLNKVREEF 237
Cdd:PLN02853 151 IDALKKRRkLITLETWKGYSIKKGPNYAPERKKAATDLTREMLQSGDWKDLEFKEYNFNALGAPPEGGHLHPLLKVRQQF 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497  238 RQIFFSMGFTEMPSNQYVETGFWNFDALYVPQQHPARDLQDTFYIKDPLTA-DLPDDktYMDNIKAVHEQGRFGSIGYRY 316
Cdd:PLN02853 231 RKIFLQMGFEEMPTNNFVESSFWNFDALFQPQQHPARDSHDTFFLKAPATTrQLPED--YVERVKTVHESGGYGSIGYGY 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497  317 NWKPEECQKLVLRTHSTAISARMLHDLAKDP-KPTRLFSIDRVFRNEAVDATHLAEFHQVEGVLADYNITLGDLIKFMEE 395
Cdd:PLN02853 309 DWKREEANKNLLRTHTTAVSSRMLYKLAQKGfKPKRYFSIDRVFRNEAVDRTHLAEFHQVEGLVCDRGLTLGDLIGVLED 388

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497  396 FFERMGVTGLRFKPTYNPYTEPSMEIFSWHEGLQKWVEIGNSGMFRPEMLESMGLPKDLRVLGWGLSLERPTMIKYKVQN 475
Cdd:PLN02853 389 FFSRLGMTKLRFKPAYNPYTEPSMEIFSYHEGLKKWVEVGNSGMFRPEMLLPMGLPEDVNVIAWGLSLERPTMILYGIDN 468

                        490       500
                 ....*....|....*....|...
gi 14318497  476 IRELLGHKVSLDFIETNPAARLD 498
Cdd:PLN02853 469 IRDLFGHKVDLGLIKRNPICRLG 491
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
5-489 4.93e-145

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 425.01  E-value: 4.93e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497    5 QLEILKKLDELDEIKS-TLATFPQHGSQDVLSALNSLKAHNKLEFSKVDTVTYDLTKEGAQILNEGSYEIKLVKLIQELG 83
Cdd:PRK04172   8 EKKVLKALKELKEATLeELAEKLGLPPEAVMRAAEWLEEKGLVKVEERVEEVYVLTEEGKKYAEEGLPERRLLNALKDGG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   84 QLQIKDVMSKL--GPQVGK-VGQARafKNGWiAKNASNELELsaklqntDLNELTDETQSILAQIKNN--SHLDSIDAKI 158
Cdd:PRK04172  88 EVSLDELKEALldKKEVGIaLGNLA--RKGW-AKIEKGKVIL-------KPDAYEDPEEKALKALAEGdkEELSEEDLKV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497  159 LNDLKKRKLIAQGKITDFNVT---KGPEFSTDLTKLE---TDLTSDMVSTNAYKDLKFKPYNFNSQGVQISSGALHPLNK 232
Cdd:PRK04172 158 LKELKKRKLVEEKERTERSVEltdAGLELLKEGIELKeeiTQLTPELLKSGEWKEKEFRPYNVKAPPPKIYPGKKHPYRE 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497  233 VREEFRQIFFSMGFTEMpSNQYVETGFWNFDALYVPQQHPARDLQDTFYIKDPLTADLPDDktYMDNIKAVHEQG-RFGS 311
Cdd:PRK04172 238 FIDEVRDILVEMGFEEM-KGPLVETEFWNFDALFQPQDHPAREMQDTFYLKYPGIGDLPEE--LVERVKEVHEHGgDTGS 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497  312 IGYRYNWKPEECQKLVLRTHSTAISARMLhdlAKDPK-PTRLFSIDRVFRNEAVDATHLAEFHQVEGVLADYNITLGDLI 390
Cdd:PRK04172 315 RGWGYKWDEDIAKRLVLRTHTTALSARYL---ASRPEpPQKYFSIGRVFRPDTIDATHLPEFYQLEGIVMGEDVSFRDLL 391

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497  391 KFMEEFFERMGVTGLRFKPTYNPYTEPSMEIFSWHEGLqKWVEIGNSGMFRPEMLESMGLpkDLRVLGWGLSLERPTMIK 470
Cdd:PRK04172 392 GILKEFYKRLGFEEVKFRPAYFPFTEPSVEVEVYHEGL-GWVELGGAGIFRPEVLEPLGI--DVPVLAWGLGIERLAMLR 468

                        490
                 ....*....|....*....
gi 14318497  471 YKVQNIRELlgHKVSLDFI 489
Cdd:PRK04172 469 LGLDDIRDL--YSSDIEWL 485
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 152-493 1.83e-130

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: 380.50  E-value: 1.83e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   152 DSIDAKILNDLKKRKlIAQGKITDFNVTKgPEFSTDLTKLETDLTSdmvsTNAYKDLKFKPYNFNSQGVQISSGALHPLN 231
Cdd:TIGR00468   2 LKDLLKQLGKLTKEE-TKPALGALINEVK-IELQDELTKLKPELES----AGLWSKLKFETYDVSLPGTKIYPGSLHPLT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   232 KVREEFRQIFFSMGFTEMPSNQyVETGFWNFDALYVPQQHPARDLQDTFYIKDpltadlpddktymdnikavheqgrfgs 311
Cdd:TIGR00468  76 RVIDEIRDIFLGLGFTEETGPE-VETDFWNFDALNIPQDHPARDMQDTFYIKD--------------------------- 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   312 igyrynwkpeecqKLVLRTHSTAisaRMLHDLAKDPKP-TRLFSIDRVFRNEAVDATHLAEFHQVEGVLADYNITLGDLI 390
Cdd:TIGR00468 128 -------------RLLLRTHTTA---VQLRTMEEQEKPpIRIFSPGRVFRNDTVDATHLPEFHQVEGLVIDKNISFTNLK 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   391 KFMEEFFERMGV-TGLRFKPTYNPYTEPSMEIFSWH-EGLQkWVEIGNSGMFRPEMLESMGLPKDLRVLGWGLSLERPTM 468
Cdd:TIGR00468 192 GFLEEFLKKMFGeTEIRFRPSYFPFTEPSAEIDVYCpEGKG-WLEVLGAGMFRPEVLEPMGIDPTYPGFAWGIGIERLAM 270

                         330       340
                  ....*....|....*....|....*
gi 14318497   469 IKYKVQNIRELLGHKvsLDFIETNP 493
Cdd:TIGR00468 271 LKYGITDIRDLYEND--LRFLRQFK 293
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 212-490 2.29e-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: 342.64  E-value: 2.29e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   212 PYNFNSQGVQISSGALHPLNKVREEFRQIFFSMGFTEMPsNQYVETGFWNFDALYVPQQHPARDLQDTFYIKDPLTAdlp 291
Cdd:pfam01409   1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVE-GPEVESDFYNFDALNIPQDHPARDMQDTFYLKKPLKP--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   292 ddktymdnikavheqgrfgsigyrynwkpeECQKLVLRTHSTAISARMLHDlaKDPKPTRLFSIDRVFRNEAVDATHLAE 371
Cdd:pfam01409  77 ------------------------------VARRLLLRTHTTPVQARTLAK--KPKPPIKIFSIGRVFRRDQVDATHLPE 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   372 FHQVEGVLADYNITLGDLIKFMEEFFERM-GVT-GLRFKPTYNPYTEPSMEIFSWHEGLQKWVEIGNSGMFRPEMLESMG 449
Cdd:pfam01409 125 FHQVEGLVVDENVTFADLKGVLEEFLRKFfGFEvKVRFRPSYFPFTEPSAEVDVYVCKLGGWLEVGGAGMVHPNVLEAVG 204

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 14318497   450 LPKDLRVLGWGLSLERPTMIKYKVQNIRELLGHkvSLDFIE 490
Cdd:pfam01409 205 IDEDYSGFAFGLGVERLAMLKYGIDDIRDLYEN--DLRFLR 243
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 228-484 8.97e-111

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: 327.20  E-value: 8.97e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497 228 HPLNKVREEFRQIFFSMGFTEMPSNqYVETGFWNFDALYVPQQHPARDLQDTFYIKDPltadlpddktymdnikavheqg 307
Cdd:cd00496   1 HPLNKVIEEIEDIFVSMGFTEVEGP-EVETDFYNFDALNIPQDHPARDMQDTFYINDP---------------------- 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497 308 rfgsigyrynwkpeecQKLVLRTHSTAISARMLHDLakdPKPTRLFSIDRVFRNEAVDATHLAEFHQVEGVLADYNITLG 387
Cdd:cd00496  58 ----------------ARLLLRTHTSAVQARALAKL---KPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKGLTFA 118

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497 388 DLIKFMEEFFERMG--VTGLRFKPTYNPYTEPSMEIFSWHEGLQKWVEIGNSGMFRPEMLESMGLPKDLRVLGWGLSLER 465
Cdd:cd00496 119 DLKGTLEEFAKELFgpITKVRFRPSYFPFTEPSFEVDVYCPGCLGWLEILGCGMVRPEVLENAGIDEEYSGFAFGIGLER 198

                       250
                ....*....|....*....
gi 14318497 466 PTMIKYKVQNIRELLGHKV 484
Cdd:cd00496 199 LAMLKYGIPDIRLFYSNDL 217
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 219-477 1.99e-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: 196.43  E-value: 1.99e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497 219 GVQISSGALHPLNKVREEFRQIFFSMGFT--EMPSnqyVETGFWNFDALYVPQQHPARDLQDTFYIKDpltadlpddkty 296
Cdd:COG0016  98 GRPRPLGSLHPLTQVIEEIEDIFVGMGFEvaEGPE---IETDWYNFEALNIPPDHPARDMQDTFYIDD------------ 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497 297 mdnikavheqgrfgsigyrynwkpeecqKLVLRTHSTAISARMLhdLAKDPkPTRLFSIDRVFRNEAVDATHLAEFHQVE 376
Cdd:COG0016 163 ----------------------------GLLLRTHTSPVQIRTM--EKQKP-PIRIIAPGRVYRRDESDATHSPMFHQVE 211

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497 377 GVLADYNITLGDLIKFMEEFFERM-GV-TGLRFKPTYNPYTEPSMEI-FSWH----EGLQ-----KWVEIGNSGMFRPEM 444
Cdd:COG0016 212 GLVVDKGISFADLKGTLEEFAKAFfGEdVKVRFRPSYFPFTEPSAEVdISCFicggKGCRvckgtGWLEILGCGMVHPNV 291

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 14318497 445 LESMGL-PKdlRVLG--WGLSLERPTMIKYKVQNIR 477
Cdd:COG0016 292 LRAVGIdPE--EYSGfaFGMGIERLAMLKYGIDDIR 325
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 212-477 7.55e-22

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 97.53  E-value: 7.55e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497  212 PYNFNSQGVQISSGALHPLNKVREEFRQIF---FSMGFTEMPSNQYVETGFWNFDALYVPQQHPARDLQDTFYIkdplta 288
Cdd:PLN02788  52 DHIFSKIGMQLHRRPDHPLGILKNAIYDYFdenYSNKFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTYYV------ 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497  289 dlpDDKTymdnikavheqgrfgsigyrynwkpeecqklVLRTHSTAISARMLHDLAkdpkpTRLFSIDRVFRNEAVDATH 368
Cdd:PLN02788 126 ---DAQT-------------------------------VLRCHTSAHQAELLRAGH-----THFLVTGDVYRRDSIDATH 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497  369 LAEFHQVEGV------------LADYNITLGDLIKFMEEFFERM-GVTGLRFKPTYNPYTEPSMEIFSWHEGlqKWVEIG 435
Cdd:PLN02788 167 YPVFHQMEGVrvfspeeweasgLDGTDLAAEDLKKTLEGLARHLfGDVEMRWVDAYFPFTNPSFELEIFFKG--EWLEVL 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 14318497  436 NSGMFRPEMLESMGLPkDLRVLGWGLSLERPTMIKYKVQNIR 477
Cdd:PLN02788 245 GCGVTEQEILKNNGRS-DNVAWAFGLGLERLAMVLFDIPDIR 285
class_II_aaRS-like_core cd00768
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
 314-466 8.90e-12

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: 64.45  E-value: 8.90e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497 314 YRYNWKPEECQKLVLRTHSTAISARMLHDLAKDPkPTRLFSIDRVFRNEA--VDATHLAEFHQVEG--VLADYNITLGD- 388
Cdd:cd00768  41 DLLPVGAENEEDLYLRPTLEPGLVRLFVSHIRKL-PLRLAEIGPAFRNEGgrRGLRRVREFTQLEGevFGEDGEEASEFe 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497 389 -LIKFMEEFFERMGVTGLRF------KPTYNPYTEPSMEIFSWHeGLQKWVEIGNSGMFRPEML---ESMGLPKDLR--- 455
Cdd:cd00768 120 eLIELTEELLRALGIKLDIVfvektpGEFSPGGAGPGFEIEVDH-PEGRGLEIGSGGYRQDEQAraaDLYFLDEALEyry 198

                       170
                ....*....|...
gi 14318497 456 --VLGWGLSLERP 466
Cdd:cd00768 199 ppTIGFGLGLERL 211
PheRS_DBD3 pfam18553
PheRS DNA binding domain 3; This is a DNA-binding fold domain found in Phenylalanyl-tRNA ...
 70-120 4.52e-11

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: 58.05  E-value: 4.52e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 14318497    70 SYEIKLVKLIQELGQLQIKDVMsKLGPQVGKVGQARAFKNGWIAKNASNEL 120
Cdd:pfam18553   1 SPEARVFNAVPPAGGISLKELM-KLGDSVAKVGFGKAMKNKWIKKDKGDGK 50
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 228-477 2.95e-10

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: 62.40  E-value: 2.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   228 HPLNKVREEFRQIFFSMGFTEMPSNQY--------VETGFWNFDALYVPQQHPARDLQDTFYIKdpltadlpddktymdn 299
Cdd:TIGR00469  42 HPLGIIRDLIEKKFNGADNNQRGNPLFkifdnfkpVVTTMENFDNLGFPADHPGRQKSDCYYIN---------------- 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   300 ikavheqgrfgsigyrynwkpeecQKLVLRTHSTAISARMLH---DLAKDPKPTRLFSIDrVFRNEAVDATHLAEFHQVE 376
Cdd:TIGR00469 106 ------------------------EQHLLRAHTSAHELECFQgglDDSDNIKSGFLISAD-VYRRDEIDKTHYPVFHQAD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   377 G----------------------------VLADYN-----ITLGD------------------LIKFMEEFFERM--GVT 403
Cdd:TIGR00469 161 GaairkrtkadlfekepgyiekfeedirgTEADLNkenvkIILDDdsiplkennpkqeyasdlAVDLCEHELKHSieGIT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   404 GLRFKP-----------------------TYNPYTEPSMEIFSWHEGlqKWVEIGNSGMFRPEMLESMGLpKDLRVLGW- 459
Cdd:TIGR00469 241 KDLFGKkissmiknkanntpkelkvrwidAYFPFTAPSWEIEIWFKD--EWLELCGCGIIRHDILLRAGV-HPSETIGWa 317

                         330
                  ....*....|....*....
gi 14318497   460 -GLSLERPTMIKYKVQNIR 477
Cdd:TIGR00469 318 fGLGLDRIAMLLFDIPDIR 336
LysRS_core cd00775
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ...
 351-415 5.80e-06

Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a lysine to the 3' OH group of ribose of the appropriate tRNA. Its assignment to class II aaRS is based upon its structure and the presence of three characteristic sequence motifs in the core domain. It is found in eukaryotes as well as some prokaryotes and archaea. However, LysRS belongs to class I aaRS's in some prokaryotes and archaea. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.


Pssm-ID: 238398 [Multi-domain]  Cd Length: 329  Bit Score: 48.35  E-value: 5.80e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14318497 351 RLFSIDRVFRNEAVDATHLAEFHQVEGVLA--DYNitlgDLIKFMEEFFERM--GVTGlRFKPTYNPYT 415
Cdd:cd00775  78 RVYEIGRNFRNEGIDLTHNPEFTMIEFYEAyaDYN----DMMDLTEDLFSGLvkKING-KTKIEYGGKE 141
PheRS_DBD2 pfam18554
PheRS DNA binding domain 2; This is a DNA-binding fold domain found in Phenylalanyl-tRNA ...
 136-169 8.18e-06

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: 42.39  E-value: 8.18e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 14318497   136 DETQSILAQIKNNsHLDSIDAKILNDLKKRKLIA 169
Cdd:pfam18554   1 DEVQEQLKLIQEG-KGDSLSDKVKNELKKRKLLQ 33
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
351-458 1.97e-05

tRNA synthetases class II (D, K and N);


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 46.40  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   351 RLFSIDRVFRNEAVDATHLAEFHQVEGVLA--DYNitlgDLIKFMEEFFERM-----GVTGLRFKPTYNPYTEPsMEIFS 423
Cdd:pfam00152  92 RVFQIARCFRDEDLRTDRQPEFTQLDLEMSfvDYE----DVMDLTEELIKEIfkeveGIAKELEGGTLLDLKKP-FPRIT 166

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 14318497   424 WHEGLQKWVEIGNsgmfrPEMLESMGLPkDLRVLG 458
Cdd:pfam00152 167 YAEAIEKLNGKDV-----EELGYGSDKP-DLRFLL 195
HisZ COG3705
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
326-455 6.27e-05

ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];


Pssm-ID: 442919 [Multi-domain]  Cd Length: 312  Bit Score: 44.78  E-value: 6.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497 326 LVLRTHSTAISARML-HDLAKDPKPTRLFSIDRVFRNEAVDATHLAEFHQV-------EGVLADynitlGDLIKFMEEFF 397
Cdd:COG3705  61 LGLRPDMTPQVARIAaTRLANRPGPLRLCYAGNVFRTRPSGLGRSREFLQAgaelighAGLEAD-----AEVIALALEAL 135

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 14318497 398 ERMGVTGLRfkptynpytepsmeifswheglqkwVEIGNSGMFRpEMLESMGLPKDLR 455
Cdd:COG3705 136 KAAGLEDFT-------------------------LDLGHVGLFR-ALLEALGLSEEQR 167
HisRS-like_core cd00773
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ...
 326-408 7.02e-05

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: 44.52  E-value: 7.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497 326 LVLRTHSTAISARML-HDLAKDPKPTRLFSIDRVFRNEAVDATHLAEFHQV-------EGVLADynitlGDLIKFMEEFF 397
Cdd:cd00773  58 LALRPDLTAPVARAVaENLLSLPLPLKLYYIGPVFRYERPQKGRYREFYQVgveiigsDSPLAD-----AEVIALAVEIL 132

                        90
                ....*....|.
gi 14318497 398 ERMGVTGLRFK 408
Cdd:cd00773 133 EALGLKDFQIK 143
lysS PRK00484
lysyl-tRNA synthetase; Reviewed
 351-398 7.91e-05

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 234778 [Multi-domain]  Cd Length: 491  Bit Score: 45.08  E-value: 7.91e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 14318497  351 RLFSIDRVFRNEAVDATHLAEFHQVEgvL----ADYNitlgDLIKFMEEFFE 398
Cdd:PRK00484 242 RVYEIGRNFRNEGIDTRHNPEFTMLE--FyqayADYN----DMMDLTEELIR 287
PLN02502 PLN02502
lysyl-tRNA synthetase
 351-434 1.26e-04

lysyl-tRNA synthetase


Pssm-ID: 215278 [Multi-domain]  Cd Length: 553  Bit Score: 44.60  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497  351 RLFSIDRVFRNEAVDATHLAEFHQVE--GVLADYNitlgDLIKFMEEFFERM--GVTGlRFKPTYNPYT---EPSMEIFS 423
Cdd:PLN02502 299 RVYEIGRQFRNEGISTRHNPEFTTCEfyQAYADYN----DMMELTEEMVSGMvkELTG-SYKIKYHGIEidfTPPFRRIS 373

                         90
                 ....*....|.
gi 14318497  424 WHEGLQKWVEI 434
Cdd:PLN02502 374 MISLVEEATGI 384
PTZ00417 PTZ00417
lysine-tRNA ligase; Provisional
 351-400 1.26e-04

lysine-tRNA ligase; Provisional


Pssm-ID: 173607 [Multi-domain]  Cd Length: 585  Bit Score: 44.62  E-value: 1.26e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 14318497  351 RLFSIDRVFRNEAVDATHLAEFHQVE--GVLADYNitlgDLIKFMEEFFERM 400
Cdd:PTZ00417 323 KVYEIGKVFRNEGIDNTHNPEFTSCEfyWAYADFY----DLIKWSEDFFSQL 370
tRNA-synt_2b pfam00587
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ...
 349-481 2.78e-04

tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.


Pssm-ID: 395469 [Multi-domain]  Cd Length: 181  Bit Score: 42.01  E-value: 2.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   349 PTRLFSIDRVFRNEAVDATH----LAEFHQVEGVL----ADYNITLGDLIKFMEEFFERMGVTG---LRFKPTYNPYTEP 417
Cdd:pfam00587  36 PLKLAQFGTCFRHEASGDTRglirVRQFHQDDAHIfhapGQSPDELEDYIKLIDRVYSRLGLEVrvvRLSNSDGSAFYGP 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14318497   418 SMEIFSWHEGLQKWVEIG---NSGMFRPEMLesmglpkDLRVLGWGLSLERPTMIKYKVQNIRELLG 481
Cdd:pfam00587 116 KLDFEVVFPSLGKQRQTGtiqNDGFRLPRRL-------GIRYKDEDNESKFPYMIHRAGLGVERFLA 175
lysS PRK02983
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
351-383 4.33e-04

bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;


Pssm-ID: 235095 [Multi-domain]  Cd Length: 1094  Bit Score: 43.03  E-value: 4.33e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 14318497   351 RLFSIDRVFRNEAVDATHLAEFHQVEG--VLADYN 383
Cdd:PRK02983  840 RVFELGRNFRNEGVDATHNPEFTLLEAyqAHADYD 874
HisS COG0124
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ...
 347-408 8.01e-04

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: 41.65  E-value: 8.01e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14318497 347 PKPTRLFSIDRVFRNEAVDATHLAEFHQV-------EGVLADYnitlgDLIKFMEEFFERMGVTGLRFK 408
Cdd:COG0124  97 PFPFKLYYIGPVFRYERPQKGRYRQFHQFgvevigsDSPLADA-----EVIALAADLLKALGLKDFTLE 160
tRNA_synthFbeta pfam17759
Phenylalanyl tRNA synthetase beta chain CLM domain; This domain corresponds to the catalytic ...
 220-452 4.35e-03

Phenylalanyl tRNA synthetase beta chain CLM domain; This domain corresponds to the catalytic like domain (CLM) in the beta chain of phe tRNA synthetase.


Pssm-ID: 465487 [Multi-domain]  Cd Length: 214  Bit Score: 38.69  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   220 VQISSGALHPLNKVREEFRQIFFSMGFTEMPSnqYVETGFWNFDALYVPQqhparDLQDTFYIKDPLTADLPddktymdn 299
Cdd:pfam17759   8 GPTTGGGLTPEQKLRRRVRDLLAAAGFTEVIT--YSFTSPKDLDKLLEDD-----PRRKAVKLANPLSEELS-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   300 ikavheqgrfgsigyrynwkpeecqklVLRTH------STAIS--ARMLHDLakdpkptRLFSIDRVFRNEAVDA----- 366
Cdd:pfam17759  73 ---------------------------VMRTSllpgllETLAYnlNRGNPDV-------RLFEIGRVFLPDELEElprep 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318497   367 THLAefhqveGVLADYNITLG-----------DLIKFMEEFFERMGVTGLRFKPTynpytepsmEIFSWHEGLQKWVEIG 435
Cdd:pfam17759 119 RRLA------GLLTGKRLPESwqgkarpvdfyDLKGIVEALLAALGIDDYEFEAA---------DHPALHPGRSAEILVG 183

                         250       260
                  ....*....|....*....|..
gi 14318497   436 NS-----GMFRPEMLESMGLPK 452
Cdd:pfam17759 184 GKvigfiGELHPEVAKNFDLPQ 205
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH