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Conserved domains on  [gi|61557070|ref|NP_001013157|]
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phenylalanine--tRNA ligase, mitochondrial [Rattus norvegicus]

Protein Classification

phenylalanine--tRNA ligase( domain architecture ID 1006086)

phenylalanine--tRNA ligase catalyzes the synthesis of phenylalanyl-tRNA (Phe)

CATH:  3.30.70.380|3.30.930.10
EC:  6.1.1.20
Gene Ontology:  GO:0005524|GO:0004826|GO:0000049|GO:0006432

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02788 super family cl33567
phenylalanine-tRNA synthetase
 29-471 1.24e-179

phenylalanine-tRNA synthetase


The actual alignment was detected with superfamily member PLN02788:

Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 508.53  E-value: 1.24e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070   29 HRAWGSRPAASQFA-VQGAPG-RVLELLGKSYPQDD-------HTNLTQKVLSKVGRNLHNQKFHPLWLIKERVKEHFYQ 99
Cdd:PLN02788   4 SSALVTPATAKSSSrRYRAPAvSAVEIGGVAIARDEvvreddpTNNVPDHIFSKIGMQLHRRPDHPLGILKNAIYDYFDE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070  100 QYMGrsrtpLFSVYDQLSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRGHMLRAHTSAHQWDLLHAGLNAFLVVGDVYR 179
Cdd:PLN02788  84 NYSN-----KFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAHQAELLRAGHTHFLVTGDVYR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070  180 RDQIDSQHYPVFHQLEGVRLFSKHELfagvkdgeslqlfeessrsahkqETHTMEAVKLVEFDLKQVLTRLVTHLFGDgL 259
Cdd:PLN02788 159 RDSIDATHYPVFHQMEGVRVFSPEEW-----------------------EASGLDGTDLAAEDLKKTLEGLARHLFGD-V 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070  260 EVRWVDCYFPFTHPSFEMEINFRGEWLEVLGCGVMEQQLVNSAGAQDRIGWAFGLGLERLAMVLYDIPDIRLFWSEDERF 339
Cdd:PLN02788 215 EMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVTEQEILKNNGRSDNVAWAFGLGLERLAMVLFDIPDIRLFWSDDERF 294

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070  340 LKQFRLSDInqSVKFQrwffqeeratgiqrkmgrqlcPFSKYPAVFNDISFWLPSEnYTENDFYDIVRTVGGDLVEKVDL 419
Cdd:PLN02788 295 TSQFKEGQL--GVKFK---------------------PYSKYPPCYKDISFWISDE-FTENNLCEVVRGIAGDLVEEVKL 350

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 61557070  420 IDKFEHPKTHRTSHCYRITYRHMERTLSQREVSSVHQAVQEAAVQLLGVEGR 471
Cdd:PLN02788 351 IDNFTNPKKGKTSHCYRIVYRSMERSLTDEEINALQDKVREEVQKKLGVELR 402
 
Name Accession Description Interval E-value
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 29-471 1.24e-179

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 508.53  E-value: 1.24e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070   29 HRAWGSRPAASQFA-VQGAPG-RVLELLGKSYPQDD-------HTNLTQKVLSKVGRNLHNQKFHPLWLIKERVKEHFYQ 99
Cdd:PLN02788   4 SSALVTPATAKSSSrRYRAPAvSAVEIGGVAIARDEvvreddpTNNVPDHIFSKIGMQLHRRPDHPLGILKNAIYDYFDE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070  100 QYMGrsrtpLFSVYDQLSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRGHMLRAHTSAHQWDLLHAGLNAFLVVGDVYR 179
Cdd:PLN02788  84 NYSN-----KFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAHQAELLRAGHTHFLVTGDVYR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070  180 RDQIDSQHYPVFHQLEGVRLFSKHELfagvkdgeslqlfeessrsahkqETHTMEAVKLVEFDLKQVLTRLVTHLFGDgL 259
Cdd:PLN02788 159 RDSIDATHYPVFHQMEGVRVFSPEEW-----------------------EASGLDGTDLAAEDLKKTLEGLARHLFGD-V 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070  260 EVRWVDCYFPFTHPSFEMEINFRGEWLEVLGCGVMEQQLVNSAGAQDRIGWAFGLGLERLAMVLYDIPDIRLFWSEDERF 339
Cdd:PLN02788 215 EMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVTEQEILKNNGRSDNVAWAFGLGLERLAMVLFDIPDIRLFWSDDERF 294

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070  340 LKQFRLSDInqSVKFQrwffqeeratgiqrkmgrqlcPFSKYPAVFNDISFWLPSEnYTENDFYDIVRTVGGDLVEKVDL 419
Cdd:PLN02788 295 TSQFKEGQL--GVKFK---------------------PYSKYPPCYKDISFWISDE-FTENNLCEVVRGIAGDLVEEVKL 350

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 61557070  420 IDKFEHPKTHRTSHCYRITYRHMERTLSQREVSSVHQAVQEAAVQLLGVEGR 471
Cdd:PLN02788 351 IDNFTNPKKGKTSHCYRIVYRSMERSLTDEEINALQDKVREEVQKKLGVELR 402
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 51-469 1.96e-157

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: 454.53  E-value: 1.96e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070    51 LELLGKSYPQDDHT-NLTQKVLSKVGRNLHNQKFHPLWLIKERVKEHFYQQYMGRSRTPLFSVYDQLSPVVTTWQNFDSL 129
Cdd:TIGR00469   8 LEINGIKYATDGQTtNVTDKIIKLTDANKHLKEDHPLGIIRDLIEKKFNGADNNQRGNPLFKIFDNFKPVVTTMENFDNL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070   130 LIPADHPSRKKGDNYYLNRGHMLRAHTSAHQWDLLHAGLN-------AFLVVGDVYRRDQIDSQHYPVFHQLEG--VRLF 200
Cdd:TIGR00469  88 GFPADHPGRQKSDCYYINEQHLLRAHTSAHELECFQGGLDdsdniksGFLISADVYRRDEIDKTHYPVFHQADGaaIRKR 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070   201 SKHELFagVKDGESLQLFEESSR------------------------SAHKQETHTMEAVKLVEFDLKQVLTRLVTHLFG 256
Cdd:TIGR00469 168 TKADLF--EKEPGYIEKFEEDIRgteadlnkenvkiildddsiplkeNNPKQEYASDLAVDLCEHELKHSIEGITKDLFG 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070   257 ---------------DGLEVRWVDCYFPFTHPSFEMEINFRGEWLEVLGCGVMEQQLVNSAGAQ--DRIGWAFGLGLERL 319
Cdd:TIGR00469 246 kkissmiknkanntpKELKVRWIDAYFPFTAPSWEIEIWFKDEWLELCGCGIIRHDILLRAGVHpsETIGWAFGLGLDRI 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070   320 AMVLYDIPDIRLFWSEDERFLKQFRLSDINQSVKFQrwffqeeratgiqrkmgrqlcPFSKYPAVFNDISFWLPSE---- 395
Cdd:TIGR00469 326 AMLLFDIPDIRLFWSNDEGFLRQFSEGDLHLIPKFK---------------------PISHHPGCFNDLAFWLPEDiedd 384

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 61557070   396 -NYTENDFYDIVRTVGGDLVEKVDLIDKFEHPKTHRTSHCYRITYRHMERTLSQREVSSVHQAVQEAAVQLLGVE 469
Cdd:TIGR00469 385 aGFHENDFMDIIRNIAGDLVEQIKLVDKFKHPKTGKKSMCFRINYQHMDRNLTNAEVNEIHDMIASALVDEFNVE 459
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 84-338 4.04e-93

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: 280.97  E-value: 4.04e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070  84 HPLWLIKERVKEHFYQqyMGrsrtplFSVYDQlSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRG--HMLRAHTSAHQW 161
Cdd:cd00496   1 HPLNKVIEEIEDIFVS--MG------FTEVEG-PEVETDFYNFDALNIPQDHPARDMQDTFYINDParLLLRTHTSAVQA 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070 162 DLLHA--GLNAFLVVGDVYRRDQIDSQHYPVFHQLEGVRLFSKhelfagvkdgeslqlfeessrsahkqethtmeavkLV 239
Cdd:cd00496  72 RALAKlkPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKG-----------------------------------LT 116

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070 240 EFDLKQVLTRLVTHLFGDGLEVRWVDCYFPFTHPSFEMEINFRG--EWLEVLGCGVMEQQLVNSAGAQ-DRIGWAFGLGL 316
Cdd:cd00496 117 FADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYCPGclGWLEILGCGMVRPEVLENAGIDeEYSGFAFGIGL 196

                       250       260
                ....*....|....*....|..
gi 61557070 317 ERLAMVLYDIPDIRLFWSEDER 338
Cdd:cd00496 197 ERLAMLKYGIPDIRLFYSNDLR 218
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 84-344 6.90e-55

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: 186.41  E-value: 6.90e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070  84 HPLWLIKERVKEHFYQqyMGrsrtplFSVYDqlSP-VVTTWQNFDSLLIPADHPSRKKGDNYYLNRGHMLRAHTSAHQwd 162
Cdd:COG0016 107 HPLTQVIEEIEDIFVG--MG------FEVAE--GPeIETDWYNFEALNIPPDHPARDMQDTFYIDDGLLLRTHTSPVQ-- 174

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070 163 lLHAGLN-----AFLVVGDVYRRDQIDSQHYPVFHQLEGVrlfskhelfagvkdgeslqlfeessrsahkqethtmeAV- 236
Cdd:COG0016 175 -IRTMEKqkppiRIIAPGRVYRRDESDATHSPMFHQVEGL-------------------------------------VVd 216

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070 237 KLVEF-DLKQVLTRLVTHLFGDGLEVRWVDCYFPFTHPSFEMEINF---RGE---------WLEVLGCG-----VMEqql 298
Cdd:COG0016 217 KGISFaDLKGTLEEFAKAFFGEDVKVRFRPSYFPFTEPSAEVDISCficGGKgcrvckgtgWLEILGCGmvhpnVLR--- 293

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 61557070 299 vnSAGaqdrI------GWAFGLGLERLAMVLYDIPDIRLFWSEDERFLKQFR 344
Cdd:COG0016 294 --AVG----IdpeeysGFAFGMGIERLAMLKYGIDDIRLFFENDLRFLRQFG 339
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 75-343 2.64e-49

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: 168.91  E-value: 2.64e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070    75 GRNLHNQKFHPLWLIKERVKEHFYQqyMGrsrtplFSVYDqlSP-VVTTWQNFDSLLIPADHPSRKKGDNYYL------- 146
Cdd:pfam01409   8 GRRIEPGGLHPLTRTLERIRDIFLG--MG------FEEVE--GPeVESDFYNFDALNIPQDHPARDMQDTFYLkkplkpv 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070   147 NRGHMLRAHTSAHQWDLLHAGLNA---FLVVGDVYRRDQIDSQHYPVFHQLEGVRlfskhelfagVKDGESLQlfeessr 223
Cdd:pfam01409  78 ARRLLLRTHTTPVQARTLAKKPKPpikIFSIGRVFRRDQVDATHLPEFHQVEGLV----------VDENVTFA------- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070   224 sahkqethtmeavklvefDLKQVLTRLVTHLFGDGLEVRWVDCYFPFTHPSFEMEINFR--GEWLEVLGCGVMEQQLVNS 301
Cdd:pfam01409 141 ------------------DLKGVLEEFLRKFFGFEVKVRFRPSYFPFTEPSAEVDVYVCklGGWLEVGGAGMVHPNVLEA 202

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 61557070   302 AG-AQDRIGWAFGLGLERLAMVLYDIPDIRLFWSEDERFLKQF 343
Cdd:pfam01409 203 VGiDEDYSGFAFGLGVERLAMLKYGIDDIRDLYENDLRFLRQF 245
FDX-ACB smart00896
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 379-471 1.81e-33

Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some phenylalanyl tRNA synthetases. The domain has a ferredoxin fold, consisting of an alpha+beta sandwich with anti-parallel beta-sheets (beta-alpha-beta x2).


Pssm-ID: 214893 [Multi-domain]  Cd Length: 93  Bit Score: 121.38  E-value: 1.81e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070    379 SKYPAVFNDISFWLPsENYTENDFYDIVRTVGGDLVEKVDLIDKFEH-PKTHRTSHCYRITYRHMERTLSQREVSSVHQA 457
Cdd:smart00896   1 SKFPAVRRDLAFVVD-EDVPAAELLDAIREAGGDLLEDVRLFDVYEGgIPEGKKSLAYRLTYQSPDRTLTDEEVNAIHDK 79

                           90
                   ....*....|....
gi 61557070    458 VQEAAVQLLGVEGR 471
Cdd:smart00896  80 IVAALEKKFGAELR 93
 
Name Accession Description Interval E-value
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 29-471 1.24e-179

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 508.53  E-value: 1.24e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070   29 HRAWGSRPAASQFA-VQGAPG-RVLELLGKSYPQDD-------HTNLTQKVLSKVGRNLHNQKFHPLWLIKERVKEHFYQ 99
Cdd:PLN02788   4 SSALVTPATAKSSSrRYRAPAvSAVEIGGVAIARDEvvreddpTNNVPDHIFSKIGMQLHRRPDHPLGILKNAIYDYFDE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070  100 QYMGrsrtpLFSVYDQLSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRGHMLRAHTSAHQWDLLHAGLNAFLVVGDVYR 179
Cdd:PLN02788  84 NYSN-----KFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAHQAELLRAGHTHFLVTGDVYR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070  180 RDQIDSQHYPVFHQLEGVRLFSKHELfagvkdgeslqlfeessrsahkqETHTMEAVKLVEFDLKQVLTRLVTHLFGDgL 259
Cdd:PLN02788 159 RDSIDATHYPVFHQMEGVRVFSPEEW-----------------------EASGLDGTDLAAEDLKKTLEGLARHLFGD-V 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070  260 EVRWVDCYFPFTHPSFEMEINFRGEWLEVLGCGVMEQQLVNSAGAQDRIGWAFGLGLERLAMVLYDIPDIRLFWSEDERF 339
Cdd:PLN02788 215 EMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVTEQEILKNNGRSDNVAWAFGLGLERLAMVLFDIPDIRLFWSDDERF 294

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070  340 LKQFRLSDInqSVKFQrwffqeeratgiqrkmgrqlcPFSKYPAVFNDISFWLPSEnYTENDFYDIVRTVGGDLVEKVDL 419
Cdd:PLN02788 295 TSQFKEGQL--GVKFK---------------------PYSKYPPCYKDISFWISDE-FTENNLCEVVRGIAGDLVEEVKL 350

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 61557070  420 IDKFEHPKTHRTSHCYRITYRHMERTLSQREVSSVHQAVQEAAVQLLGVEGR 471
Cdd:PLN02788 351 IDNFTNPKKGKTSHCYRIVYRSMERSLTDEEINALQDKVREEVQKKLGVELR 402
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 51-469 1.96e-157

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: 454.53  E-value: 1.96e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070    51 LELLGKSYPQDDHT-NLTQKVLSKVGRNLHNQKFHPLWLIKERVKEHFYQQYMGRSRTPLFSVYDQLSPVVTTWQNFDSL 129
Cdd:TIGR00469   8 LEINGIKYATDGQTtNVTDKIIKLTDANKHLKEDHPLGIIRDLIEKKFNGADNNQRGNPLFKIFDNFKPVVTTMENFDNL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070   130 LIPADHPSRKKGDNYYLNRGHMLRAHTSAHQWDLLHAGLN-------AFLVVGDVYRRDQIDSQHYPVFHQLEG--VRLF 200
Cdd:TIGR00469  88 GFPADHPGRQKSDCYYINEQHLLRAHTSAHELECFQGGLDdsdniksGFLISADVYRRDEIDKTHYPVFHQADGaaIRKR 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070   201 SKHELFagVKDGESLQLFEESSR------------------------SAHKQETHTMEAVKLVEFDLKQVLTRLVTHLFG 256
Cdd:TIGR00469 168 TKADLF--EKEPGYIEKFEEDIRgteadlnkenvkiildddsiplkeNNPKQEYASDLAVDLCEHELKHSIEGITKDLFG 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070   257 ---------------DGLEVRWVDCYFPFTHPSFEMEINFRGEWLEVLGCGVMEQQLVNSAGAQ--DRIGWAFGLGLERL 319
Cdd:TIGR00469 246 kkissmiknkanntpKELKVRWIDAYFPFTAPSWEIEIWFKDEWLELCGCGIIRHDILLRAGVHpsETIGWAFGLGLDRI 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070   320 AMVLYDIPDIRLFWSEDERFLKQFRLSDINQSVKFQrwffqeeratgiqrkmgrqlcPFSKYPAVFNDISFWLPSE---- 395
Cdd:TIGR00469 326 AMLLFDIPDIRLFWSNDEGFLRQFSEGDLHLIPKFK---------------------PISHHPGCFNDLAFWLPEDiedd 384

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 61557070   396 -NYTENDFYDIVRTVGGDLVEKVDLIDKFEHPKTHRTSHCYRITYRHMERTLSQREVSSVHQAVQEAAVQLLGVE 469
Cdd:TIGR00469 385 aGFHENDFMDIIRNIAGDLVEQIKLVDKFKHPKTGKKSMCFRINYQHMDRNLTNAEVNEIHDMIASALVDEFNVE 459
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 84-338 4.04e-93

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: 280.97  E-value: 4.04e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070  84 HPLWLIKERVKEHFYQqyMGrsrtplFSVYDQlSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRG--HMLRAHTSAHQW 161
Cdd:cd00496   1 HPLNKVIEEIEDIFVS--MG------FTEVEG-PEVETDFYNFDALNIPQDHPARDMQDTFYINDParLLLRTHTSAVQA 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070 162 DLLHA--GLNAFLVVGDVYRRDQIDSQHYPVFHQLEGVRLFSKhelfagvkdgeslqlfeessrsahkqethtmeavkLV 239
Cdd:cd00496  72 RALAKlkPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKG-----------------------------------LT 116

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070 240 EFDLKQVLTRLVTHLFGDGLEVRWVDCYFPFTHPSFEMEINFRG--EWLEVLGCGVMEQQLVNSAGAQ-DRIGWAFGLGL 316
Cdd:cd00496 117 FADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYCPGclGWLEILGCGMVRPEVLENAGIDeEYSGFAFGIGL 196

                       250       260
                ....*....|....*....|..
gi 61557070 317 ERLAMVLYDIPDIRLFWSEDER 338
Cdd:cd00496 197 ERLAMLKYGIPDIRLFYSNDLR 218
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 84-344 6.90e-55

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: 186.41  E-value: 6.90e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070  84 HPLWLIKERVKEHFYQqyMGrsrtplFSVYDqlSP-VVTTWQNFDSLLIPADHPSRKKGDNYYLNRGHMLRAHTSAHQwd 162
Cdd:COG0016 107 HPLTQVIEEIEDIFVG--MG------FEVAE--GPeIETDWYNFEALNIPPDHPARDMQDTFYIDDGLLLRTHTSPVQ-- 174

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070 163 lLHAGLN-----AFLVVGDVYRRDQIDSQHYPVFHQLEGVrlfskhelfagvkdgeslqlfeessrsahkqethtmeAV- 236
Cdd:COG0016 175 -IRTMEKqkppiRIIAPGRVYRRDESDATHSPMFHQVEGL-------------------------------------VVd 216

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070 237 KLVEF-DLKQVLTRLVTHLFGDGLEVRWVDCYFPFTHPSFEMEINF---RGE---------WLEVLGCG-----VMEqql 298
Cdd:COG0016 217 KGISFaDLKGTLEEFAKAFFGEDVKVRFRPSYFPFTEPSAEVDISCficGGKgcrvckgtgWLEILGCGmvhpnVLR--- 293

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 61557070 299 vnSAGaqdrI------GWAFGLGLERLAMVLYDIPDIRLFWSEDERFLKQFR 344
Cdd:COG0016 294 --AVG----IdpeeysGFAFGMGIERLAMLKYGIDDIRLFFENDLRFLRQFG 339
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 55-343 6.43e-50

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: 172.11  E-value: 6.43e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070    55 GKSYPQDDHTNLTQKVL-SKVGRNLHNQKF--------------HPLWLIKERVKEHFYQqyMGrsrtplFSVYDqlSPV 119
Cdd:TIGR00468  28 VKIELQDELTKLKPELEsAGLWSKLKFETYdvslpgtkiypgslHPLTRVIDEIRDIFLG--LG------FTEET--GPE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070   120 VTT-WQNFDSLLIPADHPSRKKGDNYYLNRGHMLRAHTSAHQwdlLHA-------GLNAFlVVGDVYRRDQIDSQHYPVF 191
Cdd:TIGR00468  98 VETdFWNFDALNIPQDHPARDMQDTFYIKDRLLLRTHTTAVQ---LRTmeeqekpPIRIF-SPGRVFRNDTVDATHLPEF 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070   192 HQLEGVRlfskhelfagVKDGESLQlfeessrsahkqethtmeavklvefDLKQVLTRLVTHLFGdGLEVRWVDCYFPFT 271
Cdd:TIGR00468 174 HQVEGLV----------IDKNISFT-------------------------NLKGFLEEFLKKMFG-ETEIRFRPSYFPFT 217

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 61557070   272 HPSFEMEIN-FRGE-WLEVLGCGVMEQQLVNSAGAQDRI-GWAFGLGLERLAMVLYDIPDIRLFWSEDERFLKQF 343
Cdd:TIGR00468 218 EPSAEIDVYcPEGKgWLEVLGAGMFRPEVLEPMGIDPTYpGFAWGIGIERLAMLKYGITDIRDLYENDLRFLRQF 292
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 75-343 2.64e-49

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: 168.91  E-value: 2.64e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070    75 GRNLHNQKFHPLWLIKERVKEHFYQqyMGrsrtplFSVYDqlSP-VVTTWQNFDSLLIPADHPSRKKGDNYYL------- 146
Cdd:pfam01409   8 GRRIEPGGLHPLTRTLERIRDIFLG--MG------FEEVE--GPeVESDFYNFDALNIPQDHPARDMQDTFYLkkplkpv 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070   147 NRGHMLRAHTSAHQWDLLHAGLNA---FLVVGDVYRRDQIDSQHYPVFHQLEGVRlfskhelfagVKDGESLQlfeessr 223
Cdd:pfam01409  78 ARRLLLRTHTTPVQARTLAKKPKPpikIFSIGRVFRRDQVDATHLPEFHQVEGLV----------VDENVTFA------- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070   224 sahkqethtmeavklvefDLKQVLTRLVTHLFGDGLEVRWVDCYFPFTHPSFEMEINFR--GEWLEVLGCGVMEQQLVNS 301
Cdd:pfam01409 141 ------------------DLKGVLEEFLRKFFGFEVKVRFRPSYFPFTEPSAEVDVYVCklGGWLEVGGAGMVHPNVLEA 202

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 61557070   302 AG-AQDRIGWAFGLGLERLAMVLYDIPDIRLFWSEDERFLKQF 343
Cdd:pfam01409 203 VGiDEDYSGFAFGLGVERLAMLKYGIDDIRDLYENDLRFLRQF 245
FDX-ACB smart00896
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 379-471 1.81e-33

Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some phenylalanyl tRNA synthetases. The domain has a ferredoxin fold, consisting of an alpha+beta sandwich with anti-parallel beta-sheets (beta-alpha-beta x2).


Pssm-ID: 214893 [Multi-domain]  Cd Length: 93  Bit Score: 121.38  E-value: 1.81e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070    379 SKYPAVFNDISFWLPsENYTENDFYDIVRTVGGDLVEKVDLIDKFEH-PKTHRTSHCYRITYRHMERTLSQREVSSVHQA 457
Cdd:smart00896   1 SKFPAVRRDLAFVVD-EDVPAAELLDAIREAGGDLLEDVRLFDVYEGgIPEGKKSLAYRLTYQSPDRTLTDEEVNAIHDK 79

                           90
                   ....*....|....
gi 61557070    458 VQEAAVQLLGVEGR 471
Cdd:smart00896  80 IVAALEKKFGAELR 93
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
94-344 1.94e-24

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 105.68  E-value: 1.94e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070   94 KEHFYQQYMGRSRTPLFS-----VYDQLspVVTTWQNFDSLLIPADHPSRKKGDNYYL---NRG-------------H-- 150
Cdd:PRK04172 231 KKHPYREFIDEVRDILVEmgfeeMKGPL--VETEFWNFDALFQPQDHPAREMQDTFYLkypGIGdlpeelvervkevHeh 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070  151 ---------------------MLRAHT---SAHQwdlLHAGLNA---FLVVGDVYRRDQIDSQHYPVFHQLEGVRLfskh 203
Cdd:PRK04172 309 ggdtgsrgwgykwdediakrlVLRTHTtalSARY---LASRPEPpqkYFSIGRVFRPDTIDATHLPEFYQLEGIVM---- 381

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070  204 elfagvkdGESLqlfeessrsahkqethtmeAVKlvefDLKQVLTRLVTHLfgdGL-EVRWVDCYFPFTHPSFEMEINF- 281
Cdd:PRK04172 382 --------GEDV-------------------SFR----DLLGILKEFYKRL---GFeEVKFRPAYFPFTEPSVEVEVYHe 427

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61557070  282 RGEWLEVLGCGVMEQQLVNSAGAQDRIGwAFGLGLERLAMVLYDIPDIRLFWSEDERFLKQFR 344
Cdd:PRK04172 428 GLGWVELGGAGIFRPEVLEPLGIDVPVL-AWGLGIERLAMLRLGLDDIRDLYSSDIEWLRERP 489
FDX-ACB pfam03147
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 379-471 3.68e-24

Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some phenylalanyl tRNA synthetases. The domain has a ferredoxin fold.


Pssm-ID: 460826 [Multi-domain]  Cd Length: 94  Bit Score: 96.01  E-value: 3.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070   379 SKYPAVFNDISFWLPsENYTENDFYDIVRTVGGDLVEKVDLIDKFEHPK--THRTSHCYRITYRHMERTLSQREVSSVHQ 456
Cdd:pfam03147   1 SKYPAVRRDLAFVVD-EDVPAADILKAIREAGGELLESVELFDVYRGEKipEGKKSLAFRLTFQSPERTLTDEEVNAIIE 79

                          90
                  ....*....|....*
gi 61557070   457 AVQEAAVQLLGVEGR 471
Cdd:pfam03147  80 KIVEALEKKFGAELR 94
pheT PRK00629
phenylalanyl-tRNA synthetase subunit beta; Reviewed
 377-469 2.86e-15

phenylalanyl-tRNA synthetase subunit beta; Reviewed


Pssm-ID: 234804 [Multi-domain]  Cd Length: 791  Bit Score: 78.29  E-value: 2.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070  377 PFSKYPAVFNDISFWLPsENYTENDFYDIVRTVGGDLVEKVDLIDKFEHPK--THRTSHCYRITYRHMERTLSQREVSSV 454
Cdd:PRK00629 695 PISKFPAVRRDLALVVD-EDVPAADILKAIKKAGGKLLESVELFDVYEGKGigEGKKSLAFRLTFQDPDRTLTDEEINAA 773

                         90
                 ....*....|....*
gi 61557070  455 HQAVQEAAVQLLGVE 469
Cdd:PRK00629 774 MDKIVAALEEKFGAE 788
pheT_bact TIGR00472
phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Every known example of ...
 377-471 3.15e-15

phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Every known example of the phenylalanyl-tRNA synthetase, except the monomeric form of mitochondrial, is an alpha 2 beta 2 heterotetramer. The beta subunits break into two subfamilies that are considerably different in sequence, length, and pattern of gaps. This model represents the subfamily that includes the beta subunit from Bacteria other than spirochetes, as well as a chloroplast-encoded form from Porphyra purpurea. The chloroplast-derived sequence is considerably shorter at the amino end. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273097 [Multi-domain]  Cd Length: 797  Bit Score: 78.49  E-value: 3.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070   377 PFSKYPAVFNDISFWLPSENyTENDFYDIVRTVGGDLVEKVDLIDKF--EHPKTHRTSHCYRITYRHMERTLSQREVSSV 454
Cdd:TIGR00472 702 PISKFPAVTRDISFLVPKDV-PANEIIKLIKKSGLELLEEVELFDVYqgKNIGEGKKSLALRLVLRDKERTLTDEEINKI 780

                          90
                  ....*....|....*..
gi 61557070   455 HQAVQEAAVQLLGVEGR 471
Cdd:TIGR00472 781 VEKVLNALKEKLGAELR 797
PheT COG0072
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; ...
 377-469 1.46e-13

Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; Phenylalanyl-tRNA synthetase beta subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439842 [Multi-domain]  Cd Length: 793  Bit Score: 72.89  E-value: 1.46e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070 377 PFSKYPAVFNDISFWLPsENYTENDFYDIVRTVGGDLVEKVDLIDKFEHPK--THRTSHCYRITYRHMERTLSQREVSSV 454
Cdd:COG0072 697 PISKFPAVRRDLALVVD-EDVPAADVLDAIRKAAGKLLEDVRLFDVYEGKGvpEGKKSLAFSLTLQDPDRTLTDEEIDAA 775

                        90
                ....*....|....*
gi 61557070 455 HQAVQEAAVQLLGVE 469
Cdd:COG0072 776 MDKIVAALEKKFGAE 790
PLN02853 PLN02853
Probable phenylalanyl-tRNA synthetase alpha chain
 84-332 6.53e-10

Probable phenylalanyl-tRNA synthetase alpha chain


Pssm-ID: 215458 [Multi-domain]  Cd Length: 492  Bit Score: 61.23  E-value: 6.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070   84 HPLWLIKERVKEHFYQqyMGRSRTPLFSVydqlspVVTTWQNFDSLLIPADHPSRKKGDNYYLN---------------- 147
Cdd:PLN02853 221 HPLLKVRQQFRKIFLQ--MGFEEMPTNNF------VESSFWNFDALFQPQQHPARDSHDTFFLKapattrqlpedyverv 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070  148 -----------RGHM------------LRAHTSAHQWDLLHAGLNA------FLVVGDVYRRDQIDSQHYPVFHQLEGVr 198
Cdd:PLN02853 293 ktvhesggygsIGYGydwkreeanknlLRTHTTAVSSRMLYKLAQKgfkpkrYFSIDRVFRNEAVDRTHLAEFHQVEGL- 371

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070  199 lfskhelfagVKD-GESLQlfeessrsahkqethtmeavklvefDLKQVLTRLVTHLfgdGL-EVRWVDCYFPFTHPSfe 276
Cdd:PLN02853 372 ----------VCDrGLTLG-------------------------DLIGVLEDFFSRL---GMtKLRFKPAYNPYTEPS-- 411

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 61557070  277 MEInFR-----GEWLEVLGCGVMEQQLVNSAGAQDR---IGWafGLGLERLAMVLYDIPDIR-LF 332
Cdd:PLN02853 412 MEI-FSyheglKKWVEVGNSGMFRPEMLLPMGLPEDvnvIAW--GLSLERPTMILYGIDNIRdLF 473
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 71-332 8.98e-06

phenylalanyl-tRNA synthetase alpha chain; Provisional


Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 48.04  E-value: 8.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070   71 LSKVGRNLHNQKFHPLWLIKERVKEHFYQqyMGrsrtplFSVYDQLSPVVTTWQNFDSLLIPADHPSRKKGDNYYLN--- 147
Cdd:PTZ00326 216 FNALGKKIGGGNLHPLLKVRREFREILLE--MG------FEEMPTNRYVESSFWNFDALFQPQQHPARDAQDTFFLSkpe 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070  148 --------------------------------------RGHMLRAHTSAHQWDLLH-------AGLN----AFLVVGDVY 178
Cdd:PTZ00326 288 tskvndldddyvervkkvhevggygsigwrydwkleeaRKNILRTHTTAVSARMLYklaqeykKTGPfkpkKYFSIDRVF 367

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070  179 RRDQIDSQHYPVFHQLEGVrlfskhelfagVKD-GESL-QLFeessrsahkqetHTMEavklvEFDLKQVLTRLvthlfg 256
Cdd:PTZ00326 368 RNETLDATHLAEFHQVEGF-----------VIDrNLTLgDLI------------GTIR-----EFFRRIGITKL------ 413

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070  257 dglevRWVDCYFPFTHPSfeMEInF-----RGEWLEVLGCGVMEQQLVNSAGAQDR---IGWafGLGLERLAMVLYDIPD 328
Cdd:PTZ00326 414 -----RFKPAFNPYTEPS--MEI-FgyhpgLKKWVEVGNSGIFRPEMLRPMGFPEDvtvIAW--GLSLERPTMIKYGIKN 483


                 ....*
gi 61557070  329 IR-LF 332
Cdd:PTZ00326 484 IRdLF 488
syfB CHL00192
phenylalanyl-tRNA synthetase beta chain; Provisional
 377-471 1.18e-05

phenylalanyl-tRNA synthetase beta chain; Provisional


Pssm-ID: 214391 [Multi-domain]  Cd Length: 704  Bit Score: 47.78  E-value: 1.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557070  377 PFSKYPAVFNDISFWLPsENYTENDFYDIVRTVGGDLVEKVDLIDKF--EHPKTHRTSHCYRITYRHMERTLSQREVSSV 454
Cdd:CHL00192 608 PYSSYPKIIRDLSFIIK-KSISISKIKELIYQNGDNLLESITLFDYYkgKSIPNGHTSLGLRLTFQSENKTLTNEEIDRI 686

                         90
                 ....*....|....*..
gi 61557070  455 HQAVQEAAVQLLGVEGR 471
Cdd:CHL00192 687 QQNLQKVLEKKLNAEIR 703
 
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.
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