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Conserved domains on  [gi|55976225|sp|O95363|]
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RecName: Full=Phenylalanine--tRNA ligase, mitochondrial; AltName: Full=Phenylalanyl-tRNA synthetase; Short=PheRS; Flags: Precursor

Protein Classification

phenylalanine--tRNA ligase( domain architecture ID 1006086)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02788 super family cl33567
phenylalanine-tRNA synthetase
29-450 1.34e-180

phenylalanine-tRNA synthetase


The actual alignment was detected with superfamily member PLN02788:

Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 510.08  E-value: 1.34e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225   29 HQAWGSRPPAAECATQ-RAPG-SVVELLGKSYPQDD-------HSNLTRKVLTRVGRNLHNQQHHPLWLIKERVKEHFYK 99
Cdd:PLN02788   4 SSALVTPATAKSSSRRyRAPAvSAVEIGGVAIARDEvvreddpTNNVPDHIFSKIGMQLHRRPDHPLGILKNAIYDYFDE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  100 QYVGrfgtpLFSVYDNLSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQWDLLHAGLDAFLVVGDVYR 179
Cdd:PLN02788  84 NYSN-----KFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAHQAELLRAGHTHFLVTGDVYR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  180 RDQIDSQHYPIFHQLEAVRLFSKHELfagikdgeslqlfeqssrsahkqETHTMEAVKLVEFDLKQTLTRLMAHLFGDeL 259
Cdd:PLN02788 159 RDSIDATHYPVFHQMEGVRVFSPEEW-----------------------EASGLDGTDLAAEDLKKTLEGLARHLFGD-V 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  260 EIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVMEQQLVNSAGAQDRIGWAFGLGLERLAMILYDIPDIRLFWCEDERF 339
Cdd:PLN02788 215 EMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVTEQEILKNNGRSDNVAWAFGLGLERLAMVLFDIPDIRLFWSDDERF 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  340 LKQFCVSNInqKVKFQPLSKYPAVINDISFWLPSEnYAENDFYDLVRTIGGDLVEKVDLIDKFVHPKTHKTSHCYRITYR 419
Cdd:PLN02788 295 TSQFKEGQL--GVKFKPYSKYPPCYKDISFWISDE-FTENNLCEVVRGIAGDLVEEVKLIDNFTNPKKGKTSHCYRIVYR 371
                        410       420       430
                 ....*....|....*....|....*....|.
gi 55976225  420 HMERTLSQREVRHIHQALQEAAVQLLGVEGR 450
Cdd:PLN02788 372 SMERSLTDEEINALQDKVREEVQKKLGVELR 402
 
Name Accession Description Interval E-value
PLN02788 PLN02788
phenylalanine-tRNA synthetase
29-450 1.34e-180

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 510.08  E-value: 1.34e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225   29 HQAWGSRPPAAECATQ-RAPG-SVVELLGKSYPQDD-------HSNLTRKVLTRVGRNLHNQQHHPLWLIKERVKEHFYK 99
Cdd:PLN02788   4 SSALVTPATAKSSSRRyRAPAvSAVEIGGVAIARDEvvreddpTNNVPDHIFSKIGMQLHRRPDHPLGILKNAIYDYFDE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  100 QYVGrfgtpLFSVYDNLSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQWDLLHAGLDAFLVVGDVYR 179
Cdd:PLN02788  84 NYSN-----KFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAHQAELLRAGHTHFLVTGDVYR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  180 RDQIDSQHYPIFHQLEAVRLFSKHELfagikdgeslqlfeqssrsahkqETHTMEAVKLVEFDLKQTLTRLMAHLFGDeL 259
Cdd:PLN02788 159 RDSIDATHYPVFHQMEGVRVFSPEEW-----------------------EASGLDGTDLAAEDLKKTLEGLARHLFGD-V 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  260 EIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVMEQQLVNSAGAQDRIGWAFGLGLERLAMILYDIPDIRLFWCEDERF 339
Cdd:PLN02788 215 EMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVTEQEILKNNGRSDNVAWAFGLGLERLAMVLFDIPDIRLFWSDDERF 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  340 LKQFCVSNInqKVKFQPLSKYPAVINDISFWLPSEnYAENDFYDLVRTIGGDLVEKVDLIDKFVHPKTHKTSHCYRITYR 419
Cdd:PLN02788 295 TSQFKEGQL--GVKFKPYSKYPPCYKDISFWISDE-FTENNLCEVVRGIAGDLVEEVKLIDNFTNPKKGKTSHCYRIVYR 371
                        410       420       430
                 ....*....|....*....|....*....|.
gi 55976225  420 HMERTLSQREVRHIHQALQEAAVQLLGVEGR 450
Cdd:PLN02788 372 SMERSLTDEEINALQDKVREEVQKKLGVELR 402
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
51-448 1.07e-156

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: 451.84  E-value: 1.07e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225    51 VELLGKSYPQDDHS-NLTRKVLTRVGRNLHNQQHHPLWLIKERVKEHFYKQYVGRFGTPLFSVYDNLSPVVTTWQNFDSL 129
Cdd:TIGR00469   8 LEINGIKYATDGQTtNVTDKIIKLTDANKHLKEDHPLGIIRDLIEKKFNGADNNQRGNPLFKIFDNFKPVVTTMENFDNL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225   130 LIPADHPSRKKGDNYYLNRTHMLRAHTSAHQWDLLHAGLD-------AFLVVGDVYRRDQIDSQHYPIFHQLE--AVRLF 200
Cdd:TIGR00469  88 GFPADHPGRQKSDCYYINEQHLLRAHTSAHELECFQGGLDdsdniksGFLISADVYRRDEIDKTHYPVFHQADgaAIRKR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225   201 SKHELFagIKDGESLQLFEQSSRSAH------------------------KQETHTMEAVKLVEFDLKQTLTRLMAHLFG 256
Cdd:TIGR00469 168 TKADLF--EKEPGYIEKFEEDIRGTEadlnkenvkiildddsiplkennpKQEYASDLAVDLCEHELKHSIEGITKDLFG 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225   257 ---------------DELEIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVMEQQLVNSAGAQ--DRIGWAFGLGLERL 319
Cdd:TIGR00469 246 kkissmiknkanntpKELKVRWIDAYFPFTAPSWEIEIWFKDEWLELCGCGIIRHDILLRAGVHpsETIGWAFGLGLDRI 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225   320 AMILYDIPDIRLFWCEDERFLKQFCVSNINQKVKFQPLSKYPAVINDISFWLPSE-----NYAENDFYDLVRTIGGDLVE 394
Cdd:TIGR00469 326 AMLLFDIPDIRLFWSNDEGFLRQFSEGDLHLIPKFKPISHHPGCFNDLAFWLPEDieddaGFHENDFMDIIRNIAGDLVE 405
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 55976225   395 KVDLIDKFVHPKTHKTSHCYRITYRHMERTLSQREVRHIHQALQEAAVQLLGVE 448
Cdd:TIGR00469 406 QIKLVDKFKHPKTGKKSMCFRINYQHMDRNLTNAEVNEIHDMIASALVDEFNVE 459
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
84-338 1.81e-94

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: 284.05  E-value: 1.81e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  84 HPLWLIKERVKEHFYKQyvgrfgtpLFSVYDNlSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRT--HMLRAHTSAHQW 161
Cdd:cd00496   1 HPLNKVIEEIEDIFVSM--------GFTEVEG-PEVETDFYNFDALNIPQDHPARDMQDTFYINDParLLLRTHTSAVQA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225 162 DLLHA--GLDAFLVVGDVYRRDQIDSQHYPIFHQLEAVRLFSKhelfagikdgeslqlfeqssrsahkqethtmeavkLV 239
Cdd:cd00496  72 RALAKlkPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKG-----------------------------------LT 116
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225 240 EFDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINFHG--EWLEVLGCGVMEQQLVNSAGAQ-DRIGWAFGLGL 316
Cdd:cd00496 117 FADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYCPGclGWLEILGCGMVRPEVLENAGIDeEYSGFAFGIGL 196
                       250       260
                ....*....|....*....|..
gi 55976225 317 ERLAMILYDIPDIRLFWCEDER 338
Cdd:cd00496 197 ERLAMLKYGIPDIRLFYSNDLR 218
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
84-343 8.73e-53

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: 180.25  E-value: 8.73e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  84 HPLWLIKERVKEHFykqyvGRFGtplFSVYDnlSP-VVTTWQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQwd 162
Cdd:COG0016 107 HPLTQVIEEIEDIF-----VGMG---FEVAE--GPeIETDWYNFEALNIPPDHPARDMQDTFYIDDGLLLRTHTSPVQ-- 174
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225 163 lLHAGLD-----AFLVVGDVYRRDQIDSQHYPIFHQLE--AVrlfSKHELFAgikdgeslqlfeqssrsahkqethtmea 235
Cdd:COG0016 175 -IRTMEKqkppiRIIAPGRVYRRDESDATHSPMFHQVEglVV---DKGISFA---------------------------- 222
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225 236 vklvefDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINF------------HGEWLEVLGCG-----VMEqql 298
Cdd:COG0016 223 ------DLKGTLEEFAKAFFGEDVKVRFRPSYFPFTEPSAEVDISCficggkgcrvckGTGWLEILGCGmvhpnVLR--- 293
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 55976225 299 vnSAGaqdrI------GWAFGLGLERLAMILYDIPDIRLFWCEDERFLKQF 343
Cdd:COG0016 294 --AVG----IdpeeysGFAFGMGIERLAMLKYGIDDIRLFFENDLRFLRQF 338
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
83-343 8.11e-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: 166.99  E-value: 8.11e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225    83 HHPLWLIKERVKEHFYkqyvgRFGtplFSVYDNlSPVVTTWQNFDSLLIPADHPSRKKGDNYYL-------NRTHMLRAH 155
Cdd:pfam01409  16 LHPLTRTLERIRDIFL-----GMG---FEEVEG-PEVESDFYNFDALNIPQDHPARDMQDTFYLkkplkpvARRLLLRTH 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225   156 TSAHQWDLLHAGLDA---FLVVGDVYRRDQIDSQHYPIFHQLEAVRlfskhelfagIKDGESLQlfeqssrsahkqetht 232
Cdd:pfam01409  87 TTPVQARTLAKKPKPpikIFSIGRVFRRDQVDATHLPEFHQVEGLV----------VDENVTFA---------------- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225   233 meavklvefDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINF--HGEWLEVLGCGVMEQQLVNSAG-AQDRIG 309
Cdd:pfam01409 141 ---------DLKGVLEEFLRKFFGFEVKVRFRPSYFPFTEPSAEVDVYVckLGGWLEVGGAGMVHPNVLEAVGiDEDYSG 211
                         250       260       270
                  ....*....|....*....|....*....|....
gi 55976225   310 WAFGLGLERLAMILYDIPDIRLFWCEDERFLKQF 343
Cdd:pfam01409 212 FAFGLGVERLAMLKYGIDDIRDLYENDLRFLRQF 245
FDX-ACB smart00896
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
358-450 4.04e-31

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: 114.83  E-value: 4.04e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225    358 SKYPAVINDISFWLPsENYAENDFYDLVRTIGGDLVEKVDLIDKFVH-PKTHKTSHCYRITYRHMERTLSQREVRHIHQA 436
Cdd:smart00896   1 SKFPAVRRDLAFVVD-EDVPAAELLDAIREAGGDLLEDVRLFDVYEGgIPEGKKSLAYRLTYQSPDRTLTDEEVNAIHDK 79
                           90
                   ....*....|....
gi 55976225    437 LQEAAVQLLGVEGR 450
Cdd:smart00896  80 IVAALEKKFGAELR 93
 
Name Accession Description Interval E-value
PLN02788 PLN02788
phenylalanine-tRNA synthetase
29-450 1.34e-180

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 510.08  E-value: 1.34e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225   29 HQAWGSRPPAAECATQ-RAPG-SVVELLGKSYPQDD-------HSNLTRKVLTRVGRNLHNQQHHPLWLIKERVKEHFYK 99
Cdd:PLN02788   4 SSALVTPATAKSSSRRyRAPAvSAVEIGGVAIARDEvvreddpTNNVPDHIFSKIGMQLHRRPDHPLGILKNAIYDYFDE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  100 QYVGrfgtpLFSVYDNLSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQWDLLHAGLDAFLVVGDVYR 179
Cdd:PLN02788  84 NYSN-----KFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAHQAELLRAGHTHFLVTGDVYR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  180 RDQIDSQHYPIFHQLEAVRLFSKHELfagikdgeslqlfeqssrsahkqETHTMEAVKLVEFDLKQTLTRLMAHLFGDeL 259
Cdd:PLN02788 159 RDSIDATHYPVFHQMEGVRVFSPEEW-----------------------EASGLDGTDLAAEDLKKTLEGLARHLFGD-V 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  260 EIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVMEQQLVNSAGAQDRIGWAFGLGLERLAMILYDIPDIRLFWCEDERF 339
Cdd:PLN02788 215 EMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVTEQEILKNNGRSDNVAWAFGLGLERLAMVLFDIPDIRLFWSDDERF 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  340 LKQFCVSNInqKVKFQPLSKYPAVINDISFWLPSEnYAENDFYDLVRTIGGDLVEKVDLIDKFVHPKTHKTSHCYRITYR 419
Cdd:PLN02788 295 TSQFKEGQL--GVKFKPYSKYPPCYKDISFWISDE-FTENNLCEVVRGIAGDLVEEVKLIDNFTNPKKGKTSHCYRIVYR 371
                        410       420       430
                 ....*....|....*....|....*....|.
gi 55976225  420 HMERTLSQREVRHIHQALQEAAVQLLGVEGR 450
Cdd:PLN02788 372 SMERSLTDEEINALQDKVREEVQKKLGVELR 402
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
51-448 1.07e-156

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: 451.84  E-value: 1.07e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225    51 VELLGKSYPQDDHS-NLTRKVLTRVGRNLHNQQHHPLWLIKERVKEHFYKQYVGRFGTPLFSVYDNLSPVVTTWQNFDSL 129
Cdd:TIGR00469   8 LEINGIKYATDGQTtNVTDKIIKLTDANKHLKEDHPLGIIRDLIEKKFNGADNNQRGNPLFKIFDNFKPVVTTMENFDNL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225   130 LIPADHPSRKKGDNYYLNRTHMLRAHTSAHQWDLLHAGLD-------AFLVVGDVYRRDQIDSQHYPIFHQLE--AVRLF 200
Cdd:TIGR00469  88 GFPADHPGRQKSDCYYINEQHLLRAHTSAHELECFQGGLDdsdniksGFLISADVYRRDEIDKTHYPVFHQADgaAIRKR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225   201 SKHELFagIKDGESLQLFEQSSRSAH------------------------KQETHTMEAVKLVEFDLKQTLTRLMAHLFG 256
Cdd:TIGR00469 168 TKADLF--EKEPGYIEKFEEDIRGTEadlnkenvkiildddsiplkennpKQEYASDLAVDLCEHELKHSIEGITKDLFG 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225   257 ---------------DELEIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVMEQQLVNSAGAQ--DRIGWAFGLGLERL 319
Cdd:TIGR00469 246 kkissmiknkanntpKELKVRWIDAYFPFTAPSWEIEIWFKDEWLELCGCGIIRHDILLRAGVHpsETIGWAFGLGLDRI 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225   320 AMILYDIPDIRLFWCEDERFLKQFCVSNINQKVKFQPLSKYPAVINDISFWLPSE-----NYAENDFYDLVRTIGGDLVE 394
Cdd:TIGR00469 326 AMLLFDIPDIRLFWSNDEGFLRQFSEGDLHLIPKFKPISHHPGCFNDLAFWLPEDieddaGFHENDFMDIIRNIAGDLVE 405
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 55976225   395 KVDLIDKFVHPKTHKTSHCYRITYRHMERTLSQREVRHIHQALQEAAVQLLGVE 448
Cdd:TIGR00469 406 QIKLVDKFKHPKTGKKSMCFRINYQHMDRNLTNAEVNEIHDMIASALVDEFNVE 459
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
84-338 1.81e-94

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: 284.05  E-value: 1.81e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  84 HPLWLIKERVKEHFYKQyvgrfgtpLFSVYDNlSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRT--HMLRAHTSAHQW 161
Cdd:cd00496   1 HPLNKVIEEIEDIFVSM--------GFTEVEG-PEVETDFYNFDALNIPQDHPARDMQDTFYINDParLLLRTHTSAVQA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225 162 DLLHA--GLDAFLVVGDVYRRDQIDSQHYPIFHQLEAVRLFSKhelfagikdgeslqlfeqssrsahkqethtmeavkLV 239
Cdd:cd00496  72 RALAKlkPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKG-----------------------------------LT 116
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225 240 EFDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINFHG--EWLEVLGCGVMEQQLVNSAGAQ-DRIGWAFGLGL 316
Cdd:cd00496 117 FADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYCPGclGWLEILGCGMVRPEVLENAGIDeEYSGFAFGIGL 196
                       250       260
                ....*....|....*....|..
gi 55976225 317 ERLAMILYDIPDIRLFWCEDER 338
Cdd:cd00496 197 ERLAMLKYGIPDIRLFYSNDLR 218
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
84-343 8.73e-53

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: 180.25  E-value: 8.73e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  84 HPLWLIKERVKEHFykqyvGRFGtplFSVYDnlSP-VVTTWQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQwd 162
Cdd:COG0016 107 HPLTQVIEEIEDIF-----VGMG---FEVAE--GPeIETDWYNFEALNIPPDHPARDMQDTFYIDDGLLLRTHTSPVQ-- 174
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225 163 lLHAGLD-----AFLVVGDVYRRDQIDSQHYPIFHQLE--AVrlfSKHELFAgikdgeslqlfeqssrsahkqethtmea 235
Cdd:COG0016 175 -IRTMEKqkppiRIIAPGRVYRRDESDATHSPMFHQVEglVV---DKGISFA---------------------------- 222
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225 236 vklvefDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINF------------HGEWLEVLGCG-----VMEqql 298
Cdd:COG0016 223 ------DLKGTLEEFAKAFFGEDVKVRFRPSYFPFTEPSAEVDISCficggkgcrvckGTGWLEILGCGmvhpnVLR--- 293
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 55976225 299 vnSAGaqdrI------GWAFGLGLERLAMILYDIPDIRLFWCEDERFLKQF 343
Cdd:COG0016 294 --AVG----IdpeeysGFAFGMGIERLAMLKYGIDDIRLFFENDLRFLRQF 338
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
83-343 8.11e-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: 166.99  E-value: 8.11e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225    83 HHPLWLIKERVKEHFYkqyvgRFGtplFSVYDNlSPVVTTWQNFDSLLIPADHPSRKKGDNYYL-------NRTHMLRAH 155
Cdd:pfam01409  16 LHPLTRTLERIRDIFL-----GMG---FEEVEG-PEVESDFYNFDALNIPQDHPARDMQDTFYLkkplkpvARRLLLRTH 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225   156 TSAHQWDLLHAGLDA---FLVVGDVYRRDQIDSQHYPIFHQLEAVRlfskhelfagIKDGESLQlfeqssrsahkqetht 232
Cdd:pfam01409  87 TTPVQARTLAKKPKPpikIFSIGRVFRRDQVDATHLPEFHQVEGLV----------VDENVTFA---------------- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225   233 meavklvefDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINF--HGEWLEVLGCGVMEQQLVNSAG-AQDRIG 309
Cdd:pfam01409 141 ---------DLKGVLEEFLRKFFGFEVKVRFRPSYFPFTEPSAEVDVYVckLGGWLEVGGAGMVHPNVLEAVGiDEDYSG 211
                         250       260       270
                  ....*....|....*....|....*....|....
gi 55976225   310 WAFGLGLERLAMILYDIPDIRLFWCEDERFLKQF 343
Cdd:pfam01409 212 FAFGLGVERLAMLKYGIDDIRDLYENDLRFLRQF 245
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
84-343 1.03e-48

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: 168.26  E-value: 1.03e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225    84 HPLWLIKERVKEHFYKqyvgrFGtplFSVydNLSPVVTT-WQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQwd 162
Cdd:TIGR00468  72 HPLTRVIDEIRDIFLG-----LG---FTE--ETGPEVETdFWNFDALNIPQDHPARDMQDTFYIKDRLLLRTHTTAVQ-- 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225   163 lLHAGLDA------FLVVGDVYRRDQIDSQHYPIFHQLEAVRlfskhelfagIKDGESLQlfeqssrsahkqethtmeav 236
Cdd:TIGR00468 140 -LRTMEEQekppirIFSPGRVFRNDTVDATHLPEFHQVEGLV----------IDKNISFT-------------------- 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225   237 klvefDLKQTLtRLMAHLFGDELEIRWVDCYFPFTHPSFEMEInFHGE---WLEVLGCGVMEQQLVNSAGAQDRI-GWAF 312
Cdd:TIGR00468 189 -----NLKGFL-EEFLKKMFGETEIRFRPSYFPFTEPSAEIDV-YCPEgkgWLEVLGAGMFRPEVLEPMGIDPTYpGFAW 261
                         250       260       270
                  ....*....|....*....|....*....|.
gi 55976225   313 GLGLERLAMILYDIPDIRLFWCEDERFLKQF 343
Cdd:TIGR00468 262 GIGIERLAMLKYGITDIRDLYENDLRFLRQF 292
FDX-ACB smart00896
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
358-450 4.04e-31

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: 114.83  E-value: 4.04e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225    358 SKYPAVINDISFWLPsENYAENDFYDLVRTIGGDLVEKVDLIDKFVH-PKTHKTSHCYRITYRHMERTLSQREVRHIHQA 436
Cdd:smart00896   1 SKFPAVRRDLAFVVD-EDVPAAELLDAIREAGGDLLEDVRLFDVYEGgIPEGKKSLAYRLTYQSPDRTLTDEEVNAIHDK 79
                           90
                   ....*....|....
gi 55976225    437 LQEAAVQLLGVEGR 450
Cdd:smart00896  80 IVAALEKKFGAELR 93
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
117-332 2.73e-24

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 104.91  E-value: 2.73e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  117 SPVVTT--WqNFDSLLIPADHPSRKKGDNYYLN----------------RTH-----------------------MLRAH 155
Cdd:PRK04172 256 GPLVETefW-NFDALFQPQDHPAREMQDTFYLKypgigdlpeelvervkEVHehggdtgsrgwgykwdediakrlVLRTH 334
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  156 T---SAHQwdlLHAGLDA---FLVVGDVYRRDQIDSQHYPIFHQLEavrlfskhelfaGIKDGESLqlfeqssrsahkqe 229
Cdd:PRK04172 335 TtalSARY---LASRPEPpqkYFSIGRVFRPDTIDATHLPEFYQLE------------GIVMGEDV-------------- 385
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  230 thtmeAVKlvefDLKQTLTRlMAHLFGDElEIRWVDCYFPFTHPSFEMEInFH--GEWLEVLGCGVMEQQLVNSAGAQDR 307
Cdd:PRK04172 386 -----SFR----DLLGILKE-FYKRLGFE-EVKFRPAYFPFTEPSVEVEV-YHegLGWVELGGAGIFRPEVLEPLGIDVP 453
                        250       260
                 ....*....|....*....|....*.
gi 55976225  308 IGwAFGLGLERLAMILYDIPDIR-LF 332
Cdd:PRK04172 454 VL-AWGLGIERLAMLRLGLDDIRdLY 478
FDX-ACB pfam03147
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
358-450 6.58e-22

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: 89.46  E-value: 6.58e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225   358 SKYPAVINDISFWLPsENYAENDFYDLVRTIGGDLVEKVDLIDKFVHPK--THKTSHCYRITYRHMERTLSQREVRHIHQ 435
Cdd:pfam03147   1 SKYPAVRRDLAFVVD-EDVPAADILKAIREAGGELLESVELFDVYRGEKipEGKKSLAFRLTFQSPERTLTDEEVNAIIE 79
                          90
                  ....*....|....*
gi 55976225   436 ALQEAAVQLLGVEGR 450
Cdd:pfam03147  80 KIVEALEKKFGAELR 94
pheT_bact TIGR00472
phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Every known example of ...
241-450 1.80e-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: 78.87  E-value: 1.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225   241 FDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINFHGEwleVLGC-GVMEQQLVNSAGAQDRIgWAFGLGLERL 319
Cdd:TIGR00472 615 YDLKGDVESLLELLGLSDDVYFKNTAENEELHPGQSATIYLKGK---KIGFiGELHPEIAKKYDLKEPT-FVFELDLDRL 690
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225   320 AMILYDIPdirlfwcederflkqfcvsninqkvKFQPLSKYPAVINDISFWLPSENYAeNDFYDLVRTIGGDLVEKVDLI 399
Cdd:TIGR00472 691 LESLKKVP-------------------------KYRPISKFPAVTRDISFLVPKDVPA-NEIIKLIKKSGLELLEEVELF 744
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 55976225   400 DKFV--HPKTHKTSHCYRITYRHMERTLSQREVRHIHQALQEAAVQLLGVEGR 450
Cdd:TIGR00472 745 DVYQgkNIGEGKKSLALRLVLRDKERTLTDEEINKIVEKVLNALKEKLGAELR 797
pheT PRK00629
phenylalanyl-tRNA synthetase subunit beta; Reviewed
351-448 1.26e-14

phenylalanyl-tRNA synthetase subunit beta; Reviewed


Pssm-ID: 234804 [Multi-domain]  Cd Length: 791  Bit Score: 76.36  E-value: 1.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  351 KVKFQPLSKYPAVINDISFWLPsENYAENDFYDLVRTIGGDLVEKVDLIDKFVHPK--THKTSHCYRITYRHMERTLSQR 428
Cdd:PRK00629 690 LPKYKPISKFPAVRRDLALVVD-EDVPAADILKAIKKAGGKLLESVELFDVYEGKGigEGKKSLAFRLTFQDPDRTLTDE 768
                         90       100
                 ....*....|....*....|
gi 55976225  429 EVRHIHQALQEAAVQLLGVE 448
Cdd:PRK00629 769 EINAAMDKIVAALEEKFGAE 788
PheT COG0072
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; ...
345-448 4.15e-14

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: 74.43  E-value: 4.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225 345 VSNINQKVKFQPLSKYPAVINDISFWLPsENYAENDFYDLVRTIGGDLVEKVDLIDKFVHPK--THKTSHCYRITYRHME 422
Cdd:COG0072 686 LELARKVPKYKPISKFPAVRRDLALVVD-EDVPAADVLDAIRKAAGKLLEDVRLFDVYEGKGvpEGKKSLAFSLTLQDPD 764
                        90       100
                ....*....|....*....|....*.
gi 55976225 423 RTLSQREVRHIHQALQEAAVQLLGVE 448
Cdd:COG0072 765 RTLTDEEIDAAMDKIVAALEKKFGAE 790
PLN02853 PLN02853
Probable phenylalanyl-tRNA synthetase alpha chain
123-332 1.24e-08

Probable phenylalanyl-tRNA synthetase alpha chain


Pssm-ID: 215458 [Multi-domain]  Cd Length: 492  Bit Score: 56.99  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  123 WqNFDSLLIPADHPSRKKGDNYYLN-----------------RTH----------------------MLRAHTSAHQWDL 163
Cdd:PLN02853 253 W-NFDALFQPQQHPARDSHDTFFLKapattrqlpedyvervkTVHesggygsigygydwkreeanknLLRTHTTAVSSRM 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  164 LHA-GLDAF-----LVVGDVYRRDQIDSQHYPIFHQLEAVrlfskhelfagIKD-GESLQlfeqssrsahkqethtmeav 236
Cdd:PLN02853 332 LYKlAQKGFkpkryFSIDRVFRNEAVDRTHLAEFHQVEGL-----------VCDrGLTLG-------------------- 380
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  237 klvefDLKQTLTRLMAHLFGDELeiRWVDCYFPFTHPSfeMEI-NFH---GEWLEVLGCGVMEQQLVNSAGAQDR---IG 309
Cdd:PLN02853 381 -----DLIGVLEDFFSRLGMTKL--RFKPAYNPYTEPS--MEIfSYHeglKKWVEVGNSGMFRPEMLLPMGLPEDvnvIA 451
                        250       260
                 ....*....|....*....|....
gi 55976225  310 WafGLGLERLAMILYDIPDIR-LF 332
Cdd:PLN02853 452 W--GLSLERPTMILYGIDNIRdLF 473
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
123-332 4.23e-07

phenylalanyl-tRNA synthetase alpha chain; Provisional


Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 52.28  E-value: 4.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  123 WqNFDSLLIPADHPSR----------------KKGDNYYLNR---TH----------------------MLRAHTSAHQW 161
Cdd:PTZ00326 261 W-NFDALFQPQQHPARdaqdtfflskpetskvNDLDDDYVERvkkVHevggygsigwrydwkleearknILRTHTTAVSA 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  162 DLLH-------AGLD----AFLVVGDVYRRDQIDSQHYPIFHQLEAVrlfskhelfagikdgeslqlfeqssrsahkqet 230
Cdd:PTZ00326 340 RMLYklaqeykKTGPfkpkKYFSIDRVFRNETLDATHLAEFHQVEGF--------------------------------- 386
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  231 htmeavkLVEFDLkqTLTRLMA--HLFGDELEI---RWVDCYFPFTHPSfeMEI-NFH---GEWLEVLGCGVMEQQLVNS 301
Cdd:PTZ00326 387 -------VIDRNL--TLGDLIGtiREFFRRIGItklRFKPAFNPYTEPS--MEIfGYHpglKKWVEVGNSGIFRPEMLRP 455
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 55976225  302 AGAQDR---IGWafGLGLERLAMILYDIPDIR-LF 332
Cdd:PTZ00326 456 MGFPEDvtvIAW--GLSLERPTMIKYGIKNIRdLF 488
syfB CHL00192
phenylalanyl-tRNA synthetase beta chain; Provisional
354-450 5.36e-07

phenylalanyl-tRNA synthetase beta chain; Provisional


Pssm-ID: 214391 [Multi-domain]  Cd Length: 704  Bit Score: 52.01  E-value: 5.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55976225  354 FQPLSKYPAVINDISFWLPsENYAENDFYDLVRTIGGDLVEKVDLIDKFVHP--KTHKTSHCYRITYRHMERTLSQREVR 431
Cdd:CHL00192 606 YQPYSSYPKIIRDLSFIIK-KSISISKIKELIYQNGDNLLESITLFDYYKGKsiPNGHTSLGLRLTFQSENKTLTNEEID 684
                         90
                 ....*....|....*....
gi 55976225  432 HIHQALQEAAVQLLGVEGR 450
Cdd:CHL00192 685 RIQQNLQKVLEKKLNAEIR 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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