|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02788 |
PLN02788 |
phenylalanine-tRNA synthetase |
29-407 |
2.62e-162 |
|
phenylalanine-tRNA synthetase
Pssm-ID: 215422 [Multi-domain] Cd Length: 402 Bit Score: 462.31 E-value: 2.62e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 29 HQAWGSRPPAAECATQ-RAPG-SVVELLGKSYPQDD-------HSNLTRKVLTRVGRNLHNQQHHPLWLIKERVKEHFYK 99
Cdd:PLN02788 4 SSALVTPATAKSSSRRyRAPAvSAVEIGGVAIARDEvvreddpTNNVPDHIFSKIGMQLHRRPDHPLGILKNAIYDYFDE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 100 QYVGrfgtpLFSVYDNLSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQWDLLHAGLDAFLVVGDVYR 179
Cdd:PLN02788 84 NYSN-----KFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAHQAELLRAGHTHFLVTGDVYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 180 RDQIDSQHYPIFHQLEAVRLFSKHELfagikdgeslqlfeqssrsahkqETHTMEAVKLVEFDLKQTLTRLMAHLFGDeL 259
Cdd:PLN02788 159 RDSIDATHYPVFHQMEGVRVFSPEEW-----------------------EASGLDGTDLAAEDLKKTLEGLARHLFGD-V 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 260 EIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVMEQQLVNSAGAQDRIGWAFGLGLERLAMILYDIPDIRLFWCEDERF 339
Cdd:PLN02788 215 EMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVTEQEILKNNGRSDNVAWAFGLGLERLAMVLFDIPDIRLFWSDDERF 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767939112 340 LKQFCVSNInqKVKFQPLSKYPAVINDISFWLPSEnYAENDFYDLVRTIGGDLVEKVDLIDKFVHPKK 407
Cdd:PLN02788 295 TSQFKEGQL--GVKFKPYSKYPPCYKDISFWISDE-FTENNLCEVVRGIAGDLVEEVKLIDNFTNPKK 359
|
|
| pheS_mito |
TIGR00469 |
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ... |
51-406 |
1.64e-138 |
|
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: 404.07 E-value: 1.64e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 51 VELLGKSYPQDDHS-NLTRKVLTRVGRNLHNQQHHPLWLIKERVKEHFYKQYVGRFGTPLFSVYDNLSPVVTTWQNFDSL 129
Cdd:TIGR00469 8 LEINGIKYATDGQTtNVTDKIIKLTDANKHLKEDHPLGIIRDLIEKKFNGADNNQRGNPLFKIFDNFKPVVTTMENFDNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 130 LIPADHPSRKKGDNYYLNRTHMLRAHTSAHQWDLLHAGLD-------AFLVVGDVYRRDQIDSQHYPIFHQLE--AVRLF 200
Cdd:TIGR00469 88 GFPADHPGRQKSDCYYINEQHLLRAHTSAHELECFQGGLDdsdniksGFLISADVYRRDEIDKTHYPVFHQADgaAIRKR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 201 SKHELFagIKDGESLQLFEQSSRSAH------------------------KQETHTMEAVKLVEFDLKQTLTRLMAHLFG 256
Cdd:TIGR00469 168 TKADLF--EKEPGYIEKFEEDIRGTEadlnkenvkiildddsiplkennpKQEYASDLAVDLCEHELKHSIEGITKDLFG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 257 ---------------DELEIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVMEQQLVNSAGAQ--DRIGWAFGLGLERL 319
Cdd:TIGR00469 246 kkissmiknkanntpKELKVRWIDAYFPFTAPSWEIEIWFKDEWLELCGCGIIRHDILLRAGVHpsETIGWAFGLGLDRI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 320 AMILYDIPDIRLFWCEDERFLKQFCVSNINQKVKFQPLSKYPAVINDISFWLPSE-----NYAENDFYDLVRTIGGDLVE 394
Cdd:TIGR00469 326 AMLLFDIPDIRLFWSNDEGFLRQFSEGDLHLIPKFKPISHHPGCFNDLAFWLPEDieddaGFHENDFMDIIRNIAGDLVE 405
|
410
....*....|..
gi 767939112 395 KVDLIDKFVHPK 406
Cdd:TIGR00469 406 QIKLVDKFKHPK 417
|
|
| PheRS_alpha_core |
cd00496 |
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ... |
84-338 |
6.88e-95 |
|
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: 283.67 E-value: 6.88e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 84 HPLWLIKERVKEHFYKQyvgrfgtpLFSVYDNlSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRT--HMLRAHTSAHQW 161
Cdd:cd00496 1 HPLNKVIEEIEDIFVSM--------GFTEVEG-PEVETDFYNFDALNIPQDHPARDMQDTFYINDParLLLRTHTSAVQA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 162 DLLHA--GLDAFLVVGDVYRRDQIDSQHYPIFHQLEAVRLFSKhelfagikdgeslqlfeqssrsahkqethtmeavkLV 239
Cdd:cd00496 72 RALAKlkPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKG-----------------------------------LT 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 240 EFDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINFHG--EWLEVLGCGVMEQQLVNSAGAQ-DRIGWAFGLGL 316
Cdd:cd00496 117 FADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYCPGclGWLEILGCGMVRPEVLENAGIDeEYSGFAFGIGL 196
|
250 260
....*....|....*....|..
gi 767939112 317 ERLAMILYDIPDIRLFWCEDER 338
Cdd:cd00496 197 ERLAMLKYGIPDIRLFYSNDLR 218
|
|
| PheS |
COG0016 |
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ... |
84-343 |
2.06e-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: 181.02 E-value: 2.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 84 HPLWLIKERVKEHFykqyvGRFGtplFSVYDnlSP-VVTTWQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQwd 162
Cdd:COG0016 107 HPLTQVIEEIEDIF-----VGMG---FEVAE--GPeIETDWYNFEALNIPPDHPARDMQDTFYIDDGLLLRTHTSPVQ-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 163 lLHAGLD-----AFLVVGDVYRRDQIDSQHYPIFHQLE--AVrlfSKHELFAgikdgeslqlfeqssrsahkqethtmea 235
Cdd:COG0016 175 -IRTMEKqkppiRIIAPGRVYRRDESDATHSPMFHQVEglVV---DKGISFA---------------------------- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 236 vklvefDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINF------------HGEWLEVLGCG-----VMEqql 298
Cdd:COG0016 223 ------DLKGTLEEFAKAFFGEDVKVRFRPSYFPFTEPSAEVDISCficggkgcrvckGTGWLEILGCGmvhpnVLR--- 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 767939112 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 |
4.26e-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: 4.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 83 HHPLWLIKERVKEHFYkqyvgRFGtplFSVYDNlSPVVTTWQNFDSLLIPADHPSRKKGDNYYL-------NRTHMLRAH 155
Cdd:pfam01409 16 LHPLTRTLERIRDIFL-----GMG---FEEVEG-PEVESDFYNFDALNIPQDHPARDMQDTFYLkkplkpvARRLLLRTH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 156 TSAHQWDLLHAGLDA---FLVVGDVYRRDQIDSQHYPIFHQLEAVRlfskhelfagIKDGESLQlfeqssrsahkqetht 232
Cdd:pfam01409 87 TTPVQARTLAKKPKPpikIFSIGRVFRRDQVDATHLPEFHQVEGLV----------VDENVTFA---------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 233 meavklvefDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINF--HGEWLEVLGCGVMEQQLVNSAG-AQDRIG 309
Cdd:pfam01409 141 ---------DLKGVLEEFLRKFFGFEVKVRFRPSYFPFTEPSAEVDVYVckLGGWLEVGGAGMVHPNVLEAVGiDEDYSG 211
|
250 260 270
....*....|....*....|....*....|....
gi 767939112 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 ... |
358-408 |
1.75e-12 |
|
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: 62.83 E-value: 1.75e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767939112 358 SKYPAVINDISFWLPsENYAENDFYDLVRTIGGDLVEKVDLIDKFVHPKKP 408
Cdd:smart00896 1 SKFPAVRRDLAFVVD-EDVPAAELLDAIREAGGDLLEDVRLFDVYEGGIPE 50
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02788 |
PLN02788 |
phenylalanine-tRNA synthetase |
29-407 |
2.62e-162 |
|
phenylalanine-tRNA synthetase
Pssm-ID: 215422 [Multi-domain] Cd Length: 402 Bit Score: 462.31 E-value: 2.62e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 29 HQAWGSRPPAAECATQ-RAPG-SVVELLGKSYPQDD-------HSNLTRKVLTRVGRNLHNQQHHPLWLIKERVKEHFYK 99
Cdd:PLN02788 4 SSALVTPATAKSSSRRyRAPAvSAVEIGGVAIARDEvvreddpTNNVPDHIFSKIGMQLHRRPDHPLGILKNAIYDYFDE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 100 QYVGrfgtpLFSVYDNLSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQWDLLHAGLDAFLVVGDVYR 179
Cdd:PLN02788 84 NYSN-----KFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAHQAELLRAGHTHFLVTGDVYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 180 RDQIDSQHYPIFHQLEAVRLFSKHELfagikdgeslqlfeqssrsahkqETHTMEAVKLVEFDLKQTLTRLMAHLFGDeL 259
Cdd:PLN02788 159 RDSIDATHYPVFHQMEGVRVFSPEEW-----------------------EASGLDGTDLAAEDLKKTLEGLARHLFGD-V 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 260 EIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVMEQQLVNSAGAQDRIGWAFGLGLERLAMILYDIPDIRLFWCEDERF 339
Cdd:PLN02788 215 EMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVTEQEILKNNGRSDNVAWAFGLGLERLAMVLFDIPDIRLFWSDDERF 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767939112 340 LKQFCVSNInqKVKFQPLSKYPAVINDISFWLPSEnYAENDFYDLVRTIGGDLVEKVDLIDKFVHPKK 407
Cdd:PLN02788 295 TSQFKEGQL--GVKFKPYSKYPPCYKDISFWISDE-FTENNLCEVVRGIAGDLVEEVKLIDNFTNPKK 359
|
|
| pheS_mito |
TIGR00469 |
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ... |
51-406 |
1.64e-138 |
|
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: 404.07 E-value: 1.64e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 51 VELLGKSYPQDDHS-NLTRKVLTRVGRNLHNQQHHPLWLIKERVKEHFYKQYVGRFGTPLFSVYDNLSPVVTTWQNFDSL 129
Cdd:TIGR00469 8 LEINGIKYATDGQTtNVTDKIIKLTDANKHLKEDHPLGIIRDLIEKKFNGADNNQRGNPLFKIFDNFKPVVTTMENFDNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 130 LIPADHPSRKKGDNYYLNRTHMLRAHTSAHQWDLLHAGLD-------AFLVVGDVYRRDQIDSQHYPIFHQLE--AVRLF 200
Cdd:TIGR00469 88 GFPADHPGRQKSDCYYINEQHLLRAHTSAHELECFQGGLDdsdniksGFLISADVYRRDEIDKTHYPVFHQADgaAIRKR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 201 SKHELFagIKDGESLQLFEQSSRSAH------------------------KQETHTMEAVKLVEFDLKQTLTRLMAHLFG 256
Cdd:TIGR00469 168 TKADLF--EKEPGYIEKFEEDIRGTEadlnkenvkiildddsiplkennpKQEYASDLAVDLCEHELKHSIEGITKDLFG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 257 ---------------DELEIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVMEQQLVNSAGAQ--DRIGWAFGLGLERL 319
Cdd:TIGR00469 246 kkissmiknkanntpKELKVRWIDAYFPFTAPSWEIEIWFKDEWLELCGCGIIRHDILLRAGVHpsETIGWAFGLGLDRI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 320 AMILYDIPDIRLFWCEDERFLKQFCVSNINQKVKFQPLSKYPAVINDISFWLPSE-----NYAENDFYDLVRTIGGDLVE 394
Cdd:TIGR00469 326 AMLLFDIPDIRLFWSNDEGFLRQFSEGDLHLIPKFKPISHHPGCFNDLAFWLPEDieddaGFHENDFMDIIRNIAGDLVE 405
|
410
....*....|..
gi 767939112 395 KVDLIDKFVHPK 406
Cdd:TIGR00469 406 QIKLVDKFKHPK 417
|
|
| PheRS_alpha_core |
cd00496 |
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ... |
84-338 |
6.88e-95 |
|
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: 283.67 E-value: 6.88e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 84 HPLWLIKERVKEHFYKQyvgrfgtpLFSVYDNlSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRT--HMLRAHTSAHQW 161
Cdd:cd00496 1 HPLNKVIEEIEDIFVSM--------GFTEVEG-PEVETDFYNFDALNIPQDHPARDMQDTFYINDParLLLRTHTSAVQA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 162 DLLHA--GLDAFLVVGDVYRRDQIDSQHYPIFHQLEAVRLFSKhelfagikdgeslqlfeqssrsahkqethtmeavkLV 239
Cdd:cd00496 72 RALAKlkPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKG-----------------------------------LT 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 240 EFDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINFHG--EWLEVLGCGVMEQQLVNSAGAQ-DRIGWAFGLGL 316
Cdd:cd00496 117 FADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYCPGclGWLEILGCGMVRPEVLENAGIDeEYSGFAFGIGL 196
|
250 260
....*....|....*....|..
gi 767939112 317 ERLAMILYDIPDIRLFWCEDER 338
Cdd:cd00496 197 ERLAMLKYGIPDIRLFYSNDLR 218
|
|
| PheS |
COG0016 |
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ... |
84-343 |
2.06e-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: 181.02 E-value: 2.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 84 HPLWLIKERVKEHFykqyvGRFGtplFSVYDnlSP-VVTTWQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQwd 162
Cdd:COG0016 107 HPLTQVIEEIEDIF-----VGMG---FEVAE--GPeIETDWYNFEALNIPPDHPARDMQDTFYIDDGLLLRTHTSPVQ-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 163 lLHAGLD-----AFLVVGDVYRRDQIDSQHYPIFHQLE--AVrlfSKHELFAgikdgeslqlfeqssrsahkqethtmea 235
Cdd:COG0016 175 -IRTMEKqkppiRIIAPGRVYRRDESDATHSPMFHQVEglVV---DKGISFA---------------------------- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 236 vklvefDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINF------------HGEWLEVLGCG-----VMEqql 298
Cdd:COG0016 223 ------DLKGTLEEFAKAFFGEDVKVRFRPSYFPFTEPSAEVDISCficggkgcrvckGTGWLEILGCGmvhpnVLR--- 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 767939112 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 |
4.26e-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: 4.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 83 HHPLWLIKERVKEHFYkqyvgRFGtplFSVYDNlSPVVTTWQNFDSLLIPADHPSRKKGDNYYL-------NRTHMLRAH 155
Cdd:pfam01409 16 LHPLTRTLERIRDIFL-----GMG---FEEVEG-PEVESDFYNFDALNIPQDHPARDMQDTFYLkkplkpvARRLLLRTH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 156 TSAHQWDLLHAGLDA---FLVVGDVYRRDQIDSQHYPIFHQLEAVRlfskhelfagIKDGESLQlfeqssrsahkqetht 232
Cdd:pfam01409 87 TTPVQARTLAKKPKPpikIFSIGRVFRRDQVDATHLPEFHQVEGLV----------VDENVTFA---------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 233 meavklvefDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINF--HGEWLEVLGCGVMEQQLVNSAG-AQDRIG 309
Cdd:pfam01409 141 ---------DLKGVLEEFLRKFFGFEVKVRFRPSYFPFTEPSAEVDVYVckLGGWLEVGGAGMVHPNVLEAVGiDEDYSG 211
|
250 260 270
....*....|....*....|....*....|....
gi 767939112 310 WAFGLGLERLAMILYDIPDIRLFWCEDERFLKQF 343
Cdd:pfam01409 212 FAFGLGVERLAMLKYGIDDIRDLYENDLRFLRQF 245
|
|
| pheS |
TIGR00468 |
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ... |
84-343 |
5.31e-49 |
|
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: 5.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 84 HPLWLIKERVKEHFYKqyvgrFGtplFSVydNLSPVVTT-WQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQwd 162
Cdd:TIGR00468 72 HPLTRVIDEIRDIFLG-----LG---FTE--ETGPEVETdFWNFDALNIPQDHPARDMQDTFYIKDRLLLRTHTTAVQ-- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 163 lLHAGLDA------FLVVGDVYRRDQIDSQHYPIFHQLEAVRlfskhelfagIKDGESLQlfeqssrsahkqethtmeav 236
Cdd:TIGR00468 140 -LRTMEEQekppirIFSPGRVFRNDTVDATHLPEFHQVEGLV----------IDKNISFT-------------------- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 237 klvefDLKQTLtRLMAHLFGDELEIRWVDCYFPFTHPSFEMEInFHGE---WLEVLGCGVMEQQLVNSAGAQDRI-GWAF 312
Cdd:TIGR00468 189 -----NLKGFL-EEFLKKMFGETEIRFRPSYFPFTEPSAEIDV-YCPEgkgWLEVLGAGMFRPEVLEPMGIDPTYpGFAW 261
|
250 260 270
....*....|....*....|....*....|.
gi 767939112 313 GLGLERLAMILYDIPDIRLFWCEDERFLKQF 343
Cdd:TIGR00468 262 GIGIERLAMLKYGITDIRDLYENDLRFLRQF 292
|
|
| pheS |
PRK04172 |
phenylalanine--tRNA ligase subunit alpha; |
117-332 |
1.56e-24 |
|
phenylalanine--tRNA ligase subunit alpha;
Pssm-ID: 235239 [Multi-domain] Cd Length: 489 Bit Score: 105.30 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 117 SPVVTT--WqNFDSLLIPADHPSRKKGDNYYLN----------------RTH-----------------------MLRAH 155
Cdd:PRK04172 256 GPLVETefW-NFDALFQPQDHPAREMQDTFYLKypgigdlpeelvervkEVHehggdtgsrgwgykwdediakrlVLRTH 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 156 T---SAHQwdlLHAGLDA---FLVVGDVYRRDQIDSQHYPIFHQLEavrlfskhelfaGIKDGESLqlfeqssrsahkqe 229
Cdd:PRK04172 335 TtalSARY---LASRPEPpqkYFSIGRVFRPDTIDATHLPEFYQLE------------GIVMGEDV-------------- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 230 thtmeAVKlvefDLKQTLTRlMAHLFGDElEIRWVDCYFPFTHPSFEMEInFH--GEWLEVLGCGVMEQQLVNSAGAQDR 307
Cdd:PRK04172 386 -----SFR----DLLGILKE-FYKRLGFE-EVKFRPAYFPFTEPSVEVEV-YHegLGWVELGGAGIFRPEVLEPLGIDVP 453
|
250 260
....*....|....*....|....*.
gi 767939112 308 IGwAFGLGLERLAMILYDIPDIR-LF 332
Cdd:PRK04172 454 VL-AWGLGIERLAMLRLGLDDIRdLY 478
|
|
| FDX-ACB |
smart00896 |
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ... |
358-408 |
1.75e-12 |
|
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: 62.83 E-value: 1.75e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767939112 358 SKYPAVINDISFWLPsENYAENDFYDLVRTIGGDLVEKVDLIDKFVHPKKP 408
Cdd:smart00896 1 SKFPAVRRDLAFVVD-EDVPAAELLDAIREAGGDLLEDVRLFDVYEGGIPE 50
|
|
| FDX-ACB |
pfam03147 |
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ... |
358-409 |
9.74e-09 |
|
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: 52.48 E-value: 9.74e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 767939112 358 SKYPAVINDISFWLPsENYAENDFYDLVRTIGGDLVEKVDLIDKFVHPKKPS 409
Cdd:pfam03147 1 SKYPAVRRDLAFVVD-EDVPAADILKAIREAGGELLESVELFDVYRGEKIPE 51
|
|
| PLN02853 |
PLN02853 |
Probable phenylalanyl-tRNA synthetase alpha chain |
123-332 |
1.10e-08 |
|
Probable phenylalanyl-tRNA synthetase alpha chain
Pssm-ID: 215458 [Multi-domain] Cd Length: 492 Bit Score: 56.99 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 123 WqNFDSLLIPADHPSRKKGDNYYLN-----------------RTH----------------------MLRAHTSAHQWDL 163
Cdd:PLN02853 253 W-NFDALFQPQQHPARDSHDTFFLKapattrqlpedyvervkTVHesggygsigygydwkreeanknLLRTHTTAVSSRM 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 164 LHA-GLDAF-----LVVGDVYRRDQIDSQHYPIFHQLEAVrlfskhelfagIKD-GESLQlfeqssrsahkqethtmeav 236
Cdd:PLN02853 332 LYKlAQKGFkpkryFSIDRVFRNEAVDRTHLAEFHQVEGL-----------VCDrGLTLG-------------------- 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 237 klvefDLKQTLTRLMAHLFGDELeiRWVDCYFPFTHPSfeMEI-NFH---GEWLEVLGCGVMEQQLVNSAGAQDR---IG 309
Cdd:PLN02853 381 -----DLIGVLEDFFSRLGMTKL--RFKPAYNPYTEPS--MEIfSYHeglKKWVEVGNSGMFRPEMLLPMGLPEDvnvIA 451
|
250 260
....*....|....*....|....
gi 767939112 310 WafGLGLERLAMILYDIPDIR-LF 332
Cdd:PLN02853 452 W--GLSLERPTMILYGIDNIRdLF 473
|
|
| pheT_bact |
TIGR00472 |
phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Every known example of ... |
241-402 |
1.41e-07 |
|
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: 53.83 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 241 FDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINFHGEwleVLGC-GVMEQQLVNSAGAQDRIgWAFGLGLERL 319
Cdd:TIGR00472 615 YDLKGDVESLLELLGLSDDVYFKNTAENEELHPGQSATIYLKGK---KIGFiGELHPEIAKKYDLKEPT-FVFELDLDRL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 320 AMILYDIPdirlfwcederflkqfcvsninqkvKFQPLSKYPAVINDISFWLPSENYAeNDFYDLVRTIGGDLVEKVDLI 399
Cdd:TIGR00472 691 LESLKKVP-------------------------KYRPISKFPAVTRDISFLVPKDVPA-NEIIKLIKKSGLELLEEVELF 744
|
...
gi 767939112 400 DKF 402
Cdd:TIGR00472 745 DVY 747
|
|
| PTZ00326 |
PTZ00326 |
phenylalanyl-tRNA synthetase alpha chain; Provisional |
123-332 |
3.75e-07 |
|
phenylalanyl-tRNA synthetase alpha chain; Provisional
Pssm-ID: 240361 [Multi-domain] Cd Length: 494 Bit Score: 51.89 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 123 WqNFDSLLIPADHPSR----------------KKGDNYYLNR---TH----------------------MLRAHTSAHQW 161
Cdd:PTZ00326 261 W-NFDALFQPQQHPARdaqdtfflskpetskvNDLDDDYVERvkkVHevggygsigwrydwkleearknILRTHTTAVSA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 162 DLLH-------AGLD----AFLVVGDVYRRDQIDSQHYPIFHQLEAVrlfskhelfagikdgeslqlfeqssrsahkqet 230
Cdd:PTZ00326 340 RMLYklaqeykKTGPfkpkKYFSIDRVFRNETLDATHLAEFHQVEGF--------------------------------- 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939112 231 htmeavkLVEFDLkqTLTRLMA--HLFGDELEI---RWVDCYFPFTHPSfeMEI-NFH---GEWLEVLGCGVMEQQLVNS 301
Cdd:PTZ00326 387 -------VIDRNL--TLGDLIGtiREFFRRIGItklRFKPAFNPYTEPS--MEIfGYHpglKKWVEVGNSGIFRPEMLRP 455
|
250 260 270
....*....|....*....|....*....|....*
gi 767939112 302 AGAQDR---IGWafGLGLERLAMILYDIPDIR-LF 332
Cdd:PTZ00326 456 MGFPEDvtvIAW--GLSLERPTMIKYGIKNIRdLF 488
|
|
| pheT |
PRK00629 |
phenylalanyl-tRNA synthetase subunit beta; Reviewed |
351-402 |
1.33e-06 |
|
phenylalanyl-tRNA synthetase subunit beta; Reviewed
Pssm-ID: 234804 [Multi-domain] Cd Length: 791 Bit Score: 50.55 E-value: 1.33e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 767939112 351 KVKFQPLSKYPAVINDISFWLPsENYAENDFYDLVRTIGGDLVEKVDLIDKF 402
Cdd:PRK00629 690 LPKYKPISKFPAVRRDLALVVD-EDVPAADILKAIKKAGGKLLESVELFDVY 740
|
|
| PheT |
COG0072 |
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; ... |
345-400 |
4.93e-06 |
|
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: 48.62 E-value: 4.93e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 767939112 345 VSNINQKVKFQPLSKYPAVINDISFWLPsENYAENDFYDLVRTIGGDLVEKVDLID 400
Cdd:COG0072 686 LELARKVPKYKPISKFPAVRRDLALVVD-EDVPAADVLDAIRKAAGKLLEDVRLFD 740
|
|
| |
