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Conserved domains on  [gi|1553118812|ref|WP_127577650|]
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phenylalanine--tRNA ligase subunit alpha [Sinorhizobium meliloti]

Protein Classification

phenylalanine--tRNA ligase subunit alpha( domain architecture ID 17564626)

phenylalanine--tRNA ligase subunit alpha is the catalytic subunit of the enzyme complex that catalyzes the attachment of phenylalanine to tRNA(Phe)

CATH:  3.30.930.10
EC:  6.1.1.20
Gene Ontology:  GO:0005524|GO:0006432|GO:0000287|GO:0004826|GO:0000049
PubMed:  14665676|8274143|11310981|1852601|2053131|10447505|10704480|12458790

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 1-345 0e+00

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: 601.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812   1 MSELETLERTLLAEIDAAADEGAIEAVRVGALGKKGSISELLKTLGSMSPEERQSRGARINALKNTVTEAISARKTALKD 80
Cdd:COG0016     1 MEELEALKEEALAAIAAASDLEELEALRVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812  81 AAIAERLARETVDISLPVRssPAERGRIHPISQIVDEITAIFGDMGFSIAEGPDIETDYYNFTALNFPEGHPAREMHDTF 160
Cdd:COG0016    81 AELEARLAAETIDVTLPGR--PRPLGSLHPLTQVIEEIEDIFVGMGFEVAEGPEIETDWYNFEALNIPPDHPARDMQDTF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 161 FFAPDekgerKVLRTHTSPVQIRTMEAGQPPIRIIIPGKTYRQD-SDATHSPMFHQVEGLVIDRTANVANMRWVLEEFCK 239
Cdd:COG0016   159 YIDDG-----LLLRTHTSPVQIRTMEKQKPPIRIIAPGRVYRRDeSDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 240 AFFEVDqVTMRFRPSFFPFTEPSFEVDIQCDR-SGPIVKFGEGKDWMEILGCGMVHPNVLRAGGLDPDEYQGFAWGMGLD 318
Cdd:COG0016   234 AFFGED-VKVRFRPSYFPFTEPSAEVDISCFIcGGKGCRVCKGTGWLEILGCGMVHPNVLRAVGIDPEEYSGFAFGMGIE 312

                         330       340
                  ....*....|....*....|....*..
gi 1553118812 319 RIAMLKYGMPDLRDFFNADVRWMTHYG 345
Cdd:COG0016   313 RLAMLKYGIDDIRLFFENDLRFLRQFG 339
 
Name Accession Description Interval E-value
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 1-345 0e+00

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: 601.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812   1 MSELETLERTLLAEIDAAADEGAIEAVRVGALGKKGSISELLKTLGSMSPEERQSRGARINALKNTVTEAISARKTALKD 80
Cdd:COG0016     1 MEELEALKEEALAAIAAASDLEELEALRVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812  81 AAIAERLARETVDISLPVRssPAERGRIHPISQIVDEITAIFGDMGFSIAEGPDIETDYYNFTALNFPEGHPAREMHDTF 160
Cdd:COG0016    81 AELEARLAAETIDVTLPGR--PRPLGSLHPLTQVIEEIEDIFVGMGFEVAEGPEIETDWYNFEALNIPPDHPARDMQDTF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 161 FFAPDekgerKVLRTHTSPVQIRTMEAGQPPIRIIIPGKTYRQD-SDATHSPMFHQVEGLVIDRTANVANMRWVLEEFCK 239
Cdd:COG0016   159 YIDDG-----LLLRTHTSPVQIRTMEKQKPPIRIIAPGRVYRRDeSDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 240 AFFEVDqVTMRFRPSFFPFTEPSFEVDIQCDR-SGPIVKFGEGKDWMEILGCGMVHPNVLRAGGLDPDEYQGFAWGMGLD 318
Cdd:COG0016   234 AFFGED-VKVRFRPSYFPFTEPSAEVDISCFIcGGKGCRVCKGTGWLEILGCGMVHPNVLRAVGIDPEEYSGFAFGMGIE 312

                         330       340
                  ....*....|....*....|....*..
gi 1553118812 319 RIAMLKYGMPDLRDFFNADVRWMTHYG 345
Cdd:COG0016   313 RLAMLKYGIDDIRLFFENDLRFLRQFG 339
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 38-342 1.62e-125

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: 362.40  E-value: 1.62e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812  38 ISELLKTLGSMSPEE-RQSRGARINALKNTVTEAISARKTALKDAAIAERLARETVDISLPvrSSPAERGRIHPISQIVD 116
Cdd:TIGR00468   2 LKDLLKQLGKLTKEEtKPALGALINEVKIELQDELTKLKPELESAGLWSKLKFETYDVSLP--GTKIYPGSLHPLTRVID 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 117 EITAIFGDMGFSIAEGPDIETDYYNFTALNFPEGHPAREMHDTFFFApdekgERKVLRTHTSPVQIRTMEAGQ-PPIRII 195
Cdd:TIGR00468  80 EIRDIFLGLGFTEETGPEVETDFWNFDALNIPQDHPARDMQDTFYIK-----DRLLLRTHTTAVQLRTMEEQEkPPIRIF 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 196 IPGKTYRQDS-DATHSPMFHQVEGLVIDRTANVANMRWVLEEFCKAFFEVDQVtmRFRPSFFPFTEPSFEVDIQCDrsgp 274
Cdd:TIGR00468 155 SPGRVFRNDTvDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLKKMFGETEI--RFRPSYFPFTEPSAEIDVYCP---- 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1553118812 275 ivkfgEGKDWMEILGCGMVHPNVLRAGGLDPdEYQGFAWGMGLDRIAMLKYGMPDLRDFFNADVRWMT 342
Cdd:TIGR00468 229 -----EGKGWLEVLGAGMFRPEVLEPMGIDP-TYPGFAWGIGIERLAMLKYGITDIRDLYENDLRFLR 290
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 91-344 1.34e-122

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: 353.04  E-value: 1.34e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812  91 TVDISLPVRssPAERGRIHPISQIVDEITAIFGDMGFSIAEGPDIETDYYNFTALNFPEGHPAREMHDTFFFAPDEKGE- 169
Cdd:pfam01409   1 PYDVTLPGR--RIEPGGLHPLTRTLERIRDIFLGMGFEEVEGPEVESDFYNFDALNIPQDHPARDMQDTFYLKKPLKPVa 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 170 -RKVLRTHTSPVQIRTMEAGQ-PPIRIIIPGKTYRQDS-DATHSPMFHQVEGLVIDRTANVANMRWVLEEFCKAFFEVDq 246
Cdd:pfam01409  79 rRLLLRTHTTPVQARTLAKKPkPPIKIFSIGRVFRRDQvDATHLPEFHQVEGLVVDENVTFADLKGVLEEFLRKFFGFE- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 247 VTMRFRPSFFPFTEPSFEVDIQcdrsgpivkFGEGKDWMEILGCGMVHPNVLRAGGLDpDEYQGFAWGMGLDRIAMLKYG 326
Cdd:pfam01409 158 VKVRFRPSYFPFTEPSAEVDVY---------VCKLGGWLEVGGAGMVHPNVLEAVGID-EDYSGFAFGLGVERLAMLKYG 227

                         250
                  ....*....|....*...
gi 1553118812 327 MPDLRDFFNADVRWMTHY 344
Cdd:pfam01409 228 IDDIRDLYENDLRFLRQF 245
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 109-339 1.60e-122

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: 351.85  E-value: 1.60e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 109 HPISQIVDEITAIFGDMGFSIAEGPDIETDYYNFTALNFPEGHPAREMHDTFFFapdEKGERKVLRTHTSPVQIRTMEAG 188
Cdd:cd00496     1 HPLNKVIEEIEDIFVSMGFTEVEGPEVETDFYNFDALNIPQDHPARDMQDTFYI---NDPARLLLRTHTSAVQARALAKL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 189 QPPIRIIIPGKTYRQDS-DATHSPMFHQVEGLVIDRTANVANMRWVLEEFCKAFFEvDQVTMRFRPSFFPFTEPSFEVDI 267
Cdd:cd00496    78 KPPIRIFSIGRVYRNDEiDATHLPEFHQIEGLVVDKGLTFADLKGTLEEFAKELFG-PITKVRFRPSYFPFTEPSFEVDV 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1553118812 268 QCDrsgpivkfgEGKDWMEILGCGMVHPNVLRAGGLDpDEYQGFAWGMGLDRIAMLKYGMPDLRDFFNADVR 339
Cdd:cd00496   157 YCP---------GCLGWLEILGCGMVRPEVLENAGID-EEYSGFAFGIGLERLAMLKYGIPDIRLFYSNDLR 218
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
93-340 1.14e-64

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 212.77  E-value: 1.14e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812  93 DISLPVRSSPAerGRIHPISQIVDEITAIFGDMGFSIAEGPDIETDYYNFTALNFPEGHPAREMHDTFF----------- 161
Cdd:PRK04172  219 NVKAPPPKIYP--GKKHPYREFIDEVRDILVEMGFEEMKGPLVETEFWNFDALFQPQDHPAREMQDTFYlkypgigdlpe 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 162 -------------FAPDEKG----------ERKVLRTHTSPVQIRTM-EAGQPPIRIIIPGKTYRQDS-DATHSPMFHQV 216
Cdd:PRK04172  297 elvervkevhehgGDTGSRGwgykwdediaKRLVLRTHTTALSARYLaSRPEPPQKYFSIGRVFRPDTiDATHLPEFYQL 376

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 217 EGLVIDRTANVANMRWVLEEFCKA--FFEVdqvtmRFRPSFFPFTEPSFEVdiqcdrsgpIVKFgEGKDWMEILGCGMVH 294
Cdd:PRK04172  377 EGIVMGEDVSFRDLLGILKEFYKRlgFEEV-----KFRPAYFPFTEPSVEV---------EVYH-EGLGWVELGGAGIFR 441

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1553118812 295 PNVLRAGGLDpdeYQGFAWGMGLDRIAMLKYGMPDLRDFFNADVRW 340
Cdd:PRK04172  442 PEVLEPLGID---VPVLAWGLGIERLAMLRLGLDDIRDLYSSDIEW 484
growth_prot_Scy NF041483
polarized growth protein Scy;
5-107 4.36e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 39.04  E-value: 4.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812    5 ETLERT------LLAEIDAAADEGAIEAVRVGALgkkgsiselLKTLGSMSPEERQSRGAR-INALKNTVTEAISARKTA 77
Cdd:NF041483   524 ETLERTraeaerLRAEAEEQAEEVRAAAERAARE---------LREETERAIAARQAEAAEeLTRLHTEAEERLTAAEEA 594

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1553118812   78 LKDA-AIAERLARETVDISLPVRSSPAERGR 107
Cdd:NF041483   595 LADArAEAERIRREAAEETERLRTEAAERIR 625
 
Name Accession Description Interval E-value
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 1-345 0e+00

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: 601.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812   1 MSELETLERTLLAEIDAAADEGAIEAVRVGALGKKGSISELLKTLGSMSPEERQSRGARINALKNTVTEAISARKTALKD 80
Cdd:COG0016     1 MEELEALKEEALAAIAAASDLEELEALRVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812  81 AAIAERLARETVDISLPVRssPAERGRIHPISQIVDEITAIFGDMGFSIAEGPDIETDYYNFTALNFPEGHPAREMHDTF 160
Cdd:COG0016    81 AELEARLAAETIDVTLPGR--PRPLGSLHPLTQVIEEIEDIFVGMGFEVAEGPEIETDWYNFEALNIPPDHPARDMQDTF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 161 FFAPDekgerKVLRTHTSPVQIRTMEAGQPPIRIIIPGKTYRQD-SDATHSPMFHQVEGLVIDRTANVANMRWVLEEFCK 239
Cdd:COG0016   159 YIDDG-----LLLRTHTSPVQIRTMEKQKPPIRIIAPGRVYRRDeSDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 240 AFFEVDqVTMRFRPSFFPFTEPSFEVDIQCDR-SGPIVKFGEGKDWMEILGCGMVHPNVLRAGGLDPDEYQGFAWGMGLD 318
Cdd:COG0016   234 AFFGED-VKVRFRPSYFPFTEPSAEVDISCFIcGGKGCRVCKGTGWLEILGCGMVHPNVLRAVGIDPEEYSGFAFGMGIE 312

                         330       340
                  ....*....|....*....|....*..
gi 1553118812 319 RIAMLKYGMPDLRDFFNADVRWMTHYG 345
Cdd:COG0016   313 RLAMLKYGIDDIRLFFENDLRFLRQFG 339
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 38-342 1.62e-125

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: 362.40  E-value: 1.62e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812  38 ISELLKTLGSMSPEE-RQSRGARINALKNTVTEAISARKTALKDAAIAERLARETVDISLPvrSSPAERGRIHPISQIVD 116
Cdd:TIGR00468   2 LKDLLKQLGKLTKEEtKPALGALINEVKIELQDELTKLKPELESAGLWSKLKFETYDVSLP--GTKIYPGSLHPLTRVID 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 117 EITAIFGDMGFSIAEGPDIETDYYNFTALNFPEGHPAREMHDTFFFApdekgERKVLRTHTSPVQIRTMEAGQ-PPIRII 195
Cdd:TIGR00468  80 EIRDIFLGLGFTEETGPEVETDFWNFDALNIPQDHPARDMQDTFYIK-----DRLLLRTHTTAVQLRTMEEQEkPPIRIF 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 196 IPGKTYRQDS-DATHSPMFHQVEGLVIDRTANVANMRWVLEEFCKAFFEVDQVtmRFRPSFFPFTEPSFEVDIQCDrsgp 274
Cdd:TIGR00468 155 SPGRVFRNDTvDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLKKMFGETEI--RFRPSYFPFTEPSAEIDVYCP---- 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1553118812 275 ivkfgEGKDWMEILGCGMVHPNVLRAGGLDPdEYQGFAWGMGLDRIAMLKYGMPDLRDFFNADVRWMT 342
Cdd:TIGR00468 229 -----EGKGWLEVLGAGMFRPEVLEPMGIDP-TYPGFAWGIGIERLAMLKYGITDIRDLYENDLRFLR 290
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 91-344 1.34e-122

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: 353.04  E-value: 1.34e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812  91 TVDISLPVRssPAERGRIHPISQIVDEITAIFGDMGFSIAEGPDIETDYYNFTALNFPEGHPAREMHDTFFFAPDEKGE- 169
Cdd:pfam01409   1 PYDVTLPGR--RIEPGGLHPLTRTLERIRDIFLGMGFEEVEGPEVESDFYNFDALNIPQDHPARDMQDTFYLKKPLKPVa 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 170 -RKVLRTHTSPVQIRTMEAGQ-PPIRIIIPGKTYRQDS-DATHSPMFHQVEGLVIDRTANVANMRWVLEEFCKAFFEVDq 246
Cdd:pfam01409  79 rRLLLRTHTTPVQARTLAKKPkPPIKIFSIGRVFRRDQvDATHLPEFHQVEGLVVDENVTFADLKGVLEEFLRKFFGFE- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 247 VTMRFRPSFFPFTEPSFEVDIQcdrsgpivkFGEGKDWMEILGCGMVHPNVLRAGGLDpDEYQGFAWGMGLDRIAMLKYG 326
Cdd:pfam01409 158 VKVRFRPSYFPFTEPSAEVDVY---------VCKLGGWLEVGGAGMVHPNVLEAVGID-EDYSGFAFGLGVERLAMLKYG 227

                         250
                  ....*....|....*...
gi 1553118812 327 MPDLRDFFNADVRWMTHY 344
Cdd:pfam01409 228 IDDIRDLYENDLRFLRQF 245
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 109-339 1.60e-122

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: 351.85  E-value: 1.60e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 109 HPISQIVDEITAIFGDMGFSIAEGPDIETDYYNFTALNFPEGHPAREMHDTFFFapdEKGERKVLRTHTSPVQIRTMEAG 188
Cdd:cd00496     1 HPLNKVIEEIEDIFVSMGFTEVEGPEVETDFYNFDALNIPQDHPARDMQDTFYI---NDPARLLLRTHTSAVQARALAKL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 189 QPPIRIIIPGKTYRQDS-DATHSPMFHQVEGLVIDRTANVANMRWVLEEFCKAFFEvDQVTMRFRPSFFPFTEPSFEVDI 267
Cdd:cd00496    78 KPPIRIFSIGRVYRNDEiDATHLPEFHQIEGLVVDKGLTFADLKGTLEEFAKELFG-PITKVRFRPSYFPFTEPSFEVDV 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1553118812 268 QCDrsgpivkfgEGKDWMEILGCGMVHPNVLRAGGLDpDEYQGFAWGMGLDRIAMLKYGMPDLRDFFNADVR 339
Cdd:cd00496   157 YCP---------GCLGWLEILGCGMVRPEVLENAGID-EEYSGFAFGIGLERLAMLKYGIPDIRLFYSNDLR 218
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
93-340 1.14e-64

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 212.77  E-value: 1.14e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812  93 DISLPVRSSPAerGRIHPISQIVDEITAIFGDMGFSIAEGPDIETDYYNFTALNFPEGHPAREMHDTFF----------- 161
Cdd:PRK04172  219 NVKAPPPKIYP--GKKHPYREFIDEVRDILVEMGFEEMKGPLVETEFWNFDALFQPQDHPAREMQDTFYlkypgigdlpe 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 162 -------------FAPDEKG----------ERKVLRTHTSPVQIRTM-EAGQPPIRIIIPGKTYRQDS-DATHSPMFHQV 216
Cdd:PRK04172  297 elvervkevhehgGDTGSRGwgykwdediaKRLVLRTHTTALSARYLaSRPEPPQKYFSIGRVFRPDTiDATHLPEFYQL 376

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 217 EGLVIDRTANVANMRWVLEEFCKA--FFEVdqvtmRFRPSFFPFTEPSFEVdiqcdrsgpIVKFgEGKDWMEILGCGMVH 294
Cdd:PRK04172  377 EGIVMGEDVSFRDLLGILKEFYKRlgFEEV-----KFRPAYFPFTEPSVEV---------EVYH-EGLGWVELGGAGIFR 441

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1553118812 295 PNVLRAGGLDpdeYQGFAWGMGLDRIAMLKYGMPDLRDFFNADVRW 340
Cdd:PRK04172  442 PEVLEPLGID---VPVLAWGLGIERLAMLRLGLDDIRDLYSSDIEW 484
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 101-334 7.68e-44

phenylalanyl-tRNA synthetase alpha chain; Provisional


Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 157.82  E-value: 7.68e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 101 SPAERGRIHPISQIVDEITAIFGDMGFSiaEGPD---IETDYYNFTALNFPEGHPAREMHDTFF----------FAPD-- 165
Cdd:PTZ00326  221 KKIGGGNLHPLLKVRREFREILLEMGFE--EMPTnryVESSFWNFDALFQPQQHPARDAQDTFFlskpetskvnDLDDdy 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 166 ------------------------EKGERKVLRTHTSPVQIRTM-EAGQPPIR--IIIPGKTYRQDS-------DATHSP 211
Cdd:PTZ00326  299 vervkkvhevggygsigwrydwklEEARKNILRTHTTAVSARMLyKLAQEYKKtgPFKPKKYFSIDRvfrnetlDATHLA 378

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 212 MFHQVEGLVIDRTANVANMRWVLEEFCKAfFEVDQVtmRFRPSFFPFTEPSFEVdiqcdrsgpivkFG---EGKDWMEIL 288
Cdd:PTZ00326  379 EFHQVEGFVIDRNLTLGDLIGTIREFFRR-IGITKL--RFKPAFNPYTEPSMEI------------FGyhpGLKKWVEVG 443

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1553118812 289 GCGMVHPNVLRAGGLdPDEYQGFAWGMGLDRIAMLKYGMPDLRDFF 334
Cdd:PTZ00326  444 NSGIFRPEMLRPMGF-PEDVTVIAWGLSLERPTMIKYGIKNIRDLF 488
PLN02853 PLN02853
Probable phenylalanyl-tRNA synthetase alpha chain
 93-334 1.45e-41

Probable phenylalanyl-tRNA synthetase alpha chain


Pssm-ID: 215458 [Multi-domain]  Cd Length: 492  Bit Score: 151.75  E-value: 1.45e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812  93 DISLPVRSSPAERGRIHPISQIVDEITAIFGDMGFsiAEGPD---IETDYYNFTALNFPEGHPAREMHDTFF-------- 161
Cdd:PLN02853  205 EYNFNALGAPPEGGHLHPLLKVRQQFRKIFLQMGF--EEMPTnnfVESSFWNFDALFQPQQHPARDSHDTFFlkapattr 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 162 FAPD--------------------------EKGERKVLRTHTSPVQIRTMEA-GQPPIRiiiPGKTYRQDS-------DA 207
Cdd:PLN02853  283 QLPEdyvervktvhesggygsigygydwkrEEANKNLLRTHTTAVSSRMLYKlAQKGFK---PKRYFSIDRvfrneavDR 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 208 THSPMFHQVEGLVIDRTANVANMRWVLEEFckaFFEVDQVTMRFRPSFFPFTEPSFEvdiqcdrsgpIVKFGEG-KDWME 286
Cdd:PLN02853  360 THLAEFHQVEGLVCDRGLTLGDLIGVLEDF---FSRLGMTKLRFKPAYNPYTEPSME----------IFSYHEGlKKWVE 426

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1553118812 287 ILGCGMVHPNVLRAGGLdPDEYQGFAWGMGLDRIAMLKYGMPDLRDFF 334
Cdd:PLN02853  427 VGNSGMFRPEMLLPMGL-PEDVNVIAWGLSLERPTMILYGIDNIRDLF 473
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 109-348 1.03e-39

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 144.91  E-value: 1.03e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 109 HPISQIVDEITAIFG---DMGFSI--AEGPdIETDYYNFTALNFPEGHPAREMHDTFFFAPDekgerKVLRTHTSPVQIR 183
Cdd:PLN02788   68 HPLGILKNAIYDYFDenySNKFKKfdDLSP-IVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQ-----TVLRCHTSAHQAE 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 184 TMEAGQPpiRIIIPGKTYRQDS-DATHSPMFHQVEGLVI-----------DRTANVA-NMRWVLEEFCKAFFevDQVTMR 250
Cdd:PLN02788  142 LLRAGHT--HFLVTGDVYRRDSiDATHYPVFHQMEGVRVfspeeweasglDGTDLAAeDLKKTLEGLARHLF--GDVEMR 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 251 FRPSFFPFTEPSFEVDIqcdrsgpivkFGEGKdWMEILGCGMVHPNVLRAGGLdPDEyQGFAWGMGLDRIAMLKYGMPDL 330
Cdd:PLN02788  218 WVDAYFPFTNPSFELEI----------FFKGE-WLEVLGCGVTEQEILKNNGR-SDN-VAWAFGLGLERLAMVLFDIPDI 284

                         250       260
                  ....*....|....*....|....*
gi 1553118812 331 RDFFNADVRWMTHYG-------FRP 348
Cdd:PLN02788  285 RLFWSDDERFTSQFKegqlgvkFKP 309
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 109-359 7.75e-27

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: 110.55  E-value: 7.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 109 HPISQIVDEITAIF--------GDMGFSIAEGPD-IETDYYNFTALNFPEGHPAREMHDTFFFapdekGERKVLRTHTSP 179
Cdd:TIGR00469  42 HPLGIIRDLIEKKFngadnnqrGNPLFKIFDNFKpVVTTMENFDNLGFPADHPGRQKSDCYYI-----NEQHLLRAHTSA 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 180 VQIRTMEAG-----QPPIRIIIPGKTYRQDS-DATHSPMFHQVEGLVI-------------------------------- 221
Cdd:TIGR00469 117 HELECFQGGlddsdNIKSGFLISADVYRRDEiDKTHYPVFHQADGAAIrkrtkadlfekepgyiekfeedirgteadlnk 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 222 -------------------------DRTANVAN--MRWVLEEFCKAFF--------------EVDQVTMRFRPSFFPFTE 260
Cdd:TIGR00469 197 envkiildddsiplkennpkqeyasDLAVDLCEheLKHSIEGITKDLFgkkissmiknkannTPKELKVRWIDAYFPFTA 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 261 PSFEVDIqcdrsgpivkFGEGkDWMEILGCGMVHPNVLRAGGLDPDEYQGFAWGMGLDRIAMLKYGMPDLRDFFNADVRW 340
Cdd:TIGR00469 277 PSWEIEI----------WFKD-EWLELCGCGIIRHDILLRAGVHPSETIGWAFGLGLDRIAMLLFDIPDIRLFWSNDEGF 345

                         330
                  ....*....|....*....
gi 1553118812 341 MTHYGFRPLDMPTLFGGLS 359
Cdd:TIGR00469 346 LRQFSEGDLHLIPKFKPIS 364
Phe_tRNA-synt_N pfam02912
Aminoacyl tRNA synthetase class II, N-terminal domain;
19-87 1.66e-25

Aminoacyl tRNA synthetase class II, N-terminal domain;


Pssm-ID: 460745 [Multi-domain]  Cd Length: 69  Bit Score: 97.45  E-value: 1.66e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1553118812  19 ADEGAIEAVRVGALGKKGSISELLKTLGSMSPEERQSRGARINALKNTVTEAISARKTALKDAAIAERL 87
Cdd:pfam02912   1 SDLEELEELRVKYLGKKGELTALLKGLGKLPPEERPAAGKLINELKQAIEAALEERKEELEAAELEARL 69
class_II_aaRS-like_core cd00768
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
 121-320 1.84e-08

Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.


Pssm-ID: 238391 [Multi-domain]  Cd Length: 211  Bit Score: 54.05  E-value: 1.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 121 IFGDMGFSIAEGPDIETdyynfTALNFPEGHPAREMHdtffFAPDEKGERKVLRTHTSPVQIRTMEAG--QPPIRIIIPG 198
Cdd:cd00768    12 FMAELGFQEVETPIVER-----EPLLEKAGHEPKDLL----PVGAENEEDLYLRPTLEPGLVRLFVSHirKLPLRLAEIG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812 199 KTYRQD---SDATHSPMFHQVEGLV----IDRTANVANMRWVLEEFCKAFFEVDQVTMR--FRPSFF-PFTEPSFEVdiq 268
Cdd:cd00768    83 PAFRNEggrRGLRRVREFTQLEGEVfgedGEEASEFEELIELTEELLRALGIKLDIVFVekTPGEFSpGGAGPGFEI--- 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1553118812 269 cdrsgpIVKFGEGKdWMEILGCGMVHPNVLRAGGLDPD----EY---QGFAWGMGLDRI 320
Cdd:cd00768   160 ------EVDHPEGR-GLEIGSGGYRQDEQARAADLYFLdealEYrypPTIGFGLGLERL 211
growth_prot_Scy NF041483
polarized growth protein Scy;
5-107 4.36e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 39.04  E-value: 4.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553118812    5 ETLERT------LLAEIDAAADEGAIEAVRVGALgkkgsiselLKTLGSMSPEERQSRGAR-INALKNTVTEAISARKTA 77
Cdd:NF041483   524 ETLERTraeaerLRAEAEEQAEEVRAAAERAARE---------LREETERAIAARQAEAAEeLTRLHTEAEERLTAAEEA 594

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1553118812   78 LKDA-AIAERLARETVDISLPVRSSPAERGR 107
Cdd:NF041483   595 LADArAEAERIRREAAEETERLRTEAAERIR 625
 
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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