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Conserved domains on  [gi|32566635|ref|NP_507852|]
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phenylalanine--tRNA ligase [Caenorhabditis elegans]

Protein Classification

phenylalanine--tRNA ligase( domain architecture ID 1006086)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02788 super family cl33567
phenylalanine-tRNA synthetase
 22-458 4.78e-146

phenylalanine-tRNA synthetase


The actual alignment was detected with superfamily member PLN02788:

Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 422.64  E-value: 4.78e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635   22 NAKSIRATlmSTTAAAEESRKIVKEEVFELDgrkytpDALYNLSPGVRRLLDRRILQESSNPLNLLKRRIVDYVHQTYrk 101
Cdd:PLN02788  16 SSRRYRAP--AVSAVEIGGVAIARDEVVRED------DPTNNVPDHIFSKIGMQLHRRPDHPLGILKNAIYDYFDENY-- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  102 pgnrSPLFTICESEPRVVTTYQNFDSLLTPEDHVSRRPSDTYYVNHEHCLRAHTSAHQHNLMQSGLDAFLVIGDVYRRDE 181
Cdd:PLN02788  86 ----SNKFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAHQAELLRAGHTHFLVTGDVYRRDS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  182 VDRTHYPCFHQIEGVRLYSKDELlgkkpdgknvaelfstaasaaterspekqEKHTLDATKAAEIQLKQFLENLCDELFG 261
Cdd:PLN02788 162 IDATHYPVFHQMEGVRVFSPEEW-----------------------------EASGLDGTDLAAEDLKKTLEGLARHLFG 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  262 kDAEKRWVDAYFPFTHPSWELEVFYNGQWLEVLGCGIMEQKLLESAGVTDKIGWAFGIGLERIAMVLYGIPDIRLFWSKD 341
Cdd:PLN02788 213 -DVEMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVTEQEILKNNGRSDNVAWAFGLGLERLAMVLFDIPDIRLFWSDD 291

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  342 TGFLSQFAGKMPGedVKYKQISAHPQVIFDISFFLPSTVQFNDMtsdvYDTIRTVGGELVEQVKLTDEFENKKKEKKSQT 421
Cdd:PLN02788 292 ERFTSQFKEGQLG--VKFKPYSKYPPCYKDISFWISDEFTENNL----CEVVRGIAGDLVEEVKLIDNFTNPKKGKTSHC 365

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 32566635  422 YRIVYRSHERALTKEEVNVIHKQIEQSLASSFGVTLR 458
Cdd:PLN02788 366 YRIVYRSMERSLTDEEINALQDKVREEVQKKLGVELR 402
 
Name Accession Description Interval E-value
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 22-458 4.78e-146

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 422.64  E-value: 4.78e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635   22 NAKSIRATlmSTTAAAEESRKIVKEEVFELDgrkytpDALYNLSPGVRRLLDRRILQESSNPLNLLKRRIVDYVHQTYrk 101
Cdd:PLN02788  16 SSRRYRAP--AVSAVEIGGVAIARDEVVRED------DPTNNVPDHIFSKIGMQLHRRPDHPLGILKNAIYDYFDENY-- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  102 pgnrSPLFTICESEPRVVTTYQNFDSLLTPEDHVSRRPSDTYYVNHEHCLRAHTSAHQHNLMQSGLDAFLVIGDVYRRDE 181
Cdd:PLN02788  86 ----SNKFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAHQAELLRAGHTHFLVTGDVYRRDS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  182 VDRTHYPCFHQIEGVRLYSKDELlgkkpdgknvaelfstaasaaterspekqEKHTLDATKAAEIQLKQFLENLCDELFG 261
Cdd:PLN02788 162 IDATHYPVFHQMEGVRVFSPEEW-----------------------------EASGLDGTDLAAEDLKKTLEGLARHLFG 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  262 kDAEKRWVDAYFPFTHPSWELEVFYNGQWLEVLGCGIMEQKLLESAGVTDKIGWAFGIGLERIAMVLYGIPDIRLFWSKD 341
Cdd:PLN02788 213 -DVEMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVTEQEILKNNGRSDNVAWAFGLGLERLAMVLFDIPDIRLFWSDD 291

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  342 TGFLSQFAGKMPGedVKYKQISAHPQVIFDISFFLPSTVQFNDMtsdvYDTIRTVGGELVEQVKLTDEFENKKKEKKSQT 421
Cdd:PLN02788 292 ERFTSQFKEGQLG--VKFKPYSKYPPCYKDISFWISDEFTENNL----CEVVRGIAGDLVEEVKLIDNFTNPKKGKTSHC 365

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 32566635  422 YRIVYRSHERALTKEEVNVIHKQIEQSLASSFGVTLR 458
Cdd:PLN02788 366 YRIVYRSMERSLTDEEINALQDKVREEVQKKLGVELR 402
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 50-457 1.33e-134

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: 395.60  E-value: 1.33e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635    50 ELDGRKYTPDA-LYNLSPGVRRLLDRRILQESSNPLNLLKRRIVDYVHQTYRKPGNrSPLFTICESEPRVVTTYQNFDSL 128
Cdd:TIGR00469   9 EINGIKYATDGqTTNVTDKIIKLTDANKHLKEDHPLGIIRDLIEKKFNGADNNQRG-NPLFKIFDNFKPVVTTMENFDNL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635   129 LTPEDHVSRRPSDTYYVNHEHCLRAHTSAHQHNLMQSGLD-------AFLVIGDVYRRDEVDRTHYPCFHQIEG--VRLY 199
Cdd:TIGR00469  88 GFPADHPGRQKSDCYYINEQHLLRAHTSAHELECFQGGLDdsdniksGFLISADVYRRDEIDKTHYPVFHQADGaaIRKR 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635   200 SKDELLGKKP-----------------DGKNVAELFSTAASAATERSPeKQEKHTLDATKAAEIQLKQFLENLCDELFG- 261
Cdd:TIGR00469 168 TKADLFEKEPgyiekfeedirgteadlNKENVKIILDDDSIPLKENNP-KQEYASDLAVDLCEHELKHSIEGITKDLFGk 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635   262 --------------KDAEKRWVDAYFPFTHPSWELEVFYNGQWLEVLGCGIMEQKLLESAGV--TDKIGWAFGIGLERIA 325
Cdd:TIGR00469 247 kissmiknkanntpKELKVRWIDAYFPFTAPSWEIEIWFKDEWLELCGCGIIRHDILLRAGVhpSETIGWAFGLGLDRIA 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635   326 MVLYGIPDIRLFWSKDTGFLSQFAGKMPGEDVKYKQISAHPQVIFDISFFLPSTVQFNDMTS--DVYDTIRTVGGELVEQ 403
Cdd:TIGR00469 327 MLLFDIPDIRLFWSNDEGFLRQFSEGDLHLIPKFKPISHHPGCFNDLAFWLPEDIEDDAGFHenDFMDIIRNIAGDLVEQ 406

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 32566635   404 VKLTDEFENKKKEKKSQTYRIVYRSHERALTKEEVNVIHKQIEQSLASSFGVTL 457
Cdd:TIGR00469 407 IKLVDKFKHPKTGKKSMCFRINYQHMDRNLTNAEVNEIHDMIASALVDEFNVEI 460
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 82-341 1.63e-96

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: 289.45  E-value: 1.63e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  82 NPLNLLKRRIVDYVHQTyrkpgnrspLFTICESePRVVTTYQNFDSLLTPEDHVSRRPSDTYYVNHE--HCLRAHTSAHQ 159
Cdd:cd00496   1 HPLNKVIEEIEDIFVSM---------GFTEVEG-PEVETDFYNFDALNIPQDHPARDMQDTFYINDParLLLRTHTSAVQ 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635 160 HNLMQS--GLDAFLVIGDVYRRDEVDRTHYPCFHQIEGVRLyskdellgkkpdGKNVAElfstaasaaterspekqekht 237
Cdd:cd00496  71 ARALAKlkPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVV------------DKGLTF--------------------- 117

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635 238 ldatkaaeIQLKQFLENLCDELFGKDAEKRWVDAYFPFTHPSWELEVFYNG--QWLEVLGCGIMEQKLLESAGVTDK-IG 314
Cdd:cd00496 118 --------ADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYCPGclGWLEILGCGMVRPEVLENAGIDEEySG 189

                       250       260
                ....*....|....*....|....*..
gi 32566635 315 WAFGIGLERIAMVLYGIPDIRLFWSKD 341
Cdd:cd00496 190 FAFGIGLERLAMLKYGIPDIRLFYSND 216
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 66-348 3.35e-54

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: 184.10  E-value: 3.35e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  66 PGVRRLLDRRilqessNPLNLLKRRIVDYvhqtYRKPGnrsplFTICESePRVVTTYQNFDSLLTPEDHVSRRPSDTYYV 145
Cdd:COG0016  97 PGRPRPLGSL------HPLTQVIEEIEDI----FVGMG-----FEVAEG-PEIETDWYNFEALNIPPDHPARDMQDTFYI 160

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635 146 NHEHCLRAHTSAHQ-HNLMQSGLD-AFLVIGDVYRRDEVDRTHYPCFHQIEGvrLYSkdellgkkpdGKNVAelFStaas 223
Cdd:COG0016 161 DDGLLLRTHTSPVQiRTMEKQKPPiRIIAPGRVYRRDESDATHSPMFHQVEG--LVV----------DKGIS--FA---- 222

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635 224 aaterspekqekhtldatkaaeiQLKQFLENLCDELFGKDAEKRWVDAYFPFTHPSWELEVFY------------NGQWL 291
Cdd:COG0016 223 -----------------------DLKGTLEEFAKAFFGEDVKVRFRPSYFPFTEPSAEVDISCficggkgcrvckGTGWL 279

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32566635 292 EVLGCGIMEQKLLESAGV-TDKI-GWAFGIGLERIAMVLYGIPDIRLFWSKDTGFLSQF 348
Cdd:COG0016 280 EILGCGMVHPNVLRAVGIdPEEYsGFAFGMGIERLAMLKYGIDDIRLFFENDLRFLRQF 338
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 71-348 2.09e-51

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: 173.92  E-value: 2.09e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635    71 LLDRRILQESSNPLNLLKRRIVDYVHQTyrkpGnrsplFTICESePRVVTTYQNFDSLLTPEDHVSRRPSDTYYVNHEHC 150
Cdd:pfam01409   6 LPGRRIEPGGLHPLTRTLERIRDIFLGM----G-----FEEVEG-PEVESDFYNFDALNIPQDHPARDMQDTFYLKKPLK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635   151 -------LRAHTSAHQHNLMQSGLDA---FLVIGDVYRRDEVDRTHYPCFHQIEGVRLyskdellgkkpdGKNVaelfst 220
Cdd:pfam01409  76 pvarrllLRTHTTPVQARTLAKKPKPpikIFSIGRVFRRDQVDATHLPEFHQVEGLVV------------DENV------ 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635   221 aasaaterspekqekhTLDatkaaeiQLKQFLENLCDELFGKDAEKRWVDAYFPFTHPSWELEVF--YNGQWLEVLGCGI 298
Cdd:pfam01409 138 ----------------TFA-------DLKGVLEEFLRKFFGFEVKVRFRPSYFPFTEPSAEVDVYvcKLGGWLEVGGAGM 194

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 32566635   299 MEQKLLESAGVTDKI-GWAFGIGLERIAMVLYGIPDIRLFWSKDTGFLSQF 348
Cdd:pfam01409 195 VHPNVLEAVGIDEDYsGFAFGLGVERLAMLKYGIDDIRDLYENDLRFLRQF 245
FDX-ACB smart00896
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 363-458 1.06e-21

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: 89.02  E-value: 1.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635    363 SAHPQVIFDISFFLPSTVQFNDmtsdVYDTIRTVGGELVEQVKLTDE-FENKKKEKKSQTYRIVYRSHERALTKEEVNVI 441
Cdd:smart00896   1 SKFPAVRRDLAFVVDEDVPAAE----LLDAIREAGGDLLEDVRLFDVyEGGIPEGKKSLAYRLTYQSPDRTLTDEEVNAI 76

                           90
                   ....*....|....*..
gi 32566635    442 HKQIEQSLASSFGVTLR 458
Cdd:smart00896  77 HDKIVAALEKKFGAELR 93
 
Name Accession Description Interval E-value
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 22-458 4.78e-146

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 422.64  E-value: 4.78e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635   22 NAKSIRATlmSTTAAAEESRKIVKEEVFELDgrkytpDALYNLSPGVRRLLDRRILQESSNPLNLLKRRIVDYVHQTYrk 101
Cdd:PLN02788  16 SSRRYRAP--AVSAVEIGGVAIARDEVVRED------DPTNNVPDHIFSKIGMQLHRRPDHPLGILKNAIYDYFDENY-- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  102 pgnrSPLFTICESEPRVVTTYQNFDSLLTPEDHVSRRPSDTYYVNHEHCLRAHTSAHQHNLMQSGLDAFLVIGDVYRRDE 181
Cdd:PLN02788  86 ----SNKFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAHQAELLRAGHTHFLVTGDVYRRDS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  182 VDRTHYPCFHQIEGVRLYSKDELlgkkpdgknvaelfstaasaaterspekqEKHTLDATKAAEIQLKQFLENLCDELFG 261
Cdd:PLN02788 162 IDATHYPVFHQMEGVRVFSPEEW-----------------------------EASGLDGTDLAAEDLKKTLEGLARHLFG 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  262 kDAEKRWVDAYFPFTHPSWELEVFYNGQWLEVLGCGIMEQKLLESAGVTDKIGWAFGIGLERIAMVLYGIPDIRLFWSKD 341
Cdd:PLN02788 213 -DVEMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVTEQEILKNNGRSDNVAWAFGLGLERLAMVLFDIPDIRLFWSDD 291

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  342 TGFLSQFAGKMPGedVKYKQISAHPQVIFDISFFLPSTVQFNDMtsdvYDTIRTVGGELVEQVKLTDEFENKKKEKKSQT 421
Cdd:PLN02788 292 ERFTSQFKEGQLG--VKFKPYSKYPPCYKDISFWISDEFTENNL----CEVVRGIAGDLVEEVKLIDNFTNPKKGKTSHC 365

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 32566635  422 YRIVYRSHERALTKEEVNVIHKQIEQSLASSFGVTLR 458
Cdd:PLN02788 366 YRIVYRSMERSLTDEEINALQDKVREEVQKKLGVELR 402
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 50-457 1.33e-134

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: 395.60  E-value: 1.33e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635    50 ELDGRKYTPDA-LYNLSPGVRRLLDRRILQESSNPLNLLKRRIVDYVHQTYRKPGNrSPLFTICESEPRVVTTYQNFDSL 128
Cdd:TIGR00469   9 EINGIKYATDGqTTNVTDKIIKLTDANKHLKEDHPLGIIRDLIEKKFNGADNNQRG-NPLFKIFDNFKPVVTTMENFDNL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635   129 LTPEDHVSRRPSDTYYVNHEHCLRAHTSAHQHNLMQSGLD-------AFLVIGDVYRRDEVDRTHYPCFHQIEG--VRLY 199
Cdd:TIGR00469  88 GFPADHPGRQKSDCYYINEQHLLRAHTSAHELECFQGGLDdsdniksGFLISADVYRRDEIDKTHYPVFHQADGaaIRKR 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635   200 SKDELLGKKP-----------------DGKNVAELFSTAASAATERSPeKQEKHTLDATKAAEIQLKQFLENLCDELFG- 261
Cdd:TIGR00469 168 TKADLFEKEPgyiekfeedirgteadlNKENVKIILDDDSIPLKENNP-KQEYASDLAVDLCEHELKHSIEGITKDLFGk 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635   262 --------------KDAEKRWVDAYFPFTHPSWELEVFYNGQWLEVLGCGIMEQKLLESAGV--TDKIGWAFGIGLERIA 325
Cdd:TIGR00469 247 kissmiknkanntpKELKVRWIDAYFPFTAPSWEIEIWFKDEWLELCGCGIIRHDILLRAGVhpSETIGWAFGLGLDRIA 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635   326 MVLYGIPDIRLFWSKDTGFLSQFAGKMPGEDVKYKQISAHPQVIFDISFFLPSTVQFNDMTS--DVYDTIRTVGGELVEQ 403
Cdd:TIGR00469 327 MLLFDIPDIRLFWSNDEGFLRQFSEGDLHLIPKFKPISHHPGCFNDLAFWLPEDIEDDAGFHenDFMDIIRNIAGDLVEQ 406

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 32566635   404 VKLTDEFENKKKEKKSQTYRIVYRSHERALTKEEVNVIHKQIEQSLASSFGVTL 457
Cdd:TIGR00469 407 IKLVDKFKHPKTGKKSMCFRINYQHMDRNLTNAEVNEIHDMIASALVDEFNVEI 460
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 82-341 1.63e-96

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: 289.45  E-value: 1.63e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  82 NPLNLLKRRIVDYVHQTyrkpgnrspLFTICESePRVVTTYQNFDSLLTPEDHVSRRPSDTYYVNHE--HCLRAHTSAHQ 159
Cdd:cd00496   1 HPLNKVIEEIEDIFVSM---------GFTEVEG-PEVETDFYNFDALNIPQDHPARDMQDTFYINDParLLLRTHTSAVQ 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635 160 HNLMQS--GLDAFLVIGDVYRRDEVDRTHYPCFHQIEGVRLyskdellgkkpdGKNVAElfstaasaaterspekqekht 237
Cdd:cd00496  71 ARALAKlkPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVV------------DKGLTF--------------------- 117

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635 238 ldatkaaeIQLKQFLENLCDELFGKDAEKRWVDAYFPFTHPSWELEVFYNG--QWLEVLGCGIMEQKLLESAGVTDK-IG 314
Cdd:cd00496 118 --------ADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYCPGclGWLEILGCGMVRPEVLENAGIDEEySG 189

                       250       260
                ....*....|....*....|....*..
gi 32566635 315 WAFGIGLERIAMVLYGIPDIRLFWSKD 341
Cdd:cd00496 190 FAFGIGLERLAMLKYGIPDIRLFYSND 216
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 66-348 3.35e-54

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: 184.10  E-value: 3.35e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  66 PGVRRLLDRRilqessNPLNLLKRRIVDYvhqtYRKPGnrsplFTICESePRVVTTYQNFDSLLTPEDHVSRRPSDTYYV 145
Cdd:COG0016  97 PGRPRPLGSL------HPLTQVIEEIEDI----FVGMG-----FEVAEG-PEIETDWYNFEALNIPPDHPARDMQDTFYI 160

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635 146 NHEHCLRAHTSAHQ-HNLMQSGLD-AFLVIGDVYRRDEVDRTHYPCFHQIEGvrLYSkdellgkkpdGKNVAelFStaas 223
Cdd:COG0016 161 DDGLLLRTHTSPVQiRTMEKQKPPiRIIAPGRVYRRDESDATHSPMFHQVEG--LVV----------DKGIS--FA---- 222

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635 224 aaterspekqekhtldatkaaeiQLKQFLENLCDELFGKDAEKRWVDAYFPFTHPSWELEVFY------------NGQWL 291
Cdd:COG0016 223 -----------------------DLKGTLEEFAKAFFGEDVKVRFRPSYFPFTEPSAEVDISCficggkgcrvckGTGWL 279

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32566635 292 EVLGCGIMEQKLLESAGV-TDKI-GWAFGIGLERIAMVLYGIPDIRLFWSKDTGFLSQF 348
Cdd:COG0016 280 EILGCGMVHPNVLRAVGIdPEEYsGFAFGMGIERLAMLKYGIDDIRLFFENDLRFLRQF 338
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 71-348 2.09e-51

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: 173.92  E-value: 2.09e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635    71 LLDRRILQESSNPLNLLKRRIVDYVHQTyrkpGnrsplFTICESePRVVTTYQNFDSLLTPEDHVSRRPSDTYYVNHEHC 150
Cdd:pfam01409   6 LPGRRIEPGGLHPLTRTLERIRDIFLGM----G-----FEEVEG-PEVESDFYNFDALNIPQDHPARDMQDTFYLKKPLK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635   151 -------LRAHTSAHQHNLMQSGLDA---FLVIGDVYRRDEVDRTHYPCFHQIEGVRLyskdellgkkpdGKNVaelfst 220
Cdd:pfam01409  76 pvarrllLRTHTTPVQARTLAKKPKPpikIFSIGRVFRRDQVDATHLPEFHQVEGLVV------------DENV------ 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635   221 aasaaterspekqekhTLDatkaaeiQLKQFLENLCDELFGKDAEKRWVDAYFPFTHPSWELEVF--YNGQWLEVLGCGI 298
Cdd:pfam01409 138 ----------------TFA-------DLKGVLEEFLRKFFGFEVKVRFRPSYFPFTEPSAEVDVYvcKLGGWLEVGGAGM 194

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 32566635   299 MEQKLLESAGVTDKI-GWAFGIGLERIAMVLYGIPDIRLFWSKDTGFLSQF 348
Cdd:pfam01409 195 VHPNVLEAVGIDEDYsGFAFGLGVERLAMLKYGIDDIRDLYENDLRFLRQF 245
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 71-348 1.36e-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: 170.96  E-value: 1.36e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635    71 LLDRRILQESSNPLNLLKRRIVDYVhqtyrkpgnRSPLFTICESePRVVTTYQNFDSLLTPEDHVSRRPSDTYYVNHEHC 150
Cdd:TIGR00468  61 LPGTKIYPGSLHPLTRVIDEIRDIF---------LGLGFTEETG-PEVETDFWNFDALNIPQDHPARDMQDTFYIKDRLL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635   151 LRAHTSAHQHNLMQ---SGLDAFLVIGDVYRRDEVDRTHYPCFHQIEGVRLyskdellgkkpdGKNVAelFSTaasaate 227
Cdd:TIGR00468 131 LRTHTTAVQLRTMEeqeKPPIRIFSPGRVFRNDTVDATHLPEFHQVEGLVI------------DKNIS--FTN------- 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635   228 rspekqekhtldatkaaeiqLKQFLENLCDELFGKDaEKRWVDAYFPFTHPSWELEVF-YNG-QWLEVLGCGIMEQKLLE 305
Cdd:TIGR00468 190 --------------------LKGFLEEFLKKMFGET-EIRFRPSYFPFTEPSAEIDVYcPEGkGWLEVLGAGMFRPEVLE 248

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 32566635   306 SAGVTDKI-GWAFGIGLERIAMVLYGIPDIRLFWSKDTGFLSQF 348
Cdd:TIGR00468 249 PMGIDPTYpGFAWGIGIERLAMLKYGITDIRDLYENDLRFLRQF 292
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
116-345 3.81e-29

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 119.17  E-value: 3.81e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  116 PRVVTTYQNFDSLLTPEDHVSRRPSDTYYVN------------------HEHC---------------------LRAHT- 155
Cdd:PRK04172 257 PLVETEFWNFDALFQPQDHPAREMQDTFYLKypgigdlpeelvervkevHEHGgdtgsrgwgykwdediakrlvLRTHTt 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  156 --SAHQhnlMQSGLDA---FLVIGDVYRRDEVDRTHYPCFHQIEGVrLYSKD----ELLGkkpdgknvaelfstaasaat 226
Cdd:PRK04172 337 alSARY---LASRPEPpqkYFSIGRVFRPDTIDATHLPEFYQLEGI-VMGEDvsfrDLLG-------------------- 392

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  227 erspekqekhtldatkaaeiQLKQFLENLcdelfGkdAEK-RWVDAYFPFTHPSWELEVFY-NGQWLEVLGCGIMEQKLL 304
Cdd:PRK04172 393 --------------------ILKEFYKRL-----G--FEEvKFRPAYFPFTEPSVEVEVYHeGLGWVELGGAGIFRPEVL 445

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 32566635  305 ESAGVTDKIGwAFGIGLERIAMVLYGIPDIRLFWSKDTGFL 345
Cdd:PRK04172 446 EPLGIDVPVL-AWGLGIERLAMLRLGLDDIRDLYSSDIEWL 485
FDX-ACB smart00896
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 363-458 1.06e-21

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: 89.02  E-value: 1.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635    363 SAHPQVIFDISFFLPSTVQFNDmtsdVYDTIRTVGGELVEQVKLTDE-FENKKKEKKSQTYRIVYRSHERALTKEEVNVI 441
Cdd:smart00896   1 SKFPAVRRDLAFVVDEDVPAAE----LLDAIREAGGDLLEDVRLFDVyEGGIPEGKKSLAYRLTYQSPDRTLTDEEVNAI 76

                           90
                   ....*....|....*..
gi 32566635    442 HKQIEQSLASSFGVTLR 458
Cdd:smart00896  77 HDKIVAALEKKFGAELR 93
FDX-ACB pfam03147
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 363-458 1.10e-15

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: 72.13  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635   363 SAHPQVIFDISFFLPSTVQFNDmtsdVYDTIRTVGGELVEQVKLTD--EFENKKKEKKSQTYRIVYRSHERALTKEEVNV 440
Cdd:pfam03147   1 SKYPAVRRDLAFVVDEDVPAAD----ILKAIREAGGELLESVELFDvyRGEKIPEGKKSLAFRLTFQSPERTLTDEEVNA 76

                          90
                  ....*....|....*...
gi 32566635   441 IHKQIEQSLASSFGVTLR 458
Cdd:pfam03147  77 IIEKIVEALEKKFGAELR 94
pheT PRK00629
phenylalanyl-tRNA synthetase subunit beta; Reviewed
 355-458 6.20e-15

phenylalanyl-tRNA synthetase subunit beta; Reviewed


Pssm-ID: 234804 [Multi-domain]  Cd Length: 791  Bit Score: 77.13  E-value: 6.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  355 EDVKYKQISAHPQVIFDISFFLPSTVQFndmtSDVYDTIRTVGGELVEQVKLTD--EFENKKKEKKSQTYRIVYRSHERA 432
Cdd:PRK00629 689 KLPKYKPISKFPAVRRDLALVVDEDVPA----ADILKAIKKAGGKLLESVELFDvyEGKGIGEGKKSLAFRLTFQDPDRT 764

                         90       100
                 ....*....|....*....|....*.
gi 32566635  433 LTKEEVNVIHKQIEQSLASSFGVTLR 458
Cdd:PRK00629 765 LTDEEINAAMDKIVAALEEKFGAELR 790
PLN02853 PLN02853
Probable phenylalanyl-tRNA synthetase alpha chain
 118-340 3.78e-14

Probable phenylalanyl-tRNA synthetase alpha chain


Pssm-ID: 215458 [Multi-domain]  Cd Length: 492  Bit Score: 74.32  E-value: 3.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  118 VVTTYQNFDSLLTPEDHVSRRPSDTYYVN-------------------HEH--------------------CLRAHTSAH 158
Cdd:PLN02853 248 VESSFWNFDALFQPQQHPARDSHDTFFLKapattrqlpedyvervktvHESggygsigygydwkreeanknLLRTHTTAV 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  159 Q----HNLMQSGLDA--FLVIGDVYRRDEVDRTHYPCFHQIEGVrLYSKDELLGkkpdgknvaELFSTaasaaterspek 232
Cdd:PLN02853 328 SsrmlYKLAQKGFKPkrYFSIDRVFRNEAVDRTHLAEFHQVEGL-VCDRGLTLG---------DLIGV------------ 385

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  233 qekhtldatkaaeiqLKQFLENL-CDELfgkdaekRWVDAYFPFTHPSweLEVF-YN---GQWLEVLGCGIMEQKLLESA 307
Cdd:PLN02853 386 ---------------LEDFFSRLgMTKL-------RFKPAYNPYTEPS--MEIFsYHeglKKWVEVGNSGMFRPEMLLPM 441

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 32566635  308 GVTDK---IGWafGIGLERIAMVLYGIPDIR-LFWSK 340
Cdd:PLN02853 442 GLPEDvnvIAW--GLSLERPTMILYGIDNIRdLFGHK 476
PheT COG0072
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; ...
 351-458 6.24e-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: 74.05  E-value: 6.24e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635 351 KMPGEDVKYKQISAHPQVIFDISFFLPSTVQFndmtSDVYDTIRTVGGELVEQVKLTDefenk--kkekkSQTYRIVYRS 428
Cdd:COG0072 687 ELARKVPKYKPISKFPAVRRDLALVVDEDVPA----ADVLDAIRKAAGKLLEDVRLFDvyegkgvpegkkSLAFSLTLQD 762

                        90       100       110
                ....*....|....*....|....*....|
gi 32566635 429 HERALTKEEVNVIHKQIEQSLASSFGVTLR 458
Cdd:COG0072 763 PDRTLTDEEIDAAMDKIVAALEKKFGAELR 792
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 124-337 1.92e-08

phenylalanyl-tRNA synthetase alpha chain; Provisional


Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 56.51  E-value: 1.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  124 NFDSLLTPEDHVSRRPSDTY----------------YVN-----HEH--------------------CLRAHTSAHQ--- 159
Cdd:PTZ00326 262 NFDALFQPQQHPARDAQDTFflskpetskvndldddYVErvkkvHEVggygsigwrydwkleearknILRTHTTAVSarm 341

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  160 -HNLMQSGLD-------AFLVIGDVYRRDEVDRTHYPCFHQIEGV---RLYSKDELLGkkpdgknVAELFSTAASaater 228
Cdd:PTZ00326 342 lYKLAQEYKKtgpfkpkKYFSIDRVFRNETLDATHLAEFHQVEGFvidRNLTLGDLIG-------TIREFFRRIG----- 409

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  229 spekqekhtldatkaaeiqlkqfLENLcdelfgkdaekRWVDAYFPFTHPSweLEVF-Y---NGQWLEVLGCGIMEQKLL 304
Cdd:PTZ00326 410 -----------------------ITKL-----------RFKPAFNPYTEPS--MEIFgYhpgLKKWVEVGNSGIFRPEML 453

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 32566635  305 ESAGVTDK---IGWafGIGLERIAMVLYGIPDIR-LF 337
Cdd:PTZ00326 454 RPMGFPEDvtvIAW--GLSLERPTMIKYGIKNIRdLF 488
syfB CHL00192
phenylalanyl-tRNA synthetase beta chain; Provisional
 359-458 2.35e-06

phenylalanyl-tRNA synthetase beta chain; Provisional


Pssm-ID: 214391 [Multi-domain]  Cd Length: 704  Bit Score: 50.09  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566635  359 YKQISAHPQVIFDISFFLPSTVQFNDMTSDVYdtirTVGGELVEQVKLTDEFENKK--KEKKSQTYRIVYRSHERALTKE 436
Cdd:CHL00192 606 YQPYSSYPKIIRDLSFIIKKSISISKIKELIY----QNGDNLLESITLFDYYKGKSipNGHTSLGLRLTFQSENKTLTNE 681

                         90       100
                 ....*....|....*....|..
gi 32566635  437 EVNVIHKQIEQSLASSFGVTLR 458
Cdd:CHL00192 682 EIDRIQQNLQKVLEKKLNAEIR 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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