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Conserved domains on  [gi|157743298|ref|NP_001099064|]
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phenylalanine--tRNA ligase, mitochondrial [Danio rerio]

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
 54-448 0e+00

phenylalanine-tRNA synthetase


The actual alignment was detected with superfamily member PLN02788:

Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 519.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298  54 VYPRDDMT-NVTAKILSKVGCQLHNRPHHPLWLIKERIKDHFYRSYVGrtgnpIFSVHDNLRPVVTVEQNFDSLLIPADH 132
Cdd:PLN02788  40 VVREDDPTnNVPDHIFSKIGMQLHRRPDHPLGILKNAIYDYFDENYSN-----KFKKFDDLSPIVSTKQNFDDVLVPPDH 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 133 PSCKKGENYYLNRTHMLRAHTSAHQKELVRSGLDCFLLAGDVYRRDEVDSSHYPVFHQMEGVRLFSNHELfagvengedl 212
Cdd:PLN02788 115 VSRSYNDTYYVDAQTVLRCHTSAHQAELLRAGHTHFLVTGDVYRRDSIDATHYPVFHQMEGVRVFSPEEW---------- 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 213 slferggrrtpqkqETHTLEAVKLLEFDLKRALTRLVRHLFGeDLEIRWVDCYFPFTHPSFEMEVFFQGDWMEVLGCGVM 292
Cdd:PLN02788 185 --------------EASGLDGTDLAAEDLKKTLEGLARHLFG-DVEMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVT 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 293 EQELVRSAGADNKMGWAFGLGLERLAMVLFGIPDIRLFWSEDERFLKQFRLSDIyqPVTFQPLSKYPPLFNDISFWLPaE 372
Cdd:PLN02788 250 EQEILKNNGRSDNVAWAFGLGLERLAMVLFDIPDIRLFWSDDERFTSQFKEGQL--GVKFKPYSKYPPCYKDISFWIS-D 326

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157743298 373 GYTENDFFDLVRSIGGDLVEKVTLVDTFTHPKMKKVSHCYRLVYRHMERTLTQEEVSIVHTAIQTAVEQELGVQGR 448
Cdd:PLN02788 327 EFTENNLCEVVRGIAGDLVEEVKLIDNFTNPKKGKTSHCYRIVYRSMERSLTDEEINALQDKVREEVQKKLGVELR 402
 
Name Accession Description Interval E-value
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 54-448 0e+00

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 519.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298  54 VYPRDDMT-NVTAKILSKVGCQLHNRPHHPLWLIKERIKDHFYRSYVGrtgnpIFSVHDNLRPVVTVEQNFDSLLIPADH 132
Cdd:PLN02788  40 VVREDDPTnNVPDHIFSKIGMQLHRRPDHPLGILKNAIYDYFDENYSN-----KFKKFDDLSPIVSTKQNFDDVLVPPDH 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 133 PSCKKGENYYLNRTHMLRAHTSAHQKELVRSGLDCFLLAGDVYRRDEVDSSHYPVFHQMEGVRLFSNHELfagvengedl 212
Cdd:PLN02788 115 VSRSYNDTYYVDAQTVLRCHTSAHQAELLRAGHTHFLVTGDVYRRDSIDATHYPVFHQMEGVRVFSPEEW---------- 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 213 slferggrrtpqkqETHTLEAVKLLEFDLKRALTRLVRHLFGeDLEIRWVDCYFPFTHPSFEMEVFFQGDWMEVLGCGVM 292
Cdd:PLN02788 185 --------------EASGLDGTDLAAEDLKKTLEGLARHLFG-DVEMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVT 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 293 EQELVRSAGADNKMGWAFGLGLERLAMVLFGIPDIRLFWSEDERFLKQFRLSDIyqPVTFQPLSKYPPLFNDISFWLPaE 372
Cdd:PLN02788 250 EQEILKNNGRSDNVAWAFGLGLERLAMVLFDIPDIRLFWSDDERFTSQFKEGQL--GVKFKPYSKYPPCYKDISFWIS-D 326

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157743298 373 GYTENDFFDLVRSIGGDLVEKVTLVDTFTHPKMKKVSHCYRLVYRHMERTLTQEEVSIVHTAIQTAVEQELGVQGR 448
Cdd:PLN02788 327 EFTENNLCEVVRGIAGDLVEEVKLIDNFTNPKKGKTSHCYRIVYRSMERSLTDEEINALQDKVREEVQKKLGVELR 402
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 41-446 3.07e-157

phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA synthetases, the mitochondrial form demonstrated from yeast is monomeric. It is similar to but longer than the alpha subunit (PheS) of the alpha 2 beta 2 form found in Bacteria, Archaea, and eukaryotes, and shares the characteristic motifs of class II aminoacyl-tRNA ligases. This model models the experimental example from Saccharomyces cerevisiae (designated MSF1) and its orthologs from other eukaryotic species. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 129561 [Multi-domain]  Cd Length: 460  Bit Score: 452.99  E-value: 3.07e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298   41 PQIQENSVQlfnhvYPRDDMT-NVTAKILSKVGCQLHNRPHHPLWLIKERIKDHFYRSYVGRTGNPIFSVHDNLRPVVTV 119
Cdd:TIGR00469   6 PHLEINGIK-----YATDGQTtNVTDKIIKLTDANKHLKEDHPLGIIRDLIEKKFNGADNNQRGNPLFKIFDNFKPVVTT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298  120 EQNFDSLLIPADHPSCKKGENYYLNRTHMLRAHTSAHQKELVRSGLD-------CFLLAGDVYRRDEVDSSHYPVFHQME 192
Cdd:TIGR00469  81 MENFDNLGFPADHPGRQKSDCYYINEQHLLRAHTSAHELECFQGGLDdsdniksGFLISADVYRRDEIDKTHYPVFHQAD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298  193 G--VRLFSNHELFagVENGEDLSLFERGGRRTPQ-----------------------KQETHTLEAVKLLEFDLKRALTR 247
Cdd:TIGR00469 161 GaaIRKRTKADLF--EKEPGYIEKFEEDIRGTEAdlnkenvkiildddsiplkennpKQEYASDLAVDLCEHELKHSIEG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298  248 LVRHLFG---------------EDLEIRWVDCYFPFTHPSFEMEVFFQGDWMEVLGCGVMEQELVRSAG--ADNKMGWAF 310
Cdd:TIGR00469 239 ITKDLFGkkissmiknkanntpKELKVRWIDAYFPFTAPSWEIEIWFKDEWLELCGCGIIRHDILLRAGvhPSETIGWAF 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298  311 GLGLERLAMVLFGIPDIRLFWSEDERFLKQFRLSDIYQPVTFQPLSKYPPLFNDISFWLPAE-----GYTENDFFDLVRS 385
Cdd:TIGR00469 319 GLGLDRIAMLLFDIPDIRLFWSNDEGFLRQFSEGDLHLIPKFKPISHHPGCFNDLAFWLPEDieddaGFHENDFMDIIRN 398

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157743298  386 IGGDLVEKVTLVDTFTHPKMKKVSHCYRLVYRHMERTLTQEEVSIVHTAIQTAVEQELGVQ 446
Cdd:TIGR00469 399 IAGDLVEQIKLVDKFKHPKTGKKSMCFRINYQHMDRNLTNAEVNEIHDMIASALVDEFNVE 459
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 81-336 1.95e-85

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: 260.56  E-value: 1.95e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298  81 HPLWLIKERIKDHFYRsyVGrtgnpiFSVHDNLrPVVTVEQNFDSLLIPADHPSCKKGENYYLNRT--HMLRAHTSAHQK 158
Cdd:cd00496    1 HPLNKVIEEIEDIFVS--MG------FTEVEGP-EVETDFYNFDALNIPQDHPARDMQDTFYINDParLLLRTHTSAVQA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 159 ELVRS--GLDCFLLAGDVYRRDEVDSSHYPVFHQMEGVRLFSNhelfagvengedlslferggrrtpqkqethtleavkL 236
Cdd:cd00496   72 RALAKlkPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKG------------------------------------L 115

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 237 LEFDLKRALTRLVRHLFGEDLEIRWVDCYFPFTHPSFEMEVFFQG--DWMEVLGCGVMEQELVRSAGADNKM-GWAFGLG 313
Cdd:cd00496  116 TFADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYCPGclGWLEILGCGMVRPEVLENAGIDEEYsGFAFGIG 195

                        250       260
                 ....*....|....*....|...
gi 157743298 314 LERLAMVLFGIPDIRLFWSEDER 336
Cdd:cd00496  196 LERLAMLKYGIPDIRLFYSNDLR 218
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 81-342 5.46e-53

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


Pssm-ID: 439787 [Multi-domain]  Cd Length: 339  Bit Score: 180.63  E-value: 5.46e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298  81 HPLWLIKERIKDHFyrsyvGRTGnpiFSVHDNlrP-VVTVEQNFDSLLIPADHPSCKKGENYYLNRTHMLRAHTSAHQke 159
Cdd:COG0016  107 HPLTQVIEEIEDIF-----VGMG---FEVAEG--PeIETDWYNFEALNIPPDHPARDMQDTFYIDDGLLLRTHTSPVQ-- 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 160 lVRSgldcfLLA----------GDVYRRDEVDSSHYPVFHQMEG--VrlfsnhelfagvenGEDLSLferggrrtpqkqe 227
Cdd:COG0016  175 -IRT-----MEKqkppiriiapGRVYRRDESDATHSPMFHQVEGlvV--------------DKGISF------------- 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 228 thtleAvkllefDLKRALTRLVRHLFGEDLEIRWVDCYFPFTHPSFEMEVFF------------QGDWMEVLGCGVMEQE 295
Cdd:COG0016  222 -----A------DLKGTLEEFAKAFFGEDVKVRFRPSYFPFTEPSAEVDISCficggkgcrvckGTGWLEILGCGMVHPN 290

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 157743298 296 LVRSAGADNK--MGWAFGLGLERLAMVLFGIPDIRLFWSEDERFLKQFR 342
Cdd:COG0016  291 VLRAVGIDPEeySGFAFGMGIERLAMLKYGIDDIRLFFENDLRFLRQFG 339
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 80-341 1.15e-45

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: 158.51  E-value: 1.15e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298   80 HHPLWLIKERIKDhFYRSYvgrtGnpiFSVHDNlRPVVTVEQNFDSLLIPADHPSCKKGENYYL-------NRTHMLRAH 152
Cdd:pfam01409  16 LHPLTRTLERIRD-IFLGM----G---FEEVEG-PEVESDFYNFDALNIPQDHPARDMQDTFYLkkplkpvARRLLLRTH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298  153 TSAHQ-KELVRSG---LDCFLLaGDVYRRDEVDSSHYPVFHQMEGVRLfsnhelfagvenGEDLSLFerggrrtpqkqet 228
Cdd:pfam01409  87 TTPVQaRTLAKKPkppIKIFSI-GRVFRRDQVDATHLPEFHQVEGLVV------------DENVTFA------------- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298  229 htleavkllefDLKRALTRLVRHLFGEDLEIRWVDCYFPFTHPSFEMEVFF--QGDWMEVLGCGVMEQELVRSAGADNKM 306
Cdd:pfam01409 141 -----------DLKGVLEEFLRKFFGFEVKVRFRPSYFPFTEPSAEVDVYVckLGGWLEVGGAGMVHPNVLEAVGIDEDY 209

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 157743298  307 -GWAFGLGLERLAMVLFGIPDIRLFWSEDERFLKQF 341
Cdd:pfam01409 210 sGFAFGLGVERLAMLKYGIDDIRDLYENDLRFLRQF 245
FDX-ACB smart00896
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 356-448 5.87e-32

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: 117.14  E-value: 5.87e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298   356 SKYPPLFNDISFWLPaEGYTENDFFDLVRSIGGDLVEKVTLVDTFTH-PKMKKVSHCYRLVYRHMERTLTQEEVSIVHTA 434
Cdd:smart00896   1 SKFPAVRRDLAFVVD-EDVPAAELLDAIREAGGDLLEDVRLFDVYEGgIPEGKKSLAYRLTYQSPDRTLTDEEVNAIHDK 79

                           90
                   ....*....|....
gi 157743298   435 IQTAVEQELGVQGR 448
Cdd:smart00896  80 IVAALEKKFGAELR 93
 
Name Accession Description Interval E-value
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 54-448 0e+00

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 519.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298  54 VYPRDDMT-NVTAKILSKVGCQLHNRPHHPLWLIKERIKDHFYRSYVGrtgnpIFSVHDNLRPVVTVEQNFDSLLIPADH 132
Cdd:PLN02788  40 VVREDDPTnNVPDHIFSKIGMQLHRRPDHPLGILKNAIYDYFDENYSN-----KFKKFDDLSPIVSTKQNFDDVLVPPDH 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 133 PSCKKGENYYLNRTHMLRAHTSAHQKELVRSGLDCFLLAGDVYRRDEVDSSHYPVFHQMEGVRLFSNHELfagvengedl 212
Cdd:PLN02788 115 VSRSYNDTYYVDAQTVLRCHTSAHQAELLRAGHTHFLVTGDVYRRDSIDATHYPVFHQMEGVRVFSPEEW---------- 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 213 slferggrrtpqkqETHTLEAVKLLEFDLKRALTRLVRHLFGeDLEIRWVDCYFPFTHPSFEMEVFFQGDWMEVLGCGVM 292
Cdd:PLN02788 185 --------------EASGLDGTDLAAEDLKKTLEGLARHLFG-DVEMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVT 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 293 EQELVRSAGADNKMGWAFGLGLERLAMVLFGIPDIRLFWSEDERFLKQFRLSDIyqPVTFQPLSKYPPLFNDISFWLPaE 372
Cdd:PLN02788 250 EQEILKNNGRSDNVAWAFGLGLERLAMVLFDIPDIRLFWSDDERFTSQFKEGQL--GVKFKPYSKYPPCYKDISFWIS-D 326

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157743298 373 GYTENDFFDLVRSIGGDLVEKVTLVDTFTHPKMKKVSHCYRLVYRHMERTLTQEEVSIVHTAIQTAVEQELGVQGR 448
Cdd:PLN02788 327 EFTENNLCEVVRGIAGDLVEEVKLIDNFTNPKKGKTSHCYRIVYRSMERSLTDEEINALQDKVREEVQKKLGVELR 402
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 41-446 3.07e-157

phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA synthetases, the mitochondrial form demonstrated from yeast is monomeric. It is similar to but longer than the alpha subunit (PheS) of the alpha 2 beta 2 form found in Bacteria, Archaea, and eukaryotes, and shares the characteristic motifs of class II aminoacyl-tRNA ligases. This model models the experimental example from Saccharomyces cerevisiae (designated MSF1) and its orthologs from other eukaryotic species. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 129561 [Multi-domain]  Cd Length: 460  Bit Score: 452.99  E-value: 3.07e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298   41 PQIQENSVQlfnhvYPRDDMT-NVTAKILSKVGCQLHNRPHHPLWLIKERIKDHFYRSYVGRTGNPIFSVHDNLRPVVTV 119
Cdd:TIGR00469   6 PHLEINGIK-----YATDGQTtNVTDKIIKLTDANKHLKEDHPLGIIRDLIEKKFNGADNNQRGNPLFKIFDNFKPVVTT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298  120 EQNFDSLLIPADHPSCKKGENYYLNRTHMLRAHTSAHQKELVRSGLD-------CFLLAGDVYRRDEVDSSHYPVFHQME 192
Cdd:TIGR00469  81 MENFDNLGFPADHPGRQKSDCYYINEQHLLRAHTSAHELECFQGGLDdsdniksGFLISADVYRRDEIDKTHYPVFHQAD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298  193 G--VRLFSNHELFagVENGEDLSLFERGGRRTPQ-----------------------KQETHTLEAVKLLEFDLKRALTR 247
Cdd:TIGR00469 161 GaaIRKRTKADLF--EKEPGYIEKFEEDIRGTEAdlnkenvkiildddsiplkennpKQEYASDLAVDLCEHELKHSIEG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298  248 LVRHLFG---------------EDLEIRWVDCYFPFTHPSFEMEVFFQGDWMEVLGCGVMEQELVRSAG--ADNKMGWAF 310
Cdd:TIGR00469 239 ITKDLFGkkissmiknkanntpKELKVRWIDAYFPFTAPSWEIEIWFKDEWLELCGCGIIRHDILLRAGvhPSETIGWAF 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298  311 GLGLERLAMVLFGIPDIRLFWSEDERFLKQFRLSDIYQPVTFQPLSKYPPLFNDISFWLPAE-----GYTENDFFDLVRS 385
Cdd:TIGR00469 319 GLGLDRIAMLLFDIPDIRLFWSNDEGFLRQFSEGDLHLIPKFKPISHHPGCFNDLAFWLPEDieddaGFHENDFMDIIRN 398

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157743298  386 IGGDLVEKVTLVDTFTHPKMKKVSHCYRLVYRHMERTLTQEEVSIVHTAIQTAVEQELGVQ 446
Cdd:TIGR00469 399 IAGDLVEQIKLVDKFKHPKTGKKSMCFRINYQHMDRNLTNAEVNEIHDMIASALVDEFNVE 459
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 81-336 1.95e-85

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: 260.56  E-value: 1.95e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298  81 HPLWLIKERIKDHFYRsyVGrtgnpiFSVHDNLrPVVTVEQNFDSLLIPADHPSCKKGENYYLNRT--HMLRAHTSAHQK 158
Cdd:cd00496    1 HPLNKVIEEIEDIFVS--MG------FTEVEGP-EVETDFYNFDALNIPQDHPARDMQDTFYINDParLLLRTHTSAVQA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 159 ELVRS--GLDCFLLAGDVYRRDEVDSSHYPVFHQMEGVRLFSNhelfagvengedlslferggrrtpqkqethtleavkL 236
Cdd:cd00496   72 RALAKlkPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKG------------------------------------L 115

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 237 LEFDLKRALTRLVRHLFGEDLEIRWVDCYFPFTHPSFEMEVFFQG--DWMEVLGCGVMEQELVRSAGADNKM-GWAFGLG 313
Cdd:cd00496  116 TFADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYCPGclGWLEILGCGMVRPEVLENAGIDEEYsGFAFGIG 195

                        250       260
                 ....*....|....*....|...
gi 157743298 314 LERLAMVLFGIPDIRLFWSEDER 336
Cdd:cd00496  196 LERLAMLKYGIPDIRLFYSNDLR 218
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 81-342 5.46e-53

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


Pssm-ID: 439787 [Multi-domain]  Cd Length: 339  Bit Score: 180.63  E-value: 5.46e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298  81 HPLWLIKERIKDHFyrsyvGRTGnpiFSVHDNlrP-VVTVEQNFDSLLIPADHPSCKKGENYYLNRTHMLRAHTSAHQke 159
Cdd:COG0016  107 HPLTQVIEEIEDIF-----VGMG---FEVAEG--PeIETDWYNFEALNIPPDHPARDMQDTFYIDDGLLLRTHTSPVQ-- 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 160 lVRSgldcfLLA----------GDVYRRDEVDSSHYPVFHQMEG--VrlfsnhelfagvenGEDLSLferggrrtpqkqe 227
Cdd:COG0016  175 -IRT-----MEKqkppiriiapGRVYRRDESDATHSPMFHQVEGlvV--------------DKGISF------------- 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 228 thtleAvkllefDLKRALTRLVRHLFGEDLEIRWVDCYFPFTHPSFEMEVFF------------QGDWMEVLGCGVMEQE 295
Cdd:COG0016  222 -----A------DLKGTLEEFAKAFFGEDVKVRFRPSYFPFTEPSAEVDISCficggkgcrvckGTGWLEILGCGMVHPN 290

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 157743298 296 LVRSAGADNK--MGWAFGLGLERLAMVLFGIPDIRLFWSEDERFLKQFR 342
Cdd:COG0016  291 VLRAVGIDPEeySGFAFGMGIERLAMLKYGIDDIRLFFENDLRFLRQFG 339
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 80-341 1.15e-45

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: 158.51  E-value: 1.15e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298   80 HHPLWLIKERIKDhFYRSYvgrtGnpiFSVHDNlRPVVTVEQNFDSLLIPADHPSCKKGENYYL-------NRTHMLRAH 152
Cdd:pfam01409  16 LHPLTRTLERIRD-IFLGM----G---FEEVEG-PEVESDFYNFDALNIPQDHPARDMQDTFYLkkplkpvARRLLLRTH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298  153 TSAHQ-KELVRSG---LDCFLLaGDVYRRDEVDSSHYPVFHQMEGVRLfsnhelfagvenGEDLSLFerggrrtpqkqet 228
Cdd:pfam01409  87 TTPVQaRTLAKKPkppIKIFSI-GRVFRRDQVDATHLPEFHQVEGLVV------------DENVTFA------------- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298  229 htleavkllefDLKRALTRLVRHLFGEDLEIRWVDCYFPFTHPSFEMEVFF--QGDWMEVLGCGVMEQELVRSAGADNKM 306
Cdd:pfam01409 141 -----------DLKGVLEEFLRKFFGFEVKVRFRPSYFPFTEPSAEVDVYVckLGGWLEVGGAGMVHPNVLEAVGIDEDY 209

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 157743298  307 -GWAFGLGLERLAMVLFGIPDIRLFWSEDERFLKQF 341
Cdd:pfam01409 210 sGFAFGLGVERLAMLKYGIDDIRDLYENDLRFLRQF 245
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 49-341 2.43e-44

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: 156.70  E-value: 2.43e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298   49 QLFNHVYPR--DDMTNVTAKIL-SKVGCQLHNRPH--------------HPLWLIKERIKDHFYRsyVGrtgnpiFSVHD 111
Cdd:TIGR00468  23 ALINEVKIElqDELTKLKPELEsAGLWSKLKFETYdvslpgtkiypgslHPLTRVIDEIRDIFLG--LG------FTEET 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298  112 NlrPVVTVE-QNFDSLLIPADHPSCKKGENYYLNRTHMLRAHTSA--------HQKELVRsgLDCFllaGDVYRRDEVDS 182
Cdd:TIGR00468  95 G--PEVETDfWNFDALNIPQDHPARDMQDTFYIKDRLLLRTHTTAvqlrtmeeQEKPPIR--IFSP---GRVFRNDTVDA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298  183 SHYPVFHQMEGVRLfsnhelfagvenGEDLSLferggrrtpqkqeTHtleavkllefdLKRALTRLVRHLFGEdLEIRWV 262
Cdd:TIGR00468 168 THLPEFHQVEGLVI------------DKNISF-------------TN-----------LKGFLEEFLKKMFGE-TEIRFR 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298  263 DCYFPFTHPSFEMEV--FFQGDWMEVLGCGVMEQELVRSAGADNKM-GWAFGLGLERLAMVLFGIPDIRLFWSEDERFLK 339
Cdd:TIGR00468 211 PSYFPFTEPSAEIDVycPEGKGWLEVLGAGMFRPEVLEPMGIDPTYpGFAWGIGIERLAMLKYGITDIRDLYENDLRFLR 290


                  ..
gi 157743298  340 QF 341
Cdd:TIGR00468 291 QF 292
FDX-ACB smart00896
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 356-448 5.87e-32

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: 117.14  E-value: 5.87e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298   356 SKYPPLFNDISFWLPaEGYTENDFFDLVRSIGGDLVEKVTLVDTFTH-PKMKKVSHCYRLVYRHMERTLTQEEVSIVHTA 434
Cdd:smart00896   1 SKFPAVRRDLAFVVD-EDVPAAELLDAIREAGGDLLEDVRLFDVYEGgIPEGKKSLAYRLTYQSPDRTLTDEEVNAIHDK 79

                           90
                   ....*....|....
gi 157743298   435 IQTAVEQELGVQGR 448
Cdd:smart00896  80 IVAALEKKFGAELR 93
FDX-ACB pfam03147
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 356-448 1.57e-24

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


Pssm-ID: 460826 [Multi-domain]  Cd Length: 94  Bit Score: 96.78  E-value: 1.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298  356 SKYPPLFNDISFWLPaEGYTENDFFDLVRSIGGDLVEKVTLVDTFTHPKMK--KVSHCYRLVYRHMERTLTQEEVSIVHT 433
Cdd:pfam03147   1 SKYPAVRRDLAFVVD-EDVPAADILKAIREAGGELLESVELFDVYRGEKIPegKKSLAFRLTFQSPERTLTDEEVNAIIE 79

                          90
                  ....*....|....*
gi 157743298  434 AIQTAVEQELGVQGR 448
Cdd:pfam03147  80 KIVEALEKKFGAELR 94
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
122-342 1.28e-22

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 99.91  E-value: 1.28e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 122 NFDSLLIPADHPSCKKGENYYLN----------------RTH-----------------------MLRAHT---SAHQke 159
Cdd:PRK04172 265 NFDALFQPQDHPAREMQDTFYLKypgigdlpeelvervkEVHehggdtgsrgwgykwdediakrlVLRTHTtalSARY-- 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 160 lvrsgldcflLAGD------------VYRRDEVDSSHYPVFHQMEGVRLfsnhelfagvenGEDLSLferggrRTpqkqe 227
Cdd:PRK04172 343 ----------LASRpeppqkyfsigrVFRPDTIDATHLPEFYQLEGIVM------------GEDVSF------RD----- 389

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 228 thtleavkLLEFdLKRALTRLvrhlfGEDlEIRWVDCYFPFTHPSFEMEVFFQG-DWMEVLGCGVMEQELVRSAGADNKM 306
Cdd:PRK04172 390 --------LLGI-LKEFYKRL-----GFE-EVKFRPAYFPFTEPSVEVEVYHEGlGWVELGGAGIFRPEVLEPLGIDVPV 454

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 157743298 307 GwAFGLGLERLAMVLFGIPDIRLFWSEDERFLKQFR 342
Cdd:PRK04172 455 L-AWGLGIERLAMLRLGLDDIRDLYSSDIEWLRERP 489
pheT PRK00629
phenylalanyl-tRNA synthetase subunit beta; Reviewed
 350-446 1.08e-17

phenylalanyl-tRNA synthetase subunit beta; Reviewed


Pssm-ID: 234804 [Multi-domain]  Cd Length: 791  Bit Score: 85.61  E-value: 1.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 350 VTFQPLSKYPPLFNDISFWLPaEGYTENDFFDLVRSIGGDLVEKVTLVDTFTHPKMK--KVSHCYRLVYRHMERTLTQEE 427
Cdd:PRK00629 691 PKYKPISKFPAVRRDLALVVD-EDVPAADILKAIKKAGGKLLESVELFDVYEGKGIGegKKSLAFRLTFQDPDRTLTDEE 769

                         90
                 ....*....|....*....
gi 157743298 428 VSIVHTAIQTAVEQELGVQ 446
Cdd:PRK00629 770 INAAMDKIVAALEEKFGAE 788
PheT COG0072
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; ...
 348-446 2.82e-17

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: 84.45  E-value: 2.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 348 QPVTFQPLSKYPPLFNDISFWLPaEGYTENDFFDLVRSIGGDLVEKVTLVDTFTHPKMK--KVSHCYRLVYRHMERTLTQ 425
Cdd:COG0072  691 KVPKYKPISKFPAVRRDLALVVD-EDVPAADVLDAIRKAAGKLLEDVRLFDVYEGKGVPegKKSLAFSLTLQDPDRTLTD 769

                         90       100
                 ....*....|....*....|.
gi 157743298 426 EEVSIVHTAIQTAVEQELGVQ 446
Cdd:COG0072  770 EEIDAAMDKIVAALEKKFGAE 790
pheT_bact TIGR00472
phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Every known example of ...
 352-448 9.98e-15

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


Pssm-ID: 273097 [Multi-domain]  Cd Length: 797  Bit Score: 76.56  E-value: 9.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298  352 FQPLSKYPPLFNDISFWLPaEGYTENDFFDLVRSIGGDLVEKVTLVDTFTHPKMK--KVSHCYRLVYRHMERTLTQEEVS 429
Cdd:TIGR00472 700 YRPISKFPAVTRDISFLVP-KDVPANEIIKLIKKSGLELLEEVELFDVYQGKNIGegKKSLALRLVLRDKERTLTDEEIN 778

                          90
                  ....*....|....*....
gi 157743298  430 IVHTAIQTAVEQELGVQGR 448
Cdd:TIGR00472 779 KIVEKVLNALKEKLGAELR 797
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 122-330 1.58e-08

phenylalanyl-tRNA synthetase alpha chain; Provisional


Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 56.51  E-value: 1.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 122 NFDSLLIPADHPS--------CKKGE--------NYYLNR---TH----------------------MLRAHTSA----- 155
Cdd:PTZ00326 262 NFDALFQPQQHPArdaqdtffLSKPEtskvndldDDYVERvkkVHevggygsigwrydwkleearknILRTHTTAvsarm 341

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 156 -HQ--KELVRSGldCF----LLAGD-VYRRDEVDSSHYPVFHQMEGVRLfsnhelfagvenGEDLSLferggrrtpqKQE 227
Cdd:PTZ00326 342 lYKlaQEYKKTG--PFkpkkYFSIDrVFRNETLDATHLAEFHQVEGFVI------------DRNLTL----------GDL 397

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 228 THTLEavkllEFDLKRALTRLvrhlfgedleiRWVDCYFPFTHPSfeMEVF-FQ---GDWMEVLGCGVMEQELVRSAGAD 303
Cdd:PTZ00326 398 IGTIR-----EFFRRIGITKL-----------RFKPAFNPYTEPS--MEIFgYHpglKKWVEVGNSGIFRPEMLRPMGFP 459

                        250       260       270
                 ....*....|....*....|....*....|.
gi 157743298 304 ---NKMGWafGLGLERLAMVLFGIPDIR-LF 330
Cdd:PTZ00326 460 edvTVIAW--GLSLERPTMIKYGIKNIRdLF 488
PLN02853 PLN02853
Probable phenylalanyl-tRNA synthetase alpha chain
 148-330 7.32e-07

Probable phenylalanyl-tRNA synthetase alpha chain


Pssm-ID: 215458 [Multi-domain]  Cd Length: 492  Bit Score: 51.21  E-value: 7.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 148 MLRAHTSAhqkelVRSGLdCFLLAGD------------VYRRDEVDSSHYPVFHQMEGvrlfsnheLFAGVengeDLSLF 215
Cdd:PLN02853 319 LLRTHTTA-----VSSRM-LYKLAQKgfkpkryfsidrVFRNEAVDRTHLAEFHQVEG--------LVCDR----GLTLG 380

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 216 ERGGrrtpqkqethTLEavkllEFDLKRALTRLvrhlfgedleiRWVDCYFPFTHPSfeMEVFFQ----GDWMEVLGCGV 291
Cdd:PLN02853 381 DLIG----------VLE-----DFFSRLGMTKL-----------RFKPAYNPYTEPS--MEIFSYheglKKWVEVGNSGM 432

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 157743298 292 MEQELVRSAGAD---NKMGWafGLGLERLAMVLFGIPDIR-LF 330
Cdd:PLN02853 433 FRPEMLLPMGLPedvNVIAW--GLSLERPTMILYGIDNIRdLF 473
syfB CHL00192
phenylalanyl-tRNA synthetase beta chain; Provisional
 335-443 1.38e-06

phenylalanyl-tRNA synthetase beta chain; Provisional


Pssm-ID: 214391 [Multi-domain]  Cd Length: 704  Bit Score: 50.86  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 335 ERFLKQFRLsdiyqpVTFQPLSKYPPLFNDISFWLPaEGYTENDFFDLVRSIGGDLVEKVTLVDTFTHP--KMKKVSHCY 412
Cdd:CHL00192 595 QYSIQQNNL------ISYQPYSSYPKIIRDLSFIIK-KSISISKIKELIYQNGDNLLESITLFDYYKGKsiPNGHTSLGL 667

                         90       100       110
                 ....*....|....*....|....*....|.
gi 157743298 413 RLVYRHMERTLTQEEVSIVHTAIQTAVEQEL 443
Cdd:CHL00192 668 RLTFQSENKTLTNEEIDRIQQNLQKVLEKKL 698
class_II_aaRS-like_core cd00768
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
 149-317 2.40e-03

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: 39.41  E-value: 2.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 149 LRAHTSAHQKELVRSGLDC--FLLA--GDVYRRDEVDSS--HYPVFHQMEGVRLFsnhelfagvENGEDLSLFERggrrt 222
Cdd:cd00768   55 LRPTLEPGLVRLFVSHIRKlpLRLAeiGPAFRNEGGRRGlrRVREFTQLEGEVFG---------EDGEEASEFEE----- 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743298 223 pqkqethtleavkllefdLKRALTRLVRHLFGEDLEIRWVDCYFPFTH----PSFEMEVFF-QGDWMEVLGCGVMEQELV 297
Cdd:cd00768  121 ------------------LIELTEELLRALGIKLDIVFVEKTPGEFSPggagPGFEIEVDHpEGRGLEIGSGGYRQDEQA 182

                        170       180
                 ....*....|....*....|....*....
gi 157743298 298 RSA-----GADNKMGW----AFGLGLERL 317
Cdd:cd00768  183 RAAdlyflDEALEYRYpptiGFGLGLERL 211
 
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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