NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|317044956|gb|ADU90046|]
View 

phenylalanyl-tRNA synthetase alpha chain, partial [Streptococcus equi subsp. zooepidemicus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PheS super family cl33741
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 1-170 1.17e-95

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


The actual alignment was detected with superfamily member COG0016:

Pssm-ID: 439787 [Multi-domain]  Cd Length: 339  Bit Score: 280.40  E-value: 1.17e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317044956   1 ALKQLNG-DHSKELQELRVAVLGKKGTLTELLKGLKDLSNDLRPVVGKQVNELRDFLTQAFEEQAKVVEAAKIQAKLDSE 79
Cdd:COG0016   11 ALAAIAAaSDLEELEALRVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEAAELEARLAAE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317044956  80 SIDVTLPGRQMKQGYRHVLTQISEEIEDIFLGMGFQIVDGFEVEKDYYNFERMNLPKDHPARDMQDTFYITEDILLRTHT 159
Cdd:COG0016   91 TIDVTLPGRPRPLGSLHPLTQVIEEIEDIFVGMGFEVAEGPEIETDWYNFEALNIPPDHPARDMQDTFYIDDGLLLRTHT 170

                        170
                 ....*....|.
gi 317044956 160 SPVQARTLDQH 170
Cdd:COG0016  171 SPVQIRTMEKQ 181
 
Name Accession Description Interval E-value
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 1-170 1.17e-95

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: 280.40  E-value: 1.17e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317044956   1 ALKQLNG-DHSKELQELRVAVLGKKGTLTELLKGLKDLSNDLRPVVGKQVNELRDFLTQAFEEQAKVVEAAKIQAKLDSE 79
Cdd:COG0016   11 ALAAIAAaSDLEELEALRVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEAAELEARLAAE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317044956  80 SIDVTLPGRQMKQGYRHVLTQISEEIEDIFLGMGFQIVDGFEVEKDYYNFERMNLPKDHPARDMQDTFYITEDILLRTHT 159
Cdd:COG0016   91 TIDVTLPGRPRPLGSLHPLTQVIEEIEDIFVGMGFEVAEGPEIETDWYNFEALNIPPDHPARDMQDTFYIDDGLLLRTHT 170

                        170
                 ....*....|.
gi 317044956 160 SPVQARTLDQH 170
Cdd:COG0016  171 SPVQIRTMEKQ 181
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 26-171 7.45e-50

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: 162.10  E-value: 7.45e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317044956   26 TLTELLKGLKDLSND-LRPVVGKQVNELRDFLTQAFEEQAKVVEAAKIQAKLDSESIDVTLPGRQMKQGYRHVLTQISEE 104
Cdd:TIGR00468   1 KLKDLLKQLGKLTKEeTKPALGALINEVKIELQDELTKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 317044956  105 IEDIFLGMGFQIVDGFEVEKDYYNFERMNLPKDHPARDMQDTFYITEDILLRTHTSPVQARTLDQHD 171
Cdd:TIGR00468  81 IRDIFLGLGFTEETGPEVETDFWNFDALNIPQDHPARDMQDTFYIKDRLLLRTHTTAVQLRTMEEQE 147
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 80-169 1.68e-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: 149.65  E-value: 1.68e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317044956   80 SIDVTLPGRQMKQGYRHVLTQISEEIEDIFLGMGFQIVDGFEVEKDYYNFERMNLPKDHPARDMQDTFYI-------TED 152
Cdd:pfam01409   1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVEGPEVESDFYNFDALNIPQDHPARDMQDTFYLkkplkpvARR 80

                          90
                  ....*....|....*..
gi 317044956  153 ILLRTHTSPVQARTLDQ 169
Cdd:pfam01409  81 LLLRTHTTPVQARTLAK 97
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 96-167 5.55e-37

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: 126.89  E-value: 5.55e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 317044956  96 HVLTQISEEIEDIFLGMGFQIVDGFEVEKDYYNFERMNLPKDHPARDMQDTFYI--TEDILLRTHTSPVQARTL 167
Cdd:cd00496    1 HPLNKVIEEIEDIFVSMGFTEVEGPEVETDFYNFDALNIPQDHPARDMQDTFYIndPARLLLRTHTSAVQARAL 74
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
61-152 7.71e-17

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 76.79  E-value: 7.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317044956  61 EEQAKVVEAAKIQAKLDSESI-------------DVTLPGRQMKQGYRHVLTQISEEIEDIFLGMGFQIVDGFEVEKDYY 127
Cdd:PRK04172 185 ELLKEGIELKEEITQLTPELLksgewkekefrpyNVKAPPPKIYPGKKHPYREFIDEVRDILVEMGFEEMKGPLVETEFW 264

                         90       100
                 ....*....|....*....|....*
gi 317044956 128 NFERMNLPKDHPARDMQDTFYITED 152
Cdd:PRK04172 265 NFDALFQPQDHPAREMQDTFYLKYP 289
 
Name Accession Description Interval E-value
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 1-170 1.17e-95

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: 280.40  E-value: 1.17e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317044956   1 ALKQLNG-DHSKELQELRVAVLGKKGTLTELLKGLKDLSNDLRPVVGKQVNELRDFLTQAFEEQAKVVEAAKIQAKLDSE 79
Cdd:COG0016   11 ALAAIAAaSDLEELEALRVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEAAELEARLAAE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317044956  80 SIDVTLPGRQMKQGYRHVLTQISEEIEDIFLGMGFQIVDGFEVEKDYYNFERMNLPKDHPARDMQDTFYITEDILLRTHT 159
Cdd:COG0016   91 TIDVTLPGRPRPLGSLHPLTQVIEEIEDIFVGMGFEVAEGPEIETDWYNFEALNIPPDHPARDMQDTFYIDDGLLLRTHT 170

                        170
                 ....*....|.
gi 317044956 160 SPVQARTLDQH 170
Cdd:COG0016  171 SPVQIRTMEKQ 181
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 26-171 7.45e-50

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: 162.10  E-value: 7.45e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317044956   26 TLTELLKGLKDLSND-LRPVVGKQVNELRDFLTQAFEEQAKVVEAAKIQAKLDSESIDVTLPGRQMKQGYRHVLTQISEE 104
Cdd:TIGR00468   1 KLKDLLKQLGKLTKEeTKPALGALINEVKIELQDELTKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 317044956  105 IEDIFLGMGFQIVDGFEVEKDYYNFERMNLPKDHPARDMQDTFYITEDILLRTHTSPVQARTLDQHD 171
Cdd:TIGR00468  81 IRDIFLGLGFTEETGPEVETDFWNFDALNIPQDHPARDMQDTFYIKDRLLLRTHTTAVQLRTMEEQE 147
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 80-169 1.68e-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: 149.65  E-value: 1.68e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317044956   80 SIDVTLPGRQMKQGYRHVLTQISEEIEDIFLGMGFQIVDGFEVEKDYYNFERMNLPKDHPARDMQDTFYI-------TED 152
Cdd:pfam01409   1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVEGPEVESDFYNFDALNIPQDHPARDMQDTFYLkkplkpvARR 80

                          90
                  ....*....|....*..
gi 317044956  153 ILLRTHTSPVQARTLDQ 169
Cdd:pfam01409  81 LLLRTHTTPVQARTLAK 97
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 96-167 5.55e-37

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: 126.89  E-value: 5.55e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 317044956  96 HVLTQISEEIEDIFLGMGFQIVDGFEVEKDYYNFERMNLPKDHPARDMQDTFYI--TEDILLRTHTSPVQARTL 167
Cdd:cd00496    1 HPLNKVIEEIEDIFVSMGFTEVEGPEVETDFYNFDALNIPQDHPARDMQDTFYIndPARLLLRTHTSAVQARAL 74
Phe_tRNA-synt_N pfam02912
Aminoacyl tRNA synthetase class II, N-terminal domain;
10-76 9.19e-24

Aminoacyl tRNA synthetase class II, N-terminal domain;


Pssm-ID: 460745 [Multi-domain]  Cd Length: 69  Bit Score: 88.59  E-value: 9.19e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 317044956   10 SKELQELRVAVLGKKGTLTELLKGLKDLSNDLRPVVGKQVNELRDFLTQAFEEQAKVVEAAKIQAKL 76
Cdd:pfam02912   3 LEELEELRVKYLGKKGELTALLKGLGKLPPEERPAAGKLINELKQAIEAALEERKEELEAAELEARL 69
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
61-152 7.71e-17

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 76.79  E-value: 7.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317044956  61 EEQAKVVEAAKIQAKLDSESI-------------DVTLPGRQMKQGYRHVLTQISEEIEDIFLGMGFQIVDGFEVEKDYY 127
Cdd:PRK04172 185 ELLKEGIELKEEITQLTPELLksgewkekefrpyNVKAPPPKIYPGKKHPYREFIDEVRDILVEMGFEEMKGPLVETEFW 264

                         90       100
                 ....*....|....*....|....*
gi 317044956 128 NFERMNLPKDHPARDMQDTFYITED 152
Cdd:PRK04172 265 NFDALFQPQDHPAREMQDTFYLKYP 289
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 87-167 2.04e-15

phenylalanyl-tRNA synthetase alpha chain; Provisional


Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 72.69  E-value: 2.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317044956  87 GRQMKQGYRHVLTQISEEIEDIFLGMGFQIVDGFE-VEKDYYNFERMNLPKDHPARDMQDTFYITE-------DI----- 153
Cdd:PTZ00326 220 GKKIGGGNLHPLLKVRREFREILLEMGFEEMPTNRyVESSFWNFDALFQPQQHPARDAQDTFFLSKpetskvnDLdddyv 299

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 317044956 154 -----------------------------LLRTHTSPVQARTL 167
Cdd:PTZ00326 300 ervkkvhevggygsigwrydwkleearknILRTHTTAVSARML 342
PLN02853 PLN02853
Probable phenylalanyl-tRNA synthetase alpha chain
 87-167 2.21e-10

Probable phenylalanyl-tRNA synthetase alpha chain


Pssm-ID: 215458 [Multi-domain]  Cd Length: 492  Bit Score: 58.15  E-value: 2.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317044956  87 GRQMKQGYRHVLTQISEEIEDIFLGMGFQIV--DGFeVEKDYYNFERMNLPKDHPARDMQDTFYIT---------EDI-- 153
Cdd:PLN02853 212 GAPPEGGHLHPLLKVRQQFRKIFLQMGFEEMptNNF-VESSFWNFDALFQPQQHPARDSHDTFFLKapattrqlpEDYve 290

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 317044956 154 ----------------------------LLRTHTSPVQARTL 167
Cdd:PLN02853 291 rvktvhesggygsigygydwkreeanknLLRTHTTAVSSRML 332
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 87-167 3.07e-10

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 57.85  E-value: 3.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317044956  87 GRQMKQGYRHVLTQISEEIEDIF---LGMGFQIVDG-FEVEKDYYNFERMNLPKDHPARDMQDTFYITEDILLRTHTSPV 162
Cdd:PLN02788  59 GMQLHRRPDHPLGILKNAIYDYFdenYSNKFKKFDDlSPIVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAH 138


                 ....*
gi 317044956 163 QARTL 167
Cdd:PLN02788 139 QAELL 143
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 67-163 2.81e-09

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: 55.08  E-value: 2.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317044956   67 VEAAKIQAKLDSESIDVT-----LPGRQMKQGYRHVLTQISEEIEDIFLGMG--------FQIVDGFE-VEKDYYNFERM 132
Cdd:TIGR00469   8 LEINGIKYATDGQTTNVTdkiikLTDANKHLKEDHPLGIIRDLIEKKFNGADnnqrgnplFKIFDNFKpVVTTMENFDNL 87

                          90       100       110
                  ....*....|....*....|....*....|.
gi 317044956  133 NLPKDHPARDMQDTFYITEDILLRTHTSPVQ 163
Cdd:TIGR00469  88 GFPADHPGRQKSDCYYINEQHLLRAHTSAHE 118
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH