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Conserved domains on  [gi|28175596|gb|AAH43565|]
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FARSA protein, partial [Homo sapiens]

Protein Classification

phenylalanine--tRNA ligase alpha subunit( domain architecture ID 1003922)

phenylalanine--tRNA ligase alpha subunit catalyzes a two-step reaction, first charging a phenylalanine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; forms a heterotetramer of alpha(2)beta(2); binds two magnesium ions per tetramer

EC:  6.1.1.20
Gene Ontology:  GO:0004826|GO:0006432|GO:0005524|GO:0000049
PubMed:  20223217

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00326 super family cl30525
phenylalanyl-tRNA synthetase alpha chain; Provisional
 5-483 0e+00

phenylalanyl-tRNA synthetase alpha chain; Provisional


The actual alignment was detected with superfamily member PTZ00326:

Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 769.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596    5 VAELLLRRLEASDGGLDSAELAAELGMEHQAVVGAVKSLQALGeVIEAELRSTKHWELTAEGEEIAREGSHEARVFRSIP 84
Cdd:PTZ00326   7 EENTILSKLESENEIVNSLALAESLNIDHQKVVGAIKSLESAN-YITTEMKKSNTWTLTEEGEDYLKNGSPEYRLWQKLK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596   85 PEGLAQSELMRLPSG---KVGFSKAMSNKWIRVDKSAADGPRVFRVVDSMEDEVQRRLQLV-RGGQAEKLGEKERSELRK 160
Cdd:PTZ00326  86 EGGISKADDAKKLGGkvaDIGLGNAMKKKWIKLNKGDKKVFLSRKLVDSVVDTVRLLLKIVaKGSQAEKIDSKELKELKK 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596  161 RKLLAEVTLKTYWVSKGSAFSTSISKQETELSPEMISSGSWRDRPFKPYNFLAHGVLPDSGHLHPLLKVRSQFRQIFLEM 240
Cdd:PTZ00326 166 RKLATLEKIKYFVVTKGPKFAKEIKKQITDLTQEMLLNGSWKNAEFKEYNFNALGKKIGGGNLHPLLKVRREFREILLEM 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596  241 GFTEMPTDNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPA--EALQLPMDYVQRVKRTHSQGGYGSQGYKYNWKLDEA 318
Cdd:PTZ00326 246 GFEEMPTNRYVESSFWNFDALFQPQQHPARDAQDTFFLSKPEtsKVNDLDDDYVERVKKVHEVGGYGSIGWRYDWKLEEA 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596  319 RKNLLRTHTTSASARALYRLAQ----KKPFTPVKYFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTLGHLMGVLREFF 394
Cdd:PTZ00326 326 RKNILRTHTTAVSARMLYKLAQeykkTGPFKPKKYFSIDRVFRNETLDATHLAEFHQVEGFVIDRNLTLGDLIGTIREFF 405

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596  395 TKLGITQLRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLERPTMIKYGINNIR 474
Cdd:PTZ00326 406 RRIGITKLRFKPAFNPYTEPSMEIFGYHPGLKKWVEVGNSGIFRPEMLRPMGFPEDVTVIAWGLSLERPTMIKYGIKNIR 485


                 ....*....
gi 28175596  475 ELVGHKVNL 483
Cdd:PTZ00326 486 DLFGHKVDL 494
 
Name Accession Description Interval E-value
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 5-483 0e+00

phenylalanyl-tRNA synthetase alpha chain; Provisional


Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 769.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596    5 VAELLLRRLEASDGGLDSAELAAELGMEHQAVVGAVKSLQALGeVIEAELRSTKHWELTAEGEEIAREGSHEARVFRSIP 84
Cdd:PTZ00326   7 EENTILSKLESENEIVNSLALAESLNIDHQKVVGAIKSLESAN-YITTEMKKSNTWTLTEEGEDYLKNGSPEYRLWQKLK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596   85 PEGLAQSELMRLPSG---KVGFSKAMSNKWIRVDKSAADGPRVFRVVDSMEDEVQRRLQLV-RGGQAEKLGEKERSELRK 160
Cdd:PTZ00326  86 EGGISKADDAKKLGGkvaDIGLGNAMKKKWIKLNKGDKKVFLSRKLVDSVVDTVRLLLKIVaKGSQAEKIDSKELKELKK 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596  161 RKLLAEVTLKTYWVSKGSAFSTSISKQETELSPEMISSGSWRDRPFKPYNFLAHGVLPDSGHLHPLLKVRSQFRQIFLEM 240
Cdd:PTZ00326 166 RKLATLEKIKYFVVTKGPKFAKEIKKQITDLTQEMLLNGSWKNAEFKEYNFNALGKKIGGGNLHPLLKVRREFREILLEM 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596  241 GFTEMPTDNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPA--EALQLPMDYVQRVKRTHSQGGYGSQGYKYNWKLDEA 318
Cdd:PTZ00326 246 GFEEMPTNRYVESSFWNFDALFQPQQHPARDAQDTFFLSKPEtsKVNDLDDDYVERVKKVHEVGGYGSIGWRYDWKLEEA 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596  319 RKNLLRTHTTSASARALYRLAQ----KKPFTPVKYFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTLGHLMGVLREFF 394
Cdd:PTZ00326 326 RKNILRTHTTAVSARMLYKLAQeykkTGPFKPKKYFSIDRVFRNETLDATHLAEFHQVEGFVIDRNLTLGDLIGTIREFF 405

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596  395 TKLGITQLRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLERPTMIKYGINNIR 474
Cdd:PTZ00326 406 RRIGITKLRFKPAFNPYTEPSMEIFGYHPGLKKWVEVGNSGIFRPEMLRPMGFPEDVTVIAWGLSLERPTMIKYGIKNIR 485


                 ....*....
gi 28175596  475 ELVGHKVNL 483
Cdd:PTZ00326 486 DLFGHKVDL 494
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 208-482 6.34e-116

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: 341.48  E-value: 6.34e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596   208 PYNFLAHGVLPDSGHLHPLLKVRSQFRQIFLEMGFTEMPtDNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPAEAlql 287
Cdd:pfam01409   1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVE-GPEVESDFYNFDALNIPQDHPARDMQDTFYLKKPLKP--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596   288 pmdyvqrvkrthsqggygsqgykynwkldEARKNLLRTHTTSASARALYrlaqKKPFTPVKYFSIDRVFRNETLDATHLA 367
Cdd:pfam01409  77 -----------------------------VARRLLLRTHTTPVQARTLA----KKPKPPIKIFSIGRVFRRDQVDATHLP 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596   368 EFHQIEGVVADHGLTLGHLMGVLREFFTKL-GIT-QLRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGVFRPEMLLPM 445
Cdd:pfam01409 124 EFHQVEGLVVDENVTFADLKGVLEEFLRKFfGFEvKVRFRPSYFPFTEPSAEVDVYVCKLGGWLEVGGAGMVHPNVLEAV 203

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 28175596   446 GLPENVSVIAWGLSLERPTMIKYGINNIRELVGHKVN 482
Cdd:pfam01409 204 GIDEDYSGFAFGLGVERLAMLKYGIDDIRDLYENDLR 240
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 224-482 1.45e-115

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: 339.52  E-value: 1.45e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596 224 HPLLKVRSQFRQIFLEMGFTEMPTdNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPAealqlpmdyvqrvkrthsqgg 303
Cdd:cd00496   1 HPLNKVIEEIEDIFVSMGFTEVEG-PEVETDFYNFDALNIPQDHPARDMQDTFYINDPA--------------------- 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596 304 ygsqgykynwkldearKNLLRTHTTSASARALYRLaqkkpFTPVKYFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTL 383
Cdd:cd00496  59 ----------------RLLLRTHTSAVQARALAKL-----KPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKGLTF 117

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596 384 GHLMGVLREFFTKLG--ITQLRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLE 461
Cdd:cd00496 118 ADLKGTLEEFAKELFgpITKVRFRPSYFPFTEPSFEVDVYCPGCLGWLEILGCGMVRPEVLENAGIDEEYSGFAFGIGLE 197

                       250       260
                ....*....|....*....|.
gi 28175596 462 RPTMIKYGINNIRELVGHKVN 482
Cdd:cd00496 198 RLAMLKYGIPDIRLFYSNDLR 218
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 189-481 2.43e-109

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: 326.58  E-value: 2.43e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596   189 TELSPEMISSGSWRDRPFKPYNFLAHGVLPDSGHLHPLLKVRSQFRQIFLEMGFTEMPtDNFIESSFWNFDALFQPQQHP 268
Cdd:TIGR00468  37 TKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDEIRDIFLGLGFTEET-GPEVETDFWNFDALNIPQDHP 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596   269 ARDQHDTFFLRDpaealqlpmdyvqrvkrthsqggygsqgykynwkldearKNLLRTHTTSASARALyrlaQKKPFTPVK 348
Cdd:TIGR00468 116 ARDMQDTFYIKD---------------------------------------RLLLRTHTTAVQLRTM----EEQEKPPIR 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596   349 YFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTLGHLMGVLREFFTKL-GITQLRFKPAYNPYTEPSMEVFSYHQGLKK 427
Cdd:TIGR00468 153 IFSPGRVFRNDTVDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLKKMfGETEIRFRPSYFPFTEPSAEIDVYCPEGKG 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 28175596   428 WVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLERPTMIKYGINNIRELVGHKV 481
Cdd:TIGR00468 233 WLEVLGAGMFRPEVLEPMGIDPTYPGFAWGIGIERLAMLKYGITDIRDLYENDL 286
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 215-477 3.86e-57

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: 193.35  E-value: 3.86e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596 215 GVLPDSGHLHPLLKVRSQFRQIFLEMGFT-----EmptdnfIESSFWNFDALFQPQQHPARDQHDTFFLRDpaealqlpm 289
Cdd:COG0016  98 GRPRPLGSLHPLTQVIEEIEDIFVGMGFEvaegpE------IETDWYNFEALNIPPDHPARDMQDTFYIDD--------- 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596 290 dyvqrvkrthsqggygsqgykynwkldearKNLLRTHTTSASARALyrLAQKkpfTPVKYFSIDRVFRNETLDATHLAEF 369
Cdd:COG0016 163 ------------------------------GLLLRTHTSPVQIRTM--EKQK---PPIRIIAPGRVYRRDESDATHSPMF 207

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596 370 HQIEGVVADHGLTLGHLMGVLREFFTKL-GI-TQLRFKPAYNPYTEPSMEV-FSYHQGLKK---------WVEVGNSGVF 437
Cdd:COG0016 208 HQVEGLVVDKGISFADLKGTLEEFAKAFfGEdVKVRFRPSYFPFTEPSAEVdISCFICGGKgcrvckgtgWLEILGCGMV 287

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 28175596 438 RPEMLLPMGL-PENVSVIAWGLSLERPTMIKYGINNIRELV 477
Cdd:COG0016 288 HPNVLRAVGIdPEEYSGFAFGMGIERLAMLKYGIDDIRLFF 328
 
Name Accession Description Interval E-value
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 5-483 0e+00

phenylalanyl-tRNA synthetase alpha chain; Provisional


Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 769.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596    5 VAELLLRRLEASDGGLDSAELAAELGMEHQAVVGAVKSLQALGeVIEAELRSTKHWELTAEGEEIAREGSHEARVFRSIP 84
Cdd:PTZ00326   7 EENTILSKLESENEIVNSLALAESLNIDHQKVVGAIKSLESAN-YITTEMKKSNTWTLTEEGEDYLKNGSPEYRLWQKLK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596   85 PEGLAQSELMRLPSG---KVGFSKAMSNKWIRVDKSAADGPRVFRVVDSMEDEVQRRLQLV-RGGQAEKLGEKERSELRK 160
Cdd:PTZ00326  86 EGGISKADDAKKLGGkvaDIGLGNAMKKKWIKLNKGDKKVFLSRKLVDSVVDTVRLLLKIVaKGSQAEKIDSKELKELKK 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596  161 RKLLAEVTLKTYWVSKGSAFSTSISKQETELSPEMISSGSWRDRPFKPYNFLAHGVLPDSGHLHPLLKVRSQFRQIFLEM 240
Cdd:PTZ00326 166 RKLATLEKIKYFVVTKGPKFAKEIKKQITDLTQEMLLNGSWKNAEFKEYNFNALGKKIGGGNLHPLLKVRREFREILLEM 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596  241 GFTEMPTDNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPA--EALQLPMDYVQRVKRTHSQGGYGSQGYKYNWKLDEA 318
Cdd:PTZ00326 246 GFEEMPTNRYVESSFWNFDALFQPQQHPARDAQDTFFLSKPEtsKVNDLDDDYVERVKKVHEVGGYGSIGWRYDWKLEEA 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596  319 RKNLLRTHTTSASARALYRLAQ----KKPFTPVKYFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTLGHLMGVLREFF 394
Cdd:PTZ00326 326 RKNILRTHTTAVSARMLYKLAQeykkTGPFKPKKYFSIDRVFRNETLDATHLAEFHQVEGFVIDRNLTLGDLIGTIREFF 405

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596  395 TKLGITQLRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLERPTMIKYGINNIR 474
Cdd:PTZ00326 406 RRIGITKLRFKPAFNPYTEPSMEIFGYHPGLKKWVEVGNSGIFRPEMLRPMGFPEDVTVIAWGLSLERPTMIKYGIKNIR 485


                 ....*....
gi 28175596  475 ELVGHKVNL 483
Cdd:PTZ00326 486 DLFGHKVDL 494
PLN02853 PLN02853
Probable phenylalanyl-tRNA synthetase alpha chain
 7-495 0e+00

Probable phenylalanyl-tRNA synthetase alpha chain


Pssm-ID: 215458 [Multi-domain]  Cd Length: 492  Bit Score: 768.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596    7 ELLLRRLEASDGGLDSAELAAELGMEHQAVVGAVKSLQALGeVIEAELRSTKHWELTAEGEEIAREGSHEARVFRSIPPE 86
Cdd:PLN02853   6 EALLGALSNNEEISDSGQFAASHGLDHNEVVGVIKSLHGFR-YVDAQDIKRETWVLTEEGKKYAAEGSPEVQLFAAVPAE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596   87 G-LAQSELMRL--PS-GKVGFSKAMSNKWIRVDKsaadGPRVFRVVDSMEDEVQRRLQLVRGGQAekLGEKERSEL-RKR 161
Cdd:PLN02853  85 GsISKDELQKKldPAvFDIGFKQAMKNKWLEMGG----KPQVSRKVQHVEDEVKELLLAIQEGKE--VDDKDIDALkKRR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596  162 KLLAEVTLKTYWVSKGSAFSTSISKQETELSPEMISSGSWRDRPFKPYNFLAHGVLPDSGHLHPLLKVRSQFRQIFLEMG 241
Cdd:PLN02853 159 KLITLETWKGYSIKKGPNYAPERKKAATDLTREMLQSGDWKDLEFKEYNFNALGAPPEGGHLHPLLKVRQQFRKIFLQMG 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596  242 FTEMPTDNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPAEALQLPMDYVQRVKRTHSQGGYGSQGYKYNWKLDEARKN 321
Cdd:PLN02853 239 FEEMPTNNFVESSFWNFDALFQPQQHPARDSHDTFFLKAPATTRQLPEDYVERVKTVHESGGYGSIGYGYDWKREEANKN 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596  322 LLRTHTTSASARALYRLAQKkPFTPVKYFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTLGHLMGVLREFFTKLGITQ 401
Cdd:PLN02853 319 LLRTHTTAVSSRMLYKLAQK-GFKPKRYFSIDRVFRNEAVDRTHLAEFHQVEGLVCDRGLTLGDLIGVLEDFFSRLGMTK 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596  402 LRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLERPTMIKYGINNIRELVGHKV 481
Cdd:PLN02853 398 LRFKPAYNPYTEPSMEIFSYHEGLKKWVEVGNSGMFRPEMLLPMGLPEDVNVIAWGLSLERPTMILYGIDNIRDLFGHKV 477

                        490
                 ....*....|....
gi 28175596  482 NLQMVYDSPLCRLD 495
Cdd:PLN02853 478 DLGLIKRNPICRLG 491
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
9-476 8.08e-156

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 452.75  E-value: 8.08e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596    9 LLRRLEASDGgLDSAELAAELGMEHQAVVGAVKSLQALGeVIEAELRSTKHWELTAEGEEIAREGSHEARVFRSIPPEG- 87
Cdd:PRK04172  11 VLKALKELKE-ATLEELAEKLGLPPEAVMRAAEWLEEKG-LVKVEERVEEVYVLTEEGKKYAEEGLPERRLLNALKDGGe 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596   88 LAQSELMRLPSGKVGFSKAMSN----KWIRVDKSaadgpRVFRVVDSMEDEVQRRLQLVRGGQAEKLGEKER---SELRK 160
Cdd:PRK04172  89 VSLDELKEALLDKKEVGIALGNlarkGWAKIEKG-----KVILKPDAYEDPEEKALKALAEGDKEELSEEDLkvlKELKK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596  161 RKLLAEVTLKTYWVS---KG-SAFSTSISKQE--TELSPEMISSGSWRDRPFKPYNFLAHGVLPDSGHLHPLLKVRSQFR 234
Cdd:PRK04172 164 RKLVEEKERTERSVEltdAGlELLKEGIELKEeiTQLTPELLKSGEWKEKEFRPYNVKAPPPKIYPGKKHPYREFIDEVR 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596  235 QIFLEMGFTEMpTDNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPAEAlQLPMDYVQRVKRTHSQGG-YGSQGYKYNW 313
Cdd:PRK04172 244 DILVEMGFEEM-KGPLVETEFWNFDALFQPQDHPAREMQDTFYLKYPGIG-DLPEELVERVKEVHEHGGdTGSRGWGYKW 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596  314 KLDEARKNLLRTHTTSASARALYRLAQKkpftPVKYFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTLGHLMGVLREF 393
Cdd:PRK04172 322 DEDIAKRLVLRTHTTALSARYLASRPEP----PQKYFSIGRVFRPDTIDATHLPEFYQLEGIVMGEDVSFRDLLGILKEF 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596  394 FTKLGITQLRFKPAYNPYTEPSMEVFSYHQGLkKWVEVGNSGVFRPEMLLPMGLpeNVSVIAWGLSLERPTMIKYGINNI 473
Cdd:PRK04172 398 YKRLGFEEVKFRPAYFPFTEPSVEVEVYHEGL-GWVELGGAGIFRPEVLEPLGI--DVPVLAWGLGIERLAMLRLGLDDI 474


                 ...
gi 28175596  474 REL 476
Cdd:PRK04172 475 RDL 477
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 208-482 6.34e-116

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: 341.48  E-value: 6.34e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596   208 PYNFLAHGVLPDSGHLHPLLKVRSQFRQIFLEMGFTEMPtDNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPAEAlql 287
Cdd:pfam01409   1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVE-GPEVESDFYNFDALNIPQDHPARDMQDTFYLKKPLKP--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596   288 pmdyvqrvkrthsqggygsqgykynwkldEARKNLLRTHTTSASARALYrlaqKKPFTPVKYFSIDRVFRNETLDATHLA 367
Cdd:pfam01409  77 -----------------------------VARRLLLRTHTTPVQARTLA----KKPKPPIKIFSIGRVFRRDQVDATHLP 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596   368 EFHQIEGVVADHGLTLGHLMGVLREFFTKL-GIT-QLRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGVFRPEMLLPM 445
Cdd:pfam01409 124 EFHQVEGLVVDENVTFADLKGVLEEFLRKFfGFEvKVRFRPSYFPFTEPSAEVDVYVCKLGGWLEVGGAGMVHPNVLEAV 203

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 28175596   446 GLPENVSVIAWGLSLERPTMIKYGINNIRELVGHKVN 482
Cdd:pfam01409 204 GIDEDYSGFAFGLGVERLAMLKYGIDDIRDLYENDLR 240
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 224-482 1.45e-115

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: 339.52  E-value: 1.45e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596 224 HPLLKVRSQFRQIFLEMGFTEMPTdNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPAealqlpmdyvqrvkrthsqgg 303
Cdd:cd00496   1 HPLNKVIEEIEDIFVSMGFTEVEG-PEVETDFYNFDALNIPQDHPARDMQDTFYINDPA--------------------- 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596 304 ygsqgykynwkldearKNLLRTHTTSASARALYRLaqkkpFTPVKYFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTL 383
Cdd:cd00496  59 ----------------RLLLRTHTSAVQARALAKL-----KPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKGLTF 117

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596 384 GHLMGVLREFFTKLG--ITQLRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLE 461
Cdd:cd00496 118 ADLKGTLEEFAKELFgpITKVRFRPSYFPFTEPSFEVDVYCPGCLGWLEILGCGMVRPEVLENAGIDEEYSGFAFGIGLE 197

                       250       260
                ....*....|....*....|.
gi 28175596 462 RPTMIKYGINNIRELVGHKVN 482
Cdd:cd00496 198 RLAMLKYGIPDIRLFYSNDLR 218
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 189-481 2.43e-109

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: 326.58  E-value: 2.43e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596   189 TELSPEMISSGSWRDRPFKPYNFLAHGVLPDSGHLHPLLKVRSQFRQIFLEMGFTEMPtDNFIESSFWNFDALFQPQQHP 268
Cdd:TIGR00468  37 TKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDEIRDIFLGLGFTEET-GPEVETDFWNFDALNIPQDHP 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596   269 ARDQHDTFFLRDpaealqlpmdyvqrvkrthsqggygsqgykynwkldearKNLLRTHTTSASARALyrlaQKKPFTPVK 348
Cdd:TIGR00468 116 ARDMQDTFYIKD---------------------------------------RLLLRTHTTAVQLRTM----EEQEKPPIR 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596   349 YFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTLGHLMGVLREFFTKL-GITQLRFKPAYNPYTEPSMEVFSYHQGLKK 427
Cdd:TIGR00468 153 IFSPGRVFRNDTVDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLKKMfGETEIRFRPSYFPFTEPSAEIDVYCPEGKG 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 28175596   428 WVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLERPTMIKYGINNIRELVGHKV 481
Cdd:TIGR00468 233 WLEVLGAGMFRPEVLEPMGIDPTYPGFAWGIGIERLAMLKYGITDIRDLYENDL 286
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 215-477 3.86e-57

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: 193.35  E-value: 3.86e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596 215 GVLPDSGHLHPLLKVRSQFRQIFLEMGFT-----EmptdnfIESSFWNFDALFQPQQHPARDQHDTFFLRDpaealqlpm 289
Cdd:COG0016  98 GRPRPLGSLHPLTQVIEEIEDIFVGMGFEvaegpE------IETDWYNFEALNIPPDHPARDMQDTFYIDD--------- 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596 290 dyvqrvkrthsqggygsqgykynwkldearKNLLRTHTTSASARALyrLAQKkpfTPVKYFSIDRVFRNETLDATHLAEF 369
Cdd:COG0016 163 ------------------------------GLLLRTHTSPVQIRTM--EKQK---PPIRIIAPGRVYRRDESDATHSPMF 207

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596 370 HQIEGVVADHGLTLGHLMGVLREFFTKL-GI-TQLRFKPAYNPYTEPSMEV-FSYHQGLKK---------WVEVGNSGVF 437
Cdd:COG0016 208 HQVEGLVVDKGISFADLKGTLEEFAKAFfGEdVKVRFRPSYFPFTEPSAEVdISCFICGGKgcrvckgtgWLEILGCGMV 287

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 28175596 438 RPEMLLPMGL-PENVSVIAWGLSLERPTMIKYGINNIRELV 477
Cdd:COG0016 288 HPNVLRAVGIdPEEYSGFAFGMGIERLAMLKYGIDDIRLFF 328
PheRS_DBD1 pfam18552
PheRS DNA binding domain 1; This is a DNA-binding fold domain found in Phenylalanyl-tRNA ...
 1-60 1.67e-24

PheRS DNA binding domain 1; This is a DNA-binding fold domain found in Phenylalanyl-tRNA Synthetase (EC:6.1.1.20) N-terminal region. This domain belongs to a superfamily of 'winged helix' DNA-biding domains. The topology of DBD-1 and DBD-3 closely resembles the topology of the Z-DNA-binding domain Zalpha of double-stranded RNA (dsRNA) adenosine deaminase and other domains from DNA-binding proteins. Mutational analysis indicate that DBD-1, 2 and 3 play critical roles in tRNA-Phe binding and recognition, i.e., from the drastic reduction of aminoacylation activity seen upon removal of the N-terminal domains.


Pssm-ID: 465796 [Multi-domain]  Cd Length: 59  Bit Score: 96.10  E-value: 1.67e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596     1 ADGQVAELLLRRLEAsDGGLDSAELAAELGMEHQAVVGAVKSLQALGEVIEAELRSTKHW 60
Cdd:pfam18552   1 MDKDLEEQILQYLEK-HGGVDSLDLAAELGVDHQKVVGAVKSLQALGDVITAEQRSSKHW 59
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 224-474 2.36e-19

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 90.21  E-value: 2.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596  224 HPLLKVRSQFRQIFLEM---GFTEMPTDNFIESSFWNFDALFQPQQHPARDQHDTFflrdpaealqlpmdYVQRvkrths 300
Cdd:PLN02788  68 HPLGILKNAIYDYFDENysnKFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTY--------------YVDA------ 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596  301 qggygsqgykynwkldearKNLLRTHTTSASARALYRLAQKkpftpvkYFSIDRVFRNETLDATHLAEFHQIEGV----- 375
Cdd:PLN02788 128 -------------------QTVLRCHTSAHQAELLRAGHTH-------FLVTGDVYRRDSIDATHYPVFHQMEGVrvfsp 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596  376 --VADHGLTLGH---------LMGVLREFFtklGITQLRFKPAYNPYTEPSMEVFSYHQGlkKWVEVGNSGVFRPEMLLP 444
Cdd:PLN02788 182 eeWEASGLDGTDlaaedlkktLEGLARHLF---GDVEMRWVDAYFPFTNPSFELEIFFKG--EWLEVLGCGVTEQEILKN 256

                        250       260       270
                 ....*....|....*....|....*....|..
gi 28175596  445 MGLPENVsviAW--GLSLERPTMIKYGINNIR 474
Cdd:PLN02788 257 NGRSDNV---AWafGLGLERLAMVLFDIPDIR 285
PheRS_DBD3 pfam18553
PheRS DNA binding domain 3; This is a DNA-binding fold domain found in Phenylalanyl-tRNA ...
 74-130 1.08e-18

PheRS DNA binding domain 3; This is a DNA-binding fold domain found in Phenylalanyl-tRNA Synthetase N-terminal region. This domain belongs to a superfamily of 'winged helix' DNA-biding domains. The topology of DBD-1 and DBD-3 closely resembles the topology of the Z-DNA-binding domain Zalpha of double-stranded RNA (dsRNA) adenosine deaminase and other domains from DNA-binding proteins. Mutational analysis indicate that DBD-1, 2 and 3 play critical roles in tRNAPhe binding and recognition, i.e., from the drastic reduction of aminoacylation activity seen upon removal of the N-terminal domains.


Pssm-ID: 465797 [Multi-domain]  Cd Length: 57  Bit Score: 79.62  E-value: 1.08e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596    74 SHEARVFRSIPP-EGLAQSELMRL--PSGKVGFSKAMSNKWIRVDKsaaDGPRVFRVVDS 130
Cdd:pfam18553   1 SPEARVFNAVPPaGGISLKELMKLgdSVAKVGFGKAMKNKWIKKDK---GDGKVVRKVDS 57
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 257-474 5.95e-10

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: 61.24  E-value: 5.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596   257 NFDALFQPQQHPARDQHDTFFlrdpaealqlpmdyvqrVKRTHsqggygsqgykynwkldearknLLRTHTTSASARALY 336
Cdd:TIGR00469  83 NFDNLGFPADHPGRQKSDCYY-----------------INEQH----------------------LLRAHTSAHELECFQ 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596   337 RLAQKKPFTPVKYFSIDRVFRNETLDATHLAEFHQIEGVV------ADHG---------------------------LTL 383
Cdd:TIGR00469 124 GGLDDSDNIKSGFLISADVYRRDEIDKTHYPVFHQADGAAirkrtkADLFekepgyiekfeedirgteadlnkenvkIIL 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596   384 GH------------------------------LMGVLREFFTK-------------LGITQLRFKPAYNPYTEPSMEVFS 420
Cdd:TIGR00469 204 DDdsiplkennpkqeyasdlavdlcehelkhsIEGITKDLFGKkissmiknkanntPKELKVRWIDAYFPFTAPSWEIEI 283

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 28175596   421 YHQGlkKWVEVGNSGVFRPEMLLPMGLPENVSV-IAWGLSLERPTMIKYGINNIR 474
Cdd:TIGR00469 284 WFKD--EWLELCGCGIIRHDILLRAGVHPSETIgWAFGLGLDRIAMLLFDIPDIR 336
PheRS_DBD2 pfam18554
PheRS DNA binding domain 2; This is a DNA-binding fold domain found in Phenylalanyl-tRNA ...
 133-165 8.35e-09

PheRS DNA binding domain 2; This is a DNA-binding fold domain found in Phenylalanyl-tRNA Synthetase N-terminal region. Mutational analysis indicate that DBD-1, 2 and 3 play critical roles in tRNA- Phe binding and recognition, i.e., from the drastic reduction of aminoacylation activity seen upon removal of the N-terminal domains. DBD-2 and DBD-3 constitute large insertions sequentially included between two neighboring antiparallel strands of the DBD-1 domain. Moreover, the DBD-3 pfam18553 is the domain insertion into DBD-2.


Pssm-ID: 465798 [Multi-domain]  Cd Length: 33  Bit Score: 50.87  E-value: 8.35e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 28175596   133 DEVQRRLQLVRGGQAEKLGEKERSELRKRKLLA 165
Cdd:pfam18554   1 DEVQEQLKLIQEGKGDSLSDKVKNELKKRKLLQ 33
class_II_aaRS-like_core cd00768
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
 346-463 1.11e-06

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: 49.42  E-value: 1.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596 346 PVKYFSIDRVFRNE--TLDATHLAEFHQIEGVVA----DHGLTLGHLMGVLREFFTKLGIT-QLRFKPAYN-----PYTE 413
Cdd:cd00768  75 PLRLAEIGPAFRNEggRRGLRRVREFTQLEGEVFgedgEEASEFEELIELTEELLRALGIKlDIVFVEKTPgefspGGAG 154

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 28175596 414 PSMEVFSYHqGLKKWVEVGNSGVFRPE--------MLLPMGLPENVSVIAWGLSLERP 463
Cdd:cd00768 155 PGFEIEVDH-PEGRGLEIGSGGYRQDEqaraadlyFLDEALEYRYPPTIGFGLGLERL 211
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
348-456 1.09e-04

tRNA synthetases class II (D, K and N);


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 44.09  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596   348 KYFSIDRVFRNETLDATHLAEFHQIEGVVADhgLTLGHLMGVLREFFTKL-----GITQLRFKPAYNPYTEPsMEVFSYH 422
Cdd:pfam00152  92 RVFQIARCFRDEDLRTDRQPEFTQLDLEMSF--VDYEDVMDLTEELIKEIfkeveGIAKELEGGTLLDLKKP-FPRITYA 168

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 28175596   423 QGLKKWVEVGNS----GVFRPEM--LLPMGLPENVSVIAW 456
Cdd:pfam00152 169 EAIEKLNGKDVEelgyGSDKPDLrfLLELVIDKNKFNPLW 208
HTH_11 pfam08279
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.
 7-53 1.06e-03

HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.


Pssm-ID: 429896 [Multi-domain]  Cd Length: 52  Bit Score: 37.03  E-value: 1.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 28175596     7 ELLLRRLEASDGGLDSAELAAELGMEHQAVVGAVKSLQALGEVIEAE 53
Cdd:pfam08279   1 LQILQLLLEARGPISGQELAEKLGVSRRTIRRDIKILEELGVPIEAE 47
MntR COG1321
Mn-dependent transcriptional regulator MntR, DtxR family [Transcription];
12-72 1.10e-03

Mn-dependent transcriptional regulator MntR, DtxR family [Transcription];


Pssm-ID: 440932 [Multi-domain]  Cd Length: 135  Bit Score: 39.42  E-value: 1.10e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28175596  12 RLEASDGGLDSAELAAELGMEHQAVVGAVKSLQALGEVieaELRSTKHWELTAEGEEIARE 72
Cdd:COG1321  17 ELSEEGGPVRTSDIAERLGVSPPSVTEMLKKLEEKGLV---EYEPYGGITLTEEGRELALR 74
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
9-90 2.82e-03

DNA-binding transcriptional regulator, MarR family [Transcription];


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 38.03  E-value: 2.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596   9 LLRRLeASDGGLDSAELAAELGMEHQAVVGAVKSLQALGEVieaelRSTKHWE--------LTAEGEEIARE-----GSH 75
Cdd:COG1846  43 VLAAL-AEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLV-----EREPDPEdrravlvrLTEKGRALLEEarpalEAL 116

                        90
                ....*....|....*
gi 28175596  76 EARVFRSIPPEGLAQ 90
Cdd:COG1846 117 LAELLAGLSEEELEA 131
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 8-49 5.73e-03

MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a non-specific resistance system. The expression of the mar operon is controlled by a repressor, MarR. A large number of compounds induce transcription of the mar operon. This is thought to be due to the compound binding to MarR, and the resulting complex stops MarR binding to the DNA. With the MarR repression lost, transcription of the operon proceeds. The structure of MarR is known and shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.


Pssm-ID: 432797 [Multi-domain]  Cd Length: 60  Bit Score: 35.26  E-value: 5.73e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 28175596     8 LLLRRLEASdGGLDSAELAAELGMEHQAVVGAVKSLQALGEV 49
Cdd:pfam12802   9 RVLLALARN-PGLTVAELARRLGISKQTVSRLVKRLEAKGLV 49
LysRS_core cd00775
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ...
 348-427 9.20e-03

Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a lysine to the 3' OH group of ribose of the appropriate tRNA. Its assignment to class II aaRS is based upon its structure and the presence of three characteristic sequence motifs in the core domain. It is found in eukaryotes as well as some prokaryotes and archaea. However, LysRS belongs to class I aaRS's in some prokaryotes and archaea. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.


Pssm-ID: 238398 [Multi-domain]  Cd Length: 329  Bit Score: 38.33  E-value: 9.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28175596 348 KYFSIDRVFRNETLDATHLAEFHQIEGVVA--DH----GLTLGHLMGVLREFFTKLGIT----QLRFKPaynPYtepsmE 417
Cdd:cd00775  78 RVYEIGRNFRNEGIDLTHNPEFTMIEFYEAyaDYndmmDLTEDLFSGLVKKINGKTKIEyggkELDFTP---PF-----K 149

                        90
                ....*....|
gi 28175596 418 VFSYHQGLKK 427
Cdd:cd00775 150 RVTMVDALKE 159
 
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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