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Conserved domains on  [gi|4758340|ref|NP_004452|]
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phenylalanine--tRNA ligase alpha subunit [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
 1-484 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 4758340     1 MADGQVAELLLRRLEASDGGLDSAELAAELGMEHQAVVGAVKSLQALGeVIEAELRSTKHWELTAEGEEIAREGSHEARV 80
Cdd:PTZ00326   2 MQKELEENTILSKLESENEIVNSLALAESLNIDHQKVVGAIKSLESAN-YITTEMKKSNTWTLTEEGEDYLKNGSPEYRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340    81 FRSIPPEGLAQSELMRLPSG---KVGFSKAMSNKWIRVDKSAADGPRVFRVVDSMEDEVQRRLQLV-RGGQAEKLGEKER 156
Cdd:PTZ00326  81 WQKLKEGGISKADDAKKLGGkvaDIGLGNAMKKKWIKLNKGDKKVFLSRKLVDSVVDTVRLLLKIVaKGSQAEKIDSKEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340   157 SELRKRKLLAEVTLKTYWVSKGSAFSTSISKQETELSPEMISSGSWRDRPFKPYNFLAHGVLPDSGHLHPLLKVRSQFRQ 236
Cdd:PTZ00326 161 KELKKRKLATLEKIKYFVVTKGPKFAKEIKKQITDLTQEMLLNGSWKNAEFKEYNFNALGKKIGGGNLHPLLKVRREFRE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340   237 IFLEMGFTEMPTDNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPA--EALQLPMDYVQRVKRTHSQGGYGSQGYKYNW 314
Cdd:PTZ00326 241 ILLEMGFEEMPTNRYVESSFWNFDALFQPQQHPARDAQDTFFLSKPEtsKVNDLDDDYVERVKKVHEVGGYGSIGWRYDW 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340   315 KLDEARKNLLRTHTTSASARALYRLAQ----KKPFTPVKYFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTLGHLMGV 390
Cdd:PTZ00326 321 KLEEARKNILRTHTTAVSARMLYKLAQeykkTGPFKPKKYFSIDRVFRNETLDATHLAEFHQVEGFVIDRNLTLGDLIGT 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340   391 LREFFTKLGITQLRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLERPTMIKYG 470
Cdd:PTZ00326 401 IREFFRRIGITKLRFKPAFNPYTEPSMEIFGYHPGLKKWVEVGNSGIFRPEMLRPMGFPEDVTVIAWGLSLERPTMIKYG 480

                        490
                 ....*....|....
gi 4758340   471 INNIRELVGHKVNL 484
Cdd:PTZ00326 481 IKNIRDLFGHKVDL 494
 
Name Accession Description Interval E-value
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 1-484 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 4758340     1 MADGQVAELLLRRLEASDGGLDSAELAAELGMEHQAVVGAVKSLQALGeVIEAELRSTKHWELTAEGEEIAREGSHEARV 80
Cdd:PTZ00326   2 MQKELEENTILSKLESENEIVNSLALAESLNIDHQKVVGAIKSLESAN-YITTEMKKSNTWTLTEEGEDYLKNGSPEYRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340    81 FRSIPPEGLAQSELMRLPSG---KVGFSKAMSNKWIRVDKSAADGPRVFRVVDSMEDEVQRRLQLV-RGGQAEKLGEKER 156
Cdd:PTZ00326  81 WQKLKEGGISKADDAKKLGGkvaDIGLGNAMKKKWIKLNKGDKKVFLSRKLVDSVVDTVRLLLKIVaKGSQAEKIDSKEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340   157 SELRKRKLLAEVTLKTYWVSKGSAFSTSISKQETELSPEMISSGSWRDRPFKPYNFLAHGVLPDSGHLHPLLKVRSQFRQ 236
Cdd:PTZ00326 161 KELKKRKLATLEKIKYFVVTKGPKFAKEIKKQITDLTQEMLLNGSWKNAEFKEYNFNALGKKIGGGNLHPLLKVRREFRE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340   237 IFLEMGFTEMPTDNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPA--EALQLPMDYVQRVKRTHSQGGYGSQGYKYNW 314
Cdd:PTZ00326 241 ILLEMGFEEMPTNRYVESSFWNFDALFQPQQHPARDAQDTFFLSKPEtsKVNDLDDDYVERVKKVHEVGGYGSIGWRYDW 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340   315 KLDEARKNLLRTHTTSASARALYRLAQ----KKPFTPVKYFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTLGHLMGV 390
Cdd:PTZ00326 321 KLEEARKNILRTHTTAVSARMLYKLAQeykkTGPFKPKKYFSIDRVFRNETLDATHLAEFHQVEGFVIDRNLTLGDLIGT 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340   391 LREFFTKLGITQLRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLERPTMIKYG 470
Cdd:PTZ00326 401 IREFFRRIGITKLRFKPAFNPYTEPSMEIFGYHPGLKKWVEVGNSGIFRPEMLRPMGFPEDVTVIAWGLSLERPTMIKYG 480

                        490
                 ....*....|....
gi 4758340   471 INNIRELVGHKVNL 484
Cdd:PTZ00326 481 IKNIRDLFGHKVDL 494
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 209-483 7.71e-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: 7.71e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340    209 PYNFLAHGVLPDSGHLHPLLKVRSQFRQIFLEMGFTEMPtDNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPAEAlql 288
Cdd:pfam01409   1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVE-GPEVESDFYNFDALNIPQDHPARDMQDTFYLKKPLKP--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340    289 pmdyvqrvkrthsqggygsqgykynwkldEARKNLLRTHTTSASARALYrlaqKKPFTPVKYFSIDRVFRNETLDATHLA 368
Cdd:pfam01409  77 -----------------------------VARRLLLRTHTTPVQARTLA----KKPKPPIKIFSIGRVFRRDQVDATHLP 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340    369 EFHQIEGVVADHGLTLGHLMGVLREFFTKL-GIT-QLRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGVFRPEMLLPM 446
Cdd:pfam01409 124 EFHQVEGLVVDENVTFADLKGVLEEFLRKFfGFEvKVRFRPSYFPFTEPSAEVDVYVCKLGGWLEVGGAGMVHPNVLEAV 203

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 4758340    447 GLPENVSVIAWGLSLERPTMIKYGINNIRELVGHKVN 483
Cdd:pfam01409 204 GIDEDYSGFAFGLGVERLAMLKYGIDDIRDLYENDLR 240
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 225-483 1.64e-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: 1.64e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340  225 HPLLKVRSQFRQIFLEMGFTEMPTdNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPAealqlpmdyvqrvkrthsqgg 304
Cdd:cd00496   1 HPLNKVIEEIEDIFVSMGFTEVEG-PEVETDFYNFDALNIPQDHPARDMQDTFYINDPA--------------------- 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340  305 ygsqgykynwkldearKNLLRTHTTSASARALYRLaqkkpFTPVKYFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTL 384
Cdd:cd00496  59 ----------------RLLLRTHTSAVQARALAKL-----KPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKGLTF 117

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340  385 GHLMGVLREFFTKLG--ITQLRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLE 462
Cdd:cd00496 118 ADLKGTLEEFAKELFgpITKVRFRPSYFPFTEPSFEVDVYCPGCLGWLEILGCGMVRPEVLENAGIDEEYSGFAFGIGLE 197

                       250       260
                ....*....|....*....|.
gi 4758340  463 RPTMIKYGINNIRELVGHKVN 483
Cdd:cd00496 198 RLAMLKYGIPDIRLFYSNDLR 218
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 190-482 2.74e-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: 2.74e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340    190 TELSPEMISSGSWRDRPFKPYNFLAHGVLPDSGHLHPLLKVRSQFRQIFLEMGFTEMPtDNFIESSFWNFDALFQPQQHP 269
Cdd:TIGR00468  37 TKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDEIRDIFLGLGFTEET-GPEVETDFWNFDALNIPQDHP 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340    270 ARDQHDTFFLRDpaealqlpmdyvqrvkrthsqggygsqgykynwkldearKNLLRTHTTSASARALyrlaQKKPFTPVK 349
Cdd:TIGR00468 116 ARDMQDTFYIKD---------------------------------------RLLLRTHTTAVQLRTM----EEQEKPPIR 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340    350 YFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTLGHLMGVLREFFTKL-GITQLRFKPAYNPYTEPSMEVFSYHQGLKK 428
Cdd:TIGR00468 153 IFSPGRVFRNDTVDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLKKMfGETEIRFRPSYFPFTEPSAEIDVYCPEGKG 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 4758340    429 WVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLERPTMIKYGINNIRELVGHKV 482
Cdd:TIGR00468 233 WLEVLGAGMFRPEVLEPMGIDPTYPGFAWGIGIERLAMLKYGITDIRDLYENDL 286
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 216-478 4.38e-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: 192.96  E-value: 4.38e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340  216 GVLPDSGHLHPLLKVRSQFRQIFLEMGFT-----EmptdnfIESSFWNFDALFQPQQHPARDQHDTFFLRDpaealqlpm 290
Cdd:COG0016  98 GRPRPLGSLHPLTQVIEEIEDIFVGMGFEvaegpE------IETDWYNFEALNIPPDHPARDMQDTFYIDD--------- 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340  291 dyvqrvkrthsqggygsqgykynwkldearKNLLRTHTTSASARALyrLAQKkpfTPVKYFSIDRVFRNETLDATHLAEF 370
Cdd:COG0016 163 ------------------------------GLLLRTHTSPVQIRTM--EKQK---PPIRIIAPGRVYRRDESDATHSPMF 207

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340  371 HQIEGVVADHGLTLGHLMGVLREFFTKL-GI-TQLRFKPAYNPYTEPSMEV-FSYHQGLKK---------WVEVGNSGVF 438
Cdd:COG0016 208 HQVEGLVVDKGISFADLKGTLEEFAKAFfGEdVKVRFRPSYFPFTEPSAEVdISCFICGGKgcrvckgtgWLEILGCGMV 287

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 4758340  439 RPEMLLPMGL-PENVSVIAWGLSLERPTMIKYGINNIRELV 478
Cdd:COG0016 288 HPNVLRAVGIdPEEYSGFAFGMGIERLAMLKYGIDDIRLFF 328
 
Name Accession Description Interval E-value
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 1-484 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 4758340     1 MADGQVAELLLRRLEASDGGLDSAELAAELGMEHQAVVGAVKSLQALGeVIEAELRSTKHWELTAEGEEIAREGSHEARV 80
Cdd:PTZ00326   2 MQKELEENTILSKLESENEIVNSLALAESLNIDHQKVVGAIKSLESAN-YITTEMKKSNTWTLTEEGEDYLKNGSPEYRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340    81 FRSIPPEGLAQSELMRLPSG---KVGFSKAMSNKWIRVDKSAADGPRVFRVVDSMEDEVQRRLQLV-RGGQAEKLGEKER 156
Cdd:PTZ00326  81 WQKLKEGGISKADDAKKLGGkvaDIGLGNAMKKKWIKLNKGDKKVFLSRKLVDSVVDTVRLLLKIVaKGSQAEKIDSKEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340   157 SELRKRKLLAEVTLKTYWVSKGSAFSTSISKQETELSPEMISSGSWRDRPFKPYNFLAHGVLPDSGHLHPLLKVRSQFRQ 236
Cdd:PTZ00326 161 KELKKRKLATLEKIKYFVVTKGPKFAKEIKKQITDLTQEMLLNGSWKNAEFKEYNFNALGKKIGGGNLHPLLKVRREFRE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340   237 IFLEMGFTEMPTDNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPA--EALQLPMDYVQRVKRTHSQGGYGSQGYKYNW 314
Cdd:PTZ00326 241 ILLEMGFEEMPTNRYVESSFWNFDALFQPQQHPARDAQDTFFLSKPEtsKVNDLDDDYVERVKKVHEVGGYGSIGWRYDW 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340   315 KLDEARKNLLRTHTTSASARALYRLAQ----KKPFTPVKYFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTLGHLMGV 390
Cdd:PTZ00326 321 KLEEARKNILRTHTTAVSARMLYKLAQeykkTGPFKPKKYFSIDRVFRNETLDATHLAEFHQVEGFVIDRNLTLGDLIGT 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340   391 LREFFTKLGITQLRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLERPTMIKYG 470
Cdd:PTZ00326 401 IREFFRRIGITKLRFKPAFNPYTEPSMEIFGYHPGLKKWVEVGNSGIFRPEMLRPMGFPEDVTVIAWGLSLERPTMIKYG 480

                        490
                 ....*....|....
gi 4758340   471 INNIRELVGHKVNL 484
Cdd:PTZ00326 481 IKNIRDLFGHKVDL 494
PLN02853 PLN02853
Probable phenylalanyl-tRNA synthetase alpha chain
 8-496 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 4758340     8 ELLLRRLEASDGGLDSAELAAELGMEHQAVVGAVKSLQALGeVIEAELRSTKHWELTAEGEEIAREGSHEARVFRSIPPE 87
Cdd:PLN02853   6 EALLGALSNNEEISDSGQFAASHGLDHNEVVGVIKSLHGFR-YVDAQDIKRETWVLTEEGKKYAAEGSPEVQLFAAVPAE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340    88 G-LAQSELMRL--PS-GKVGFSKAMSNKWIRVDKsaadGPRVFRVVDSMEDEVQRRLQLVRGGQAekLGEKERSEL-RKR 162
Cdd:PLN02853  85 GsISKDELQKKldPAvFDIGFKQAMKNKWLEMGG----KPQVSRKVQHVEDEVKELLLAIQEGKE--VDDKDIDALkKRR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340   163 KLLAEVTLKTYWVSKGSAFSTSISKQETELSPEMISSGSWRDRPFKPYNFLAHGVLPDSGHLHPLLKVRSQFRQIFLEMG 242
Cdd:PLN02853 159 KLITLETWKGYSIKKGPNYAPERKKAATDLTREMLQSGDWKDLEFKEYNFNALGAPPEGGHLHPLLKVRQQFRKIFLQMG 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340   243 FTEMPTDNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPAEALQLPMDYVQRVKRTHSQGGYGSQGYKYNWKLDEARKN 322
Cdd:PLN02853 239 FEEMPTNNFVESSFWNFDALFQPQQHPARDSHDTFFLKAPATTRQLPEDYVERVKTVHESGGYGSIGYGYDWKREEANKN 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340   323 LLRTHTTSASARALYRLAQKkPFTPVKYFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTLGHLMGVLREFFTKLGITQ 402
Cdd:PLN02853 319 LLRTHTTAVSSRMLYKLAQK-GFKPKRYFSIDRVFRNEAVDRTHLAEFHQVEGLVCDRGLTLGDLIGVLEDFFSRLGMTK 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340   403 LRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLERPTMIKYGINNIRELVGHKV 482
Cdd:PLN02853 398 LRFKPAYNPYTEPSMEIFSYHEGLKKWVEVGNSGMFRPEMLLPMGLPEDVNVIAWGLSLERPTMILYGIDNIRDLFGHKV 477

                        490
                 ....*....|....
gi 4758340   483 NLQMVYDSPLCRLD 496
Cdd:PLN02853 478 DLGLIKRNPICRLG 491
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
10-477 6.80e-156

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 452.75  E-value: 6.80e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340    10 LLRRLEASDGgLDSAELAAELGMEHQAVVGAVKSLQALGeVIEAELRSTKHWELTAEGEEIAREGSHEARVFRSIPPEG- 88
Cdd:PRK04172  11 VLKALKELKE-ATLEELAEKLGLPPEAVMRAAEWLEEKG-LVKVEERVEEVYVLTEEGKKYAEEGLPERRLLNALKDGGe 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340    89 LAQSELMRLPSGKVGFSKAMSN----KWIRVDKSaadgpRVFRVVDSMEDEVQRRLQLVRGGQAEKLGEKER---SELRK 161
Cdd:PRK04172  89 VSLDELKEALLDKKEVGIALGNlarkGWAKIEKG-----KVILKPDAYEDPEEKALKALAEGDKEELSEEDLkvlKELKK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340   162 RKLLAEVTLKTYWVS---KG-SAFSTSISKQE--TELSPEMISSGSWRDRPFKPYNFLAHGVLPDSGHLHPLLKVRSQFR 235
Cdd:PRK04172 164 RKLVEEKERTERSVEltdAGlELLKEGIELKEeiTQLTPELLKSGEWKEKEFRPYNVKAPPPKIYPGKKHPYREFIDEVR 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340   236 QIFLEMGFTEMpTDNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPAEAlQLPMDYVQRVKRTHSQGG-YGSQGYKYNW 314
Cdd:PRK04172 244 DILVEMGFEEM-KGPLVETEFWNFDALFQPQDHPAREMQDTFYLKYPGIG-DLPEELVERVKEVHEHGGdTGSRGWGYKW 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340   315 KLDEARKNLLRTHTTSASARALYRLAQKkpftPVKYFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTLGHLMGVLREF 394
Cdd:PRK04172 322 DEDIAKRLVLRTHTTALSARYLASRPEP----PQKYFSIGRVFRPDTIDATHLPEFYQLEGIVMGEDVSFRDLLGILKEF 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340   395 FTKLGITQLRFKPAYNPYTEPSMEVFSYHQGLkKWVEVGNSGVFRPEMLLPMGLpeNVSVIAWGLSLERPTMIKYGINNI 474
Cdd:PRK04172 398 YKRLGFEEVKFRPAYFPFTEPSVEVEVYHEGL-GWVELGGAGIFRPEVLEPLGI--DVPVLAWGLGIERLAMLRLGLDDI 474


                 ...
gi 4758340   475 REL 477
Cdd:PRK04172 475 RDL 477
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 209-483 7.71e-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: 7.71e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340    209 PYNFLAHGVLPDSGHLHPLLKVRSQFRQIFLEMGFTEMPtDNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPAEAlql 288
Cdd:pfam01409   1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVE-GPEVESDFYNFDALNIPQDHPARDMQDTFYLKKPLKP--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340    289 pmdyvqrvkrthsqggygsqgykynwkldEARKNLLRTHTTSASARALYrlaqKKPFTPVKYFSIDRVFRNETLDATHLA 368
Cdd:pfam01409  77 -----------------------------VARRLLLRTHTTPVQARTLA----KKPKPPIKIFSIGRVFRRDQVDATHLP 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340    369 EFHQIEGVVADHGLTLGHLMGVLREFFTKL-GIT-QLRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGVFRPEMLLPM 446
Cdd:pfam01409 124 EFHQVEGLVVDENVTFADLKGVLEEFLRKFfGFEvKVRFRPSYFPFTEPSAEVDVYVCKLGGWLEVGGAGMVHPNVLEAV 203

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 4758340    447 GLPENVSVIAWGLSLERPTMIKYGINNIRELVGHKVN 483
Cdd:pfam01409 204 GIDEDYSGFAFGLGVERLAMLKYGIDDIRDLYENDLR 240
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 225-483 1.64e-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: 1.64e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340  225 HPLLKVRSQFRQIFLEMGFTEMPTdNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPAealqlpmdyvqrvkrthsqgg 304
Cdd:cd00496   1 HPLNKVIEEIEDIFVSMGFTEVEG-PEVETDFYNFDALNIPQDHPARDMQDTFYINDPA--------------------- 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340  305 ygsqgykynwkldearKNLLRTHTTSASARALYRLaqkkpFTPVKYFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTL 384
Cdd:cd00496  59 ----------------RLLLRTHTSAVQARALAKL-----KPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKGLTF 117

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340  385 GHLMGVLREFFTKLG--ITQLRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLE 462
Cdd:cd00496 118 ADLKGTLEEFAKELFgpITKVRFRPSYFPFTEPSFEVDVYCPGCLGWLEILGCGMVRPEVLENAGIDEEYSGFAFGIGLE 197

                       250       260
                ....*....|....*....|.
gi 4758340  463 RPTMIKYGINNIRELVGHKVN 483
Cdd:cd00496 198 RLAMLKYGIPDIRLFYSNDLR 218
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 190-482 2.74e-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: 2.74e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340    190 TELSPEMISSGSWRDRPFKPYNFLAHGVLPDSGHLHPLLKVRSQFRQIFLEMGFTEMPtDNFIESSFWNFDALFQPQQHP 269
Cdd:TIGR00468  37 TKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDEIRDIFLGLGFTEET-GPEVETDFWNFDALNIPQDHP 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340    270 ARDQHDTFFLRDpaealqlpmdyvqrvkrthsqggygsqgykynwkldearKNLLRTHTTSASARALyrlaQKKPFTPVK 349
Cdd:TIGR00468 116 ARDMQDTFYIKD---------------------------------------RLLLRTHTTAVQLRTM----EEQEKPPIR 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340    350 YFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTLGHLMGVLREFFTKL-GITQLRFKPAYNPYTEPSMEVFSYHQGLKK 428
Cdd:TIGR00468 153 IFSPGRVFRNDTVDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLKKMfGETEIRFRPSYFPFTEPSAEIDVYCPEGKG 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 4758340    429 WVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLERPTMIKYGINNIRELVGHKV 482
Cdd:TIGR00468 233 WLEVLGAGMFRPEVLEPMGIDPTYPGFAWGIGIERLAMLKYGITDIRDLYENDL 286
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 216-478 4.38e-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: 192.96  E-value: 4.38e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340  216 GVLPDSGHLHPLLKVRSQFRQIFLEMGFT-----EmptdnfIESSFWNFDALFQPQQHPARDQHDTFFLRDpaealqlpm 290
Cdd:COG0016  98 GRPRPLGSLHPLTQVIEEIEDIFVGMGFEvaegpE------IETDWYNFEALNIPPDHPARDMQDTFYIDD--------- 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340  291 dyvqrvkrthsqggygsqgykynwkldearKNLLRTHTTSASARALyrLAQKkpfTPVKYFSIDRVFRNETLDATHLAEF 370
Cdd:COG0016 163 ------------------------------GLLLRTHTSPVQIRTM--EKQK---PPIRIIAPGRVYRRDESDATHSPMF 207

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340  371 HQIEGVVADHGLTLGHLMGVLREFFTKL-GI-TQLRFKPAYNPYTEPSMEV-FSYHQGLKK---------WVEVGNSGVF 438
Cdd:COG0016 208 HQVEGLVVDKGISFADLKGTLEEFAKAFfGEdVKVRFRPSYFPFTEPSAEVdISCFICGGKgcrvckgtgWLEILGCGMV 287

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 4758340  439 RPEMLLPMGL-PENVSVIAWGLSLERPTMIKYGINNIRELV 478
Cdd:COG0016 288 HPNVLRAVGIdPEEYSGFAFGMGIERLAMLKYGIDDIRLFF 328
PheRS_DBD1 pfam18552
PheRS DNA binding domain 1; This is a DNA-binding fold domain found in Phenylalanyl-tRNA ...
 2-61 1.62e-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: 1.62e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340      2 ADGQVAELLLRRLEAsDGGLDSAELAAELGMEHQAVVGAVKSLQALGEVIEAELRSTKHW 61
Cdd:pfam18552   1 MDKDLEEQILQYLEK-HGGVDSLDLAAELGVDHQKVVGAVKSLQALGDVITAEQRSSKHW 59
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 225-475 2.26e-19

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 90.21  E-value: 2.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340   225 HPLLKVRSQFRQIFLEM---GFTEMPTDNFIESSFWNFDALFQPQQHPARDQHDTFflrdpaealqlpmdYVQRvkrths 301
Cdd:PLN02788  68 HPLGILKNAIYDYFDENysnKFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTY--------------YVDA------ 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340   302 qggygsqgykynwkldearKNLLRTHTTSASARALYRLAQKkpftpvkYFSIDRVFRNETLDATHLAEFHQIEGV----- 376
Cdd:PLN02788 128 -------------------QTVLRCHTSAHQAELLRAGHTH-------FLVTGDVYRRDSIDATHYPVFHQMEGVrvfsp 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340   377 --VADHGLTLGH---------LMGVLREFFtklGITQLRFKPAYNPYTEPSMEVFSYHQGlkKWVEVGNSGVFRPEMLLP 445
Cdd:PLN02788 182 eeWEASGLDGTDlaaedlkktLEGLARHLF---GDVEMRWVDAYFPFTNPSFELEIFFKG--EWLEVLGCGVTEQEILKN 256

                        250       260       270
                 ....*....|....*....|....*....|..
gi 4758340   446 MGLPENVsviAW--GLSLERPTMIKYGINNIR 475
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 ...
 75-131 1.07e-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: 1.07e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340     75 SHEARVFRSIPP-EGLAQSELMRL--PSGKVGFSKAMSNKWIRVDKsaaDGPRVFRVVDS 131
Cdd:pfam18553   1 SPEARVFNAVPPaGGISLKELMKLgdSVAKVGFGKAMKNKWIKKDK---GDGKVVRKVDS 57
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 258-475 5.33e-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: 61.63  E-value: 5.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340    258 NFDALFQPQQHPARDQHDTFFlrdpaealqlpmdyvqrVKRTHsqggygsqgykynwkldearknLLRTHTTSASARALY 337
Cdd:TIGR00469  83 NFDNLGFPADHPGRQKSDCYY-----------------INEQH----------------------LLRAHTSAHELECFQ 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340    338 RLAQKKPFTPVKYFSIDRVFRNETLDATHLAEFHQIEGVV------ADHG---------------------------LTL 384
Cdd:TIGR00469 124 GGLDDSDNIKSGFLISADVYRRDEIDKTHYPVFHQADGAAirkrtkADLFekepgyiekfeedirgteadlnkenvkIIL 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340    385 GH------------------------------LMGVLREFFTK-------------LGITQLRFKPAYNPYTEPSMEVFS 421
Cdd:TIGR00469 204 DDdsiplkennpkqeyasdlavdlcehelkhsIEGITKDLFGKkissmiknkanntPKELKVRWIDAYFPFTAPSWEIEI 283

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 4758340    422 YHQGlkKWVEVGNSGVFRPEMLLPMGLPENVSV-IAWGLSLERPTMIKYGINNIR 475
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 ...
 134-166 7.81e-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: 7.81e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 4758340    134 DEVQRRLQLVRGGQAEKLGEKERSELRKRKLLA 166
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 ...
 347-464 1.12e-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: 1.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340  347 PVKYFSIDRVFRNE--TLDATHLAEFHQIEGVVA----DHGLTLGHLMGVLREFFTKLGIT-QLRFKPAYN-----PYTE 414
Cdd:cd00768  75 PLRLAEIGPAFRNEggRRGLRRVREFTQLEGEVFgedgEEASEFEELIELTEELLRALGIKlDIVFVEKTPgefspGGAG 154

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4758340  415 PSMEVFSYHqGLKKWVEVGNSGVFRPE--------MLLPMGLPENVSVIAWGLSLERP 464
Cdd:cd00768 155 PGFEIEVDH-PEGRGLEIGSGGYRQDEqaraadlyFLDEALEYRYPPTIGFGLGLERL 211
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
349-434 1.15e-04

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


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 44.09  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340    349 KYFSIDRVFRNETLDATHLAEFHQIEGVVADhgLTLGHLMGVLREFFTKL-----GITQLRFKPAYNPYTEPsMEVFSYH 423
Cdd:pfam00152  92 RVFQIARCFRDEDLRTDRQPEFTQLDLEMSF--VDYEDVMDLTEELIKEIfkeveGIAKELEGGTLLDLKKP-FPRITYA 168

                          90
                  ....*....|.
gi 4758340    424 QGLKKWVEVGN 434
Cdd:pfam00152 169 EAIEKLNGKDV 179
HTH_11 pfam08279
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.
 8-54 1.05e-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: 1.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 4758340      8 ELLLRRLEASDGGLDSAELAAELGMEHQAVVGAVKSLQALGEVIEAE 54
Cdd:pfam08279   1 LQILQLLLEARGPISGQELAEKLGVSRRTIRRDIKILEELGVPIEAE 47
MntR COG1321
Mn-dependent transcriptional regulator MntR, DtxR family [Transcription];
13-73 1.11e-03

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


Pssm-ID: 440932 [Multi-domain]  Cd Length: 135  Bit Score: 39.42  E-value: 1.11e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4758340   13 RLEASDGGLDSAELAAELGMEHQAVVGAVKSLQALGEVieaELRSTKHWELTAEGEEIARE 73
Cdd:COG1321  17 ELSEEGGPVRTSDIAERLGVSPPSVTEMLKKLEEKGLV---EYEPYGGITLTEEGRELALR 74
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
10-91 2.91e-03

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 38.03  E-value: 2.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340   10 LLRRLeASDGGLDSAELAAELGMEHQAVVGAVKSLQALGEVI----EAELRSTKHwELTAEGEEIARE-----GSHEARV 80
Cdd:COG1846  43 VLAAL-AEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVErepdPEDRRAVLV-RLTEKGRALLEEarpalEALLAEL 120

                        90
                ....*....|.
gi 4758340   81 FRSIPPEGLAQ 91
Cdd:COG1846 121 LAGLSEEELEA 131
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 9-50 5.57e-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: 5.57e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 4758340      9 LLLRRLEASdGGLDSAELAAELGMEHQAVVGAVKSLQALGEV 50
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 ...
 349-428 9.55e-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: 9.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758340  349 KYFSIDRVFRNETLDATHLAEFHQIEGVVA--DH----GLTLGHLMGVLREFFTKLGIT----QLRFKPaynPYtepsmE 418
Cdd:cd00775  78 RVYEIGRNFRNEGIDLTHNPEFTMIEFYEAyaDYndmmDLTEDLFSGLVKKINGKTKIEyggkELDFTP---PF-----K 149

                        90
                ....*....|
gi 4758340  419 VFSYHQGLKK 428
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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