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Conserved domains on  [gi|124505829|ref|XP_001351028|]
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phenylalanine--tRNA ligase alpha subunit [Plasmodium falciparum 3D7]

Protein Classification

phenylalanine--tRNA ligase alpha subunit( domain architecture ID 11488385)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 72-575 0e+00

phenylalanyl-tRNA synthetase alpha chain; Provisional


:

Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 822.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829  72 NEYTTSLKISKKYNIDHNKVMGMIKKLETLYYIINLIKSFNTYHLSDEGKQYLKEGSPEFIVIKYVIQNNKCTLEDLKKN 151
Cdd:PTZ00326  19 NEIVNSLALAESLNIDHQKVVGAIKSLESANYITTEMKKSNTWTLTEEGEDYLKNGSPEYRLWQKLKEGGISKADDAKKL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 152 LGKIGDIGLNTNLKNRTIQLNKADKCLT-CNCNLHDIQDFTQIYLDIINQYghdeellfahlknknhtknalnnnemkns 230
Cdd:PTZ00326  99 GGKVADIGLGNAMKKKWIKLNKGDKKVFlSRKLVDSVVDTVRLLLKIVAKG----------------------------- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 231 CKDNNIINNLIQDLKKRKLLEIKKNSYSHVIKTSIFKKDIKKQITDINYLLLKNEEYKKYDIKKYNFFSSGKKINKGNIH 310
Cdd:PTZ00326 150 SQAEKIDSKELKELKKRKLATLEKIKYFVVTKGPKFAKEIKKQITDLTQEMLLNGSWKNAEFKEYNFNALGKKIGGGNLH 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 311 LLTKQMRTFKEIFFSLGFEEMETHNYVESSFWCFDALYIPQQHPSRDLQDTFFIKEPETCIDKFVDTEYIDNIKRVHTHG 390
Cdd:PTZ00326 230 PLLKVRREFREILLEMGFEEMPTNRYVESSFWNFDALFQPQQHPARDAQDTFFLSKPETSKVNDLDDDYVERVKKVHEVG 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 391 DYGSFGWNYKWKLEESKKNVLRTHTTANSCRALFKLAKEYKEAGCIKPKKYFSIDRVFRNENLDSTHLAEFHQVEGLIID 470
Cdd:PTZ00326 310 GYGSIGWRYDWKLEEARKNILRTHTTAVSARMLYKLAQEYKKTGPFKPKKYFSIDRVFRNETLDATHLAEFHQVEGFVID 389

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 471 KNIGLSHLIGTLAAFYKHIGIHKLKFKPTFNPYTEPSMEIYGYHEQSKKWLEVGNSGIFRPEMLRSMGFSEEVSVIAWGL 550
Cdd:PTZ00326 390 RNLTLGDLIGTIREFFRRIGITKLRFKPAFNPYTEPSMEIFGYHPGLKKWVEVGNSGIFRPEMLRPMGFPEDVTVIAWGL 469

                        490       500
                 ....*....|....*....|....*
gi 124505829 551 SLERPTMIKYNIKNIRDLFGYKSVV 575
Cdd:PTZ00326 470 SLERPTMIKYGIKNIRDLFGHKVDL 494
 
Name Accession Description Interval E-value
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 72-575 0e+00

phenylalanyl-tRNA synthetase alpha chain; Provisional


Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 822.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829  72 NEYTTSLKISKKYNIDHNKVMGMIKKLETLYYIINLIKSFNTYHLSDEGKQYLKEGSPEFIVIKYVIQNNKCTLEDLKKN 151
Cdd:PTZ00326  19 NEIVNSLALAESLNIDHQKVVGAIKSLESANYITTEMKKSNTWTLTEEGEDYLKNGSPEYRLWQKLKEGGISKADDAKKL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 152 LGKIGDIGLNTNLKNRTIQLNKADKCLT-CNCNLHDIQDFTQIYLDIINQYghdeellfahlknknhtknalnnnemkns 230
Cdd:PTZ00326  99 GGKVADIGLGNAMKKKWIKLNKGDKKVFlSRKLVDSVVDTVRLLLKIVAKG----------------------------- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 231 CKDNNIINNLIQDLKKRKLLEIKKNSYSHVIKTSIFKKDIKKQITDINYLLLKNEEYKKYDIKKYNFFSSGKKINKGNIH 310
Cdd:PTZ00326 150 SQAEKIDSKELKELKKRKLATLEKIKYFVVTKGPKFAKEIKKQITDLTQEMLLNGSWKNAEFKEYNFNALGKKIGGGNLH 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 311 LLTKQMRTFKEIFFSLGFEEMETHNYVESSFWCFDALYIPQQHPSRDLQDTFFIKEPETCIDKFVDTEYIDNIKRVHTHG 390
Cdd:PTZ00326 230 PLLKVRREFREILLEMGFEEMPTNRYVESSFWNFDALFQPQQHPARDAQDTFFLSKPETSKVNDLDDDYVERVKKVHEVG 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 391 DYGSFGWNYKWKLEESKKNVLRTHTTANSCRALFKLAKEYKEAGCIKPKKYFSIDRVFRNENLDSTHLAEFHQVEGLIID 470
Cdd:PTZ00326 310 GYGSIGWRYDWKLEEARKNILRTHTTAVSARMLYKLAQEYKKTGPFKPKKYFSIDRVFRNETLDATHLAEFHQVEGFVID 389

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 471 KNIGLSHLIGTLAAFYKHIGIHKLKFKPTFNPYTEPSMEIYGYHEQSKKWLEVGNSGIFRPEMLRSMGFSEEVSVIAWGL 550
Cdd:PTZ00326 390 RNLTLGDLIGTIREFFRRIGITKLRFKPAFNPYTEPSMEIFGYHPGLKKWVEVGNSGIFRPEMLRPMGFPEDVTVIAWGL 469

                        490       500
                 ....*....|....*....|....*
gi 124505829 551 SLERPTMIKYNIKNIRDLFGYKSVV 575
Cdd:PTZ00326 470 SLERPTMIKYGIKNIRDLFGHKVDL 494
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 310-572 4.76e-107

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: 320.26  E-value: 4.76e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 310 HLLTKQMRTFKEIFFSLGFEEMETHnYVESSFWCFDALYIPQQHPSRDLQDTFFIKEPEtcidkfvdteyidnikrvhth 389
Cdd:cd00496    1 HPLNKVIEEIEDIFVSMGFTEVEGP-EVETDFYNFDALNIPQDHPARDMQDTFYINDPA--------------------- 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 390 gdygsfgwnykwkleeskKNVLRTHTTANSCRALFKLakeykeagcIKPKKYFSIDRVFRNENLDSTHLAEFHQVEGLII 469
Cdd:cd00496   59 ------------------RLLLRTHTSAVQARALAKL---------KPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVV 111

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 470 DKNIGLSHLIGTLAAFYKHIG--IHKLKFKPTFNPYTEPSMEIYGYHEQSKKWLEVGNSGIFRPEMLRSMGFSEEVSVIA 547
Cdd:cd00496  112 DKGLTFADLKGTLEEFAKELFgpITKVRFRPSYFPFTEPSFEVDVYCPGCLGWLEILGCGMVRPEVLENAGIDEEYSGFA 191

                        250       260
                 ....*....|....*....|....*
gi 124505829 548 WGLSLERPTMIKYNIKNIRDLFGYK 572
Cdd:cd00496  192 FGIGLERLAMLKYGIPDIRLFYSND 216
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 294-570 1.14e-104

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: 315.29  E-value: 1.14e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829  294 KYNFFSSGKKINKGNIHLLTKQMRTFKEIFFSLGFEEMETHnYVESSFWCFDALYIPQQHPSRDLQDTFFIKEPETcidk 373
Cdd:pfam01409   1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVEGP-EVESDFYNFDALNIPQDHPARDMQDTFYLKKPLK---- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829  374 fvdteyidnikrvhthgdygsfgwnykwklEESKKNVLRTHTTANSCRALfklAKEYKeagciKPKKYFSIDRVFRNENL 453
Cdd:pfam01409  76 ------------------------------PVARRLLLRTHTTPVQARTL---AKKPK-----PPIKIFSIGRVFRRDQV 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829  454 DSTHLAEFHQVEGLIIDKNIGLSHLIGTLAAFYKHI-GIH-KLKFKPTFNPYTEPSMEIYGYHEQSKKWLEVGNSGIFRP 531
Cdd:pfam01409 118 DATHLPEFHQVEGLVVDENVTFADLKGVLEEFLRKFfGFEvKVRFRPSYFPFTEPSAEVDVYVCKLGGWLEVGGAGMVHP 197

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 124505829  532 EMLRSMGFSEEVSVIAWGLSLERPTMIKYNIKNIRDLFG 570
Cdd:pfam01409 198 NVLEAVGIDEDYSGFAFGLGVERLAMLKYGIDDIRDLYE 236
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 240-572 1.04e-97

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: 299.23  E-value: 1.04e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829  240 LIQDLKKRKLLEIKKNSYSHVIKTSIFKKDIKKQITDINYLLLKNEEYKKYDIKKYNFFSSGKKINKGNIHLLTKQMRTF 319
Cdd:TIGR00468   2 LKDLLKQLGKLTKEETKPALGALINEVKIELQDELTKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDEI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829  320 KEIFFSLGFEEMETHnYVESSFWCFDALYIPQQHPSRDLQDTFFIKepetcidkfvdteyidnikrvhthgdygsfgwny 399
Cdd:TIGR00468  82 RDIFLGLGFTEETGP-EVETDFWNFDALNIPQDHPARDMQDTFYIK---------------------------------- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829  400 kwkleesKKNVLRTHTTANSCRALFKLAKeykeagciKPKKYFSIDRVFRNENLDSTHLAEFHQVEGLIIDKNIGLSHLI 479
Cdd:TIGR00468 127 -------DRLLLRTHTTAVQLRTMEEQEK--------PPIRIFSPGRVFRNDTVDATHLPEFHQVEGLVIDKNISFTNLK 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829  480 GTLAAFYKHI-GIHKLKFKPTFNPYTEPSMEIYGYHEQSKKWLEVGNSGIFRPEMLRSMGFSEEVSVIAWGLSLERPTMI 558
Cdd:TIGR00468 192 GFLEEFLKKMfGETEIRFRPSYFPFTEPSAEIDVYCPEGKGWLEVLGAGMFRPEVLEPMGIDPTYPGFAWGIGIERLAML 271

                         330
                  ....*....|....
gi 124505829  559 KYNIKNIRDLFGYK 572
Cdd:TIGR00468 272 KYGITDIRDLYEND 285
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 301-569 1.71e-55

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: 190.65  E-value: 1.71e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 301 GKKINKGNIHLLTKQMRTFKEIFFSLGFEeMETHNYVESSFWCFDALYIPQQHPSRDLQDTFFIKEpetcidkfvdteyi 380
Cdd:COG0016   98 GRPRPLGSLHPLTQVIEEIEDIFVGMGFE-VAEGPEIETDWYNFEALNIPPDHPARDMQDTFYIDD-------------- 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 381 dnikrvhthgdygsfgwnykwkleeskKNVLRTHTTANSCRALfklaKEYKEagcikPKKYFSIDRVFRNENLDSTHLAE 460
Cdd:COG0016  163 ---------------------------GLLLRTHTSPVQIRTM----EKQKP-----PIRIIAPGRVYRRDESDATHSPM 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 461 FHQVEGLIIDKNIGLSHLIGTLAAFYKHI-GIH-KLKFKPTFNPYTEPSMEIYGYHEQSK----------KWLEVGNSGI 528
Cdd:COG0016  207 FHQVEGLVVDKGISFADLKGTLEEFAKAFfGEDvKVRFRPSYFPFTEPSAEVDISCFICGgkgcrvckgtGWLEILGCGM 286

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 124505829 529 FRPEMLRSMGF-SEEVSVIAWGLSLERPTMIKYNIKNIRDLF 569
Cdd:COG0016  287 VHPNVLRAVGIdPEEYSGFAFGMGIERLAMLKYGIDDIRLFF 328
 
Name Accession Description Interval E-value
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 72-575 0e+00

phenylalanyl-tRNA synthetase alpha chain; Provisional


Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 822.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829  72 NEYTTSLKISKKYNIDHNKVMGMIKKLETLYYIINLIKSFNTYHLSDEGKQYLKEGSPEFIVIKYVIQNNKCTLEDLKKN 151
Cdd:PTZ00326  19 NEIVNSLALAESLNIDHQKVVGAIKSLESANYITTEMKKSNTWTLTEEGEDYLKNGSPEYRLWQKLKEGGISKADDAKKL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 152 LGKIGDIGLNTNLKNRTIQLNKADKCLT-CNCNLHDIQDFTQIYLDIINQYghdeellfahlknknhtknalnnnemkns 230
Cdd:PTZ00326  99 GGKVADIGLGNAMKKKWIKLNKGDKKVFlSRKLVDSVVDTVRLLLKIVAKG----------------------------- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 231 CKDNNIINNLIQDLKKRKLLEIKKNSYSHVIKTSIFKKDIKKQITDINYLLLKNEEYKKYDIKKYNFFSSGKKINKGNIH 310
Cdd:PTZ00326 150 SQAEKIDSKELKELKKRKLATLEKIKYFVVTKGPKFAKEIKKQITDLTQEMLLNGSWKNAEFKEYNFNALGKKIGGGNLH 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 311 LLTKQMRTFKEIFFSLGFEEMETHNYVESSFWCFDALYIPQQHPSRDLQDTFFIKEPETCIDKFVDTEYIDNIKRVHTHG 390
Cdd:PTZ00326 230 PLLKVRREFREILLEMGFEEMPTNRYVESSFWNFDALFQPQQHPARDAQDTFFLSKPETSKVNDLDDDYVERVKKVHEVG 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 391 DYGSFGWNYKWKLEESKKNVLRTHTTANSCRALFKLAKEYKEAGCIKPKKYFSIDRVFRNENLDSTHLAEFHQVEGLIID 470
Cdd:PTZ00326 310 GYGSIGWRYDWKLEEARKNILRTHTTAVSARMLYKLAQEYKKTGPFKPKKYFSIDRVFRNETLDATHLAEFHQVEGFVID 389

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 471 KNIGLSHLIGTLAAFYKHIGIHKLKFKPTFNPYTEPSMEIYGYHEQSKKWLEVGNSGIFRPEMLRSMGFSEEVSVIAWGL 550
Cdd:PTZ00326 390 RNLTLGDLIGTIREFFRRIGITKLRFKPAFNPYTEPSMEIFGYHPGLKKWVEVGNSGIFRPEMLRPMGFPEDVTVIAWGL 469

                        490       500
                 ....*....|....*....|....*
gi 124505829 551 SLERPTMIKYNIKNIRDLFGYKSVV 575
Cdd:PTZ00326 470 SLERPTMIKYGIKNIRDLFGHKVDL 494
PLN02853 PLN02853
Probable phenylalanyl-tRNA synthetase alpha chain
 73-572 0e+00

Probable phenylalanyl-tRNA synthetase alpha chain


Pssm-ID: 215458 [Multi-domain]  Cd Length: 492  Bit Score: 543.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829  73 EYTTSLKISKKYNIDHNKVMGMIKKLETLYYI-INLIKSFnTYHLSDEGKQYLKEGSPEFIVIKYVIQNNKCTLEDLKKN 151
Cdd:PLN02853  17 EISDSGQFAASHGLDHNEVVGVIKSLHGFRYVdAQDIKRE-TWVLTEEGKKYAAEGSPEVQLFAAVPAEGSISKDELQKK 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 152 LGK-IGDIGLNTNLKNRTIQLNKADKcltcncnlhdiqdftqiyldIINQYGHDEELLFAHLKnknhtknALNNNEmkns 230
Cdd:PLN02853  96 LDPaVFDIGFKQAMKNKWLEMGGKPQ--------------------VSRKVQHVEDEVKELLL-------AIQEGK---- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 231 ckdnNIINNLIQDLKKRKLLeIKK---NSYShVIKTSIFKKDIKKQITDINYLLLKNEEYKKYDIKKYNFFSSGKKINKG 307
Cdd:PLN02853 145 ----EVDDKDIDALKKRRKL-ITLetwKGYS-IKKGPNYAPERKKAATDLTREMLQSGDWKDLEFKEYNFNALGAPPEGG 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 308 NIHLLTKQMRTFKEIFFSLGFEEMETHNYVESSFWCFDALYIPQQHPSRDLQDTFFIKEPETCidKFVDTEYIDNIKRVH 387
Cdd:PLN02853 219 HLHPLLKVRQQFRKIFLQMGFEEMPTNNFVESSFWNFDALFQPQQHPARDSHDTFFLKAPATT--RQLPEDYVERVKTVH 296

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 388 THGDYGSFGWNYKWKLEESKKNVLRTHTTANSCRALFKLAKeykeaGCIKPKKYFSIDRVFRNENLDSTHLAEFHQVEGL 467
Cdd:PLN02853 297 ESGGYGSIGYGYDWKREEANKNLLRTHTTAVSSRMLYKLAQ-----KGFKPKRYFSIDRVFRNEAVDRTHLAEFHQVEGL 371

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 468 IIDKNIGLSHLIGTLAAFYKHIGIHKLKFKPTFNPYTEPSMEIYGYHEQSKKWLEVGNSGIFRPEMLRSMGFSEEVSVIA 547
Cdd:PLN02853 372 VCDRGLTLGDLIGVLEDFFSRLGMTKLRFKPAYNPYTEPSMEIFSYHEGLKKWVEVGNSGMFRPEMLLPMGLPEDVNVIA 451

                        490       500
                 ....*....|....*....|....*
gi 124505829 548 WGLSLERPTMIKYNIKNIRDLFGYK 572
Cdd:PLN02853 452 WGLSLERPTMILYGIDNIRDLFGHK 476
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
72-571 4.16e-134

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 399.59  E-value: 4.16e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829  72 NEYTTSLKISKKYNIDHNKVMGMIKKLETLYYIINLIKSFNTYHLSDEGKQYLKEGSPEFIVIKYVIQNNKCTLEDLKKN 151
Cdd:PRK04172  18 LKEATLEELAEKLGLPPEAVMRAAEWLEEKGLVKVEERVEEVYVLTEEGKKYAEEGLPERRLLNALKDGGEVSLDELKEA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 152 L--GKIGDIGLNTNLKNRTIQLNKADkcltcncnlhdiqdftqiyLDIINQYGHDEEllfahlknknhtKNALNNNEMKN 229
Cdd:PRK04172  98 LldKKEVGIALGNLARKGWAKIEKGK-------------------VILKPDAYEDPE------------EKALKALAEGD 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 230 SCKDNNIINNLIQDLKKRKLLEIKKNSYSHVIKTSIFKK------DIKKQITDINYLLLKNEEYKKYDIKKYNFFSSGKK 303
Cdd:PRK04172 147 KEELSEEDLKVLKELKKRKLVEEKERTERSVELTDAGLEllkegiELKEEITQLTPELLKSGEWKEKEFRPYNVKAPPPK 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 304 INKGNIHLLTKQMRTFKEIFFSLGFEEMETHnYVESSFWCFDALYIPQQHPSRDLQDTFFIKEPETCidkFVDTEYIDNI 383
Cdd:PRK04172 227 IYPGKKHPYREFIDEVRDILVEMGFEEMKGP-LVETEFWNFDALFQPQDHPAREMQDTFYLKYPGIG---DLPEELVERV 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 384 KRVHTHG-DYGSFGWNYKWKLEESKKNVLRTHTTANSCRALFKLAKeykeagciKPKKYFSIDRVFRNENLDSTHLAEFH 462
Cdd:PRK04172 303 KEVHEHGgDTGSRGWGYKWDEDIAKRLVLRTHTTALSARYLASRPE--------PPQKYFSIGRVFRPDTIDATHLPEFY 374

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 463 QVEGLIIDKNIGLSHLIGTLAAFYKHIGIHKLKFKPTFNPYTEPSMEIYGYHEqSKKWLEVGNSGIFRPEMLRSMGFseE 542
Cdd:PRK04172 375 QLEGIVMGEDVSFRDLLGILKEFYKRLGFEEVKFRPAYFPFTEPSVEVEVYHE-GLGWVELGGAGIFRPEVLEPLGI--D 451

                        490       500
                 ....*....|....*....|....*....
gi 124505829 543 VSVIAWGLSLERPTMIKYNIKNIRDLFGY 571
Cdd:PRK04172 452 VPVLAWGLGIERLAMLRLGLDDIRDLYSS 480
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 310-572 4.76e-107

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: 320.26  E-value: 4.76e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 310 HLLTKQMRTFKEIFFSLGFEEMETHnYVESSFWCFDALYIPQQHPSRDLQDTFFIKEPEtcidkfvdteyidnikrvhth 389
Cdd:cd00496    1 HPLNKVIEEIEDIFVSMGFTEVEGP-EVETDFYNFDALNIPQDHPARDMQDTFYINDPA--------------------- 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 390 gdygsfgwnykwkleeskKNVLRTHTTANSCRALFKLakeykeagcIKPKKYFSIDRVFRNENLDSTHLAEFHQVEGLII 469
Cdd:cd00496   59 ------------------RLLLRTHTSAVQARALAKL---------KPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVV 111

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 470 DKNIGLSHLIGTLAAFYKHIG--IHKLKFKPTFNPYTEPSMEIYGYHEQSKKWLEVGNSGIFRPEMLRSMGFSEEVSVIA 547
Cdd:cd00496  112 DKGLTFADLKGTLEEFAKELFgpITKVRFRPSYFPFTEPSFEVDVYCPGCLGWLEILGCGMVRPEVLENAGIDEEYSGFA 191

                        250       260
                 ....*....|....*....|....*
gi 124505829 548 WGLSLERPTMIKYNIKNIRDLFGYK 572
Cdd:cd00496  192 FGIGLERLAMLKYGIPDIRLFYSND 216
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 294-570 1.14e-104

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: 315.29  E-value: 1.14e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829  294 KYNFFSSGKKINKGNIHLLTKQMRTFKEIFFSLGFEEMETHnYVESSFWCFDALYIPQQHPSRDLQDTFFIKEPETcidk 373
Cdd:pfam01409   1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVEGP-EVESDFYNFDALNIPQDHPARDMQDTFYLKKPLK---- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829  374 fvdteyidnikrvhthgdygsfgwnykwklEESKKNVLRTHTTANSCRALfklAKEYKeagciKPKKYFSIDRVFRNENL 453
Cdd:pfam01409  76 ------------------------------PVARRLLLRTHTTPVQARTL---AKKPK-----PPIKIFSIGRVFRRDQV 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829  454 DSTHLAEFHQVEGLIIDKNIGLSHLIGTLAAFYKHI-GIH-KLKFKPTFNPYTEPSMEIYGYHEQSKKWLEVGNSGIFRP 531
Cdd:pfam01409 118 DATHLPEFHQVEGLVVDENVTFADLKGVLEEFLRKFfGFEvKVRFRPSYFPFTEPSAEVDVYVCKLGGWLEVGGAGMVHP 197

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 124505829  532 EMLRSMGFSEEVSVIAWGLSLERPTMIKYNIKNIRDLFG 570
Cdd:pfam01409 198 NVLEAVGIDEDYSGFAFGLGVERLAMLKYGIDDIRDLYE 236
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 240-572 1.04e-97

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: 299.23  E-value: 1.04e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829  240 LIQDLKKRKLLEIKKNSYSHVIKTSIFKKDIKKQITDINYLLLKNEEYKKYDIKKYNFFSSGKKINKGNIHLLTKQMRTF 319
Cdd:TIGR00468   2 LKDLLKQLGKLTKEETKPALGALINEVKIELQDELTKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDEI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829  320 KEIFFSLGFEEMETHnYVESSFWCFDALYIPQQHPSRDLQDTFFIKepetcidkfvdteyidnikrvhthgdygsfgwny 399
Cdd:TIGR00468  82 RDIFLGLGFTEETGP-EVETDFWNFDALNIPQDHPARDMQDTFYIK---------------------------------- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829  400 kwkleesKKNVLRTHTTANSCRALFKLAKeykeagciKPKKYFSIDRVFRNENLDSTHLAEFHQVEGLIIDKNIGLSHLI 479
Cdd:TIGR00468 127 -------DRLLLRTHTTAVQLRTMEEQEK--------PPIRIFSPGRVFRNDTVDATHLPEFHQVEGLVIDKNISFTNLK 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829  480 GTLAAFYKHI-GIHKLKFKPTFNPYTEPSMEIYGYHEQSKKWLEVGNSGIFRPEMLRSMGFSEEVSVIAWGLSLERPTMI 558
Cdd:TIGR00468 192 GFLEEFLKKMfGETEIRFRPSYFPFTEPSAEIDVYCPEGKGWLEVLGAGMFRPEVLEPMGIDPTYPGFAWGIGIERLAML 271

                         330
                  ....*....|....
gi 124505829  559 KYNIKNIRDLFGYK 572
Cdd:TIGR00468 272 KYGITDIRDLYEND 285
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 301-569 1.71e-55

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: 190.65  E-value: 1.71e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 301 GKKINKGNIHLLTKQMRTFKEIFFSLGFEeMETHNYVESSFWCFDALYIPQQHPSRDLQDTFFIKEpetcidkfvdteyi 380
Cdd:COG0016   98 GRPRPLGSLHPLTQVIEEIEDIFVGMGFE-VAEGPEIETDWYNFEALNIPPDHPARDMQDTFYIDD-------------- 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 381 dnikrvhthgdygsfgwnykwkleeskKNVLRTHTTANSCRALfklaKEYKEagcikPKKYFSIDRVFRNENLDSTHLAE 460
Cdd:COG0016  163 ---------------------------GLLLRTHTSPVQIRTM----EKQKP-----PIRIIAPGRVYRRDESDATHSPM 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 461 FHQVEGLIIDKNIGLSHLIGTLAAFYKHI-GIH-KLKFKPTFNPYTEPSMEIYGYHEQSK----------KWLEVGNSGI 528
Cdd:COG0016  207 FHQVEGLVVDKGISFADLKGTLEEFAKAFfGEDvKVRFRPSYFPFTEPSAEVDISCFICGgkgcrvckgtGWLEILGCGM 286

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 124505829 529 FRPEMLRSMGF-SEEVSVIAWGLSLERPTMIKYNIKNIRDLF 569
Cdd:COG0016  287 VHPNVLRAVGIdPEEYSGFAFGMGIERLAMLKYGIDDIRLFF 328
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 324-569 1.91e-17

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 84.43  E-value: 1.91e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 324 FSLGFEEMETHNYVESSFWCFDALYIPQQHPSRDLQDTFfikepetcidkfvdteYIDNikrvhthgdygsfgwnykwkl 403
Cdd:PLN02788  85 YSNKFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTY----------------YVDA--------------------- 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 404 eeskKNVLRTHTTANSCRALFKLAKEYKEAGcikpkkyfsidRVFRNENLDSTHLAEFHQVEGLIIDKN-----IGLS-- 476
Cdd:PLN02788 128 ----QTVLRCHTSAHQAELLRAGHTHFLVTG-----------DVYRRDSIDATHYPVFHQMEGVRVFSPeeweaSGLDgt 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 477 -----HLIGTLAAFYKHI-GIHKLKFKPTFNPYTEPSMEIYGYHEQskKWLEVGNSGIFRPEMLRSMGFSEEVsviAW-- 548
Cdd:PLN02788 193 dlaaeDLKKTLEGLARHLfGDVEMRWVDAYFPFTNPSFELEIFFKG--EWLEVLGCGVTEQEILKNNGRSDNV---AWaf 267

                        250       260
                 ....*....|....*....|.
gi 124505829 549 GLSLERPTMIKYNIKNIRdLF 569
Cdd:PLN02788 268 GLGLERLAMVLFDIPDIR-LF 287
class_II_aaRS-like_core cd00768
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
 317-555 3.04e-09

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: 57.13  E-value: 3.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 317 RTFKEIFFSLGFEEMETHNYVESSFWCFDALYIPQQHPSRDLQDTFFikepetcidkfvdteyidnikrvhthgdygsfg 396
Cdd:cd00768    7 QKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKDLLPVGAENEEDL--------------------------------- 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 397 wnykwkleeskknVLRTHTTANscraLFKLAKEYKEAGcikPKKYFSIDRVFRNE--NLDSTHLAEFHQVEGLI----ID 470
Cdd:cd00768   54 -------------YLRPTLEPG----LVRLFVSHIRKL---PLRLAEIGPAFRNEggRRGLRRVREFTQLEGEVfgedGE 113

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829 471 KNIGLSHLIGTLAAFYKHIGI-HKLKFK-----PTFNPYTEPSMEIYGYHEqSKKWLEVGNSGIFRPEMLRSM------- 537
Cdd:cd00768  114 EASEFEELIELTEELLRALGIkLDIVFVektpgEFSPGGAGPGFEIEVDHP-EGRGLEIGSGGYRQDEQARAAdlyflde 192

                        250
                 ....*....|....*....
gi 124505829 538 -GFSEEVSVIAWGLSLERP 555
Cdd:cd00768  193 aLEYRYPPTIGFGLGLERL 211
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 344-566 4.55e-08

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: 55.85  E-value: 4.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829  344 FDALYIPQQHPSRDLQDTFFIKEpetcidkfvdteyidnikrvhTHgdygsfgwnykwkleeskknVLRTHTTANSCRAL 423
Cdd:TIGR00469  84 FDNLGFPADHPGRQKSDCYYINE---------------------QH--------------------LLRAHTSAHELECF 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829  424 FKLAKEYKEAgcikPKKYFSIDRVFRNENLDSTHLAEFHQVEGLII---------DKNIGLSHLI-----GTLAAFYKH- 488
Cdd:TIGR00469 123 QGGLDDSDNI----KSGFLISADVYRRDEIDKTHYPVFHQADGAAIrkrtkadlfEKEPGYIEKFeedirGTEADLNKEn 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829  489 --------------------------------------IGIHKLKFKP-----------------------TFNPYTEPS 507
Cdd:TIGR00469 199 vkiildddsiplkennpkqeyasdlavdlcehelkhsiEGITKDLFGKkissmiknkanntpkelkvrwidAYFPFTAPS 278

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505829  508 MEIYGYHEQskKWLEVGNSGIFRPEMLRSMGFSEEVSV-IAWGLSLERPTMIKYNIKNIR 566
Cdd:TIGR00469 279 WEIEIWFKD--EWLELCGCGIIRHDILLRAGVHPSETIgWAFGLGLDRIAMLLFDIPDIR 336
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
440-465 6.64e-04

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


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 42.17  E-value: 6.64e-04
                          10        20
                  ....*....|....*....|....*.
gi 124505829  440 KYFSIDRVFRNENLDSTHLAEFHQVE 465
Cdd:pfam00152  92 RVFQIARCFRDEDLRTDRQPEFTQLD 117
 
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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