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Conserved domains on  [gi|1803532212|gb|KAF1518091|]
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Phenylalanine--tRNA ligase, mitochondrial, partial [Eudyptes sclateri]

Protein Classification

phenylalanine--tRNA ligase( domain architecture ID 1006086)

phenylalanine--tRNA ligase catalyzes the synthesis of phenylalanyl-tRNA (Phe)

CATH:  3.30.70.380|3.30.930.10
EC:  6.1.1.20
Gene Ontology:  GO:0005524|GO:0004826|GO:0000049|GO:0006432

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02788 super family cl33567
phenylalanine-tRNA synthetase
 33-452 3.43e-174

phenylalanine-tRNA synthetase


The actual alignment was detected with superfamily member PLN02788:

Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 493.90  E-value: 3.43e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212  33 HSSSKSVPSDFAAST----PCSNTVELLGKAYPQDN-------YSNVTEKILSKVGKNLHNKKHHPLWLIKEQVKDHFYK 101
Cdd:PLN02788    4 SSALVTPATAKSSSRryraPAVSAVEIGGVAIARDEvvreddpTNNVPDHIFSKIGMQLHRRPDHPLGILKNAIYDYFDE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 102 QYIGrrgtpLFSVYDGLSPVVTVQQNFDSLLIPQNHASRRKEDNYYLNRDHMLRAHTSAHQWDLIHSGLDAFLAVGDVYR 181
Cdd:PLN02788   84 NYSN-----KFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAHQAELLRAGHTHFLVTGDVYR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 182 RDTIDNSHYPVFHQMEGVRLFSCHELfsnikdgeglqlfeqghrtahkqECHTMEAVRLVEFNLKQVLTKLMTHIFGDgL 261
Cdd:PLN02788  159 RDSIDATHYPVFHQMEGVRVFSPEEW-----------------------EASGLDGTDLAAEDLKKTLEGLARHLFGD-V 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 262 QVRWVDCYFPFTHPSFEMEIHFQGEWMEVLGCGVMEQQLVNSAGAQDKIGWAFGLGLERLAMILYDIPDIRLFWSEDERF 341
Cdd:PLN02788  215 EMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVTEQEILKNNGRSDNVAWAFGLGLERLAMVLFDIPDIRLFWSDDERF 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 342 LKQFIVPHIwqKIKFQPLSRYPPLINDISFWLPSEtYSKNDFYDLARTVGGDLIEKVVLVDEFTHPETKKVSHCYRIIYR 421
Cdd:PLN02788  295 TSQFKEGQL--GVKFKPYSKYPPCYKDISFWISDE-FTENNLCEVVRGIAGDLVEEVKLIDNFTNPKKGKTSHCYRIVYR 371

                         410       420       430
                  ....*....|....*....|....*....|.
gi 1803532212 422 HPERTLTQDEVHRIHQAIEESAVQELGVEGR 452
Cdd:PLN02788  372 SMERSLTDEEINALQDKVREEVQKKLGVELR 402
 
Name Accession Description Interval E-value
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 33-452 3.43e-174

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 493.90  E-value: 3.43e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212  33 HSSSKSVPSDFAAST----PCSNTVELLGKAYPQDN-------YSNVTEKILSKVGKNLHNKKHHPLWLIKEQVKDHFYK 101
Cdd:PLN02788    4 SSALVTPATAKSSSRryraPAVSAVEIGGVAIARDEvvreddpTNNVPDHIFSKIGMQLHRRPDHPLGILKNAIYDYFDE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 102 QYIGrrgtpLFSVYDGLSPVVTVQQNFDSLLIPQNHASRRKEDNYYLNRDHMLRAHTSAHQWDLIHSGLDAFLAVGDVYR 181
Cdd:PLN02788   84 NYSN-----KFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAHQAELLRAGHTHFLVTGDVYR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 182 RDTIDNSHYPVFHQMEGVRLFSCHELfsnikdgeglqlfeqghrtahkqECHTMEAVRLVEFNLKQVLTKLMTHIFGDgL 261
Cdd:PLN02788  159 RDSIDATHYPVFHQMEGVRVFSPEEW-----------------------EASGLDGTDLAAEDLKKTLEGLARHLFGD-V 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 262 QVRWVDCYFPFTHPSFEMEIHFQGEWMEVLGCGVMEQQLVNSAGAQDKIGWAFGLGLERLAMILYDIPDIRLFWSEDERF 341
Cdd:PLN02788  215 EMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVTEQEILKNNGRSDNVAWAFGLGLERLAMVLFDIPDIRLFWSDDERF 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 342 LKQFIVPHIwqKIKFQPLSRYPPLINDISFWLPSEtYSKNDFYDLARTVGGDLIEKVVLVDEFTHPETKKVSHCYRIIYR 421
Cdd:PLN02788  295 TSQFKEGQL--GVKFKPYSKYPPCYKDISFWISDE-FTENNLCEVVRGIAGDLVEEVKLIDNFTNPKKGKTSHCYRIVYR 371

                         410       420       430
                  ....*....|....*....|....*....|.
gi 1803532212 422 HPERTLTQDEVHRIHQAIEESAVQELGVEGR 452
Cdd:PLN02788  372 SMERSLTDEEINALQDKVREEVQKKLGVELR 402
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 53-450 1.24e-149

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: 433.73  E-value: 1.24e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212  53 VELLGKAYPQDNYS-NVTEKILSKVGKNLHNKKHHPLWLIKEQVKDHFYKQYIGRRGTPLFSVYDGLSPVVTVQQNFDSL 131
Cdd:TIGR00469   8 LEINGIKYATDGQTtNVTDKIIKLTDANKHLKEDHPLGIIRDLIEKKFNGADNNQRGNPLFKIFDNFKPVVTTMENFDNL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 132 LIPQNHASRRKEDNYYLNRDHMLRAHTSAHQWDLIHSGLD-------AFLAVGDVYRRDTIDNSHYPVFHQMEG--VRLF 202
Cdd:TIGR00469  88 GFPADHPGRQKSDCYYINEQHLLRAHTSAHELECFQGGLDdsdniksGFLISADVYRRDEIDKTHYPVFHQADGaaIRKR 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 203 SCHELFsnIKDGEGLQLFEQGHR------------------------TAHKQECHTMEAVRLVEFNLKQVLTKLMTHIFG 258
Cdd:TIGR00469 168 TKADLF--EKEPGYIEKFEEDIRgteadlnkenvkiildddsiplkeNNPKQEYASDLAVDLCEHELKHSIEGITKDLFG 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 259 ---------------DGLQVRWVDCYFPFTHPSFEMEIHFQGEWMEVLGCGVMEQQLVNSAGAQ--DKIGWAFGLGLERL 321
Cdd:TIGR00469 246 kkissmiknkanntpKELKVRWIDAYFPFTAPSWEIEIWFKDEWLELCGCGIIRHDILLRAGVHpsETIGWAFGLGLDRI 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 322 AMILYDIPDIRLFWSEDERFLKQFIVPHIWQKIKFQPLSRYPPLINDISFWLPSET-----YSKNDFYDLARTVGGDLIE 396
Cdd:TIGR00469 326 AMLLFDIPDIRLFWSNDEGFLRQFSEGDLHLIPKFKPISHHPGCFNDLAFWLPEDIeddagFHENDFMDIIRNIAGDLVE 405

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1803532212 397 KVVLVDEFTHPETKKVSHCYRIIYRHPERTLTQDEVHRIHQAIEESAVQELGVE 450
Cdd:TIGR00469 406 QIKLVDKFKHPKTGKKSMCFRINYQHMDRNLTNAEVNEIHDMIASALVDEFNVE 459
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 86-340 6.41e-91

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: 274.81  E-value: 6.41e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212  86 HPLWLIKEQVKDHFYKQyigrrgtpLFSVYDGlSPVVTVQQNFDSLLIPQNHASRRKEDNYYLNR--DHMLRAHTSAHQW 163
Cdd:cd00496     1 HPLNKVIEEIEDIFVSM--------GFTEVEG-PEVETDFYNFDALNIPQDHPARDMQDTFYINDpaRLLLRTHTSAVQA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 164 DLIHS--GLDAFLAVGDVYRRDTIDNSHYPVFHQMEGVRLFSchelfsnikdgeglqlfeqghrtahkqechtmeavRLV 241
Cdd:cd00496    72 RALAKlkPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDK-----------------------------------GLT 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 242 EFNLKQVLTKLMTHIFGDGLQVRWVDCYFPFTHPSFEMEIHFQG--EWMEVLGCGVMEQQLVNSAGAQDK-IGWAFGLGL 318
Cdd:cd00496   117 FADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYCPGclGWLEILGCGMVRPEVLENAGIDEEySGFAFGIGL 196

                         250       260
                  ....*....|....*....|..
gi 1803532212 319 ERLAMILYDIPDIRLFWSEDER 340
Cdd:cd00496   197 ERLAMLKYGIPDIRLFYSNDLR 218
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 86-345 9.30e-54

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: 182.94  E-value: 9.30e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212  86 HPLWLIKEQVKDHFYKqyIGrrgtplFSVYDGlsP-VVTVQQNFDSLLIPQNHASRRKEDNYYLNRDHMLRAHTSAHQwd 164
Cdd:COG0016   107 HPLTQVIEEIEDIFVG--MG------FEVAEG--PeIETDWYNFEALNIPPDHPARDMQDTFYIDDGLLLRTHTSPVQ-- 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 165 lIHSGLD-----AFLAVGDVYRRDTIDNSHYPVFHQMEG--VrlfschelfsnikdGEGLqlfeqghrtahkqechTMeA 237
Cdd:COG0016   175 -IRTMEKqkppiRIIAPGRVYRRDESDATHSPMFHQVEGlvV--------------DKGI----------------SF-A 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 238 vrlvefNLKQVLTKLMTHIFGDGLQVRWVDCYFPFTHPSFEMEIHF------------QGEWMEVLGCG-----VMEqql 300
Cdd:COG0016   223 ------DLKGTLEEFAKAFFGEDVKVRFRPSYFPFTEPSAEVDISCficggkgcrvckGTGWLEILGCGmvhpnVLR--- 293

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1803532212 301 vnSAGAQDKI--GWAFGLGLERLAMILYDIPDIRLFWSEDERFLKQF 345
Cdd:COG0016   294 --AVGIDPEEysGFAFGMGIERLAMLKYGIDDIRLFFENDLRFLRQF 338
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 84-345 1.10e-48

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: 166.60  E-value: 1.10e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212  84 KHHPLWLIKEQVKDHFYKqyIGrrgtplFSVYDGlSPVVTVQQNFDSLLIPQNHASRRKEDNYYLNRDH-------MLRA 156
Cdd:pfam01409  15 GLHPLTRTLERIRDIFLG--MG------FEEVEG-PEVESDFYNFDALNIPQDHPARDMQDTFYLKKPLkpvarrlLLRT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 157 HTSAHQwdLIHSGLDAFL-----AVGDVYRRDTIDNSHYPVFHQMEGVRLfschelfsnikdGEGLqlfeqghrtahkqe 231
Cdd:pfam01409  86 HTTPVQ--ARTLAKKPKPpikifSIGRVFRRDQVDATHLPEFHQVEGLVV------------DENV-------------- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 232 chTMEavrlvefNLKQVLTKLMTHIFGDGLQVRWVDCYFPFTHPSFEMEI--HFQGEWMEVLGCGVMEQQLVNSAG-AQD 308
Cdd:pfam01409 138 --TFA-------DLKGVLEEFLRKFFGFEVKVRFRPSYFPFTEPSAEVDVyvCKLGGWLEVGGAGMVHPNVLEAVGiDED 208

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1803532212 309 KIGWAFGLGLERLAMILYDIPDIRLFWSEDERFLKQF 345
Cdd:pfam01409 209 YSGFAFGLGVERLAMLKYGIDDIRDLYENDLRFLRQF 245
FDX-ACB smart00896
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 360-452 6.20e-30

Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some phenylalanyl tRNA synthetases. The domain has a ferredoxin fold, consisting of an alpha+beta sandwich with anti-parallel beta-sheets (beta-alpha-beta x2).


Pssm-ID: 214893 [Multi-domain]  Cd Length: 93  Bit Score: 111.75  E-value: 6.20e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212  360 SRYPPLINDISFWLPSETySKNDFYDLARTVGGDLIEKVVLVDEFTH--PETKKvSHCYRIIYRHPERTLTQDEVHRIHQ 437
Cdd:smart00896   1 SKFPAVRRDLAFVVDEDV-PAAELLDAIREAGGDLLEDVRLFDVYEGgiPEGKK-SLAYRLTYQSPDRTLTDEEVNAIHD 78

                           90
                   ....*....|....*
gi 1803532212  438 AIEESAVQELGVEGR 452
Cdd:smart00896  79 KIVAALEKKFGAELR 93
 
Name Accession Description Interval E-value
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 33-452 3.43e-174

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 493.90  E-value: 3.43e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212  33 HSSSKSVPSDFAAST----PCSNTVELLGKAYPQDN-------YSNVTEKILSKVGKNLHNKKHHPLWLIKEQVKDHFYK 101
Cdd:PLN02788    4 SSALVTPATAKSSSRryraPAVSAVEIGGVAIARDEvvreddpTNNVPDHIFSKIGMQLHRRPDHPLGILKNAIYDYFDE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 102 QYIGrrgtpLFSVYDGLSPVVTVQQNFDSLLIPQNHASRRKEDNYYLNRDHMLRAHTSAHQWDLIHSGLDAFLAVGDVYR 181
Cdd:PLN02788   84 NYSN-----KFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAHQAELLRAGHTHFLVTGDVYR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 182 RDTIDNSHYPVFHQMEGVRLFSCHELfsnikdgeglqlfeqghrtahkqECHTMEAVRLVEFNLKQVLTKLMTHIFGDgL 261
Cdd:PLN02788  159 RDSIDATHYPVFHQMEGVRVFSPEEW-----------------------EASGLDGTDLAAEDLKKTLEGLARHLFGD-V 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 262 QVRWVDCYFPFTHPSFEMEIHFQGEWMEVLGCGVMEQQLVNSAGAQDKIGWAFGLGLERLAMILYDIPDIRLFWSEDERF 341
Cdd:PLN02788  215 EMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVTEQEILKNNGRSDNVAWAFGLGLERLAMVLFDIPDIRLFWSDDERF 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 342 LKQFIVPHIwqKIKFQPLSRYPPLINDISFWLPSEtYSKNDFYDLARTVGGDLIEKVVLVDEFTHPETKKVSHCYRIIYR 421
Cdd:PLN02788  295 TSQFKEGQL--GVKFKPYSKYPPCYKDISFWISDE-FTENNLCEVVRGIAGDLVEEVKLIDNFTNPKKGKTSHCYRIVYR 371

                         410       420       430
                  ....*....|....*....|....*....|.
gi 1803532212 422 HPERTLTQDEVHRIHQAIEESAVQELGVEGR 452
Cdd:PLN02788  372 SMERSLTDEEINALQDKVREEVQKKLGVELR 402
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 53-450 1.24e-149

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: 433.73  E-value: 1.24e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212  53 VELLGKAYPQDNYS-NVTEKILSKVGKNLHNKKHHPLWLIKEQVKDHFYKQYIGRRGTPLFSVYDGLSPVVTVQQNFDSL 131
Cdd:TIGR00469   8 LEINGIKYATDGQTtNVTDKIIKLTDANKHLKEDHPLGIIRDLIEKKFNGADNNQRGNPLFKIFDNFKPVVTTMENFDNL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 132 LIPQNHASRRKEDNYYLNRDHMLRAHTSAHQWDLIHSGLD-------AFLAVGDVYRRDTIDNSHYPVFHQMEG--VRLF 202
Cdd:TIGR00469  88 GFPADHPGRQKSDCYYINEQHLLRAHTSAHELECFQGGLDdsdniksGFLISADVYRRDEIDKTHYPVFHQADGaaIRKR 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 203 SCHELFsnIKDGEGLQLFEQGHR------------------------TAHKQECHTMEAVRLVEFNLKQVLTKLMTHIFG 258
Cdd:TIGR00469 168 TKADLF--EKEPGYIEKFEEDIRgteadlnkenvkiildddsiplkeNNPKQEYASDLAVDLCEHELKHSIEGITKDLFG 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 259 ---------------DGLQVRWVDCYFPFTHPSFEMEIHFQGEWMEVLGCGVMEQQLVNSAGAQ--DKIGWAFGLGLERL 321
Cdd:TIGR00469 246 kkissmiknkanntpKELKVRWIDAYFPFTAPSWEIEIWFKDEWLELCGCGIIRHDILLRAGVHpsETIGWAFGLGLDRI 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 322 AMILYDIPDIRLFWSEDERFLKQFIVPHIWQKIKFQPLSRYPPLINDISFWLPSET-----YSKNDFYDLARTVGGDLIE 396
Cdd:TIGR00469 326 AMLLFDIPDIRLFWSNDEGFLRQFSEGDLHLIPKFKPISHHPGCFNDLAFWLPEDIeddagFHENDFMDIIRNIAGDLVE 405

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1803532212 397 KVVLVDEFTHPETKKVSHCYRIIYRHPERTLTQDEVHRIHQAIEESAVQELGVE 450
Cdd:TIGR00469 406 QIKLVDKFKHPKTGKKSMCFRINYQHMDRNLTNAEVNEIHDMIASALVDEFNVE 459
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 86-340 6.41e-91

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: 274.81  E-value: 6.41e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212  86 HPLWLIKEQVKDHFYKQyigrrgtpLFSVYDGlSPVVTVQQNFDSLLIPQNHASRRKEDNYYLNR--DHMLRAHTSAHQW 163
Cdd:cd00496     1 HPLNKVIEEIEDIFVSM--------GFTEVEG-PEVETDFYNFDALNIPQDHPARDMQDTFYINDpaRLLLRTHTSAVQA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 164 DLIHS--GLDAFLAVGDVYRRDTIDNSHYPVFHQMEGVRLFSchelfsnikdgeglqlfeqghrtahkqechtmeavRLV 241
Cdd:cd00496    72 RALAKlkPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDK-----------------------------------GLT 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 242 EFNLKQVLTKLMTHIFGDGLQVRWVDCYFPFTHPSFEMEIHFQG--EWMEVLGCGVMEQQLVNSAGAQDK-IGWAFGLGL 318
Cdd:cd00496   117 FADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYCPGclGWLEILGCGMVRPEVLENAGIDEEySGFAFGIGL 196

                         250       260
                  ....*....|....*....|..
gi 1803532212 319 ERLAMILYDIPDIRLFWSEDER 340
Cdd:cd00496   197 ERLAMLKYGIPDIRLFYSNDLR 218
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 86-345 9.30e-54

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: 182.94  E-value: 9.30e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212  86 HPLWLIKEQVKDHFYKqyIGrrgtplFSVYDGlsP-VVTVQQNFDSLLIPQNHASRRKEDNYYLNRDHMLRAHTSAHQwd 164
Cdd:COG0016   107 HPLTQVIEEIEDIFVG--MG------FEVAEG--PeIETDWYNFEALNIPPDHPARDMQDTFYIDDGLLLRTHTSPVQ-- 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 165 lIHSGLD-----AFLAVGDVYRRDTIDNSHYPVFHQMEG--VrlfschelfsnikdGEGLqlfeqghrtahkqechTMeA 237
Cdd:COG0016   175 -IRTMEKqkppiRIIAPGRVYRRDESDATHSPMFHQVEGlvV--------------DKGI----------------SF-A 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 238 vrlvefNLKQVLTKLMTHIFGDGLQVRWVDCYFPFTHPSFEMEIHF------------QGEWMEVLGCG-----VMEqql 300
Cdd:COG0016   223 ------DLKGTLEEFAKAFFGEDVKVRFRPSYFPFTEPSAEVDISCficggkgcrvckGTGWLEILGCGmvhpnVLR--- 293

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1803532212 301 vnSAGAQDKI--GWAFGLGLERLAMILYDIPDIRLFWSEDERFLKQF 345
Cdd:COG0016   294 --AVGIDPEEysGFAFGMGIERLAMLKYGIDDIRLFFENDLRFLRQF 338
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 77-345 1.35e-49

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: 170.57  E-value: 1.35e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212  77 GKNLHNKKHHPLWLIKEQVKDHFYKQyigrrgtpLFSVYDGlSPVVTVQQNFDSLLIPQNHASRRKEDNYYLNRDHMLRA 156
Cdd:TIGR00468  63 GTKIYPGSLHPLTRVIDEIRDIFLGL--------GFTEETG-PEVETDFWNFDALNIPQDHPARDMQDTFYIKDRLLLRT 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 157 HTSA---HQWDLIHSGLDAFLAVGDVYRRDTIDNSHYPVFHQMEGVRlfschelfsnIKDGEGLQlfeqghrtahkqech 233
Cdd:TIGR00468 134 HTTAvqlRTMEEQEKPPIRIFSPGRVFRNDTVDATHLPEFHQVEGLV----------IDKNISFT--------------- 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 234 tmeavrlvefNLKQVLTKLMTHIFGdGLQVRWVDCYFPFTHPSFEMEI-HFQGE-WMEVLGCGVMEQQLVNSAGAQDKI- 310
Cdd:TIGR00468 189 ----------NLKGFLEEFLKKMFG-ETEIRFRPSYFPFTEPSAEIDVyCPEGKgWLEVLGAGMFRPEVLEPMGIDPTYp 257

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1803532212 311 GWAFGLGLERLAMILYDIPDIRLFWSEDERFLKQF 345
Cdd:TIGR00468 258 GFAWGIGIERLAMLKYGITDIRDLYENDLRFLRQF 292
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 84-345 1.10e-48

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: 166.60  E-value: 1.10e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212  84 KHHPLWLIKEQVKDHFYKqyIGrrgtplFSVYDGlSPVVTVQQNFDSLLIPQNHASRRKEDNYYLNRDH-------MLRA 156
Cdd:pfam01409  15 GLHPLTRTLERIRDIFLG--MG------FEEVEG-PEVESDFYNFDALNIPQDHPARDMQDTFYLKKPLkpvarrlLLRT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 157 HTSAHQwdLIHSGLDAFL-----AVGDVYRRDTIDNSHYPVFHQMEGVRLfschelfsnikdGEGLqlfeqghrtahkqe 231
Cdd:pfam01409  86 HTTPVQ--ARTLAKKPKPpikifSIGRVFRRDQVDATHLPEFHQVEGLVV------------DENV-------------- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 232 chTMEavrlvefNLKQVLTKLMTHIFGDGLQVRWVDCYFPFTHPSFEMEI--HFQGEWMEVLGCGVMEQQLVNSAG-AQD 308
Cdd:pfam01409 138 --TFA-------DLKGVLEEFLRKFFGFEVKVRFRPSYFPFTEPSAEVDVyvCKLGGWLEVGGAGMVHPNVLEAVGiDED 208

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1803532212 309 KIGWAFGLGLERLAMILYDIPDIRLFWSEDERFLKQF 345
Cdd:pfam01409 209 YSGFAFGLGVERLAMLKYGIDDIRDLYENDLRFLRQF 245
FDX-ACB smart00896
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 360-452 6.20e-30

Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some phenylalanyl tRNA synthetases. The domain has a ferredoxin fold, consisting of an alpha+beta sandwich with anti-parallel beta-sheets (beta-alpha-beta x2).


Pssm-ID: 214893 [Multi-domain]  Cd Length: 93  Bit Score: 111.75  E-value: 6.20e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212  360 SRYPPLINDISFWLPSETySKNDFYDLARTVGGDLIEKVVLVDEFTH--PETKKvSHCYRIIYRHPERTLTQDEVHRIHQ 437
Cdd:smart00896   1 SKFPAVRRDLAFVVDEDV-PAAELLDAIREAGGDLLEDVRLFDVYEGgiPEGKK-SLAYRLTYQSPDRTLTDEEVNAIHD 78

                           90
                   ....*....|....*
gi 1803532212  438 AIEESAVQELGVEGR 452
Cdd:smart00896  79 KIVAALEKKFGAELR 93
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
127-343 4.19e-25

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 107.61  E-value: 4.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 127 NFDSLLIPQNHASRRKEDNYYLNRD----------------H-----------------------MLRAHT---SAHQwd 164
Cdd:PRK04172  265 NFDALFQPQDHPAREMQDTFYLKYPgigdlpeelvervkevHehggdtgsrgwgykwdediakrlVLRTHTtalSARY-- 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 165 lIHSGLDA---FLAVGDVYRRDTIDNSHYPVFHQMEGVRLfschelfsnikdGEGLqlfeqghrtahkqechtmeAVRlv 241
Cdd:PRK04172  343 -LASRPEPpqkYFSIGRVFRPDTIDATHLPEFYQLEGIVM------------GEDV-------------------SFR-- 388

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 242 efNLKQVLTKLMTHI-FGDglqVRWVDCYFPFTHPSFEMEI-HFQGEWMEVLGCGVMEQQLVNSAGAQDKIGwAFGLGLE 319
Cdd:PRK04172  389 --DLLGILKEFYKRLgFEE---VKFRPAYFPFTEPSVEVEVyHEGLGWVELGGAGIFRPEVLEPLGIDVPVL-AWGLGIE 462

                         250       260
                  ....*....|....*....|....
gi 1803532212 320 RLAMILYDIPDIRLFWSEDERFLK 343
Cdd:PRK04172  463 RLAMLRLGLDDIRDLYSSDIEWLR 486
FDX-ACB pfam03147
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 360-452 1.31e-22

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


Pssm-ID: 460826 [Multi-domain]  Cd Length: 94  Bit Score: 91.77  E-value: 1.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 360 SRYPPLINDISFWLPSETySKNDFYDLARTVGGDLIEKVVLVDEFTH---PETKKvSHCYRIIYRHPERTLTQDEVHRIH 436
Cdd:pfam03147   1 SKYPAVRRDLAFVVDEDV-PAADILKAIREAGGELLESVELFDVYRGekiPEGKK-SLAFRLTFQSPERTLTDEEVNAII 78

                          90
                  ....*....|....*.
gi 1803532212 437 QAIEESAVQELGVEGR 452
Cdd:pfam03147  79 EKIVEALEKKFGAELR 94
PheT COG0072
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; ...
 346-450 1.05e-17

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


Pssm-ID: 439842 [Multi-domain]  Cd Length: 793  Bit Score: 85.99  E-value: 1.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 346 IVPHIWQKIKFQPLSRYPPLINDISFWLPsETYSKNDFYDLARTVGGDLIEKVVLVDEFTH---PETKKvSHCYRIIYRH 422
Cdd:COG0072   685 LLELARKVPKYKPISKFPAVRRDLALVVD-EDVPAADVLDAIRKAAGKLLEDVRLFDVYEGkgvPEGKK-SLAFSLTLQD 762

                          90       100
                  ....*....|....*....|....*...
gi 1803532212 423 PERTLTQDEVHRIHQAIEESAVQELGVE 450
Cdd:COG0072   763 PDRTLTDEEIDAAMDKIVAALEKKFGAE 790
pheT PRK00629
phenylalanyl-tRNA synthetase subunit beta; Reviewed
 353-450 9.16e-17

phenylalanyl-tRNA synthetase subunit beta; Reviewed


Pssm-ID: 234804 [Multi-domain]  Cd Length: 791  Bit Score: 82.91  E-value: 9.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 353 KIKFQPLSRYPPLINDISFWLPSETYSkNDFYDLARTVGGDLIEKVVLVDEFT---HPETKKvSHCYRIIYRHPERTLTQ 429
Cdd:PRK00629  690 LPKYKPISKFPAVRRDLALVVDEDVPA-ADILKAIKKAGGKLLESVELFDVYEgkgIGEGKK-SLAFRLTFQDPDRTLTD 767

                          90       100
                  ....*....|....*....|.
gi 1803532212 430 DEVHRIHQAIEESAVQELGVE 450
Cdd:PRK00629  768 EEINAAMDKIVAALEEKFGAE 788
PLN02853 PLN02853
Probable phenylalanyl-tRNA synthetase alpha chain
 127-334 4.61e-10

Probable phenylalanyl-tRNA synthetase alpha chain


Pssm-ID: 215458 [Multi-domain]  Cd Length: 492  Bit Score: 61.61  E-value: 4.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 127 NFDSLLIPQNHASRRKEDNYYLN-----------------------------------RD----HMLRAHTSAHQ----W 163
Cdd:PLN02853  254 NFDALFQPQQHPARDSHDTFFLKapattrqlpedyvervktvhesggygsigygydwkREeankNLLRTHTTAVSsrmlY 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 164 DLIHSGLDA--FLAVGDVYRRDTIDNSHYPVFHQMEGVrlfschelfsnIKDgEGLQLfeqGHrtahkqechtmeavrLV 241
Cdd:PLN02853  334 KLAQKGFKPkrYFSIDRVFRNEAVDRTHLAEFHQVEGL-----------VCD-RGLTL---GD---------------LI 383

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 242 EFnLKQVLTKL-MThifgdglQVRWVDCYFPFTHPSfeMEI---HFQ-GEWMEVLGCGVMEQQLVNSAGAQDK---IGWa 313
Cdd:PLN02853  384 GV-LEDFFSRLgMT-------KLRFKPAYNPYTEPS--MEIfsyHEGlKKWVEVGNSGMFRPEMLLPMGLPEDvnvIAW- 452

                         250       260
                  ....*....|....*....|..
gi 1803532212 314 fGLGLERLAMILYDIPDIR-LF 334
Cdd:PLN02853  453 -GLSLERPTMILYGIDNIRdLF 473
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 127-334 4.57e-09

phenylalanyl-tRNA synthetase alpha chain; Provisional


Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 58.44  E-value: 4.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 127 NFDSLLIPQNHASRRKEDNYYLNR-----------DHM------------------------------LRAHTSA----- 160
Cdd:PTZ00326  262 NFDALFQPQQHPARDAQDTFFLSKpetskvndlddDYVervkkvhevggygsigwrydwkleearkniLRTHTTAvsarm 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 161 -HQW--DLIHSGL---DAFLAVGDVYRRDTIDNSHYPVFHQMEGVrlfschelfsnIKDgEGLQLfeqGHrtahkqecht 234
Cdd:PTZ00326  342 lYKLaqEYKKTGPfkpKKYFSIDRVFRNETLDATHLAEFHQVEGF-----------VID-RNLTL---GD---------- 396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 235 meavrlvefnLKQVLTKLMTHIfgdGL-QVRWVDCYFPFTHPSfeMEI---HFQ-GEWMEVLGCGVMEQQLVNSAGAQDK 309
Cdd:PTZ00326  397 ----------LIGTIREFFRRI---GItKLRFKPAFNPYTEPS--MEIfgyHPGlKKWVEVGNSGIFRPEMLRPMGFPED 461

                         250       260
                  ....*....|....*....|....*....
gi 1803532212 310 ---IGWafGLGLERLAMILYDIPDIR-LF 334
Cdd:PTZ00326  462 vtvIAW--GLSLERPTMIKYGIKNIRdLF 488
syfB CHL00192
phenylalanyl-tRNA synthetase beta chain; Provisional
 354-452 8.79e-07

phenylalanyl-tRNA synthetase beta chain; Provisional


Pssm-ID: 214391 [Multi-domain]  Cd Length: 704  Bit Score: 51.24  E-value: 8.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803532212 354 IKFQPLSRYPPLINDISFWLPsETYSKNDFYDLARTVGGDLIEKVVLVDEFTH---PETKKvSHCYRIIYRHPERTLTQD 430
Cdd:CHL00192  604 ISYQPYSSYPKIIRDLSFIIK-KSISISKIKELIYQNGDNLLESITLFDYYKGksiPNGHT-SLGLRLTFQSENKTLTNE 681

                          90       100
                  ....*....|....*....|..
gi 1803532212 431 EVHRIHQAIEESAVQELGVEGR 452
Cdd:CHL00192  682 EIDRIQQNLQKVLEKKLNAEIR 703
 
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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