SYFB_HUMAN
ID SYFB_HUMAN Reviewed; 589 AA.
AC Q9NSD9; B4DFM0; O95708; Q4ZFX1; Q57ZJ5; Q9NZZ6;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Phenylalanine--tRNA ligase beta subunit;
DE EC=6.1.1.20 {ECO:0000269|PubMed:20223217};
DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit;
DE Short=PheRS;
GN Name=FARSB; Synonyms=FARSLB, FRSB; ORFNames=HSPC173;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-585.
RA Motegi H., Noda T., Shiba K.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-585.
RX PubMed=10049785; DOI=10.1006/bbrc.1999.0141;
RA Rodova M., Ankilova V., Safro M.G.;
RT "Human phenylalanyl-tRNA synthetase: cloning, characterization of the
RT deduced amino acid sequences in terms of the structural domains and
RT coordinately regulated expression of the alpha and beta subunits in chronic
RT myeloid leukemia cells.";
RL Biochem. Biophys. Res. Commun. 255:765-773(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-585.
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ILE-585.
RC TISSUE=Brain cortex;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-585.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-585.
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [11] {ECO:0007744|PDB:3L4G}
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBUNIT.
RX PubMed=20223217; DOI=10.1016/j.str.2010.01.002;
RA Finarov I., Moor N., Kessler N., Klipcan L., Safro M.G.;
RT "Structure of human cytosolic phenylalanyl-tRNA synthetase: evidence for
RT kingdom-specific design of the active sites and tRNA binding patterns.";
RL Structure 18:343-353(2010).
RN [12]
RP INVOLVEMENT IN RILDBC1, AND VARIANTS RILDBC1 ARG-76; SER-252; GLU-262;
RP GLN-305; GLN-401 AND PRO-461.
RX PubMed=29979980; DOI=10.1016/j.ajhg.2018.06.006;
RA Xu Z., Lo W.S., Beck D.B., Schuch L.A., Olahova M., Kopajtich R.,
RA Chong Y.E., Alston C.L., Seidl E., Zhai L., Lau C.F., Timchak D.,
RA LeDuc C.A., Borczuk A.C., Teich A.F., Juusola J., Sofeso C., Mueller C.,
RA Pierre G., Hilliard T., Turnpenny P.D., Wagner M., Kappler M., Brasch F.,
RA Bouffard J.P., Nangle L.A., Yang X.L., Zhang M., Taylor R.W., Prokisch H.,
RA Griese M., Chung W.K., Schimmel P.;
RT "Bi-allelic mutations in Phe-tRNA synthetase associated with a multi-system
RT pulmonary disease support non-translational function.";
RL Am. J. Hum. Genet. 103:100-114(2018).
RN [13]
RP INVOLVEMENT IN RILDBC1, AND VARIANT RILDBC1 MET-256.
RX PubMed=29573043; DOI=10.1002/humu.23424;
RA Antonellis A., Oprescu S.N., Griffin L.B., Heider A., Amalfitano A.,
RA Innis J.W.;
RT "Compound heterozygosity for loss-of-function FARSB variants in a patient
RT with classic features of recessive aminoacyl-tRNA synthetase-related
RT disease.";
RL Hum. Mutat. 39:834-840(2018).
RN [14]
RP VARIANT RILDBC1 LYS-285.
RX PubMed=30014610; DOI=10.1002/humu.23595;
RA Zadjali F., Al-Yahyaee A., Al-Nabhani M., Al-Mubaihsi S., Gujjar A.,
RA Raniga S., Al-Maawali A.;
RT "Homozygosity for FARSB mutation leads to Phe-tRNA synthetase-related
RT disease of growth restriction, brain calcification, and interstitial lung
RT disease.";
RL Hum. Mutat. 39:1355-1359(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) +
CC L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668,
CC Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20;
CC Evidence={ECO:0000269|PubMed:20223217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19414;
CC Evidence={ECO:0000305|PubMed:20223217};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A5K464};
CC -!- SUBUNIT: Heterotetramer; dimer of two heterodimers formed by FARSA and
CC FARSB. {ECO:0000269|PubMed:20223217}.
CC -!- INTERACTION:
CC Q9NSD9; P54253: ATXN1; NbExp=3; IntAct=EBI-353803, EBI-930964;
CC Q9NSD9; Q9Y285: FARSA; NbExp=7; IntAct=EBI-353803, EBI-725361;
CC Q9NSD9; P42858: HTT; NbExp=3; IntAct=EBI-353803, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:29573043}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NSD9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NSD9-2; Sequence=VSP_056866;
CC -!- DISEASE: Rajab interstitial lung disease with brain calcifications 1
CC (RILDBC1) [MIM:613658]: An autosomal recessive, lethal
CC neurodevelopmental disorder characterized by multiple clinical
CC manifestations including intrauterine growth restriction, failure to
CC thrive, developmental delay, hypotonia, interstitial lung disease, and
CC liver dysfunction. Brain imaging shows abnormal periventricular white
CC matter, basal ganglia echogenicity, cerebral volume loss, incomplete
CC closure of the Sylvian fissures, and normal myelination.
CC {ECO:0000269|PubMed:29573043, ECO:0000269|PubMed:29979980,
CC ECO:0000269|PubMed:30014610}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 2 subfamily. {ECO:0000305}.
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DR EMBL; D84430; BAA95608.1; -; mRNA.
DR EMBL; AF042346; AAD02220.1; -; mRNA.
DR EMBL; AF161521; AAF29136.1; -; mRNA.
DR EMBL; AK294158; BAG57481.1; -; mRNA.
DR EMBL; AC097461; AAX88958.1; -; Genomic_DNA.
DR EMBL; AC104772; AAX81986.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70804.1; -; Genomic_DNA.
DR EMBL; BC017783; AAH17783.1; -; mRNA.
DR CCDS; CCDS2454.1; -. [Q9NSD9-1]
DR RefSeq; NP_005678.3; NM_005687.4. [Q9NSD9-1]
DR RefSeq; XP_006712232.1; XM_006712169.2. [Q9NSD9-2]
DR RefSeq; XP_011508768.1; XM_011510466.2. [Q9NSD9-2]
DR RefSeq; XP_016858599.1; XM_017003110.1. [Q9NSD9-2]
DR PDB; 3L4G; X-ray; 3.30 A; B/D/F/H/J/L/N/P=1-589.
DR PDBsum; 3L4G; -.
DR AlphaFoldDB; Q9NSD9; -.
DR SMR; Q9NSD9; -.
DR BioGRID; 115367; 124.
DR ComplexPortal; CPX-2208; Phenylalanyl-tRNA synthetase complex.
DR DIP; DIP-32869N; -.
DR IntAct; Q9NSD9; 37.
DR MINT; Q9NSD9; -.
DR STRING; 9606.ENSP00000281828; -.
DR ChEMBL; CHEMBL4105969; -.
DR DrugBank; DB00120; Phenylalanine.
DR GlyGen; Q9NSD9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NSD9; -.
DR PhosphoSitePlus; Q9NSD9; -.
DR SwissPalm; Q9NSD9; -.
DR BioMuta; FARSB; -.
DR DMDM; 296452943; -.
DR EPD; Q9NSD9; -.
DR jPOST; Q9NSD9; -.
DR MassIVE; Q9NSD9; -.
DR MaxQB; Q9NSD9; -.
DR PaxDb; Q9NSD9; -.
DR PeptideAtlas; Q9NSD9; -.
DR PRIDE; Q9NSD9; -.
DR ProteomicsDB; 82538; -. [Q9NSD9-1]
DR ABCD; Q9NSD9; 1 sequenced antibody.
DR Antibodypedia; 34360; 291 antibodies from 29 providers.
DR DNASU; 10056; -.
DR Ensembl; ENST00000281828.8; ENSP00000281828.6; ENSG00000116120.11. [Q9NSD9-1]
DR GeneID; 10056; -.
DR KEGG; hsa:10056; -.
DR MANE-Select; ENST00000281828.8; ENSP00000281828.6; NM_005687.5; NP_005678.3.
DR UCSC; uc002vne.2; human. [Q9NSD9-1]
DR CTD; 10056; -.
DR DisGeNET; 10056; -.
DR GeneCards; FARSB; -.
DR HGNC; HGNC:17800; FARSB.
DR HPA; ENSG00000116120; Low tissue specificity.
DR MalaCards; FARSB; -.
DR MIM; 609690; gene.
DR MIM; 613658; phenotype.
DR neXtProt; NX_Q9NSD9; -.
DR OpenTargets; ENSG00000116120; -.
DR Orphanet; 178506; Brain calcification, Rajab type.
DR PharmGKB; PA162388068; -.
DR VEuPathDB; HostDB:ENSG00000116120; -.
DR eggNOG; KOG2472; Eukaryota.
DR GeneTree; ENSGT00530000063489; -.
DR HOGENOM; CLU_020279_2_0_1; -.
DR InParanoid; Q9NSD9; -.
DR OMA; FPGRCAN; -.
DR OrthoDB; 378921at2759; -.
DR PhylomeDB; Q9NSD9; -.
DR TreeFam; TF105681; -.
DR BRENDA; 6.1.1.20; 2681.
DR PathwayCommons; Q9NSD9; -.
DR Reactome; R-HSA-379716; Cytosolic tRNA aminoacylation.
DR SignaLink; Q9NSD9; -.
DR BioGRID-ORCS; 10056; 798 hits in 1084 CRISPR screens.
DR ChiTaRS; FARSB; human.
DR GeneWiki; FARSB; -.
DR GenomeRNAi; 10056; -.
DR Pharos; Q9NSD9; Tchem.
DR PRO; PR:Q9NSD9; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9NSD9; protein.
DR Bgee; ENSG00000116120; Expressed in left ventricle myocardium and 195 other tissues.
DR Genevisible; Q9NSD9; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0009328; C:phenylalanine-tRNA ligase complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IDA:UniProtKB.
DR GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR CDD; cd00769; PheRS_beta_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.50.40.10; -; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR005146; B3/B4_tRNA-bd.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR045060; Phe-tRNA-ligase_IIc_bsu.
DR InterPro; IPR004531; Phe-tRNA-synth_IIc_bsu_arc_euk.
DR InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
DR InterPro; IPR041616; PheRS_beta_core.
DR InterPro; IPR040659; PhetRS_B1.
DR InterPro; IPR005147; tRNA_synthase_B5-dom.
DR PANTHER; PTHR10947; PTHR10947; 1.
DR Pfam; PF03483; B3_4; 1.
DR Pfam; PF03484; B5; 1.
DR Pfam; PF18262; PhetRS_B1; 1.
DR Pfam; PF17759; tRNA_synthFbeta; 1.
DR SMART; SM00873; B3_4; 1.
DR SMART; SM00874; B5; 1.
DR SUPFAM; SSF46955; SSF46955; 2.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00471; pheT_arch; 1.
DR PROSITE; PS51483; B5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Aminoacyl-tRNA synthetase; ATP-binding;
KW Cytoplasm; Disease variant; Intellectual disability; Ligase; Magnesium;
KW Metal-binding; Neurodegeneration; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..589
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000127016"
FT DOMAIN 302..379
FT /note="B5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"
FT BINDING 357
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"
FT BINDING 363
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"
FT BINDING 366
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"
FT BINDING 367
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"
FT VAR_SEQ 1..99
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056866"
FT VARIANT 76
FT /note="C -> R (in RILDBC1; dbSNP:rs1419129874)"
FT /evidence="ECO:0000269|PubMed:29979980"
FT /id="VAR_081054"
FT VARIANT 252
FT /note="F -> S (in RILDBC1; dbSNP:rs1466642025)"
FT /evidence="ECO:0000269|PubMed:29979980"
FT /id="VAR_081055"
FT VARIANT 256
FT /note="T -> M (in RILDBC1; dbSNP:rs753710639)"
FT /evidence="ECO:0000269|PubMed:29573043"
FT /id="VAR_081056"
FT VARIANT 262
FT /note="K -> E (in RILDBC1; dbSNP:rs1553554543)"
FT /evidence="ECO:0000269|PubMed:29979980"
FT /id="VAR_081057"
FT VARIANT 285
FT /note="E -> K (in RILDBC1; dbSNP:rs767956337)"
FT /evidence="ECO:0000269|PubMed:30014610"
FT /id="VAR_081058"
FT VARIANT 305
FT /note="R -> Q (in RILDBC1; has no defect in protein
FT synthesis; dbSNP:rs773579570)"
FT /evidence="ECO:0000269|PubMed:29979980"
FT /id="VAR_081059"
FT VARIANT 401
FT /note="R -> Q (in RILDBC1; dbSNP:rs1553553086)"
FT /evidence="ECO:0000269|PubMed:29979980"
FT /id="VAR_081060"
FT VARIANT 461
FT /note="T -> P (in RILDBC1; dbSNP:rs1396171148)"
FT /evidence="ECO:0000269|PubMed:29979980"
FT /id="VAR_081061"
FT VARIANT 585
FT /note="V -> I (in dbSNP:rs7185)"
FT /evidence="ECO:0000269|PubMed:10049785,
FT ECO:0000269|PubMed:11042152, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1,
FT ECO:0000269|Ref.6"
FT /id="VAR_071245"
FT CONFLICT 281
FT /note="Q -> R (in Ref. 3; AAF29136)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="G -> V (in Ref. 1; BAA95608)"
FT /evidence="ECO:0000305"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 8..15
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 23..30
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 41..45
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 56..66
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 77..87
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:3L4G"
FT TURN 112..117
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 133..145
FT /evidence="ECO:0007829|PDB:3L4G"
FT TURN 146..155
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 194..200
FT /evidence="ECO:0007829|PDB:3L4G"
FT TURN 205..214
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:3L4G"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 251..258
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 260..274
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 305..310
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 311..318
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 324..333
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 342..351
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 361..372
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 392..406
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 420..423
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 438..441
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 445..447
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 455..464
FT /evidence="ECO:0007829|PDB:3L4G"
FT TURN 465..467
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 472..483
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 490..505
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 508..521
FT /evidence="ECO:0007829|PDB:3L4G"
FT TURN 528..531
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 532..537
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 543..553
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 556..564
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 566..571
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 578..584
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 586..588
FT /evidence="ECO:0007829|PDB:3L4G"
SQ SEQUENCE 589 AA; 66116 MW; 6425BA46D124BC08 CRC64;
MPTVSVKRDL LFQALGRTYT DEEFDELCFE FGLELDEITS EKEIISKEQG NVKAAGASDV
VLYKIDVPAN RYDLLCLEGL VRGLQVFKER IKAPVYKRVM PDGKIQKLII TEETAKIRPF
AVAAVLRNIK FTKDRYDSFI ELQEKLHQNI CRKRALVAIG THDLDTLSGP FTYTAKRPSD
IKFKPLNKTK EYTACELMNI YKTDNHLKHY LHIIENKPLY PVIYDSNGVV LSMPPIINGD
HSRITVNTRN IFIECTGTDF TKAKIVLDII VTMFSEYCEN QFTVEAAEVV FPNGKSHTFP
ELAYRKEMVR ADLINKKVGI RETPENLAKL LTRMYLKSEV IGDGNQIEIE IPPTRADIIH
ACDIVEDAAI AYGYNNIQMT LPKTYTIANQ FPLNKLTELL RHDMAAAGFT EALTFALCSQ
EDIADKLGVD ISATKAVHIS NPKTAEFQVA RTTLLPGLLK TIAANRKMPL PLKLFEISDI
VIKDSNTDVG AKNYRHLCAV YYNKNPGFEI IHGLLDRIMQ LLDVPPGEDK GGYVIKASEG
PAFFPGRCAE IFARGQSVGK LGVLHPDVIT KFELTMPCSS LEINVGPFL
