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Database: UniProt/TrEMBL
Entry: D8GSA4_CLOLD
LinkDB: D8GSA4_CLOLD
Original site: D8GSA4_CLOLD 
ID   D8GSA4_CLOLD            Unreviewed;       793 AA.
AC   D8GSA4;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   11-JUN-2014, entry version 27.
DE   RecName: Full=Phenylalanine--tRNA ligase beta subunit;
DE            EC=6.1.1.20;
DE   AltName: Full=Phenylalanyl-tRNA synthetase beta subunit;
GN   Name=pheT; OrderedLocusNames=CLJU_c34410;
OS   Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=748727;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55383 / DSM 13528 / PETC;
RX   PubMed=20616070; DOI=10.1073/pnas.1004716107;
RA   Kopke M., Held C., Hujer S., Liesegang H., Wiezer A., Wollherr A.,
RA   Ehrenreich A., Liebl W., Gottschalk G., Durre P.;
RT   "Clostridium ljungdahlii represents a microbial production platform
RT   based on syngas.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:13087-13092(2010).
CC   -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP +
CC       diphosphate + L-phenylalanyl-tRNA(Phe).
CC   -!- COFACTOR: Binds 2 magnesium ions per tetramer (By similarity).
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta
CC       subunit family. Type 1 subfamily.
CC   -!- SIMILARITY: Contains 1 B5 domain.
CC   -!- SIMILARITY: Contains 1 FDX-ACB domain.
CC   -!- SIMILARITY: Contains 1 tRNA-binding domain.
CC   -!- SIMILARITY: Contains B5 domain.
CC   -!- SIMILARITY: Contains Bdomain.
CC   -!- SIMILARITY: Contains FDX-ACB domain.
CC   -!- SIMILARITY: Contains tRNA-binding domain.
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DR   EMBL; CP001666; ADK16486.1; -; Genomic_DNA.
DR   RefSeq; YP_003781588.1; NC_014328.1.
DR   EnsemblBacteria; ADK16486; ADK16486; CLJU_c34410.
DR   GeneID; 9447057; -.
DR   KEGG; clj:CLJU_c34410; -.
DR   PATRIC; 42488257; VBICloLju82977_3486.
DR   HOGENOM; HOG000292087; -.
DR   KO; K01890; -.
DR   OMA; RTSCDET; -.
DR   BioCyc; CLJU748727:GHMO-3440-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008033; P:tRNA processing; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.56.20; -; 1.
DR   Gene3D; 3.30.70.380; -; 1.
DR   Gene3D; 3.50.40.10; -; 1.
DR   HAMAP; MF_00283; Phe_tRNA_synth_beta1; 1.
DR   InterPro; IPR005146; B3/B4_tRNA-bd.
DR   InterPro; IPR009061; DNA-bd_dom_put.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004532; Phe-tRNA-ligase_IIc_bsu.
DR   InterPro; IPR020825; Phe-tRNA_synthase_B3/B4.
DR   InterPro; IPR005121; PheS_beta_Fdx_antiC-bd.
DR   InterPro; IPR002547; tRNA-bd_dom.
DR   InterPro; IPR005147; tRNA_synthase_B5-dom.
DR   Pfam; PF03483; B3_4; 1.
DR   Pfam; PF03484; B5; 1.
DR   Pfam; PF03147; FDX-ACB; 1.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   SMART; SM00873; B3_4; 1.
DR   SMART; SM00874; B5; 1.
DR   SMART; SM00896; FDX-ACB; 1.
DR   SUPFAM; SSF46955; SSF46955; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF54991; SSF54991; 1.
DR   SUPFAM; SSF56037; SSF56037; 1.
DR   TIGRFAMs; TIGR00472; pheT_bact; 1.
DR   PROSITE; PS51483; B5; 1.
DR   PROSITE; PS51447; FDX_ACB; 1.
DR   PROSITE; PS50886; TRBD; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Protein biosynthesis; RNA-binding; tRNA-binding.
FT   DOMAIN       39    150       tRNA-binding (By similarity).
FT   DOMAIN      404    479       B5 (By similarity).
FT   DOMAIN      699    792       FDX-ACB (By similarity).
FT   METAL       457    457       Magnesium (By similarity){EA3}.
FT   METAL       463    463       Magnesium; via carbonyl oxygen (By
FT                                similarity){EA3}.
FT   METAL       466    466       Magnesium (By similarity){EA3}.
FT   METAL       467    467       Magnesium (By similarity){EA3}.
SQ   SEQUENCE   793 AA;  89026 MW;  BCBD493EC822D432 CRC64;
     MKVPVKWLKD YVKIDIPGKE LGDRLTLSGS KLEEAIVTGD EIQNVVTGKI MKIESHPQAD
     KLVVCQVDIG KEEPIQIITA ATNMKEQDIV PVALHDSTLH GGVKIKKGKL RGLMSNGMFC
     SEEELGIAGD KPVYGLMILK EDTPIGKDIK EVLDMTSTIL DFEITSNRPD CLSIIGMARE
     TAATLNESYK IPELDYKPSC SENIQDTLKV EIKDKLCKRY MARGIKDVKI EPSPSWMQER
     LLEAGVRPIN NIVDITNFVM LEIGEPMHAY DVREIKSGTI VVDTAKDGEK FTTLDEEERQ
     LNQDMLTIRD GDRTIGLAGI MGGLNSEIRD DTSSIVFECA NFDGTNIRVS SQKLALRTEA
     SGRFEKDLDP NLAEIAMNRA CNLVEMLKAG KVMEGTIDVY DEKIEPHSVD VDSNWVNKFL
     GTEIPKENMV DYLNRLELKT QLKGDILHID VPTFRGDINI REDVAEEVAR IYGYSNVPTT
     VIESVSTRGG KNPKQKLDDK LVETLISSGL NQSISYSFVS RKVFDKILLP EDSKLRNAIA
     IKNPLGEDYS IMRTTTLASM MECLGRNYSR KNEIVRLFEI GRVYLPLENG DTLPEEDNIV
     TIGMYGECDY FNLKGIVENI LDTLGIEKIS FKRESDNPTF HPGRTAALYV NRKLAGVLGE
     IHPTVCENYG IDERCYIAEL NLDVLYEHAD SDKKYRPLPK FPAVSRDLAV LVDDNIMVQE
     VEDIIRKQGG NILEKVKLFD VYRGKQIESG KKSIAYSISY RAENKTLTDK EVNKVHSKII
     RSLEHNLGAQ LRQ
//
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