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Database: UniProt
Entry: A8WNF7_CAEBR
LinkDB: A8WNF7_CAEBR
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ID   A8WNF7_CAEBR            Unreviewed;       591 AA.
AC   A8WNF7;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000256|ARBA:ARBA00017032};
DE            EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN   Name=fars-3 {ECO:0000313|WormBase:CBG00621};
GN   Synonyms=Cbr-fars-3 {ECO:0000313|EMBL:CAP22011.1};
GN   ORFNames=CBG00621 {ECO:0000313|WormBase:CBG00621}, CBG_00621
GN   {ECO:0000313|EMBL:CAP22011.1};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP22011.1, ECO:0000313|Proteomes:UP000008549};
RN   [1] {ECO:0000313|EMBL:CAP22011.1, ECO:0000313|Proteomes:UP000008549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000313|EMBL:CAP22011.1,
RC   ECO:0000313|Proteomes:UP000008549};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC       family. Type 2 subfamily. {ECO:0000256|ARBA:ARBA00007438}.
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DR   EMBL; HE600999; CAP22011.1; -; Genomic_DNA.
DR   RefSeq; XP_002630211.1; XM_002630165.1.
DR   AlphaFoldDB; A8WNF7; -.
DR   STRING; 6238.A8WNF7; -.
DR   EnsemblMetazoa; CBG00621.1; CBG00621.1; WBGene00023990.
DR   GeneID; 8571726; -.
DR   KEGG; cbr:CBG_00621; -.
DR   CTD; 8571726; -.
DR   WormBase; CBG00621; CBP00180; WBGene00023990; Cbr-fars-3.
DR   eggNOG; KOG2472; Eukaryota.
DR   HOGENOM; CLU_020279_2_0_1; -.
DR   InParanoid; A8WNF7; -.
DR   OMA; FPGRCAN; -.
DR   OrthoDB; 5473299at2759; -.
DR   Proteomes; UP000008549; Unassembled WGS sequence.
DR   GO; GO:0009328; C:phenylalanine-tRNA ligase complex; IBA:GO_Central.
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; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd00769; PheRS_beta_core; 1.
DR   Gene3D; 3.30.56.10; -; 2.
DR   Gene3D; 3.50.40.10; Phenylalanyl-trna Synthetase, Chain B, domain 3; 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   NCBIfam; TIGR00471; pheT_arch; 1.
DR   PANTHER; PTHR10947:SF0; PHENYLALANINE--TRNA LIGASE BETA SUBUNIT; 1.
DR   PANTHER; PTHR10947; PHENYLALANYL-TRNA SYNTHETASE BETA CHAIN AND LEUCINE-RICH REPEAT-CONTAINING PROTEIN 47; 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; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF56037; PheT/TilS domain; 1.
DR   SUPFAM; SSF46955; Putative DNA-binding domain; 2.
DR   PROSITE; PS51483; B5; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008549}.
FT   DOMAIN          304..380
FT                   /note="B5"
FT                   /evidence="ECO:0000259|PROSITE:PS51483"
SQ   SEQUENCE   591 AA;  66136 MW;  8DB73179C60F4711 CRC64;
     MPTVGIKKVI LDKHFNRNYT EKEFDELCFE YGLELDEITS EKAAVEKERG TDAAVDLNDQ
     EVYKIDIPAN RYDLLSVEGL ARAIRIFKQE IPSPQYKFAD VPKSGLQKII VKKETAQVRP
     FVVGAVLRNI SFDADSYASF IDLQDKLHQN ICRKRTLVAI GTHDLDTVQG PFEYRAEAPK
     DIKFKPLNQT KEYTAEELMT LYSSDSHLKA YLPIIQNHPV YPVIYDKNGV VCSMPPIING
     EHSKITLNTK NVFIEATATD KQKAFVVLDT IVTLFSQYCA KPFTVEQVEV VYEETGVKEV
     YPLLAYREMT VTTPEINTKI GIQLKEEEMA TLLNKMSLKA EVVGKETLKV VVPPTRHDIL
     HACDVAEDVG VAYGYNNLVT RLPESNTVAV AFPINKLCDN LRIEIAAAGW TEALNFALCS
     RDDISTKLRQ PEALSHAVHI GNPKTLEFQV ARTSLLPGLL KTLASNRDMP LPLKLFELQD
     VIVKDSTMDV GARNERRLAA VYYNKAAGFE IIQGFLDRMM RMLNVNPAKA DNGYYIEADE
     NPTYFPGRCA KIIGPKGVVL GHIGALHPEV ITSFGLTLPC GAVEFNVEPF L
//
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