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Database: UniProt
Entry: A0A369RYN4_9METZ
LinkDB: A0A369RYN4_9METZ
Original site: A0A369RYN4_9METZ 
ID   A0A369RYN4_9METZ        Unreviewed;       623 AA.
AC   A0A369RYN4;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000256|ARBA:ARBA00017032};
DE            EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN   ORFNames=TrispH2_009143 {ECO:0000313|EMBL:RDD39569.1};
OS   Trichoplax sp. H2.
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=287889 {ECO:0000313|EMBL:RDD39569.1, ECO:0000313|Proteomes:UP000253843};
RN   [1] {ECO:0000313|EMBL:RDD39569.1, ECO:0000313|Proteomes:UP000253843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Panama {ECO:0000313|EMBL:RDD39569.1,
RC   ECO:0000313|Proteomes:UP000253843};
RC   TISSUE=Whole clonal animals {ECO:0000313|EMBL:RDD39569.1};
RX   PubMed=30042472; DOI=10.1038/s41598-018-29400-y;
RA   Kamm K., Osigus H.J., Stadler P.F., DeSalle R., Schierwater B.;
RT   "Trichoplax genomes reveal profound admixture and suggest stable wild
RT   populations without bisexual reproduction.";
RL   Sci. Rep. 8:11168-11168(2018).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RDD39569.1}.
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DR   EMBL; NOWV01000130; RDD39569.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369RYN4; -.
DR   STRING; 287889.A0A369RYN4; -.
DR   Proteomes; UP000253843; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; IEA:InterPro.
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, ECO:0000313|EMBL:RDD39569.1};
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:UP000253843}.
FT   DOMAIN          318..396
FT                   /note="B5"
FT                   /evidence="ECO:0000259|PROSITE:PS51483"
SQ   SEQUENCE   623 AA;  70009 MW;  23E9445E55D14DFC CRC64;
     MPIINIKRDL LFKALQKEYT DDKFAEVCFE YGIELDEVTS EKDIIAREQG EDKAANASED
     VIYKIEIPAN RYDLLCIEGL VRSLQIFFEI VPSPTFTKII PENREKLYIK PATAKVRPHC
     VAAILRNVTL TSDTYSSMID LQEKLHQNIC RRRALVAIGL HNLDTVQGPF YYDAKAPEDI
     KFKPLNKDKE YTAAELMELY KSDGHLKHYL HIIKDKPVYP IIYDSNGVVL SMPPIINGEH
     TKLSTNTRNI FIDVTATDLT KASRLSFSSG IFSITALTAK IVLDTLVTMI SEHCGQKYSA
     EVVDVIQPDG KVVTYPELTT RHEIISLKDV YSLAGISLDT EKIAKLLTRM SLSTTVINEK
     EVKVEVPPTR HDIHIAIAYG YNNIPRSMPK SSTIAQEFPI NKLSNLLRQE IAQAGFTEAL
     TFTLCSRDDV SEKLNKNLAS SKATHISNPK TQEFQVVRTT LLPGLLKTVA SNRSMSLPLR
     LFEIADVVIK DDKTGNYKYY GYCCCMFKKI NDSDSILMFV EDTGARNERR LCALYYNKSP
     GFEIIHGLAD RSMQLLGIPF GKSDKGYYIK GADDPLYFPG RGADIIVHGN RIGSLGVLHP
     DVISKFDLNM PCSALECNIT DFL
//
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