ID A0A022Q8R2_ERYGU Unreviewed; 896 AA.
AC A0A022Q8R2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN ORFNames=MIMGU_mgv1a001070mg {ECO:0000313|EMBL:EYU23959.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU23959.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU23959.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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; KI632147; EYU23959.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A022Q8R2; -.
DR STRING; 4155.A0A022Q8R2; -.
DR eggNOG; KOG2472; Eukaryota.
DR Proteomes; UP000030748; 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; IPR005174; DUF295.
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; PF03478; DUF295; 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:UP000030748}.
FT DOMAIN 607..687
FT /note="B5"
FT /evidence="ECO:0000259|PROSITE:PS51483"
SQ SEQUENCE 896 AA; 102102 MW; 5362A8142F9D9DD6 CRC64;
MALSLISRRS SYRNWISNTA QKKASAYGVE PWLMIKDGCG EEDGVDMFYS VAENQGLRVR
GEDGAVVGSS HGWVALCKWQ RVREGCFRMF LHNPLFRHCV NLPRVKTLSN PNPNPNPNPN
PKIISSKHEL YKPRKVILSN DQAGWNKSCR AIMSYGPQDR LAYCCPDFSK KWIHIGVNYK
YDDFVYSSKR EKLFCVTKFG MLESWDLEDR FSPKMNWNWK MTRMTDDEEE KKYLVFAELS
NRLFLVRHNA IGFDVDEIIE TEGELRRMDG TLDGMTFFIG STGHGFVVEG MDHHQMKKMN
LLPDSIYFTD TKELVNPDNK SEEEFDDLCF KFGIELDDVT TEKAILRKEK HLDEEKPSED
EEVIYKIEVP ANRYDLLCLE GLAQALRIFE GLDPIPTYSL ANISQESMLK MHVKSETSKI
RPYVVCAVLR GVTFDEARYN SFIDLQDRLH QNICRRRTLV AIGTHDLDTI EGPFTYEALP
PPEINFIPLK QTKNFRADEL MQFYKSDMKL KKFLHIIENS PVFPVIYDRS RTVLSLPPII
NGAHSAISLK TKNVFIECTA TDLTKANIVL NTMVTMFSVY CERKFEVEPV EVIYDDGKSY
ISPDLSLYQM MVMVNLSYIS STIGVSLPAH EVARSLNKMQ LHAKHSVLEN NETGFTISVP
PTRSDILHPI DVAEDFGISY GYNEIPKKKF PSVKPQILNQ FTDLIKEEIA MAGYTEVLLF
ILCSYKENFT MLNRKDDKST AVINGNPRTA EFEVSRTSLM NGILKSIGHN KDHPKPIKIF
EVGDVVLLDE TKDVGASNRR HLAAVYCGVA SGFELIHGLV DRVMEVTGNP FVSPGDKTGY
YILSSNEPEF LPGRQASIIY KGKQVGTFGI VHPQVLDNFG IPDPCSYMEV DIESFL
//
