ID M2Y3D3_GALSU Unreviewed; 614 AA.
AC M2Y3D3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN ORFNames=Gasu_22380 {ECO:0000313|EMBL:EME30329.1};
OS Galdieria sulphuraria (Red alga).
OC Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC Galdieria.
OX NCBI_TaxID=130081 {ECO:0000313|EMBL:EME30329.1, ECO:0000313|Proteomes:UP000030680};
RN [1] {ECO:0000313|Proteomes:UP000030680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX PubMed=23471408; DOI=10.1126/science.1231707;
RA Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA Lercher M.J., Weber A.P.;
RT "Gene transfer from bacteria and archaea facilitated evolution of an
RT extremophilic eukaryote.";
RL Science 339:1207-1210(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; KB454500; EME30329.1; -; Genomic_DNA.
DR RefSeq; XP_005706849.1; XM_005706792.1.
DR AlphaFoldDB; M2Y3D3; -.
DR STRING; 130081.M2Y3D3; -.
DR EnsemblPlants; EME30329; EME30329; Gasu_22380.
DR GeneID; 17089063; -.
DR Gramene; EME30329; EME30329; Gasu_22380.
DR KEGG; gsl:Gasu_22380; -.
DR eggNOG; KOG2472; Eukaryota.
DR OMA; FPGRCAN; -.
DR OrthoDB; 5473299at2759; -.
DR Proteomes; UP000030680; 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; 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 ECO:0000313|EMBL:EME30329.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EME30329.1};
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:UP000030680}.
FT DOMAIN 311..389
FT /note="B5"
FT /evidence="ECO:0000259|PROSITE:PS51483"
SQ SEQUENCE 614 AA; 70179 MW; 5E14BE6A0AE83211 CRC64;
MPTVTVDREL FLRSVPGIDS DEDVESICYE FGLEVDEVCY ETWTFGSRAR SGIEVTLPNE
DGKEEQHQVF KIEVPANRTD LLSADGIIKA LRVFRGIDKP LEFSSSLSSS PIRLIIKPAV
QKVRQYMLSA VIRGVVLNRL RYQSIIDFQE KLHQNICRQR SLVSIGLHDL DKVEPPFVYD
ALRPTEITFV PLGLDKEFRA DQLFEYYDRD PQLRKYTSLI RQFDRFPVVL DAKNRILSLP
PVINGDLSKV TLSTRNIFVD CTGTDWTKTQ MVIRTIVAII SQYCEEPFVE PVIIETMSVD
QSSQEMISPN MELHSFKLEL ERAKRMLGVD LLPDKAVELL NRMQLFATIE EDSRNSLHVQ
VPIHRDDILH TCDIIEDLAV AYGYDNLPER FPCTVTQGRL LGINMFSDLV RREGLAQQGF
TEVLTWVTVS QAENFDMMQR PDDGNTAVRI ANPKTLEFQS CRFSLLPGIL KTLRENRMVK
LPIRLFELSD TVHIQRDHEV GAVNRRSLCA VYCSSTAGFE LIHGLLEHIM KVVSLPNKAT
SKGSKYFWLD DKNCEDNAYF PGRRALIMFG EREIGVLGWI HPQVLQNFGL NNPCSALELD
IDLLFSLSNY FLKS
//
