ID A0A2K5CXS0_AOTNA Unreviewed; 587 AA.
AC A0A2K5CXS0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000256|ARBA:ARBA00017032};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN Name=FARSB {ECO:0000313|Ensembl:ENSANAP00000013484.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000013484.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000013484.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A2K5CXS0; -.
DR Ensembl; ENSANAT00000031311.1; ENSANAP00000013484.1; ENSANAG00000024637.1.
DR GeneTree; ENSGT00530000063489; -.
DR Proteomes; UP000233020; Unplaced.
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; 1.
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:UP000233020}.
FT DOMAIN 300..377
FT /note="B5"
FT /evidence="ECO:0000259|PROSITE:PS51483"
SQ SEQUENCE 587 AA; 65737 MW; 4B8145A96F723533 CRC64;
MPTVSVKRDL LFQALGRTYS ECRPCTLGPT PLLGGWTSEK EIISKEQGSV KAAGASDVVL
YKIDVPANRY DLLCLEGLVR GLQVFKERIK PPAYKRVMPD GKIQKLIITE ETAKIRPFAA
AAVLRNIKFT KDRYDSFIEL QEKLHQNICR KRALVAIGTH DLDTLSGPFT YTAKRPSDIK
FKPLNKTKEY TACELMNIYK TDNHLKQYLH IIENKPLYPV ICDSNGVVLS MPPIINGDHS
RITVNTRNVF IECTGTDFTK AKIVLDIIVT MFSEYCEKQF TVEAAEVVFP NGKSYTFPEL
AYRKEIVRAD LINKKVGIRE TPENLAKLLT RMYLKSEVIG DGNQIEIEIP PTRADIMHAC
DIVEDAAIAY GYNNIQMTLP KTYTIANQFP LNKLTELLRH DMAAAGFTEV LTFALCSQED
IADKLGVDIS ATKAVHISNP KTAEFQVART TLLPGLLKTI AANRKMPLPL KLFEISDIVI
KDSNTDVGAK NYRHLCAVYY NKNPGFEIIH GLLDRIMQLL DVPPGEDKEG YVIRASEGPA
FFPGRCAEIF ARGQSIGKLG VLHPDVITKF ELTMPCSSLE INIEPFL
//