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Database: UniProt
Entry: A0A093R3J0_PHACA
LinkDB: A0A093R3J0_PHACA
Original site: A0A093R3J0_PHACA 
ID   A0A093R3J0_PHACA        Unreviewed;       569 AA.
AC   A0A093R3J0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000256|ARBA:ARBA00017032};
DE            EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
DE   Flags: Fragment;
GN   ORFNames=N336_05345 {ECO:0000313|EMBL:KFW95366.1};
OS   Phalacrocorax carbo (Great cormorant) (Pelecanus carbo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Suliformes; Phalacrocoracidae;
OC   Phalacrocorax.
OX   NCBI_TaxID=9209 {ECO:0000313|EMBL:KFW95366.1, ECO:0000313|Proteomes:UP000053238};
RN   [1] {ECO:0000313|EMBL:KFW95366.1, ECO:0000313|Proteomes:UP000053238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N336 {ECO:0000313|EMBL:KFW95366.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KL445625; KFW95366.1; -; Genomic_DNA.
DR   RefSeq; XP_009511129.1; XM_009512834.1.
DR   AlphaFoldDB; A0A093R3J0; -.
DR   GeneID; 104051721; -.
DR   KEGG; pcao:104051721; -.
DR   CTD; 10056; -.
DR   OrthoDB; 5473299at2759; -.
DR   Proteomes; UP000053238; 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; 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, ECO:0000313|EMBL:KFW95366.1};
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:UP000053238}.
FT   DOMAIN          283..360
FT                   /note="B5"
FT                   /evidence="ECO:0000259|PROSITE:PS51483"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFW95366.1"
FT   NON_TER         569
FT                   /evidence="ECO:0000313|EMBL:KFW95366.1"
SQ   SEQUENCE   569 AA;  63737 MW;  4554CEFB8F97456D CRC64;
     DEEFNELCFE FGLELDEVTS EKDIISKEKG EEKAKGASDT VLYKIDVPAN RYDLLCLEGL
     VRGLQVFKER INLPRYEKII PAQGEGQRLI ITEETVQVRP HAVAAVLRNI TFTKERYDSF
     IDLQEKLHQN ICRRRALVAI GTHDLDTISG PFTFTAKAPS EIKFKPLNQS QEYTASQIMD
     LYRTDSHLRH YLHLIENKPL YPVIYDSKGV VLSMPPIING DHTKISVNTR NVFVECTGTD
     ITKAKIVLDI IVTMFSEYCE KPFSVEAAEV VYPNGKTHIY PELAYRKEKV KPELINKKIG
     ISETPSSLAK LLTRMCLKSH VIGNGNNIEI EIPPTRADII HACDIVEDAA IAYGYNNIQM
     TIPKTYTIAN QLPLNKLTEL LRLDVAAAGF TEALTFALCS QEDIADKLGM DISATKAVRI
     ANPKTAEFQV ARTTLLPGLL KTIAANRKMP LPLKLFEISD VVVKDPNTDV GARNYRHFCA
     VYYNKSPGFE IIHGLLDRVM QLLEVPPNEE NGYTIKATEG SAFFPGRCAE IFAKGQSVGK
     LGVLHPDVIT KFELTMPCSA LEINIEPFM
//
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