ID E2A2Q0_CAMFO Unreviewed; 589 AA.
AC E2A2Q0;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000256|ARBA:ARBA00017032};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN ORFNames=EAG_08349 {ECO:0000313|EMBL:EFN72288.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN72288.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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; GL436195; EFN72288.1; -; Genomic_DNA.
DR RefSeq; XP_011250474.1; XM_011252172.2.
DR AlphaFoldDB; E2A2Q0; -.
DR STRING; 104421.E2A2Q0; -.
DR EnsemblMetazoa; XM_011252172.2; XP_011250474.1; LOC105247793.
DR GeneID; 105247793; -.
DR KEGG; cfo:105247793; -.
DR InParanoid; E2A2Q0; -.
DR OMA; FPGRCAN; -.
DR OrthoDB; 5473299at2759; -.
DR Proteomes; UP000000311; 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 ECO:0000313|EMBL:EFN72288.1}; 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:UP000000311}.
FT DOMAIN 301..377
FT /note="B5"
FT /evidence="ECO:0000259|PROSITE:PS51483"
SQ SEQUENCE 589 AA; 66422 MW; 2507E837E07C49C1 CRC64;
MPTIGIKRDL LFQALDKTYS DDEFQDLCFK FGLELDEVTT EKQMIAKEQG SSQEDASEDI
IYKIDIPANR YDLLCLESLS VGLLIFLNKI PIPHYKTIKS KTGIEKIVMS PECLKIRGHI
VAAILRNVTL TQDSYNSFID LQDKLHQNIG RKRSLVSIGT HDLDTIKGPF LYDAKPPTEI
CFKPLNQDKE YTGEGIMQLY ATHSQLKQYL PIIKDSPVYP VIYDSNGIIL SLPPIINGDH
SKITLNTKNI FIECTATDLT KARIAVDTIV CAFSQYCSKK YVAETVEVVY PDNQTFYYPS
LKYRVEEINC NKALNYIGIK QTPEQIAQLL SKMSLKSKVK DNDKLVVEIP PTRHDVIHLC
DIYEDIAIAY GYNEIEKTIP HMSTIAAEFP LNKLTDQIRI ELAEAGFTEA LTFSLCSRED
VADKLGYKIE DVPAVHISNP KTLEFQVART SLLPGLLKTI SANKKMPLPH KLFEVSDVVL
RDDKTEVGAR NNRRLCAVYA NKSAGFEIIH GLVDRILLLL EVPWSTNKDK SGYYLHAADD
PTFFPQRCAE IVCNGEVIGK MGVLHPNVLS KFELNVPCSA MEINIEPFL
//
