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Database: UniProt
Entry: A0A183IV58_9BILA
LinkDB: A0A183IV58_9BILA
Original site: A0A183IV58_9BILA 
ID   A0A183IV58_9BILA        Unreviewed;       386 AA.
AC   A0A183IV58;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   13-SEP-2023, entry version 22.
DE   RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE            EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN   ORFNames=SBAD_LOCUS7505 {ECO:0000313|EMBL:VDP13344.1};
OS   Soboliphyme baturini.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Dioctophymatida; Dioctophymatoidea; Soboliphymatidae; Soboliphyme.
OX   NCBI_TaxID=241478 {ECO:0000313|Proteomes:UP000050793, ECO:0000313|WBParaSite:SBAD_0000779001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SBAD_0000779001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDP13344.1, ECO:0000313|Proteomes:UP000270296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) +
CC         L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668,
CC         Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20;
CC         Evidence={ECO:0000256|ARBA:ARBA00000395};
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DR   EMBL; UZAM01010687; VDP13344.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A183IV58; -.
DR   WBParaSite; SBAD_0000779001-mRNA-1; SBAD_0000779001-mRNA-1; SBAD_0000779001.
DR   Proteomes; UP000050793; Unplaced.
DR   Proteomes; UP000270296; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00496; PheRS_alpha_core; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004530; Phe-tRNA-synth_IIc_mito.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   NCBIfam; TIGR00469; pheS_mito; 1.
DR   PANTHER; PTHR11538:SF41; PHENYLALANINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF01409; tRNA-synt_2d; 2.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000270296}.
FT   DOMAIN          157..373
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   386 AA;  45078 MW;  760FCE1ED9CA3F23 CRC64;
     MFFSGLRRCI LNYAFYCTVS ATLKSKPIRP TSVNVLEREY FTDKTYNIPP WILSLIGRNL
     LSVDGSPLRL LKLKIQDFID KVYLDDDNKP VFKFFENTNP VVSTKQNFDN LLIPRNHPCR
     ALSDTYYISS EYLLRTHTSA HQCELIASGY DQFLIAGDVY RRDQIDRNHF PCFHQLEGVY
     LTKVPELRRL LSNRLRQSAA DTILPVENPP KQECHSDDCY HLLQQHLKQC LEGLVRHLFG
     DDIVFRWISS YFPFTYPSWE IEIFHRDSWL EILGCGIVQQ QILVNAQFPD KVGWAFGLGL
     ERLAMVLYGI PDIRLFWSTD SGFSSQFVGL DFRKSYKYKV GITISDLCSV VRFEFYIQLC
     QYFAFSLYKM VYPEKLPVTR VSEMSS
//
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