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Database: UniProt
Entry: A0A0V1CS92_TRIBR
LinkDB: A0A0V1CS92_TRIBR
Original site: A0A0V1CS92_TRIBR 
ID   A0A0V1CS92_TRIBR        Unreviewed;       756 AA.
AC   A0A0V1CS92;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000256|ARBA:ARBA00015409};
DE            EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
DE   Flags: Fragment;
GN   Name=farsa-b {ECO:0000313|EMBL:KRY52038.1};
GN   ORFNames=T03_17420 {ECO:0000313|EMBL:KRY52038.1};
OS   Trichinella britovi (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY52038.1, ECO:0000313|Proteomes:UP000054653};
RN   [1] {ECO:0000313|EMBL:KRY52038.1, ECO:0000313|Proteomes:UP000054653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS120 {ECO:0000313|EMBL:KRY52038.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Phe-tRNA synthetase alpha subunit type 2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00006703}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRY52038.1}.
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DR   EMBL; JYDI01000112; KRY52038.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1CS92; -.
DR   STRING; 45882.A0A0V1CS92; -.
DR   Proteomes; UP000054653; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   Gene3D; 1.10.10.2320; -; 1.
DR   Gene3D; 1.10.10.2330; -; 1.
DR   Gene3D; 3.30.1370.240; -; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   InterPro; IPR040724; PheRS_DBD1.
DR   InterPro; IPR040586; PheRS_DBD2.
DR   InterPro; IPR040725; PheRS_DBD3.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   NCBIfam; TIGR00468; pheS; 1.
DR   PANTHER; PTHR11538:SF40; PHENYLALANINE--TRNA LIGASE ALPHA SUBUNIT; 1.
DR   PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF18552; PheRS_DBD1; 1.
DR   Pfam; PF18554; PheRS_DBD2; 1.
DR   Pfam; PF18553; PheRS_DBD3; 1.
DR   Pfam; PF01409; tRNA-synt_2d; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Ligase {ECO:0000313|EMBL:KRY52038.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054653}.
FT   DOMAIN          227..498
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          721..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        721..741
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        742..756
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         756
FT                   /evidence="ECO:0000313|EMBL:KRY52038.1"
SQ   SEQUENCE   756 AA;  86283 MW;  095C384D2A86E349 CRC64;
     MEKNLADAVL VLLSQKSPID SDEIARHLNV SHQHIVGVIK SIEAMDHVIK TEQHSRKQWE
     LTEEGKEIIK NGSHEAILWQ HVPNDGIIMD DLMRTVPNAK VGFNKAMSLG WIRLDKTGPK
     PLVLRKVETI DDAVHDCLNK INSLNFDDVS AQNKSDLKKR RLINEIVIKT FRVFRDEKFT
     TSLVKEETDL TVDLLTDNLW KEKKFKPYNF NAFGVVPVRG YLHPLMKVRT EFRQIFLEMG
     FTEMPTQRYV ESSFWNFDAL FQPQQHPARD EQDTFFISKP MCTKNLPSEY VKRVEKVHSV
     GDYGSSGYGY EWKIEEAEKN VLRTHTTASS IRMLYEIAKK PFKPVRYFSI DRVFRNESLD
     ATHLAEFHQV EGLIAGENLS LGHLMGILQE FYKRLGIEKL RFKPAYNPYT EPSMEIFSYH
     SSLKKWVEIG NSGMFRPEVL LPLGLAENVT VIAPTMIKYG INNIRDLIGP RHVCRVKMEI
     GLKGLTLITT EQGCTGVPFA RALAKKALLE KSYSKILVVT NLSDSVSVWQ KIAPDSHEII
     HDLPIVEENF SNAEYQEAML NLLLENKSQG VDRRNLIIFE NFSSSMLLMG TGGAVRFVHK
     LTSQHPCLVI GCGSGTTVDE NLASFACTIY TLRLSSCGKV VIAVKCKSPP GRNLWNFQIT
     DQFDFDHVQL YNEKQQNGPD NWPLVDSSNR LEVPASLERL VGFRLSLNEQ EMADKRNLTL
     PYEKSGESEK SQARIIYYAE KDDDIDEDDP DSDLNI
//
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