ID A0A0V0TPT7_9BILA Unreviewed; 744 AA.
AC A0A0V0TPT7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000256|ARBA:ARBA00015409};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000256|ARBA:ARBA00030612};
GN Name=farsa-b {ECO:0000313|EMBL:KRX41034.1};
GN ORFNames=T05_1973 {ECO:0000313|EMBL:KRX41034.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX41034.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX41034.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX41034.1};
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:KRX41034.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDJ01000182; KRX41034.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0TPT7; -.
DR Proteomes; UP000055048; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:KRX41034.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000055048}.
FT DOMAIN 227..460
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 709..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..729
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..744
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 744 AA; 84939 MW; 8C58748D2BBCFD1C CRC64;
MEKNLADAVL VLLSQKSPID SDEIARHLNV SHQHIVGVIK SIEAMDHVIK TEQHSRKQWE
LTEEGKEIIK NGSHEAILWQ HVPNDGIIMD DLMRTVPNAK VGFNKAMSLG WIRLDKTGPK
PLVLRKVETI DDAVQDCLNK 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 VIAWGLSLER QVCMKMEIGL KGLTLITTEQ
GCTGVPFARA LAKKALLEKS YSKILVVTNL SDSVSVWQKI APDSHEIIHD LPIVEENFSN
AEYQEAMLNL LLENKSQGVD RRNLIIFENF SSSMLLMGTG GAVRFVHKLT SQHPCLVVGC
GSGTTVDENL ASFACTIYTL RLSSCGKVVI AVKCKSPPGR NLWNFQITDQ FDFDHVQLYN
EKQQNGPDNW PHVDSSNRLE VPASLERLVG FRLSLNEQEM ADKRNLTLPY EKSGESEKSQ
ARIIYYAEKD DDIDEDDPDS DLNI
//