ID A0A0V0S619_9BILA Unreviewed; 744 AA.
AC A0A0V0S619;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000256|ARBA:ARBA00015409};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN Name=farsa-b {ECO:0000313|EMBL:KRX21962.1};
GN ORFNames=T07_8403 {ECO:0000313|EMBL:KRX21962.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX21962.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX21962.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX21962.1};
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:KRX21962.1}.
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; JYDL01000035; KRX21962.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0S619; -.
DR STRING; 6336.A0A0V0S619; -.
DR Proteomes; UP000054630; 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:KRX21962.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630}.
FT DOMAIN 227..486
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 710..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..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; 85059 MW; 55A68F2573E65994 CRC64;
MEKNLADAVL VLLSQKSPID SDEIARHLNV SHQHIVGVIK SIEAMDHVIK TEQHSRKQWE
LTEEGKEIIK NGSHEAILWQ HVPNDGIIMD DLMRTVPNAK VGFNKAMSLG WIRLDKTGLK
PLVLRKVETI DDAVQDCLNK INTLNFDDVS DQNKSDLKKR 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 QFLVKMEIGL KGLTLITTEQ
GCTGVPFARA LAKKALLEKS YSKILVVTNL SDSVSVWQKI APDFHEIIHD LPIVEENFSN
AEYQEAMLNL LLENKSQGVD RRNLIIFENF SSSVLLMGTG GAVRFVHKLT SQHPCLVVGC
GSGTTVDENL ASFSCTIYTL RLSSCGKVAI AVKCKSPPGR NLWNFQITEQ FDFDHIQLYN
EKQQNGPDNW PLVDSSNRLE VPASLERLVG FRLSLNEQEM ADKRNLTLPY EKSGESEKSQ
ARIIYYAEKD DDIDEDDPDS DLNI
//
