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Database: UniProt
Entry: A0A0V0TPT7_9BILA
LinkDB: A0A0V0TPT7_9BILA
Original site: A0A0V0TPT7_9BILA 
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}.
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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
//
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