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Database: UniProt
Entry: A0A0V1HMV6_9BILA
LinkDB: A0A0V1HMV6_9BILA
Original site: A0A0V1HMV6_9BILA 
ID   A0A0V1HMV6_9BILA        Unreviewed;       727 AA.
AC   A0A0V1HMV6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   22-FEB-2023, entry version 21.
DE   RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE            EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN   Name=FARSB {ECO:0000313|EMBL:KRZ12094.1};
GN   ORFNames=T11_4586 {ECO:0000313|EMBL:KRZ12094.1};
OS   Trichinella zimbabwensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ12094.1, ECO:0000313|Proteomes:UP000055024};
RN   [1] {ECO:0000313|EMBL:KRZ12094.1, ECO:0000313|Proteomes:UP000055024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ12094.1};
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:KRZ12094.1}.
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DR   EMBL; JYDP01000043; KRZ12094.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1HMV6; -.
DR   Proteomes; UP000055024; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00769; PheRS_beta_core; 1.
DR   Gene3D; 3.30.56.10; -; 2.
DR   Gene3D; 3.50.40.10; Phenylalanyl-trna Synthetase, Chain B, domain 3; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR005146; B3/B4_tRNA-bd.
DR   InterPro; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR045060; Phe-tRNA-ligase_IIc_bsu.
DR   InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
DR   InterPro; IPR041616; PheRS_beta_core.
DR   InterPro; IPR040659; PhetRS_B1.
DR   InterPro; IPR005147; tRNA_synthase_B5-dom.
DR   PANTHER; PTHR10947:SF0; PHENYLALANINE--TRNA LIGASE BETA SUBUNIT; 1.
DR   PANTHER; PTHR10947; PHENYLALANYL-TRNA SYNTHETASE BETA CHAIN AND LEUCINE-RICH REPEAT-CONTAINING PROTEIN 47; 1.
DR   Pfam; PF03483; B3_4; 1.
DR   Pfam; PF03484; B5; 1.
DR   Pfam; PF18262; PhetRS_B1; 1.
DR   Pfam; PF17759; tRNA_synthFbeta; 1.
DR   SMART; SM00873; B3_4; 1.
DR   SMART; SM00874; B5; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF56037; PheT/TilS domain; 1.
DR   SUPFAM; SSF46955; Putative DNA-binding domain; 2.
DR   PROSITE; PS51483; B5; 1.
PE   4: Predicted;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KRZ12094.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          324..402
FT                   /note="B5"
FT                   /evidence="ECO:0000259|PROSITE:PS51483"
SQ   SEQUENCE   727 AA;  82423 MW;  19476DA046A7BC4E CRC64;
     MKMTIGFLHL TDLSNSTVKF LIYFNIIATL LYVSAESLFV FCILFIRRAV VVILKGTVSK
     STMPTITIKR RLFKDYFGDI KDEELDQLLF RFGLELDEVT TEVFSDGSGK NVEEVVLKIE
     IPANRCDLLC WEGLIRALLI FYKSCEQPKY MIASSKMKPT IQLKVTKEVE TIRPYVVAAV
     LRNVTFNRDA YDSFIALQEK LHQNICRKRQ LVAIGTHDLD KVKGPFVYSA KSPQEICFKP
     LNEKEKFTAA QLMTHYSKDN HLRQYLHIIE HSPLFPYICD SEGAVLSMPP IINSDQSKIT
     LQTKNILIEC TAVDLHRAQI VLDTIVCMFS VYCDQPYQID PVEVITPGGI RQTYPILSCR
     TGKVGSEDMV LYRIPPTRHD ILHECDIIED VAIAYGYNNI KKELPPAAAI SDQLYLNKIT
     EAMRKEIACA GFTEILTFSL CSRADVSMKL NQPEELNRAV EIANPKTLEF QASCFMFMHF
     IARTLLLPGI LKTLAHNKDK ALPLKLFEIQ DVVERNDNSG KDPVNRRHFC AVYYGKTSGF
     ETIHGLLDHF MRLLEVSSNP ALGYCIKEDL LPFYFPGRCA SIMLRGEKKI GHMGILHPSV
     CRAFDLNLVC SCLELCFEDP LSRVGSFVAS TGLLPRSSLS DRPAGSSPRP YCPSGCYRPC
     RPVSLVHALS VTFSHSEGRA RVQYLLANNN NDHHLTLYVN LIMTNILQRK TRYNGGIFVS
     KVQFYFT
//
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