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Database: UniProt
Entry: A0A128A586_9ARCH
LinkDB: A0A128A586_9ARCH
Original site: A0A128A586_9ARCH 
ID   A0A128A586_9ARCH        Unreviewed;       489 AA.
AC   A0A128A586;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE            EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN   ORFNames=NDEV_1757 {ECO:0000313|EMBL:CUR52519.1};
OS   Candidatus Nitrosotalea devanaterra.
OC   Archaea; Nitrososphaerota; Nitrosotalea.
OX   NCBI_TaxID=1078905 {ECO:0000313|EMBL:CUR52519.1, ECO:0000313|Proteomes:UP000196239};
RN   [1] {ECO:0000313|Proteomes:UP000196239}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lehtovirta-Morley L.E., Vieille C.;
RL   Submitted (OCT-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}.
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DR   EMBL; LN890280; CUR52519.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A128A586; -.
DR   KEGG; ndv:NDEV_1757; -.
DR   Proteomes; UP000196239; Chromosome 1.
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   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   NCBIfam; TIGR00468; pheS; 1.
DR   PANTHER; PTHR11538:SF40; PHENYLALANINE--TRNA LIGASE ALPHA SUBUNIT; 1.
DR   PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF01409; tRNA-synt_2d; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:CUR52519.1};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Ligase {ECO:0000313|EMBL:CUR52519.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          244..486
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   489 AA;  55748 MW;  8847F14DA459F582 CRC64;
     MSQVLHPIEQ KILKTLAEKK NLTPEDLSEI TKLSLDQIRR GIEWLKFKSL ANVVESEKTL
     VTLGKRGNEA SEKGLPERQL VNYLRSLDGY SCEMNAAKDY LKNEFGPAIA NAKKNGWIEV
     HENRLMLKGY HDLSSEEKII KTISKTPMGV STDNFEDKDA LESLKKRPEF IVLTSKKSAL
     VGLTEQGMEA AKSVPDNIDF ESVSETSHKV EPDAKVVRAI DVEAAAPVIF AAKSHPLRDV
     IDEVREIFVS LGFSEIIGSN VQSSFWNFDA LFTPQDHPAR EMQDTFYLAD VKAKTIAKPD
     QIKKVSDAHK KGWNYQWQNE EARRLVLRTH TTCVTIRELA DQKHDEARLF SIGKVFRNEK
     LSYKHLAEFH QVEGVVVGKN VTLRDLMGLQ TEFYHKMGIK KIKFWPTFFP YTEPSLQSMI
     YNEKLGKWVE LFGMGIFRPE VTKPLGIKNP VLAWGGGIER IAMLRYGLTD VRELYENNFG
     WLRSVPKCQ
//
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