ID K0IH98_NITGG Unreviewed; 494 AA.
AC K0IH98;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN Name=pheS {ECO:0000313|EMBL:AFU59280.1};
GN OrderedLocusNames=Ngar_c23550 {ECO:0000313|EMBL:AFU59280.1};
OS Nitrososphaera gargensis (strain Ga9.2).
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrososphaerales;
OC Nitrososphaeraceae; Nitrososphaera.
OX NCBI_TaxID=1237085 {ECO:0000313|EMBL:AFU59280.1, ECO:0000313|Proteomes:UP000008037};
RN [1] {ECO:0000313|EMBL:AFU59280.1, ECO:0000313|Proteomes:UP000008037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ga9.2 {ECO:0000313|Proteomes:UP000008037};
RX PubMed=23057602; DOI=10.1111/j.1462-2920.2012.02893.x;
RA Spang A., Poehlein A., Offre P., Zumbragel S., Haider S., Rychlik N.,
RA Nowka B., Schmeisser C., Lebedeva E.V., Rattei T., Bohm C., Schmid M.,
RA Galushko A., Hatzenpichler R., Weinmaier T., Daniel R., Schleper C.,
RA Spieck E., Streit W., Wagner M.;
RT "The genome of the ammonia-oxidizing Candidatus Nitrososphaera gargensis:
RT insights into metabolic versatility and environmental adaptations.";
RL Environ. Microbiol. 14:3122-45(2012).
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; CP002408; AFU59280.1; -; Genomic_DNA.
DR AlphaFoldDB; K0IH98; -.
DR STRING; 1237085.Ngar_c23550; -.
DR KEGG; nga:Ngar_c23550; -.
DR PATRIC; fig|1237085.11.peg.2330; -.
DR HOGENOM; CLU_025086_2_2_2; -.
DR InParanoid; K0IH98; -.
DR OrthoDB; 372178at2157; -.
DR Proteomes; UP000008037; Chromosome.
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 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000313|EMBL:AFU59280.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008037}.
FT DOMAIN 244..490
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 494 AA; 55411 MW; 755F4DDFE9452B9E CRC64;
MSSAPTLHPI ERSILKALAN NDSDAGSLAA STGLSIDQVR RGIEWLKFKN LISISESSIL
KVQLGSEGAA AIANGLPERR LVNAVKQGKA TIGEILTSGT VKNEEVNAAI AGARRNQWIQ
FVEGRMEATA LAEKQSAEET FLANLKNGTA AEVGKMTESE KKILEQLKKR PNYVEIKEEK
ESRISLTGAG RALIPTLDEG QGERRLTSEM ITSGRWKQTK FSALDVEAPA PAVYPGRRHP
LIDIIEEVKE IFVGLGFSEI DGPMVQSGFW NFDALFTPQD HPAREMQDTF YISGQRQHIP
ASDEQKKRIA KVHEKGWGSK WDIKEAERVV LRTHTTPVTL RHLATIKPEV GRYFSVGRVF
RNEKVSYKHL VEFHQVEGVA TAPRASLRDL MGLQKEFYAK MGIKKVKFWP TFFPYTEPSL
QSMVYNERLE KWVELFGMGI FRPEVTEPLG IKNPVLAWGG GLERIAMLRF GLDDVRELYG
NRLAWLRSVP RCQL
//
