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Entry: A0A2G1Z1H3_9PROT
LinkDB: A0A2G1Z1H3_9PROT
Original site: A0A2G1Z1H3_9PROT 
ID   A0A2G1Z1H3_9PROT        Unreviewed;       358 AA.
AC   A0A2G1Z1H3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   08-MAY-2019, entry version 10.
DE   RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00281};
DE            EC=6.1.1.20 {ECO:0000256|HAMAP-Rule:MF_00281};
DE   AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00281};
DE            Short=PheRS {ECO:0000256|HAMAP-Rule:MF_00281};
GN   Name=pheS {ECO:0000256|HAMAP-Rule:MF_00281};
GN   ORFNames=COB93_07655 {ECO:0000313|EMBL:PHQ69589.1};
OS   Sneathiella sp.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sneathiellales;
OC   Sneathiellaceae; Sneathiella.
OX   NCBI_TaxID=1964365 {ECO:0000313|EMBL:PHQ69589.1};
RN   [1] {ECO:0000313|EMBL:PHQ69589.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NORP162 {ECO:0000313|EMBL:PHQ69589.1};
RX   PubMed=29099490; DOI=10.1038/ismej.2017.187;
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy
RT   inhabits the cold, oxic subseafloor aquifer.";
RL   ISME J. 12:1-16(2018).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate +
CC         H(+) + L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413,
CC         Rhea:RHEA-COMP:9668, Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58095,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78531, ChEBI:CHEBI:456215;
CC         EC=6.1.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00281,
CC         ECO:0000256|SAAS:SAAS01124652};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00281};
CC       Note=Binds 2 magnesium ions per tetramer. {ECO:0000256|HAMAP-
CC       Rule:MF_00281};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00281, ECO:0000256|SAAS:SAAS01133340}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00281,
CC       ECO:0000256|SAAS:SAAS00089481}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. Phe-tRNA synthetase alpha subunit type 1 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00281, ECO:0000256|SAAS:SAAS00541523}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PHQ69589.1}.
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DR   EMBL; NVRR01000114; PHQ69589.1; -; Genomic_DNA.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00281; Phe_tRNA_synth_alpha1; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR   InterPro; IPR004188; Phe-tRNA_ligase_II_N.
DR   InterPro; IPR022911; Phe_tRNA_ligase_alpha1_bac.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   Pfam; PF02912; Phe_tRNA-synt_N; 1.
DR   Pfam; PF01409; tRNA-synt_2d; 1.
DR   SUPFAM; SSF46589; SSF46589; 1.
DR   TIGRFAMs; TIGR00468; pheS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110915};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110882}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS00461853};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110936, ECO:0000313|EMBL:PHQ69589.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS00017000};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS00017079};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110884};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110938}.
FT   DOMAIN      110    346       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   COILED       71     91       {ECO:0000256|SAM:Coils}.
FT   METAL       258    258       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00281}.
SQ   SEQUENCE   358 AA;  40048 MW;  CA035608B9C5878F CRC64;
     MQDIEKLEGE LLGEIGNITN LDALESLRIS ALGKKGSVSL MMRGLGQMDP AERQIIAPQL
     NKLKTTVGDA VDAAKARLHA AELDIKLAAE RIDISLPARP ETQGRIHPIS QVMDEITEIF
     ADMGFDIAEG PDIEDDFHNF TALNIPPEHP ARQMHDTFYL PEKEDGSRQL LRTHTSTVQI
     RTMQSQEPPH RIVVPGRTFR CDSDQTHTPM FHQIEGLVID KTSHMGHLKG VLVEFCKAFF
     EVDDVTMRFR PSYFPFTEPS AEMDIKCTFA GDHVKIGEGD DWLEILGCGM VNPRVLAHCG
     IDPNEYQGFA WGMGIDRIAM LKYGIPDLRA FFDADLRWLK HYGFVPLDVP TLGGGLSR
//
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