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Entry: M5AM53_9ACTN
LinkDB: M5AM53_9ACTN
Original site: M5AM53_9ACTN 
ID   M5AM53_9ACTN            Unreviewed;       341 AA.
AC   M5AM53;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   08-MAY-2019, entry version 40.
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   ECO:0000313|EMBL:BAN02385.1};
GN   ORFNames=YM304_20710 {ECO:0000313|EMBL:BAN02385.1};
OS   Ilumatobacter coccineus YM16-304.
OC   Bacteria; Actinobacteria; Acidimicrobiia; Acidimicrobiales;
OC   Ilumatobacteraceae; Ilumatobacter.
OX   NCBI_TaxID=1313172 {ECO:0000313|EMBL:BAN02385.1};
RN   [1] {ECO:0000313|EMBL:BAN02385.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YM16-304 {ECO:0000313|EMBL:BAN02385.1};
RA   Sekine M., Hosoyama A., Hanamaki T., Nishiko R., Takarada Y.,
RA   Omata S., Nakazawa H., Fujinami S., Yamazaki S., Fujita N.;
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAN02385.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YM16-304 {ECO:0000313|EMBL:BAN02385.1};
RX   PubMed=23524358; DOI=10.1099/ijs.0.047316-0;
RA   Matsumoto A., Kasai H., Matsuo Y., Shizuri Y., Ichikawa N., Fujita N.,
RA   Omura S., Takahashi Y.;
RT   "Ilumatobacter nonamiense sp. nov. and Ilumatobacter coccineum sp.
RT   nov., isolated from seashore sand.";
RL   Int. J. Syst. Evol. Microbiol. 63:3404-3408(2013).
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}.
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DR   EMBL; AP012057; BAN02385.1; -; Genomic_DNA.
DR   STRING; 1313172.YM304_20710; -.
DR   EnsemblBacteria; BAN02385; BAN02385; YM304_20710.
DR   KEGG; aym:YM304_20710; -.
DR   PATRIC; fig|467094.3.peg.2111; -.
DR   KO; K01889; -.
DR   BioCyc; ICOC1313172:G1HFY-2093-MONOMER; -.
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, ECO:0000313|EMBL:BAN02385.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110882};
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:BAN02385.1};
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      122    320       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   METAL       267    267       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00281}.
SQ   SEQUENCE   341 AA;  37172 MW;  2D8B13A987EB9FB7 CRC64;
     MNPDILTEIT SARDAALAEI ASASTPDAVA SMTTRFAGKK GELAGLKKRL GSLDSIDEKK
     AAGAAINEAM AAVDAALDEQ RSALNAAALA AQVENERLDL TEYVGKPTRG KAHLVTQAWE
     RLEDVFVGLG FQVAEGPEVE TDWHNFEALN MGEGHPARGE FDTLFVDHVP PGGAPGSTVL
     RTHTSPVQIR TMLEKEPPIY IVAPGRVFRR DTPDATHMPV FHQIEGLVID RNISMADLAG
     TIQAFTTAFF GKDWNSRLRP DYFPFTEPSA EFDIQRPDGS WIELGGCGMV HPNVLRAGGI
     DPEEWSGFAF GFGIDRMALM RHGVDDLRAM YADDLRFTSQ F
//
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