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Database: UniProt
Entry: A0A1H7CZK9_9RHOB
LinkDB: A0A1H7CZK9_9RHOB
Original site: A0A1H7CZK9_9RHOB 
ID   A0A1H7CZK9_9RHOB        Unreviewed;       357 AA.
AC   A0A1H7CZK9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   08-MAY-2019, entry version 7.
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=SAMN05444007_10930 {ECO:0000313|EMBL:SEJ93987.1};
OS   Cribrihabitans marinus.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cribrihabitans.
OX   NCBI_TaxID=1227549 {ECO:0000313|EMBL:SEJ93987.1, ECO:0000313|Proteomes:UP000199379};
RN   [1] {ECO:0000313|EMBL:SEJ93987.1, ECO:0000313|Proteomes:UP000199379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29340 {ECO:0000313|EMBL:SEJ93987.1,
RC   ECO:0000313|Proteomes:UP000199379};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FNYD01000009; SEJ93987.1; -; Genomic_DNA.
DR   BioCyc; GCF_900109035:BMX57_RS15125-MONOMER; -.
DR   Proteomes; UP000199379; Unassembled WGS sequence.
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:SEJ93987.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110882};
KW   Complete proteome {ECO:0000313|Proteomes:UP000199379};
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};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199379}.
FT   DOMAIN      116    349       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   METAL       257    257       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00281}.
SQ   SEQUENCE   357 AA;  39580 MW;  30012A414B224F5C CRC64;
     MDELKAKYLG QIADAGDEAA LEAIRVAAVG KKGEVSLKMR ELGKMTPEER QEAGPALNAL
     KSEITSALAA KKAALADAAL DERLRGEWLD VTLPGRPRRQ GTLHPITQAT EELTAIFAEL
     GFSVAEGPRI ENDWYNFDAL NIPGHHPARA EMDTFYMARA EGDNRPPHVL RTHTSPVQIR
     SMEAHGAPIR IICPGGVYRA DYDQTHTPMF HQVEGLALDR DISMANLKWV LEEFCRAFFE
     IDDVELRFRA SHFPFTEPSA EVDIRCSWEG GALKIGEGDD WMEILGSGMV HPKVIAAGGI
     DPEIYQGFAF GIGIDRLAML KYGIPDLRAF FDSDLRWLRH YGFAALDMPN LHGGLSR
//
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