GenomeNet

Database: UniProt
Entry: E4T4I4_PALPW
LinkDB: E4T4I4_PALPW
Original site: E4T4I4_PALPW 
ID   E4T4I4_PALPW            Unreviewed;       339 AA.
AC   E4T4I4;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   08-MAY-2019, entry version 53.
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   OrderedLocusNames=Palpr_1482 {ECO:0000313|EMBL:ADQ79628.1};
OS   Paludibacter propionicigenes (strain DSM 17365 / JCM 13257 / WB4).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC   Paludibacteraceae; Paludibacter.
OX   NCBI_TaxID=694427 {ECO:0000313|EMBL:ADQ79628.1, ECO:0000313|Proteomes:UP000008718};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WB4;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Munk A.C., Brettin T.,
RA   Detter J.C., Han C., Tapia R., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Paludibacter propionicigenes DSM 17365.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADQ79628.1, ECO:0000313|Proteomes:UP000008718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17365 / JCM 13257 / WB4
RC   {ECO:0000313|Proteomes:UP000008718};
RX   PubMed=21475585; DOI=10.4056/sigs.1503846;
RA   Gronow S., Munk C., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brambilla E., Rohde M., Goker M., Detter J.C.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Paludibacter propionicigenes type strain
RT   (WB4).";
RL   Stand. Genomic Sci. 4:36-44(2011).
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:SAAS01166938};
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:SAAS00346031}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00281,
CC       ECO:0000256|SAAS:SAAS00345973}.
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002345; ADQ79628.1; -; Genomic_DNA.
DR   RefSeq; WP_013444997.1; NC_014734.1.
DR   STRING; 694427.Palpr_1482; -.
DR   EnsemblBacteria; ADQ79628; ADQ79628; Palpr_1482.
DR   KEGG; ppn:Palpr_1482; -.
DR   eggNOG; ENOG4105CSS; Bacteria.
DR   eggNOG; COG0016; LUCA.
DR   HOGENOM; HOG000242675; -.
DR   KO; K01889; -.
DR   OMA; DWHNFTA; -.
DR   OrthoDB; 469058at2; -.
DR   BioCyc; PPRO694427:G1GQ6-1489-MONOMER; -.
DR   Proteomes; UP000008718; Chromosome.
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; 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   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:ADQ79628.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110882}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008718};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS00424209};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110936, ECO:0000313|EMBL:ADQ79628.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008718}.
FT   DOMAIN      107    314       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   COILED        5     29       {ECO:0000256|SAM:Coils}.
FT   COILED       48     76       {ECO:0000256|SAM:Coils}.
FT   METAL       250    250       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00281}.
SQ   SEQUENCE   339 AA;  38712 MW;  4F9A396723C013BA CRC64;
     MKNRIKQLLE EINQLAAGNQ EELEALRIKY LSKKGEISTL FNDFRNVANE EKRDVGQLLN
     ELKNSAQDKI NELKDAFGAT TNTENKPDLT RSADPVKLGT RHPLSLVKHE IVDIFSRIGF
     TVAEGPEIED DWHVFGALNF PPEHPARDMQ DTFFIEQNPD VLLRTHTSSV QSHVMATQKP
     PIRMLFPGRV YRNEAISYRA HCFFHQVEGL YIDKDVSFAD LKQALMYFAK EMFGENTEIR
     LRPSYFPFTE PSAEMDISCN ICGGKGCPFC KHTGWVEILG CGMVDPNVLE NCGIDSKVYS
     GYAFGMGVER ITNLKYQVKD LRMFSENDVR FLQQFESAY
//
DBGET integrated database retrieval system