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Database: UniProt
Entry: L0JZ22_9EURY
LinkDB: L0JZ22_9EURY
Original site: L0JZ22_9EURY 
ID   L0JZ22_9EURY            Unreviewed;       607 AA.
AC   L0JZ22;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000256|HAMAP-Rule:MF_00284};
DE            EC=6.1.1.20 {ECO:0000256|HAMAP-Rule:MF_00284};
DE   AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000256|HAMAP-Rule:MF_00284};
DE            Short=PheRS {ECO:0000256|HAMAP-Rule:MF_00284};
GN   Name=pheT {ECO:0000256|HAMAP-Rule:MF_00284};
GN   ORFNames=Natoc_2506 {ECO:0000313|EMBL:AGB38277.1};
OS   Natronococcus occultus SP4.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natronococcus.
OX   NCBI_TaxID=694430 {ECO:0000313|EMBL:AGB38277.1, ECO:0000313|Proteomes:UP000010878};
RN   [1] {ECO:0000313|EMBL:AGB38277.1, ECO:0000313|Proteomes:UP000010878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP4 {ECO:0000313|EMBL:AGB38277.1,
RC   ECO:0000313|Proteomes:UP000010878};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA   Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA   Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Eisen J., Klenk H.-P.,
RA   Klenk H.-P.;
RT   "FINISHED of Natronococcus occultus SP4, DSM 3396.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) +
CC         L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668,
CC         Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00284};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|HAMAP-Rule:MF_00284};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00284}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00284}.
CC   -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC       family. Type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_00284}.
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DR   EMBL; CP003929; AGB38277.1; -; Genomic_DNA.
DR   RefSeq; WP_015321717.1; NC_019974.1.
DR   AlphaFoldDB; L0JZ22; -.
DR   STRING; 694430.Natoc_2506; -.
DR   GeneID; 14404190; -.
DR   KEGG; nou:Natoc_2506; -.
DR   eggNOG; arCOG00412; Archaea.
DR   HOGENOM; CLU_020279_3_0_2; -.
DR   OrthoDB; 10073at2157; -.
DR   Proteomes; UP000010878; 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:InterPro.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00769; PheRS_beta_core; 1.
DR   Gene3D; 3.30.56.10; -; 2.
DR   Gene3D; 3.50.40.10; Phenylalanyl-trna Synthetase, Chain B, domain 3; 1.
DR   HAMAP; MF_00284; Phe_tRNA_synth_beta2; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR005146; B3/B4_tRNA-bd.
DR   InterPro; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR045060; Phe-tRNA-ligase_IIc_bsu.
DR   InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
DR   InterPro; IPR022918; Phe_tRNA_ligase_beta2_arc.
DR   InterPro; IPR041616; PheRS_beta_core.
DR   InterPro; IPR005147; tRNA_synthase_B5-dom.
DR   PANTHER; PTHR10947:SF0; PHENYLALANINE--TRNA LIGASE BETA SUBUNIT; 1.
DR   PANTHER; PTHR10947; PHENYLALANYL-TRNA SYNTHETASE BETA CHAIN AND LEUCINE-RICH REPEAT-CONTAINING PROTEIN 47; 1.
DR   Pfam; PF03484; B5; 1.
DR   Pfam; PF17759; tRNA_synthFbeta; 1.
DR   SMART; SM00873; B3_4; 1.
DR   SMART; SM00874; B5; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF46955; Putative DNA-binding domain; 2.
DR   PROSITE; PS51483; B5; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00284};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00284}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00284};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00284};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00284};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00284};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00284};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00284}; Reference proteome {ECO:0000313|Proteomes:UP000010878}.
FT   DOMAIN          282..399
FT                   /note="B5"
FT                   /evidence="ECO:0000259|PROSITE:PS51483"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          316..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..352
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         377
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00284"
FT   BINDING         383
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00284"
FT   BINDING         386
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00284"
FT   BINDING         387
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00284"
SQ   SEQUENCE   607 AA;  67551 MW;  A4240AAEBA8E7561 CRC64;
     MPTVDIDPDE LRELTGHEEK SDEELQEDLF GLGLEFEGWT EDDEFELEFA PDRLDRLSVE
     GVARSMRYQY GDAQGVHVPS TNSADWTIEV EESVPDERPY VTGAVIRDVD LDEDGLDSLI
     QLQEKLHATM GRKRAKGAIG IHDLTMLRGS PATEGNPTIR YVGVEPDEDR FVPLDADTEM
     TPGEVLEEHQ TGREYAELVS EYERYPAIYD DLGLFSFPPV INGRRTEVST DSRDLFVEMT
     GTDQWTIDKM LNIVCYALAA RGATLEDVRV EYHDGELVRP DLSTKTKRIP HDRIESILGI
     GLDPDEVIDL AERSGLDAAR SEDGATDDDE STITPLEDRD GLEERGGTEG SSESEADDAA
     STDDLVYEVT IPPYRVDVLH PLDVIDDLGR AYGFNDLEPR YPEVGTVGGR HDRSRLERAV
     RTQLVGLGFE DLLNFHMIDE EQNYERLDVE PGTDAYGTGE PATIKEPYSE DFTMLRTWTL
     PSLLQVLENN THRAYPQHLS EVGFAAKLDE TENTGVAEGR HVGAVLADHE AGYEDAKARL
     QAIARDFDAT LETPATEHPT FIPGRAADVV LDGEVVGVVG EIHPKVLVEH DLEVPVAAFE
     FDLKALR
//
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