SYFB_PYRHO
ID SYFB_PYRHO Reviewed; 556 AA.
AC O73984;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00284};
DE EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00284};
DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00284};
DE Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00284};
GN Name=pheT {ECO:0000255|HAMAP-Rule:MF_00284}; OrderedLocusNames=PH0657;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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:0000255|HAMAP-Rule:MF_00284};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00284};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00284}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00284}.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00284,
CC ECO:0000305}.
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; BA000001; BAA29748.1; -; Genomic_DNA.
DR PIR; B71111; B71111.
DR RefSeq; WP_010884752.1; NC_000961.1.
DR PDB; 2CXI; X-ray; 1.94 A; A/B/C=1-348.
DR PDBsum; 2CXI; -.
DR AlphaFoldDB; O73984; -.
DR SMR; O73984; -.
DR STRING; 70601.3257065; -.
DR EnsemblBacteria; BAA29748; BAA29748; BAA29748.
DR GeneID; 1442987; -.
DR KEGG; pho:PH0657; -.
DR eggNOG; arCOG00412; Archaea.
DR OMA; FPGRCAN; -.
DR OrthoDB; 55024at2157; -.
DR BRENDA; 6.1.1.20; 5244.
DR EvolutionaryTrace; O73984; -.
DR Proteomes; UP000000752; 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; 3.30.930.10; -; 1.
DR Gene3D; 3.50.40.10; -; 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; IPR004531; Phe-tRNA-synth_IIc_bsu_arc_euk.
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; PTHR10947; 1.
DR Pfam; PF03483; B3_4; 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; SSF46955; SSF46955; 2.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00471; pheT_arch; 1.
DR PROSITE; PS51483; B5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Magnesium; Metal-binding; Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..556
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000127009"
FT DOMAIN 278..353
FT /note="B5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
FT BINDING 331
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
FT BINDING 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
FT BINDING 340
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
FT BINDING 341
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:2CXI"
FT HELIX 8..15
FT /evidence="ECO:0007829|PDB:2CXI"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:2CXI"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:2CXI"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:2CXI"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:2CXI"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:2CXI"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:2CXI"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:2CXI"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:2CXI"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:2CXI"
FT HELIX 116..131
FT /evidence="ECO:0007829|PDB:2CXI"
FT TURN 132..138
FT /evidence="ECO:0007829|PDB:2CXI"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:2CXI"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:2CXI"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:2CXI"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:2CXI"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:2CXI"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:2CXI"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:2CXI"
FT STRAND 196..204
FT /evidence="ECO:0007829|PDB:2CXI"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:2CXI"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:2CXI"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:2CXI"
FT STRAND 230..238
FT /evidence="ECO:0007829|PDB:2CXI"
FT HELIX 240..255
FT /evidence="ECO:0007829|PDB:2CXI"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:2CXI"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:2CXI"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:2CXI"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:2CXI"
FT HELIX 287..294
FT /evidence="ECO:0007829|PDB:2CXI"
FT HELIX 300..309
FT /evidence="ECO:0007829|PDB:2CXI"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:2CXI"
FT STRAND 320..325
FT /evidence="ECO:0007829|PDB:2CXI"
FT HELIX 335..346
FT /evidence="ECO:0007829|PDB:2CXI"
SQ SEQUENCE 556 AA; 64195 MW; D3DB228E4AB7CBC0 CRC64;
MPKFDVSKSD LERLIGRSFS IEEWEDLVLY AKCELDDVWE ENGKVYFKLD SKDTNRPDLW
SAEGVARQIK WALGIEKGLP KYEVKKSNVT VYVDEKLKDI RPYGVYAIVE GLRLDEDSLS
QMIQLQEKIA LTFGRRRREV AIGIFDFDKI KPPIYYKAAE KTEKFAPLGY KEEMTLEEIL
EKHEKGREYG HLIKDKQFYP LLIDSEGNVL SMPPIINSEF TGRVTTDTKN VFIDVTGWKL
EKVMLALNVM VTALAERGGK IRSVRVVYKD FEIETPDLTP KEFEVELDYI RKLSGLELND
GEIKELLEKM MYEVEISRGR AKLKYPAFRD DIMHARDILE DVLIAYGYNN IEPEEPKLAV
QGRGDPFKDF EDAIRDLMVG FGLQEVMTFN LTNKEVQFKK MNIPEEEIVE IANPISQRWS
ALRKWILPSL MEFLSNNTHE EYPQRIFEVG LATLIDESRE TKTVSEPKLA VALAGTGYTF
TNAKEILDAL MRHLGFEYEI EEVEHGSFIP GRAGKIIVNG RDIGIIGEVH PQVLENWNIE
VPVVAFEIFL RPLYRH
