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Database: UniProt
Entry: A0A0A6YTH4_9FLAO
LinkDB: A0A0A6YTH4_9FLAO
Original site: A0A0A6YTH4_9FLAO 
ID   A0A0A6YTH4_9FLAO        Unreviewed;       477 AA.
AC   A0A0A6YTH4;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000256|ARBA:ARBA00017032};
DE   AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000256|ARBA:ARBA00033189};
DE   Flags: Fragment;
GN   ORFNames=HMPREF9074_07473 {ECO:0000313|EMBL:KHE70680.1};
OS   Capnocytophaga sp. oral taxon 329 str. F0087.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=706436 {ECO:0000313|EMBL:KHE70680.1, ECO:0000313|Proteomes:UP000030579};
RN   [1] {ECO:0000313|EMBL:KHE70680.1, ECO:0000313|Proteomes:UP000030579}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0087 {ECO:0000313|EMBL:KHE70680.1,
RC   ECO:0000313|Proteomes:UP000030579};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (OCT-2014) 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|ARBA:ARBA00000395};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|ARBA:ARBA00011209}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC       family. Type 1 subfamily. {ECO:0000256|ARBA:ARBA00008653}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KHE70680.1}.
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DR   EMBL; AFHP02000042; KHE70680.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A6YTH4; -.
DR   STRING; 706436.HMPREF9074_07473; -.
DR   eggNOG; COG0072; Bacteria.
DR   eggNOG; COG0073; Bacteria.
DR   HOGENOM; CLU_016891_1_1_10; -.
DR   OrthoDB; 9805455at2; -.
DR   Proteomes; UP000030579; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd02796; tRNA_bind_bactPheRS; 1.
DR   Gene3D; 3.30.56.10; -; 2.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.50.40.10; Phenylalanyl-trna Synthetase, Chain B, domain 3; 1.
DR   InterPro; IPR005146; B3/B4_tRNA-bd.
DR   InterPro; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR045060; Phe-tRNA-ligase_IIc_bsu.
DR   InterPro; IPR004532; Phe-tRNA-ligase_IIc_bsu_bact.
DR   InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
DR   InterPro; IPR002547; tRNA-bd_dom.
DR   InterPro; IPR033714; tRNA_bind_bactPheRS.
DR   InterPro; IPR005147; tRNA_synthase_B5-dom.
DR   NCBIfam; TIGR00472; pheT_bact; 1.
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; PF03483; B3_4; 1.
DR   Pfam; PF03484; B5; 1.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   SMART; SM00873; B3_4; 1.
DR   SMART; SM00874; B5; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF56037; PheT/TilS domain; 1.
DR   SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR   PROSITE; PS51483; B5; 1.
DR   PROSITE; PS50886; TRBD; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000313|EMBL:KHE70680.1};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00209};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PROSITE-
KW   ProRule:PRU00209}.
FT   DOMAIN          42..155
FT                   /note="TRNA-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50886"
FT   DOMAIN          414..477
FT                   /note="B5"
FT                   /evidence="ECO:0000259|PROSITE:PS51483"
FT   NON_TER         477
FT                   /evidence="ECO:0000313|EMBL:KHE70680.1"
SQ   SEQUENCE   477 AA;  52192 MW;  A34DC292D7AFE55A CRC64;
     MKISYNWLKQ YLKLDLAAEE TGVILTDLGL EVEGIEPFES VKGGLKGVVV GLVLECEKHP
     NADKLKVTKV DVGQEAPLQI VCGAPNVAKG QKVPVATIGT VLYDHEGKPF EIKKGKIRGE
     ESYGMICAED ELGLGESHEG IMVLDDKYAV GTPCAEVFQV ETDEVFEIGL TPNRADAMSH
     YGVARDLRAG LIQKGVSLEL ITPSVTKFHV DNRSVKVDIE VTNKKLVPRY TGVAISNVRV
     GESPAWLQNR LKAIGITPKN NVVDATNYVL HGLGQPLHAF DADHIVGRKL IVKTAEAGTV
     FTTLDGVKRT LDAEDLMIYD AEKPLCIAGV LGGQDSGVTH STRNVFLESA YFDPVSVRKT
     AKRHSISTDA SYRFERGINI EDCKYALMYA AVLIENIAGG VISSDVIDFY PKKKDDFQVF
     LAFENVDKLI GQKIPRDTIK SILHSLDIKV SSLTERGLGL LIPSYRVDVQ READVIE
//
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