ID A0A1F6E9Z6_9BACT Unreviewed; 596 AA.
AC A0A1F6E9Z6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OGG70042.1};
GN ORFNames=A3C20_02625 {ECO:0000313|EMBL:OGG70042.1};
OS Candidatus Kaiserbacteria bacterium RIFCSPHIGHO2_02_FULL_55_25.
OC Bacteria; Candidatus Kaiserbacteria.
OX NCBI_TaxID=1798498 {ECO:0000313|EMBL:OGG70042.1, ECO:0000313|Proteomes:UP000176914};
RN [1] {ECO:0000313|EMBL:OGG70042.1, ECO:0000313|Proteomes:UP000176914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGG70042.1}.
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DR EMBL; MFLL01000006; OGG70042.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6E9Z6; -.
DR Proteomes; UP000176914; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 3.30.56.10; -; 2.
DR Gene3D; 3.30.70.380; Ferrodoxin-fold anticodon-binding domain; 1.
DR Gene3D; 3.50.40.10; Phenylalanyl-trna Synthetase, Chain B, domain 3; 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; IPR005121; Fdx_antiC-bd.
DR InterPro; IPR036690; Fdx_antiC-bd_sf.
DR InterPro; IPR045060; Phe-tRNA-ligase_IIc_bsu.
DR InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
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; PF03483; B3_4; 1.
DR Pfam; PF03484; B5; 1.
DR Pfam; PF03147; FDX-ACB; 1.
DR SMART; SM00873; B3_4; 1.
DR SMART; SM00874; B5; 1.
DR SMART; SM00896; FDX-ACB; 1.
DR SUPFAM; SSF54991; Anticodon-binding domain of PheRS; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF56037; PheT/TilS domain; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 2.
DR PROSITE; PS51483; B5; 1.
DR PROSITE; PS51447; FDX_ACB; 1.
PE 4: Predicted;
FT DOMAIN 289..367
FT /note="B5"
FT /evidence="ECO:0000259|PROSITE:PS51483"
FT DOMAIN 508..596
FT /note="FDX-ACB"
FT /evidence="ECO:0000259|PROSITE:PS51447"
SQ SEQUENCE 596 AA; 65938 MW; 33DF4C30BB1C398B CRC64;
MKISRNWLQT YFEKPLPEAQ ALADALTFHA FEIESVENDV LDVKVTPNRG HDCLSHRGVA
KELSAILELP MKADALRQTV SLEPRTDEVA VTIETPLCPR YIAGYITGVK VGPSPDWLRS
SLESVGQRSI NNVVDATNYV MFNLGQPLHA FDAGQLKEKN GYSIEVRNAK KGEKMIALDD
KEYELAESML VIGDKNSGAA IGIAGVKGGK PAGISETTKD IIIESANFDG VSVRRTAAAL
KLRTDASSRF EQVLSPELAA YGMRAAADLI LQLAGGELAG FTDEYPAKQG IRTVSVTLSK
INAVLGTKLA ESDVADAFRR LELPYQSDEV RPHRVTVTPP FERLDLVIAE DLIEEVARIV
GYDKIPAVEL SKFTGKVEIN PNFYAAEKSR EELVAQGYSE VFTSVFADKG ERVVANKVDG
VRPYLRATLQ DGLKDALEKN IRNKDLLGLK EVKLFEIGTV WRKGREEIVL GTADKSGVRE
SELTTSDVVN DVYEMLPVST TERYQTYSKY PFIVRDIALW VPAGIKPEDV LEVIRTHAGE
LLVRSEKFDE FTKGEKTSYA FRLVFQSFDK TLTDGDANER MESIYAAVKG KGWEVR
//
