ID A6VRE6_MARMS Unreviewed; 373 AA.
AC A6VRE6;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN OrderedLocusNames=Mmwyl1_0083 {ECO:0000313|EMBL:ABR69025.1};
OS Marinomonas sp. (strain MWYL1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=400668 {ECO:0000313|EMBL:ABR69025.1};
RN [1] {ECO:0000313|EMBL:ABR69025.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWYL1 {ECO:0000313|EMBL:ABR69025.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA Richardson P.;
RT "Complete sequence of Marinomonas sp. MWYL1.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
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DR EMBL; CP000749; ABR69025.1; -; Genomic_DNA.
DR AlphaFoldDB; A6VRE6; -.
DR STRING; 400668.Mmwyl1_0083; -.
DR KEGG; mmw:Mmwyl1_0083; -.
DR eggNOG; COG0016; Bacteria.
DR HOGENOM; CLU_022696_2_0_6; -.
DR OrthoDB; 489670at2; -.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0043039; P:tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 3.30.70.380; Ferrodoxin-fold anticodon-binding domain; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR005121; Fdx_antiC-bd.
DR InterPro; IPR036690; Fdx_antiC-bd_sf.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR PANTHER; PTHR11538:SF41; PHENYLALANINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF01409; tRNA-synt_2d; 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 PROSITE; PS51447; FDX_ACB; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:ABR69025.1};
KW Ligase {ECO:0000313|EMBL:ABR69025.1}.
FT DOMAIN 267..373
FT /note="FDX-ACB"
FT /evidence="ECO:0000259|PROSITE:PS51447"
SQ SEQUENCE 373 AA; 42363 MW; 68A70D992606CEEF CRC64;
MSKHNYLTHE QLLSALSLRD LTNPKHGMHA MQQLISEAET AVAALWSCYL QRINANPIVP
VYENYDALGY PVDGASRDIR YSRYVSDSLM LRTQTSSSVP TWLSSWRSLR PESLGIISHG
LVYRRDCIDR WHCAEPHQLD IWIVMPKAQA EDTQILSDSI SALMKTLLPN HVVQQSKSPH
PYTINGVQLD AIEGQNLIEV GECGNIDPDL LTRNGWSSDD YTGVAIGLGL DRVLMLRKGI
PDIRLLRDPD PRIQQQMLDL SPWRPVSRQP KAERDISIVV NRDTDMDIIG DQVRLTLGEQ
AHWLEELQLL SRTEYQQLPK SAIERLGMTS TQVNLLLRIN LRHPTRSVPT SLANELRNKI
YLSLNQGHNY LAN
//
