ID A0A1B7P1U4_9EURO Unreviewed; 522 AA.
AC A0A1B7P1U4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 13-SEP-2023, entry version 23.
DE RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
DE AltName: Full=Phenylalanyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031194};
GN ORFNames=ACJ72_02836 {ECO:0000313|EMBL:OAX82817.1};
OS Emergomyces africanus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX NCBI_TaxID=1955775 {ECO:0000313|EMBL:OAX82817.1, ECO:0000313|Proteomes:UP000091918};
RN [1] {ECO:0000313|EMBL:OAX82817.1, ECO:0000313|Proteomes:UP000091918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 136260 {ECO:0000313|EMBL:OAX82817.1,
RC ECO:0000313|Proteomes:UP000091918};
RA Cuomo C.A., Schwartz I.S., Kenyon C., de Hoog G.S., Govender N.P.,
RA Botha A., Moreno L., de Vries M., Munoz J.F., Stielow J.B.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (JUL-2015) 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 -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
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:OAX82817.1}.
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DR EMBL; LGUA01000252; OAX82817.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7P1U4; -.
DR STRING; 1658172.A0A1B7P1U4; -.
DR OrthoDB; 1095527at2759; -.
DR Proteomes; UP000091918; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00496; PheRS_alpha_core; 1.
DR Gene3D; 3.30.70.380; Ferrodoxin-fold anticodon-binding domain; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR005121; Fdx_antiC-bd.
DR InterPro; IPR036690; Fdx_antiC-bd_sf.
DR InterPro; IPR004530; Phe-tRNA-synth_IIc_mito.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR NCBIfam; TIGR00469; pheS_mito; 1.
DR PANTHER; PTHR11538:SF41; PHENYLALANINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF03147; FDX-ACB; 1.
DR Pfam; PF01409; tRNA-synt_2d; 2.
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; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51447; FDX_ACB; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:OAX82817.1};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000091918};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 141..419
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT DOMAIN 421..522
FT /note="FDX-ACB"
FT /evidence="ECO:0000259|PROSITE:PS51447"
FT REGION 57..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 522 AA; 59175 MW; AE525399C88A5A47 CRC64;
MRLPAIGRIQ RLAANHGPIT ARSPGYSARH QLNPLASSRS SSSTATRAEA AAVSALGEVR
GQSKKPQSGH QIPPVKLLPG GVKQGEKTYP TDEWTNTPSN IISHIGRRLY LDENHPLAIT
RQLIESQFTG PEFGNYAEPN PIVSTAQNFD VLGFPADHPG RSRTDTYYVN KTTVLRTHTS
AHQQSYFQRL SLNEETRPEE EGYTVVADVY RRDAIDRSHY PVFHQMEAAR LWKRPRDNPL
KYSWQTAETI MKAANNIPAH NVKVEDPNPT IHPERNPLQT EHLSVEETEA IATHLKRSLE
RLVVKIFTAA REGTPESARA DQEPLKVRWV EAYFPFTSPS WELEVFYQGD WLEVLGCGVV
KQELLISSDA PHRIGWAFGL GLERIAMLLF NIPDIRLFWS QDPRFLSQFQ AGRITRFVPF
SKHPACYKDV AFWVPPSAAS AAGGRTPFHE NDMMEIVRDV AGNLVEDVQL VDEFTHPKTG
RKSFCYRVNY RSLERTLTNE ETNKLHEMVR KELVERAGVE IR
//
