ID A0A1V8UDK9_9PEZI Unreviewed; 534 AA.
AC A0A1V8UDK9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 alpha subunit {ECO:0000256|ARBA:ARBA00030612};
GN ORFNames=B0A51_11912 {ECO:0000313|EMBL:OQO21564.1};
OS Rachicladosporium sp. CCFEE 5018.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO21564.1, ECO:0000313|Proteomes:UP000192386};
RN [1] {ECO:0000313|Proteomes:UP000192386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Phe-tRNA synthetase alpha subunit type 2 subfamily.
CC {ECO:0000256|ARBA:ARBA00006703}.
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:OQO21564.1}.
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DR EMBL; NAEU01000550; OQO21564.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8UDK9; -.
DR STRING; 1974281.A0A1V8UDK9; -.
DR Proteomes; UP000192386; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 1.10.10.2320; -; 1.
DR Gene3D; 1.10.10.2330; -; 1.
DR Gene3D; 3.30.1370.240; -; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR InterPro; IPR040725; PheRS_DBD3.
DR NCBIfam; TIGR00468; pheS; 1.
DR PANTHER; PTHR11538:SF40; PHENYLALANINE--TRNA LIGASE ALPHA SUBUNIT; 1.
DR PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF18553; PheRS_DBD3; 1.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000192386}.
FT DOMAIN 383..503
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 534 AA; 59839 MW; 7BB7B914ECCD6839 CRC64;
MPGQRGPVPV PLHNGSRDLT LDILEALEEN DPFQTQSQFP ETPQAEIKAA LDRLASRSMV
EYDTQDREIV VLTAEGQQIA DEGSHEYKVW KAVKASGKLS IKELPQKVAA ESAKVGQGNA
FKLKWIKKDG DSLVPIADSV QDVTRELLEH VATNAAFPDP KQLKDYQKRK LVATQKQIAY
KVRKGPRWAK EIPVEVTDLT AEMLEDGSWQ TANFKPYNFK ALGANQNSGA LHPLNKVREE
FRKIFFNWDF IEMPTARFVD SGFWNFDALF VPQQHPARDL QDTFYVSDPP SSGPPGPDPI
ADAALDEMEA DSATFSTSTS KSSKLDYAKY ASDVRTVHET GAFGSIGYRY PYNEAETTRL
VLRTHTTAVS TYCLHRLAAN PRPARYFSID RVFRNETVDA THLAEFHQIE GVIADYGLTL
GGLMDFLASF FKKLGITNLR FKPAYNPYTE PSMEVFGFHA GLDKWVEIGN SGMFRPEMLL
PMGLPEDLRV YGFGLSLERP TMIKYGVSNI RELLGHKVDL GFIESNAAVR LDKD
//