ID A0A1J4MJ89_9CRYT Unreviewed; 509 AA.
AC A0A1J4MJ89;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN ORFNames=cubi_01141 {ECO:0000313|EMBL:OII74297.1};
OS Cryptosporidium ubiquitum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX NCBI_TaxID=857276 {ECO:0000313|EMBL:OII74297.1, ECO:0000313|Proteomes:UP000186176};
RN [1] {ECO:0000313|EMBL:OII74297.1, ECO:0000313|Proteomes:UP000186176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=39726 {ECO:0000313|EMBL:OII74297.1};
RA Liu S., Roellig D.M., Guo Y., Li N., Frace M.A., Tang K., Zhang L.,
RA Feng Y., Xiao L.;
RT "Reductive evolution of mitochondrial metabolism and differential evolution
RT of invasion-related proteins in Cryptosporidium.";
RL Submitted (OCT-2016) 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:OII74297.1}.
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DR EMBL; LRBP01000012; OII74297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4MJ89; -.
DR VEuPathDB; CryptoDB:cubi_01141; -.
DR OrthoDB; 4619at2759; -.
DR Proteomes; UP000186176; 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; IPR040724; PheRS_DBD1.
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; PF18552; PheRS_DBD1; 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 Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:OII74297.1};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000313|EMBL:OII74297.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 373..505
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 509 AA; 58728 MW; 1EFE4192219FEC01 CRC64;
MEIEPETILE KLESLNCSLS SVSLSEEFKC EHERIIGIIK SLESRDIIET QFVSDNVLSL
TDEGKDYLTN GSPEFRLIRI ILEQEGHKIK QNEAMKLLGD STFKIGLSKC LQKKLIKLNK
ELGLIEISVN SNKESLNVDE LKKNLDIVGV KGIKESELSK QDMQILAELK KRKLVISNKM
SYFMINRGEK FTVKLKPVIT DLTQEMIMNS SWENNEFKPY NFNAKGKRLP RGNVHPLTRT
LRKFKRILSQ MGFEEMPTNR WVESSFWNFD ALFQPQKHPA RDSHDTFFLE TPSTFRNEME
LSQDHIDQVK KVHEIGGYGS IGLSYNWSIE EASKNLLRTH TTAVSVRMLY QLAQMYLNSE
NGLSFDQFQR KAYFSIDRVF RNESIDATHL AEFHQVEGLI VDKNLTLADL IGTLKTFYEK
IGISDLKFKP AFNPYTEPSM EIFGYHTTLK KWIEVGNSGL FRPEMLRPLG FPSDVVVIAW
GLSLERPTMI SYNIPNIRDL FSFKAKIFS
//
