ID   ERF1_CRYHO              Reviewed;         429 AA.
AC   Q5CG95;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Eukaryotic peptide chain release factor subunit 1;
DE            Short=Eukaryotic release factor 1;
DE            Short=eRF1;
GN   Name=erf1; ORFNames=Chro.60391;
OS   Cryptosporidium hominis.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX   NCBI_TaxID=237895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TU502;
RX   PubMed=15510150; DOI=10.1038/nature02977;
RA   Xu P., Widmer G., Wang Y., Ozaki L.S., Alves J.M., Serrano M.G., Puiu D.,
RA   Manque P., Akiyoshi D., Mackey A.J., Pearson W.R., Dear P.H., Bankier A.T.,
RA   Peterson D.L., Abrahamsen M.S., Kapur V., Tzipori S., Buck G.A.;
RT   "The genome of Cryptosporidium hominis.";
RL   Nature 431:1107-1112(2004).
CC   -!- FUNCTION: Directs the termination of nascent peptide synthesis
CC       (translation) in response to the termination codons UAA, UAG and UGA.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of two subunits, one of which binds GTP.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AAEL01000357; EAL35628.1; -; Genomic_DNA.
DR   RefSeq; XP_665860.1; XM_660768.1.
DR   AlphaFoldDB; Q5CG95; -.
DR   SMR; Q5CG95; -.
DR   GeneID; 3413843; -.
DR   KEGG; cho:Chro.60391; -.
DR   VEuPathDB; CryptoDB:Chro.60391; -.
DR   VEuPathDB; CryptoDB:ChTU502y2012_415g0180; -.
DR   VEuPathDB; CryptoDB:CHUDEA6_3380; -.
DR   VEuPathDB; CryptoDB:GY17_00000350; -.
DR   InParanoid; Q5CG95; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003747; F:translation release factor activity; IEA:InterPro.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   Gene3D; 3.30.420.60; -; 1.
DR   Gene3D; 3.30.960.10; -; 1.
DR   InterPro; IPR042226; eFR1_2_sf.
DR   InterPro; IPR005140; eRF1_1_Pelota.
DR   InterPro; IPR024049; eRF1_1_sf.
DR   InterPro; IPR005141; eRF1_2.
DR   InterPro; IPR005142; eRF1_3.
DR   InterPro; IPR029064; L30e-like.
DR   InterPro; IPR004403; Peptide_chain-rel_eRF1/aRF1.
DR   PANTHER; PTHR10113; PTHR10113; 1.
DR   Pfam; PF03463; eRF1_1; 1.
DR   Pfam; PF03464; eRF1_2; 1.
DR   Pfam; PF03465; eRF1_3; 1.
DR   SMART; SM01194; eRF1_1; 1.
DR   SUPFAM; SSF55315; SSF55315; 1.
DR   SUPFAM; SSF55481; SSF55481; 1.
DR   TIGRFAMs; TIGR03676; aRF1/eRF1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Protein biosynthesis.
FT   CHAIN           1..429
FT                   /note="Eukaryotic peptide chain release factor subunit 1"
FT                   /id="PRO_0000143149"
SQ   SEQUENCE   429 AA;  48306 MW;  ACDE913BA567AFBC CRC64;
     MSDNDTNVKQ WKVRRLIATL EAARGNGTSM ISLVIKPKDE ISRISKMLAD EYGTASNIKS
     RVNRLSVLSA ITSTQQRLKL YNRTPQNGLV VYCGTLITED GKEKKVNIDF EPFKPINTSL
     YLCDNKFHVD ALKELLETDD KFGFIIVDGN GALYGVVQGS SREVLLRFNV DLPKKHGRGG
     QSALRFARLR MEKRHNYLRK VAETATTMFI TNDQVNVAAL ILAGSADFKN ELAQSDIFDQ
     RLASKILKIV DVSYGGDNGF NQAIELSSDA LQNVKFVQEK KLITKFFDEV AQDTGKYVYG
     INETLQALEM GAIELLIVWE NLETKRMVVK NPSTGEEKVF LNSPTEQHDE SKFKDPETGA
     ELDVIEILPL TEWLVNTYQN YGAQLEFVTN KSQEGNQFQK GFGGFGGILR YKVDFQDYAV
     VEDDLDEFI