ID   ICT1_SALSA              Reviewed;         191 AA.
AC   B5XAM2;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Peptidyl-tRNA hydrolase ICT1, mitochondrial;
DE            EC=3.1.1.29;
DE   AltName: Full=Immature colon carcinoma transcript 1 protein homolog;
DE   Flags: Precursor;
GN   Name=mrpl58 {ECO:0000250|UniProtKB:Q14197}; Synonyms=ict1;
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thyroid;
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
CC   -!- FUNCTION: Essential peptidyl-tRNA hydrolase component of the
CC       mitochondrial large ribosomal subunit. Acts as a codon-independent
CC       translation release factor that has lost all stop codon specificity and
CC       directs the termination of translation in mitochondrion, possibly in
CC       case of abortive elongation. May be involved in the hydrolysis of
CC       peptidyl-tRNAs that have been prematurely terminated and thus in the
CC       recycling of stalled mitochondrial ribosomes (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-
CC         amino acid + H(+); Xref=Rhea:RHEA:54448, Rhea:RHEA-COMP:10123,
CC         Rhea:RHEA-COMP:13883, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:59874, ChEBI:CHEBI:78442, ChEBI:CHEBI:138191;
CC         EC=3.1.1.29;
CC   -!- SUBUNIT: Component of the mitochondrial 39S ribosomal subunit.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. Mitochondrion-specific ribosomal protein mL62 subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: In contrast to other members of the family, lacks the regions
CC       that come into close contact with the mRNA in the ribosomal A-site and
CC       determine the STOP codon specificity, explaining the loss of codon
CC       specificity for translation release factor activity. {ECO:0000305}.
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DR   EMBL; BT048091; ACI67892.1; -; mRNA.
DR   RefSeq; NP_001134526.1; NM_001141054.1.
DR   AlphaFoldDB; B5XAM2; -.
DR   SMR; B5XAM2; -.
DR   STRING; 8030.ENSSSAP00000076936; -.
DR   GeneID; 100196025; -.
DR   KEGG; sasa:100196025; -.
DR   CTD; 3396; -.
DR   OMA; IIRSQEA; -.
DR   OrthoDB; 1611415at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa28.
DR   Bgee; ENSSSAG00000065783; Expressed in zone of skin and 16 other tissues.
DR   GO; GO:0005762; C:mitochondrial large ribosomal subunit; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; ISS:UniProtKB.
DR   GO; GO:0016150; F:translation release factor activity, codon nonspecific; ISS:UniProtKB.
DR   GO; GO:0070126; P:mitochondrial translational termination; ISS:UniProtKB.
DR   InterPro; IPR000352; Pep_chain_release_fac_I.
DR   Pfam; PF00472; RF-1; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Mitochondrion; Protein biosynthesis; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT   TRANSIT         1..34
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..191
FT                   /note="Peptidyl-tRNA hydrolase ICT1, mitochondrial"
FT                   /id="PRO_0000394242"
SQ   SEQUENCE   191 AA;  21486 MW;  AC35DF712E284657 CRC64;
     MATSVAKYFL LSRCSGIIRS VTLQGKLPPV CIRNSQCPSF SYGNRASDNP QDGHVNIPVD
     RLTVSYSRSS GPGGQHVNKV STKAEVRFHV YTADWIPEDV RQKIILNNKN RINKAGELLV
     TSEQSRSQQR NMGDCIQKIS DIIAKATEKP HEPSAEDIAL RASRLEKRNK ERLKQKKLHS
     AVKQTRRVCF D