ICT1_AILME
ID ICT1_AILME Reviewed; 206 AA.
AC D2HD32;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 25-MAY-2022, entry version 44.
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;
GN ORFNames=PANDA_008549;
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(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; GL192703; EFB25606.1; -; Genomic_DNA.
DR RefSeq; XP_002919882.1; XM_002919836.3.
DR AlphaFoldDB; D2HD32; -.
DR SMR; D2HD32; -.
DR STRING; 9646.ENSAMEP00000009573; -.
DR Ensembl; ENSAMET00000033921; ENSAMEP00000026977; ENSAMEG00000027504.
DR GeneID; 100466987; -.
DR KEGG; aml:100466987; -.
DR CTD; 3396; -.
DR eggNOG; KOG3429; Eukaryota.
DR GeneTree; ENSGT00390000013268; -.
DR HOGENOM; CLU_089470_6_1_1; -.
DR InParanoid; D2HD32; -.
DR OMA; IIRSQEA; -.
DR OrthoDB; 1611415at2759; -.
DR TreeFam; TF315161; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Hydrolase; Mitochondrion; Protein biosynthesis; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..206
FT /note="Peptidyl-tRNA hydrolase ICT1, mitochondrial"
FT /id="PRO_0000394241"
SQ SEQUENCE 206 AA; 23697 MW; 349A03FC8B8FA04C CRC64;
MATAWCLPWT LRRAGAWLLT PPLRCPRRAL HKQADGTEFQ SIYSLDKLYP ESRGSDTAWK
VPDDAQQTNK DIPLDRLTIS YCRSSGPGGQ NVNKVNSKAE VRFHLATAEW IAEPVRQKMA
IMHKNKINRS GELILTSECS RYQFRNLADC LQKIRDMIAE ASQTPKEPSK EDAALHRIRI
ENMNRERLRK KRIHSAIKTG RRVDMD
