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Database: UniProt
Entry: I1LIQ7_SOYBN
LinkDB: I1LIQ7_SOYBN
Original site: I1LIQ7_SOYBN 
ID   I1LIQ7_SOYBN            Unreviewed;       190 AA.
AC   I1LIQ7;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=peptidyl-tRNA hydrolase {ECO:0000256|ARBA:ARBA00013260};
DE            EC=3.1.1.29 {ECO:0000256|ARBA:ARBA00013260};
GN   ORFNames=GLYMA_11G098800 {ECO:0000313|EMBL:KRH29121.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH29121.1};
RN   [1] {ECO:0000313|EMBL:KRH29121.1, ECO:0000313|EnsemblPlants:KRH29121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH29121};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH29121.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRH29121}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH29121};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH29121.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH29121.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs
CC       which drop off the ribosome during protein synthesis.
CC       {ECO:0000256|ARBA:ARBA00003043}.
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; Evidence={ECO:0000256|ARBA:ARBA00033690};
CC   -!- SIMILARITY: Belongs to the PTH2 family.
CC       {ECO:0000256|ARBA:ARBA00038050}.
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DR   EMBL; CM000844; KRH29121.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1LIQ7; -.
DR   SMR; I1LIQ7; -.
DR   STRING; 3847.I1LIQ7; -.
DR   PaxDb; 3847-GLYMA11G10490-1; -.
DR   EnsemblPlants; KRH29121; KRH29121; GLYMA_11G098800.
DR   Gramene; KRH29121; KRH29121; GLYMA_11G098800.
DR   eggNOG; KOG3282; Eukaryota.
DR   HOGENOM; CLU_073661_0_3_1; -.
DR   InParanoid; I1LIQ7; -.
DR   OMA; GHAAVEC; -.
DR   Proteomes; UP000008827; Chromosome 11.
DR   ExpressionAtlas; I1LIQ7; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IBA:GO_Central.
DR   CDD; cd02430; PTH2; 1.
DR   Gene3D; 3.40.1490.10; Bit1; 1.
DR   InterPro; IPR023476; Pep_tRNA_hydro_II_dom_sf.
DR   InterPro; IPR002833; PTH2.
DR   NCBIfam; TIGR00283; arch_pth2; 1.
DR   PANTHER; PTHR12649; PEPTIDYL-TRNA HYDROLASE 2; 1.
DR   PANTHER; PTHR12649:SF11; PEPTIDYL-TRNA HYDROLASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF01981; PTH2; 1.
DR   SUPFAM; SSF102462; Peptidyl-tRNA hydrolase II; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008827}.
SQ   SEQUENCE   190 AA;  21207 MW;  6B65CA0C8646C399 CRC64;
     MDLTWLSAIL VGAGYLALGY FIGSQYPPRF LFSHKLSTKH KEDASLLNDN DNKKRNTKSK
     LKDPLEIEQL AEILDDFKMI LVVRNDLKMG KGKIAAQCSH ATLGLYKKIL RRAPKALNRW
     EMSAQPKVVV KIESEEDMLA LQERAKSLKL PTHITIDAGR TQIAPNSRTV MAILGPVEVV
     DEVTGGLKLL
//
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