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Database: UniProt
Entry: L8IR93_9CETA
LinkDB: L8IR93_9CETA
Original site: L8IR93_9CETA 
ID   L8IR93_9CETA            Unreviewed;       180 AA.
AC   L8IR93;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=peptidyl-tRNA hydrolase {ECO:0000256|ARBA:ARBA00013260};
DE            EC=3.1.1.29 {ECO:0000256|ARBA:ARBA00013260};
DE   Flags: Fragment;
GN   ORFNames=M91_15748 {ECO:0000313|EMBL:ELR58836.1};
OS   Bos mutus (wild yak).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=72004 {ECO:0000313|EMBL:ELR58836.1, ECO:0000313|Proteomes:UP000011080};
RN   [1] {ECO:0000313|EMBL:ELR58836.1, ECO:0000313|Proteomes:UP000011080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=yakQH1 {ECO:0000313|Proteomes:UP000011080};
RX   PubMed=22751099; DOI=10.1038/ng.2343;
RA   Qiu Q., Zhang G., Ma T., Qian W., Wang J., Ye Z., Cao C., Hu Q., Kim J.,
RA   Larkin D.M., Auvil L., Capitanu B., Ma J., Lewin H.A., Qian X., Lang Y.,
RA   Zhou R., Wang L., Wang K., Xia J., Liao S., Pan S., Lu X., Hou H., Wang Y.,
RA   Zang X., Yin Y., Ma H., Zhang J., Wang Z., Zhang Y., Zhang D., Yonezawa T.,
RA   Hasegawa M., Zhong Y., Liu W., Zhang Y., Huang Z., Zhang S., Long R.,
RA   Yang H., Wang J., Lenstra J.A., Cooper D.N., Wu Y., Wang J., Shi P.,
RA   Wang J., Liu J.;
RT   "The yak genome and adaptation to life at high altitude.";
RL   Nat. Genet. 44:946-949(2012).
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; JH880797; ELR58836.1; -; Genomic_DNA.
DR   AlphaFoldDB; L8IR93; -.
DR   STRING; 72004.ENSBMUP00000006178; -.
DR   Proteomes; UP000011080; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:ELR58836.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011080};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        16..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ELR58836.1"
SQ   SEQUENCE   180 AA;  19419 MW;  7EC2B9166E3C4795 CRC64;
     QMISRSLVME YLTNPGALSL AAGVACGVCL GWGLRMRFGM LPKSSVRETN PDTETEASIL
     GESGEYKMIL VVRNDLKMGK GKVAAQCSHA AVSAYKQIQR RNPELLKEWE YCGQPKVVVK
     APDEETLVEL LTHAKVLGLT VSLIQDAGRT QIAPGSRTVL GIGPGPADLI DKVTGHLKLY
//
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