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Database: UniProt
Entry: C4WXX0_ACYPI
LinkDB: C4WXX0_ACYPI
Original site: C4WXX0_ACYPI 
ID   C4WXX0_ACYPI            Unreviewed;       160 AA.
AC   C4WXX0;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   RecName: Full=peptidyl-tRNA hydrolase {ECO:0000256|ARBA:ARBA00013260};
DE            EC=3.1.1.29 {ECO:0000256|ARBA:ARBA00013260};
GN   Name=ACYPI008234 {ECO:0000313|EMBL:BAH72740.1};
GN   Synonyms=100167437 {ECO:0000313|EnsemblMetazoa:NP_001155748.1};
OS   Acyrthosiphon pisum (Pea aphid).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Aphidomorpha;
OC   Aphidoidea; Aphididae; Macrosiphini; Acyrthosiphon.
OX   NCBI_TaxID=7029 {ECO:0000313|EMBL:BAH72740.1};
RN   [1] {ECO:0000313|EMBL:BAH72740.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LSR1 {ECO:0000313|EMBL:BAH72740.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:BAH72740.1};
RA   Shigenobu S., Nakabachi A., Richards S.;
RT   "A full-length cDNA resource of the pea aphid, Acyrthosiphon pisum.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LSR1 {ECO:0000313|Proteomes:UP000007819};
RA   Jiang H., Abraham K., Ali S., Alsbrooks S.L., Anim B.N., Anosike U.S.,
RA   Attaway T., Bandaranaike D.P., Battles P.K., Bell S.N., Bell A.V.,
RA   Beltran B., Bickham C., Bustamante Y., Caleb T., Canada A., Cardenas V.,
RA   Carter K., Chacko J., Chandrabose M.N., Chavez D., Chavez A., Chen L.,
RA   Chu H.-S., Claassen K.J., Cockrell R., Collins M., Cooper J.A., Cree A.,
RA   Curry S.M., Da Y., Dao M.D., Das B., Davila M.-L., Davy-Carroll L.,
RA   Denson S., Dinh H., Ebong V.E., Edwards J.R., Egan A., El-Daye J.,
RA   Escobedo L., Fernandez S., Fernando P.R., Flagg N., Forbes L.D.,
RA   Fowler R.G., Fu Q., Gabisi R.A., Ganer J., Garbino Pronczuk A.,
RA   Garcia R.M., Garner T., Garrett T.E., Gonzalez D.A., Hamid H.,
RA   Hawkins E.S., Hirani K., Hogues M.E., Hollins B., Hsiao C.-H., Jabil R.,
RA   James M.L., Jhangiani S.N., Johnson B., Johnson Q., Joshi V., Kalu J.B.,
RA   Kam C., Kashfia A., Keebler J., Kisamo H., Kovar C.L., Lago L.A.,
RA   Lai C.-Y., Laidlaw J., Lara F., Le T.-K., Lee S.L., Legall F.H.,
RA   Lemon S.J., Lewis L.R., Li B., Liu Y., Liu Y.-S., Lopez J., Lozado R.J.,
RA   Lu J., Madu R.C., Maheshwari M., Maheshwari R., Malloy K., Martinez E.,
RA   Mathew T., Mercado I.C., Mercado C., Meyer B., Montgomery K., Morgan M.B.,
RA   Munidasa M., Nazareth L.V., Nelson J., Ng B.M., Nguyen N.B., Nguyen P.Q.,
RA   Nguyen T., Obregon M., Okwuonu G.O., Onwere C.G., Orozco G., Parra A.,
RA   Patel S., Patil S., Perez A., Perez Y., Pham C., Primus E.L., Pu L.-L.,
RA   Puazo M., Qin X., Quiroz J.B., Reese J., Richards S., Rives C.M.,
RA   Robberts R., Ruiz S.J., Ruiz M.J., Santibanez J., Schneider B.W.,
RA   Sisson I., Smith M., Sodergren E., Song X.-Z., Song B.B., Summersgill H.,
RA   Thelus R., Thornton R.D., Trejos Z.Y., Usmani K., Vattathil S.,
RA   Villasana D., Walker D.L., Wang S., Wang K., White C.S., Williams A.C.,
RA   Williamson J., Wilson K., Woghiren I.O., Woodworth J.R., Worley K.C.,
RA   Wright R.A., Wu W., Young L., Zhang L., Zhang J., Zhu Y., Muzny D.M.,
RA   Weinstock G., Gibbs R.A.;
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:NP_001155748.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2022) to UniProtKB.
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; AK342892; BAH72740.1; -; mRNA.
DR   RefSeq; NP_001155748.1; NM_001162276.2.
DR   AlphaFoldDB; C4WXX0; -.
DR   EnsemblMetazoa; NM_001162276.2; NP_001155748.1; LOC100167437.
DR   GeneID; 100167437; -.
DR   KEGG; api:100167437; -.
DR   eggNOG; KOG3282; Eukaryota.
DR   HOGENOM; CLU_073661_2_2_1; -.
DR   InParanoid; C4WXX0; -.
DR   OMA; RGDLKMS; -.
DR   OrthoDB; 169876at2759; -.
DR   Proteomes; UP000007819; Unassembled WGS sequence.
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   2: Evidence at transcript level;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007819}.
SQ   SEQUENCE   160 AA;  17232 MW;  FC299E226F34B819 CRC64;
     MFDISNYEFI TPFVVGLLVG TGVSYSYRNI RPLLFGPLNA LSVNNKLVLV VRNDLGMTKG
     KIAAQCSHAS VECYKAAMQH KPQMAKMWQM TGQKKIVVSI GNGEKGLQEL SKVAKSHKVL
     SCIVYDAGAT QVKAGTPTVI GIGPANSDVI DQITGHLKLI
//
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