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Database: UniProt
Entry: C4WT47_ACYPI
LinkDB: C4WT47_ACYPI
Original site: C4WT47_ACYPI 
ID   C4WT47_ACYPI            Unreviewed;       160 AA.
AC   C4WT47;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=peptidyl-tRNA hydrolase {ECO:0000256|ARBA:ARBA00013260};
DE            EC=3.1.1.29 {ECO:0000256|ARBA:ARBA00013260};
GN   Name=ACYPI008026 {ECO:0000313|EMBL:BAH71067.1};
GN   Synonyms=100167214 {ECO:0000313|EnsemblMetazoa:NP_001155737.1};
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:BAH71067.1};
RN   [1] {ECO:0000313|EMBL:BAH71067.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LSR1 {ECO:0000313|EMBL:BAH71067.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:BAH71067.1};
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_001155737.1}
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; AK340463; BAH71067.1; -; mRNA.
DR   RefSeq; NP_001155737.1; NM_001162265.2.
DR   AlphaFoldDB; C4WT47; -.
DR   EnsemblMetazoa; NM_001162265.2; NP_001155737.1; GeneID_100167214.
DR   GeneID; 100167214; -.
DR   KEGG; api:100167214; -.
DR   CTD; 51651; -.
DR   Proteomes; UP000007819; 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   Gene3D; 3.40.1490.10; Bit1; 1.
DR   InterPro; IPR023476; Pep_tRNA_hydro_II_dom_sf.
DR   InterPro; IPR002833; PTH2.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007819};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   160 AA;  17666 MW;  396A71371C7618B9 CRC64;
     MTFTNDKMYD GLILGVLIGL ALNAIYNYTF KTKCTSQDAK SVGKSQQQEP KSIPNKKGEF
     KMALLVRHDL KMGKGKVAAQ CAVVSVIAYN KTKLRNLPSK CARVVLRAPD LKTLECIQKQ
     CKLFDIPTAT FTENDQITVL AIGPANETSI NAQVHSLKLY
//
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