ID Q86Y79 PRELIMINARY; PRT; 214 AA. AC Q86Y79; DT 01-JUN-2003 (TrEMBLrel. 24, Created) DT 01-JUN-2003 (TrEMBLrel. 24, Last sequence update) DT 01-MAR-2004 (TrEMBLrel. 26, Last annotation update) DE C9orf115 protein. GN Name=C9orf115; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Placenta; RX MEDLINE=22388257; PubMed=12477932; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., RA Krzywinski M.I., Skalska U., Smailus D.E., Schnerch A., Schein J.E., RA Jones S.J., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Placenta; RA Director MGC Project; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The natural substrate for this enzyme may be peptidyl- CC tRNAs which drop off the ribosome during protein synthesis (By CC similarity). CC -!- CATALYTIC ACTIVITY: N-substituted aminoacyl-tRNA + H(2)O = N- CC substituted amino acid + tRNA. CC -!- SUBCELLULAR LOCATION: Cytoplasmic (By similarity). CC -!- SIMILARITY: Belongs to the PTH family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC047012; AAH47012.1; -. DR HSSP; P23932; 2PTH. DR GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IEA. DR GO; GO:0006412; P:protein biosynthesis; IEA. DR InterPro; IPR001328; PeptRNAhydrolase. DR Pfam; PF01195; Pept_tRNA_hydro; 1. DR ProDom; PD005324; PeptRNAhydrolase; 1. DR PROSITE; PS01196; PEPT_TRNA_HYDROL_2; UNKNOWN_1. KW Hydrolase. SQ SEQUENCE 214 AA; 22936 MW; DBA3959411DA8248 CRC64; MRPGGFLGAG QRLSRAMSRC VLEPRPPGKR WMVAGLGNPG LPGTRHSVGM AVLGQLARRL GVAESWTRDR HCAADLALAP LGDAQLVLLR PRRLMNANGR SVARAAELFG LTAEEVYLVH DELDKPLGRL ALKLGGSARG HNGVRSCISC LNSNAMPRLR VGIGRPAHPE AVQAHVLGCF SPAEQELLPL LLDRATDLIL DHIRERSQGP SLGP //