ID YME1_YEAST STANDARD; PRT; 747 AA. AC P32795; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE YME1 PROTEIN (EC 3.4.24.-) (TAT-BINDING HOMOLOG 11) (OSD1 PROTEIN). GN YME1 OR YTA11 OR OSD1 OR YPR024W OR YP9367.04. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycetes; Saccharomycetales; OC Saccharomycetaceae; Saccharomyces. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 93360977. RA Thorsness P.E., White K.H., Fox T.D.; RT "Inactivation of YME1, a member of the ftsH-SEC18-PAS1-CDC48 family RT of putative ATPase-encoding genes, causes increased escape of DNA RT from mitochondria in Saccharomyces cerevisiae."; RL Mol. Cell. Biol. 13:5418-5426(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=S288C; RX MEDLINE; 95274317. RA Schnall R., Mannhaupt G., Stucka R., Tauer R., Ehnle S., RA Schwarzlose C., Vetter I., Feldmann H.; RT "Identification of a set of yeast genes coding for a novel family of RT putative ATPases with high similarity to constituents of the 26S RT protease complex."; RL Yeast 10:1141-1155(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=D273-10B; RX MEDLINE; 95349611. RA Nakai T., Yasuhara T., Fujiki Y., Ohashi A.; RT "Multiple genes, including a member of the AAA family, are essential RT for degradation of unassembled subunit 2 of cytochrome c oxidase in RT yeast mitochondria."; RL Mol. Cell. Biol. 15:4441-4452(1995). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=S288C / AB972; RA Badcock K., Churcher C.M., Barrell B.G., Rajandream M.A.; RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: PUTATIVE ATP-DEPENDENT PROTEASE. CAUSES AN INCREASED CC ESCAPE OF DNA FROM MITOCHONDRIA. IMPORTANT TO MAINTAIN THE CC INTEGRITY OF THE MITOCHONDRIAL COMPARTMENT. REQUIRED BOTH FOR THE CC DEGRADATION OF UNASSEMBLED SUBUNIT 2 OF CYTOCHROME C OXIDASE AND CC FOR EFFICIENT ASSEMBLY OF MITOCHONDRIAL RESPIRATORY CHAIN. CC -!- COFACTOR: BINDS ONE ZINC ION (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE AAA FAMILY OF ATPASES. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY M41 (ZINC CC METALLOPROTEASE). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; L14616; AAA02883.1; -. DR EMBL; X81067; CAA56954.1; -. DR EMBL; D16332; BAA03839.1; -. DR EMBL; Z49274; CAA89278.1; -. DR EMBL; Z71255; CAA95020.1; -. DR SGD; L0002522; YME1. DR INTERPRO; IPR000642; -. DR INTERPRO; IPR001939; -. DR PFAM; PF00004; AAA; 1. DR PFAM; PF01434; Peptidase_M41; 1. DR PROSITE; PS00674; AAA; 1. KW ATP-binding; Mitochondrion; Hydrolase; Metalloprotease; Zinc. FT NP_BIND 321 328 ATP (POTENTIAL). FT METAL 540 540 ZINC (CATALYTIC) (BY SIMILARITY). FT ACT_SITE 541 541 BY SIMILARITY. FT METAL 544 544 ZINC (CATALYTIC) (BY SIMILARITY). FT CONFLICT 52 52 N -> T (IN REF. 2). FT CONFLICT 88 88 T -> N (IN REF. 2). FT CONFLICT 584 584 T -> A (IN REF. 3). SQ SEQUENCE 747 AA; 81771 MW; CA7C5C90097C4F8B CRC64; MNVSKILVSP TVTTNVLRIF APRLPQIGAS LLVQKKWALR SKKFYRFYSE KNSGEMPPKK EADSSGKASN KSTISSIDNS QPPPPSNTND KTKQANVAVS HAMLATREQE ANKDLTSPDA QAAFYKLLLQ SNYPQYVVSR FETPGIASSP ECMELYMEAL QRIGRHSEAD AVRQNLLTAS SAGAVNPSLA SSSSNQSGYH GNFPSMYSPL YGSRKEPLHV VVSESTFTVV SRWVKWLLVF GILTYSFSEG FKYITENTTL LKSSEVADKS VDVAKTNVKF DDVCGCDEAR AELEEIVDFL KDPTKYESLG GKLPKGVLLT GPPGTGKTLL ARATAGEAGV DFFFMSGSEF DEVYVGVGAK RIRDLFAQAR SRAPAIIFID ELDAIGGKRN PKDQAYAKQT LNQLLVELDG FSQTSGIIII GATNFPEALD KALTRPGRFD KVVNVDLPDV RGRADILKHH MKKITLADNV DPTIIARGTP GLSGAELANL VNQAAVYACQ KNAVSVDMSH FEWAKDKILM GAERKTMVLT DAARKATAFH EAGHAIMAKY TNGATPLYKA TILPRGRALG ITFQLPEMDK VDITKRECQA RLDVCMGGKI AEELIYGKDN TTSGCGSDLQ SATGTARAMV TQYGMSDDVG PVNLSENWES WSNKIRDIAD NEVIELLKDS EERARRLLTK KNVELHRLAQ GLIEYETLDA HEIEQVCKGE KLDKLKTSTN TVVEGPDSDE RKDIGDDKPK IPTMLNA //