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-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE) DE YME1 PROTEIN (EC 3.4.24.-) (TAT-BINDING HOMOLOG 11) (OSD1 PROTEIN). GN YME1 OR YTA11 OR OSD1 OR YP9367.04. OS SACCHAROMYCES CEREVISIAE (BAKER'S YEAST). OC EUKARYOTA; FUNGI; ASCOMYCOTINA; HEMIASCOMYCETES. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 93360977. RA THORSNESS P.E., WHITE K.H., FOX T.D.; 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.; 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.; 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., RAJANDREAM M.A.; RL SUBMITTED (MAY-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. 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 AND REQUIRES A ZINC ATOM (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE AAA FAMILY OF ATPASES. 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; G295582; -. DR EMBL; X81067; G531752; -. DR EMBL; D16332; G684978; -. DR EMBL; Z49274; G809589; -. DR LISTA; SC01409; YME1. DR SGD; L0002522; YME1. DR PROSITE; PS00674; AAA. 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; E8F0EECD CRC32; 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 //