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 05-JUL-2004 (Rel. 44, Last annotation update) DE YME1 protein (EC 3.4.24.-) (TAT-binding homolog 11) (OSD1 protein). GN Name=YME1; Synonyms=OSD1, YTA11; OrderedLocusNames=YPR024W; GN ORFNames=YP9367.04; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93360977; PubMed=8355690; RA Thorsness P.E., White K.H., Fox T.D.; RT "Inactivation of YME1, a member of the ftsH-SEC18-PAS1-CDC48 family of RT putative ATPase-encoding genes, causes increased escape of DNA from RT 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; PubMed=7754704; 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; PubMed=7623837; 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; RX MEDLINE=97313271; PubMed=9169875; RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., RA Botstein D., Bowman S., Bruckner M., Carpenter J., Cherry J.M., RA Chung E., Churcher C.M., Coster F., Davis K., Davis R.W., RA Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., RA Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., RA Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., RA Hunicke-Smith S., Hyman R., Johnston M., Kalman S., Kleine K., RA Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., RA Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., RA Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., RA Petel F.X., Pohl T.M., Purnelle D., Schafer M., Scharfe M., RA Scherens B., Schramm S., Schroeder M., Sdicu A.M., Tettelin H., RA Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., RA Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., RA Zhong W.W., Zollner A., Vo D.H., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."; RL Nature 387:103-105(1997). 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 1 zinc ion (Potential). CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase CC family. CC -!- SIMILARITY: In the C-terminal section; belongs to peptidase family CC M41. 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 PIR; S54498; S46608. DR HSSP; P28691; 1LV7. DR GermOnline; 144289; -. DR MEROPS; M41.004; -. DR SGD; S0006228; YME1. DR GO; GO:0005739; C:mitochondrion; IDA. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR003959; AAA_ATPase_centr. DR InterPro; IPR003960; AAA_sub. DR InterPro; IPR000642; Peptidase_M41. DR InterPro; IPR005936; Pept_M41_FtsH. DR Pfam; PF00004; AAA; 1. DR Pfam; PF01434; Peptidase_M41; 1. DR SMART; SM00382; AAA; 1. DR TIGRFAMs; TIGR01241; FtsH_fam; 1. DR PROSITE; PS00674; AAA; 1. KW ATP-binding; Hydrolase; Metalloprotease; Mitochondrion; 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 //