ID YME1_YEAST Reviewed; 747 AA. AC P32795; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 04-DEC-2007, entry version 74. DE Protein YME1 (EC 3.4.24.-) (TAT-binding homolog 11) (Protein OSD1). GN Name=YME1; Synonyms=OSD1, YTA11; OrderedLocusNames=YPR024W; GN ORFNames=YP9367.04; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 24657 / 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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204511 / 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., Brueckner 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.W., 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 B., Rajandream M.A., Rechmann S., RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., RA Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., RA Zollner A., Vo D.H., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."; RL Nature 387:103-105(1997). RN [5] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923954; PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [6] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). 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 -!- INTERACTION: CC P25573:-; NbExp=1; IntAct=EBI-27785, EBI-21740; CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- MISCELLANEOUS: Present with 20100 molecules/cell in log phase SD CC medium. CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase CC family. CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase CC M41 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; L14616; AAA02883.1; -; Genomic_DNA. DR EMBL; X81067; CAA56954.1; -; Genomic_DNA. DR EMBL; D16332; BAA03839.1; -; Genomic_DNA. DR EMBL; Z49274; CAA89278.1; -; Genomic_DNA. DR EMBL; Z71255; CAA95020.1; -; Genomic_DNA. DR PIR; S54498; S46608. DR RefSeq; NP_015349.1; -. DR HSSP; P28691; 1LV7. DR IntAct; P32795; -. DR MEROPS; M41.004; -. DR PeptideAtlas; P32795; -. DR Ensembl; YPR024W; Saccharomyces cerevisiae. DR GeneID; 856135; -. DR GenomeReviews; U00094_GR; YPR024W. DR KEGG; sce:YPR024W; -. DR CYGD; YPR024w; -. DR SGD; S000006228; YME1. DR LinkHub; P32795; -. DR GermOnline; YPR024W; Saccharomyces cerevisiae. DR GO; GO:0031942; C:i-AAA complex; IDA:SGD. DR GO; GO:0004176; F:ATP-dependent peptidase activity; TAS:SGD. DR GO; GO:0007005; P:mitochondrion organization and biogenesis; TAS:SGD. DR InterPro; IPR003593; AAA+_ATPase_core. DR InterPro; IPR003959; AAA_ATPase_core. DR InterPro; IPR003960; AAA_ATPase_sub. DR InterPro; IPR005936; Pept_M41_FtsH. DR InterPro; IPR000642; Peptidase_M41. 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. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Hydrolase; Membrane; Metal-binding; KW Metalloprotease; Mitochondrion; Nucleotide-binding; Protease; Zinc. FT CHAIN 1 747 Protein YME1. FT /FTId=PRO_0000084664. FT NP_BIND 321 328 ATP (Potential). FT ACT_SITE 541 541 By similarity. FT METAL 540 540 Zinc (catalytic) (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; 81772 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 //