MMF1_YEAST
ID MMF1_YEAST Reviewed; 145 AA.
AC P40185; D6VVN0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Protein MMF1, mitochondrial;
DE AltName: Full=Isoleucine biosynthesis and maintenance of intact mitochondria 1;
DE AltName: Full=Maintenance of mitochondrial function 1;
DE Flags: Precursor;
GN Name=MMF1; Synonyms=IBM1; OrderedLocusNames=YIL051C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND
RP CHARACTERIZATION.
RX PubMed=11442631; DOI=10.1046/j.1365-2443.2001.00443.x;
RA Kim J.-M., Yoshikawa H., Shirahige K.;
RT "A member of the YER057c/yjgf/Uk114 family links isoleucine biosynthesis
RT and intact mitochondria maintenance in Saccharomyces cerevisiae.";
RL Genes Cells 6:507-517(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP PROTEIN SEQUENCE OF 18-28.
RC STRAIN=ATCC 26786 / X2180-1A;
RA Frutiger S., Paquet N., Pasquali C., Ravier F., Sanchez J.-C., Hughes G.J.,
RA Hochstrasser D.F.;
RL Submitted (JUN-1995) to UniProtKB.
RN [6]
RP PROTEIN SEQUENCE OF N-TERMINUS, SUBCELLULAR LOCATION, AND CHARACTERIZATION.
RX PubMed=11003673; DOI=10.1128/mcb.20.20.7784-7797.2000;
RA Oxelmark E., Marchini A., Malanchi I., Magherini F., Jaquet L.,
RA Hajibagheri M.A., Blight K.J., Jauniaux J.-C., Tommasino M.;
RT "Mmf1p, a novel yeast mitochondrial protein conserved throughout evolution
RT and involved in maintenance of the mitochondrial genome.";
RL Mol. Cell. Biol. 20:7784-7797(2000).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Plays a role in the maintenance of mitochondrial DNA.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:11003673, ECO:0000269|PubMed:11442631}.
CC -!- MISCELLANEOUS: Present with 168000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RutC family. {ECO:0000305}.
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; AB050474; BAB20814.1; -; Genomic_DNA.
DR EMBL; Z38060; CAA86171.1; -; Genomic_DNA.
DR EMBL; AY558301; AAS56627.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08496.1; -; Genomic_DNA.
DR PIR; S48428; S48428.
DR RefSeq; NP_012213.3; NM_001179401.3.
DR PDB; 3QUW; X-ray; 1.75 A; A=1-145.
DR PDBsum; 3QUW; -.
DR AlphaFoldDB; P40185; -.
DR SMR; P40185; -.
DR BioGRID; 34939; 102.
DR DIP; DIP-4714N; -.
DR IntAct; P40185; 6.
DR MINT; P40185; -.
DR STRING; 4932.YIL051C; -.
DR iPTMnet; P40185; -.
DR SWISS-2DPAGE; P40185; -.
DR MaxQB; P40185; -.
DR PaxDb; P40185; -.
DR PRIDE; P40185; -.
DR TopDownProteomics; P40185; -.
DR EnsemblFungi; YIL051C_mRNA; YIL051C; YIL051C.
DR GeneID; 854760; -.
DR KEGG; sce:YIL051C; -.
DR SGD; S000001313; MMF1.
DR VEuPathDB; FungiDB:YIL051C; -.
DR eggNOG; KOG2317; Eukaryota.
DR GeneTree; ENSGT00420000029792; -.
DR HOGENOM; CLU_100715_7_2_1; -.
DR InParanoid; P40185; -.
DR OMA; ATDKAPQ; -.
DR BioCyc; YEAST:G3O-31322-MON; -.
DR PRO; PR:P40185; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40185; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0019239; F:deaminase activity; IBA:GO_Central.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IMP:SGD.
DR GO; GO:0032543; P:mitochondrial translation; IGI:SGD.
DR GO; GO:1901565; P:organonitrogen compound catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.1330.40; -; 1.
DR InterPro; IPR006056; RidA.
DR InterPro; IPR019897; RidA_CS.
DR InterPro; IPR035959; RutC-like_sf.
DR InterPro; IPR006175; YjgF/YER057c/UK114.
DR PANTHER; PTHR11803; PTHR11803; 1.
DR Pfam; PF01042; Ribonuc_L-PSP; 1.
DR SUPFAM; SSF55298; SSF55298; 1.
DR TIGRFAMs; TIGR00004; TIGR00004; 1.
DR PROSITE; PS01094; UPF0076; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Mitochondrion; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..17
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:11003673, ECO:0000269|Ref.5"
FT CHAIN 18..145
FT /note="Protein MMF1, mitochondrial"
FT /id="PRO_0000036209"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:3QUW"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:3QUW"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:3QUW"
FT HELIX 65..82
FT /evidence="ECO:0007829|PDB:3QUW"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:3QUW"
FT STRAND 90..98
FT /evidence="ECO:0007829|PDB:3QUW"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:3QUW"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:3QUW"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:3QUW"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:3QUW"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:3QUW"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:3QUW"
SQ SEQUENCE 145 AA; 15908 MW; F2DC4E32C04CED45 CRC64;
MFLRNSVLRT APVLRRGITT LTPVSTKLAP PAAASYSQAM KANNFVYVSG QIPYTPDNKP
VQGSISEKAE QVFQNVKNIL AESNSSLDNI VKVNVFLADM KNFAEFNSVY AKHFHTHKPA
RSCVGVASLP LNVDLEMEVI AVEKN
