MMF1_SCHPO
ID MMF1_SCHPO Reviewed; 162 AA.
AC O43003;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
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=pmf1; ORFNames=SPBC2G2.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12185840; DOI=10.1002/yea.868;
RA Marchini A., Accardi R., Malanchi I., Schyr E., Oxelmark E., De Pinto V.,
RA Jauniaux J.-C., Maundrell K., Tommasino M.;
RT "Schizosaccharomyces pombe Pmf1p is structurally and functionally related
RT to Mmf1p of Saccharomyces cerevisiae.";
RL Yeast 19:703-711(2002).
CC -!- FUNCTION: Plays a role in the maintenance of mitochondrial DNA.
CC {ECO:0000269|PubMed:12185840}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12185840}.
CC Cytoplasm {ECO:0000269|PubMed:12185840}.
CC -!- SIMILARITY: Belongs to the RutC family. {ECO:0000305}.
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DR EMBL; CU329671; CAA17884.1; -; Genomic_DNA.
DR PIR; T40143; T40143.
DR RefSeq; NP_596433.1; NM_001022352.2.
DR AlphaFoldDB; O43003; -.
DR SMR; O43003; -.
DR BioGRID; 276989; 3.
DR STRING; 4896.SPBC2G2.04c.1; -.
DR iPTMnet; O43003; -.
DR MaxQB; O43003; -.
DR PaxDb; O43003; -.
DR PRIDE; O43003; -.
DR EnsemblFungi; SPBC2G2.04c.1; SPBC2G2.04c.1:pep; SPBC2G2.04c.
DR GeneID; 2540461; -.
DR KEGG; spo:SPBC2G2.04c; -.
DR PomBase; SPBC2G2.04c; mmf1.
DR VEuPathDB; FungiDB:SPBC2G2.04c; -.
DR eggNOG; KOG2317; Eukaryota.
DR HOGENOM; CLU_100715_7_2_1; -.
DR InParanoid; O43003; -.
DR OMA; GSYFKEP; -.
DR PhylomeDB; O43003; -.
DR PRO; PR:O43003; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR GO; GO:0019239; F:deaminase activity; IBA:GO_Central.
DR GO; GO:0009097; P:isoleucine biosynthetic process; ISO:PomBase.
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 3: Inferred from homology;
KW Cytoplasm; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT CHAIN ?..162
FT /note="Protein mmf1, mitochondrial"
FT /id="PRO_0000036210"
SQ SEQUENCE 162 AA; 17543 MW; 04C34DD516C0BB38 CRC64;
MLRALGSRLL VASRPAAYRS FQQSLRPVPR FFIHKMSTKT PINSPKLSSA GPYNQAIKAN
GVIYCSGQIP VANGKVIEGT VGDQTRQCLL NLQEVLTEAG SSLNKIVKVN IFLADMDDFA
AVNKVYTEVL PDPKPARSCV AVKTVPLSTQ GVKIEIECIA LE
