CO111_SCHPO
ID CO111_SCHPO Reviewed; 753 AA.
AC Q9UTM2;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Rsm22-cox11 tandem protein 1, mitochondrial;
DE Contains:
DE RecName: Full=37S ribosomal protein S22-1;
DE EC=2.1.1.-;
DE Contains:
DE RecName: Full=Cytochrome c oxidase assembly protein cox11-1;
DE Flags: Precursor;
GN Name=cox1101; Synonyms=cox11, cox11-a;
GN ORFNames=SPAC1420.04c, SPAPB17E12.01c;
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 PROTEOLYTIC CLEAVAGE, AND SUBCELLULAR LOCATION.
RX PubMed=16835444; DOI=10.1128/ec.00092-06;
RA Khalimonchuk O., Ott M., Funes S., Ostermann K., Roedel G., Herrmann J.M.;
RT "Sequential processing of a mitochondrial tandem protein: insights into
RT protein import in Schizosaccharomyces pombe.";
RL Eukaryot. Cell 5:997-1006(2006).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Rsm22-1 is involved in mitochondrion-encoded protein
CC synthesis. {ECO:0000250}.
CC -!- FUNCTION: Cox11-1 exerts its effect at some terminal stage of
CC cytochrome c oxidase synthesis, probably by being involved in the
CC insertion of the copper B into subunit I. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [37S ribosomal protein S22-1]: Mitochondrion
CC matrix {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Cytochrome c oxidase assembly protein cox11-1]:
CC Mitochondrion inner membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}; Intermembrane side {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo by mitochondrial processing
CC peptidase (MPP) yield mature proteins including rsm22-1 and cox11-1.
CC {ECO:0000269|PubMed:16835444}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the methyltransferase
CC superfamily. Rsm22 family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the COX11/CtaG
CC family. {ECO:0000305}.
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DR EMBL; CU329670; CAB57323.2; -; Genomic_DNA.
DR RefSeq; NP_593279.2; NM_001018675.2.
DR AlphaFoldDB; Q9UTM2; -.
DR SMR; Q9UTM2; -.
DR BioGRID; 279274; 2.
DR STRING; 4896.SPAC1420.04c.1; -.
DR MaxQB; Q9UTM2; -.
DR PaxDb; Q9UTM2; -.
DR EnsemblFungi; SPAC1420.04c.1; SPAC1420.04c.1:pep; SPAC1420.04c.
DR GeneID; 2542827; -.
DR KEGG; spo:SPAC1420.04c; -.
DR PomBase; SPAC1420.04c; cox1101.
DR VEuPathDB; FungiDB:SPAC1420.04c; -.
DR eggNOG; KOG2539; Eukaryota.
DR eggNOG; KOG2540; Eukaryota.
DR HOGENOM; CLU_425883_0_0_1; -.
DR InParanoid; Q9UTM2; -.
DR OMA; LPWKEES; -.
DR PhylomeDB; Q9UTM2; -.
DR PRO; PR:Q9UTM2; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031304; C:intrinsic component of mitochondrial inner membrane; IDA:PomBase.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:PomBase.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0005507; F:copper ion binding; ISO:PomBase.
DR GO; GO:0008168; F:methyltransferase activity; ISM:PomBase.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; ISO:PomBase.
DR GO; GO:0032543; P:mitochondrial translation; TAS:PomBase.
DR Gene3D; 2.60.370.10; -; 1.
DR HAMAP; MF_00155; CtaG; 1.
DR InterPro; IPR023471; CtaG/Cox11_dom_sf.
DR InterPro; IPR007533; Cyt_c_oxidase_assmbl_CtaG.
DR InterPro; IPR015324; Ribosomal_Rsm22-like.
DR Pfam; PF04442; CtaG_Cox11; 1.
DR Pfam; PF09243; Rsm22; 1.
DR SUPFAM; SSF110111; SSF110111; 1.
PE 1: Evidence at protein level;
KW Membrane; Methyltransferase; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Transferase;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 40..753
FT /note="Rsm22-cox11 tandem protein 1, mitochondrial"
FT /id="PRO_0000352836"
FT CHAIN 40..568
FT /note="37S ribosomal protein S22-1"
FT /id="PRO_0000352837"
FT CHAIN 569..753
FT /note="Cytochrome c oxidase assembly protein cox11-1"
FT /id="PRO_0000352838"
FT TRANSMEM 571..591
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 592..753
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT SITE 568..569
FT /note="Cleavage; by mitochondrial processing peptidase"
SQ SEQUENCE 753 AA; 86175 MW; 4CDDE49F0CEC1995 CRC64;
MPILTCRYKI LFLYNLRNCF TFQNQRCLIP YGTTTTIRWY NANFQAVQNN FSDYKNELIS
SHRPEASSLL DFLVKDQKKS GDISLHTKFN LYVDDLLKKS EKGQIKKFIN DIKKDLATES
QLPLSAPFKD ESTRTMTDPQ VLAYIHQSMP YQYASLYSVL TDLKIVNSDV SCKSQHILDC
GKGPGIGALA SYSVFPTPNS VSIVEENPFL KKIIYDIHHN IYPSTSPNPT SPVTLNRLPL
GKKDSYTLVI ASNKLLEMKS EKELFDYLRS LWSLVSNDGG LLVLCERGTK RGFSLIQRAR
TFLLQKSKNT SDKQFNAHIV APCPHDGRCP IDIENGVRAN ICSFKQHFFL SPFSRLYVPR
SHRRSSDRSH YSYVVIQKGI TRPLNNTTQR FKNDEDLLEN VNVTSPTLKN WPRIIRPPLK
RDGHVIIDVC DSDARLRRNI VPKSQGKLAY RLARKSAWGD LFPLEGKVQS TSPSSKITKH
LKDASSTYSI NPPSYNKPKV ERNTTADPIF VGKRFYSTNR HKAFSRFADF NSHRFPCIFT
SFSCYNCISG TRKYSRQYSR DKFHYNQRTT IYYLVAISIF ALGLTYAAVP LYRLFCSKTG
YGGTLNTDQS RMNAERMVPR KDNKRIRVTF NGDVAGNLSW KLWPQQREIY VLPGETALGF
YTAENTSDHD IVGVATYNIV PGQAAVYFSK VACFCFEEQK LDAHEKVDLP VFFFIDPEFA
DDPNMKDIDD ILLSYTFFEA RYDTNGNLLT KLN
