ID CCM1_CANAL Reviewed; 768 AA.
AC Q5A8W9; A0A1D8PQ70; Q5A8P4;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Mitochondrial 15S rRNA processing factor CCM1;
DE Flags: Precursor;
GN Name=CCM1; OrderedLocusNames=CAALFM_C603440WA;
GN ORFNames=CaO19.13127, CaO19.5704;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- FUNCTION: Regulates mitochondrial small subunit maturation by
CC controlling 15S rRNA 5'-end processing. Localizes to the 5' precursor
CC of the 15S rRNA in a position that is subsequently occupied by mS47 in
CC the mature yeast mtSSU. Uses structure and sequence-specific RNA
CC recognition, binding to a single-stranded region of the precursor and
CC specifically recognizing bases -6 to -1. The exchange of Ccm1 for mS47
CC is coupled to the irreversible removal of precursor rRNA that is
CC accompanied by conformational changes of the mitoribosomal proteins
CC uS5m and mS26. These conformational changes signal completion of 5'-end
CC rRNA processing through protection of the mature 5'-end of the 15S rRNA
CC and stabilization of mS47. The removal of the 5' precursor together
CC with the dissociation of Ccm1 may be catalyzed by the 5'-3'
CC exoribonuclease Pet127. Involved in the specific removal of group I
CC introns in mitochondrial encoded transcripts.
CC {ECO:0000250|UniProtKB:P48237}.
CC -!- SUBUNIT: Binds to mitochondrial small subunit 15S rRNA.
CC {ECO:0000250|UniProtKB:P48237}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P48237}.
CC -!- MISCELLANEOUS: Involved in mitochondrial-nuclear incompatibility, a
CC major determinant in reproductive isolation between species, through
CC hybrid incompatibility of Ccm1 and its interacting partner 15S rRNA
CC between yeast species. {ECO:0000250|UniProtKB:P48237}.
CC -!- SIMILARITY: Belongs to the CCM1 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; CP017628; AOW30274.1; -; Genomic_DNA.
DR RefSeq; XP_718046.1; XM_712953.1.
DR AlphaFoldDB; Q5A8W9; -.
DR SMR; Q5A8W9; -.
DR STRING; 237561.Q5A8W9; -.
DR EnsemblFungi; C6_03440W_A-T; C6_03440W_A-T-p1; C6_03440W_A.
DR GeneID; 3640274; -.
DR KEGG; cal:CAALFM_C603440WA; -.
DR CGD; CAL0000174731; orf19.13127.
DR VEuPathDB; FungiDB:C6_03440W_A; -.
DR eggNOG; ENOG502QUX2; Eukaryota.
DR HOGENOM; CLU_019745_0_0_1; -.
DR InParanoid; Q5A8W9; -.
DR OrthoDB; 2714798at2759; -.
DR PRO; PR:Q5A8W9; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR002885; Pentatricopeptide_rpt.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR47934; PENTATRICOPEPTIDE REPEAT-CONTAINING PROTEIN PET309, MITOCHONDRIAL; 1.
DR PANTHER; PTHR47934:SF6; PENTATRICOPEPTIDE REPEAT-CONTAINING PROTEIN PET309, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF01535; PPR; 2.
DR PROSITE; PS51375; PPR; 6.
PE 3: Inferred from homology;
KW Mitochondrion; mRNA processing; mRNA splicing; Reference proteome; Repeat;
KW Transit peptide.
FT TRANSIT 1..90
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 91..768
FT /note="Mitochondrial 15S rRNA processing factor CCM1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000402256"
FT REPEAT 274..308
FT /note="PPR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 309..344
FT /note="PPR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 347..381
FT /note="PPR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 382..417
FT /note="PPR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 418..452
FT /note="PPR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 634..664
FT /note="PPR 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REGION 28..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 768 AA; 88529 MW; 7C4C5CE8D08FA0BE CRC64;
MIRLIRWNNV QSLVFKRCLF VPSNSLTNKR KRRIPPSKPR SSNRKDGDIE PYRMTDQNQT
PNTGSIARLP AEVKKELKDL RSFTKVIAQH LKPEQENDSL TSAEKPDTSQ LPPIDIEEAT
DDIFGEISGT KKLSANAVPP PPPPPGLDIP DEIKERLGLL SELLVPAKTS NNKLPEKQVE
NNWKLLLSQL DQAGGLSGLS KRSVSKFFSK IPPKNLKNLI PMIENMYNKA EMSIPHPIYY
MFVRSLTLGD KISDSQMQLI NKYFQEISKQ TDLKIDHYET MILAYVKNNH MEKIDGILAQ
MKKKNIEISK MIYTSIVRGY IFYQKDHQRA LDTFDSMKFL SQKTQPDEKV YTDVIVSCVM
HREIERALDL YYELKDKGMN VNQNLLSTLA KGCSRSKQFK TQAWNFLFQV YDHGWVPNLQ
TYEHMLYIAA RDGDVELTRV LFYKMLQTNS VTIRAFRYLI LSYSKYVPPH KRKEKHLILL
NHKGQLFRQN ILQDVDFSKP VHGFPFLPSS HIPDSKFVLA ESSAIWAHTV MNNPSFLRQQ
TLVASYVSIA LELGDFTEFK DRFDSASYLN TDGIPKVREI EIIEPRQDEP TEKATTTEEQ
NASSETDNNS LIRSPILNQL QQNINDNQFK APRDSYLYNL AIKAAGKFKN YGFAQEILHE
RGQFRKSNSF KLLSPKQQNQ DDFQFAGYLV ECWTNMNLLE DAYAVVLSSV DRFPWSWREL
GVLNNAAMKL GSLELAEAVR KVAQVTQVKH HGKIKRQDFK TYVMKRGY
//
