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Database: UniProt
Entry: C5DX00_ZYGRC
LinkDB: C5DX00_ZYGRC
Original site: C5DX00_ZYGRC 
ID   C5DX00_ZYGRC            Unreviewed;       171 AA.
AC   C5DX00;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Mitochondrial inner membrane protease subunit 2 {ECO:0000256|ARBA:ARBA00013650};
GN   OrderedLocusNames=ZYRO0F01078g {ECO:0000313|EMBL:CAR28311.1};
OS   Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS   / NRRL Y-229) (Candida mogii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=559307 {ECO:0000313|EMBL:CAR28311.1, ECO:0000313|Proteomes:UP000008536};
RN   [1] {ECO:0000313|Proteomes:UP000008536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC   Y-229 {ECO:0000313|Proteomes:UP000008536};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC       inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC       protein {ECO:0000256|ARBA:ARBA00004434}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family. IMP2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00007066}.
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DR   EMBL; CU928178; CAR28311.1; -; Genomic_DNA.
DR   RefSeq; XP_002497244.1; XM_002497199.1.
DR   AlphaFoldDB; C5DX00; -.
DR   STRING; 559307.C5DX00; -.
DR   MEROPS; S26.012; -.
DR   GeneID; 8204997; -.
DR   KEGG; zro:ZYRO0F01078g; -.
DR   HOGENOM; CLU_028723_4_1_1; -.
DR   InParanoid; C5DX00; -.
DR   Proteomes; UP000008536; Chromosome F.
DR   GO; GO:0042720; C:mitochondrial inner membrane peptidase complex; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IEA:InterPro.
DR   GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR   CDD; cd06530; S26_SPase_I; 1.
DR   Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR   InterPro; IPR037730; IMP2.
DR   InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR   InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR   InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR   InterPro; IPR019533; Peptidase_S26.
DR   PANTHER; PTHR46041; MITOCHONDRIAL INNER MEMBRANE PROTEASE SUBUNIT 2; 1.
DR   PANTHER; PTHR46041:SF2; MITOCHONDRIAL INNER MEMBRANE PROTEASE SUBUNIT 2; 1.
DR   Pfam; PF10502; Peptidase_S26; 2.
DR   PRINTS; PR00727; LEADERPTASE.
DR   SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR   PROSITE; PS00761; SPASE_I_3; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008536};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..171
FT                   /note="Mitochondrial inner membrane protease subunit 2"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002948105"
FT   DOMAIN          9..100
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   DOMAIN          109..148
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        37
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        87
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   171 AA;  19593 MW;  F6D29FCC5CD8C872 CRC64;
     MPSQKAFRYS LITLTWIPVI MTINDNVCHV AKIEGSSMRP TLNANERSIS SDWVFLWKFN
     CKKAFNLNRD DIILFKSPMD PNKVYCKRIK GIQYDSVKTR HPYPRSVVNI PRNHVWVEGD
     NVFHSVDSNN FGSLSTGLVV GKAIKVIWPP SRWGADLQLS TGRQNILTTR E
//
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