ID H2AMR8_KAZAF Unreviewed; 167 AA.
AC H2AMR8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Mitochondrial inner membrane protease subunit 2 {ECO:0000256|ARBA:ARBA00013650};
GN Name=KAFR0A02300 {ECO:0000313|EMBL:CCF55668.1};
GN ORFNames=KAFR_0A02300 {ECO:0000313|EMBL:CCF55668.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF55668.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF55668.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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}.
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; HE650821; CCF55668.1; -; Genomic_DNA.
DR RefSeq; XP_003954803.1; XM_003954754.1.
DR AlphaFoldDB; H2AMR8; -.
DR STRING; 1071382.H2AMR8; -.
DR GeneID; 13886349; -.
DR KEGG; kaf:KAFR_0A02300; -.
DR eggNOG; KOG1568; Eukaryota.
DR HOGENOM; CLU_028723_4_1_1; -.
DR InParanoid; H2AMR8; -.
DR OrthoDB; 447775at2759; -.
DR Proteomes; UP000005220; Chromosome 1.
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; 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; 1.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 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:UP000005220};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..167
FT /note="Mitochondrial inner membrane protease subunit 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003559568"
FT DOMAIN 7..99
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 34
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 80
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 167 AA; 19317 MW; A518061F6C178ADC CRC64;
MKRYTKLVLL TISWLPVAMT TAELVNISKI NGKSMRPTLN PSDKDTDWVI LKLFRPAKNL
QRNDIILFKS PFDPKILFCK RVKGLDKDLI RLEHENIRVP RGHIWVEGDN VHSVDSRTFG
PISKGLILGK VKCIVWPPRR WGTDLNKWAG RDAMVNEDDK MHFIDSE
//
