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Database: UniProt
Entry: A0A0C7N045_9SACH
LinkDB: A0A0C7N045_9SACH
Original site: A0A0C7N045_9SACH 
ID   A0A0C7N045_9SACH        Unreviewed;       179 AA.
AC   A0A0C7N045;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Mitochondrial inner membrane protease subunit {ECO:0000256|RuleBase:RU362041};
DE            EC=3.4.21.- {ECO:0000256|RuleBase:RU362041};
GN   ORFNames=LALA0_S02e11496g {ECO:0000313|EMBL:CEP61308.1};
OS   Lachancea lanzarotensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP61308.1, ECO:0000313|Proteomes:UP000054304};
RN   [1] {ECO:0000313|EMBL:CEP61308.1, ECO:0000313|Proteomes:UP000054304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP61308.1,
RC   ECO:0000313|Proteomes:UP000054304};
RA   Neuveglise Cecile;
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC       Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273,
CC       ECO:0000256|RuleBase:RU362041}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family. IMP1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00038445}.
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DR   EMBL; LN736361; CEP61308.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C7N045; -.
DR   STRING; 1245769.A0A0C7N045; -.
DR   HOGENOM; CLU_028723_4_3_1; -.
DR   OrthoDB; 447775at2759; -.
DR   Proteomes; UP000054304; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; 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; IPR036286; LexA/Signal_pep-like_sf.
DR   InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR   InterPro; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR   InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR   InterPro; IPR019533; Peptidase_S26.
DR   NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR   PANTHER; PTHR12383:SF16; MITOCHONDRIAL INNER MEMBRANE PROTEASE SUBUNIT 1; 1.
DR   PANTHER; PTHR12383; PROTEASE FAMILY S26 MITOCHONDRIAL INNER MEMBRANE PROTEASE-RELATED; 1.
DR   Pfam; PF10502; Peptidase_S26; 1.
DR   PRINTS; PR00727; LEADERPTASE.
DR   SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR   PROSITE; PS00501; SPASE_I_1; 1.
DR   PROSITE; PS00760; SPASE_I_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU362041};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Mitochondrion {ECO:0000256|RuleBase:RU362041};
KW   Mitochondrion inner membrane {ECO:0000256|RuleBase:RU362041};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU362041};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054304}.
FT   DOMAIN          11..150
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        39
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        83
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   179 AA;  20111 MW;  94BC761C13EA53EA CRC64;
     MTSTVKLWLN TGSFALRSFC LVHVIHSHFY EFTETRGESM LPTLSATRDY VHASKKYRNG
     RDCQIGDCIV AVKPTDPYQR VCKRITGMPG DYILIDPSAK EGADLDTQAF DSFIQVPPGH
     VWLTGDNLSQ SLDSRTYNSL PMGLIKGKIV AANDFNKPFW QDGALLGFRR IVNTYLDEV
//
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