ID G3JU92_CORMM Unreviewed; 166 AA.
AC G3JU92;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Mitochondrial inner membrane protease subunit 1, putative {ECO:0000313|EMBL:EGX87799.1};
GN ORFNames=CCM_09421 {ECO:0000313|EMBL:EGX87799.1};
OS Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX87799.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX87799.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX87799.1,
RC ECO:0000313|Proteomes:UP000001610};
RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT valued traditional Chinese medicine.";
RL Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}.
CC -!- SIMILARITY: Belongs to the peptidase S26 family. IMP1 subfamily.
CC {ECO:0000256|ARBA:ARBA00038445}.
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DR EMBL; JH126407; EGX87799.1; -; Genomic_DNA.
DR RefSeq; XP_006674618.1; XM_006674555.1.
DR AlphaFoldDB; G3JU92; -.
DR STRING; 983644.G3JU92; -.
DR GeneID; 18171424; -.
DR KEGG; cmt:CCM_09421; -.
DR VEuPathDB; FungiDB:CCM_09421; -.
DR eggNOG; KOG0171; Eukaryota.
DR HOGENOM; CLU_028723_4_3_1; -.
DR InParanoid; G3JU92; -.
DR OMA; CKGPSME; -.
DR OrthoDB; 447775at2759; -.
DR Proteomes; UP000001610; 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; IPR019533; Peptidase_S26.
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; 2.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR PROSITE; PS00760; SPASE_I_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:EGX87799.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protease {ECO:0000313|EMBL:EGX87799.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001610};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..166
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003446519"
FT DOMAIN 30..97
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 110..148
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 41
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 85
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 166 AA; 18623 MW; C96E4FFB7E59591A CRC64;
MASRFLQRPS VRISVGMTKL WFAWHLVATH GFQVDPADGP SMLPTFSTYG DWIGTDKRFR
YGRGVRIGDL VLYQMPYAAH DMGVKRVTGL PGDYVSVGTP GQPGQEIMIQ IPDGHCWIVG
DNLVASRDSR TFGPLPLALI QGKVVAKVLP WNERQWFENP LQRVEQ
//
