ID F2Q0F1_TRIEC Unreviewed; 206 AA.
AC F2Q0F1;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Mitochondrial inner membrane protease subunit {ECO:0000256|RuleBase:RU362041};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU362041};
GN ORFNames=TEQG_06490 {ECO:0000313|EMBL:EGE07576.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; DS995762; EGE07576.1; -; Genomic_DNA.
DR AlphaFoldDB; F2Q0F1; -.
DR VEuPathDB; FungiDB:TEQG_06490; -.
DR eggNOG; KOG0171; Eukaryota.
DR HOGENOM; CLU_028723_4_3_1; -.
DR Proteomes; UP000009169; 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; 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; 2.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 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|RuleBase:RU362041}.
FT DOMAIN 64..127
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 142..186
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 73
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 117
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 206 AA; 23291 MW; 2ECC51F020256559 CRC64;
MDRTVGIETL GKAHEDAKKL AADIRMTSRV FGFGALSRHK RAFVCTLHLA GTFCWFKIFN
EHFYELKASD GPSMYPTIHF QGDWLLISKH YKNGRDVEFG DIIVYKKPHD FHSEVAKRVV
GLPGDYVLKN PPLNGETVVE HDAQMIQVPE AHVWVSGDDA PWSIDSKDYG PVPMGLIIGR
ALGRVWYPFN YERFDNTLKP VTTAGP
//
