ID   I2H8M7_TETBL            Unreviewed;       773 AA.
AC   I2H8M7;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=Mitochondrial intermediate peptidase {ECO:0000256|ARBA:ARBA00018046};
DE            EC=3.4.24.59 {ECO:0000256|ARBA:ARBA00012441};
GN   Name=TBLA0I00710 {ECO:0000313|EMBL:CCH62729.1};
GN   ORFNames=TBLA_0I00710 {ECO:0000313|EMBL:CCH62729.1};
OS   Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS   10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX   NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH62729.1, ECO:0000313|Proteomes:UP000002866};
RN   [1] {ECO:0000313|EMBL:CCH62729.1, ECO:0000313|Proteomes:UP000002866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC   UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal octapeptide as second stage of
CC         processing of some proteins imported into the mitochondrion.;
CC         EC=3.4.24.59; Evidence={ECO:0000256|ARBA:ARBA00000436};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}.
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR   EMBL; HE806324; CCH62729.1; -; Genomic_DNA.
DR   RefSeq; XP_004182248.1; XM_004182200.1.
DR   AlphaFoldDB; I2H8M7; -.
DR   STRING; 1071380.I2H8M7; -.
DR   MEROPS; M03.006; -.
DR   GeneID; 14497907; -.
DR   KEGG; tbl:TBLA_0I00710; -.
DR   eggNOG; KOG2090; Eukaryota.
DR   HOGENOM; CLU_001805_0_0_1; -.
DR   InParanoid; I2H8M7; -.
DR   OMA; ALMFEYM; -.
DR   OrthoDB; 735202at2759; -.
DR   Proteomes; UP000002866; Chromosome 9.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06457; M3A_MIP; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR033851; M3A_MIP.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003435};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002866};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          292..757
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   773 AA;  88634 MW;  628D3A85E9481E64 CRC64;
     MRGSIALKKI LNDSTSLYFQ RFFKTSPVRN ITRSNPLVSK DLKKQDLQKL FDDPKYFNSI
     NNTGLNSNTS ESTGNIISTG LFKNPFLTSP KGLKEFTHYS LLNASNILQQ LKNDDTFNGL
     ANYIIRLDQL SDTLCRVIDL CEFIRSCHPE KSFVQAAQEC HEHMYAFMNT LNTDIALCDR
     LRTVLDNKEV LKRLTDEEIK VGKLLLEDFE KSGIQMSPEI RDRFISLSQD ISLAGQDFLN
     NTSYTEKDYI KIKCDEFDKA CDYPALKYKL SKDLSGKYYK IPTYGKIPYT ALLKCKDEEL
     RKKLWVAFHS CSNKQIERLT KIIKHRIELA KLLSKSSYSE YTLEGKMAKG PKEVNNFLNA
     LLKSILPEVT KELEPISNKK CLSEGFSLET SEQSILNNIK PWDRDYYNPI QATSEGAYQM
     LIMEYFTLGN IIHGLSNLFN SIYGIRFEPG KIEDGETWSK DVRKLNVISE DEGLIGVIYC
     DLFEREGKSE SPSHYTICCS REIYSEEHDL STIQTGVNNK TGKNFQLPIV SLVCNFQVTN
     AKESRRICFL QHHEIETLFH EMGHAMHSML GRTRFQTISG TRCVSDFVEI PSILMEFFAN
     NPKVLIDISR HYDSGESIDI EVLNKYLENT KQFKACETYS QGKMALLDQR LHAENANSLD
     NIDVVEIYHN LEKELSVLPD TESNWCGRFG HLYGYGALYY CYLFDRAIAT KIWESLFQND
     PFSRKGGNIF KEQLLKWGGS KDPWKCVADV LGEPKLQFGG PEAMEYIGNS SKL
//