ID   M7T809_EUTLA            Unreviewed;      1016 AA.
AC   M7T809;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Presequence protease, mitochondrial {ECO:0000256|ARBA:ARBA00020167};
DE   AltName: Full=Pitrilysin metalloproteinase {ECO:0000256|ARBA:ARBA00034552};
GN   ORFNames=UCREL1_10267 {ECO:0000313|EMBL:EMR62785.1};
OS   Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS   armeniacae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX   NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR62785.1, ECO:0000313|Proteomes:UP000012174};
RN   [1] {ECO:0000313|Proteomes:UP000012174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX   PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA   Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT   "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT   EL1.";
RL   Genome Announc. 1:E0022813-E0022813(2013).
CC   -!- FUNCTION: Degrades mitochondrial transit peptides after their cleavage
CC       in the intermembrane space or in the matrix, and presequence peptides;
CC       clearance of these peptides is required to keep the presequence
CC       processing machinery running (By similarity). Preferentially cleaves
CC       the N-terminal side of paired basic amino acid residues (By
CC       similarity). Also degrades other unstructured peptides (By similarity).
CC       May function as an ATP-dependent peptidase as opposed to a
CC       metalloendopeptidase. {ECO:0000256|ARBA:ARBA00034467}.
CC   -!- SUBUNIT: Monomer and homodimer; homodimerization is induced by binding
CC       of the substrate. {ECO:0000256|ARBA:ARBA00011853}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC       {ECO:0000256|ARBA:ARBA00004569}. Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. PreP subfamily.
CC       {ECO:0000256|ARBA:ARBA00007575}.
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DR   EMBL; KB707371; EMR62785.1; -; Genomic_DNA.
DR   RefSeq; XP_007798113.1; XM_007799922.1.
DR   AlphaFoldDB; M7T809; -.
DR   STRING; 1287681.M7T809; -.
DR   MEROPS; M16.A19; -.
DR   KEGG; ela:UCREL1_10267; -.
DR   eggNOG; KOG2019; Eukaryota.
DR   HOGENOM; CLU_009165_0_0_1; -.
DR   OMA; NYLYYIR; -.
DR   OrthoDB; 5477696at2759; -.
DR   Proteomes; UP000012174; Unassembled WGS sequence.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR013578; Peptidase_M16C_assoc.
DR   PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR   PANTHER; PTHR43016:SF13; PRESEQUENCE PROTEASE, MITOCHONDRIAL; 1.
DR   Pfam; PF08367; M16C_assoc; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SMART; SM01264; M16C_associated; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:EMR62785.1};
KW   Protease {ECO:0000313|EMBL:EMR62785.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012174};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          489..747
FT                   /note="Peptidase M16C associated"
FT                   /evidence="ECO:0000259|SMART:SM01264"
SQ   SEQUENCE   1016 AA;  113354 MW;  C7C48AA9A0271C23 CRC64;
     MLRNTVKIAA RKAVTELSQY PKPGDKLHGF TLLRSKHVPE LEMTALHLKH DKTGADYLHI
     ARDDSNNVFS IGFKTNPPDD TGVPHILEHT TLCGSEKYPI RDPFFKMLPR TLSNFMNAFT
     ASDHTYYPFA TTNAQDFQNL MSVYLDATLH PLLKQTDFTQ EGWRIGPENP QVAAAEGGEA
     KAEDSKLVFK GVVYNEMKGQ MSDAGYIFYI RFQDHIFPSI NNSGGDPQKI TDLTYEQLKS
     FHAEHYHPSN AKLMTYGDMP LADHLKEIDA RMDVFDKIQA DVECKQPITL SDGPKTVKVF
     GPIDPLADPD KQYKTSVSWI TGDTRDVLES FSLAILSSLL MDGYGSPLYK GLVESGLGTD
     WSPNSGYDSS AMTGIFSIGL TGVAQENVEK VKGEVQRILS EVRGKGFEKS KIDGYLHQLE
     LSLKHKTANF GVSVLHRLKG KWFNGADPFK SLAWNDTVAA FEAKLAEGGY LEGLMDKYLL
     KDNTFDFTMA PSETFSAELA KEEEDRLASK IVQATKDAGG EEEARKFFEQ RELELLSEQG
     KSNTQDLSCL PTVYVKDIPR QKEAVEVRDE TAHGTTIQWH EAPTNGLTYF RAINTLENLP
     DELRVLIPLF TDSIMRLGTK DMAMEQLEDL IKLKTGGVSI GYHSTPSPTD FHQASEGLAF
     TGMALDRNVP VMFDLIRKLV LETNFDSPEA ALRIRQLLEA SADGVVNDIA SSGHAFARRY
     AESGLTRNAY FGEQVGGLSQ VKLTTSLAGR SPSDQYEDVI EKLKQIQKFA LAGNTMRTAL
     TCGSDSSQEN SKALGQFMIS RPAEPVSFSP SNQKFTRDIK AFFPLPYQVY YGSLALPTVS
     YTSSYGAPLQ ILAQLLTHKH LHHEIREKGG AYGGGAYMKG LDGLFGFYSY RDPNPQNTLS
     VMRNAGRWAL DKEWSSQDFE EAKISVFQSV DAPRSVNTEG MDRFVSGITE EMKQKRREQL
     LDVTKDQVRE VAQKYIVDAL AKEEERVVFL GKKQDWVDNS WNIHEMDVNG VALPES
//