ID A0A4Q4WEI1_9PEZI Unreviewed; 1017 AA.
AC A0A4Q4WEI1;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=Presequence protease, mitochondrial {ECO:0000256|ARBA:ARBA00020167};
DE AltName: Full=Pitrilysin metalloproteinase {ECO:0000256|ARBA:ARBA00034552};
GN ORFNames=DL769_011443 {ECO:0000313|EMBL:RYP45716.1};
OS Monosporascus sp. CRB-8-3.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariales incertae sedis; Monosporascus.
OX NCBI_TaxID=2211644 {ECO:0000313|EMBL:RYP45716.1, ECO:0000313|Proteomes:UP000292472};
RN [1] {ECO:0000313|EMBL:RYP45716.1, ECO:0000313|Proteomes:UP000292472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRB-8-3 {ECO:0000313|EMBL:RYP45716.1,
RC ECO:0000313|Proteomes:UP000292472};
RA Robinson A.J., Natvig D.O.;
RT "Complete Genomes of Monosporascus.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RYP45716.1}.
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DR EMBL; QJNZ01001834; RYP45716.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q4WEI1; -.
DR STRING; 2211644.A0A4Q4WEI1; -.
DR Proteomes; UP000292472; 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:0006508; P:proteolysis; IEA:InterPro.
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:0000256|ARBA:ARBA00023049};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00023049};
KW Reference proteome {ECO:0000313|Proteomes:UP000292472};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 488..746
FT /note="Peptidase M16C associated"
FT /evidence="ECO:0000259|SMART:SM01264"
SQ SEQUENCE 1017 AA; 113387 MW; C3F35588640D141D CRC64;
MLRNTVKSAA KKAITELSRY PKPGEKLHGF TLLRAKHVPE LELTALHLKH DKTGADYLHI
ARDDSNNVFS IGFKTNPPDD TGVPHILEHT TLCGSEKYPI RDPFFKMLPR TLSNFMNAFT
ASDHTYYPFA TTNAQDFQNL MSVYLDATLH PLLKETDFTQ EGWRIGPENP QVAAAEGEAT
PDDSKLVFKG VVYNEMKGQM SDAGYLFYIR FQDHIFPSIN NSGGDPKKIT DLTYEQLKKF
HAEHYHPSNA KLITYGDMPL ADHLKEIDTR IEVFERIQAD LESKTPVNLT DGPRTVTVFG
PVDPLADPDK QYKTSVSWIT GDTTDVLESF SLALLSSLLM DGYGSPLYKG LVESGLGTDW
SPNSGYDSSA ITGIFSVGLT GVARENVEKV KDEVQKILRE VREEGFERSK IDGYLHQLEL
SLKHKTANFG ISVLHRLKGK WFNGADPFKS LAWNNTVAAF EAKLAEGGYL EGLMDKYLLN
DNTLTFTMAP SETFGADLAK EEDERLASKI IEAAREAGGE QEARKFFEQR ELDLLVEQGK
SSTQDLSCLP TVHVRDIPRR KEPVVVRDEV AHGTAIQWRE APTNGLTYFR AINKLENLPD
ELRVLIPLFA DSIMRLGTKD MTMEQLEDLI KLKTGGLSVG YHSTPSPTDF QQASEGLVFT
GMALDRNVPA MFDLIRKLVL ETNFDSPEAA LRIRQLLEAS ADGVVNDIAS SGHAFARRYA
ESSLTRNAYL GEQVGGLSQV KLITSLASRP QSDQYEDVIE KLKQIQNFAL AGDNMRTALT
CGSDSSQDVS KALSEFMAAR PTEPISFSPA APKQSLARDI KAFFPLPYQV YYGSLALPTV
SYTSHHGAPL QILAQLLTHK HLHHEIREKG GAYGGGAYMK GLDGLFGFYS YRDPNPQNTL
SIMRNAGRWA LDKQWSDQDF EEAKISVFQS IDAPKAVNTE GMDRFVSGIT EEMKQKRREE
LLDTTKDQVR EVAQTYIVDA LAKGEERVAF LGKKQDWVDG SWRIHEMDIN GAATPES
//