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Database: UniProt
Entry: A0A4Q4WEI1_9PEZI
LinkDB: A0A4Q4WEI1_9PEZI
Original site: A0A4Q4WEI1_9PEZI 
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
//
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