ID A0A175W4L1_9PEZI Unreviewed; 1010 AA.
AC A0A175W4L1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Presequence protease, mitochondrial {ECO:0000256|ARBA:ARBA00020167};
DE AltName: Full=Pitrilysin metalloproteinase {ECO:0000256|ARBA:ARBA00034552};
GN ORFNames=MMYC01_205853 {ECO:0000313|EMBL:KXX78677.1};
OS Madurella mycetomatis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariales incertae sedis; Madurella.
OX NCBI_TaxID=100816 {ECO:0000313|EMBL:KXX78677.1, ECO:0000313|Proteomes:UP000078237};
RN [1] {ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA van de Sande W.W.J.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KXX78677.1, ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA Van De Sande W.;
RT "Madurella mycetomatis genome sequencing.";
RL Submitted (JAN-2016) 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:KXX78677.1}.
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DR EMBL; LCTW02000111; KXX78677.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A175W4L1; -.
DR STRING; 100816.A0A175W4L1; -.
DR VEuPathDB; FungiDB:MMYC01_205853; -.
DR OrthoDB; 5477696at2759; -.
DR Proteomes; UP000078237; 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:KXX78677.1};
KW Protease {ECO:0000313|EMBL:KXX78677.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078237};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 487..745
FT /note="Peptidase M16C associated"
FT /evidence="ECO:0000259|SMART:SM01264"
SQ SEQUENCE 1010 AA; 112496 MW; C3B816EB3896C7D9 CRC64;
MLRSTARRGA RAVTELSQLP KPGDKLHGFT LLRTKHVPEL ELTALHLRHD KTGAEHLHIA
RDDSNNVFSI GFKTNPPDDT GVPHILEHTT LCGSEKYPIR DPFFKMLPRT LSNFMNAFTA
SDHTFYPFAT TNAQDFKNLM SVYLDATLRP LLKESDFTQE GWRIGPENPQ ALAAGVEAKP
EDRKLVFKGV VYNEMKGQMS DAGYLFYIRF QDHIFPDINN SGGDPQKITD LTYEQLKKFH
AEHYHPSNAK VFTYGDMPLA DHLREIDAQL NVFERIRGDP AIHRPIDLAS GPREVKLYGP
IDPLVDPNKQ FKTSVSWVMG DTSNVVESFS LALISALLTD GYGSPLYKGL IETGLGTDWS
PNSGYDSSAK VGIFSIGLTG VQEADVPKLK PTVQDILRRV REKGFERSKI DGYLHQLELG
LKHKTANFGM SLLHRLKPKW FTGVDPFNSL AWNDTLAAFE AAYAKGGYLE GLMDKYLLND
NTLTFTMAPS PEFAQELAKE EEARLQDKIA DAVKSVGGKD QAQAAFEARE LALLVEQGKS
NTEDLSCLPS VHVEDIPRQK EPVVLRHDML GKVKLQLREA PTNGLTYFRA INTLENLPDE
LRSLIPLFTD SIMRLGTKDM TMEQLEDLMK LKTGGVSVGY HSASRPTDFT QASEGLIFTG
MALDRNVPVM FDLLRKLIVE TNFDSPEAAQ QIRQLLQASA DGVVNDIASS GHAFARRAAE
AGLTWDAFLK EQVSGLSQVR LVTSLASRPE SDQLEDVIAK LKQIQQFALT GNVRAAITCD
SESVASNSNA LSKFLNSVPS HSVAFPTRQA PQYSRNIKSF YPLPYQVYYG ALALPTVSYT
SPDGAPLQIL SSLLTHKHLH HEIREKGGAY GGGAYSRAVD GIFGFYSYRD PNPLNTINIM
RNAGQWAVDK KWSDRDLEDA KISVFQGVDA PRAVNEEGMG HFVYGITEEM KQKRREQLLD
VTKDQVREVA QKYIVDALAK QSERVVFLGE KRDFVDNSWT VNEMDIDGAA
//
