ID   G0SGG8_CHATD            Unreviewed;      1011 AA.
AC   G0SGG8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Presequence protease, mitochondrial {ECO:0000256|ARBA:ARBA00020167};
DE   AltName: Full=Pitrilysin metalloproteinase {ECO:0000256|ARBA:ARBA00034552};
GN   ORFNames=CTHT_0066280 {ECO:0000313|EMBL:EGS17307.1};
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS   (Thermochaetoides thermophila).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX   NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN   [1] {ECO:0000313|EMBL:EGS17307.1, ECO:0000313|Proteomes:UP000008066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC   {ECO:0000313|Proteomes:UP000008066};
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA   Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
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; GL988047; EGS17307.1; -; Genomic_DNA.
DR   RefSeq; XP_006696925.1; XM_006696862.1.
DR   AlphaFoldDB; G0SGG8; -.
DR   STRING; 759272.G0SGG8; -.
DR   GeneID; 18260666; -.
DR   KEGG; cthr:CTHT_0066280; -.
DR   eggNOG; KOG2019; Eukaryota.
DR   HOGENOM; CLU_009165_0_0_1; -.
DR   OMA; NYLYYIR; -.
DR   OrthoDB; 5477696at2759; -.
DR   Proteomes; UP000008066; 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: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   Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          487..745
FT                   /note="Peptidase M16C associated"
FT                   /evidence="ECO:0000259|SMART:SM01264"
SQ   SEQUENCE   1011 AA;  113187 MW;  0BB9A50A35E74F92 CRC64;
     MFRNTAKRAA KAASDLAQLS KPGDKLHGFT VLRTKHVPEL ELTALHLRHD KTGAEHLHIA
     RDDSNNVFSI GFKTNPPDDT GVPHILEHTT LCGSEKYPIR DPFFKMLPRT LSNFMNAFTA
     SDHTFYPFAT TNAQDFKNLM SVYLDATLHP LLKKSDFQQE GWRIGPENPQ ALAAGGEARP
     EDRKLVFKGV VYNEMKGQMS DASYLFYIRF QDHIFPDINN SGGDPQKITD LTYEQLKKFH
     AEHYHPSNAK LFTYGNFPLA DHLKEIDAQL SAFEQIQADK ANHRPIDLTS GPREVRLFGP
     VDPLVDPNKQ FKTSVSWVLG DTSNVVESFS LALISALLTD GYGSPMYKGL IEAGLGTDWS
     PNTGYDSSAK VGIFSVGLTG VQEDDVPKVK PTIQKILRNM REKGFDRHKI DGYLHQLELS
     LKHKTANFGM SLLQRLKPKW FTGVDPFDSL AWNDTLAAFE AEYAKGGYLE GLMDKYLLND
     NTLTFTMAPS PDFIQEIARE EEARLKERIN KAVEALGSEE KAQQEFEAQE LALLAEQNKT
     NTEDLSCLPS VHVKDIPRQK EPVVLRHETV GTIKLQLREA PTNGLTYFRA INTLESLPDE
     LRSLVPLFTD SIMRLGTKDM TMEQLEDLIK LKTGGVSVGY HSASSPTDFT QAVEGIAFSG
     MALDRNVPVM FDLLRKLVVE TNFDSPEAPQ QIRQLLQAAA DGVVNDIASS GHAYARRAAE
     AGLSMDAWLK EQVGGLTQVR LVTSLASRPE SDQFRDVIEK LKRIQELAFA GTMRVAITCD
     SNSVGNNVQA LSQFLQSLPS TPASFPARKP IDFSRNIKSF YPLPYQVYYG ALALPTVSYT
     SADNAPLSIL ASLLTHKHMH HEVREKGGAY GAGAYSRPLD GVFGFYSYRD PNPVNTINIM
     RNAGRWAVDK KWSDRDLEDA KISVFQGVDA PRAVNEEGMS TFVYGITEEM KQKRREQLLD
     VTKDQVREVA QKYIVEALEK QSERLVFLGE KREFVDNTWT VNEMDITRPA R
//