ID U4L8J9_PYROM Unreviewed; 1019 AA.
AC U4L8J9;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Presequence protease, mitochondrial {ECO:0000256|ARBA:ARBA00020167};
DE AltName: Full=Pitrilysin metalloproteinase {ECO:0000256|ARBA:ARBA00034552};
GN ORFNames=PCON_13823 {ECO:0000313|EMBL:CCX14230.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX14230.1};
RN [1] {ECO:0000313|EMBL:CCX14230.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX14230.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX14230.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(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; HF935944; CCX14230.1; -; Genomic_DNA.
DR AlphaFoldDB; U4L8J9; -.
DR STRING; 1076935.U4L8J9; -.
DR MEROPS; M16.013; -.
DR eggNOG; KOG2019; Eukaryota.
DR OMA; NYLYYIR; -.
DR OrthoDB; 5477696at2759; -.
DR Proteomes; UP000018144; 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:CCX14230.1};
KW Protease {ECO:0000313|EMBL:CCX14230.1}.
FT DOMAIN 494..744
FT /note="Peptidase M16C associated"
FT /evidence="ECO:0000259|SMART:SM01264"
SQ SEQUENCE 1019 AA; 113997 MW; 35341592FC1057CB CRC64;
MLRGGLSLGR QALGRRAGLF QSPKRTFAAL TDLKKLPQPG DKLHGFTVQR AKKVPELQLA
AVELKHDTTG ANYIHVARDD TNNVFAIGFK TNPNDDTGVP HILEHTTLCG SEKYPVRDPF
FKMLNRSLSN YMNAFTSGDH TTYPFATTNR VDFNNLMDVY LDATLKPLLQ ESDFKQEGWR
IGPENPTDPL SPLLFKGVVY NEMKGQMSDS SYLYYIRFQD HIFPDLHNSG GDPQKITDLT
LEQLRKFHKD HYNPSNAKIF TYGDAPIEEH LTRLNERLAG FGQSPMDTDL RLPITLDESK
MITVEGPIDP LTDKDAQHKT SVSWIMNDIS DVDETFALRI MSNYLLDGYG SPLYQGLIDE
KLGSDFTPNT GFDTSAKKSI FSVGLQNVRK EDVRTVQEKI SIILEDVCKR GFNEKKIDGI
LHQLELGLKH KTATFGMSLM QGLTPAWFNG VDPFDSLSWE STVNKFKERY AEGGYLEGLL
KKYLLGTHTL TFTMVPEKGY SHSLATEEKE RLHREIEKAG GEAARESLVK QELELLEIQE
AARDMDLSCL PTVKVSDIPR EMEAKPLQHG KIGDVPVQWR EAPTNGLTYF RAVNPLEDLP
EDLRMYLPLF TDAILRLGTA KKSMEQLEDE IKLKTGGIKA GTHISTNHSN LEITEEGLVF
SGYCLDKNVP DMLELLRTVL LETNFYAISK LRTLVQGIAS GFVNSLAESG HSFARTFAAA
HLTPGARSAE VMGGMTQVRL ISNLASKEIY NDTLDILRQI GKFAARQNGL RIAITCGTES
VSDNEKAVKK FIDALPIAET PIRDSPLFDF EAPTKALFPL PYQVSYTGMC VKTVPYTHQD
GAALQMLSQL LTHKHLHHEI REKGGAYGGG AFHRGAGGIF GFYSYRDPNV ANTLKVMEEA
GQWAMQKQWA ERDLEEAKLS VFQGVDAPQS VSEEGMVYFL DRITDEMRQV RRQQLLDVSI
ADIRNVAQKY LVDQVAAGQT AVAVLGEPKD VVDDSWNIFP LSLDPQAQPD MSQFEKVTL
//
