ID E4ZZQ7_LEPMJ Unreviewed; 1031 AA.
AC E4ZZQ7;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Presequence protease, mitochondrial {ECO:0000256|ARBA:ARBA00020167};
DE AltName: Full=Pitrilysin metalloproteinase {ECO:0000256|ARBA:ARBA00034552};
GN ORFNames=LEMA_P103040.1 {ECO:0000313|EMBL:CBX97173.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(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; FP929130; CBX97173.1; -; Genomic_DNA.
DR RefSeq; XP_003840652.1; XM_003840604.1.
DR AlphaFoldDB; E4ZZQ7; -.
DR STRING; 985895.E4ZZQ7; -.
DR EnsemblFungi; CBX97173; CBX97173; LEMA_P103040.1.
DR GeneID; 13283586; -.
DR eggNOG; KOG2019; Eukaryota.
DR HOGENOM; CLU_009165_0_0_1; -.
DR InParanoid; E4ZZQ7; -.
DR OMA; NYLYYIR; -.
DR OrthoDB; 5477696at2759; -.
DR Proteomes; UP000002668; Genome.
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:0004222; F:metalloendopeptidase activity; IEA:EnsemblFungi.
DR GO; GO:0016485; P:protein processing; IEA:EnsemblFungi.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:EnsemblFungi.
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; 1.
DR SMART; SM01264; M16C_associated; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:CBX97173.1};
KW Protease {ECO:0000313|EMBL:CBX97173.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668}.
FT DOMAIN 501..758
FT /note="Peptidase M16C associated"
FT /evidence="ECO:0000259|SMART:SM01264"
SQ SEQUENCE 1031 AA; 115827 MW; 004F6AD47148FB85 CRC64;
MLRSARWQLR TPHVASANRT SFLPSPPSAS NRHVSSFPNV GEKLHGFTLK RVKQVPELEL
TALHLEHDKT GADYLHIARE DANNVFSIGF KTNPPDATGV PHILEHTTLC GSQKYPIRDP
FFKMLPRTLS NFMNAWTFPD HTGYPFATTN VQDFKNLMSV YLDATLHPLL KENDFTQEGW
RIGPENPMAA ETEDPDAKKL VFKGVVYNEM KGQMSDASYL FYTKFQEHLF PAINNSGGDP
QKITDLTWEQ LRKFHADHYH PSNAKILTYG DMPLESHLHE VDQRLNAFDR ITVTQDIKGP
ITLDAPKHVT VSGPLDPLVP QDRQYKTSVT WLMGDTRDAV ENFGLGVLSS LLMSGYGSPL
YRNLIESGLG ADFSANTGYD SAGTRGVFTV GLDAVKADDV PGVREAIVKT FAEVRKNGFD
KIKVDGILHQ LELSLKHKTA NFGMSILQRL KPGWFNGIDP MDALAWQETV DAFQKKHAEG
DYLEGLIEKY LFSENTLTFT MRPSETFSEE LAEEESQRLA SKISETTKQF PSEKDAQEYL
EKRERELLEV QEKARNEDLS CLPTVHVKDI PREKERKPIQ QLNLDEVSAQ FREVPTNGLT
YFRAVHKFSE IPDELRVMIP LFTSAIMRLG TKDKTMEQLE EQIKLKTGGI SVAYHCSQSP
NRLNKLSEGF VFSGYAFDRN VPDLYELLRM IIQETNFDGP EAEKKVRELL QSSASGAINS
IAESGHSYAM RYAEATVGHG GLIEQTSGLT QVKLMTSLAS QESLADVMSK LKAIQGFAIA
NRCNFRVAIN CGPESATSNQ EALRRFLHTL PKEVPSFKIG EQQTFPRGTK TFFPLPYQVY
YSAQAYRTVA YNDELSGPLE ILAKMLTFKQ LHPEIREKGG AYGGGAYARG LSGVFGMYSY
RDPNPLNSLK IMADAGTWAR DWAWTNRDLE EAKLSVFQSL DAPQSVSSEG MRVFLNGITD
EMWQTRRERL LDTTTLQVRQ VAQKYLVEGA ANARTVVLGE KKDWVKESHG WNLRDLGMTA
ASSEQAGGEE Q
//
