ID F0XMZ5_GROCL Unreviewed; 476 AA.
AC F0XMZ5;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=mitochondrial processing peptidase {ECO:0000256|ARBA:ARBA00012299};
DE EC=3.4.24.64 {ECO:0000256|ARBA:ARBA00012299};
DE AltName: Full=Beta-MPP {ECO:0000256|ARBA:ARBA00031018};
GN ORFNames=CMQ_1958 {ECO:0000313|EMBL:EFX00877.1};
OS Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS (Graphiocladiella clavigera).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN [1] {ECO:0000313|EMBL:EFX00877.1, ECO:0000313|Proteomes:UP000007796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal transit peptides from precursor proteins
CC imported into the mitochondrion, typically with Arg in position P2.;
CC EC=3.4.24.64; Evidence={ECO:0000256|ARBA:ARBA00001098};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|RuleBase:RU004447}.
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DR EMBL; GL629795; EFX00877.1; -; Genomic_DNA.
DR RefSeq; XP_014170359.1; XM_014314884.1.
DR AlphaFoldDB; F0XMZ5; -.
DR STRING; 655863.F0XMZ5; -.
DR MEROPS; M16.003; -.
DR GeneID; 25974893; -.
DR eggNOG; KOG0960; Eukaryota.
DR HOGENOM; CLU_009902_4_2_1; -.
DR InParanoid; F0XMZ5; -.
DR OrthoDB; 167798at2759; -.
DR Proteomes; UP000007796; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851:SF149; GH01077P; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007796};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 52..198
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 204..392
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 476 AA; 52469 MW; 598CE5BC777D1203 CRC64;
MASRRLALNL GRGLKAPRAG LSLPPLRRGL ATPVTSPGIK VQSTTLKNGL TVASHYSPYA
QTSTVGVWID AGSRAETEET NGTAHFLEHL AFKGTSKRTQ HQLELEIENL GAHLNAYTSR
ENTVYFAKAL NEDVPQCVDI LADILQNSKL EESAIERERD VILRESEEVE KQIEEVVFDH
LHATAFQQQP LGRTILGPRQ NIQDITRTEL SNYIKNNYSA DRMVLVGAGG FAHEQLVELA
EKHFTSLPAT SPPSGALLEF KKKSDFIGSD VRVRDDTIPT ANIAIAVEGV SWNDDDYFTA
LVAQAIVGNY DKALGNAPHQ GSKLSGFVHK NDLANSFMSF STSYSDTGLW GIYLVTDKLT
RIDDLVHFAL REWSRLSLNV SQAEVERAKA QLKASILLSL DGTTAVAEDI GRQIITTGTR
QSPAEIERVI DAITEKDVMD FANRKLWDQD IAISAVGSIE GLFDYARIRG DMSRNF
//
