ID G1XTM8_ARTOA Unreviewed; 552 AA.
AC G1XTM8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Alpha-MPP {ECO:0000256|ARBA:ARBA00030006};
DE AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000256|ARBA:ARBA00032315};
GN ORFNames=AOL_s00215g157 {ECO:0000313|EMBL:EGX43421.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX43421.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX43421.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
CC -!- FUNCTION: Substrate recognition and binding subunit of the essential
CC mitochondrial processing protease (MPP), which cleaves the
CC mitochondrial sequence off newly imported precursors proteins.
CC {ECO:0000256|ARBA:ARBA00002123}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|RuleBase:RU004447}.
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:EGX43421.1}.
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DR EMBL; ADOT01000316; EGX43421.1; -; Genomic_DNA.
DR RefSeq; XP_011127661.1; XM_011129359.1.
DR AlphaFoldDB; G1XTM8; -.
DR STRING; 756982.G1XTM8; -.
DR GeneID; 22898554; -.
DR eggNOG; KOG2067; Eukaryota.
DR HOGENOM; CLU_009902_5_2_1; -.
DR InParanoid; G1XTM8; -.
DR OMA; LKYHHSP; -.
DR OrthoDB; 7099at2759; -.
DR Proteomes; UP000008784; 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; METALLOPROTEASE; 1.
DR PANTHER; PTHR11851:SF49; MITOCHONDRIAL-PROCESSING PEPTIDASE SUBUNIT ALPHA; 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:UP000008784}.
FT DOMAIN 50..197
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 204..454
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 552 AA; 60426 MW; 45593F7DFC57C43E CRC64;
MFRTSLRAAR RLPRTPIANP TYRRSFASLK PSSAESPDFE KVTTLPNGVR VATEAMPGHF
SGVGVYLDAG ARYEDDSLRG VSHIVDRLAF KSTKQRTMES MYESIERLGG NVQCISSRES
IMYQSAVFNH DVSTAMGLLA ETILDPLITQ EEVEQQLETA DYEIGEIWGK SELILPELLH
GVAYHNNTLG NPLLCPKERL RVIDRSTIEK YRSIFYKPER IVVAFAGVQH QDAIKLVEQY
FGGMKSTAQL ASAAQSLPSS ANPKQAPLPS SNPKTLLSKM PFLKNLSTTA SPSASHAYPY
LDPRNPYPNL TVPSLYTGGQ TEVAPKYGPG ENKELTHIYI AFETPGIVSK DIYALATLQT
LLGGGGSFSA GGPGKGMYSR LYTNVLNQYG WIESCVAFHH SYNDSGMFGI AASCEKEASG
AIADVVLREM ANTFTSSGYN ALQVSEVERA KNQLRSSLLM NLESRMIELE DLGKQVQCHG
RKIGPAEMCK EIEKLTVHDL RRIAEKVFTG KVVNVGGGSG RPSVVVQGTE EAVNVIGSVD
RRARKYGLGR KP
//