ID D5GDJ2_TUBMM Unreviewed; 504 AA.
AC D5GDJ2;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Alpha-MPP {ECO:0000256|ARBA:ARBA00030006};
DE AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000256|ARBA:ARBA00032315};
GN ORFNames=GSTUM_00000965001 {ECO:0000313|EMBL:CAZ82585.1};
OS Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ82585.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ82585.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ82585.1,
RC ECO:0000313|Proteomes:UP000006911};
RX PubMed=20348908; DOI=10.1038/nature08867;
RA Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA Ottonello S., Wincker P.;
RT "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT of symbiosis.";
RL Nature 464:1033-1038(2010).
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}.
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DR EMBL; FN430146; CAZ82585.1; -; Genomic_DNA.
DR RefSeq; XP_002838394.1; XM_002838348.1.
DR AlphaFoldDB; D5GDJ2; -.
DR STRING; 656061.D5GDJ2; -.
DR EnsemblFungi; CAZ82585; CAZ82585; GSTUM_00000965001.
DR GeneID; 9188174; -.
DR KEGG; tml:GSTUM_00000965001; -.
DR eggNOG; KOG2067; Eukaryota.
DR HOGENOM; CLU_009902_5_2_1; -.
DR InParanoid; D5GDJ2; -.
DR OMA; LKYHHSP; -.
DR OrthoDB; 7099at2759; -.
DR Proteomes; UP000006911; 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:UP000006911}.
FT DOMAIN 56..203
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 209..407
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 504 AA; 55360 MW; 1AE59D6FF76E6027 CRC64;
MIRSTSLKKF SPPLSILKPR CPFQSARRAF ASSILNIPTK DPVELDSITT LPNGVRVATE
ALPGHFSGLG VYIDAGSRYE NSRIRGVSHL IDRLAFKSTS SRSSDMMLET LESFGGTVQC
ASSRESLMYQ AAVFNKDVPS MLGLLAETIR DPLITEEEVV QQLDTAAYEI QEIWAKPELI
LPELLHMTAY RDNTLGNPLL CPGDRLDEIK RETILEYRNI FYRPERIVIA FAGVDHSMAV
KLAEQYFGDM KTDVHSPYPG INLPNPSHYT GGTTTLPPSD LPSHLPTFTH LQIAFEGLPI
SDPDIYALAT LQTLLGGGGS FSAGGPGKGM YSRLFTNVLN QNGWIESCIA FNHSYTDSGL
FGIAASCHPG TGPHLVDVIL KEFSTTFTKS VYSGLKSEEV DRAKKQLQSS LLMNLESRMV
ELEDLGRQVQ VHGKKLSPLE MCREIEKLGV KDVRRVAERV LLGQVENAGK GRGGATVVVQ
GGEAEVTAMG DLLEVVRRYR LGRE
//
