ID A0A2T4AD81_TRIHA Unreviewed; 474 AA.
AC A0A2T4AD81;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=M431DRAFT_85598 {ECO:0000313|EMBL:PTB55045.1};
OS Trichoderma harzianum CBS 226.95.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=983964 {ECO:0000313|EMBL:PTB55045.1, ECO:0000313|Proteomes:UP000241690};
RN [1] {ECO:0000313|EMBL:PTB55045.1, ECO:0000313|Proteomes:UP000241690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 226.95 {ECO:0000313|EMBL:PTB55045.1,
RC ECO:0000313|Proteomes:UP000241690};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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; KZ679680; PTB55045.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4AD81; -.
DR STRING; 983964.A0A2T4AD81; -.
DR OrthoDB; 167798at2759; -.
DR Proteomes; UP000241690; 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:UP000241690};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 50..196
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 202..390
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 474 AA; 52480 MW; 71EC59ADCD914CD7 CRC64;
MASRRLALNL SQGLRARSGL SAAGSLRRGF ATPSTVGKTQ TTTLKNGLTV ATEYSPWAQT
STVGMWIDAG SRAETNETNG TAHFLEHLAF KGTAKRSQHQ LELEIENMGG HLNAYTSREN
TVYFAKAFNS DVPQTVDILS DILQNSKLEP SAIERERDVI LRESEEVEKQ VEEVVFDHLH
ATAFQHQPLG RTILGPRQNI RDITRTELTN YIKNNYTADR MVLAAAGGVP HEQLVELAEK
HFSGLASQGP QTEAYLLSKQ KADFVGSDVR VRDDTMATAN VAIAVEGVSW NSEDYYTALV
AQAIVGNYDK AMGNAPHQGS KLSGYVHKHE LANSFMSFST SYSDTGLWGI YLVTDNTTRL
DDLVHFSIRE WMRLCTNVSQ AEVERAKAQL KASILLSLDG TTAVAEDIGR QLITTGRRAS
PGEIERKIDA ITDKDVTDFA NRYLWDKDIA ISAVGKIEGL FDYQRLRNTM KPKF
//
