ID A0A094I718_9PEZI Unreviewed; 478 AA.
AC A0A094I718;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=V501_02312 {ECO:0000313|EMBL:KFZ16261.1};
OS Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ16261.1, ECO:0000313|Proteomes:UP000029315};
RN [1] {ECO:0000313|EMBL:KFZ16261.1, ECO:0000313|Proteomes:UP000029315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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}.
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:KFZ16261.1}.
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DR EMBL; JPKD01000821; KFZ16261.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094I718; -.
DR STRING; 1420914.A0A094I718; -.
DR MEROPS; M16.980; -.
DR HOGENOM; CLU_009902_4_2_1; -.
DR Proteomes; UP000029315; 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:UP000029315}.
FT DOMAIN 51..197
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 203..394
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 478 AA; 52599 MW; FE85DD7DF220C664 CRC64;
MASRRLALNL TQGLSKRAAF NAPVRRGFAT PVTTKNGVAT ECTTLSNGMT IATEHSPWAQ
TSTVGVWIDA GSRAETDKTN GTAHFLEHLA FKGTSNRTQQ QLELEIENMG GHLNAYTSRE
NTVYYAKAFN ADVPATVNIL SDILQNSKLE KSAIERERDV ILRESEEVDK QLEEVVFDHL
HATAFQGQPL GRTILGPAEN IQSIQREDLV DYIKTNYTAD RMVLVGAGGV PHAQLVELAE
KHFAGLPSGP ISQASAAVAQ LQKRKPEFVG SEVRIRDDTI PTANIAIAVE GVSWKDEDYF
TALVTQAIVG NWDKAMGNAP HMGSKLSGFV HKNDLANSFM SFSTSYSDTG LWGIYLVSDN
LTRLDDLVHF TLREWSRLSY NVTEAEVERA KAQLKASILL SLDGTTAVAE DIGRQIITSG
RRMGPEEVER VVSKITEKDI MDFAQRKLWD QDIAISAVGS IEGLLDYNRI RGDMSRNA
//
