ID A0A0D2EJP2_9EURO Unreviewed; 478 AA.
AC A0A0D2EJP2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=Z517_11352 {ECO:0000313|EMBL:KIW74582.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW74582.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW74582.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW74582.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-2015) 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; KN846976; KIW74582.1; -; Genomic_DNA.
DR RefSeq; XP_013278390.1; XM_013422936.1.
DR AlphaFoldDB; A0A0D2EJP2; -.
DR STRING; 1442368.A0A0D2EJP2; -.
DR MEROPS; M16.003; -.
DR GeneID; 25310842; -.
DR VEuPathDB; FungiDB:Z517_11352; -.
DR HOGENOM; CLU_009902_4_2_1; -.
DR OrthoDB; 167798at2759; -.
DR Proteomes; UP000053029; 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:UP000053029}.
FT DOMAIN 50..197
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 202..393
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 478 AA; 53466 MW; BDEA247208E2BDED CRC64;
MASQRLALNL QRSLRSRQAL KAIQSPLRRY ANPVTPSRTE STTLSNGLTI ATEHSPWAQT
STVGVWIDAG SRAETDKTNG TAHFLEHLAF KGTGRRTQHQ LELEIENMGG HLNAYTSREN
TVYYAKSFNS DVPKTVDILS DILQNSKLEP AAIERERDVI LREQEEVDKQ LEEVVFDHLH
ATAYMHQPLG RTILGPKENI ETISRQDLVD YITTNYTADR MVLVGAGGIP HEELVKLAEK
HFGHLRSAPP TSYAAEVAAE QKRKPSFIGS EVRIRDDTIP TAHIAIAVEG VSWKDDEYFP
ALVTQAIVGN WDRTMGNSPY LGSRLSTFVN ANNLANSFMS FSTSYSDTGL WGIYLVSENK
TQIDDLVHFT LREWSRLSFN VTEAETERAK AQLKASILLS LDGTTAVAED IGRQIVTTGR
RMDPAEIERV IGQITAKDVM RFCQKKLWDQ DIAISAVGSI EGLLDYNRIR NDMARNFS
//
