ID B6HAG9_PENRW Unreviewed; 479 AA.
AC B6HAG9;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
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=Pc16g12780 {ECO:0000313|EMBL:CAP93948.1}, PCH_Pc16g12780
GN {ECO:0000313|EMBL:CAP93948.1};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP93948.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP93948.1, ECO:0000313|Proteomes:UP000000724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC {ECO:0000313|Proteomes:UP000000724};
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
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; AM920431; CAP93948.1; -; Genomic_DNA.
DR RefSeq; XP_002561577.1; XM_002561531.1.
DR AlphaFoldDB; B6HAG9; -.
DR STRING; 500485.B6HAG9; -.
DR MEROPS; M16.980; -.
DR GeneID; 8315003; -.
DR KEGG; pcs:Pc16g12780; -.
DR VEuPathDB; FungiDB:PCH_Pc16g12780; -.
DR eggNOG; KOG0960; Eukaryota.
DR HOGENOM; CLU_009902_4_2_1; -.
DR OMA; IDVVCDM; -.
DR OrthoDB; 167798at2759; -.
DR BioCyc; PCHR:PC16G12780-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c16.
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:UP000000724}.
FT DOMAIN 51..198
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 479 AA; 53074 MW; 8B5F802C69AFA48A CRC64;
MASRRLAFNL NQALRTRAAL KSIQPVKRGF ASPVALPSTT QSTTLSNGFT IATDHSPWAQ
TSTVGVWIDA GSRAETDKTN GTAHFLEHLA FKGTNKRSQH QLELEIENMG AHLNAYTSRE
NTVYYAKAFN NDVPKAVDIL ADILQNSKLE AGAIERERDV ILREQEEVDK QLEEVVFDHL
HATAYQTQPL GRTILGPKEN IQTITRDNLT DYIKTNYTAD RMVLVGAGGI PHEQLVRLAE
EHFGGLPSKP PTSAALALTA EQKRTPEFIG SEVRLRDDTI PSAHIALAVE GVSWKDDDYF
TALVTQAIVG NWDRAMGQSP FLGSKLSSHV SHHNLANSFM SFSTSYSDTG LWGIYLVSEN
LTQLDDLVHF TLREWSRLCT NVTSAEVERA KAQLKASILL SLDGTTAVAE DIGRQIITTG
RRLSPEDIER TVSQITEKDV MDFATRKLWD QDLAMSAVGS IEGVLDYQRM RGDMSRMIS
//
