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Database: UniProt
Entry: A0A1L9P5X3_ASPVE
LinkDB: A0A1L9P5X3_ASPVE
Original site: A0A1L9P5X3_ASPVE 
ID   A0A1L9P5X3_ASPVE        Unreviewed;       814 AA.
AC   A0A1L9P5X3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=ASPVEDRAFT_58746 {ECO:0000313|EMBL:OJI96927.1};
OS   Aspergillus versicolor CBS 583.65.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=1036611 {ECO:0000313|EMBL:OJI96927.1, ECO:0000313|Proteomes:UP000184073};
RN   [1] {ECO:0000313|Proteomes:UP000184073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 583.65 {ECO:0000313|Proteomes:UP000184073};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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; KV878125; OJI96927.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9P5X3; -.
DR   STRING; 1036611.A0A1L9P5X3; -.
DR   VEuPathDB; FungiDB:ASPVEDRAFT_58746; -.
DR   OrthoDB; 167798at2759; -.
DR   Proteomes; UP000184073; Unassembled WGS sequence.
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   CDD; cd05238; Gne_like_SDR_e; 1.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; PF01370; Epimerase; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000184073}.
FT   DOMAIN          3..204
FT                   /note="NAD-dependent epimerase/dehydratase"
FT                   /evidence="ECO:0000259|Pfam:PF01370"
FT   DOMAIN          386..533
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          538..729
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   814 AA;  89215 MW;  BE4C63A68206C61F CRC64;
     MSIIITGAGG YVGQELASAL LASDPNLTVT LADVVAPDVP ASATQHASRT KCVKADLTSP
     AVVDELFSST NRYDTVYLLH GIMSSGAEAN FELGVRVNLD ATRYILDRLR AVQPGVKVVF
     TSSLAVYGLA PKGFVIDETN FPPVPESSYG TQKLVIEFLL NDYSRRGFLD GRAVRLPTVT
     VRAGKPTQAA SSFASGIIRE PFNGEKAVLP VNRDVEMWVC SPYTVVKNLM HAATVPKEAF
     GDSRSVNLPG IVVSVQEMLD ALEEVGGKEK RALVEEKYDA DIDRIVQTWS PHFNPARALK
     LGFSEDIPIL ENGRPASSSS IPPPSLSTPT FHPVTMASRR LAFNLNQALR SRAALKSIQP
     VKRGFASPVA LPSTTQSTTL SNGFTIATEH SPWAQTSTVG VWIDAGSRAE TDKTNGTAHF
     LEHLAFKGTN KRSQHQLELE IENMGAHLNA YTSRENTVYY AKSFNNDVPK AVDILADILQ
     HSKLESSAIE RERDVILREQ EEVDKQLEEV VFDHLHATAY QRQPLGRTIL GPKENIQTIT
     RDNLTEYINT NYTADRMVLV GAGGIPHQDL VRLAEQHFGS LPSKPPTSAA AALSAEQKRQ
     PEFIGSEVRI RDDTLPTAHI ALAAEGVSWK DDDYFTALVA QAIVGNWDRA MGNSPYLGSK
     LSSFVERNNL ANSFMSFSTS YSDTGLWGIY LVSENMTGLD DLIHFALREW SRLSFNVTAA
     EVERAKAQLK ASILLSLDGT TAVAEDIGRQ IITTGRRLSP EDIERTIGQI TEKDVMDFAN
     RKLWDQDIAM SAVGSIEGIL DYNRIRADMS RNTY
//
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