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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//