ID A0A074YTP6_AURSE Unreviewed; 487 AA.
AC A0A074YTP6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=AUEXF2481DRAFT_38022 {ECO:0000313|EMBL:KEQ97512.1};
OS Aureobasidium subglaciale (strain EXF-2481) (Aureobasidium pullulans var.
OS subglaciale).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043005 {ECO:0000313|EMBL:KEQ97512.1, ECO:0000313|Proteomes:UP000030641};
RN [1] {ECO:0000313|EMBL:KEQ97512.1, ECO:0000313|Proteomes:UP000030641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2481 {ECO:0000313|EMBL:KEQ97512.1,
RC ECO:0000313|Proteomes:UP000030641};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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; KL584754; KEQ97512.1; -; Genomic_DNA.
DR RefSeq; XP_013345910.1; XM_013490456.1.
DR AlphaFoldDB; A0A074YTP6; -.
DR STRING; 1043005.A0A074YTP6; -.
DR MEROPS; M16.980; -.
DR GeneID; 25365998; -.
DR HOGENOM; CLU_009902_4_2_1; -.
DR InParanoid; A0A074YTP6; -.
DR OMA; IDVVCDM; -.
DR OrthoDB; 167798at2759; -.
DR Proteomes; UP000030641; 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:UP000030641}.
FT DOMAIN 59..206
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 211..402
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 487 AA; 54023 MW; F4E0921EF96DDBD4 CRC64;
MASTMATRRL ALNLQHATRS RTAINAIKAG SPSLFRGLAT PVSHGSKTES TTLSNGFTIA
TEHSPYAQTS TVGVWIDAGS RAETDKTNGT AHFLEHLAFK GTQKRSQSQL ELEIENMGGH
LNAYTSRENT VYYAKSFNSD VPNTVDILSD ILQNSKLETQ AIERERDVIL REQEEVDKQL
EEVVFDHLHA TAFMNQPLGR TILGPKENIQ SISRDDLTNY IKTNYTADRM VLVGSGGVPH
KELVQLAEKY FSNIPMAPPT STAQALANAQ KEKPDFVGSE VRIRDDTIPT ANIAIAVEGV
SWKDDDYFTA LVTQAIVGNW DRAMGNSPYL GSKLSTFIHE HKLANSFMSF STSYSDTGLW
GIYLVTDAVT RIDDLVHFTL REWSRLSFQV SESEVERAKA QLKASILLSL DGTTAVAEDI
GRQIITTGRR LAPEEVERVV GQITAKDVME FAKRKLWDRD IAISAVGQIE GLLDYSRIRN
DMTRMLS
//
