ID A0A1Y1XVY1_9FUNG Unreviewed; 469 AA.
AC A0A1Y1XVY1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=K493DRAFT_232042 {ECO:0000313|EMBL:ORX89919.1};
OS Basidiobolus meristosporus CBS 931.73.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Basidiobolomycetes; Basidiobolales; Basidiobolaceae;
OC Basidiobolus.
OX NCBI_TaxID=1314790 {ECO:0000313|EMBL:ORX89919.1, ECO:0000313|Proteomes:UP000193498};
RN [1] {ECO:0000313|EMBL:ORX89919.1, ECO:0000313|Proteomes:UP000193498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 931.73 {ECO:0000313|EMBL:ORX89919.1,
RC ECO:0000313|Proteomes:UP000193498};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORX89919.1}.
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DR EMBL; MCFE01000412; ORX89919.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1XVY1; -.
DR STRING; 1314790.A0A1Y1XVY1; -.
DR InParanoid; A0A1Y1XVY1; -.
DR OrthoDB; 167798at2759; -.
DR Proteomes; UP000193498; 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:UP000193498}.
FT DOMAIN 54..201
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 206..390
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 469 AA; 51969 MW; C97E2E92836F42A8 CRC64;
MTSRVLLPKA LKPLIPFAPT LKATRTLPIL HQRFGTVTEA PRTRISKLAN GFTVATESIP
TAKTATVGVW IDAGSRAENS KNNGTAHFLE HMAFKGTKRR TQRELEVMIE NMGGHLNAYT
SREQTVYYAK TFKSDLPAAV DILSDILLNS TLNPGAVERE RDVIVREQEE VDKIMEEVVF
DHLHATAFQE HSLGRTILGP KENILSIKRD DLVNYITTNY KADRMVLVGA GGVDHEELVS
LAEKHFSLLP SSDGPRPESK RPKFVGSEIK LTDNTASQAH IALAVEGVGW SSPDYYPMLI
LQSIIGNWDR AFSTPSGSSF RLSSVVAAKQ LANSFMSFNT SYSDTGLFGI YMISENKDKL
DELVFTAQKE WARLSVTVTD AEVERAKQQL KAALLLNLDG STAIAEDIGR QMITMSKRVE
PKEVEATINS ITGDDVRRIA QQYLYDRDIA VVGLGPVDKL PEYSQIRIN
//
