ID A0A0J1B4M9_9TREE Unreviewed; 449 AA.
AC A0A0J1B4M9;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=CC85DRAFT_285354 {ECO:0000313|EMBL:KLT42629.1};
OS Cutaneotrichosporon oleaginosum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT42629.1, ECO:0000313|Proteomes:UP000053611};
RN [1] {ECO:0000313|EMBL:KLT42629.1, ECO:0000313|Proteomes:UP000053611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBC0246 {ECO:0000313|EMBL:KLT42629.1,
RC ECO:0000313|Proteomes:UP000053611};
RG DOE Joint Genome Institute;
RA Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT T. oleaginosus allow insights into substrate utilization and the diverse
RT evolutionary trajectories of mating systems in fungi.";
RL Submitted (MAR-2015) 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 ---------------------------------------------------------------------------
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; KQ087203; KLT42629.1; -; Genomic_DNA.
DR RefSeq; XP_018279120.1; XM_018423083.1.
DR AlphaFoldDB; A0A0J1B4M9; -.
DR STRING; 879819.A0A0J1B4M9; -.
DR GeneID; 28983686; -.
DR OrthoDB; 167798at2759; -.
DR Proteomes; UP000053611; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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; 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.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KLT42629.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053611}.
FT DOMAIN 60..171
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 176..364
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 449 AA; 49468 MW; B61C85E78DADF4C5 CRC64;
MRGCTSVSAG RRCARCVQCG AVASPIVIAP ITGDVLPLIA PRNSPKLPSL RISSARLTSQ
HLAFKGTKSR SQMQLELEVE NLGAHLNAYT SREQTVYYAK AFDKDVPAVV NILSDILQNS
KLDESAIERE RDVILREQEE VDKQLEEVVF DHLHAIAFQG HKLGNTILGP KEHINSISKA
DLSGYIAKNY TADRMALVGA GSITHEALVE LAKENFASLP VSSNPIPLGQ ASHEPTQFTG
SEVRIRDDTM STCNIAIAVE GVGWRSPDYW PMLVMQSIFG NWDRSLGASP LLSSRLSHII
SSNNLANSFM SFSTSYSDTG LWGIYAVSEN LMNLDDLTHF IMKEWQRMSI GPSTAEVERA
KSQLKASLLL GLDGTTAIAE DIGRQTITTG KRYTPKEIER YVNAVTVQDI KRVAEKYLWD
RPLCVSAIGR VEGLLDYNRM SADMSSLTY
//
