ID J8PN01_SACAR Unreviewed; 482 AA.
AC J8PN01;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Alpha-MPP {ECO:0000256|ARBA:ARBA00030006};
DE AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000256|ARBA:ARBA00032315};
GN ORFNames=SU7_1421 {ECO:0000313|EMBL:EJS43490.1};
OS Saccharomyces arboricola (strain H-6 / AS 2.3317 / CBS 10644) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1160507 {ECO:0000313|EMBL:EJS43490.1, ECO:0000313|Proteomes:UP000006968};
RN [1] {ECO:0000313|EMBL:EJS43490.1, ECO:0000313|Proteomes:UP000006968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H-6 / AS 2.3317 / CBS 10644
RC {ECO:0000313|Proteomes:UP000006968};
RX PubMed=23368932; DOI=10.1186/1471-2164-14-69;
RA Liti G., Nguyen Ba A.N., Blythe M., Mueller C.A., Bergstroem A.,
RA Cubillos F.A., Dafhnis-Calas F., Khoshraftar S., Malla S., Mehta N.,
RA Siow C.C., Warringer J., Moses A.M., Louis E.J., Nieduszynski C.A.;
RT "High quality de novo sequencing and assembly of the Saccharomyces
RT arboricolus genome.";
RL BMC Genomics 14:69-69(2013).
CC -!- FUNCTION: Substrate recognition and binding subunit of the essential
CC mitochondrial processing protease (MPP), which cleaves the
CC mitochondrial sequence off newly imported precursors proteins.
CC {ECO:0000256|ARBA:ARBA00002123}.
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:EJS43490.1}.
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DR EMBL; ALIE01000097; EJS43490.1; -; Genomic_DNA.
DR AlphaFoldDB; J8PN01; -.
DR HOGENOM; CLU_009902_5_2_1; -.
DR OrthoDB; 7099at2759; -.
DR Proteomes; UP000006968; Chromosome VIII.
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; METALLOPROTEASE; 1.
DR PANTHER; PTHR11851:SF49; MITOCHONDRIAL-PROCESSING PEPTIDASE SUBUNIT ALPHA; 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:UP000006968}.
FT DOMAIN 29..176
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 182..374
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 482 AA; 53294 MW; 8FDDA5839D3C57D5 CRC64;
MLRNSAKRLY SNIARTDNFK LSSLANGLKV ATSNSPGHFS ALGLYIDAGS RFEGRNLKGC
THILDRLAFR STEHIEGRAM AETLELLGGN YQCTSSRENI MYQASVFNQD VGKMLKLMSE
TVRFPKITEQ ELQEQKVSAE YEIDEVWMKP ELVLPELLHT AAYSGETLGS PLICPRELIP
SISKYYLLDY RNKLYTPENT VAAFVGVPHD KALELADKYL GDWQSTHPPI SKKTAHYTGG
ESCIPPAPIF GNLPELFHIQ IGFEGLPIDH PDIYALATLQ TLLGGGGSFS AGGPGKGMYS
RLYTHVLNQY YFVENCVAFN HSYSDSGIFG ISLSCIPQAA PQAVEVIAQQ MYNTFANKDL
ELTEDEVTRA KNQLKSSLLM NLESKLVELE DMGRQVLMHG RKIPINEMIS KIEDLKPHDI
SRVAEMIFTG NVNNAGKGIG KATVVMQGDR SAFGDVENVL NAYGLGNNTP IENGSTKKTS
WF
//
