ID A0A0D2ALQ7_9PEZI Unreviewed; 575 AA.
AC A0A0D2ALQ7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Alpha-MPP {ECO:0000256|ARBA:ARBA00030006};
DE AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000256|ARBA:ARBA00032315};
GN ORFNames=PV09_08376 {ECO:0000313|EMBL:KIW00024.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW00024.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW00024.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW00024.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KN847568; KIW00024.1; -; Genomic_DNA.
DR RefSeq; XP_016209893.1; XM_016362258.1.
DR AlphaFoldDB; A0A0D2ALQ7; -.
DR STRING; 253628.A0A0D2ALQ7; -.
DR GeneID; 27316349; -.
DR VEuPathDB; FungiDB:PV09_08376; -.
DR HOGENOM; CLU_009902_5_2_1; -.
DR InParanoid; A0A0D2ALQ7; -.
DR OrthoDB; 7099at2759; -.
DR Proteomes; UP000053259; 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; METALLOPROTEASE; 1.
DR PANTHER; PTHR11851:SF49; MITOCHONDRIAL-PROCESSING PEPTIDASE SUBUNIT ALPHA; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053259}.
FT DOMAIN 48..195
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 201..246
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 353..473
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 263..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 575 AA; 62640 MW; 9CBA1B67B6AC44CF CRC64;
MLRPAATRAA SRLTRHVPRC SRAFASAVAE ERDPVDLNEI TTLPNGVRVV SEALAGHFSG
IGVYIDAGSR YENEHLSGVS HIMDRLAFKS TTKRSGDEML ESIETLGGNI QCASSRESLM
YQSATFNSAV STTVALLAET IRDPKITDSE IEQQLATADY EINEIWAKPE LILPELVHVA
AYRDNTLGHP LLCPKERLPY INRTVIDQYR RLLYKPERMV VAFAGVDHLT AVRLTEQYFG
DMKRGEGAVL PLLNADGSVA TSQNAPLSNA DASASASSSS SHQSLPTSAV QNESRLLDKI
PFIKNLSTSA SRSASVSNPS TFTPPDLTEP SHYTGGFLSL PAIPPPLNPA LPRLSHIHLA
FEGLPISHDD IYALATLQTL LGGGGSFSAG GPGKGMYSRL YTNVLNQHGW VESCVAFNHS
YSDSGLFGIS ASCAPAHVAN MLEVMCRELS ALGSETGWQR LKEGEVGRAK NQLKSNLLMN
LESRMVELED LGRQVQMHGR KIGVKEMCDK VDRLTIADLR RVARQVFGGE VRNAGGGSGA
PTVVLQEGDE EGFKRKDFEW AEIQDRIARW KLGRR
//
