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Database: UniProt
Entry: K3VYS8_FUSPC
LinkDB: K3VYS8_FUSPC
Original site: K3VYS8_FUSPC 
ID   K3VYS8_FUSPC            Unreviewed;       565 AA.
AC   K3VYS8;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Alpha-MPP {ECO:0000256|ARBA:ARBA00030006};
DE   AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000256|ARBA:ARBA00032315};
GN   ORFNames=FPSE_08681 {ECO:0000313|EMBL:EKJ71175.1};
OS   Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ71175.1, ECO:0000313|Proteomes:UP000007978};
RN   [1] {ECO:0000313|EMBL:EKJ71175.1, ECO:0000313|Proteomes:UP000007978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CS3096 {ECO:0000313|EMBL:EKJ71175.1,
RC   ECO:0000313|Proteomes:UP000007978};
RX   PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA   Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA   Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT   "Comparative pathogenomics reveals horizontally acquired novel virulence
RT   genes in fungi infecting cereal hosts.";
RL   PLoS Pathog. 8:E1002952-E1002952(2012).
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:EKJ71175.1}.
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DR   EMBL; AFNW01000294; EKJ71175.1; -; Genomic_DNA.
DR   RefSeq; XP_009260074.1; XM_009261799.1.
DR   AlphaFoldDB; K3VYS8; -.
DR   EnsemblFungi; EKJ71175; EKJ71175; FPSE_08681.
DR   GeneID; 20367299; -.
DR   KEGG; fpu:FPSE_08681; -.
DR   eggNOG; KOG2067; Eukaryota.
DR   HOGENOM; CLU_009902_5_2_1; -.
DR   OrthoDB; 7099at2759; -.
DR   Proteomes; UP000007978; Chromosome 1.
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:UP000007978};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          59..206
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          212..462
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          256..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..297
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   565 AA;  61408 MW;  DA194F8D7C2A4B42 CRC64;
     MLRQFSAGLP KARASCSKVL GQASKFSMAR RSMATVKVKG IEKDPTELDK VTTLPNGLRV
     ASEALPGSFA GVGVYIEGGS RFENDSLRGV SHIMDRLAFK STSKRSADDM LEQVEALGGN
     IQCASSRESM MYQAATFNNA VPQTIELLAE TIRDPQITDL EVAEQIETAR YEIREIWSKP
     ELILPELVHT AAFKDNTLGN PLLCPEERLG SIDKNTVMAY RDLFYRPERM VVAYAGVEHS
     EAVRLTEKFF GDMQKGAQQV TEATGSETSE SELSDSEASA SSASSSPQQS SGLLSRFFKN
     TPSAPQNLNN LPSQADIIRP SKYTGGFSWL PAQPPNLSGL PTFTHIHLAF EGLPVSSDDI
     YALATLQTLL GGGGSFSAGG PGKGMYSRLY TNVLNQHGWV ESCMAFNHSY TDSGLFGISA
     SCLPGRTAAM LDVMCQELRA LTLTTGFSRL QETEVARAKN QLRSSLLMNL ESRMVELEDL
     GRSIQVHGRK IPVKDMCRRI ENLTVADLRR VATMIVGGHV KNPGGGSGAP TVVLQEAQAY
     GVSSHTMSWD QIQDRIDSWK LGSLS
//
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