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
//