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Database: UniProt
Entry: M2RE39_COCSN
LinkDB: M2RE39_COCSN
Original site: M2RE39_COCSN 
ID   M2RE39_COCSN            Unreviewed;       572 AA.
AC   M2RE39;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Alpha-MPP {ECO:0000256|ARBA:ARBA00030006};
DE   AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000256|ARBA:ARBA00032315};
GN   ORFNames=COCSADRAFT_36385 {ECO:0000313|EMBL:EMD65034.1};
OS   Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot and
OS   spot blotch fungus) (Bipolaris sorokiniana).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD65034.1, ECO:0000313|Proteomes:UP000016934};
RN   [1] {ECO:0000313|EMBL:EMD65034.1, ECO:0000313|Proteomes:UP000016934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [2] {ECO:0000313|Proteomes:UP000016934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(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}.
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DR   EMBL; KB445642; EMD65034.1; -; Genomic_DNA.
DR   RefSeq; XP_007699158.1; XM_007700968.1.
DR   AlphaFoldDB; M2RE39; -.
DR   STRING; 665912.M2RE39; -.
DR   GeneID; 19138721; -.
DR   KEGG; bsc:COCSADRAFT_36385; -.
DR   eggNOG; KOG2067; Eukaryota.
DR   HOGENOM; CLU_009902_5_2_1; -.
DR   OMA; LKYHHSP; -.
DR   OrthoDB; 7099at2759; -.
DR   Proteomes; UP000016934; 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:UP000016934}.
FT   DOMAIN          57..204
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          210..255
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          350..470
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   572 AA;  61928 MW;  26FB30533E1BB698 CRC64;
     MLRPRSCRPL SQGLSRPYSS LRAPPACAGR RSLATAVAQE RDPAELDHIT TLPNGIRVAT
     EALPGHFSGI GVYVDAGSRY ENDALRGVSH IIDRLAFKST RSTTGDQMME KIETLGGNIQ
     CASSRESLMY QSATFNSAVP TTVGVLAETI RDPLITEDEV QQQLETADYE IGEIWSKPEL
     ILPELVHMAA YKDNTLGNPL LCPKERLPLI NRAVVEAYRK EFFKPERIVV AFAGVNHNEA
     VRLTEEYFGD MEKGTGPALP SVGSDGAAAS QANFTADHPM PKGALPGSSN LISKIPFLKN
     LSTSASSTAN LTTAPDLNFP PIDTSIPSQY TGGFLTLPPI PPPANPMLPR LSHIHLAFEA
     LPISSPDIYA LATLQTLLGG GGSFSAGGPG KGMYSRLYTN VLNQHGWVES CVAFNHSYTD
     SGLFGIAASC APSYTAHMLE VMCRELKSLS DETGFAALKD GEVQRAKNQL RSSLLMNLES
     RMVELEDLGR QVQVHGRKVG VKEMCSKIEA VTVKDLRRVA KQVFGGDVHN AGKGSGAPTV
     VLQEGEMEGL KRKDLTWDDI QSRIAKWKLG RR
//
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