ID   F2PUT9_TRIEC            Unreviewed;       588 AA.
AC   F2PUT9;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, 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=TEQG_04666 {ECO:0000313|EMBL:EGE05657.1};
OS   Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN   [1] {ECO:0000313|Proteomes:UP000009169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(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}.
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DR   EMBL; DS995741; EGE05657.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2PUT9; -.
DR   VEuPathDB; FungiDB:TEQG_04666; -.
DR   eggNOG; KOG2067; Eukaryota.
DR   HOGENOM; CLU_009902_5_2_1; -.
DR   Proteomes; UP000009169; 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;
FT   DOMAIN          49..196
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          202..255
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          366..486
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          256..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..289
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   588 AA;  64019 MW;  6EE719792F044CD1 CRC64;
     MHRLALRAGR SRKPSIPRLA PRSFATVRQP ENKDPVELDQ ITTLSNGLRV ATESLPGPFA
     GVGVYIDAGS RYENNELRGV SHIVDRLAFK STSKRNADQM LESLESLGGN IQCASSRESL
     MYQSASFNST VPTTLGLLAE TIRDPLITED EVAQQLAVAE YEITELWAKP EMILPELVNM
     AAYKDNTLGN PLLCPRERLG QITKSTVDKY RTAFFNPNKM VVAFAGVSHT DAVRMTEQYF
     GDMKNQKSPL LAQFGSETSS THGEEEVPTF PAFSPSSTTP TESPDSSAPH SPSSTPPSSP
     SSPGLLSRVP FFKNLSTSAP NQATVSPLNP SLLQTDLIDV SRPSYYTGGF MSLPRIPPPA
     NPAMPRLSHI HLAFEALPIS SPDIYALATL QTLLGGGGSF SAGGPGKGMY SRLYTNVLNQ
     HGWVESCMAF NLSYTDSGLF GISASCVPNS IANMLEVMCR ELQALTLDSG YSGLQIQEVN
     RAKNQLRSSL LMNLESRMVE LEDLGRQVQV HGRKIGVQEM CKKIEALTVD DLRRVAKQVF
     GGLVQNRGQG TGRPTVVIQE GEMEGTKLAP LQWTEIQQRI AKWGLGRA
//