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Database: UniProt
Entry: Q1WMQ9_COPDI
LinkDB: Q1WMQ9_COPDI
Original site: Q1WMQ9_COPDI 
ID   Q1WMQ9_COPDI            Unreviewed;       245 AA.
AC   Q1WMQ9;
DT   02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   SubName: Full=Mitochondrial intermediate peptidase {ECO:0000313|EMBL:AAZ20150.1};
DE   Flags: Fragment;
GN   Name=MIP {ECO:0000313|EMBL:AAZ20150.1};
OS   Coprinellus disseminatus (Fairy ink cap fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinellus.
OX   NCBI_TaxID=71703 {ECO:0000313|EMBL:AAZ20150.1};
RN   [1] {ECO:0000313|EMBL:AAZ20150.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TJ-01-19.2 {ECO:0000313|EMBL:AAZ20150.1};
RX   PubMed=16461425; DOI=10.1534/genetics.105.051128;
RA   James T.Y., Srivilai P., Kuees U., Vilgalys R.;
RT   "Evolution of the bipolar mating system of the mushroom Coprinellus
RT   disseminatus from its tetrapolar ancestors involves loss of mating-type-
RT   specific pheromone receptor function.";
RL   Genetics 172:1877-1891(2006).
CC   -!- FUNCTION: Cleaves proteins, imported into the mitochondrion, to their
CC       mature size. While most mitochondrial precursor proteins are processed
CC       to the mature form in one step by mitochondrial processing peptidase
CC       (MPP), the sequential cleavage by MIP of an octapeptide after initial
CC       processing by MPP is a required step for a subgroup of nuclear-encoded
CC       precursor proteins destined for the matrix or the inner membrane.
CC       {ECO:0000256|ARBA:ARBA00025208}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR   EMBL; DQ056221; AAZ20150.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1WMQ9; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          2..227
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAZ20150.1"
SQ   SEQUENCE   245 AA;  27495 MW;  6D5B34F2BB639847 CRC64;
     VVLLTEFARP SVSRGPTVLE WYEVLTLFHE MGHAVHSMLG RTEYQNVSGT RCATDFVELP
     SILMEHFLNS PTVLSLFDAD STTTLRATGN NHADPCHSID TYSQILLAAV DQRYHSPSVL
     DPSFDSTAEL ANLHNTRGLM PYVPETSFQT QFGHLFGYGA TYYSYLFDRA IASRVWSKVF
     AENPLDRSRG ERLRGEVLMH GGAKDPWHMV SALMKMPELE SGNAEAMREV GKWRIEDEVG
     ISGRH
//
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