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Database: UniProt
Entry: Q1WN51_COPDI
LinkDB: Q1WN51_COPDI
Original site: Q1WN51_COPDI 
ID   Q1WN51_COPDI            Unreviewed;       170 AA.
AC   Q1WN51;
DT   02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   SubName: Full=Mitochondrial intermediate peptidase {ECO:0000313|EMBL:AAZ09351.1};
DE   Flags: Fragment;
GN   Name=MIP {ECO:0000313|EMBL:AAZ09351.1};
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:AAZ09351.1};
RN   [1] {ECO:0000313|EMBL:AAZ09351.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TJ-00-99.1 {ECO:0000313|EMBL:AAZ09351.1};
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   -!- 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|RuleBase:RU003435}.
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DR   EMBL; DQ056044; AAZ09351.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1WN51; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1370.40; -; 1.
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   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          20..165
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAZ09351.1"
FT   NON_TER         170
FT                   /evidence="ECO:0000313|EMBL:AAZ09351.1"
SQ   SEQUENCE   170 AA;  19070 MW;  10443169D8D5A07E CRC64;
     GHRIQESQAF ESVKRHRLPN QEGVYQLPLV VLLTEFARPS VSRGPTVLEW YEVLTLFHEM
     GHAMHSMLGR TEYQNVSGTR CATDFVELPS ILMEHFLNSP TVLSLFDADS TTTLRATGNN
     HADPCHSIDT YSQILLAAVD QRYHSPSVLD PSFDSTAELA HLHNTRGLMP
//
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