ID   A0A427XGM2_9TREE        Unreviewed;       400 AA.
AC   A0A427XGM2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Peptidase M48 domain-containing protein {ECO:0000259|Pfam:PF01435};
GN   ORFNames=EHS24_003040 {ECO:0000313|EMBL:RSH77966.1};
OS   Apiotrichum porosum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Apiotrichum.
OX   NCBI_TaxID=105984 {ECO:0000313|EMBL:RSH77966.1, ECO:0000313|Proteomes:UP000279236};
RN   [1] {ECO:0000313|EMBL:RSH77966.1, ECO:0000313|Proteomes:UP000279236}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27194 {ECO:0000313|EMBL:RSH77966.1,
RC   ECO:0000313|Proteomes:UP000279236};
RA   Aliyu H., Gorte O., Ochsenreither K.;
RT   "Genome sequence of Apiotrichum porosum DSM 27194.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003983};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003983};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC       inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC       protein {ECO:0000256|ARBA:ARBA00004434}.
CC   -!- SIMILARITY: Belongs to the peptidase M48 family.
CC       {ECO:0000256|RuleBase:RU003983}.
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:RSH77966.1}.
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DR   EMBL; RSCE01000014; RSH77966.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A427XGM2; -.
DR   STRING; 105984.A0A427XGM2; -.
DR   OrthoDB; 5490879at2759; -.
DR   Proteomes; UP000279236; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07331; M48C_Oma1_like; 1.
DR   Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR   InterPro; IPR001915; Peptidase_M48.
DR   PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR   PANTHER; PTHR22726:SF1; METALLOENDOPEPTIDASE OMA1, MITOCHONDRIAL; 1.
DR   Pfam; PF01435; Peptidase_M48; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003983};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW   Reference proteome {ECO:0000313|Proteomes:UP000279236};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT   TRANSMEM        80..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          198..357
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
FT   REGION          37..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..374
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..400
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   400 AA;  43929 MW;  903F5C34E0C7540F CRC64;
     MRPLLTATRI ARPAAKSLAS IPAARTVRPA VLKQLPRRGF TTSPPKSARY ERFDFPSSGQ
     PGGSNNVTNF LRRRLGGDRG MIVFGVATGF GVIYYIAHLE RVPETGRLRF MDCSPEQEQE
     IGKASFVETM DQFGMKCLPP NHPITRRVRE IATRIVEGNA LGHMKSAPGL GAVEARMSQW
     GIDENGNIYS GDRADDQNST KNEWEVFVVD DPKTKNAFVI PGGKIFVFTG ILPVSANDDG
     LATVMGHEIA HVVARHGAER MSSMKVLFGI SFLFESLGLD VGLTRLLVTF LLQLPNSRTN
     ESEADTIGLN LMAKACYHPS EAPKMWERMS AADGGGGNLD FMSTHPANAK RIKALMKEQP
     EATKLREDRC QNVPTNKDFS DAMRNLSTSS SSNDRQSVWA
//