ID   A0A0J0XMK1_9TREE        Unreviewed;       513 AA.
AC   A0A0J0XMK1;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Peptidase M48 domain-containing protein {ECO:0000259|Pfam:PF01435};
GN   ORFNames=CC85DRAFT_285716 {ECO:0000313|EMBL:KLT42312.1};
OS   Cutaneotrichosporon oleaginosum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX   NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT42312.1, ECO:0000313|Proteomes:UP000053611};
RN   [1] {ECO:0000313|EMBL:KLT42312.1, ECO:0000313|Proteomes:UP000053611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBC0246 {ECO:0000313|EMBL:KLT42312.1,
RC   ECO:0000313|Proteomes:UP000053611};
RG   DOE Joint Genome Institute;
RA   Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA   Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT   "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT   T. oleaginosus allow insights into substrate utilization and the diverse
RT   evolutionary trajectories of mating systems in fungi.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; KQ087207; KLT42312.1; -; Genomic_DNA.
DR   RefSeq; XP_018278803.1; XM_018423219.1.
DR   AlphaFoldDB; A0A0J0XMK1; -.
DR   STRING; 879819.A0A0J0XMK1; -.
DR   GeneID; 28983822; -.
DR   OrthoDB; 336005at2759; -.
DR   Proteomes; UP000053611; 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:SF18; PEPTIDASE_M48 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01435; Peptidase_M48; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053611};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        114..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          258..439
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   513 AA;  57867 MW;  277B75BCE70C50D5 CRC64;
     MPPPPLRWGW QRRALIAPLL SQRPILLPTF RTYTRSPLPP TSPPRLRPPL RPLPPSTTTP
     VLVRALRASP PRRDILFLSM PALKSTLLGI TRFSLLALPF VWRYKLWRKY KRTSWLLIQI
     PIFALCIVVA LGLDQSPRTG RWRLLLMSEN EELAWSYRKH KEVLAHDGPL ILPPDDLRSE
     QVARVATRLV TALEEQNDNV VCGAAWPPRE DIMEAIYDHE DRMSRRRTRV IEVEPSAVAH
     SNFVPFRPLS SNPLKGENIK ASDWDIYLID LPQLNAFALP SKEIFVYTGL LDVLPQGDDS
     LVAAVLAHEI AHVAERHSVE NLGFLNLAAV VFDVLRGISF AFTISFPVVT DGAGMFLNWL
     NDVVAERAYS RKIEEEADSV GLEIMARAGY DPRAMLDLWE LMAAVEADAE AMGYGRSLES
     RFQLLRTHPT SEARQEAIAN QLPKAMRLWQ EARTPQRAAI EKILAEKADM PEPRALASDE
     VRIGAVVAKI QPRVNFAVVP ELPEPEPEPE RAV
//