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Database: UniProt
Entry: A0A0J0XYJ9_9TREE
LinkDB: A0A0J0XYJ9_9TREE
Original site: A0A0J0XYJ9_9TREE 
ID   A0A0J0XYJ9_9TREE        Unreviewed;       601 AA.
AC   A0A0J0XYJ9;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KLT46130.1};
GN   ORFNames=CC85DRAFT_324940 {ECO:0000313|EMBL:KLT46130.1};
OS   Cutaneotrichosporon oleaginosum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX   NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT46130.1, ECO:0000313|Proteomes:UP000053611};
RN   [1] {ECO:0000313|EMBL:KLT46130.1, ECO:0000313|Proteomes:UP000053611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBC0246 {ECO:0000313|EMBL:KLT46130.1,
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|PIRSR:PIRSR634016-3};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
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DR   EMBL; KQ087178; KLT46130.1; -; Genomic_DNA.
DR   RefSeq; XP_018282621.1; XM_018426276.1.
DR   AlphaFoldDB; A0A0J0XYJ9; -.
DR   STRING; 879819.A0A0J0XYJ9; -.
DR   GeneID; 28986879; -.
DR   OrthoDB; 3085317at2759; -.
DR   Proteomes; UP000053611; Unassembled WGS sequence.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd09601; M1_APN-Q_like; 1.
DR   Gene3D; 2.60.40.1910; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR   InterPro; IPR045357; Aminopeptidase_N-like_N.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR034016; M1_APN-typ.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR634016-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053611};
KW   Zinc {ECO:0000256|PIRSR:PIRSR634016-3}.
FT   DOMAIN          12..178
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          267..483
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   ACT_SITE        338
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT   BINDING         337
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         341
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         360
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            424
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ   SEQUENCE   601 AA;  66755 MW;  801E65BF0ACE8969 CRC64;
     MSDYRLPTSV RPTHYELAVR TDLAALRYEA EVIISLEVLE DTPTIVFHMH PSLSVTHLAL
     NAGSTQELAL SALHTDADKE RATVKLAEPL KKGAAKLAVR YEAELNGNMM GYYRSNSDPD
     ENGKRLVYAL TQFEPTAARR ALPCWDEPLF KATFGVTLIA RKHEVVLANM DAEGCKPFSP
     AAVKFEDIFA DGYVAGSTLA PTFSSASNPD GWVATRFTPT PLMSTYLLAW ACGEFTHIEA
     LHKSAITGKT IPLRVYATNN IDQAKMALDA TASALRVYEE LFRIAYPLPK LDTLVAHDFD
     MGAMENWGLI TGRTAAYLVN ERSSLASLKR CGTIQCHEVA HMWFGNIVTM RWWDNLWLNE
     AFATLMGSLV LPERIWPEWK MAGEFLEAHW DRALSLDAKR SSHPIQVECP DSNKIATIFD
     AISYSKGASV LRMLMSVVGE EKFFQGVATY LNKHLYGNAE MQDLWDGISS SVGKDVGDMM
     NAWTMRVGFP VVRVEELGNS KLKLSQARFL STGDAKPEEN KTTWWVPLEV KTVDKDGAQV
     DHSAVLSDRE MEYNVASDTF KLNAEAVGVY RVAYTPERLG KLGSQAASFS PADRLGLIKN
     R
//
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