ID A0A0J0XSE9_9TREE Unreviewed; 859 AA.
AC A0A0J0XSE9;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=CC85DRAFT_284037 {ECO:0000313|EMBL:KLT44001.1};
OS Cutaneotrichosporon oleaginosum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT44001.1, ECO:0000313|Proteomes:UP000053611};
RN [1] {ECO:0000313|EMBL:KLT44001.1, ECO:0000313|Proteomes:UP000053611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBC0246 {ECO:0000313|EMBL:KLT44001.1,
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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family.
CC {ECO:0000256|RuleBase:RU361240}.
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DR EMBL; KQ087190; KLT44001.1; -; Genomic_DNA.
DR RefSeq; XP_018280492.1; XM_018422590.1.
DR AlphaFoldDB; A0A0J0XSE9; -.
DR STRING; 879819.A0A0J0XSE9; -.
DR GeneID; 28983193; -.
DR OrthoDB; 277019at2759; -.
DR Proteomes; UP000053611; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03875; M28_Fxna_like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR048024; Fxna-like_M28_dom.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147:SF54; ENDOPLASMIC RETICULUM METALLOPEPTIDASE 1-RELATED; 1.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|RuleBase:RU361240};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU361240};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW Reference proteome {ECO:0000313|Proteomes:UP000053611};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|RuleBase:RU361240}.
FT TRANSMEM 380..396
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 403..428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 448..469
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 481..498
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 504..522
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 534..557
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 577..598
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 610..629
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 141..337
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 859 AA; 94648 MW; 82DF342040B4D1FA CRC64;
MASGNGQQGR SKAQPERRPR ERTPWLLLLP VVLIFPYILS RLHYALPAPQ PPVDAEGRPQ
PSEEIVIGHI QKLEDIGYRT VGTEEAVRGE EYVIAEVRKI EERCKANGVL DCEVWIQRGN
GYHEFSIMGH DVLKVYAGIR NVVLQIRAKK PLTPRTLKKD AILLGSHIDS TLPSPGAADD
GMGVGVMLDV ARVLVDRNEP FDNSVIFMWN GGEETLQDGS HLYSTQHPTA AEVRAMFNLE
AAGTTGGALL FQATSQEMID AFSRAPYPRG TVIAADVFSS GIILSDTDFG QFEEYLNVSG
LDMAVVGHSY FYHTRKDSTQ FIEVGTSQHF TSNAMAIVDY LLSPGSPLGA AGEWSPPDVV
YMSLYDRIFL SWTMKNADKA YLAITAVIAA ITLANIRRER GRAFAIALLG APLGLAGGLI
TANIVAFVMS ASGNQMGWFS HEGLPVALYG PASVLGHLAT QHALSALISP AHRVFLEHAH
YYSQLVSLAV WMLILQAFRV RSAYLFAGIA CTVLLGAFVT EARTLVFGGR NRALPFIGAY
IMPLVLLLAL AMEAYTTTLD IFVPLTGRMG KDAPVEHIIA IITSVCTLVF FPIISPLFSR
ISRATQRKVL VALVVVTLGV AALFASPFWS PYDFMHPKRL GVQYTYNHTS GQETAHIAFM
DTGRNSAVMK ELHDQFGGGA ALVRTEQADD NADWDVLYPV SSFLETYSFA LPKTTFDWPE
MTFEATREKT AHGHTRIHIK TEHEGLVWPA LSFDADLVDW SFDFDPPHGR KRHHIKAAAS
VDEHVMELEL IMRLKDDEPF HLHWSAMDLN QMVPGTAPRR GPNMPASKWL TAMDEWARER
YAGGIDICMN GVVVGVLTL
//
