ID   A0A238EZV4_9BASI        Unreviewed;       966 AA.
AC   A0A238EZV4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=BQ2448_5013 protein {ECO:0000313|EMBL:SCV67402.1};
GN   ORFNames=BQ2448_5013 {ECO:0000313|EMBL:SCV67402.1};
OS   Microbotryum intermedium.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX   NCBI_TaxID=269621 {ECO:0000313|EMBL:SCV67402.1, ECO:0000313|Proteomes:UP000198372};
RN   [1] {ECO:0000313|Proteomes:UP000198372}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jeantristanb JTB J.-T., Ricardo R.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC       pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}. Vacuole
CC       membrane {ECO:0000256|ARBA:ARBA00004576}; Single-pass type II membrane
CC       protein {ECO:0000256|ARBA:ARBA00004576}.
CC   -!- SIMILARITY: Belongs to the peptidase S9B family.
CC       {ECO:0000256|ARBA:ARBA00006150}.
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DR   EMBL; FMSP01000002; SCV67402.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238EZV4; -.
DR   STRING; 269621.A0A238EZV4; -.
DR   OrthoDB; 2876738at2759; -.
DR   Proteomes; UP000198372; Unassembled WGS sequence.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002469; Peptidase_S9B_N.
DR   PANTHER; PTHR11731:SF200; DIPEPTIDYL PEPTIDASE FAMILY MEMBER 2; 1.
DR   PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR   Pfam; PF00930; DPPIV_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022438};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022438};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198372};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT   TRANSMEM        84..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          223..660
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          746..947
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..50
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   966 AA;  107943 MW;  A3A03037416586EE CRC64;
     MSDVTWPRSL RPIMPTPFAP PITSTPSRNA EDRAYNDDEH DDDDLSSLDE EDAEKVGMMI
     ERSLAEVDST YRPTKARAAR RRTFCLLFLS ILLGCLFTAS TLSHLFRGPH TFNGGGLKPI
     SLEHLMNGTF SIKTEKLDWL AEDLIWDIRC AAGDGVYSHR SNDGSIFLED VNSGTSRVLV
     KSDAIRDVSS AERSQSRQSV TDSRIDAEQG SGQPLYWTKF AVSADLKYVL FATNPVSQWR
     HSSHANFYVH TVESGETVAL RPPSTTPHTA VASFSPKDHH IAYVHANDLY IVESPPSTGD
     GRSAIRVTVS GSPTTFNGVP DWVYEEEIFG SDSASWWSPD GSKLAFLSFD EQRVPEFSFP
     VYNPAAWGPG GGVPYPTETV MRYPKPGYAN PLVTIHVFDL ASYSAIPPRP TPIEDEAKPP
     VVDPRVLEMT YELVLSKPFD PNDMLVSEVT WVGKGDLMIK VTDRTAQVQR TAHFRLDEAV
     TNRKIVGQVV REENFGEIDG GWIEPTQTIV GIDSTLILHS SQNEASADVT RPKPSFPPGY
     LDIVADSEGF RHVAYFSPPD TATPIFLTRG KWEVVETLSA VDISRGLVYF IAANPSIERH
     LYSIPLPKTT AELHALNQAG AKPIAPTPLT DVTKMGHHTV SFSPFGGFYV INYRGPELPW
     QKLYKVDDQS FTKVLTDNAD LAQKDAAFQH VEISYSTLEL EGGYSVNIQE LRPPLMDISG
     RMKYPLLVEV YGGPNSQKVS TAFERDWHHF LVTSMGYIVV RIDPRGTGFK GRHFRVGIRN
     QLGFLEASDV VEATRQLVSA RSYIDPKRLG IWGWSYGGYL TAKVVETSSS LFTLAMSVAP
     VTDWRYYDSV YTERYMSTPK LNGEGYKKAA VVDMEGFKKL DYLLAHGSGD DNVHFLNSAA
     LLDKMTFASV RTFRFRMFTD SDHSIGMRNA YPELFQWMTA FLVEKWGEGG RSKQKWRTHT
     KEHFIE
//