ID   A0A1G4JAA8_9SACH        Unreviewed;       814 AA.
AC   A0A1G4JAA8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=LAMI_0D03312g1_1 {ECO:0000313|EMBL:SCU86716.1};
GN   ORFNames=LAMI_0D03312G {ECO:0000313|EMBL:SCU86716.1};
OS   Lachancea mirantina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1230905 {ECO:0000313|EMBL:SCU86716.1, ECO:0000313|Proteomes:UP000191024};
RN   [1] {ECO:0000313|EMBL:SCU86716.1, ECO:0000313|Proteomes:UP000191024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 11717 {ECO:0000313|EMBL:SCU86716.1};
RA   Devillers H.;
RL   Submitted (MAR-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; LT598463; SCU86716.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4JAA8; -.
DR   STRING; 1230905.A0A1G4JAA8; -.
DR   OrthoDB; 2876738at2759; -.
DR   Proteomes; UP000191024; Chromosome d.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; IPR002471; Pept_S9_AS.
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.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022438};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191024};
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        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          145..502
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          606..806
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   814 AA;  92149 MW;  E5489EF94C08E6C0 CRC64;
     MEDGYQELDE PNRKKRGSLE AWIKLGVILV LLVWGSALLI SSLPLEHHSD HKNGLRHIPK
     RTKNGQLKVS FANLRNDTFS PVTRSLRWLY SDDATEDDQG FFLTEVNGTY VVRSVFDKDY
     SRVLLEKSDF VYAGQNLTAE SIIASPDQEH ILLKTDTVKN WRHSTFGSYY VFDTKDHSIN
     FVGNNISLAL WSPNSNDVAY VFENNVYVYS SKAGKTIAQV THDGSSQVFN GIPDWVYEEE
     VFEGNQALWW STSGEYLSFL KINETEVHEF PIAYYVQHDD DIYPEIRKIK YPKSGTPNPS
     AEIQLFHLET QHLSSVFAGN SSTLVTEMTW LGGEQLLVKV TDRTSDTLSI LLVDAGKGGV
     VTTPRVCPSG EGWWEITHRT TYLPKDIKKG RKDEGYIDLM PVDGFNHLAY FSPPETDEPV
     ILTRGEWEVV DGPTAVDLET NNVYFIATKK SSTERHLYRV NILKPEKIEA ITDTSKPGTF
     SVSFSSGSGL ALLNYLGPDI PYQKIVTLRT HKKDSTIHGN IVGKTLYYLE DNAALHRVLN
     LYDVPKKTFG TLELGHDQNG KSVTANYYEI LPNDFDPSRR DHYPVFFFAY GGPNSQQVLQ
     IFSVGFNEVV SSQLDAIVVV VDGRGTGFRG KDFRSYVRDN LGDLEAQDQI EAAKIYGNKP
     YVNQDKISLF GWSYGGYLTL KTLEKDAGKH FKYGMSVAPV TDWRFYDSVY TERYMHTPQE
     NPEGYRKAKV SNATALGQAQ RFLLMHGTGD DNVHFQNSLK FLDLLDLAGV ENYDFHVFPD
     SDHSIRYHNA NIIVFDKLLN WIGQAYDGQF VKIG
//