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Database: UniProt
Entry: A0A1G4M6V4_LACFM
LinkDB: A0A1G4M6V4_LACFM
Original site: A0A1G4M6V4_LACFM 
ID   A0A1G4M6V4_LACFM        Unreviewed;       819 AA.
AC   A0A1G4M6V4;
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=LAFE_0A04610g1_1 {ECO:0000313|EMBL:SCV99504.1};
GN   ORFNames=LAFE_0A04610G {ECO:0000313|EMBL:SCV99504.1};
OS   Lachancea fermentati (Zygosaccharomyces fermentati).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=4955 {ECO:0000313|EMBL:SCV99504.1, ECO:0000313|Proteomes:UP000190831};
RN   [1] {ECO:0000313|EMBL:SCV99504.1, ECO:0000313|Proteomes:UP000190831}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 6772 {ECO:0000313|EMBL:SCV99504.1};
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; LT598487; SCV99504.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4M6V4; -.
DR   STRING; 4955.A0A1G4M6V4; -.
DR   OMA; MRTPQEN; -.
DR   OrthoDB; 2876738at2759; -.
DR   Proteomes; UP000190831; Chromosome a.
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:UP000190831};
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          149..505
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          608..811
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   819 AA;  93429 MW;  EC3E358A9341551F CRC64;
     MRLHSDGYEE IDEGGNKRKS LLVTLTKVGV LLVLLIWGTV IVLKTVNGIV HQPLNRPKNR
     GNSRTTKDGH LKVSFANVRN NTFTPKIQPL QWISGPNSTT DDNGLFVTHI NDSYVVKSVF
     DPHYSKTLFK GHSFLYGQQN LTVDTMIASP DLQKVIIRTN TTKNWRHSTF GSYFVFSTEK
     SEYQMIGENI SVVEWSPNSI DIAYVLDNDL YLYSVEKQKT TKRITDDGSA QVFNGKPDWV
     YEEEVLEGDS AMWWSPEGDY LSFFKTNETE VYEFPIPYFV QHSDDVYPEV RMIKYPKSGS
     PNPVVHLNIY DLEKERTMNV NIDDDSVLIT DVLWVGAERL LARVTDRTSD ILSMVLVDAK
     KDAFYEVPRV EFSDDGWWEI THDTLYVPKD KSRDRHDDGY LDVVPINGYN HLVYFSSCDL
     SNPVILTDGD WEVVDGPAAF DYESNDVYFL ATKKSSMERH LYSVNIHKPL VIKEITDTSK
     DGYFDVTFSS GSRFTLLTYR GPDVPFQKII DLRSSKTDET IHGNVVGKTL YYLETNEELK
     GHLESYAIPR ITYQELNLGT DEKGNQILVN SYEILPNDFN PRLEKHYPVF FFGYGGPGSQ
     QVAKTFSVGF NQVVASQLNA IVVVVDGRGT GFKGREFRSL VRDNLGDYEA QDQISAAALY
     AKKSFVDEEK ISLFGWSYGG YLTLKTLEKD AGKHFKYGMS VAPVTDWRLY DSVYTERYMH
     TPQQNPEGYA SAKVHNATAL GEAKRFLLVH GTGDDNVHFQ NSLKFLDMLD IEGIENYDVH
     VFPDSDHSIR YHNANTIVFD KLLNWAKQAF EGHFISDMY
//
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