ID A0A1G4KGT6_9SACH Unreviewed; 874 AA.
AC A0A1G4KGT6;
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_0H10902g1_1 {ECO:0000313|EMBL:SCV03780.1};
GN ORFNames=LAMI_0H10902G {ECO:0000313|EMBL:SCV03780.1};
OS Lachancea mirantina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1230905 {ECO:0000313|EMBL:SCV03780.1, ECO:0000313|Proteomes:UP000191024};
RN [1] {ECO:0000313|Proteomes:UP000191024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Devillers H.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT598468; SCV03780.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4KGT6; -.
DR STRING; 1230905.A0A1G4KGT6; -.
DR OrthoDB; 177966at2759; -.
DR Proteomes; UP000191024; Chromosome h.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0006751; P:glutathione catabolic process; IEA:InterPro.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017149; GSH_degradosome_Dug2.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR43270; BETA-ALA-HIS DIPEPTIDASE; 1.
DR PANTHER; PTHR43270:SF8; DI- AND TRIPEPTIDASE DUG2-RELATED; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR Pfam; PF00400; WD40; 1.
DR PIRSF; PIRSF037237; Peptidase_WD_repeats_DUG2; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000191024};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 64..97
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 383..398
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 624..765
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 874 AA; 98110 MW; DEF53E1827F6C2F0 CRC64;
MRSMQDHPSL LHRWDHSYAI LSTVAFPHKK LLFAGTHDSK ILCFNLDTYN LVQTVSLGNL
DDEQTHTRSS VLCLAKSQDE RFLFSAGADS LVRVWEVTLN TRTSCVSMKE LATIYSSVDI
GDVFSVKYLD SHQTVIFGCQ NASMLFLPNV LDKMSHSKNY SDLNCLPQLR FDKFFDSTFR
GGPGTVSRTS SSDQLACSVH SKPVILEVPA ENTIKYAHNG FIYSIQPLND HNHSLPAYFY
PSGVSRDDVD FVISCGGDGI SKLWSLTLNA DSSANVTLVT EYDNDESILC EFVKFPFLYC
GLNGGRIKIW DINTNEPIAT LQAPSKSDLM SITVYNDHIF ATHKEGITKF HEENIYHWKA
HQGLVLSAEI LRKKCTCFEH VRLVTGGNDG ALALWDINDL VDSVCENLDY QTLQVKERRE
SEDANSLGKY EDTFFGNEHM LESLRELISF QTVSALADTQ HSIHGRRCAS YLQQLLLKFG
ATTSELLCGK SGSNPIVYAV FHSKAANKNR VLWYAHYDVV AAGDPAAWES DPFALTCENG
HLKGRGVSDN KGPLLAAIYS VGWLHYRNEL NNDIVFLIEG QEESDSSGFS EILGQHIDRI
GSKIDWVLFS NSIWLDQTMP CLNYGLRGVI NAKITITSEQ PDRHSGVDGG MHREPTSDLF
RIISKLQDDE GNVQIPGFYD SLKELSESEA NHFKEILARA ALDDNIGMEN LITRWTKPSF
SITTMKVSGP GNATVIPQKA SICLSIRLVP EQDLNIIKCS LESYLLECFQ KLKTTNKMDV
KILNEAEPWL GDPHNRIYLV LSEEIKEAWG KEPLLVREGG SIPQIRYLER IFDAPAAHIP
CGQSTDNAHL ANEQLRIINW YKTRRILTNT FNKL
//
