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Database: UniProt
Entry: G3BDM6_CANTC
LinkDB: G3BDM6_CANTC
Original site: G3BDM6_CANTC 
ID   G3BDM6_CANTC            Unreviewed;       868 AA.
AC   G3BDM6;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN   ORFNames=CANTEDRAFT_132133 {ECO:0000313|EMBL:EGV60341.1};
OS   Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS   10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX   NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN   [1] {ECO:0000313|EMBL:EGV60341.1, ECO:0000313|Proteomes:UP000000707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC   NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA   Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA   Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA   Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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DR   EMBL; GL996528; EGV60341.1; -; Genomic_DNA.
DR   RefSeq; XP_006689555.1; XM_006689492.1.
DR   AlphaFoldDB; G3BDM6; -.
DR   STRING; 590646.G3BDM6; -.
DR   GeneID; 18249593; -.
DR   KEGG; cten:CANTEDRAFT_132133; -.
DR   eggNOG; KOG2276; Eukaryota.
DR   HOGENOM; CLU_008535_0_0_1; -.
DR   OrthoDB; 177966at2759; -.
DR   Proteomes; UP000000707; Unassembled WGS sequence.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006751; P:glutathione catabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 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   PIRSF; PIRSF037237; Peptidase_WD_repeats_DUG2; 1.
DR   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000707}.
FT   DOMAIN          619..759
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   REGION          18..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   868 AA;  98200 MW;  8C0A3FF26A7F0442 CRC64;
     MDYVDTIRNS SFQSATELRE SYSPSPFPSS SIPPSGSIKP SCLQDTMNSE SLPLEPPHLT
     HLWNSDDSII SSIIAPLRKR LICGTQNGKI LIYSLEDYTH LETLSEPEMT GSNLCLSLTE
     DEKYLFTAGS DSLIKIYDLS SERIQCIKII YSSIDIGDIF SIYYCEFLKH LFIGCQNASI
     VWCKVDFSNV DYAIAIDRNN LPHLRYNKFF DSTGPGGKVS TQAKEINFLK EISLCEVETI
     NSVSFAHFGY IYNLRVFTNE FLLSNFPQYS KILISGGGDG LINIWGIQCD PQTEKLTLSK
     VESLHNEESI LSMHINQTYL YAGLSSGVIN VWDLLTFQMI KSFSTPNNEQ VNALVTMGQM
     IIYGNKLGLN LIYNRRVYKL NSDPILTLYS YEYRPDDQIA LVAGGKKVVT LYNMVGSSER
     ETIKTFKGVL NNDMLVKNLK KFISYKTISK YPELCMDDSR NCTKFLIKLF DSFGAKSTHL
     IPIDNGNPII ISTFKNTSNS KNAKRLLYYG HYDVVEAEER NNWSVNPFEL TNKNGYLYGR
     GSSDNKGPTL AIIHAIAELF ESNELDVDFT FVIEGEEENG SKQFKETVLE NLDLIGDIDW
     ILLSNSYWLD DERPCLNYGL RGVINCSIQV ESDHPDRHSG VHGGVCKEPT MDLVQVLNTL
     SDPVTNEILI PNFYDNINES SPKELEFFDK IVSYNPKFRL DELIAQWTKP SFTIHKIEVS
     GPNNDTIIPK TATASVSMRI VPNQEVNQIK DSLINFLTDN FTKLNSTNKI DISISHEVEP
     WLGDVENTFY KVLYANLQKN WEIEPLLIRE GGSIPSIRFL EKTLNAPACQ IPCGQSSDNA
     HLQDEKLRFL NLVKLKDVVK DSIHDLSK
//
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