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Database: UniProt
Entry: C5M2D0_CANTT
LinkDB: C5M2D0_CANTT
Original site: C5M2D0_CANTT 
ID   C5M2D0_CANTT            Unreviewed;       323 AA.
AC   C5M2D0;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CTRG_00219 {ECO:0000313|EMBL:EER35480.1};
OS   Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294747 {ECO:0000313|EMBL:EER35480.1, ECO:0000313|Proteomes:UP000002037};
RN   [1] {ECO:0000313|EMBL:EER35480.1, ECO:0000313|Proteomes:UP000002037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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DR   EMBL; GG692395; EER35480.1; -; Genomic_DNA.
DR   RefSeq; XP_002545438.1; XM_002545392.1.
DR   AlphaFoldDB; C5M2D0; -.
DR   STRING; 294747.C5M2D0; -.
DR   MEROPS; M20.002; -.
DR   EnsemblFungi; CTRG_00219-t43_1; CTRG_00219-t43_1-p1; CTRG_00219.
DR   GeneID; 8301876; -.
DR   KEGG; ctp:CTRG_00219; -.
DR   VEuPathDB; FungiDB:CTRG_00219; -.
DR   eggNOG; KOG2275; Eukaryota.
DR   HOGENOM; CLU_021802_11_0_1; -.
DR   OrthoDB; 3672990at2759; -.
DR   Proteomes; UP000002037; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR047177; Pept_M20A.
DR   InterPro; IPR002933; Peptidase_M20.
DR   PANTHER; PTHR45962; N-FATTY-ACYL-AMINO ACID SYNTHASE/HYDROLASE PM20D1; 1.
DR   PANTHER; PTHR45962:SF1; N-FATTY-ACYL-AMINO ACID SYNTHASE_HYDROLASE PM20D1; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002037};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   323 AA;  37122 MW;  EF7FD93BCAA44B3B CRC64;
     MTSEKELPLH VGRDKRTIRR AHHFGVISLI LIVLLFVTFS YNDNVKSLMD APHEPDSLCP
     IIPKINPSKY LTNPETLQYI LHNKKYHKQI RKRLSNAVKI PTEIYDDMIN PSNIESLEEL
     YKLDPRWEQF EKFQKFLKKT YPLIHKHLKL KKINKFGLIY TWKGSDETKK PIMLAAHQDV
     VPVSLETESQ WKYPPFGGEF DGEFIYGRGV SDCKNLLMAL MNTIELLLKE GDLKPKRTII
     LSFGYDEEAS GNGAKEISEY LLNKYGENSI FQIIDEGDNE GITEIEGIKF ILPSIGEKGH
     LNSIIELFTK GGHSSIPPKT YIN
//
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