ID A0A2H1A7B3_CANAR Unreviewed; 568 AA.
AC A0A2H1A7B3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN ORFNames=B9J08_000216 {ECO:0000313|EMBL:PIS58765.1}, CA7LBN_001887
GN {ECO:0000313|EMBL:QWW23086.1};
OS Candida auris (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=498019 {ECO:0000313|EMBL:PIS58765.1, ECO:0000313|Proteomes:UP000230249};
RN [1] {ECO:0000313|EMBL:PIS58765.1, ECO:0000313|Proteomes:UP000230249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B8441 {ECO:0000313|EMBL:PIS58765.1,
RC ECO:0000313|Proteomes:UP000230249};
RX PubMed=27988485; DOI=.1093/cid/ciw691;
RA Lockhart S.R., Etienne K.A., Vallabhaneni S., Farooqi J., Chowdhary A.,
RA Govender N.P., Colombo A.L., Calvo B., Cuomo C.A., Desjardins C.A.,
RA Berkow E.L., Castanheira M., Magobo R.E., Jabeen K., Asghar R.J.,
RA Meis J.F., Jackson B., Chiller T., Litvintseva A.P.;
RT "Simultaneous emergence of multidrug-resistant Candida auris on 3
RT continents confirmed by whole-genome sequencing and epidemiological
RT analyses.";
RL Clin. Infect. Dis. 64:134-140(2017).
RN [2] {ECO:0000313|EMBL:PIS58765.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B8441 {ECO:0000313|EMBL:PIS58765.1};
RA Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N.,
RA Cuomo C.A.;
RT "Candida auris genome assembly and annotation.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QWW23086.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CA7LBN {ECO:0000313|EMBL:QWW23086.1};
RA Finianos M.;
RT "Candida auris outbreak in lebanese hospital.";
RL Submitted (JUN-2021) 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; PEKT02000001; PIS58765.1; -; Genomic_DNA.
DR EMBL; CP076750; QWW23086.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H1A7B3; -.
DR STRING; 498019.A0A2H1A7B3; -.
DR EnsemblFungi; B9J08_000216-t37_1; B9J08_000216-t37_1-p1; B9J08_000216.
DR VEuPathDB; FungiDB:B9J08_000216; -.
DR VEuPathDB; FungiDB:CJI96_0000943; -.
DR VEuPathDB; FungiDB:CJI97_000218; -.
DR VEuPathDB; FungiDB:CJJ07_001148; -.
DR VEuPathDB; FungiDB:CJJ09_002189; -.
DR VEuPathDB; FungiDB:QG37_02579; -.
DR OMA; IYRFQPG; -.
DR Proteomes; UP000230249; Unassembled WGS sequence.
DR Proteomes; UP000825438; Chromosome II.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05674; M20_yscS; 1.
DR Gene3D; 1.10.150.900; -; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR017141; Pept_M20_carboxypep.
DR InterPro; IPR047177; Pept_M20A.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
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; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037217; Carboxypeptidase_S; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 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 ECO:0000256|PIRSR:PIRSR037217-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000230249};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR037217-2}.
FT TRANSMEM 15..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 277..435
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 161
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-1"
FT ACT_SITE 228
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-1"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 541
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
SQ SEQUENCE 568 AA; 63636 MW; B46813E885FFE03C CRC64;
MIGLPDESSK KSKKYGAVSI AAIVVVIVFF STNLFAWSKI LLLGQDTDIC PIVKIERPES
FYKDNSTVTN ILQGDEFRKV SAEKLSKAVQ VDTQIYDDPP EVDSNPEYWA KFKKFHKYLE
KTFPTVYEHL EVNTVNTYGL VFYWKGSNSK LKPLMLTAHQ DVVPVQEETL GDWSHPPFEG
YFDGKTMFGR GVSDCKNVLV SIMETLEILI KQDFKPERGI IAAFGMDEEV SGWHGASHIA
GYLEERFGKD GIYAIIDEGA GLTKDPFTGN IIAMPGTGEK GYVDVEISLT TPGGHSSVPP
DHTSIGILSE LAYVIEQEQY EPVLTELNPT LHMLQCQAAH DHRKKIPGIL RKSILRAGYD
KVANSFVLKQ LSKIPSLRYL MQTSQALDII SGGEKNNALP ENAKLLVNHR VAIEKNVDSV
KEAITKKVLA VAKKHDVGLN AFGKKLLEPT AKGNFDVHVS GKSTETAPVT PIGDELWGYV
AGVTRHIFED YVFTNLTDPV VVAPAIMTGN TDTRHYWNLT DHIYRYSPMF MLDFLKDTNV
HSVDEHIEFD NHLRLLAFFY EFIQVVQQ
//
