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Database: UniProt
Entry: A0A2P7YUD2_9ASCO
LinkDB: A0A2P7YUD2_9ASCO
Original site: A0A2P7YUD2_9ASCO 
ID   A0A2P7YUD2_9ASCO        Unreviewed;       403 AA.
AC   A0A2P7YUD2;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN   ORFNames=C7M61_001366 {ECO:0000313|EMBL:PSK39568.1};
OS   [Candida] pseudohaemulonii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC   Candida/Metschnikowiaceae.
OX   NCBI_TaxID=418784 {ECO:0000313|EMBL:PSK39568.1, ECO:0000313|Proteomes:UP000241107};
RN   [1] {ECO:0000313|EMBL:PSK39568.1, ECO:0000313|Proteomes:UP000241107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B12108 {ECO:0000313|EMBL:PSK39568.1,
RC   ECO:0000313|Proteomes:UP000241107};
RA   Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N.,
RA   Cuomo C.A.;
RT   "Candida pseudohaemulonii genome assembly and annotation.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. M28E subfamily.
CC       {ECO:0000256|ARBA:ARBA00043962}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PSK39568.1}.
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DR   EMBL; PYFQ01000002; PSK39568.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P7YUD2; -.
DR   STRING; 418784.A0A2P7YUD2; -.
DR   EnsemblFungi; C7M61_001366_t1; PSK39568.1; C7M61_001366.
DR   VEuPathDB; FungiDB:C7M61_001366; -.
DR   OrthoDB; 1384212at2759; -.
DR   Proteomes; UP000241107; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147:SF26; ENDOPLASMIC RETICULUM METALLOPEPTIDASE 1; 1.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU361240};
KW   Metal-binding {ECO:0000256|RuleBase:RU361240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW   Reference proteome {ECO:0000313|Proteomes:UP000241107};
KW   Zinc {ECO:0000256|RuleBase:RU361240}.
FT   DOMAIN          185..390
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   403 AA;  44702 MW;  DF639D53BDCF2B1D CRC64;
     MKLTTFVATL AAANAISFNF YDNLFHSSVP DRVLKVAEDS YIAASEADKL RLRREGKRFI
     DVTESLPVKD AVSQGMVAQS GGNGLLTWFS KNIETLKKPI PKYNYPTKAT HQDIVEPLLS
     KIDIEGVKAH LAKFSSFYTR YYKSETGLES ANWLHETIQE IVKVLPEDAV YIRKFKHNGW
     DQYSIAVSIK GKVEDKVVVG AHQDSINLLF PNLLRAPGAD DDGLGTVTTL EALRLVSGAI
     ANGDFKPYNT LEFHYYSAEE GGLLGSIDVF SNYFAENATV VGMLQQDMTG YTAGTTDAGV
     EPHFGLISDY TSVDLNEFIK VIVESYCAIP FHETECGYAC SDHASALENG YPASFLIESE
     FKYTAKQIHL TLDTMDRLDF DHIKEHVKLT VGYAVELALA KKL
//
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