ID   A0A074XEK2_9PEZI        Unreviewed;       522 AA.
AC   A0A074XEK2;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN   ORFNames=M436DRAFT_47267 {ECO:0000313|EMBL:KEQ73041.1};
OS   Aureobasidium namibiae CBS 147.97.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ73041.1, ECO:0000313|Proteomes:UP000027730};
RN   [1] {ECO:0000313|EMBL:KEQ73041.1, ECO:0000313|Proteomes:UP000027730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ73041.1,
RC   ECO:0000313|Proteomes:UP000027730};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M28 family.
CC       {ECO:0000256|RuleBase:RU361240}.
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DR   EMBL; KL584710; KEQ73041.1; -; Genomic_DNA.
DR   RefSeq; XP_013427011.1; XM_013571557.1.
DR   AlphaFoldDB; A0A074XEK2; -.
DR   STRING; 1043004.A0A074XEK2; -.
DR   GeneID; 25410683; -.
DR   HOGENOM; CLU_024336_0_1_1; -.
DR   OrthoDB; 51543at2759; -.
DR   Proteomes; UP000027730; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
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   CDD; cd02130; PA_ScAPY_like; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147:SF17; AMINOPEPTIDASE Y; 1.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF52025; PA domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW   Hydrolase {ECO:0000256|RuleBase:RU361240};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027730};
KW   Signal {ECO:0000256|RuleBase:RU361240};
KW   Zinc {ECO:0000256|RuleBase:RU361240}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT   CHAIN           20..522
FT                   /note="Peptide hydrolase"
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT                   /id="PRO_5005104460"
FT   DOMAIN          158..239
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          269..479
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   522 AA;  55545 MW;  0B609E2EC2F20CE7 CRC64;
     MAILRTCTAL ACVAVAASAR QLPLVADDSY NPAPSSPIVV SNGTSNGTVI DTKKLQADID
     INKLVARAEA LSKIADLSLS EYNHPTRVIG SQGHLGTVDY IYSELSKLGD YYNVTNQTFP
     AVSGNVFESR LVVGYEVPKS ASPMSLTPPT KQHEPVYGKL LLVPNGGCSA SDFSRNMTGH
     IALIKRGTCS FGDKSANAGK AGADAAIIYN NDNSTLSGTL GSPSPYHIAT FGVSAAEAAP
     WVAALQNGTT GLDAIAYIDS TVDEIMTTNV IAQTTAGDPE NCVMLGGHSD SVAAGPGIND
     DGSGTISLLE IATQLTKYEV NNCVRFGWWA GEEEGLLGST YYAEQLSAAE NQKIRLFMDY
     DASPLIPNGV FQIYNSTNGQ NPAGSGELRV LYEDWYKEQG LNYTYIVFDG RSDYVGFLDA
     GIPSGGIATG AEGIKTKEEA SIFGGEAGSQ YDPCYHELCD DIHNLDLTEW EANTKLIAHS
     VATYAKSFDG FPKRVAAVEE RSLSGSKKST PQFKYRGNEL IM
//