ID   A0A0G2IE94_9EURO        Unreviewed;       516 AA.
AC   A0A0G2IE94;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   13-SEP-2023, entry version 23.
DE   RecName: Full=Aspartyl aminopeptidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=EMCG_00079 {ECO:0000313|EMBL:KKZ68908.1};
OS   Emmonsia crescens UAMH 3008.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX   NCBI_TaxID=1247875 {ECO:0000313|EMBL:KKZ68908.1, ECO:0000313|Proteomes:UP000034164};
RN   [1] {ECO:0000313|Proteomes:UP000034164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 3008 {ECO:0000313|Proteomes:UP000034164};
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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:KKZ68908.1}.
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DR   EMBL; LCZI01000001; KKZ68908.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2IE94; -.
DR   VEuPathDB; FungiDB:EMCG_00079; -.
DR   Proteomes; UP000034164; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05658; M18_DAP; 1.
DR   Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR28570:SF4; VACUOLAR AMINOPEPTIDASE 1; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000256|RuleBase:RU004386};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   516 AA;  55730 MW;  567662D0EED32FE0 CRC64;
     MTRQFQPSLR ASTSSLRSQA TAQLPHQPQP QFQQQANKYA GPKPSPTSPE SYAQPFCDFM
     TSNPTIFHAV ASFCSQLDDH GFIRLSERDV WSSTLKRGGK YYCSRNGSSL IAFTIGSDYE
     SGNGFGIVAG HVDALCAKLK PVSKLSNKAG FVQLGVAPYA GSLGSTWWDR DLGIGGRVLV
     RDAETGAVES KLVKLDWPIA RIPTLAVHFG TPSQGPFNKE TQAVPIIGVD NSDLFGNQEG
     DVQVDDEIKQ GTFAATQPPR LIKAIAKQLG VSDLSTIVNW ELELFDTQAA QVGGLDKEFI
     FAGRIDDKLC CYSAQEALLA SPDSASTGII KMVGMFDGEE IGSLMRQGAR SNYMSSVIER
     ITEAFAPSYG PNVLSQTVAN SFLLSSDVIH AVNPNFLNVY LENHAPRLNI GVAISADPNG
     HMTTDSVSTA IIQRVADKCG STLQVFQIRN DSRSGGTIGP MTSARIGMRA VDAGIPQLSM
     HSIRATTGNL DPGLGVKLFK GFFDHFEEVD REFQDF
//