ID   C1GJM4_PARBD            Unreviewed;       517 AA.
AC   C1GJM4;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Aspartyl aminopeptidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PADG_07460 {ECO:0000313|EMBL:EEH42640.1};
OS   Paracoccidioides brasiliensis (strain Pb18).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH42640.1, ECO:0000313|Proteomes:UP000001628};
RN   [1] {ECO:0000313|EMBL:EEH42640.1, ECO:0000313|Proteomes:UP000001628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pb18 {ECO:0000313|EMBL:EEH42640.1,
RC   ECO:0000313|Proteomes:UP000001628};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
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}.
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DR   EMBL; KN275967; EEH42640.1; -; Genomic_DNA.
DR   RefSeq; XP_010762858.1; XM_010764556.1.
DR   AlphaFoldDB; C1GJM4; -.
DR   STRING; 502780.C1GJM4; -.
DR   GeneID; 22585948; -.
DR   KEGG; pbn:PADG_07460; -.
DR   VEuPathDB; FungiDB:PADG_07460; -.
DR   eggNOG; KOG2596; Eukaryota.
DR   HOGENOM; CLU_019532_3_0_1; -.
DR   InParanoid; C1GJM4; -.
DR   OMA; LLDTHYY; -.
DR   OrthoDB; 1156at2759; -.
DR   Proteomes; UP000001628; 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   Reference proteome {ECO:0000313|Proteomes:UP000001628};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
FT   REGION          16..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   517 AA;  56285 MW;  4D6F0A95BBA9A454 CRC64;
     MTRQFQSNLR VSMSSLRSQL PITQAEPHYQ PQSTEETRRR EDSPPSSISP ESYAQPFCDF
     MTSNPTIFHA VASFCSQLEA HGFKALSERD VWSSTLKPGG KYFCTRNGSS LVAFTIGSDY
     KPGNGFAIVG GHADALCAKL KPVSKLQTKA GYVQLGVAPY AGSLSSTWWD RDLGIGGRVL
     VRDLDTGTIE SKLVKLDWAI ARIPSLAVHF GPQSRGPFNK ETQMVPIIAL DNSDLFENQE
     TAVKEDIEIK QGTYAATQPP RLVKVIAEQL GVSDLSTIVN WELELFDIQP AQIGGLDKEF
     IFAGRIDDKL CCYSAQEALL ASSDNMSTGV VKMVGMFDSE EIGSLLRQGA RSNFMSSIIE
     RIVETFSPSY GPNILSQTVA NSFFLSSDVT HAVNPNFLNV YMEGHSPRLN VGVAVSADPN
     GHMATDSISA AILQRVAEKC GSALQIFQIR NDGVSGGTIG PMTSARIGMR AIDAGIVQLS
     MHSIRAMTGN MDPGLGVKLF KGFFDYFEEV DHEFRGC
//