ID C1GQ69_PARBA Unreviewed; 606 AA.
AC C1GQ69;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00011965};
DE EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN ORFNames=PAAG_00664 {ECO:0000313|EMBL:EEH37743.1};
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH37743.1, ECO:0000313|Proteomes:UP000002059};
RN [1] {ECO:0000313|EMBL:EEH37743.1, ECO:0000313|Proteomes:UP000002059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal aspartate or glutamate from a
CC peptide, with a preference for aspartate.; EC=3.4.11.21;
CC Evidence={ECO:0000256|ARBA:ARBA00001335};
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}.
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DR EMBL; KN293993; EEH37743.1; -; Genomic_DNA.
DR RefSeq; XP_002796805.1; XM_002796759.2.
DR AlphaFoldDB; C1GQ69; -.
DR STRING; 502779.C1GQ69; -.
DR GeneID; 9100255; -.
DR KEGG; pbl:PAAG_00664; -.
DR VEuPathDB; FungiDB:PAAG_00664; -.
DR eggNOG; KOG2596; Eukaryota.
DR HOGENOM; CLU_019532_2_0_1; -.
DR OMA; GPILKVN; -.
DR OrthoDB; 1156at2759; -.
DR Proteomes; UP000002059; Partially assembled 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:SF3; ASPARTYL AMINOPEPTIDASE; 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:0000313|EMBL:EEH37743.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002059};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT REGION 507..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 606 AA; 66060 MW; 065EAEDB81C408BA CRC64;
MLSKLTGESL CTARFSISSL ARESIAAHYS TTHSNPTRNI FFSLPNQSPP EHQHPLQSWH
TMTHSRKLSS FPPLSTSNFK AQANDFLSFV NASPTPFHAV ASASKRLVDA GFKEVKERDS
WSSTCKPGGK YYVTRNGSTI IAFAIGQKWK PGNSISMIGA HTDSPCLRIK PVSKKSGSGF
IQVGVETYGG GLWHTWFDRD LGIAGRVMVR NADESIEAKL IHIHRPILRI PTLAIHLERQ
ETFSFNKETQ LFPIAGLVAA ELARKDKDPK AKEYLEIRSK EKNNNGNSGN DVNDAASNAT
FYPIKPTTER HHPFLIELIA SELSTTPHEI VDFELLLYDT QKACLGGLLD EFIFSARLDN
LNMSFCAIMG LINSLAHPGA LDKESSIRLV ALFDDEEIGS RTAQGAFSNI LGATLRRLSV
LPAETSASAK APPPDLSTAY EQSLSTSFLV SADMAHSVHP NYAVKYESDH KPEMNKGPVI
KINANAFYAT NSPGIVILQE SARLAGNNHH DDQAGSTSAT SPSPETSFKG VPLQLFVVRN
DSSSGSTIGP MLSASLGVRT VDLGNPQLSM HSIREMGGSN DVGYAIRLFE SFFEHYTELA
GKILVG
//
