ID C1HE11_PARBA Unreviewed; 887 AA.
AC C1HE11;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 2.
DT 08-NOV-2023, entry version 65.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=PAAG_09004 {ECO:0000313|EMBL:EEH40551.2};
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:EEH40551.2, ECO:0000313|Proteomes:UP000002059};
RN [1] {ECO:0000313|EMBL:EEH40551.2, 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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR EMBL; KN294051; EEH40551.2; -; Genomic_DNA.
DR RefSeq; XP_015701743.1; XM_015846701.1.
DR AlphaFoldDB; C1HE11; -.
DR STRING; 502779.C1HE11; -.
DR MEROPS; M01.006; -.
DR GeneID; 9092298; -.
DR KEGG; pbl:PAAG_09004; -.
DR VEuPathDB; FungiDB:PAAG_09004; -.
DR eggNOG; KOG1046; Eukaryota.
DR HOGENOM; CLU_003705_0_2_1; -.
DR OMA; NVWSQFV; -.
DR OrthoDB; 3085317at2759; -.
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:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF171; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|RuleBase:RU364040,
KW ECO:0000313|EMBL:EEH40551.2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000002059};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 14..211
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 251..468
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 546..863
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 324
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 409
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 887 AA; 99208 MW; 90C0667B38DF3222 CRC64;
MNPTDRDTLP DAAKPTHYDL SLFNLKLGSS WAYNGKVKID MKISRPTSEI VLNAKELTVD
SAEVSFADGK PPIKSTNISY DKTSERAILK FPSNIQPGPC VLIVDFTGTM NNHMAGFYRS
KYKPIGTPSV GTPKDDQNYY MLSTQFEACD ARQAFPCFDE PNLKATFDFE IETPKDLVAL
SNMPVKEMRQ GSLEDLQFVK FQRTPVMSTY LLAWAVGDFE YVEALTKRKY NGASIPVRVY
TTRGLKEQAR FALDYAHRTI DYFSEIFQID YPLPKSDLLA VHEFAMGAME NWGLVTYRTT
AVLFEEGKSD AKYKNRVAYV IAHELAHQWF GNLVTMDWWN ELWLNEGFAT WVGWLAIDHF
HPEREIWSQF VAEGLQSAFQ LDSLRASHPI EVPVKNALEV DQIFDHISYL KGSSVIRMLS
SQLGQETFLR GVSDYLKAHS YGNATTNDLW SALSKASNQD VAAFMDPWIR KIGFPLVTVK
ELPDQLSISQ KRFLTSGDAK PEEDETVWWI PLGVKTDATT STAVQEHKGL TTRSRSIKGI
GSDQSFYKLN KDQCGFYRTN YPAERLAKLG KSQDQLSTED KIGLIGDAAA LAVAGEGTTA
ALLAFIEGFR GEENYLVWSQ IASTLSNLRS IFATNEEAAA GLKNFVRKLV TPAVEKIGWV
FKDGEDYLTG QLRVLLISMA GNSGHEATLS EARRRFNTWS TNSDQNTIHP SLRSAVYGLA
IAEGGKPEYD TVMTEYLRTD SIDGKEICLL SLGRTRIPEL IDSYAQFLVF SGKVAVQDMH
TGALAMAANP KARIRFWEFV KGNWDGVEKR LGSNKVVFER FLRMGLGKFA EGRVAGEIRG
FFFEGGMDLG GIERGLGVVL DTIGTNAGYR EREEAAVVGW LREGGYL
//
