ID   A0A238FQG2_9BASI        Unreviewed;       961 AA.
AC   A0A238FQG2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN   ORFNames=BQ2448_6556 {ECO:0000313|EMBL:SCV74124.1};
OS   Microbotryum intermedium.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX   NCBI_TaxID=269621 {ECO:0000313|EMBL:SCV74124.1, ECO:0000313|Proteomes:UP000198372};
RN   [1] {ECO:0000313|Proteomes:UP000198372}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jeantristanb JTB J.-T., Ricardo R.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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; FMSP01000020; SCV74124.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238FQG2; -.
DR   STRING; 269621.A0A238FQG2; -.
DR   OrthoDB; 3085317at2759; -.
DR   Proteomes; UP000198372; 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: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; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 1.
DR   Pfam; PF11838; ERAP1_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
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   Hydrolase {ECO:0000256|RuleBase:RU364040};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR634016-3,
KW   ECO:0000256|RuleBase:RU364040};
KW   Metalloprotease {ECO:0000256|RuleBase:RU364040};
KW   Protease {ECO:0000256|RuleBase:RU364040};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198372};
KW   Zinc {ECO:0000256|PIRSR:PIRSR634016-3, ECO:0000256|RuleBase:RU364040}.
FT   DOMAIN          34..210
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          323..540
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          619..937
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   ACT_SITE        395
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT   BINDING         394
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         398
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         417
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            481
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ   SEQUENCE   961 AA;  107086 MW;  A5ABAA78EADBD706 CRC64;
     MFLCHASSGF ANLDNLAAAP APDAEQVRLT DKVVPSHYEL VIKTDLENLS FSGTAEITID
     VLEDVPSLVL NVAEPLMLKH AVLSHTSLKT ESTRPASELK LHTKRERVEI TFAGGHVAAG
     QVKLGLRWEG GLDNSMQGYY RSSYPAPGGK DGDTAYYALT QFEPTRARRA YPCFDEPAFK
     ATYAIKMISR TDSVALSNCD VIDTKHLGSG GAFPRTDLLT EAFFTEAGPT AVKTEGKTEG
     KTEGKTEGTI SAPAAKLVSY GEFKDDWTLT TFSTTPKVSS YLVAFANGPF EYIEASYKSP
     LSGRTVPMRA YATKDNIHQA GLALETKVRI LPIYEKMFDI EYPLPKLDTL VASDFDAEAM
     ENWGLITGRT SAYLYDPKKS GIETRKVVIG VQSHEVAHQW FGNIVTFDWW HGLWLNESFA
     TLIGEVIMID EIEPSWKIHS SFINRHLSSA FRLDSLRSSH PIEMPCPDEE TIQQIFDAIS
     YSKGASVLKM LSNFIGQKTF IHGVSLYLKK FLYGNTITTD LWDGIAKASG KDVAKIMENW
     TKKVGFPVIT VEETSEGLKV TQNRFLSTGD PTPEEDETIW QIPLELLIVQ DGKVNVNYDL
     LLTERETVIP IKDVANITYK FNSETCGVYR TLYPQDRLAK LGEEAGKENT HFSLSDRMGL
     VGDAMALATS GYAKTSGSLT LFSKLTNEKE NLVWQAVGDS LGSISATWWD QPEDVRAAIS
     KLRRTLFGPI ADRLGFVYSD DEDVDTIELR TMAISIAAAA DDKATLAEYK RRFTLFLEKD
     DESLIPSDLR DSIYAQSVKH GGVAEYEKVL SVYNKPETPA HRTSAMMALC AATDQALLDR
     TFNMLKGDEV RTQDFMYFTG SLSSNRVAKR QMWQFLQDNY ELFARRFKGN FSIGGVIRSC
     FATLTTEEDA AAVEVWAKDI DSSAWSQSLS QGLDRMRSNA KWLERDAKDV EQWLKENQYF
     A
//