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Database: UniProt
Entry: S3D928_GLAL2
LinkDB: S3D928_GLAL2
Original site: S3D928_GLAL2 
ID   S3D928_GLAL2            Unreviewed;       880 AA.
AC   S3D928;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN   ORFNames=GLAREA_10672 {ECO:0000313|EMBL:EPE34977.1};
OS   Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE34977.1, ECO:0000313|Proteomes:UP000016922};
RN   [1] {ECO:0000313|EMBL:EPE34977.1, ECO:0000313|Proteomes:UP000016922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX   PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA   Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA   Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT   "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT   the fungus Glarea lozoyensis.";
RL   BMC Genomics 14:339-339(2013).
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; KE145355; EPE34977.1; -; Genomic_DNA.
DR   RefSeq; XP_008077964.1; XM_008079773.1.
DR   AlphaFoldDB; S3D928; -.
DR   STRING; 1116229.S3D928; -.
DR   MEROPS; M01.007; -.
DR   GeneID; 19469718; -.
DR   KEGG; glz:GLAREA_10672; -.
DR   eggNOG; KOG1046; Eukaryota.
DR   HOGENOM; CLU_003705_0_1_1; -.
DR   OrthoDB; 3085317at2759; -.
DR   Proteomes; UP000016922; 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; 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   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:UP000016922};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT   DOMAIN          30..212
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          252..469
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          543..856
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   ACT_SITE        325
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT   BINDING         324
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         328
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         347
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            410
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ   SEQUENCE   880 AA;  98470 MW;  2D5D54692EE01CE3 CRC64;
     MPPSDVADRE ILPDNIKAIN YDISIHDLEM GGAFGYQGTV NILSKIVKPS KDITLNTHEI
     KIHSAELLSG DKSFKSTGTS YDSAKQRATL AFADEIPVAE NANLVIKFQG TINNDMAGFY
     RSKYKPTVAP APSVAKDGED HVMFSTQFES CDARRAFPCF DEPNLKATFD FEIELPDDQV
     ALSNMPEKGT RKSKDGFKVV SFDRTPVMST YLLTWAVGDF EYIEDFTKRK YKGKHLPVRV
     YTTRGLKSQA QYALDHAPQI IDYFSEIFDI EYPLPKSDLL AVHEFSHGAM EGWGLVTYRT
     TAVLFDEKTS DSKYKNRIAY VVAHELAHQW FGNLVTMDWW SELWLNEGFA TWVGWLATDK
     IHPEWNVWSQ FVSEGMQTAF TLDSLRSSHP IEVPVRDGLD VDQVFDAISY LKGSSTIRML
     ATHLGQETFL KGVSNYLKAH AYGNATTNDL WSALSEASGQ DINSLIDPWV RKIGFPVLTV
     AEEPGQIGIK QSRYLSTGDV KPDEDTTTWW VPLGLQGKTG TKGTTSIALT QKEDTIRDID
     DTFYKINKDN AGFYRVNYPP ARLAKLGSQI DQLSTMDKIG LVGDAGALAL SGQATTSGLL
     AFAEGLQSET DYLVWSQILD SLGTVKSIFS DNQEIHAGLQ KFTLKLITPA VERIGIEQKP
     DDDFLTTRLR SLLVISAGLN GHEKIISEAK KRFELYTSGS DKSAINSNLR AAIFGIAMRL
     GDAPEYHALK KEWQTTLSVD GKEIALRAMG RLQSLDLLPD YLDFVFEEVA TQDKHTAGMA
     LAANPKTRAA FWQYIQDNFQ AIYDSLSKNM VVLDRFLKTS LSKFDSREME QEIAKFFEGK
     DNRGYDRTLG VIKDTILTRA AYKERDAEVV LEWLKANGYA
//
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