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
//