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Database: UniProt
Entry: A0A420HWX5_9PEZI
LinkDB: A0A420HWX5_9PEZI
Original site: A0A420HWX5_9PEZI 
ID   A0A420HWX5_9PEZI        Unreviewed;       974 AA.
AC   A0A420HWX5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN   ORFNames=OnM2_037029 {ECO:0000313|EMBL:RKF61968.1};
OS   Erysiphe neolycopersici.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Erysiphales; Erysiphaceae; Erysiphe.
OX   NCBI_TaxID=212602 {ECO:0000313|EMBL:RKF61968.1, ECO:0000313|Proteomes:UP000286134};
RN   [1] {ECO:0000313|EMBL:RKF61968.1, ECO:0000313|Proteomes:UP000286134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMSG2 {ECO:0000313|EMBL:RKF61968.1};
RX   PubMed=30253736; DOI=10.1186/s12864-018-5069-z;
RA   Wu Y., Ma X., Pan Z., Kale S.D., Song Y., King H., Zhang Q., Presley C.,
RA   Deng X., Wei C.I., Xiao S.;
RT   "Comparative genome analyses reveal sequence features reflecting distinct
RT   modes of host-adaptation between dicot and monocot powdery mildew.";
RL   BMC Genomics 19:705-705(2018).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RKF61968.1}.
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DR   EMBL; MCFK01003720; RKF61968.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A420HWX5; -.
DR   STRING; 212602.A0A420HWX5; -.
DR   Proteomes; UP000286134; 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:SF174; ALANINE/ARGININE AMINOPEPTIDASE-RELATED; 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|ARBA:ARBA00022438,
KW   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:UP000286134};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT   DOMAIN          117..306
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          341..558
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          632..949
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   ACT_SITE        414
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT   BINDING         413
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   BINDING         436
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            499
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ   SEQUENCE   974 AA;  110336 MW;  22B4A6609561EE4C CRC64;
     MPIIGHSLDI ASPFITSRSP LINFSKLVAQ KRAFNSISRY FLPANQHLYR QRNLPNSLSL
     HNYNYNQQRK KLSNSPAARY CSYRRNAMCK LDKETNTVGS SIEVSSKREI LPTNVIPRHY
     DITLEPNFED FTYNGFIIIE LDVVEDSTSI SLNTLELEIQ NTKIFSGSDL ICSSPVISYD
     ESSQISKFSF ENPLPKGITA QLQIKFKGQL NDKMAGFYRS TYKNADGTQG VLATTQMEAT
     DARRAFPCFD EPALKAEFTI TLIADKNLTC LSNMDVSSQK DVKSDISDTV KKAVKFNKSP
     LMSTYLVAFI VGELNYIETD QFRVPVRVYA PPNQDIEHGR FSLDLAARTL EFYEKKFDSK
     FPLPKMDMVA IPDFAAGAME NWGLITYRVV DLIFDEKTSG AAVKERVAEV VQHELAHQWF
     GNLVTMDFWD GLWLNEGFAT WMSWYSCNIF YPEWKVWESY VTDNLQSALA LDSLRSSHPI
     EVPVKRADEV NQIFDAISYS KGSCVLRMIS KHLGEDVFMK GIRLYLKKHA YGNTQTGDLW
     AALSEASGEE VGKIMDIWTK NVGYPIITVT ENEKEKKINV KQNRFLRTND VKPEEDNVLY
     PVFLGLRSKN GVNDSLVLSK REQDFEVPDF DFFKINADHS GIYRTSYSSQ RLKKLGEAAK
     EGLLTVEDRA GMIADAAAVA ASGYGKTSDV LDLLKEFSHE KEFVVLSEIL SRLSTIQSTW
     IFEDQQVKDG LIKFQRDLVS EKAHKAGWEF KESDGHIEQQ KKSILFSSAG FSGDAVVIAA
     AREMFAKFAQ GDVSAIHPNI RGSVFGIVLK YGGKEEYDTI LKTYKNSKNS DERNTALRSL
     GRARDPELIK RTLSLPFSSE VKEQDIYLPI SALRSHPAGI QALYTWMTEN WEELIRRIPP
     GLSMLGSVVS MCTSAFNSEA DLERIEQFFS TKSTKGFDQS LAQSLDSIRS KDSWIKRDRQ
     DVKEWVIKYT ENAN
//
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