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
//