ID A0A179H557_PURLI Unreviewed; 888 AA.
AC A0A179H557;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=VFPFJ_07561 {ECO:0000313|EMBL:OAQ85172.1};
OS Purpureocillium lilacinum (Paecilomyces lilacinus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Purpureocillium.
OX NCBI_TaxID=33203 {ECO:0000313|EMBL:OAQ85172.1, ECO:0000313|Proteomes:UP000078340};
RN [1] {ECO:0000313|EMBL:OAQ85172.1, ECO:0000313|Proteomes:UP000078340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLFJ-1 {ECO:0000313|EMBL:OAQ85172.1};
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yin W., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins and their inhibition on
RT Phytophthora in bio-control Purpureocillium lilacinum.";
RL Submitted (FEB-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}.
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:OAQ85172.1}.
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DR EMBL; LSBI01000007; OAQ85172.1; -; Genomic_DNA.
DR RefSeq; XP_018176029.1; XM_018324635.1.
DR AlphaFoldDB; A0A179H557; -.
DR STRING; 33203.A0A179H557; -.
DR GeneID; 28889684; -.
DR KEGG; plj:VFPFJ_07561; -.
DR OMA; MMEYVAI; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000078340; 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; 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 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:UP000078340};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 33..222
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 257..474
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 548..865
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 330
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 415
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 888 AA; 98318 MW; E070AD831E588E2B CRC64;
MCKLHADADV AGGGGAAPGS THGRELLPAN VIPRHYDLTL EPNFEKLTYE GTVVIDVDVV
EDSSSIAVNT LELDIHSAKV SAGGQTVSSS PKVSYNEDTQ TSTFGFDGSL AKGTKAQLEI
TFTGQLNDKM AGFYRSTYKR DDGSEGILAT TQMEATDARR AFPCFDEPSL KAKFTVTLIA
DKALTCLSNM DVASESEVQS KISGGAKKAV RFNTSPLMST YLLAFIVGEL NYVESLDFRV
PVRVYAPPGQ DIEHGRFALD LAVRTLKFYE KVFGIDFPLP KMDQVAIPDF AAGAMENWGL
ITYRVVDLLL DEKTSGAATK ERLAEVVQHE LAHQWFGNLV TMDWWEGLWL NEGFATWASW
YSSNAFFPEW KVWETYVTDN LQSALGLDSL RSSHPIEVPV KRADEINQIF DAISYSKGSC
ILRMISTHIG EDTFLEGVRQ YLKKHAYGNT QTGDLWDALS AASGQPIHDI MSTWTKNVGY
PVIAVTEKDE PGTIHVKQNR FLRTGDVKPE EDKVLYPVFL SVRTKDGVDK SLALNEREKD
FKLSDGDFFK VNANHTGIYR TSYTPDRLEK LGKAAKDGLL TVEDRAGMIA DAGALAASGY
QKTSGVLSLL KGFDSESEFV VWNEIISRLG AVDSAWIFED PAVKNGLEAF LRDLVAPKAH
QLGWQFSDSD GHVEQQFKAM MFGSAGLAGD KKIVAAAKEM FAKFVGGDKS AVHPNIRRSV
MAIALKYGGK EEYEHVLNYY RSSTSSDERN TCLRVLGRAK DPELIKRTLG LLFGSEVKDQ
DVYMPVSGLR THAEGIEALF AYMEENWELV YKRLPPGLTM LGSMVMIFTS GFTKKEQLAK
VDKFFEGKNT NGFNQSLEQS KDAVRSKISW LERDREDVAA WLKANGYA
//
