ID A0A2P7ZAC8_9PEZI Unreviewed; 875 AA.
AC A0A2P7ZAC8;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 08-NOV-2023, entry version 18.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=B9Z65_2304 {ECO:0000313|EMBL:PSK45164.1};
OS Elsinoe australis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Elsinoe.
OX NCBI_TaxID=40998 {ECO:0000313|EMBL:PSK45164.1, ECO:0000313|Proteomes:UP000243723};
RN [1] {ECO:0000313|EMBL:PSK45164.1, ECO:0000313|Proteomes:UP000243723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NL1 {ECO:0000313|EMBL:PSK45164.1,
RC ECO:0000313|Proteomes:UP000243723};
RA Cheng Q.;
RT "Draft genome sequence of Elsinoe australis.";
RL Submitted (MAY-2017) 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:PSK45164.1}.
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DR EMBL; NHZQ01000251; PSK45164.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P7ZAC8; -.
DR STRING; 40998.A0A2P7ZAC8; -.
DR Proteomes; UP000243723; 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 ECO:0000313|EMBL:PSK45164.1};
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:UP000243723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 14..213
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 262..464
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 536..850
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 320
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 405
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 875 AA; 98222 MW; 7624E1C739E4021D CRC64;
MATDRDVLPS TVKPTNYNLS LYDLELGGSW SYQGTVKIDV EVKADTKEIT LNTFRLKIQS
AEVQTDAGKT EGSIKTNNVS YDEKNQRSTL HFDQAIPQSH KAVISITFQG TMNNDMAGFY
RSKYKPAVPA AKSVPKDDQY HYMFSTQFES SDARRAFPCF DEPNLKASFE FEIEIPEDQT
ALSNMGEKEV KQSKKSGFKT VVFDKSPVMS TYLYAWAFGD FEYIEDFTRR KYNGKNLPVR
VYSTKGLINQ GKLALESAHQ IIFKIDYPLP KVDLLAVHEF SHGAMENWGL ITYRTTAVLF
DEYASDQKYK NRVVYVVAHE LAHQWFGNLV TMDWWNELWL NEGFATWVGW YAVDYLHPDW
NVWGQFVTEG MQTAFGLDSL RTSHPIEVPV RNALEVDQIF DAISYLKGSS VIRMLAAHLT
PEVFLSGVAD YLQTHKYGNA KTNDLWSALS KVSNQNVNAF MDPWIRKIGF PVVTVAEEPG
QISIKQSRFL SAGGVKADED TTTWWVPLGL KSGSTKAQTS ALTNKEDTIR EIDDNFYKLN
SDQTGFYRTN LPPQRLTSLS GHLDKLSVED KIGLIGDAAA LAISGDATTA GVLSFLEGFA
SETNYLVWSE ILSTLGNIRS VFSDDEKLSD GLRAFTLKLV SDATDKIGWT FEPKEDYLTG
QLRALLISTA GLAGHEHTVA EAQKRFKAYF DGDAKAIHPS LRLAVFKIAI KNSGKDAYLQ
VRKEYESTTS VDGKEITLAA MGRVPSAELA RDYLDWSFSG PVATQDLHTP ARALALNSAV
RIEVWNFIKK NWSTIFDKLS GNMVVLERFL RMSLTKFASN DIEKDIENFF RDKDQKGFDR
GLAVVSDTIK GLAGYRERDG GVIGEWLSAR GYGKK
//
