ID A0A329S3L3_9STRA Unreviewed; 902 AA.
AC A0A329S3L3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=PC110_g12106 {ECO:0000313|EMBL:RAW31544.1}, PC113_g4651
GN {ECO:0000313|EMBL:KAG2864342.1}, PC115_g12457
GN {ECO:0000313|EMBL:KAG2911806.1}, PC117_g6396
GN {ECO:0000313|EMBL:KAG2947948.1}, PC118_g13854
GN {ECO:0000313|EMBL:KAG2975540.1};
OS Phytophthora cactorum.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=29920 {ECO:0000313|EMBL:RAW31544.1, ECO:0000313|Proteomes:UP000251314};
RN [1] {ECO:0000313|EMBL:RAW31544.1, ECO:0000313|Proteomes:UP000251314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10300 {ECO:0000313|EMBL:RAW31544.1,
RC ECO:0000313|Proteomes:UP000251314};
RA Armitage A.D., Lysoe E., Nellist C.F., Harrison R.J., Brurberg M.B.;
RT "Draft genome of the strawberry crown rot pathogen Phytophthora cactorum.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAG2864342.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=15-7 {ECO:0000313|EMBL:KAG2864342.1}, 4032
RC {ECO:0000313|EMBL:KAG2911806.1}, 4040 {ECO:0000313|EMBL:KAG2947948.1},
RC and P415 {ECO:0000313|EMBL:KAG2975540.1};
RA Armitage A.D., Nellist C.F., Bates H., Vickerstaff R.J., Harrison R.J.;
RT "Effector identification in a new, highly contiguous assembly of the
RT strawberry crown rot pathogen Phytophthora cactorum.";
RL Submitted (OCT-2018) 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:RAW31544.1}.
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DR EMBL; RCMG01000082; KAG2864342.1; -; Genomic_DNA.
DR EMBL; RCMI01000416; KAG2911806.1; -; Genomic_DNA.
DR EMBL; RCMK01000121; KAG2947948.1; -; Genomic_DNA.
DR EMBL; RCML01000489; KAG2975540.1; -; Genomic_DNA.
DR EMBL; MJFZ01000317; RAW31544.1; -; Genomic_DNA.
DR STRING; 29920.A0A329S3L3; -.
DR Proteomes; UP000251314; Unassembled WGS sequence.
DR Proteomes; UP000697107; Unassembled WGS sequence.
DR Proteomes; UP000735874; Unassembled WGS sequence.
DR Proteomes; UP000736787; Unassembled WGS sequence.
DR Proteomes; UP000774804; 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:UP000251314};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 17..218
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 253..470
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 566..880
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 411
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 902 AA; 101949 MW; BF539BA8340BA745 CRC64;
MPAEPEVFKR LPTCVVPEKY HVDYELIDLL NFRFEGSERV LLRVDQATSV ITCHAVELFV
YDVSVEDSAA GKTQQAQQIT YQTKDDSVSF HFAEPLKPGS KVTLKLQFHG FLNDQLRGFY
RTEYEHQGEK RVLAVTQFEA CDARRAFVCW DEPALKATFE ISMVTETDLV ALSNAHVVET
LVRPKKNAHI RKNTRSEVSG SMEKVWKFAE SPVMSTYLVA MVVGEFDMIS DLTKEGVVVN
VYTAPGQSAR GRFALDVATK ALSFFTESFD IPYPLKKLDM VAIPDFLGAM ENWGLVTYTE
TFLLVDQKLS SHEIKADAAR AICHELSHQW FGNLVTMNWW TGLWLNEGFA QFMEFDAAHD
IFPEWKLWET FVQDIMLGSA FVKDAMVSSH PIEVVVNHPD EADEIFDAIS YHKGSSMVRM
LSEYLGRDVF YRGVHDYLVK FSYKNTVTED LWEALEKESG QKLKDMADTW TKQVGFPLLT
VKQDADGKCV LVQERFFADT SLNAEDNTLW DVPLTFCTSE DPSAIKRLGI WDAKTASKDS
TVPTTPFEAG DEINKQIQVP AGPKGWIKLN PNQAGFYLVN YSPALWKCLE IPVKEQLLGV
PDRVSLLNSV FTFARAGVLD LPVALDFTNA YVDESASLCW KEISRNLGYY SNLFRDEPFY
PEFQRYIRTL FAQVMKRLGW DADASKQADA DEGEFRKTVI YRLGLANDQD IIKEAKKRFH
EYIAGDASAL SGDLRGSVFD IEMTYGEAAN AKLLQELYNK SDFAEERNDC LGAMGSVSGT
AAKLQVLDWA VENVRSQDIH SPFISVASDK LGAQVAWQYV QDKWDVLAKK YSAMTLGYIV
CGVVSRFQSE AMAVEVEAFM VSKETSGYKR RLEVALEGVR LKSAAYCRDC ETLAKWLKER
AV
//
