ID A0A162PN15_9PEZI Unreviewed; 960 AA.
AC A0A162PN15;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
DE Flags: Fragment;
GN ORFNames=CI238_03839 {ECO:0000313|EMBL:KZL87360.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL87360.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL87360.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL87360.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) 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:KZL87360.1}.
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DR EMBL; LFIW01000256; KZL87360.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162PN15; -.
DR STRING; 1573173.A0A162PN15; -.
DR Proteomes; UP000076584; 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:UP000076584};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 113..301
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 336..553
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 625..942
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 409
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 408
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 412
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 494
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KZL87360.1"
SQ SEQUENCE 960 AA; 107958 MW; DFA095028AA2590D CRC64;
LTAFVPLRLW PPPPPSMAFR FVTKRTVDQT SRIIHHTRRP VARIPYQLRN YNAFATQTSA
PRATPPRRSV RLQNPQRIAA TRHCSFKRNM CKHGEAGGGT LNYPRELLPT NVVPRHYDLT
LEPNFETLKF DGLVKIDFDV AEDSNTVSLN THEIEIKHAS LSLSADGQQK SLSDPVITYD
EPKQVHSFEF KDKLTKGEKG TLEIKFVGEL NDKMAGFYRS YYNKPDGTKG IMATSQMEPT
DARRAFPCFD EPALKAEFTV TLIADKALTC LSNMDVAEEK ELPSGKKVVR FNKSPVMSTY
LVAFIVGELN YIETNDFRVP IRVYAPPSED IERGRYALDI GVKALEFYEK AFGLPYPLPK
LDQVAIPDFA AGAMENWGLV TYRTVEVLFD DKTSGAAAKE RVSTVITHEI AHQWFGNIVS
PDWWHALWLN EGFAEFASRY SMNAFFPEWK LKESFVREDL QAALGLDGLR SSHPIEVPVH
KAEEINEIFD SISYAKGSCV VHMISAYLGE EVFMEGVRKY LKRHAWGNAT TNDLWQALSE
ASGKDVGSIM NIWTQNVGYP VVSVTESGKS ISVEQHRFLT TGDVKPEEDK VLYPISLNVR
TKGGINKDLM LTTRDAKFEI DDAEFFKINA DSTGFYRTKY AIDRLEKLGN AAELLSVQDR
VGIVADTSAL ATSGYQKTSS SLSLFKALSN AGEAEYLVWD QILTRLGSIK MAWIEDDAIV
EKLTEFQRNI VSGIAHKLGW EFSSNDGHVE QQYKALTFSA AGMSGDEKVV AAAKEMFDKF
VAGDKTAIHP NIRSSVFSIV LKFGGEKEYD AVLNYYKIAE TADERNSALR TLGQARDPKL
RQRTLDLLLN GEVRDQDIYI PIGSLRSSKG GIEALFDWLQ TRWDDIYTKF PAQSSMIGSI
VSYCTSGLTK QEQLDQLEKF FAEKEKKGFV RALSQSTDSI KAKIAWTSRD TEDLRKWLGL
//
