ID D2V3L6_NAEGR Unreviewed; 959 AA.
AC D2V3L6;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=NAEGRDRAFT_57020 {ECO:0000313|EMBL:EFC48792.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC48792.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC48792.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG738850; EFC48792.1; -; Genomic_DNA.
DR RefSeq; XP_002681536.1; XM_002681490.1.
DR AlphaFoldDB; D2V3L6; -.
DR STRING; 5762.D2V3L6; -.
DR EnsemblProtists; EFC48792; EFC48792; NAEGRDRAFT_57020.
DR GeneID; 8852511; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_57020; -.
DR eggNOG; KOG1046; Eukaryota.
DR InParanoid; D2V3L6; -.
DR OMA; ERFFLSM; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF300; 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:EFC48792.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Membrane {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:UP000006671};
KW Transmembrane {ECO:0000256|RuleBase:RU364040};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364040};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT TRANSMEM 24..48
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364040"
FT DOMAIN 75..289
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 324..531
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 619..933
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 396
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 395
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 484
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 959 AA; 109286 MW; 96FC63B756BE60D1 CRC64;
MLSSSGHHDA TRIGQENVAE KRRLTIISIV VVAILTIIVA GVTIWATYLI RGWDGVIEDD
GVKTYPYRLP DTILPRHYDI EIEALLDGAT TFNGVVSIRL EVTTETNVVE LSAEEMQFVA
IIKATEDQKK QHAKNGVLPA VDGKLAGISI KSEKTSSEVV LSGFSTAVLE KYRKIQVHTK
NNLEKGAFYI LRIEYQAPIR TDMRGFYSSK AADGSTVLST QFESEDGRAA IPLFDEPKFK
ATYQMTITTK LKDEKTRVLF NTDEIERTNL PDGRVKVKFD KTPLMSTYLI AFIIGQYDYI
EKTDGKIRHR IYTPVGKSEQ GRAALEASIK VTKFFQDLYQ VEYPINKMDH ISIPSFASGA
MENFGLITYR ETYIIFDNAT ASQLDKENGI EVVSHEISHQ FNGNIITCAF WTHLWLNEGF
ATFMETYALD KTYPDWKRGL KKLTNSVIYA ADADSVPSAD PIVRLYDKIQ SKDEIDSLFN
SITYDKGGAV LSMFFNYLGE DKFVQWIRSY FAKYKNQNAE TKQLLELLPV QNVQETATNF
GTWLHQPGMP IVQVNENADG TISLSQNRFF SYANATQVDQ FKNSTWWIPL TYVTSADGDV
KKVEMSSKVP SLKITDKVYK FNYHKTGFYR VNYSTKMWKN LIAKIEDFDT EDRFDLFNDI
FSIATSTVEN IDSSLMFEML LALKNDDTSI LWENMYQSIL KLHQLLAAES VSNSFSRMVK
DLVKNKYESI GWTNVPGADE DEENLDELRP FVLNLACRFG LTECVTEAFK RYQERNSTII
PPILRNAVYR AVVSNGGERE YYQILNQFKA EQDSVERTKL MYALAYTQQI PLLQTTLDLA
LSPHVKPQDS IFLIREVARN VPSGPNVAWN FVRTRYDAIL SKCGQDQVSN RLVYGVGSLF
TNIFERDELI QFFAPNIEKL SMKHYSNTLE AIEKNAKFLS KHLPAINTYL TEKYPPQTL
//
