ID D2W090_NAEGR Unreviewed; 746 AA.
AC D2W090;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Acylamino-acid-releasing enzyme {ECO:0000256|ARBA:ARBA00018421};
DE EC=3.4.19.1 {ECO:0000256|ARBA:ARBA00012917};
GN ORFNames=NAEGRDRAFT_74773 {ECO:0000313|EMBL:EFC37532.1};
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:EFC37532.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC37532.1,
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of an N-acetyl or N-formyl amino acid from the N-
CC terminus of a polypeptide.; EC=3.4.19.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000721};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; GG738917; EFC37532.1; -; Genomic_DNA.
DR RefSeq; XP_002670276.1; XM_002670230.1.
DR AlphaFoldDB; D2W090; -.
DR STRING; 5762.D2W090; -.
DR MEROPS; S09.004; -.
DR EnsemblProtists; EFC37532; EFC37532; NAEGRDRAFT_74773.
DR GeneID; 8857405; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_74773; -.
DR eggNOG; KOG2100; Eukaryota.
DR InParanoid; D2W090; -.
DR OMA; QEIATPF; -.
DR OrthoDB; 2877590at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR045550; AARE_N.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR PANTHER; PTHR42776:SF4; ACYLAMINO-ACID-RELEASING ENZYME; 1.
DR PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR Pfam; PF19283; APEH_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT DOMAIN 12..270
FT /note="Acylamino-acid-releasing enzyme N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19283"
FT DOMAIN 529..744
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 746 AA; 84012 MW; 19B4647B475AC896 CRC64;
MSLNVDSQTA SRVSQLYEDL KTIPTLSGGL ILPSSCIEIN CTVSDHQNDK NISLSKQYQL
VNDHQVVGSP YPSITPADIH LVSTSPSGKR RAVFKCIASD GKPNANTAAL DYQIEIYSNQ
VLQLRILVKD IHGKVFTDET FGRVSWSSCE NKLLYVAEMK QELVKPYWEK YSRTNDKLPE
NDNPYQYKYD YEAKEDWGEQ ILLKTPHIYE LDILVKKVTH IDLIPATDSA GSPHYLPGST
NFVYTAFERP VRKLGIRFCV QRDAKLFYCD RISVKQIASE YRGPRRPVFS PCGTKLAFLA
IENSVNYHNS TSKLVVVNWT TEGAKDSQVI VDIVDEVKCN DEIEAMNTFP GLYNIDLPLS
CWSSDSRYIV MNSTWRSVQS IVVIDTQKTS NNVRRLFNSN TYESYVLLSH EPQSKKVLYY
KTTPTMPYQI YVGKLDYDSL EVSNITLIED ALSLINTELN DSGIKEKLES ISWKVLHIPI
EKGSKVYMDC ILYIPKGPKS FVNGSGSDKH SLLLIPHGGP HGSCSTIFAA RFIYFALCGY
AVLLLNYRGS VGFSQSFAGC LPGNIGDMDV KDCYNSYRYI LDENVIPVDE NSVSVYGGSH
GGFLSGHLVG QYPSQFKAGI LLNPVINLAT IFSESDIPDW CYNESLGNDY YDEACVTKEM
LTQMYDRSPI AHVSNVTAAV LLLVGEVDRR VPKEQPREFY HSLRLLGKCK EARMLVYPEN
DHPIAKPKDD FDSMVSSALF LYKHSN
//