ID A0A024TFX8_9STRA Unreviewed; 524 AA.
AC A0A024TFX8;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=prolyl aminopeptidase {ECO:0000256|ARBA:ARBA00012568};
DE EC=3.4.11.5 {ECO:0000256|ARBA:ARBA00012568};
GN ORFNames=H310_13182 {ECO:0000313|EMBL:ETV92496.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV92496.1};
RN [1] {ECO:0000313|EMBL:ETV92496.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETV92496.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001585};
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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DR EMBL; KI913999; ETV92496.1; -; Genomic_DNA.
DR RefSeq; XP_008878803.1; XM_008880581.1.
DR AlphaFoldDB; A0A024TFX8; -.
DR STRING; 157072.A0A024TFX8; -.
DR EnsemblFungi; H310_13182-t26_2; H310_13182-t26_2-p1; H310_13182.
DR EnsemblProtists; ETV92496; ETV92496; H310_13182.
DR GeneID; 20090232; -.
DR VEuPathDB; FungiDB:H310_13182; -.
DR eggNOG; KOG2597; Eukaryota.
DR OrthoDB; 2899215at2759; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR008283; Peptidase_M17_N.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11963:SF23; ZGC:152830; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 366..373
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 524 AA; 56232 MW; DACCA6420845F6D0 CRC64;
MQRLQQKVLG KVKLLGLKDS LPTTTGKAAH VLFVPKTSSN ESLRTALPFA VSEEVLNDFN
GHAKETLLLY PKDGQRTLLV GLGDKIDEVS LRDATHEALV NLKGRGVRHA FLRAPHIDNM
TEQRVAELMA QASVLSNYEF NRHLSAPEDP TVDEKLPLRD IFVQTPASDE DACRVAETLA
VAEETLFARN LGNERSDVVT PAFVEAVAIE SAKTLPNLRV TVLQDDELRA KGLNMMALVG
QAGVCPPRLV LLEYDGNATA PADRIALVGK VQSPSRHYPF VMKDAQGITF DTGGLNLKPT
GSMEDMHMDM CGSAAVLGAV RAAAKNGLRV NVIAALALAE NAIGSKAAKP HTIVKSLKGL
TVEVNNTDAE GRLVLADALT YVQQQFKPHT VIDVATLTGA CVVALGEYSA GLFSNADDLA
TALEVAGKST HERCWRLPIF AEHTAELKGF QSDSRSTGAG RYGGASTAAA FLQQFIEKDV
KWAHLDIAGP AMYSAARSFF PKGATGFGVQ VLHEYLKRTT VASA
//
