ID A0A509APA2_PLABA Unreviewed; 635 AA.
AC A0A509APA2;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=leucyl aminopeptidase {ECO:0000256|ARBA:ARBA00012565};
DE EC=3.4.11.1 {ECO:0000256|ARBA:ARBA00012565};
GN ORFNames=PBANKA_1309900 {ECO:0000313|EMBL:VUC57481.1};
OS Plasmodium berghei (strain Anka).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5823 {ECO:0000313|EMBL:VUC57481.1, ECO:0000313|Proteomes:UP000074855};
RN [1] {ECO:0000313|EMBL:VUC57481.1, ECO:0000313|Proteomes:UP000074855}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ANKA {ECO:0000313|EMBL:VUC57481.1,
RC ECO:0000313|Proteomes:UP000074855};
RX PubMed=25359557; DOI=10.1186/preaccept-1233682211145405;
RA Otto T.D., Bohme U., Jackson A.P., Hunt M., Franke-Fayard B.,
RA Hoeijmakers W.A., Religa A.A., Robertson L., Sanders M., Ogun S.A.,
RA Cunningham D., Erhart A., Billker O., Khan S.M., Stunnenberg H.G.,
RA Langhorne J., Holder A.A., Waters A.P., Newbold C.I., Pain A., Berriman M.,
RA Janse C.J.;
RT "A comprehensive evaluation of rodent malaria parasite genomes and gene
RT expression.";
RL BMC Biol. 12:86-86(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa
CC is preferably Leu, but may be other amino acids including Pro
CC although not Arg or Lys, and Yaa may be Pro. Amino acid amides and
CC methyl esters are also readily hydrolyzed, but rates on arylamides
CC are exceedingly low.; EC=3.4.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000135};
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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DR EMBL; LK023128; VUC57481.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A509APA2; -.
DR STRING; 5823.A0A509APA2; -.
DR VEuPathDB; PlasmoDB:PBANKA_1309900; -.
DR InParanoid; A0A509APA2; -.
DR OMA; LFYEYVT; -.
DR OrthoDB; 2899215at2759; -.
DR Proteomes; UP000074855; Chromosome 13.
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 HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11963:SF23; ZGC:152830; 1.
DR Pfam; PF00883; Peptidase_M17; 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 ECO:0000313|EMBL:VUC57481.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000074855}.
FT DOMAIN 487..494
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 635 AA; 72094 MW; 01F79C4F38441EB9 CRC64;
MYLTRLNINF VDKIFENKFY KNIIKRYYFY NIKHSQKKFF FSFFISNSIK NKNNYNSDCR
EFLTFNTYHY QKTPKYKIES LNFSKTIKKF YSTNNIKNFN ISFSKFEKMS LKVPQVINLD
PTVLPVNYTT PIDDIEIVLK DGIKESCNFD DGLAIFLVNS KSEKDNGNTK ISSQIKDSKI
NEFLSKNDDI FNGKLGTFKS FYMANEKNKY INLSFIRCGT IDEEMTEFEI RKIVSSLVQI
LHDNKSVSTS IIFEIGINES LFRFFLETVF YEYVVDERFK SNDNKSSGNS ENMKNLQIFL
RNYNNNYNKQ VKKSRTYFMG TYFASQLISA PSNYCNPVSL ANVSVELAEK LNLECKILGI
KELENLKMGA YLSVGKGSMY PNRFIHLTYK GKGDIKKKIA LVGKGITFDS GGYNLKASPG
SMIDLMKFDM SGCAAVLGCA YCIGSIKPEN VEVHFLSAVC ENMVSKNSYR PGDIITASNG
KTIEVGNTDA EGRLTLADAL VYAENIGVDH IIDIATLTGA MLYSLGTSYA GVFGNDNKLI
NKILESSKSS NEPVWWLPII KEYRASLNSK YADINNISSN VKASSVVASL FLNEFIQSTS
WAHIDIAGVA WNFKDRKPKG FGVRLLSEFI LNHSI
//
