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Database: UniProt
Entry: A0A509AMG3_PLABA
LinkDB: A0A509AMG3_PLABA
Original site: A0A509AMG3_PLABA 
ID   A0A509AMG3_PLABA        Unreviewed;       534 AA.
AC   A0A509AMG3;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Alpha-MPP {ECO:0000256|ARBA:ARBA00030006};
GN   ORFNames=PBANKA_1237900 {ECO:0000313|EMBL:VUC57275.1};
OS   Plasmodium berghei (strain Anka).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX   NCBI_TaxID=5823 {ECO:0000313|EMBL:VUC57275.1, ECO:0000313|Proteomes:UP000074855};
RN   [1] {ECO:0000313|EMBL:VUC57275.1, ECO:0000313|Proteomes:UP000074855}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ANKA {ECO:0000313|EMBL:VUC57275.1,
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   -!- FUNCTION: Substrate recognition and binding subunit of the essential
CC       mitochondrial processing protease (MPP), which cleaves the
CC       mitochondrial sequence off newly imported precursors proteins.
CC       {ECO:0000256|ARBA:ARBA00002123}.
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DR   EMBL; LK023127; VUC57275.1; -; Genomic_DNA.
DR   RefSeq; XP_679923.1; XM_674831.1.
DR   AlphaFoldDB; A0A509AMG3; -.
DR   STRING; 5823.A0A509AMG3; -.
DR   VEuPathDB; PlasmoDB:PBANKA_1237900; -.
DR   InParanoid; A0A509AMG3; -.
DR   OMA; LKYHHSP; -.
DR   OrthoDB; 7099at2759; -.
DR   Proteomes; UP000074855; Chromosome 12.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   PANTHER; PTHR11851:SF49; MITOCHONDRIAL-PROCESSING PEPTIDASE SUBUNIT ALPHA; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000074855}.
FT   DOMAIN          114..261
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          271..454
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   534 AA;  61264 MW;  59F41F79E556BA53 CRC64;
     MNTNIQKLKL VLNKTKLGTK SYSHDVSKLK RNPNLEKLYT GDKHDFSKVI FKKEQIEDVI
     KEVKFDYYYF NEGKKNKYKD IPLNVSIIKE SDLPPYKPVD EKLNFSILEN DLKIISTNKN
     SGVCSIGLYI KCGSRYEEIN DKINEQGMSV MIENMAFHST AHLSHLRAIK SLEKIGANVS
     CNAFREHIVY TCECLNEYLP IVINLLIGNV LFPRFLSWEM KNNVNRLNTM RAKLFENNEM
     YITELLHNTA WYNNTLGNKL YVSESNIENY TSENLRNFML KHFSPKNMTL VGINVDHNEL
     TKWTSRAFQD YVPIPYIKQK EVTPNYTGGF ISVEDKNIKK TNIAIAYETK GGWKTSDMIT
     LTVLQTLMGG GGSFSTGGPG KGMYSRLFLN VLNNYNFIES CMAFSTQHSD TGLFGLYFTG
     DPANTKDIIN SMALEFHKMN KCTDEELNRA KKSLKSFMWM SLEYKSILME DLARQMMILN
     RILSGKQLCD AIDAVTKEDI NRVVSQFLKT KPTVVVYGNI SHSPHYDEIC KMLG
//
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