ID   Q8MVZ1_PLAFA            Unreviewed;      1560 AA.
AC   Q8MVZ1;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 75.
DE   SubName: Full=Putative stromal processing peptidase {ECO:0000313|EMBL:AAM64111.1};
OS   Plasmodium falciparum (malaria parasite P. falciparum).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=5833 {ECO:0000313|EMBL:AAM64111.1};
RN   [1] {ECO:0000313|EMBL:AAM64111.1}
RP   NUCLEOTIDE SEQUENCE.
RA   van Dooren G.G., McFadden G.I.;
RL   Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAM64111.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11976331; DOI=10.1074/jbc.M201748200;
RA   Van Dooren G.G., Su V., D'Ombrain M.C., McFadden G.I.;
RT   "Processing of an apicoplast leader sequence in Plasmodium falciparum and
RT   the identification of a putative leader cleavage enzyme.";
RL   J. Biol. Chem. 277:23612-23619(2002).
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DR   EMBL; AF453250; AAM64111.1; -; mRNA.
DR   MEROPS; M16.A21; -.
DR   VEuPathDB; PlasmoDB:PF3D7_1440200; -.
DR   VEuPathDB; PlasmoDB:Pf7G8-2_000514100; -.
DR   VEuPathDB; PlasmoDB:Pf7G8_140045500; -.
DR   VEuPathDB; PlasmoDB:PfCD01_140045700; -.
DR   VEuPathDB; PlasmoDB:PfDd2_140044700; -.
DR   VEuPathDB; PlasmoDB:PfGA01_140045800; -.
DR   VEuPathDB; PlasmoDB:PfGB4_140046400; -.
DR   VEuPathDB; PlasmoDB:PfGN01_140045600; -.
DR   VEuPathDB; PlasmoDB:PfHB3_140046000; -.
DR   VEuPathDB; PlasmoDB:PfIT_140046700; -.
DR   VEuPathDB; PlasmoDB:PfKE01_140045200; -.
DR   VEuPathDB; PlasmoDB:PfKH01_140045800; -.
DR   VEuPathDB; PlasmoDB:PfKH02_140046000; -.
DR   VEuPathDB; PlasmoDB:PfML01_140045900; -.
DR   VEuPathDB; PlasmoDB:PfNF135_140044400; -.
DR   VEuPathDB; PlasmoDB:PfNF54_140044000; -.
DR   VEuPathDB; PlasmoDB:PfSD01_140043600; -.
DR   VEuPathDB; PlasmoDB:PfSN01_140047500; -.
DR   VEuPathDB; PlasmoDB:PfTG01_140045600; -.
DR   BRENDA; 3.4.21.102; 4889.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004655; F:porphobilinogen synthase activity; IEA:InterPro.
DR   GO; GO:0033014; P:tetrapyrrole biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR001731; ALAD.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11458; DELTA-AMINOLEVULINIC ACID DEHYDRATASE; 1.
DR   PANTHER; PTHR11458:SF0; DELTA-AMINOLEVULINIC ACID DEHYDRATASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 3.
PE   2: Evidence at transcript level;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1560
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004312775"
FT   DOMAIN          125..184
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          305..354
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          1388..1459
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   1560 AA;  185548 MW;  4B8698437DB045D3 CRC64;
     MLKSDGVLLL YILIINLICC LNGNSKKRAY ILNTPKSSNC KRSSFRRWNN PVNNNINELK
     EDEDLIKYEL QNGLSNIIYK KRKSVNKKKY ILNNENHVIL PTYKISDEYK CYINPIDYNY
     EELHVYMEVN TGSVNEKKNQ QGISHLCEHV SYMGSKNRKN IVDKNIRTNA YTDFHHIVFY
     ISVSLNNEIY KENFYSDFKC DQFIKNIREE DIEDYDIYTV DEFNYKHAIL SQCIDTMVEV
     LKGETQFNKE RITKEKKAIF SEYSIINNIE YKMNSDIIKV LHKENRLSHR LPIGKLELLK
     RYGEKDVKEY FNLFFRPENV NFFVYGDVNV DIAQKLISSK LENIKGKDLK EQDKIYLNIL
     NDRCTLRSRN KNLPAVFHMF GNNSDIKVKE EEEEEVKKNI QLEKNEKNIE TKDEKFHINN
     NENITFKDTD ENFQEDDYNN KKENDCNTYD DDNIIDLEKY KEFKRNENDI VCELKFRNYL
     KNKYGVNMEE EKLLNKNEMK NINTSFEIIK YSLNNVNINI LLKEEIKSVR TLEDLKISVI
     KEVIFYCLSF RFNIHRNNLF NSIDINEYTN INEGATIRTI EIKTTIKAFE KTIECFYNFI
     KSLLKYGFSE DELLNYKMNE IDYEDDLKDV EEKKSGQIID HQNISHDVSE AYTNSNKHSS
     KNMKLIHPHD DDYDDNHNDA EKDMNNKMNE QDEEYILDST KINETYTDEI QKIIDYNTCQ
     HIYLNEKREK KIKREIFEKL KLQEINNFAK QYFQYLFNIF NPYSNMKPHC VVIHVPSKNE
     NLFHKNKIRK LFFNNIYSMN DVQNYSINIQ NKLLSPHYVY ENITKKLSQA RYIIPQKREN
     KYSEDIFNFI VNKMEDHKNE NIFDVNNMCL SLPFYGLSTN PDLNMFKKCY CIKENKDDHI
     NNVNDHMNET KILPQITESS VQPSLPTSSK KSNNNLCVDM KEKPKTMEIN NKYNNMHDDV
     VCDNRRNNLS EKGVTFLNLK NYVLSLKNQK EIENYELLNG IKVNLYKTKV DKKNIYMRLI
     IPHNDIIKKK KENVHLLLFS IICLFEGGEI ENVTREHVEI HCSNKSINIY IDINDEYFFI
     DIYTHNKYEN ISSAFSILNN IILETKIENT ALPRVVDKLK KDFFEYKNSL QSLLLGQTIS
     YVTGGKIGYQ NFEVSDTENI TMDDVQRMLK HIFSDLSLFE LTIVGDFSDF IHYYILHYLG
     TLQGKIIEQE GEKKRSDVCL KNNKDNIIIE KHRTNNLSNE SYPINEKKKK NEDNGCKSNS
     EILLNDYYSM LCPFADFEEK SKNTTYVYIK EKEEHGIFLL VGKGANMYGF LSNGIHISFY
     LMEYLKRIIN GEEKNKNCEN IYKDEYICNE LDKIKSQVLE DFHFEDKHNI NEYLKKKKKL
     YTSPLFFNAV SYIIQYILNS KLFHYLREKK ELTYDSSFEF ISYEKYFAGF FTILVQTNPR
     DLELIKKEVL SCIELFTTNY NNFSDYLIEN SKLSYLNKKN KDLKYFVDKI SGMQLTHFPL
     KYKNKHILKD NILLNKIQKI DVLLVLFILF NQTKNYHISY GISAPHDIWK ETYKNINKLY
//