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Database: UniProt
Entry: E9AL20_LEIMU
LinkDB: E9AL20_LEIMU
Original site: E9AL20_LEIMU 
ID   E9AL20_LEIMU            Unreviewed;      1032 AA.
AC   E9AL20;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   SubName: Full=Pitrilysin-like metalloprotease (Metallo-peptidase, clan me, family m16c) {ECO:0000313|EMBL:CBZ23623.1};
GN   ORFNames=LMXM_07_0100 {ECO:0000313|EMBL:CBZ23623.1};
OS   Leishmania mexicana (strain MHOM/GT/2001/U1103).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=929439 {ECO:0000313|EMBL:CBZ23623.1, ECO:0000313|Proteomes:UP000007259};
RN   [1] {ECO:0000313|Proteomes:UP000007259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|Proteomes:UP000007259};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural change
RT   between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; FR799560; CBZ23623.1; -; Genomic_DNA.
DR   RefSeq; XP_003872154.1; XM_003872105.1.
DR   AlphaFoldDB; E9AL20; -.
DR   MEROPS; M16.009; -.
DR   GeneID; 13447025; -.
DR   KEGG; lmi:LMXM_07_0100; -.
DR   VEuPathDB; TriTrypDB:LmxM.07.0100; -.
DR   OMA; FPFQVHY; -.
DR   OrthoDB; 5477696at2759; -.
DR   PhylomeDB; E9AL20; -.
DR   Proteomes; UP000007259; Chromosome 7.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR013578; Peptidase_M16C_assoc.
DR   PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR   PANTHER; PTHR43016:SF13; PRESEQUENCE PROTEASE, MITOCHONDRIAL; 1.
DR   Pfam; PF08367; M16C_assoc; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SMART; SM01264; M16C_associated; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:CBZ23623.1};
KW   Metalloprotease {ECO:0000313|EMBL:CBZ23623.1};
KW   Protease {ECO:0000313|EMBL:CBZ23623.1}.
FT   DOMAIN          496..760
FT                   /note="Peptidase M16C associated"
FT                   /evidence="ECO:0000259|SMART:SM01264"
FT   REGION          160..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          496..523
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1032 AA;  115444 MW;  D583F843964B40AE CRC64;
     MLRRSVRCLA LRTSRREDLV FRSMHGFTLL KMRRIDDLHL VAYEMEHVRT GALYYHIDVE
     DNNNTFCIGF RTPAENNKGT SHVLEHTTLC GSKKYPVRDP FFMMLKRSLS SFMNAMTGSD
     YTLYPFSTTN RKDFQNLLDV YLDAVLHPLL REEDFKQEGH RVELEDKSTG SEDAAAQPSK
     RTRRLINNGV VFNEMRGVVS DPSNHFVHSL MRAMLPHTHY TYISGGYPPD ILGLSYDELL
     SFQRRHYHPS NSITFTYGNL HPESHMAALN SYFADFEHAA PVVVPTLADQ HRFTEPQLVH
     LEGPLDAMGN PQRQKRVAVS YAVPKENNKL EDVVALSVLD SLLSSGPSSP MFKNLIESQI
     GSKYAPMQGY AFYLSSPIIT YGVAGMDEER ADAEAEVLQA VESALRTVQR DGFDERRVRS
     VIFQEELQHR HRSADYGLNT CTGLCAMGLC RAQNNPLDFI NWLPHLRRLA DDNAASLLPR
     IETHLLSNPH RAVVSVSAKK EYLNKLQDQL KEADEAVNAS ATEADKDLVE KETKEGLQRL
     RAPQPNDVLP TLRIEDIPTE SFSEPLPCRS SLSSTNGQVY TITHPTNGLV YVHGLIPFNA
     SLTSAMEHGE LAQVPQSVML LESLIGRTGA GKLSYKDHSI AVKLACSGFG FEPLLNESYM
     HKSTTITGTS YSFYTTKEKL KEALDLLSVT LLEPRFSADD ADVYSCALSN LKMACSSLIQ
     SLQAEGNRYA VIRAVGELTR RGELREHWWG LSQSTHASEM LEKLQGCPEV SREAVSALLA
     DYAVFAREMA TDMSRSLVWA TCEDAHREEV ERMLKEFLDA FPRTDSAART HLFLPPRSTE
     KGVQQIIKKL PIDTSFVGLA IPNKLKWENP DQARVRVGCT LLSNEYLHRR VREEGGAYGS
     SCAASLHGEV GGVSMSSYRD PSPELTAKAF LEAGDWLSDR KNVTAERVSE AKLRLFSSID
     SPYAADSYGE AYFYNDLRQD TKQALRDALL SVTPEDVVNV AHYFTPQFTT IISILQPAGE
     SSDPAAVPPE VS
//
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