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
//