ID   E9B227_LEIMU            Unreviewed;       621 AA.
AC   E9B227;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Putative aminopeptidase {ECO:0000313|EMBL:CBZ29284.1};
GN   ORFNames=LMXM_30_2260 {ECO:0000313|EMBL:CBZ29284.1};
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:CBZ29284.1, ECO:0000313|Proteomes:UP000007259};
RN   [1] {ECO:0000313|EMBL:CBZ29284.1, ECO:0000313|Proteomes:UP000007259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|EMBL:CBZ29284.1,
RC   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).
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DR   EMBL; FR799583; CBZ29284.1; -; Genomic_DNA.
DR   RefSeq; XP_003877747.1; XM_003877698.1.
DR   AlphaFoldDB; E9B227; -.
DR   GeneID; 13451991; -.
DR   KEGG; lmi:LMXM_30_2260; -.
DR   VEuPathDB; TriTrypDB:LmxM.30.2260; -.
DR   OMA; EHHCSII; -.
DR   OrthoDB; 163542at2759; -.
DR   PhylomeDB; E9B227; -.
DR   Proteomes; UP000007259; Chromosome 30.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR   InterPro; IPR045357; Aminopeptidase_N-like_N.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   4: Predicted;
KW   Aminopeptidase {ECO:0000313|EMBL:CBZ29284.1};
KW   Hydrolase {ECO:0000313|EMBL:CBZ29284.1};
KW   Protease {ECO:0000313|EMBL:CBZ29284.1}.
FT   DOMAIN          203..310
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          389..577
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   REGION          50..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          137..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          506..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..152
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..532
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   621 AA;  66229 MW;  E19A61438A9EED99 CRC64;
     MDSSAYIWNP VQCTVQLVFS RPSSGAAIRA GSAYHGTSII RYRREPYRDT ADSAAGTASS
     SAASPSEGNS EYEDFLRHRR VIAEKNALHL HALTTAGGIY KDARVLDVQS YQVRCVSISA
     DAGAAVLRVV SVEQEDAGAA SAGSSTSGGA GKRKGSSKVW KKGGTDVAEH DAQTSGDSPT
     PAAVDWGSKL ILFEGAGSLP PFSEVDLTTQ FIGRVQSFDC GGIYAAGGIS SNPSTEDVPL
     LTHFEVRFAR CAFPAPDDPQ YRLEWQLKSI QVPSSFRTIL TNGEERGRKE LAAQQAVQVS
     FAPCGPLPAY VFSFACFPGI AEVESMSAAG DGLEVVEGSL DVPKFAGDIV SGLSDTSNLS
     HTPVPVRVLA RRQARIATAT LERVLRLTIE SVIALQHLFQ CPLPLLQCEH LDVLLGPTMP
     YISGMEHHCS IILNEAIYQP GRKTAAAGGG SAHSTAEVEQ TELIVHELTH HWVGNALGLP
     FAVKEGICQV IEQCVGDTLL GKPMRTYKAD SSGSAKPESS SPSSSTAKPP KSTIRASEKG
     HEFTGTSYQH ALSAIKRLVA EHGFDRFVAC LRQLMHVHVV VPAIAVEESG GIQVLRYVRS
     GIATPPYLST EQFLRNVESA L
//