ID Q4CXX8_TRYCC Unreviewed; 426 AA.
AC Q4CXX8;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE SubName: Full=Aminopeptidase, putative {ECO:0000313|EMBL:EAN85135.1};
DE Flags: Fragment;
GN ORFNames=Tc00.1047053510325.69 {ECO:0000313|EMBL:EAN85135.1};
OS Trypanosoma cruzi (strain CL Brener).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=353153 {ECO:0000313|EMBL:EAN85135.1, ECO:0000313|Proteomes:UP000002296};
RN [1] {ECO:0000313|EMBL:EAN85135.1, ECO:0000313|Proteomes:UP000002296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL Brener {ECO:0000313|EMBL:EAN85135.1,
RC ECO:0000313|Proteomes:UP000002296};
RX PubMed=16020725; DOI=10.1126/science.1112631;
RA El-Sayed N.M., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G.,
RA Tran A.N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G.,
RA Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B.,
RA Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F.,
RA Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H.,
RA da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G.,
RA Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y.,
RA Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J.,
RA Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y.,
RA Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M.,
RA Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J.,
RA Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C.,
RA Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D.,
RA Andersson B.;
RT "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT disease.";
RL Science 309:409-415(2005).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAN85135.1}.
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DR EMBL; AAHK01001498; EAN85135.1; -; Genomic_DNA.
DR RefSeq; XP_806986.1; XM_801893.1.
DR AlphaFoldDB; Q4CXX8; -.
DR SMR; Q4CXX8; -.
DR STRING; 353153.Q4CXX8; -.
DR PaxDb; 353153-Q4CXX8; -.
DR EnsemblProtists; EAN85135; EAN85135; Tc00.1047053510325.69.
DR GeneID; 3537129; -.
DR KEGG; tcr:510325.69; -.
DR eggNOG; KOG1046; Eukaryota.
DR InParanoid; Q4CXX8; -.
DR OMA; DRVNEQH; -.
DR OrthoDB; 167138at2759; -.
DR Proteomes; UP000002296; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
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; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF170; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:EAN85135.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002296};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 15..195
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 229..426
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT ACT_SITE 301
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 385
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
FT NON_TER 426
FT /evidence="ECO:0000313|EMBL:EAN85135.1"
SQ SEQUENCE 426 AA; 47305 MW; D776E8F4B665489F CRC64;
MSSATNSVKL HNPFVPSSYD LHVSVDLANW RYEGKEKVVL RRSPGVEASR EVQLHCGNSV
NIQCVTGAAI AGRDEKAGTL QLLLDGEPAD GHTVTFAFSH EIREEMRGLY RAVFKTSDGA
EHRMAATHFE PTAARLFYIC QDEPSARADF TLHVSLPSSM AGFTVLSNGP LKSKETQGDT
VIHHFETIPA VPPYLTSCFV GELEFVGTTA CGIPVKVYTT VGKSYKAAFA LKTTAFALEY
FEKFFKCKYP LPKLDVVAVP DFPIGGMENW GCIACVESIL LEEQTSSVVS LKRAASLICH
EVSHNWFGNL VTINWWEGLW LKEGFASWCG YDAAHHLEPS WKLNEDAAME VTGALVTDMY
EHSHPVEVPI HDPAEITQIF DDISYSKGMG LVFMLQAFLG EKWAASVAHY IQKHQYSDTR
TIQLWQ
//
