ID Q4E1H6_TRYCC Unreviewed; 725 AA.
AC Q4E1H6;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Leishmanolysin-like peptidase {ECO:0000256|RuleBase:RU366077};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366077};
GN ORFNames=Tc00.1047053508165.310 {ECO:0000313|EMBL:EAN98641.1};
OS Trypanosoma cruzi (strain CL Brener).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=353153 {ECO:0000313|EMBL:EAN98641.1, ECO:0000313|Proteomes:UP000002296};
RN [1] {ECO:0000313|EMBL:EAN98641.1, ECO:0000313|Proteomes:UP000002296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL Brener {ECO:0000313|EMBL:EAN98641.1,
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Preference for hydrophobic residues at P1 and P1' and basic
CC residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-
CC Tyr-|-Leu-Lys-Lys-.; EC=3.4.24.36;
CC Evidence={ECO:0000256|ARBA:ARBA00001249};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR601577-2,
CC ECO:0000256|RuleBase:RU366077};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR601577-2,
CC ECO:0000256|RuleBase:RU366077};
CC -!- SIMILARITY: Belongs to the peptidase M8 family.
CC {ECO:0000256|ARBA:ARBA00005860, ECO:0000256|RuleBase:RU366077}.
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:EAN98641.1}.
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DR EMBL; AAHK01000047; EAN98641.1; -; Genomic_DNA.
DR RefSeq; XP_820492.1; XM_815399.1.
DR AlphaFoldDB; Q4E1H6; -.
DR SMR; Q4E1H6; -.
DR PaxDb; 353153-Q4E1H6; -.
DR EnsemblProtists; EAN98641; EAN98641; Tc00.1047053508165.310.
DR GeneID; 3553172; -.
DR KEGG; tcr:508165.310; -.
DR eggNOG; KOG2556; Eukaryota.
DR InParanoid; Q4E1H6; -.
DR OrthoDB; 24037at2759; -.
DR Proteomes; UP000002296; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.10.170.20; -; 1.
DR Gene3D; 3.90.132.10; Leishmanolysin , domain 2; 1.
DR Gene3D; 2.30.34.10; Leishmanolysin domain 4; 1.
DR InterPro; IPR001577; Peptidase_M8.
DR InterPro; IPR021287; Trans-sialidase_CS.
DR PANTHER; PTHR10942; LEISHMANOLYSIN-LIKE PEPTIDASE; 1.
DR PANTHER; PTHR10942:SF0; LEISHMANOLYSIN-LIKE PEPTIDASE; 1.
DR Pfam; PF01457; Peptidase_M8; 1.
DR Pfam; PF11052; Tr-sialidase_C; 1.
DR PRINTS; PR00782; LSHMANOLYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366077};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR601577-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|PIRSR:PIRSR601577-2};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366077};
KW Reference proteome {ECO:0000313|Proteomes:UP000002296};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU366077};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601577-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|RuleBase:RU366077"
FT CHAIN 34..725
FT /note="Leishmanolysin-like peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366077"
FT /id="PRO_5023964658"
FT REGION 571..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 243
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-1"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
SQ SEQUENCE 725 AA; 78810 MW; 8BF32EFA292A760C CRC64;
MHIPQAMRQP HHATPPLPLL VLLLMYCATA CIAAAPATQY WRGLDEMMRS GLLSTAVVRE
VPRKGQGTMR AYTVATQDDN SGWEPIRIKV FTDGLKSTRR KKTYCEKVGD ECDSFLGEWI
TCKEEHLLSE AKKKLYTEKI LPGAVKLHAE RLLVKPTERN ITVPSNLNEA CKHFKVPTEH
MRYGVAADFV IYASAGPSGT NSRAVWAATC NTWEDFRPSI GAINFDPRYM TDTAWSVRVA
AHEIAHALGF SKESMEEKSL VKNSANIVRE KVRKMVAGDH VQEKAKAHFG CDSLEGMELE
DEGGTREKAI PHWKERHARD ELMAPIVGAG YYTALTMAVF ADMEYYRVNW SMAEPMGWGN
GTGCDFLEKK CNATENLAGK YPHMFCNDSD KETLRCTSDR RHVGTCTAII VENEGSPTDK
DFCPVVSSYF HEKSSGIKYN TCSDGTVTSP PGSLTGGDSW CLDAELLETK DGKHKSVKGV
CAQVLCAEGT VKVKYLGNTD NWHECPEGSV IPVTLENFEK DGKIKCPKYV EVCTIAANGS
SLVIPSVLED DKGEEQEEQV EESVVAPVVS PAAEPHAEAS SPGQPHTEMP SPRVQAAPQQ
PREEIKAQAS TAEEPYEEEP RAAASSTEEP RAEASIAGKT SEAPVVQAAL QQPQQESKAG
QNATVGDSAN TEQVPANTSQ GSVGKAAFSN SHAAGEATGD GGTVRESGLL PSLPLLLGLW
GFAAL
//
