ID S9VY44_9TRYP Unreviewed; 448 AA.
AC S9VY44;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00011965};
DE EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN ORFNames=STCU_05005 {ECO:0000313|EMBL:EPY28575.1}, STCU_06209
GN {ECO:0000313|EMBL:EPY26323.1}, STCU_07530
GN {ECO:0000313|EMBL:EPY23710.1}, STCU_07884
GN {ECO:0000313|EMBL:EPY23074.1};
OS Strigomonas culicis.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Strigomonadinae; Strigomonas.
OX NCBI_TaxID=28005 {ECO:0000313|EMBL:EPY28575.1, ECO:0000313|Proteomes:UP000015354};
RN [1] {ECO:0000313|EMBL:EPY28575.1, ECO:0000313|Proteomes:UP000015354}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23560078;
RA Motta M.C., Martins A.C., de Souza S.S., Catta-Preta C.M., Silva R.,
RA Klein C.C., de Almeida L.G., de Lima Cunha O., Ciapina L.P., Brocchi M.,
RA Colabardini A.C., de Araujo Lima B., Machado C.R., de Almeida Soares C.M.,
RA Probst C.M., de Menezes C.B., Thompson C.E., Bartholomeu D.C., Gradia D.F.,
RA Pavoni D.P., Grisard E.C., Fantinatti-Garboggini F., Marchini F.K.,
RA Rodrigues-Luiz G.F., Wagner G., Goldman G.H., Fietto J.L., Elias M.C.,
RA Goldman M.H., Sagot M.F., Pereira M., Stoco P.H., de Mendonca-Neto R.P.,
RA Teixeira S.M., Maciel T.E., de Oliveira Mendes T.A., Urmenyi T.P.,
RA de Souza W., Schenkman S., de Vasconcelos A.T.;
RT "Predicting the Proteins of Angomonas deanei, Strigomonas culicis and Their
RT Respective Endosymbionts Reveals New Aspects of the Trypanosomatidae
RT Family.";
RL PLoS ONE 8:E60209-E60209(2013).
RN [2] {ECO:0000313|EMBL:EPY28575.1}
RP NUCLEOTIDE SEQUENCE.
RA Motta M.C.M., Martins A.C.A., Preta C.M.C.C., Silva R., de Souza S.S.,
RA Klein C.C., de Almeida L.G.P., Cunha O.L., Colabardini A.C., Lima B.A.,
RA Machado C.R., Soares C.M.A., de Menezes C.B.A., Bartolomeu D.C.,
RA Grisard E.C., Fantinatti-Garboggini F., Rodrigues-Luiz G.F., Wagner G.,
RA Goldman G.H., Fietto J.L.R., Ciapina L.P., Brocchi M., Elias M.C.,
RA Goldman M.H.S., Sagot M.-F., Pereira M., Stoco P.H., Teixeira S.M.R.,
RA de Mendonca-Neto R.P., Maciel T.E.F., Mendes T.A.O., Urmenyi T.P.,
RA Teixeira M.M.G., de Camargo E.F.P., de Sousa W., Schenkman S.,
RA de Vasconcelos A.T.R.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal aspartate or glutamate from a
CC peptide, with a preference for aspartate.; EC=3.4.11.21;
CC Evidence={ECO:0000256|ARBA:ARBA00001335};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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:EPY28575.1}.
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DR EMBL; ATMH01007884; EPY23074.1; -; Genomic_DNA.
DR EMBL; ATMH01007530; EPY23710.1; -; Genomic_DNA.
DR EMBL; ATMH01006209; EPY26323.1; -; Genomic_DNA.
DR EMBL; ATMH01005005; EPY28575.1; -; Genomic_DNA.
DR AlphaFoldDB; S9VY44; -.
DR EnsemblProtists; EPY23074; EPY23074; STCU_07884.
DR EnsemblProtists; EPY23710; EPY23710; STCU_07530.
DR EnsemblProtists; EPY26323; EPY26323; STCU_06209.
DR EnsemblProtists; EPY28575; EPY28575; STCU_05005.
DR OrthoDB; 1156at2759; -.
DR Proteomes; UP000015354; 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; cd05658; M18_DAP; 1.
DR Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU004386};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004386};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU004386};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW Reference proteome {ECO:0000313|Proteomes:UP000015354};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 448 AA; 49102 MW; 833CEAA0E14BE12D CRC64;
MLKSEITGTY AREFVDFLNK ACTPFHAVKV TSDILRNAGF TELTEGKIWP ELSCGDKYYV
TRNDSSIVAF TVGGKYTSGN GIKIIGAHTD SPNLALKPKT RSTKDKYERV AVQCYGGGLW
HTWFDRDLTV AGRVVVKRET LEKRFVKIDK PILRIPSLAI HLTSGTERES FAPNKERHVI
PLIATELASK IEGADGAAKS SHCIPLMKLI ASAVDCKEEE IVDYDLSVID TQAATIGGVE
DEFIFSARLD NLISCFCATK ALINTLNNMN EDSMIRMVCL FDHEEVGSSS PQGAGGTLIP
DVIEYIVNNK CLRATLVANS FLLSVDGAHA LHPNYSEKHE DNHRPQLHLG PVIKYNANTR
YATNGLTAAI VKDVAKKGEV PIQEFVVKND SPCGSTIGPI LSTLSGIKTA DIGNAMLSMH
SVREMCGTVD IYYLTKLIES FFENYAAV
//
