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Database: UniProt
Entry: A0A061DD89_BABBI
LinkDB: A0A061DD89_BABBI
Original site: A0A061DD89_BABBI 
ID   A0A061DD89_BABBI        Unreviewed;       520 AA.
AC   A0A061DD89;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Dipeptidyl peptidase 1 {ECO:0000256|ARBA:ARBA00014709};
DE            EC=3.4.14.1 {ECO:0000256|ARBA:ARBA00012059};
DE   AltName: Full=Cathepsin C {ECO:0000256|ARBA:ARBA00029779};
DE   AltName: Full=Cathepsin J {ECO:0000256|ARBA:ARBA00029762};
DE   AltName: Full=Dipeptidyl peptidase I {ECO:0000256|ARBA:ARBA00032961};
DE   AltName: Full=Dipeptidyl transferase {ECO:0000256|ARBA:ARBA00030778};
GN   ORFNames=BBBOND_0212020 {ECO:0000313|EMBL:CDR96060.1};
OS   Babesia bigemina.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Babesiidae; Babesia.
OX   NCBI_TaxID=5866 {ECO:0000313|EMBL:CDR96060.1, ECO:0000313|Proteomes:UP000033188};
RN   [1] {ECO:0000313|Proteomes:UP000033188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bond {ECO:0000313|Proteomes:UP000033188};
RA   Aslett M., De Silva N.;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, except
CC         when Xaa is Arg or Lys, or Yaa or Zaa is Pro.; EC=3.4.14.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000738};
CC   -!- COFACTOR:
CC       Name=chloride; Xref=ChEBI:CHEBI:17996;
CC         Evidence={ECO:0000256|ARBA:ARBA00001923};
CC   -!- SUBUNIT: Tetramer of heterotrimers consisting of exclusion domain,
CC       heavy- and light chains. {ECO:0000256|ARBA:ARBA00011610}.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
CC       {ECO:0000256|ARBA:ARBA00008455}.
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DR   EMBL; LK391708; CDR96060.1; -; Genomic_DNA.
DR   RefSeq; XP_012768246.1; XM_012912792.1.
DR   AlphaFoldDB; A0A061DD89; -.
DR   STRING; 5866.A0A061DD89; -.
DR   EnsemblProtists; CDR96060; CDR96060; BBBOND_0212020.
DR   GeneID; 24564601; -.
DR   KEGG; bbig:BBBOND_0212020; -.
DR   VEuPathDB; PiroplasmaDB:BBBOND_0212020; -.
DR   OMA; CYIASQM; -.
DR   OrthoDB; 5475703at2759; -.
DR   Proteomes; UP000033188; Chromosome 2.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 2.40.128.80; Cathepsin C, exclusion domain; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR014882; CathepsinC_exc.
DR   InterPro; IPR036496; CathepsinC_exc_dom_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR025661; Pept_asp_AS.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   PANTHER; PTHR12411:SF947; CATHEPSIN O; 1.
DR   PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR   Pfam; PF08773; CathepsinC_exc; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF75001; Dipeptidyl peptidase I (cathepsin C), exclusion domain; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   3: Inferred from homology;
KW   Chloride {ECO:0000256|ARBA:ARBA00023214};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033188};
KW   Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..520
FT                   /note="Dipeptidyl peptidase 1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018594735"
FT   DOMAIN          251..498
FT                   /note="Peptidase C1A papain C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00645"
SQ   SEQUENCE   520 AA;  58258 MW;  A9BBB42BCE4D1A3F CRC64;
     MLPLLCLIHL LASVVQVRAD LPIHALVTDI SGKWRIFQSR AVGGLDVACG SDVPNSPEGN
     LLLGNYLAYL KTHFCLDRTT DVHLSLDVTA YSDNTNAPNR SMWRALAVKD KRGNVVGRWT
     AVSDQGFEII FHNNARYFFY LHYTKRDGDQ YETDVTKTQI GWVYEPQGSS DAHATRRCAY
     AARVDGTKPR VSTIVQLKSN DVKNKYRQIS RFISHDTGGV LSAASNKISP KKGPYPCDCS
     SRNQLDFDDD VPESFVWHTQ ATIPVVNQQQ CGSCYAIATK YVLHARFLIA LERCGERTPE
     QEKALEELSH NYFYPEDTSD CSMFNQGCKG GYPYLMGKQM HELGISVVKG NAQQCAILSA
     ERRYFAKDYG YVSGCSQCTA CQGEELIMRE IYANGPVVTA VDAAILNTEY DGSVISPVDS
     EHNSGVCDVE QHPILTGWEY TSHAVAIVGW GQQLEQGKMV KYWLCRNSWG PEWGEDGYFK
     IERGKNVFGV ESEAVFVDPD LSRFKQAPAD ARLHDIHYHY
//
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