ID A0A077Z0X8_TRITR Unreviewed; 816 AA.
AC A0A077Z0X8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=TTRE_0000051401 {ECO:0000313|EMBL:CDW52255.1};
OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW52255.1};
RN [1] {ECO:0000313|EMBL:CDW52255.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW52255.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT "The whipworm genome and dual-species transcriptomics of an intimate host-
RT pathogen interaction.";
RL Submitted (MAR-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; HG805817; CDW52255.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077Z0X8; -.
DR STRING; 36087.A0A077Z0X8; -.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.128.80; Cathepsin C, exclusion domain; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
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; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR PANTHER; PTHR12411:SF942; DIPEPTIDYL PEPTIDASE 1; 1.
DR Pfam; PF08773; CathepsinC_exc; 1.
DR Pfam; PF00112; Peptidase_C1; 2.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00645; Pept_C1; 2.
DR SUPFAM; SSF54001; Cysteine proteinases; 2.
DR SUPFAM; SSF75001; Dipeptidyl peptidase I (cathepsin C), exclusion domain; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 2.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 2.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 2.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT DOMAIN 87..322
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
FT DOMAIN 575..811
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 816 AA; 93532 MW; 041431E90E3615E9 CRC64;
MDTTAMDKLK RQFINNKDYI DAVNRAQSKW VATAYKEWET ESFEDMIRKA GARKASKQEQ
KFNFQYFCSW PKPPPSSAET KRIAAALPEH FDWRNVSGVN YVSDVRDQHR CGSCYIFASV
AVLESRYRIL TQNEEKPTFS PQDVLNCSPY AQGCDGGFPF LIAGKHAEDF GMVTESCEPY
TAHQFPCRNN RDVTPCERYY ATNYQYVGGY YGASNEDLIK LAVYHNGPVA VGIQVYPDFY
AYRSGIYHHV KDAMNFNTSP YGWNPFVAVD HAVTVVGYGV ERGTKYWIVK NSWGKYWGEN
GYVKILRGTN ECGIESLAFE STPIIPKMDQ EVVHILLLLL LFYCSSTGAD TPSNCSFDEV
AGTWKFFESN RGLSKHTNCS STNPDQFRHV QVMQLLFPNV AIDSYGNTGV WTLIVNQGFE
VNVNNRKYFA FTEWTERSGH HAISICDKTR PGWAHDKYSR DWSCFAGQKI QRSHKLRSKR
QYKQPVTEAT TAESSFNRVN YQHPFYAEYR YINDLRFIEK INEVQSNWKA TAYPQFEHLS
RLEIVRKMGG PKSRIYSRPK PATVSERVKS LASELPENFD WRNVSGINYV SPVRSQGQCG
SCYAFASAAM LESRYRILTE NTYQPVFSPQ DIVDCSPYSQ GCDGGFPYLI GGKYAEDYGW
VLEECSPYKG KKQDEQLCDV DRHCKRFYAT DYAYVGGFYG GCNEPLMRLA LVENGPIVVG
MNVFDDFLHY KGGIYHHTKL KDTMNWPRKW NPYEITNHAV VIVGYGVDDQ TDMDYWIVKN
SWGTHWGEDG YFRIRRGVDE CGIESSAFEA TPIPTF
//
