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Database: UniProt
Entry: U6GI37_EIMAC
LinkDB: U6GI37_EIMAC
Original site: U6GI37_EIMAC 
ID   U6GI37_EIMAC            Unreviewed;       783 AA.
AC   U6GI37;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
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=EAH_00000990 {ECO:0000313|EMBL:CDI78244.1};
OS   Eimeria acervulina (Coccidian parasite).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=5801 {ECO:0000313|EMBL:CDI78244.1};
RN   [1] {ECO:0000313|EMBL:CDI78244.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDI78244.1};
RA   Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA   Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA   Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA   Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA   Tomley F., Pain A.;
RT   "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDI78244.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDI78244.1};
RA   Aslett M.;
RL   Submitted (OCT-2013) 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; HG670841; CDI78244.1; -; Genomic_DNA.
DR   RefSeq; XP_013251513.1; XM_013396059.1.
DR   AlphaFoldDB; U6GI37; -.
DR   MEROPS; C01.165; -.
DR   EnsemblProtists; CDI78244; CDI78244; EAH_00000990.
DR   GeneID; 25268169; -.
DR   VEuPathDB; ToxoDB:EAH_00000990; -.
DR   OMA; TQLGWYS; -.
DR   OrthoDB; 5475703at2759; -.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   DOMAIN          433..761
FT                   /note="Peptidase C1A papain C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00645"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          308..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          375..402
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   783 AA;  84642 MW;  CFB08F3BEE696A4C CRC64;
     MTPPTSGVIQ SCGSGTPNRN TENLREEIAD PQKYLDKHGG VSTVIEVELT DETMPFTSFF
     DSAANPHRHS WQSLVVKDSN NNLGGTWTMV YDEGYEVSLR DRTHLFGLMK YSKNEECPAA
     ADGDLEDSNG RTACYTTDST KTQLGWYSSI GVDGSVLSGC FYGEKRLEGE DKGNEALPSS
     FVYVRGTASS EGNANKEAAA TTAAANAAAG VGTTPRESAA FDYFLSEDFV NAHNSDEHKS
     WIASANSSFI QQHRSILPSL IKYFGHSKVN STDGTEAFPS FLQGASGSSN STSSTAQLYA
     CPCKEGEVPE DTRRHVPEKA TQPVLSPQSL VQTAAKTVEI KAHEQEQVLQ QQHVQQQQVE
     QQQVEQQQVQ QQQVQQAQQQ QVQQAQQQQV QQQQQVQQQQ QVQQQQQVQQ QQVQQQPVQQ
     QQPVQQQQED FELPAAFAWP NPFTDPSFSE APTNQGGCGS CYAISALYAL QQRFAIAAAK
     AIDRSNSSSS SENAQEQQGV SPSLLQQVQQ LQKTAVPKLS PQFILSCSFY NQGCNGGLPY
     LVGKQAKETG VLGEECMPYV GMDTLTCPVL QPTSSSSSSS SSSSSSTDSF VSFLAADNGS
     GSCHGPEQRW FAKSYGYVGG CYECSHCSGE EQIMREIMSN GPVAAAFDAP ASLFTYVSGV
     FTAPAYTPHA RVCDSPSATD SRRSSLGGWE YTNHAVTIVG WGETDAAAAT TATPAAAGDS
     GKLKYWIVRN TWGSSWGKGG YFLLIRGVNA GGIESQASFI DPDLTRGKGK QLFDSLLAAH
     SNK
//
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