ID A0A0N4Z918_PARTI Unreviewed; 1311 AA.
AC A0A0N4Z918;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=tripeptidyl-peptidase II {ECO:0000256|ARBA:ARBA00012462};
DE EC=3.4.14.10 {ECO:0000256|ARBA:ARBA00012462};
OS Parastrongyloides trichosuri (Possum-specific nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Parastrongyloides.
OX NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0000380900.1};
RN [1] {ECO:0000313|WBParaSite:PTRK_0000380900.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal tripeptide from a polypeptide.;
CC EC=3.4.14.10; Evidence={ECO:0000256|ARBA:ARBA00001910};
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR STRING; 131310.A0A0N4Z918; -.
DR WBParaSite; PTRK_0000380900.1; PTRK_0000380900.1; PTRK_0000380900.
DR Proteomes; UP000038045; Unplaced.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008240; F:tripeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.710; -; 1.
DR Gene3D; 2.20.25.690; -; 1.
DR Gene3D; 2.60.40.3170; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR046939; TPPII_C_sf.
DR InterPro; IPR048384; TPPII_GBD.
DR InterPro; IPR048383; TPPII_Ig-like-1.
DR InterPro; IPR022229; TPPII_Ig-like-2.
DR InterPro; IPR046940; TPPII_Ig-like_sf.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR PANTHER; PTHR43806:SF14; TRIPEPTIDYL-PEPTIDASE 2; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF12580; TPPII; 1.
DR Pfam; PF21316; TPPII_GBD; 1.
DR Pfam; PF21223; TPPII_Ig-like-1; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 38..506
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 534..650
FT /note="Tripeptidyl-peptidase II first Ig-like"
FT /evidence="ECO:0000259|Pfam:PF21223"
FT DOMAIN 671..755
FT /note="Tripeptidyl-peptidase II galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21316"
FT DOMAIN 794..978
FT /note="Tripeptidyl peptidase II second Ig-like"
FT /evidence="ECO:0000259|Pfam:PF12580"
FT REGION 1178..1201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 47
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 270
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 455
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1311 AA; 145889 MW; C265EA0EDE00173A CRC64;
MDDIKNDNIL ENFPVEELVP KIPTQQKLFL EKYPEYDGRN VLIAILDTGI DVSLPSLQVT
STGERKIVDV IDCSGAGDID ISKVVTAKDG CITGLTGRKL KIPEHWDNPS GKYHIGVKNI
HELYTKGLST RVNKYKKDNV WNGSQNLSVA DVRKALKKHE EEIGGKTEKL ADKSKRDDLI
AQLDFLKNAD KYEDDEGPTA DIIVFQDSKK SWKICLDTSY RGRLGMCTLL SQFKESGDYA
FLNDIDKLSY SFTVRDNGNL LEIVTPIGSH GSHVANIAAA HYPDNRARDG IAPGAKIVSM
CIGDSRLGST ETGAALMRAF NMCVEMKVDI VNLSYGEAVH LSNEGRVIEA IDTMVNKHGI
TFLSSAGNNG PALSTGGGPG STTSSVIGVG ACVTNAMSES MYSVREKVLS NMYPWSSRGP
NPDGWLGVSI MAPGGAICGV PKYCAKGNQL MNGTSMSSPN AVGAVSCLIS GLKAESVPIS
PFRMRMMLEN TSLPLDSKKS DSFGYGKGLV QIDNAFEYAK NSAFSFIDPD LTGFEIGIGN
NTKKPRGIYL RESYETKKPK EHFVTVTPKF RPLSDVEKQI NFEANCILTC KDSFVKYPKF
VNLPSDGKQF SIFVDPTQVP PGTVKYTEII GYENDHKELG ALFTIPITII NPMTVPDNGK
LDGSFDMVPS IPRRMFVTVP SGCDYFIMKL KNSGNTNTAK YIMHCLQLLP NMAYRNTETH
KMINMEPDSE CMQTVKVKEN RTVEICLTKF WNSLGNSELS YEIEFYGAIP NLKKFDMMSS
NVFSPISITN CNFRHYTSTP TLTLKKLISS VKPVIAKVEP LGTRDIFDDG TQIFQLHLTY
NLTVPKATEY EFYYPGLSGM LYESGIDHIF MQIFSESKKY IHSSSSFGDR YPIKLEKGDY
KIHVQLRHFS DVLLEKYNEL PLSIKAKLAK DIELEAFYNP NGQFVSGKKK VTSLNLQPGE
TKTIYVSPIA LDKLPKEATI GTHLTGTMTF AKGDHISARI SVKYQCNYFI THDVTSKTEK
GSLVCALTTK NGKEPKENSI KSALITGLTK ASDVIVAQEF LTRLTTEFGD KAEFYHEFLK
KLLALKHEDN KLIMDTCDKI LKNIDESELL KYFGKKQSNV PENDKIKKEM DDKKEALIAA
YAAIFNYVVD SNLIISTSKI PKIFRKNFLS LKGVDNNDKK EEDKKNECKE SVDDSSSPSE
IDSSTAYEIV ADGGEKYTLI DVQDAYASLT KWIDEADSKI LVQTIKYCVA NENFGLALKH
LLKLQEDKKY INNRDIDSAI ISLVESLGWI HISNSMSNKL LKKYPSSYRL F
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