ID A0A016SAT2_9BILA Unreviewed; 1394 AA.
AC A0A016SAT2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Tripeptidyl-peptidase 2 {ECO:0000256|ARBA:ARBA00020244};
DE EC=3.4.14.10 {ECO:0000256|ARBA:ARBA00012462};
DE AltName: Full=Tripeptidyl aminopeptidase {ECO:0000256|ARBA:ARBA00032232};
GN Name=Acey_s0263.g583 {ECO:0000313|EMBL:EYB87394.1};
GN Synonyms=Acey-F21H12.6 {ECO:0000313|EMBL:EYB87394.1};
GN ORFNames=Y032_0263g583 {ECO:0000313|EMBL:EYB87394.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB87394.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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}.
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:EYB87394.1}.
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DR EMBL; JARK01001599; EYB87394.1; -; Genomic_DNA.
DR Proteomes; UP000024635; Unassembled WGS sequence.
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; IPR022232; TPPII_C_art.
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; PF12583; TPPII_C; 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}; Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 124..587
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 616..731
FT /note="Tripeptidyl-peptidase II first Ig-like"
FT /evidence="ECO:0000259|Pfam:PF21223"
FT DOMAIN 755..833
FT /note="Tripeptidyl-peptidase II galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21316"
FT DOMAIN 873..1056
FT /note="Tripeptidyl peptidase II second Ig-like"
FT /evidence="ECO:0000259|Pfam:PF12580"
FT DOMAIN 1109..1166
FT /note="Tripeptidyl peptidase II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12583"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1265..1297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 131
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 352
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 537
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1394 AA; 156006 MW; 7760625C2E452A1B CRC64;
MFPHRNPEDE DSDEYPEGDQ FGNPVRNHLR DPAEIRFRDS VELHFFGVYR YSVGGGSSEE
EDDLDDVEVD DESLYGEDPM DDTNELEQPV ETKSNFPVDT FIYKAESQQP EFVKDHGKYA
DGCNVLIAIL DTGVDPSLPC LERTSFGARK IVDCIDCSGA GDVDTSVVKS AQNGVVIGLT
GRKLNIPEQW VNPTGKWHLG IKPIYELYPK TLRKTVKEDW QKESWESAHQ LAKADALRLL
LAHEESVGGF SDNVKDKHDR ENLACQVDFL KSMDKLEDKG PVADCIVWHD GHNWKACIDT
SFRGRLALCH PMGEFRTTGD FSKLSHRDEA CYTFRIENNG NRLEICVPSG AHGTHVACIA
AAYSKDEPGS SGLAPGAQIV SMMIGDNRID SMETGTALTR ALNLCVEMKV DIVNMSFGEG
AHFPASGRII EEIQRIVYEH NVVFVASAGN SGPALSTVGS PGGTTPGVMG IGARICPDQA
EALYGVFNEV KNVLYPWSAR GPCVDGALGV SLCAPGAAFA GVPRYSRKAK QMMNGTSMSS
PNAAGAIACM ISKMRANGYQ WNPFRIRLCL ENTAKEISDE PFPFGTGRGL LQIKNALDHF
ENYALYMPNT CLVDIRVRVT NYNRSKRGVY IREFKESREI QEYTVTVEPK FKEFADNLYQ
ADFSVNIVLQ SDVDYVQHPS LFMLTSEGRS FTLKVDPTGL RPGGVYYTEL RGMHAESFDM
GPIFRVPITL VIPETVNEVD CSIDRTFEKV GTIPIRQFIH VPPEATICQV LVEDLSRKPM
DRFTLHCVQL EDDKCYRNSE SYKILGPDSH EWTKSFPVVG DRTLEVCLVR GWTRSDVEGS
VRIFTRFYGV QRYPLVNLVH GSPYTPIRIR AAPFRPVEIK PTISLNTLYV AVKPSTAKIE
PLGPRDLMPN GKQIHRLMLV YKFNMLKSCE VRLELPGVTT YLYESPYDCV LMQLFSSSKE
FIGASSSYPE RYTYKVEKGE YTAHVQVRQP ETSQLELLMD SPLHVRVHIS PAISLDVTSV
PNGGDDAFKW VNKPLAPGQQ TTLYAGSISD DKVPKVIQVV GGCILTGSLF VVADTELKQA
DRSAVSYIFT EYSTRPSKAL SMVTLREKKT DSTGQDEKDM NDAIRDTQIS WLPKLKDPVA
VERLYSELIA KHPTHLPLLL MKMKLLVDKK RSKTETETMN LIIQQILEQC QVEEVLKYFG
ARQDHNVEQI ALKKNMEERK AAIIDCLLAR AHTTVESHLK KNDELAATLR KQLIPVFGLS
QEEEKATKGE KVKEELLSDD SDAESSKTTE EKGDATKPSL KEVDAVYHEL LSWVAADDPK
VLLLSAKHSI AHAHYGRACS YLQKLIEDMK ANSKDTSNIE LALIELCETL GWYHIVTRLT
NERLVRNRSS YRPF
//
