ID A0A2A2LHY8_9BILA Unreviewed; 1059 AA.
AC A0A2A2LHY8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 ORFNames=WR25_11347 {ECO:0000313|EMBL:PAV85821.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV85821.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV85821.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV85821.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:PAV85821.1}.
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DR EMBL; LIAE01006722; PAV85821.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2LHY8; -.
DR STRING; 2018661.A0A2A2LHY8; -.
DR Proteomes; UP000218231; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; 2.60.40.3170; -; 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; IPR022398; Peptidase_S8_His-AS.
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; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000218231};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 31..277
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 301..418
FT /note="Tripeptidyl-peptidase II first Ig-like"
FT /evidence="ECO:0000259|Pfam:PF21223"
FT DOMAIN 443..521
FT /note="Tripeptidyl-peptidase II galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21316"
FT DOMAIN 560..750
FT /note="Tripeptidyl peptidase II second Ig-like"
FT /evidence="ECO:0000259|Pfam:PF12580"
FT DOMAIN 800..859
FT /note="Tripeptidyl peptidase II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12583"
FT REGION 952..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1059 AA; 117131 MW; 3CEBD4BD87200743 CRC64;
MASFKSSGQY AKLTAYDSAT YTFRIDPSGN RVEIAVANGS HGSHVAGIAA AHYPDEPKRN
GLAPGAKIVA MIIGDNRIDS METGTGLTRA INICAEMNVD VINMSYGEGT HLYNTGAIIN
EMQKIVEKKK AIFLISAGNN GPALSTVGAP GGTTTGIIGV GALLTPCMAD PLYGVFNPAE
CNLYSWSSRG PCPDGWLGVS LCAPGAAFAG VPQCERQSLQ MMNGTSMSSP NCAGAVASLL
SGLKARNIAW TPIIIRTALE NTAKKLENSD TFSCGQGLVQ IKNAFDYLQK HPSFLPETFC
RFNVRVSQTN ISKRGVYLRE ATETSSKQEF NVAIRPVFEE LSDHSHQFSF ERHFHLKTTV
PWIKMPATFV SVAQERTFFM TVDPTMLPEG SVHYAEVVGI DDANPELGPL FRVPVTVIRP
EAMTKDNDFT ANYKFDAPSG IPVRKFLATP NEASCAEITV KNLSKEHLDR FVLHCVHLEE
HKSFRNSEAY KTLGPDGSEW KKWIRVAPGR TLEVCLTRSW TREKHTNVEM EVRFHGTQKP
TELNIVHGAG PAQFRISSAP FRPVDVTPSI SLSYLVVPHK PASSKTEPLT ARDLFTVSGE
PKQVFQIINT YNLKVTKTCE VRLEVSGISP YLYESPIDSL FMQIFSTSKE YVSAASSFPD
RYTHKLEKGD YVVKVQMRSA NEAVLSKFAD SPLLVQMKLD SAVSVSVHSD LASAISGSSG
FKWSSKSLQP SQQIALYASC VSEDKFPKNI APVGGAYFVG KMTVMDDAEA KKVDTCPVTY
HIPEFSTRPS KALSMVVLKE KKKFTEQTTE MEEAIRDVQI SWLEKLKDPV AAEGLYVELI
GKHPTHLPLL TTKLKILMNN RKMNSNERKT MMLIIEQILE ICNPNEVLQY LGAKQENSED
LTCLKKQMDE RKGAIIDALI AKTNALLDTH LKTSTEDVPR ILRQGIEAIL EEKKDETKDG
DKKKEKEGEK DAQAQLPVDG KEETPSSEEE QTAMVSRKEV DDAYTELLKW IGTDDPKVGI
FEFIFSQKMS RTIMNSYFQE FLLIVQPDPL NILIIQLSS
//
