ID A0A067D187_SAPPC Unreviewed; 1232 AA.
AC A0A067D187;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Tripeptidyl-peptidase II {ECO:0008006|Google:ProtNLM};
GN ORFNames=SPRG_02495 {ECO:0000313|EMBL:KDO32797.1};
OS Saprolegnia parasitica (strain CBS 223.65).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO32797.1, ECO:0000313|Proteomes:UP000030745};
RN [1] {ECO:0000313|EMBL:KDO32797.1, ECO:0000313|Proteomes:UP000030745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO32797.1,
RC ECO:0000313|Proteomes:UP000030745};
RX PubMed=23785293;
RA Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA Russ C., Tyler B.M., van West P.;
RT "Distinctive expansion of potential virulence genes in the genome of the
RT oomycete fish pathogen Saprolegnia parasitica.";
RL PLoS Genet. 9:E1003272-E1003272(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity for peptide
CC bonds, and a preference for a large uncharged residue in P1.
CC Hydrolyzes peptide amides.; EC=3.4.21.62;
CC Evidence={ECO:0000256|ARBA:ARBA00023529};
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 EMBL; KK583194; KDO32797.1; -; Genomic_DNA.
DR RefSeq; XP_012196459.1; XM_012341069.1.
DR AlphaFoldDB; A0A067D187; -.
DR STRING; 695850.A0A067D187; -.
DR EnsemblProtists; KDO32797; KDO32797; SPRG_02495.
DR GeneID; 24125048; -.
DR KEGG; spar:SPRG_02495; -.
DR VEuPathDB; FungiDB:SPRG_02495; -.
DR OMA; SLRDFQC; -.
DR OrthoDB; 2441948at2759; -.
DR Proteomes; UP000030745; 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: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; 2.
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; 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; 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, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000030745};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 32..489
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 524..636
FT /note="Tripeptidyl-peptidase II first Ig-like"
FT /evidence="ECO:0000259|Pfam:PF21223"
FT DOMAIN 653..743
FT /note="Tripeptidyl-peptidase II galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21316"
FT DOMAIN 779..961
FT /note="Tripeptidyl peptidase II second Ig-like"
FT /evidence="ECO:0000259|Pfam:PF12580"
FT ACT_SITE 41
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 257
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 444
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1232 AA; 132752 MW; 4A4827F116D5A581 CRC64;
MASAQFSPSE EIVPKHETLA SHLLQLYPEY DGRNTVVAIF DTGVDPGAPG LQFTSDGKRK
IIDVVDATGS SDVDMATVLS PTDGKLTLAS GKVLTLNPAW TATEFRVGTK RAYDLYPDPL
VARIKTERKE KWDIADREAK NAVQSALAAW TAAHGAAPTP ADLEARLDLH ARLELLEKTA
FEDPGPIYDC VTFFDGTQWR AAVDASESGD LTSVQAMTNY RVAHEWSTFD DASQLNYALN
IYDDGKVLSI VCDAGSHGTH VAGIVAAYDA ADAKNNGVAP GAQIVSVKIG DSRLGSMETI
VGIARGALAV LDNKCDVVNM SYGEFASTHN SGRTIDVIQE LVDRHGVTFV SSAGNEGPAL
GTIGAPGGTS GCILGVGAYV SPAMMAAEYS MKDTPSSAVG LYTWSSRGPT YDGDVGVNVC
APGGAITSVP NWTLTKKMLM NGTSMSSPNC AGNVALLISG LKAQGIAYTP YSLRRALENT
AISVPTAEAF SMGRGLIQVL PALEYLVQHA NNFDGSKKFP LYHDIRVPSR HNARGIYLRE
VADLADNSLA VVVTPVFHKD AENADRIAYE THLRLVPTKP WIRCADALTL LHQGRNFKVD
VDTAVLTPGA HYGEVVAYDR ENPSRGAVFR IPVTVVKPEV LPAPETSLVK AMVPGAIART
FYHVPEGATW MNVSVSRRAD GSEPSRVLYV LHLMQHALHA RQSATSTHHY LYVDSTGDVT
HSFPVRAAST VELCLAQNWN SIGATTAHMD VAFHGIEPTP TAVHLVGGDA YARVDVRCPL
RNEAIAPSAV LNKWTTRLRP TSSVVSPLGP RDKFSENRQT YQLLLTYTLK MAEDGKVTPS
LPLVNGRLYE SPFDGQMLLV FDEQKKYMGV SDAYPRPISL KKGTYTVRAQ LRHQDPSILD
GLKTAVLAIT RDIKDVAITI YDSPDGPSTN GKAVGTKTLK KGVYSTVFVG EPAFDKLPKG
LAAGDTLAGS ITYGQKHNHF KGVSQKPDGF PLTYTVPSAP TPVKEPEAVV PEDVRSEDEL
ANDAVRDLLV ARLVKLQGKE EFLARWTALC ETYPAHLPLL QARLHHYKHD AHTEIAAAAD
AVLAAIDADA LAAHYGLKLL PNDAAAAKVR KTKDAEKAAL VDALSRKARA LGTAGDVDGF
QAAFTALQQW ADVSEAAHVH ASLLQHAAHP GLALQRLQKL DALAMDEREK HLTQRDLHKA
RIDLYTSLGW KHYASYAANW QVLNAPADYA LF
//
