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Database: UniProt
Entry: A0A087GNW2_ARAAL
LinkDB: A0A087GNW2_ARAAL
Original site: A0A087GNW2_ARAAL 
ID   A0A087GNW2_ARAAL        Unreviewed;      1312 AA.
AC   A0A087GNW2;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=tripeptidyl-peptidase II {ECO:0000256|ARBA:ARBA00012462};
DE            EC=3.4.14.10 {ECO:0000256|ARBA:ARBA00012462};
GN   OrderedLocusNames=AALP_Aa6g128200 {ECO:0000313|EMBL:KFK31564.1};
OS   Arabis alpina (Alpine rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX   NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK31564.1, ECO:0000313|Proteomes:UP000029120};
RN   [1] {ECO:0000313|Proteomes:UP000029120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120};
RX   PubMed=27246759; DOI=10.1038/nplants.2014.23;
RA   Willing E.M., Rawat V., Mandakova T., Maumus F., James G.V.,
RA   Nordstroem K.J., Becker C., Warthmann N., Chica C., Szarzynska B.,
RA   Zytnicki M., Albani M.C., Kiefer C., Bergonzi S., Castaings L.,
RA   Mateos J.L., Berns M.C., Bujdoso N., Piofczyk T., de Lorenzo L.,
RA   Barrero-Sicilia C., Mateos I., Piednoel M., Hagmann J., Chen-Min-Tao R.,
RA   Iglesias-Fernandez R., Schuster S.C., Alonso-Blanco C., Roudier F.,
RA   Carbonero P., Paz-Ares J., Davis S.J., Pecinka A., Quesneville H.,
RA   Colot V., Lysak M.A., Weigel D., Coupland G., Schneeberger K.;
RT   "Genome expansion of Arabis alpina linked with retrotransposition and
RT   reduced symmetric DNA methylation.";
RL   Nat. Plants 1:14023-14023(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}.
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DR   EMBL; CM002874; KFK31564.1; -; Genomic_DNA.
DR   EnsemblPlants; KFK31564; KFK31564; AALP_AA6G128200.
DR   Gramene; KFK31564; KFK31564; AALP_AA6G128200.
DR   eggNOG; KOG1114; Eukaryota.
DR   OMA; SLRDFQC; -.
DR   OrthoDB; 2441948at2759; -.
DR   Proteomes; UP000029120; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblPlants.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IEA:EnsemblPlants.
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   CDD; cd04857; Peptidases_S8_Tripeptidyl_Aminopeptidase_II; 1.
DR   Gene3D; 1.25.40.710; -; 1.
DR   Gene3D; 2.60.40.3170; -; 1.
DR   Gene3D; 6.10.250.3080; -; 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; IPR034051; TPP_II_domain.
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:UP000029120};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          68..531
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          577..685
FT                   /note="Tripeptidyl-peptidase II first Ig-like"
FT                   /evidence="ECO:0000259|Pfam:PF21223"
FT   DOMAIN          706..788
FT                   /note="Tripeptidyl-peptidase II galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21316"
FT   DOMAIN          830..1013
FT                   /note="Tripeptidyl peptidase II second Ig-like"
FT                   /evidence="ECO:0000259|Pfam:PF12580"
FT   ACT_SITE        77
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        304
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        490
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1312 AA;  144359 MW;  B66E2F8436940D1B CRC64;
     MPSSSSETLT ASRVGCGGGG GGGVGGVGAD NASVANFKLN ESTFLASLMP KKEIRADCFV
     EAYPEYDGRG VVIAIFDSGF DPSAAGLHVT TDGKPKVLDV IDCTGSGDID TSTVVKADED
     GLIRGASGAP LVVNSSWKNP TGEWRVGCKL VYQLFTDDLT SRVKKERKKN WDEKNQEEIA
     KAVKNLYDFD QKHSKVEGAK LKKTQEDLQS RVDFLKKQAE KYEDKGPVID AVVWHDGEVW
     RVALDTQSLE EDPDSGKLAD FSPLTNYRIE RKYGVFSRLD ACAFVANMYD EGKVLSIVTD
     SSPHGTHVAG IATAHHPEEH LLNGVAPGAQ IISCKIGDTR LGSMETGTGL SRALIACLEH
     KCDLVNMSYG EPALLPDYGR FVDLVTEAVN KRRLIFVSSA GNSGPALTTV GAPGGTTSSM
     IGVGAYVSPA MAAGAHSVVQ PPGEGLEYTW SSRGPTPDGD LGVCISAPGG AVAPVPTWTL
     QRRMLMNGTS MASPSACGAI ALLLSAMKAE GIPVSPYSVR RALENTSAPV GDLPEDKLST
     GQGLMQVDKA YEYLKKFKDC PCVFYQIKVN LSGKTTPTSR GIYLREATAC RQSTEWTVQV
     EPKFHEGASN LKELVPFEEC LELHSTDEGV VRVPDYLLLT HNGRSFNVVV DPTNLGDGVH
     YFEVYGIDCK APERGPLFRI PVTITIPKTV ANRPPVISFQ QMSFISGHIE RRFIEVPLGA
     TWAEATIRTS GFDTSRRFYI DTLQLCPLRR PIKWESATTF ASPSAKSFAF PVVSGQTMEL
     ALAQFWSSGL GSREPTIVDF EIEFHGIGVD KEELILDGSE APIKVEAEAL LASEKLVPVA
     VLNKIRVPYQ PVDAQLKTLA TGRDRLLSGK QILALTLTYK FKLEEAAEVK PYIPLLNNRI
     YDTKFESQFY MISDANKRVY AMGDVYPESS KLPKGDYKLQ LYLRHENVQL LEKLKQLIVF
     IERNMGEIRL NLHSEPDGPI TGNGAFKSSI LMPGVKEAFY VGPPTKDKIP KNTPQGSVLV
     GEISYGKLSF DEKEGKSPKD NPVSYPISYV VPPNKPEEDK KAVSAPNSCK SVSERLEEEV
     RDTKIKFLGS LKQETEEERS EWKKLCACLK SEYPDYTPLL SKILEGLLSR SDAGDKINHY
     EEIIDAANEV VSSVDVDELG RFLLQKSEPE DEEAENLKKK MEMTRDQLAD ALYQKGLALA
     RFENLKGEKE GEGGEESGQK DKFEENYKEL TKWVDVKSSK FGTLTVLREK RLSRLGTALK
     VLDDLIQNEN EIANKKLYEL KLSLLEELGW NHLVTYEKQW MQVRFPTSLP LF
//
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