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Database: UniProt
Entry: A0A2G9HYM9_9LAMI
LinkDB: A0A2G9HYM9_9LAMI
Original site: A0A2G9HYM9_9LAMI 
ID   A0A2G9HYM9_9LAMI        Unreviewed;       749 AA.
AC   A0A2G9HYM9;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Tripeptidyl-peptidase II {ECO:0000313|EMBL:PIN22583.1};
DE            EC=3.4.14.10 {ECO:0000313|EMBL:PIN22583.1};
GN   ORFNames=CDL12_04695 {ECO:0000313|EMBL:PIN22583.1};
OS   Handroanthus impetiginosus.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC   Handroanthus.
OX   NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN22583.1, ECO:0000313|Proteomes:UP000231279};
RN   [1] {ECO:0000313|Proteomes:UP000231279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX   PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA   Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT   "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT   Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT   forest tree.";
RL   Gigascience 7:1-16(2018).
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:PIN22583.1}.
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DR   EMBL; NKXS01000731; PIN22583.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G9HYM9; -.
DR   STRING; 429701.A0A2G9HYM9; -.
DR   OrthoDB; 769887at2759; -.
DR   Proteomes; UP000231279; Unassembled WGS sequence.
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; cd02120; PA_subtilisin_like; 1.
DR   CDD; cd04852; Peptidases_S8_3; 1.
DR   Gene3D; 2.60.40.2310; -; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 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; IPR034197; Peptidases_S8_3.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   InterPro; IPR045051; SBT.
DR   InterPro; IPR041469; Subtilisin-like_FN3.
DR   PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR   PANTHER; PTHR10795:SF560; SUBTILISIN-LIKE PROTEASE SBT5.6; 1.
DR   Pfam; PF17766; fn3_6; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 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   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:UP000231279};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..749
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013970489"
FT   DOMAIN          28..108
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          140..601
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          651..746
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   REGION          206..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..233
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        149
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        222
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        543
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   749 AA;  79870 MW;  5914AABFA23AF7CE CRC64;
     MNNNHFSIPS LLLLLNILLA SASAPRKVYI VYLGEHSGEK TIQDIEDDHH SYLQYVKGSK
     EEAKASIIYS YKHVINGFSA LLTPQEAAAI SGMDGVISVF ESQERRVHTT RSWDFISLLE
     ANFDPTQANG EALLRRANYG KDVIVGVLDT GVWPESQSFN DRGMDPVPTS WKGICQSGVA
     FNTSNCNRKL IGARYYLRDY ESRNGQVQPT EDYRSPRDSS GHGTHTASTI GGRRVPNAAS
     FGGFGNGTAT GGAPLVRLAI YKMCWSGVCY DGDVMSAFDD AIADGVHVIS ASIGPNTSIP
     YANDIGAIGA LHAVKRNIVV SFSAGNSGPN LSTVTNTAPW VITVGASSID RVFPSQVELG
     NGMIIEGQSV TPFQRRTYPL VYASQVEIPG STTSRTTGLC SYGTLSPPLV RGKAVFCLAG
     DFFQALEVQR AGGAAAVLGN PRNGIGVQVT PYVIPGIVIL RNDTNRMYNY IVSNKAPTVT
     LPPATTSTGA KPAPFMASFS SKGPNNVEPN ILKPDITAPG LNILAAWTEA FSPLKYFIIS
     GTSMSCPHVS AIAALLKAIH PNWSSAAIRS AIMTTAKQTN NLGRPITDAL LNPATPFEYG
     SGHIQPSRAA DPGLVYDASY NDYLRFLCGS IGNSLDPSFP CPRVAPPPSA LNYPSLAIAN
     LRGTMTVTRN VTNVGAATSS YSVTINEPSG FSVRISPTRL NFNAVGQTLS FGITVQAQST
     ARRNEFVFGS YTWSDGIHQV RSPIAVSAA
//
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