ID A0A2G9H321_9LAMI Unreviewed; 821 AA.
AC A0A2G9H321;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Cucumisin {ECO:0000313|EMBL:PIN11912.1};
DE EC=3.4.21.25 {ECO:0000313|EMBL:PIN11912.1};
GN ORFNames=CDL12_15479 {ECO:0000313|EMBL:PIN11912.1};
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:PIN11912.1, 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 ECO:0000256|RuleBase:RU003355}.
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:PIN11912.1}.
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DR EMBL; NKXS01002829; PIN11912.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G9H321; -.
DR STRING; 429701.A0A2G9H321; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000231279; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
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; IPR023827; Peptidase_S8_Asp-AS.
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:SF384; SUBTILISIN-LIKE PROTEASE SBT2.6; 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; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 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}.
FT DOMAIN 27..131
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 158..640
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 723..815
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 167
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 241
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 603
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 821 AA; 87694 MW; 9918C4EA62523B69 CRC64;
MKNVEMNGSF MVLILFGVLL YGKAEIYIVT LEGEPVVSYR GGVDGFEATA MEPDSSEKID
VTSEMVISYA HHLEKRHDML LDMLFDQGTY KKVYSYRHLI NGFAVHISPE QAEILGRAPG
VKSVERDWKV KKLTTHTPQF LGLPTGVWPT GGGFDRAGED IVIGFVDSGI YPHHPSFANH
HTDPYGPVPQ YRGKCEVDPD TKKDFCNGKI IGAQHFAEAA KTAGAFNPDI DFDSPLDGDG
HGSHTAAIAA GNNGIPVRMH GFEFGKASGM APRARIAVYK ALYRIFGGFV ADVVAAIDQA
VHDGVDILNL SVGPNSPPAT TKTTFLNPFD ATLLSAVKAG VFVVQAAGNG GPFPKTLVSY
SPWIASVAAA VDDRRYKNHL TMGNGKLLAG IGLSPATHAN QTYTMVAAND VLLDSSVGKY
SPSDCQRPEV LNKNLVQGNI LLCGYSFNFV GGTASIKRVS ETAKSLGAVG FVLAVENASP
GTKFDPVPVG IPGILVTDVG MSMELIDYYN ASTPRDWTGR VQSFKAVGSI GEGLKPILQK
SAPQVALFSA RGPNIKDYSF QDADLLKPDI LAPGSLIWAA WAPNGTDEPN YIGEGFAMIS
GTSMAAPHIA GIAALVKKKY PHWSPAAIKS ALMTTSTTLD RAERPLQAQQ YSGSETIALV
PATPFDYGSG HVNPRAALDP GLIFDAGYED YLGFLCTTPG IDAQEIKKYA NAPCNYTLGH
PSNLNTPSIT ISHLVGTQTV TRTVTNVAEE ETYVITARMA PAVAIETSPP AMTLRSGTSH
EFSVTLTVRS VTGTYSFGEV LLKGSRGHKV RIPVVAMGYD R
//
