ID A0A059CUE1_EUCGR Unreviewed; 707 AA.
AC A0A059CUE1;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KCW81560.1};
DE Flags: Fragment;
GN ORFNames=EUGRSUZ_C02918 {ECO:0000313|EMBL:KCW81560.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW81560.1};
RN [1] {ECO:0000313|EMBL:KCW81560.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW81560.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; KK198755; KCW81560.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059CUE1; -.
DR STRING; 71139.A0A059CUE1; -.
DR MEROPS; S08.006; -.
DR EnsemblPlants; KCW81560; KCW81560; EUGRSUZ_C02918.
DR Gramene; KCW81560; KCW81560; EUGRSUZ_C02918.
DR eggNOG; ENOG502QPQR; Eukaryota.
DR InParanoid; A0A059CUE1; -.
DR OMA; NERYANT; -.
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; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-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:SF838; OS02G0665300 PROTEIN; 1.
DR PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR Pfam; PF17766; fn3_6; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 6..87
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 110..544
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 337..423
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 618..706
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 119
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 180
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 504
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KCW81560.1"
FT NON_TER 707
FT /evidence="ECO:0000313|EMBL:KCW81560.1"
SQ SEQUENCE 707 AA; 75527 MW; 17E193FA51A9F051 CRC64;
TSDLQTYIVH VTPPDGQRLS ELKDLESWYY SFLPTDSTTS RNERRLLYSY QNVMTGFAAR
LTPDEVATMQ DKPGFVAAHP EQIYSLQTTH SPQFLGLPLS QGSSNSSTMG KGIIIGIMDT
GVTPDHPSFS GDGMPPPPAK WKGRCDFKPS QCNNKLIGAK TFDSSAKKNV TMPPTDDVGH
GTHTASTAAG ASVQQANTLR MAEGTAGGMA PYAHLAIYKV CFTTSCFLGD ILAGLDAALA
DGVDVISISI GGGSAPFYMD GIAVATFAAV QRGIFVSCSA GNSGPFSESL SNEAPWILTV
GASTIDRNIV SNAKLGNGEE YEGETIYQPS FPSTLLPLVY PGIDGTEGSV YCVPGQLKSS
QVEGKIVLCE RGFVGRYFQA IEVKRAGGAG MIMMNQEIDG FSTLADAYDL PASHVSYFAG
NKIKAYINAT RTPTATIMFK GTVFGNPTAP ALTSFSSRGP SLISPGILKP DIIGPGVNIL
AAWPFPIRND TKAKYYFNII SGTSMSCPHL SGIAALIKGI HPDWSPATIK SAIMTTAKQL
NVKQNPILDE RLQPADVFAI GAGHVDPAKA IDPGFIYDMH PNDYIPYLCG LGYTDKQVAT
IAHKPVKCSG VSSIPEGELN YPSFSVNLGP PQTFTRTVTN VGTDYSPYVV TVVPPQGVHV
TVKPNKLNFS KLNQKATYSI TLSRANSTQD VAKFTQGFLR WDSKKYS
//