ID A0A218WDB2_PUNGR Unreviewed; 761 AA.
AC A0A218WDB2;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Subtilisin-like protease SBT1.9 {ECO:0008006|Google:ProtNLM};
GN ORFNames=CDL15_Pgr014537 {ECO:0000313|EMBL:OWM70864.1};
OS Punica granatum (Pomegranate).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Lythraceae; Punica.
OX NCBI_TaxID=22663 {ECO:0000313|EMBL:OWM70864.1, ECO:0000313|Proteomes:UP000197138};
RN [1] {ECO:0000313|Proteomes:UP000197138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Dabenzi {ECO:0000313|Proteomes:UP000197138};
RX PubMed=28654223; DOI=10.1111/tpj.13625;
RA Qin G., Xu C., Ming R., Tang H., Guyot R., Kramer E.M., Hu Y., Yi X.,
RA Qi Y., Xu X., Gao Z., Pan H., Jian J., Tian Y., Yue Z., Xu Y.;
RT "The pomegranate (Punica granatum L.) genome and the genomics of
RT punicalagin biosynthesis.";
RL Plant J. 91:1108-1128(2017).
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:OWM70864.1}.
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DR EMBL; MTKT01004609; OWM70864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218WDB2; -.
DR Proteomes; UP000197138; 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; 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:SF514; SUBTILISIN-LIKE PROTEASE; 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};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 31..114
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 138..579
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 652..753
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 147
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 218
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 538
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 761 AA; 81465 MW; C262939E48EF4895 CRC64;
MAKVFGDFSL LFLFFLTASI VFTFSLAERS TYIVHMDKSF MPKAFRSHHN WYSSMVGSLG
SIASGNNRRS SPSLLYSYDT VVHGFSAVVS PAELETLKRS PGFVSAYPDR NVTVDTTHTF
EFLGLSPSMG LWPASGYGKD VIVGVIDSGV WPESESYKDD GMTQVPSRWK GKCEVGQEFN
SSMCNLKLIG ARYFNKGVTA ANPGIKISMN SARDTEGHGT HTSSTVAGNY VKGATFFGYA
EGTARGVAPR ARIAMYKVLW DEGRYASDVL AGMDQAVADG VDVISISMGF DGVPIYEDPV
AIASFGAMAK GIIVSSSAGN DGPALGTLHN GIPWILTVAA GTIDRTFAGT LVLGNGMTII
GWTMFPASAI VNSFPLIYNE SLSACNSSKL LSKAPNGIIL CKDIGSLRQQ IDSITESNLL
GAIFVSDYDE PFELGGMTCP GVVISSKDSP SVIKYAKTVR EPVASIKFQQ TIVGTKPAPA
TAFYTSRGPS PYNIGIAKPD VMAPGSLVLA SWIPNGYAAQ LGANVFLSSK FTMISGTSMA
CPHASGVAAL LKAAHPEWSP AAIRSAIMTT ADPYDNTFSP VRDNGRDFEP ASPLAMGAGH
INPNLAMNPG LVYDATPEDY VNLLCSMNLT EKQILVITRS SGQYNCSTPS HDLNYPSFFV
SYSNKTETMV RNFHRTVTNV GNGPATYTVE VAAPKGSIVE VYPKKLVFGQ TNEKQSYSVS
VKYKRDEKGK VSFGSLVWVD GAGKYGVRSP IVISPTLKFQ K
//
