ID B8LLN6_PICSI Unreviewed; 522 AA.
AC B8LLN6;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Picea sitchensis (Sitka spruce) (Pinus sitchensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX NCBI_TaxID=3332 {ECO:0000313|EMBL:ABR16566.1};
RN [1] {ECO:0000313|EMBL:ABR16566.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Green portion of the leader tissue
RC {ECO:0000313|EMBL:ABR16566.1};
RA Ralph S.G., Chun H.E., Liao N., Ali J., Reid K., Kolosova N., Cooper N.,
RA Cullis C., Jancsik S., Moore R., Mayo M., Wagner S., Holt R.A.,
RA Jones S.J.M., Marra M.A., Ritland C.E., Ritland K., Bohlmann J.;
RT "Full length cDNA sequences from Sitka Spruce (Picea sitchensis).";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; EF676680; ABR16566.1; -; mRNA.
DR AlphaFoldDB; B8LLN6; -.
DR OMA; DTGNLCY; -.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; 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; 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 PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR PANTHER; PTHR10795:SF542; SUBTILISIN-LIKE PROTEASE SBT1.5; 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.
PE 2: Evidence at transcript level;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..522
FT /note="Peptidase S8/S53 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002876940"
FT DOMAIN 36..115
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 138..518
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 377..443
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT REGION 210..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 522 AA; 55595 MW; D4407D616C7AC7A3 CRC64;
MVYRMEINKA CHALFFMIVS LALWVPSSDA LGARQSYIIY MDKSMMPDHF SLHQHWYSSM
IKEVSGSNSD PTALLYTYDT VTHGFAACLT STEAQAMENM DGCLSVFQDS TYGLHTTRTP
DFLGLSSSHG LWPLSRYGDD IIVGVLDTGI WPESKSFNDQ GLTPVPARWK GECEVGTEFN
ASHCNNKLIG ARYFLKGYEA KFGRIDEKED YRSPRDADGH GTHTSSIAAG SEVPGSSLLG
FATGTARGIA TKARVAVYKV CWGSCLGSDM LAAMEAAVAD GVDLLSISIA SRAIVPYYDD
MIAIGALGAI QKGVFVSCSA GNEGPIYSAI FNTAPWITTV GASTIDREFP APVVLGNGQN
YRGSSLYKGE PVGNEQLPLV YGKTASRNET ANLCLAGSHD PKMVSGKIVL CDLGGITAEK
ALVVQQAGGA GLILANGPAD GEDLLTECDS FSSTTVGAKS AEDIKAYINN TRNPRATIKE
EGLTVLGKAR APVVAALSSR GPNPVVPEIL KPDRIAPAST YF
//
