ID A0A1U8B8U6_NELNU Unreviewed; 1082 AA.
AC A0A1U8B8U6;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Subtilisin-like protease SBT4.14 {ECO:0000313|RefSeq:XP_010272744.1};
GN Name=LOC104608439 {ECO:0000313|RefSeq:XP_010272744.1};
OS Nelumbo nucifera (Sacred lotus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010272744.1};
RN [1] {ECO:0000313|RefSeq:XP_010272744.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_010272744.1; XM_010274442.1.
DR AlphaFoldDB; A0A1U8B8U6; -.
DR GeneID; 104608439; -.
DR KEGG; nnu:104608439; -.
DR eggNOG; ENOG502QRA7; Eukaryota.
DR InParanoid; A0A1U8B8U6; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000189703; Unplaced.
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; 2.
DR CDD; cd04852; Peptidases_S8_3; 1.
DR Gene3D; 2.60.40.2310; -; 2.
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; 2.
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:SF541; SUBTILISIN-LIKE PROTEASE SBT4.14; 1.
DR Pfam; PF17766; fn3_6; 2.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 2.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 2.
DR PROSITE; PS51892; SUBTILASE; 2.
DR PROSITE; PS00138; SUBTILASE_SER; 2.
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:UP000189703};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 6..75
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 98..539
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 610..706
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT DOMAIN 809..921
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 980..1079
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 106
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 170
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 499
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1082 AA; 116026 MW; 95D55FD983912DB8 CRC64;
MGQLPHHQPV DVPESHHKIL TDALGSSEVA KERIMHSYTR SFNGFVANLT EDEARKLSET
EGVVSVFKSG KHKLHTTKAW DFLGFSDLLV KRDRVVESNI IVGVLDSGIN MQSECFSDTN
LGPPPAKWKG TCGPFDDFTC NKKIIGARWF KVDKNIPAPD VASPVDYRGH GSHTASIIAG
RVVEGANFFG LAAGDARGAV PSARIAVYKV CYVDGYCSDE DILAAFDHAI ADGVDIINLS
VGEDPGYSVT DAIAIGSFHA MQKRILTIAS AGNDGPLEGS VVNFSPWMLT VGATTTDRQF
MTRVVLDNGN NLTGISVNTF DMANSMYPLI RGSDAVSLEG TSVMLASRCV EGSLNVTLIK
DKIVFCLTIG GPGKAGEIIS EGGGSGAIMQ VSDIADTPEV FSLPVTVLGE VDGKVLSDYI
ENTQNPQATI YKSEEIQIPA PFVASFSSRG PNPVYQNILK PDLVAPGKHI LAASTLKTSV
TGKPNDKRFS NFLLRSGTSM AAPFAAGAAA YIKSLHPTWS PAAIKSALMT TTKAVNMSFE
YAKLRDFAYG AGQIDPLRAA DPGLVYDLNE KSYVKFLCNL FGPSSIVNKF YGAYSLVNCS
TYAPPSGRDD LNYPSILFPI RNRKKPSEAV YWRTVTNVDN GPAEYTATVL APAGVEIIVE
PLTLKFSRQY ENQIFKVTVR VPASNVPPYV LSASLEWKDN VHTILSMFKY DRSPVSDVCN
CYDRAMDPEK VKGKLVYCED FVGSADYSVQ KMGGVGTILE SDNAIFDAAF IFMPPSTMVN
HNQGKIIMDY INSTSSPKAV IFKTQAFKVA APSVASFSSR GPNPVSNKVL KPDIAAPGTN
ILAAYTGIVS ISGWPDDDRF SNFITMSGTS MATPHISGVA AYVKSMHPTW SPAAIKSAIM
TTATPMSSTV NPEAEFAYGA GQVNPLKAVS PGLVYDMDEM QYIEFLCTEG YSGTALGMII
GSNPLDCSSP PSSEAGQDAL NYPTMQLTVD GATEPVTGVF RRTVTNVGLA DSIYTATINA
APGVEITVEP MTLSFSSIGE TQSFIVSVKA KPKNDESILS GSSLVWSDSV HTVRSPIVIY
YP
//
