ID W7JH37_PLAFA Unreviewed; 689 AA.
AC W7JH37;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=subtilisin {ECO:0000256|ARBA:ARBA00023619};
DE EC=3.4.21.62 {ECO:0000256|ARBA:ARBA00023619};
GN ORFNames=C923_01054 {ECO:0000313|EMBL:EWC78277.1};
OS Plasmodium falciparum UGT5.1.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=1237627 {ECO:0000313|EMBL:EWC78277.1, ECO:0000313|Proteomes:UP000030697};
RN [1] {ECO:0000313|EMBL:EWC78277.1, ECO:0000313|Proteomes:UP000030697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UGT5.1 {ECO:0000313|EMBL:EWC78277.1,
RC ECO:0000313|Proteomes:UP000030697};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium falciparum UGT5.1.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity for peptide
CC bonds, and a preference for a large uncharged residue in P1.
CC Hydrolyzes peptide amides.; EC=3.4.21.62;
CC Evidence={ECO:0000256|ARBA:ARBA00023529};
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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DR EMBL; KE124447; EWC78277.1; -; Genomic_DNA.
DR AlphaFoldDB; W7JH37; -.
DR MEROPS; S08.012; -.
DR EnsemblProtists; EWC78277; EWC78277; C923_01054.
DR Proteomes; UP000030697; 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; cd07473; Peptidases_S8_Subtilisin_like; 1.
DR Gene3D; 3.30.70.2380; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR017314; Pept_S8A_PfSUB_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; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034204; PfSUB1-like_cat_dom.
DR InterPro; IPR041089; SUB1_ProdP9.
DR PANTHER; PTHR42884:SF14; NEUROENDOCRINE CONVERTASE 1; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF18213; SUB1_ProdP9; 1.
DR PIRSF; PIRSF037900; Subtilisin_rel_PfSUB_1; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 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:UP000030697};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..689
FT /note="subtilisin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004894521"
FT DOMAIN 139..218
FT /note="SUB1 protease prodomain ProdP9"
FT /evidence="ECO:0000259|Pfam:PF18213"
FT DOMAIN 367..640
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 99..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 373
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 429
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 607
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 689 AA; 77761 MW; 461003321F7F7CF9 CRC64;
MMLNKKVVAL CTLTLHLFCI FLCLGKEVRS EENGKIQDDA KKIVSELRFL EKVEDVIEKS
NIGGNEVDAD ENSFNPDTEV PIEEIEEIKM RELKDVKEEK NKNDNHNNNN NNNISSSSSS
SSNTFGEEKE EVSKKKKKLR LIVSENHATT PSFFQESLLE PDVLSFLESK GNLSNLKNIN
SMIIELKEDT TDDELISYIK ILEEKGALIE SDKLVSADNI DISGIKDAIR RGEENIDVND
YKSMLEVEND AEDYDKMFGM FNESHAATSK RKRHSTNERG YDTFSSPSYK TYSKSDYLYD
DDNNNNNYYY SHSSNGHNSS SRNSSSSRSR PGKYHFNDEF RNLQWGLDLS RLDETQELIN
EHQVMSTRIC VIDSGIDYNH PDLKDNIELN LKELHGRKGF DDDNNGIVDD IYGANFVNNS
GNPMDDNYHG THVSGIISAI GNNNIGVVGV DVNSKLIICK ALDEHKLGRL GDMFKCLDYC
ISRNAHMING SFSFDEYSGI FNSSVEYLQR KGILFFVSAS NCSHPKSSTP DIRKCDLSIN
AKYPPILSTV YDNVISVANL KKNDNNNHYS LSINSFYSNK YCQLAAPGTN IYSTAPHNSY
RKLNGTSMAA PHVAAIASLI FSINPDLSYK KVIQILKDSI VYLPSLKNMV AWAGYADINK
AVNLAIKSKK TYINSNISNK WKKKSRYLH
//
