ID Q7RQ80_PLAYO Unreviewed; 1225 AA.
AC Q7RQ80;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=subtilisin {ECO:0000256|ARBA:ARBA00023619};
DE EC=3.4.21.62 {ECO:0000256|ARBA:ARBA00023619};
GN ORFNames=PY01222 {ECO:0000313|EMBL:EAA20512.1};
OS Plasmodium yoelii yoelii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=73239 {ECO:0000313|EMBL:EAA20512.1, ECO:0000313|Proteomes:UP000008553};
RN [1] {ECO:0000313|EMBL:EAA20512.1, ECO:0000313|Proteomes:UP000008553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17XNL {ECO:0000313|EMBL:EAA20512.1,
RC ECO:0000313|Proteomes:UP000008553};
RX PubMed=12368865; DOI=10.1038/nature01099;
RA Carlton J.M., Angiuoli S.V., Suh B.B., Kooij T.W., Pertea M., Silva J.C.,
RA Ermolaeva M.D., Allen J.E., Selengut J.D., Koo H.L., Peterson J.D., Pop M.,
RA Kosack D.S., Shumway M.F., Bidwell S.L., Shallom S.J., van Aken S.E.,
RA Riedmuller S.B., Feldblyum T.V., Cho J.K., Quackenbush J., Sedegah M.,
RA Shoaibi A., Cummings L.M., Florens L., Yates J.R., Raine J.D., Sinden R.E.,
RA Harris M.A., Cunningham D.A., Preiser P.R., Bergman L.W., Vaidya A.B.,
RA van Lin L.H., Janse C.J., Waters A.P., Smith H.O., White O.R.,
RA Salzberg S.L., Venter J.C., Fraser C.M., Hoffman S.L., Gardner M.J.,
RA Carucci D.J.;
RT "Genome sequence and comparative analysis of the model rodent malaria
RT parasite Plasmodium yoelii yoelii.";
RL Nature 419:512-519(2002).
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}.
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:EAA20512.1}.
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DR EMBL; AABL01000318; EAA20512.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7RQ80; -.
DR STRING; 73239.Q7RQ80; -.
DR PaxDb; 73239-Q7RQ80; -.
DR EnsemblProtists; EAA20512; EAA20512; EAA20512.
DR VEuPathDB; PlasmoDB:Py17XNL_000900155; -.
DR InParanoid; Q7RQ80; -.
DR OMA; EYSTWNL; -.
DR Proteomes; UP000008553; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.2370; -; 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; 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; IPR040935; Pro_sub2.
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; PF18513; Pro_sub2; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000008553};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1225
FT /note="subtilisin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004290750"
FT TRANSMEM 1082..1106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 496..583
FT /note="Subtilisin-like protease 2 prodomain"
FT /evidence="ECO:0000259|Pfam:PF18513"
FT DOMAIN 692..942
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 82..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 564..620
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 86..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..177
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 700
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 743
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 906
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1225 AA; 140862 MW; 124D5AC42B8D49DF CRC64;
MLRTFYVLSL MLIEFILHKG QYNKHICSKN LKKYNFVGKK HRILASIIED REKQVEDITD
GYKPIFNIYE ISAAFHKKKD IADKKKRRRY GNQQSIENRR IAEENERRLS NQLDDIQFIE
LSNKYPNIGK QNSQQNKVNK INNQNGASNS NDNIRNDEDE DEGEDEDEDD DLIEGRKDNL
EEDDLVEKNG ANLKRGNMHG QEEKNKNINT TPGNENNSKN VNDNKKSGIS LKDKIDNNEQ
HNSGLKGTTK YLDDNIKTYT FDHYKLITNS DNILNDIKVD ASDISKLSIN SLSIEYNEVN
KTEYTHQRHI VLTNKGNRRY KIFLMTKNPK FTKTEDIEEP EMSFIQTETG ENTNEKEDEE
NYLNENLYSG FGTIDYENGY SKKKKKINSE HASELNDKIS NSQNIEKSDS HENEKYNHGF
IGKIQSFFSF LSIPSSKKDD SIGSEKKSEE RNNVDSKPKL NKKPNDTAKK NNSNKILTVD
KVTDQYLLNL KNKNMKEQEL IFIFHGDLDL HSKKMKTIIN EANVKFTKYI NMHFKDVKNI
RYDISSPINF VCFFIPIIFD MSNLKILKEA LIILHNELKN YIDNWNFSNT YIAFDTDYEN
EDIDNAMNKL NENMKKYIKK PKKLYNIKYS FLRKMWGLES IFSLSKNRNQ KNAGIEEKIL
NALPKELKEY STWNLSFIRV FNAWLLSGYG NKNVKICVID SGVDKNHIDL AKNIYTPKYS
DRYEMTDDFF DFMVKNPIDT SGHGTHVSGI AAASANSLGM VGVAPDVNLI SLRFIDGDSY
GGSFHVIKAI NVCILNKSPI INASWGSRNY DTNMFLAIER LKYTFKGKGT VFIAAAGNEN
KNNDLYPIYP ASYKLPNVYS VGSINKFLQI SPFSNYGANS VHILAPGHHI YSTTPMNTYK
MNTGTSMAAP HVSGVAGLIY SVCHKQGFIP ESDEVLDIIT RTSIKIVSKD KKTIHNSLIN
AEAAVLTTLL GGLWMQMDCH FAKFYLNKDQ QKNIPVVFSA YKDGMYESDI IIGIQPEDSN
SKEYGEIVIP IKILTNPKLK NFNLSPRVGK KIHIDANESN DDILSYICEN ALYNLYEHDN
SFLISSLILF FIGIILIALA SIVFFLKHHQ SKQRDAEKYM HQKMVDRAHG IKYNFKDAGA
DGIKRINTMD DNINNHRNTQ RFTIVQNEDN MYVLKKKSSI QAKYEPRNEL VKRPLVKRPI
VKHADINVNF KNIDELYEPQ NNSPE
//
