GenomeNet

Database: UniProt
Entry: Q7RQ80_PLAYO
LinkDB: Q7RQ80_PLAYO
Original site: Q7RQ80_PLAYO 
ID   Q7RQ80_PLAYO            Unreviewed;      1225 AA.
AC   Q7RQ80;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   02-DEC-2020, entry version 92.
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.
CC       {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AABL01000318; EAA20512.1; -; Genomic_DNA.
DR   EnsemblProtists; EAA20512; EAA20512; EAA20512.
DR   EuPathDB; PlasmoDB:PY01222; -.
DR   InParanoid; Q7RQ80; -.
DR   OMA; EYSTWNL; -.
DR   Proteomes; UP000008553; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.200; -; 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   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF18513; Pro_sub2; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; SSF52743; 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|RuleBase:RU003355};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003355,
KW   ECO:0000313|EMBL:EAA20512.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008553};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU003355}; 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="Pro_sub2"
FT                   /evidence="ECO:0000259|Pfam:PF18513"
FT   DOMAIN          692..942
FT                   /note="Peptidase_S8"
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..584
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          600..620
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        86..103
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..152
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..177
FT                   /note="Acidic"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..225
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..240
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..469
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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
//
DBGET integrated database retrieval system