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Database: UniProt
Entry: A0A509AID5_PLABA
LinkDB: A0A509AID5_PLABA
Original site: A0A509AID5_PLABA 
ID   A0A509AID5_PLABA        Unreviewed;      1230 AA.
AC   A0A509AID5;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   02-DEC-2020, entry version 9.
DE   RecName: Full=Subtilisin {ECO:0000256|ARBA:ARBA00023619};
DE            EC=3.4.21.62 {ECO:0000256|ARBA:ARBA00023619};
GN   ORFNames=PBANKA_0911700 {ECO:0000313|EMBL:VUC55658.1};
OS   Plasmodium berghei (strain Anka).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX   NCBI_TaxID=5823 {ECO:0000313|EMBL:VUC55658.1, ECO:0000313|Proteomes:UP000074855};
RN   [1] {ECO:0000313|EMBL:VUC55658.1, ECO:0000313|Proteomes:UP000074855}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ANKA {ECO:0000313|EMBL:VUC55658.1,
RC   ECO:0000313|Proteomes:UP000074855};
RX   PubMed=25359557; DOI=10.1186/preaccept-1233682211145405;
RA   Otto T.D., Bohme U., Jackson A.P., Hunt M., Franke-Fayard B.,
RA   Hoeijmakers W.A., Religa A.A., Robertson L., Sanders M., Ogun S.A.,
RA   Cunningham D., Erhart A., Billker O., Khan S.M., Stunnenberg H.G.,
RA   Langhorne J., Holder A.A., Waters A.P., Newbold C.I., Pain A., Berriman M.,
RA   Janse C.J.;
RT   "A comprehensive evaluation of rodent malaria parasite genomes and gene
RT   expression.";
RL   BMC Biol. 12:86-86(2014).
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}.
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DR   EMBL; LK023124; VUC55658.1; -; Genomic_DNA.
DR   OMA; EYSTWNL; -.
DR   Proteomes; UP000074855; Chromosome 9.
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:VUC55658.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000074855};
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..1230
FT                   /note="Subtilisin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5021449794"
FT   TRANSMEM        1087..1111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          501..588
FT                   /note="Pro_sub2"
FT                   /evidence="ECO:0000259|Pfam:PF18513"
FT   DOMAIN          697..931
FT                   /note="Peptidase_S8"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   REGION          144..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          392..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          93..113
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          569..589
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          605..625
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        144..162
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..183
FT                   /note="Acidic"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..214
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..247
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..470
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1230 AA;  141325 MW;  00C86E6504E07827 CRC64;
     MLRTFYVLSL MLIEFILHNG QYNKHICSKN SKKYNFVGKK HRILVSDIED RENHIEGIAD
     IYKPIFNIYE ISAEFHKKKN IADKKKKRKY GINQSIEKRR IAEENERRQL NKTEGTQFLE
     LSNRYPNIGK QNSQQNKVNE INNQNAASNS NDNIGNDNIG NDNIGNDEDD DEDDDEDLIE
     GRKDNLEEDD LIEKNDSNLP RGKMHEKEEK NKNINTTPGN ESSNKNVNDK KKNGISLKDK
     IDNKQNNGGL KEKGNNLDDN IKTYTFDHYK IITNSDNILN DIKVDASDIS KLSINSINIE
     YNEKNKAEYT HQRHIVLSNN GNRRYKIFLM TKNPKFTKTE DIEEPGMSFI QTETGENEDE
     KEDEENYLNE NLYSGFGTID YENDYSKKKK KIESEHASGL NDKISNSQNI EKSGSHENEK
     YNHGYIEKIR SFFSFLSMPS SKKDDSIGSE KKTEERSNTD SKAKLNKKTN DMAKKNNSNA
     FLSVDKIIDQ YLLNLKNKNM KEQELIFIFH GNLDLHSKEM KTVINEANAK FTKYINMHFK
     DVKNIRYDIS SPINFVCFFI PIIFDMSNLK ILKEALIILN NELKDYIDNW NFSNTYVAFD
     NNYENEDIDN VMNKLNENME KYIKKPKKLY NIKYSFLRKI WGLKSIISLS KNQDKKDAEI
     EEKILSALPK ELKEYSTWNL SFIRVFNAWL LSGYGNKNVK ICVIDSGIDK NHIDLANNIY
     TPKYSDRYEM TDELFDFMVK NPIDTSGHGT HVSGIAAASA NSLGMVGVAP NINLISLRFI
     DGDNYGGSFH VIKAINICIL NKSPIINASW GSRNYDTNMF LAIERLKYTF KGKGTVFIAA
     AGNENKNNDL YPIYPASYKL QNVYSVGSIN KFLQISPFSN YGANSVHILA PGHHIYSTTP
     MNTYKMNTGT SMAAPHVSGV AGLIYSVCYK QGFIPDADEV LEIITRTSIK IVSKDKKTIH
     NSLINAEAAV LTTLLGGLWI QMDCHFAKFY LNENKQKSVP IVFSAYKDGV YESDIIIGIQ
     PEDANSKEYG EIVIPIKILT NPKLKDFSLS PRVGKKIRID ENESNDDILS YICENALYNL
     YEHDNSFLIS SLILFFIGII LIVLASIVFF LKHHQSKQRD GEKYMHQKMV DRTYNVKYNF
     KDSGTDGIKR INTLDDNINN HRNTQRFTIV QNEDNMYVLK KKSSIQAKYE PRNELVKRSL
     VKRPIVKHAD INVNFSNVDV LYEPKNNSSE
//
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