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
//
