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Database: UniProt
Entry: B3L5H8_PLAKH
LinkDB: B3L5H8_PLAKH
Original site: B3L5H8_PLAKH 
ID   B3L5H8_PLAKH            Unreviewed;      1341 AA.
AC   B3L5H8;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   02-DEC-2020, entry version 67.
DE   RecName: Full=Subtilisin {ECO:0000256|ARBA:ARBA00023619};
DE            EC=3.4.21.62 {ECO:0000256|ARBA:ARBA00023619};
GN   ORFNames=PKNH_0935100 {ECO:0000313|EMBL:CAA9988395.1};
OS   Plasmodium knowlesi (strain H).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=5851 {ECO:0000313|EMBL:CAA9988395.1, ECO:0000313|Proteomes:UP000031513};
RN   [1] {ECO:0000313|EMBL:CAA9988395.1, ECO:0000313|Proteomes:UP000031513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H {ECO:0000313|EMBL:CAA9988395.1,
RC   ECO:0000313|Proteomes:UP000031513};
RA   Pain A., Boehme U., Berry A.E., Mungall K., Finn R., Jackson A.P.,
RA   Mourier T., Mistry J., Pasini E.M., Aslett M., Balasubrammaniam S.,
RA   Borgwardt K., Brooks K., Carret C., Carver T.J., Cherevach I.,
RA   Chillingworth T., Clarke T.G., Galinski M.R., Hall N., Harper D.,
RA   Harris D., Hauser H., Ivens A., Janssen C.S., Keane T., Larke N., Lapp S.,
RA   Marti M., Moule S., Meyer I.M., Ormond D., Peters N., Sanders M.,
RA   Sanders S., Sergeant T.J., Simmonds M., Smith F., Squares R., Thurston S.,
RA   Tivey A.R., Walker D., White B., Zuiderwijk E., Churcher C., Quail M.A.,
RA   Cowman A.F., Turner C.M.R., Rajandream M.A., Kocken C.H.M., Thomas A.W.,
RA   Newbold C.I., Barrell B.G., Berriman M.;
RT   "The genome of Plasmodium knowlesi strain H, a zoonotic malaria parasite
RT   with host range from monkey to man.";
RL   Nature 455:799-803(2008).
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; AM910991; CAA9988395.1; -; Genomic_DNA.
DR   RefSeq; XP_002259376.1; XM_002259340.1.
DR   EnsemblProtists; CAQ40149; CAQ40149; PKH_093480.
DR   GeneID; 7320840; -.
DR   Proteomes; UP000031513; Chromosome 9.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   CDD; cd07473; Peptidases_S8_Subtilisin_like; 1.
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; IPR034204; PfSUB1-like_cat_dom.
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   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003355};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003355,
KW   ECO:0000313|EMBL:CAA9988395.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031513};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU003355}.
FT   DOMAIN          623..710
FT                   /note="Pro_sub2"
FT                   /evidence="ECO:0000259|Pfam:PF18513"
FT   DOMAIN          850..1101
FT                   /note="Peptidase_S8"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
SQ   SEQUENCE   1341 AA;  153097 MW;  7901E5A0CC1269F6 CRC64;
     MLSLLYVLWL MLMNIFFQYD WHRKKILSEL GNYNVKLVKR KSRILSDSKT GRINFLDEIK
     ESYRPLFDVY ELSAKFEKLR NTKEKEEEKR GRQKQKQKKK KKKKKKNDHI EEEEQDKKTP
     SLNLIQLSST QSDETEHIKK RISKPFPIAL AHRRKPISIK KHAADSIHML NDGKSDKEGD
     ARMNVNNDAD VFTKLVNEGN IEDFGKLGED EQGETKERNL KSQSFQGDDT EEVNSVVKEG
     RHSNERKRED KNDDEDDQDV EGKADQETIQ KTDQRAEQEA NQRAVQETNQ REEQEANQRE
     EQEANQREEQ EADEESNQRA EQEANQREEQ EADEESNQRA EQEADEESNQ RAEQEADEEA
     DQEAEYELKE GENVAQQDII VQEFDHYKIV TNSHDILNDI YVDASDISKL SIGSINIAYS
     EQNKTSFTHQ RHIVLNNRGN KKYRVVLMTK NPKFTELEDE ESENAATNTF IEKEKVERKK
     TSDGHGEEDN DRTNLYGGKG TLDFSKAYRN NRKGSGRQVG NPNVEMYSAG DTSGGGIRGT
     INRLFSFLSF KGNPDESASG TDPSKDSGGR SGDNEDQKGN ANEGGNRHGS IPQDDRTHDL
     NEILSVDKLV DQYLLNLKNN TPDKQELILV LRGDLDLHSP YMKLVIKRSN AKFEQHIKRN
     FEQIDKIVYD ISSPINFLCF FVPTIFDMNN FHLLKEALMV LHKELERYME NWSFSNTYVT
     LDAPQIQGDG SGASADWRND SQKKDAPVEG GAGSQADHHG NDHAEGSQYR KGRKFIKKKK
     KLYNGKYSFL RKIWSFDTIS AFAAKMKKKN TDIENEILNF LPKELREYST WNLSVIRVFN
     AWFLAGYGNK NVKVCIIDSG IDKNHVDLMK NVYIPEYSEQ YEMTEDFYDF MVKNPTDSSG
     HGTHVTGIVG GVANGLGMVG VAPDVTLISL RFIDGVKYGG SFHAIKAINV CILNKTPIIN
     ASWGSNKYDA NIYLAVQRLK YTFNGKGTVL VTAAGNENKN NDEHPLYPSN FKLPHVYSVA
     SISKNFEISP FSNYGVKSVH IMAPGHHIYS TTPNNSYKIN TGTSMAAPHV CGVNALIYSV
     CYNQGFIPSA EEVLDILTRT AIKIISRRRR TINDSLVNAE AAVLTTLLGG LWMQMDCHFV
     KFNLESGKKK HIPVVFSAYK KGIYETDIVI AVISTEENSN VYGEILIPIR IVTDPKVDNF
     KESPRTGKKM IIDENEASHD EVLSYICENA LYNLYEMDSN FLVTSLVLFF VAFILMVVGT
     IIFIKRKRHS KYCDDEDHYH NILRSSVLEQ HHILGNTTNQ QLEVAKRNHA EKMRHSVRFS
     LLMGKQNACL FKERASQRLN F
//
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