ID A0A0Y9WPD8_PLABE Unreviewed; 1644 AA.
AC A0A0Y9WPD8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Petidase, M16 family, putative {ECO:0000313|EMBL:CXI43691.1};
GN ORFNames=PBK173_000206800 {ECO:0000313|EMBL:CXI43691.1},
GN PBNK65E_000198900 {ECO:0000313|EMBL:SCN25404.1}, PBNK65NY_000198100
GN {ECO:0000313|EMBL:SCM22375.1}, PBSP11A_000197900
GN {ECO:0000313|EMBL:SCO62143.1}, PBSP11RLL_000197800
GN {ECO:0000313|EMBL:SCO60384.1};
OS Plasmodium berghei.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5821 {ECO:0000313|EMBL:CXI43691.1, ECO:0000313|Proteomes:UP000069549};
RN [1] {ECO:0000313|EMBL:CXI43691.1, ECO:0000313|Proteomes:UP000069549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K173 {ECO:0000313|EMBL:CXI43691.1,
RC ECO:0000313|Proteomes:UP000069549}, NK65 ny
RC {ECO:0000313|EMBL:SCM22375.1, ECO:0000313|Proteomes:UP000516480},
RC NK65e {ECO:0000313|EMBL:SCN25404.1,
RC ECO:0000313|Proteomes:UP000220214}, SP11 Antwerpcl1
RC {ECO:0000313|EMBL:SCO62143.1, ECO:0000313|Proteomes:UP000219860}, and
RC SP11 RLL {ECO:0000313|EMBL:SCO60384.1,
RC ECO:0000313|Proteomes:UP000219974};
RG Pathogen Informatics;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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DR EMBL; LT160029; CXI43691.1; -; Genomic_DNA.
DR EMBL; LT608145; SCM22375.1; -; Genomic_DNA.
DR EMBL; LT614635; SCN25404.1; -; Genomic_DNA.
DR EMBL; LT608273; SCO60384.1; -; Genomic_DNA.
DR EMBL; LT608257; SCO62143.1; -; Genomic_DNA.
DR VEuPathDB; PlasmoDB:PBANKA_0926500; -.
DR OMA; EFHKKCY; -.
DR Proteomes; UP000069549; Chromosome 9.
DR Proteomes; UP000219860; Chromosome 9.
DR Proteomes; UP000219974; Chromosome 9.
DR Proteomes; UP000220214; Chromosome 9.
DR Proteomes; UP000516480; Chromosome 9.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 1.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 3.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1644
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014242929"
FT DOMAIN 401..508
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT REGION 136..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1644 AA; 193365 MW; ADAB645F5CE0A950 CRC64;
MYFNIFIFLI ILIYENQSSC QNPIYNSKKN YGLSNEQFRA ILFGLNYDLP NKNNIDRENV
ENHSLFFRNF VDDDIQINKQ NEKTQSQIEI MNNEKIKSSD TIHDNKNVNN YSITSGNEKT
NDGLLQKTLR KNKLSEKDNS YNNTSTNINK NENSVFNEPT NANDYIRTKE DSNDFKPETL
QKNINVKNNK GNPNLLKDKK TNINENKTQG NINQNTRINK SVNDMTNELD NHIENFVKEG
NEMNNSNVQE KHQGKDLLHN NGNNKDTQMD HNDEPQILSN GKKKKNTKYI SMNPRAIKHK
EENVNYSPKK IISGLPNSGN GVLKEIQPVK YNENINKKLN DASKGNENLQ KTTNTDENIF
SENITLKNIT NDTNYYKYFK LKENGFRGLG IINKYSSKGC FSISVDCGRY NDLDDIPGIS
NLLQRAIFYK SKKRDTTLLS ELGVNSSKYN SHINESFTNF YASGNSEDIY YLLNLFVQNL
FYPIFNEESI ENEVNEISNK YISMENNPET CIKITSQYLT HFKYSNFFIY GNYITLCENI
LKKKIDIKKK LYEFHRKCYQ PKNMSISILL GKRSNSSDHY NINDIMNMVV QFFGKIKNYN
YEENDIKKQN NMKLEENLSN RQVNNYNNRI FTYNDAQINL NEEINNKNDM SIPFINKLKY
ALDLNQKSKY IEILKKEGWE NQIFLYWSSK INIYIYKKIE EFKVMRFFRE LFSNFRKDGL
YYKISVENEY AYDFQIINIC NKYYLNYGIL IKLTEKGKSN IAHLIYIFQT FINEISKLFD
HDSLNKGVNK YILDYYRETT LTTNINFRKD GINICLNDLI NYSNTLLIYL ENPLEFLTNN
NLVENVNKNG FRNEIKITSL IGSLIRNENM HIINVVDKFT ITNQIRIPNT SIEYSIGDNP
YIIDEGKITN NINFTFPEFK ICPFSNFKKN AILNENSFFC VSYNSKENFN YSKSNKQTFV
SDDNEYVKSS ILYNIPCLIK SSYGYNIFFK KGLTETSRVN ADFIFFFPSK NFTFYEAIFT
RIHIIILKKK IKQMLSDYTN CSVNVNIKDN VESYILHVDS NSYYFGDMLN KIEDLLSIKE
VPTSDEFNYA YDELNLYVKR KDNVVVGDSL NIIHSLFNKY IPTNKEIYDI LNAYFFYPLY
NSYIKYINNF FHKNYINIFI YGNLSIPNEI NIKNETNYGI NTEYNSTNSV INNNNGVNYN
TYSYINNTYT MYNKHALGKG DNMLEDKEEN IHEEYKENSI EILQNGIGIK YIIDLCESFI
RNVTNNVIRK SESTYYATKL INNEDIEIDI QIPDKNVGNS SITVSYIIES ETILSDMLIN
IIVDLISSDF IKFAKIKYND GYTVDVKTLS TKYGFGGIIF VIQSFDNDVE KLEEDICGFV
KHLTFQLMNI DIYDLVKKMQ YMKKQYILNN TIFTFNQEYS TILDEIINGN ECFDKKYKIV
KIFDELINCP KIILNKANYI LQNAKKLIFK EYKTSNAPNN VNEQMNYIYS NKRCNYSHNK
NDILSNIELS NTVNFTKATT LNNGVPNYNV FRMNNMHKNW NYIINVSNFL EIKRKGFVQY
VIDYFKNPYK LSLNHNNYLD YKSCDDEMHK DNFHVFHNFI NDINEIREYF LAKFSNDQEN
KEKCSINYEE IKKHCYEVNA RMYG
//
