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Database: UniProt
Entry: A0A1Y1JJ66_PLAGO
LinkDB: A0A1Y1JJ66_PLAGO
Original site: A0A1Y1JJ66_PLAGO 
ID   A0A1Y1JJ66_PLAGO        Unreviewed;      2294 AA.
AC   A0A1Y1JJ66;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Histone deacetylase 2 {ECO:0000313|EMBL:GAW80503.1};
GN   ORFNames=PGO_080670 {ECO:0000313|EMBL:GAW80503.1};
OS   Plasmodium gonderi.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=77519 {ECO:0000313|EMBL:GAW80503.1, ECO:0000313|Proteomes:UP000195521};
RN   [1] {ECO:0000313|Proteomes:UP000195521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 30045 {ECO:0000313|Proteomes:UP000195521};
RA   Arisue N., Honma H., Kawai S., Tougan T., Tanabe K., Horii T.;
RT   "Plasmodium gonderi genome.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the inositol phosphokinase (IPK) family.
CC       {ECO:0000256|ARBA:ARBA00007374}.
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:GAW80503.1}.
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DR   EMBL; BDQF01000009; GAW80503.1; -; Genomic_DNA.
DR   EnsemblProtists; GAW80503; GAW80503; PGO_080670.
DR   OMA; AWLYLCC; -.
DR   OrthoDB; 124800at2759; -.
DR   Proteomes; UP000195521; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0032958; P:inositol phosphate biosynthetic process; IEA:InterPro.
DR   CDD; cd09992; HDAC_classII; 1.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 3.
DR   Gene3D; 3.30.470.160; Inositol polyphosphate kinase; 1.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR005522; IPK.
DR   InterPro; IPR038286; IPK_sf.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR10625:SF4; HISTONE DEACETYLASE 6, ISOFORM G; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR   Pfam; PF00850; Hist_deacetyl; 3.
DR   Pfam; PF03770; IPK; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 2.
DR   SUPFAM; SSF56104; SAICAR synthase-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000195521};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          505..607
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   DOMAIN          787..898
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   DOMAIN          1050..1173
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          80..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          205..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          901..1040
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1366..1390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1918..1951
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..112
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..221
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..341
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        922..948
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        949..994
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1008..1025
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1026..1040
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1371..1390
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1918..1942
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2294 AA;  265478 MW;  276ED9C17F838B69 CRC64;
     MKNETTYNEN ISDNKQSSLK QDTIARLKLP DKRAYFNNFI IEKFNSISDI SLYLRGTNNI
     DENANEEEQD DLYLGGYNTV ANDDHERSPN LRSANGRSNR IGDKRMRGGR MRSGSVRSDS
     VITSSIRRDR VRSRNVRSNS MRSSIVGNKK NSDMNRITSN HVSDNHVISN RISSNHISSN
     HISSNHISNN RVRRSLDSYP QVTVNRSFSS PSLTKRSWSD QTSSNSKRKK LESNAEGRRQ
     KKLETKNTSR KKNNTGRGKE HKKRRSRSDI SQGDRRKKKK KKSNEKREIR NVKQGLGIRN
     NIINKNTSKG KNKVVNNFSI RKNRQMKRSQ HSSTSSNNDD EFNANKRILD KIFLSLKRKG
     NTNEYINNSF YIECDDILEI DSDMEEDTDV EPSIHDAPDG GPNTYAEAIV PYNPVKPNKN
     LHLTEEDFYS ISKSSSKMNK EREAIDNFYK YKPIQHRKNH DLSEVKNGKI FSSPKNCNQS
     VEYDCIGFVC DEEYMCQNLH FDENHVESPD RIKCIIKILK EKNVINKMVQ IKCREALFEE
     IKECHSTSHI NNIFYSLKRI LKYKKKDVIY PFDKHDTYYT SYTGTVSKRA VGGLLNLCDA
     ILSNKNEKFK YIDFKKSFRY NYNFFKNIPP SSVRRYMGNK INHYNHLKRS KSESNLHVMH
     HFQHNDSNHH LDFDIPYKGN NSNIKCDKYK QQSNIPFKKI NNKTVSTSNY CYNSNQAYDM
     ITPNENISIP HKNNKEESVL RLCEVSSPQK QKSLIDEAIS SINQPTDDVE LDDNVSKNTC
     ADNNPSNKEE FPVFNKLYRS YSTTMCNVKE CTNNSNSFTD INCGFAAIRP PGHHCSRNNP
     SGFCIFNNIS VACKYIFKKY GIRKIFIFDW DVHHDNGTQE IFYNDKDVLC FSIHRFDKKK
     SKGQKRKSRR CLNTLGGKTS NGEKGKNRDG SDDNGKSIRN RKGENNKSGS KGFKVSSNGN
     AKSGTIPDDG TSEVNGELTC SSSSDSSNGI INKSLNSEKK KEKTQKRNMN MNTSMSTNTS
     SKMNAKTKTM RKKKPKTNRK YKRNLRSYEE NLFYPRTGAK SELGSKNGYK FNINVPLEKG
     YNNCDVYYVF KYLLLPILEN FQPEFIFISC GFDASINDPL GECNLTHNFY QWMTLQLKHF
     ANIFCKGRII LVLEGGYNLN YLPKCTLACI KALIKKNKNR KMQYQIAHES DTTAQLAKDE
     RTTTEGALEK VSNVSQSKKE IISNGNNTNK SNEVVNKNAA DNSKDSIFKK MEDWRQVKHG
     NLINNSNKEC DHINFYKFKN NTWHNKNSYE QFKHSGGKTY TTNITSKKKE LITAGKLHYS
     TYKVIKYFLC ILKGDPFHLN IKLPPYNTFM KKKGFENKKI SRDRTINIYS RSNDRNDNSP
     QGDSYSNNED GNCVVDQYGK NCYHHEDTLI EGEENSGGAL LNFYVNENEK EYNKYHQENM
     KQYPQSSTTM SNLSNSDLYI SNDELEQHSQ SSDSSMNNRR KVIMLNKLKL KLNKSSNMMN
     NSPTGYSSSI SKMTKKRKKQ KNNFHVSADK NKNMKEIDIW NHSEIPKENN NIEEVSDKNS
     NENDTIDNCV RDQRVEEEDA LNMQHSTSMN HTPNMEQLSI ILQETDENDS HLNCDLTNLK
     YCKDQLQNSF TMYTKRKKGF IFFYCSGHRN QWVLPIHKKI MRIIKLCSEL EAYFYAWLYL
     CCGKEICISE TMSDYSAVLE DKVRVNNLSL NVVFSEEQKK HAKEFIKFTV PCYYSFLRRN
     QLFQLGYRKG ESYQLQCELE NEVQIMQMIN AVKTIKPVKE TNAGDHVEFL EGINETKENE
     VVANHNKSFI EDSNIYPNDC TPDREEVKKE IDKNGDVIDI ADEVDVADKV DVNDNVNVAN
     NMNVADVIDM TDENYDREKN NTNHENHKIN NSNKGIVHTL GNYEYGVVIV NSDEIHTNPS
     ECDKNKSHDF SEHNDNEKNR IESKSSNPMN SNISIIKMDE EVLKKDKNIE LDQENGKLRL
     KMNHSGKNLN GDEEKTAICL ANVLCRMRHP CVMDIKMGAR LYGDDCDEES IQKKIQKAKM
     RSCLSHGFHL TSIIGWNKKK QEPFFTSKED AHSVKKDDDF VDIFKSYFLA CDNVHISILL
     LKKLLLILEH MKNFFETQQF FVFYGASLLF VFDSDPSKNE NDLEGSIDVK GNITCEMSAA
     TSDHLHTFEK FINGQERDIT EINNDNLDQN SMKEKKNKEE KFNKWKDEYY EDIFNFKEKI
     QNIFEQSLTL EEKNIYMQSK LNSKILKSAT IYIIDFAHAN FNRNEKDDGF LLGITSLHRI
     MRKTIEKIQS LYLI
//
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