ID W7A6T7_9APIC Unreviewed; 2152 AA.
AC W7A6T7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Histone deacetylase domain-containing protein {ECO:0000259|Pfam:PF00850};
GN ORFNames=C922_02196 {ECO:0000313|EMBL:EUD67490.1};
OS Plasmodium inui San Antonio 1.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=1237626 {ECO:0000313|EMBL:EUD67490.1, ECO:0000313|Proteomes:UP000030640};
RN [1] {ECO:0000313|EMBL:EUD67490.1, ECO:0000313|Proteomes:UP000030640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=San Antonio 1 {ECO:0000313|EMBL:EUD67490.1,
RC ECO:0000313|Proteomes:UP000030640};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium inui San Antonio 1.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the inositol phosphokinase (IPK) family.
CC {ECO:0000256|ARBA:ARBA00007374}.
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DR EMBL; KI965466; EUD67490.1; -; Genomic_DNA.
DR RefSeq; XP_008816017.1; XM_008817795.1.
DR EnsemblProtists; EUD67490; EUD67490; C922_02196.
DR GeneID; 20037470; -.
DR VEuPathDB; PlasmoDB:C922_02196; -.
DR OrthoDB; 124800at2759; -.
DR Proteomes; UP000030640; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 503..605
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT DOMAIN 810..921
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT DOMAIN 1060..1185
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 88..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1509..1541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1775..1813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2023..2067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..757
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..938
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..988
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1034
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1791..1807
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2034..2051
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2052..2067
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2152 AA; 244527 MW; 60D68976C8DA6ACF CRC64;
MKNGIINTQS KNDSKQTPLK QDTIARLKLP DKGAYFNNFI IPKFDNLNDI SLYLRESNNV
ADSVQDVVMD DVFMDDLIGA SDGETLRNGN LRSSYGRSSS VKSSRNGDTT LLRSARNKRN
SLVIDSLVSS NHVSRNHVSG NHVSSNHFSS SLIRRYRSSN NRSPSNQSIS NLYPGDRLVG
DLPLEMLTSN KQNGKLRSIY KRRKSEGKDG TPRKQNGEAK KNLNTRHHEG RRKGERKRRS
KSDMNQGDRK RKKELSQKRE FRNTKKGLTI RNNLINKNAS KGRNKLQKDY SARKKRYIRT
RKLSYASSSN DGEFSANKYM LDKIYQSLKR KVNTMEQLNN SFYIEYDESA DLDTGRESGT
DLEVAGGGAL DDFPPAFSAN VNFSSSGDVA QGTVLGTPEG SSSSYANNAL EEYYPPEPPK
NRLLRKNNYH THCNTNKAHK TRNVNHLYKY TDSNYKDHQL GHIKNGKIFS SPKSGSDNVE
YDCIGFVCDE EYMCKNLHFD VNHLESPDRI KCIIKALKKK NVINKMLQIK CREALYEEIK
ECHTSTHINN IFYSLKRKLK YKKKDVIYPF DKHDTYYTSY TGTVSKRAVG GLLNLCDAIL
SNKNEKFKYI DFKKSFQYNY NFFKNIRPNG VRSFLGNRIK HDTHLKRSKS ENNLYVMNRF
EGSGIGRSNN SGGRSGVGCV RGLSDSTKNK QPSNAAAKRG THKALSTSNY CYSVNRVPSD
SLAREKPPNG EPTRENHPNE DPTREDHPSE VPSTLAEHNK EESTPCLSET SSPQEGVNLT
DKATPPEQPE EDTQSANVIE ERPPTNNPSN REEVPIFKKL FRSYSTSMCS VKECTTSSNS
FTDINCGFAA IRPPGHHCSR NSPSGFCIFN NISVASKYIF KKYGIRKIFI FDWDVHHDNG
TQEIFYSDED VLCFSIHRFD KKKDDRKNKK RKKRKKGEGA VNKGANSSAG GGTAYGKKGK
KKDSSDDNGK SSKEGKEEIN KGSSKKFKAD TKGASILGPI LGTTEGAIST KLDTRKTATI
CSDSSNGTPS SVPHNDDTKM KKKKKEKKKR TKERKNLKTY EENLFYPRTG AKNELGSKSG
YKFNINVPLE KGYNNCDVYY VFKYLLLPIL ENFQPEFIFI SCGFDASIND PLGECNLTHN
FYQWMTLQLK NFANIFCKGR IILVLEGGYN LNYLPKCTLA CIKALIKKNR NTEEYYPHMQ
NGQWTGKPSN DAGMITKGVG LSRGTPPNGV PAIKEALPKD IHISEPKGAP SKDELTSSND
SAFIKMQNWR QVKHGNLISN NYKNDDHVNF YKFKCYSDYY KTSNRNFRHF PGKTCTSNMT
SKKKELITRG KLHYSTYKVI KYFLCILKGD PFHLNIKLPP YNSFLKKKGL EDKQLSIERK
ITIFKKVDSR ADYLRFDGTN YSHYGEGHYQ NNLHRGGCGT PDDAPYGEED GGIMNSYVKK
KIEQWKRYNQ TYKRQYTMSS TTISNLSHSD LYISNDELDY NVSSSESSRS IKRKVVLLNK
LKLKISKHGN MSSAPALSGP LPKMEKRNNR QRKGQTQTQK HTKMFSILSG DNQEIGGIKI
WDLTKIPEED DIIHVSDHNS SERPGRAGVT GGNGERVAAN LNLAQCPPHQ SDHHDSHLGF
DLTNLKYCQD QLQNSFTMYT QRKKGFIFFY GSGHRNQWVL PPNKKITRII KLCSDLEAYF
YAWLYLCCGR EICISGTMVD YASILEDEVT VKGISLSVDL SQEQKKQAKE LLKFTVPCYH
SFLKKTQLRQ LGYQEGAPQD VEIVHVVEER LGSRGTIDAT EDNNNWKEQT IDAPLHEKDE
NKSNNDDNSE NSKNSVVTIN SEENYTCQNV DLKSESNSLL EQNDNENNVI EQKTIDSVSD
NPNVTKKSEP LLKSEKNKTA ICLANVLSKM RHPCVMDVKM GVRLYGDDCD EDSIKKKIQK
AKSRSCLSHG FHLTSVIGWD KKKEEPFFIS KEDAHSIRND DDFVDAFMSY FLACDNVYLS
KMLLKKLLLV LEHMEAFFES QELFAFYGTS LLFVFDSDPS KNKSDGEESA EAEGNPTTEL
TELTNVKNSN FEVDPEGERS NKTEKEDKED IFDFMEQMQS IFEDSLTSEE RDIYMQTKLN
SKILKSANIY IIDFAHASLN SNQKDEGFLL GITSLHRIMK KTIEKIQNLY LP
//
