ID Q8ILG1_PLAF7 Unreviewed; 2657 AA.
AC Q8ILG1;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=diphosphoinositol-pentakisphosphate 1-kinase {ECO:0000256|ARBA:ARBA00012893};
DE EC=2.7.4.24 {ECO:0000256|ARBA:ARBA00012893};
GN ORFNames=PF3D7_1430300 {ECO:0000313|EMBL:CZU00000.1};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329 {ECO:0000313|EMBL:CZU00000.1, ECO:0000313|Proteomes:UP000001450};
RN [1] {ECO:0000313|EMBL:CZU00000.1, ECO:0000313|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.,
RA Eisen J.A., Rutherford K., Salzberg S.L., Craig A., Kyes S., Chan M.S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
CC subfamily. {ECO:0000256|ARBA:ARBA00005609}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LN999946; CZU00000.1; -; Genomic_DNA.
DR RefSeq; XP_001348456.1; XM_001348420.1.
DR AlphaFoldDB; Q8ILG1; -.
DR SMR; Q8ILG1; -.
DR IntAct; Q8ILG1; 1.
DR STRING; 36329.Q8ILG1; -.
DR PaxDb; 5833-PF14_0282; -.
DR EnsemblProtists; CZU00000; CZU00000; PF3D7_1430300.
DR GeneID; 811864; -.
DR KEGG; pfa:PF3D7_1430300; -.
DR VEuPathDB; PlasmoDB:PF3D7_1430300; -.
DR HOGENOM; CLU_000707_1_0_1; -.
DR InParanoid; Q8ILG1; -.
DR OMA; KVPHANY; -.
DR OrthoDB; 5476261at2759; -.
DR PhylomeDB; Q8ILG1; -.
DR Reactome; R-PFA-1855167; Synthesis of pyrophosphates in the cytosol.
DR Proteomes; UP000001450; Chromosome 14.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; IBA:GO_Central.
DR GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IBA:GO_Central.
DR GO; GO:0052723; F:inositol hexakisphosphate 1-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0052724; F:inositol hexakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000828; F:inositol hexakisphosphate kinase activity; IBA:GO_Central.
DR GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006020; P:inositol metabolic process; IBA:GO_Central.
DR GO; GO:0032958; P:inositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.11950; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR037446; His_Pase_VIP1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR040557; VIP1_N.
DR PANTHER; PTHR12750; DIPHOSPHOINOSITOL PENTAKISPHOSPHATE KINASE; 1.
DR PANTHER; PTHR12750:SF9; INOSITOL HEXAKISPHOSPHATE AND DIPHOSPHOINOSITOL-PENTAKISPHOSPHATE KINASE; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR Pfam; PF18086; PPIP5K2_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000313|EMBL:CZU00000.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001450};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 38..124
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT REGION 532..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1368..1400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1571..1595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1712..1822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2025..2108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2155..2175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2463..2550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..741
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1712..1761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1762..1778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1779..1822
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2158..2174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2657 AA; 306807 MW; 4AA679A6D91877C2 CRC64;
MDEGKKKSKS RKHITSLDEE KLFDNISKDD CGIIKKFTLG VCAMESKVES APMECILKRL
AKSGDFHIIK FKEDMILNHD IDCWPIVDCL IAFYSTGFPL KKAIEYVKKY KPITLNNLEK
QMILRSRLQI YEELKKWRVP HANYVVVDHD TVKRGEHIFE EYYDYIVYDN IRLNKPFIEK
PINADNHNNW IYYPKNTGGG CKKLFRKIKD RSSEYCPEIH KVRTNGTYIY EEFLSTFGTD
IKVYTVGQMF AHAEARKSPA LDGKVCRTSD GKEVRYAVIL SEAEKIIAYR IVEAFQQTVC
GFDILRTTMG PFVCDVNGWS FVKGNIKYYN DCAHILRAMF LAKLEEKYNI IPRDLADNWY
NIENEEEVLR KTFRQPDDLH CSHHEELCSV IIVMRHGDRK PKQKMKFFTT KPLILDYFNS
EENLYNVISN RYAHDDTIKI NNNELHTTNY NTQDVLKYNA KLDHATNQYQ GTHKNHSNSK
TFNYNCENNC SSKCNGHIND TQKDIKIPCA HHESLCNNST NTNKENINEN NKSCENNKSC
ENSKSCENNK SCENSKSCEN NKSCENSKSC ENNNDNQNNC TCNDKNKPIK DLNNQDKTDT
FLLSDNKTMN EKNSSNNKNI NPDTCNTSTQ TDEVKQANLY KSYTKKEIKF KSPEELEDLF
LRNNVILNDI EKEFKLIKEQ LYNIQQKLEK DDINEKNGQK LDAPSKKEDL TRSTMKDKDN
ENVDDKKEIP HRKKLGHDHD ENNNNTSGIC NDTSGTCNNT SSTCNNNNTS GICNDNTCNN
NTCNSSCSNI KLNVHCKNKP SEEERCTTCS GEDALNLMTK EELEIKRGEY EVMIENHKTL
QKILERGDGF TGINRKIQLK PVDFIIVNDK VIVTKILVVA KWGGELTRMG RRQSENLGKR
FRATLYPGDS DGLLRLHSTF RHDFKIFTSD EGRCQITSAA FTKGFLDLDG ELTPILVAMV
IRNSKAHSLL DDNNPCLERS ECKEYIDEIL NKNNDIDEDL LKKLTPGKNA RGFRESLRKI
SNFYELMDKV RTTIYEFLKS LNQEVQKWLN LFPYDEYALY VIDILHEIQV RWKSLTKMWY
KKNKNKYDTS KIPDIVDNVR FDLIHHHSYL GSGLDKAFEI YNQIEPLANF ISQAEYGITP
QDKVKIGVHI VGKLLRKLIH DVTYYRDEEE RNKKNNKGNN VLKNALHISY MNPFYFKKTD
ELQKKDKDQH QRDTSKNFNM CKYDTKQNFL DNFLFKRDSN EINKKLETNN KSNIINDKAD
MLYNANDKKE KTINDVVEET TVQNIHDEKG DNMYKYEHGK NKEDTIKPVD INININGDNN
INGDNNINGD NNINGENNIN GENNINGENN INGENNINGE NNINGENNIN GENNINGDNN
INGDNKKNGD NNNNNMEEGD ETKELVIEKE EKTFNNEKNK HLDKSYLRCA SICSENCKRN
LITQNEYQRK DKLEKCSSLT EKYVPDISTN IIKNRKECIC KNNLYDNEKK NNSLYRCDDL
ICNMKYSETI NGTNSEPSNS KRVLNKALCI GGYSNSINNN NVNGNHKNIN DDNNINDNNI
NDNNINDNNI NDNNINDNNN NNNNNNNNNN YCNNNYNNNS TSTFLDTNIG ESYNELKNYK
STVTYNTNVK DIYTPKLINK KEALVINSSD LWAHQNKYRK ENNEKQKMKK IKNMIDNDFN
EKKEDSNDRG VSYKYSENFL KKESGSYFMR TVEDSDKRHK TKIDEDQMDS TSNVHEKTKE
LKNSGSLENK ENKENKQNKQ NKQNKEYTQY TQYTQNKQNK EYNDKHGDNL INDVKGDHMK
GTNVDEEDKE KTKNGCSELD TNNIKEDTDV NINGKENPND ENVNGQVDVE AEADAEADID
VDEDEEEHEH DDDEDIIRLK ETDARRLGIR SPWRMVRSRY YVTSASHMIS LLNILIHAKK
ADNTISQNII DNDSFKSVSD VTDLHYLSHL VFRVWERKHL KRDDSNRFRI EILFSSGAKD
GFGQNYELLE KDAKAQQQKY ERHFNKYFDD TKRINADKSL GATTGGVNAA DTQNGTTKST
GNNSVIDTQN GTTKSTGNNS VIDTQNGTTK STGNNSVIDT QNGTTKSTGN NSVIDTQNGT
TKRTGNNSVI ETGNVQENYK NMNNHLNNNN NLEEGDTNRS HVPAEEYINR TTTRENENVK
NKNNSNNMKD INRNGTKIGD TCEEKYEVEN LENKDKSIIN DKNNINCVIT TNNCYSDREE
KGNFVSAEGV SNNSIINKKE IRIEHDKNIR SGHFSNSVDE IILNNNKKKN TMNLNILNKE
IKKSSLHSIS NSSVNPFVFD SLNVFRRENE GKSPHIINYN KREASYGFGC LNEKKMDSIN
NNLSRAGSYM VRSISSNLRK KSKQKDILKL DYDKKEKEDI TKENLLTYEN EYINNSSNEI
NSKSYRSYSC ISDRSYYRNK KEFEIGNEEH NRKNKLNAFN HIMDNDKLKN QFIRKHTLEI
NHIDNNDNNN ENNNNNNNNE NNNNNISNNN NNISNNNNNN ISNNNNNSSN NNNNNCSNNN
NSSSNNNNSS SNNKNNNLNS NLNSNNNNNI YQDKKKVNLF SHVYEHFNEN KKNSTSSLKF
FYKTYMPDYE KIIENDKKAE TFDVPPYCEL APLIVLTKNC QLSTFENILT KLLNNYSKNT
KNKDKNKMDK VSKNKSK
//
