ID W7A435_9APIC Unreviewed; 2283 AA.
AC W7A435;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=diphosphoinositol-pentakisphosphate 1-kinase {ECO:0000256|ARBA:ARBA00012893};
DE EC=2.7.4.24 {ECO:0000256|ARBA:ARBA00012893};
GN ORFNames=C922_03069 {ECO:0000313|EMBL:EUD66435.1};
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:EUD66435.1, ECO:0000313|Proteomes:UP000030640};
RN [1] {ECO:0000313|EMBL:EUD66435.1, ECO:0000313|Proteomes:UP000030640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=San Antonio 1 {ECO:0000313|EMBL:EUD66435.1,
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 -!- 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}.
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DR EMBL; KI965471; EUD66435.1; -; Genomic_DNA.
DR RefSeq; XP_008816883.1; XM_008818661.1.
DR EnsemblProtists; EUD66435; EUD66435; C922_03069.
DR GeneID; 20038343; -.
DR VEuPathDB; PlasmoDB:C922_03069; -.
DR OrthoDB; 5476261at2759; -.
DR Proteomes; UP000030640; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IEA:InterPro.
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:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; IEA:UniProtKB-EC.
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; 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 Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 31..117
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT REGION 489..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1220..1346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1461..1500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1532..1668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1794..1894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1908..1976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1234..1249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1287..1310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1476..1497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1582..1597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1598..1637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1638..1661
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1807..1823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1841..1888
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1951..1976
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2283 AA; 256044 MW; C2B63F818BF90AC4 CRC64;
MKLRKHGGSL DEEKFFENVS KDDSGMIKKF TLGVCAMESK VESAPMECIL KRLAKSGDFN
IIKFKGDMIL NHDIDSWPIV DCLIAFYSTG FPLKKAIEYV KKYKPITLNN LSRQLILRSR
LQIYEELKKW KVPHANYVVV DHDAVKRGEH VFEEYYDYIV YNNIRLNKPF IEKPINADNH
NNWIYYPKNT GGGCKKLFRK VKDRSSEYCP DVHRVRNNGM YIYEEFLSTF GTDVKVYTVG
QMFAHAEARK SPALDGKVCR TSDGKEVRYA VILSEAEKII AYRIVEAFQQ TVCGFDILRT
TMGPFVCDVN GWSFVKGNIK YYNDCAHILR AMFLAKLEEK YNIIPRDLAD NWYNIENEEE
VLRKTFRQPD DLHCSHHEEL CSVIIVMRHG DRKPKQKMKF LTDRPLLLDY FNCEENLYNV
IENKLAADDQ QKANQMELSN SNNNLSVSCV PSDRVDSSMF QYDAAAKAPS TLSKISFISQ
KSGEVVSAAS AERDPSAANA SNGANGVNGA TASNASNASN PANGLPPDEQ ERRDSLYKEY
TKKEIKFKSP EELQDLFLRN NIILGDVEKE YKALKAEAEA RRAELAMRSA SVGRDEAVEG
NETVRRNETV RRNETVRRNE TVRRNETVRR NETVRGNETL GRSDGEASLK REEDPPKSDV
AASARDVTAP KGDVSEARPH AAMTQEELEA KLSEYEIMIE NHKTLQKVLE RGDGFTGINR
KIQLKPVEFL VLDDKIVVTR ILTVAKWGGE LTRMGRRQSE NLGKRFRATL YPGDSDGLLR
LHSTFRHDFK IFTSDEGRCQ ITSAAFTKGF LDLDGELTPI LVAMVIRNSK AHSLLDDNRP
SLNRTQCKQY IDNVLNQDKD IDEDLLKKLT SGKHARGLRE SLRKISNFFQ LMEKIRKTIY
DFLKGLNQEV QKWLNLFPYD EYALYVIDIL HEIQVRWKSL TKMWFKKNKN NYDTSKIPDI
VDNIRFDLIH HHSYLGCGLD KAFEIYNQIE PLANFISQAE YGITPEEKVK IGVNIVGKLL
RKLIHDVTFY RDEEVRNKRN NKGCFDLKNA LNISYINSFN LSKNDKTGLP TGEKNPQQQV
LENAKVDAQH ANWLDKEIQK DTPKLFSMCK YDSRQIFIDN RLQKGAEQLL PATMATIATD
PCATKTELSL WNEATSSSVA TNTVNAVNTA TAPYSNGAYY SGAYPSEAFS SAAFSCVTSS
SGRPSLSEPQ VKKSIYSELN QKGGKVGSDA QVGGSPGGGT STQVGKDPTC AESTEAVESK
TGEGGPIGLN GGLTDFTGNG LLDLSKHTNG ERPEEGDIHH RDEFEGGTRT PDRSSTKGAS
GAASDDPQGG STHIGSSPVD NTVSSSNVGS SVVGMVGSPA SVCPNEKNPF KAAGGGVTYN
INAKDLYTPK LINKKEALVI NSSDLWAHQN KYRKENNEKQ KMKKIKNAKE SELNLKREDN
VEVGSDYRGL DKYGSNRMKG VGGISGSGSD TTAKDLRGKV NARLDGHKSE EERGRNGAAR
NGAACNGAAR NGAACNGAAC NGASCNGEAR NGAARNGAAR NGAARNGAAR NGPACNGAAR
SGTDQDGALR SAYECSQQGD KEGMKNEQGS NNMSQRKAEE KTYQEYQIEE TYRQVDNDEE
QQKEEKKQEK DEQQNQEKEK EEEDGEEAED DEGEEEHDHD DDEDIIRLKE TDARRLGIRS
PWRMVRSRYY VTSASHMISL LSILIHAKNI DSSTGQNIID NDSIKSVGDV TDLHYLSHLV
FRVWERKQLK RNDSNRFRIE ILFSSGARDG FGQNYELLEK DAKAQQQKYE RHFSKYVDDS
RRGEGGGEVN LSNQISRANS AVSKGEKKPS GEKQSDGRPP GETPSGETSP TEKSLLEKLN
TASNNQSASA SDKVESKDSL SQAVPQGQED KGKVSAGNAF WLSDGVEGRP ASLGGCVPSS
KCDLVNTERK DGSGIDNEKG NLGGSDSALR NDTSHRIETS LRRETSPRRD TSLRKDAVRR
NLLRRQFSAN SENLFRRAEE EEDANFHQGV YKRDLSFQFG GVHDKLSSMN NNATRTGSYM
MRSISSNLRK KKYKQKDGLN VEYEKKKKED ITKENLLTYE PECSIDMGTQ EGNPKSRRSF
SCLSDRSFYI NPIQIELEGD ANASKNFNGR RNSLIENESA RNTLQHSLQH KIERPFQHKI
ERPFQHKIEH PFEKNSEHDP KDNKKANVFS HVFQHFNENK KNSTSNLKFF YKTYMPDYEK
IIENDKKAET FDVPPYCELA PLIVLTKNCQ LSTFENILTH ILNKYSKGGK GKDKGPKAGP
KPT
//
