ID U6LN89_9EIME Unreviewed; 1783 AA.
AC U6LN89;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase {ECO:0000256|RuleBase:RU365032};
DE EC=2.7.4.24 {ECO:0000256|RuleBase:RU365032};
GN ORFNames=EBH_0035860 {ECO:0000313|EMBL:CDJ50738.1};
OS Eimeria brunetti.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=51314 {ECO:0000313|EMBL:CDJ50738.1};
RN [1] {ECO:0000313|EMBL:CDJ50738.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ50738.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ50738.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ50738.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Bifunctional inositol kinase that acts in concert with the
CC IP6K kinases to synthesize the diphosphate group-containing inositol
CC pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-
CC diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-
CC InsP4, also respectively called InsP7 and InsP8, may regulate a variety
CC of cellular processes, including apoptosis, vesicle trafficking,
CC cytoskeletal dynamics, and exocytosis. Phosphorylates inositol
CC hexakisphosphate (InsP6). {ECO:0000256|RuleBase:RU365032}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-1D-myo-
CC inositol 2,3,4,5,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:37459,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:74946,
CC ChEBI:CHEBI:456216; EC=2.7.4.24;
CC Evidence={ECO:0000256|RuleBase:RU365032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP
CC + H(+) = 1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate
CC + ADP; Xref=Rhea:RHEA:10276, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58628, ChEBI:CHEBI:77983, ChEBI:CHEBI:456216;
CC EC=2.7.4.24; Evidence={ECO:0000256|RuleBase:RU365032};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|RuleBase:RU365032}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
CC subfamily. {ECO:0000256|ARBA:ARBA00005609,
CC ECO:0000256|RuleBase:RU365032}.
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; HG712385; CDJ50738.1; -; Genomic_DNA.
DR EnsemblProtists; CDJ50738; CDJ50738; EBH_0035860.
DR VEuPathDB; ToxoDB:EBH_0035860; -.
DR OrthoDB; 5476261at2759; -.
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; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR037446; His_Pase_VIP1.
DR InterPro; IPR029033; His_PPase_superfam.
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 SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU365032};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU365032};
KW Kinase {ECO:0000256|RuleBase:RU365032};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365032}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|RuleBase:RU365032}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..1783
FT /note="Inositol hexakisphosphate and diphosphoinositol-
FT pentakisphosphate kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013107891"
FT REGION 13..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1153..1179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1236..1255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1372..1417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1452..1481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1538..1563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1599..1621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1655..1706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1744..1783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1261..1294
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 13..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1086
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1237..1255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1603..1620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1655..1684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1754..1783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1783 AA; 190863 MW; 54D7A429337CEE70 CRC64;
MLLLLLLLCP RQLQQQQPRR PQQEMQQEMQ QPQQSPKLQQ QQKAQQQQQQ EKQQQQEKEQ
QQKKQGETLL QQGSRPSPPA LLQQPQQLQQ QNQRQQQQEQ QPPRLPMGAK SQQQHSSCSR
RKMTLQQQQQ QQQQQEALGA KTAGVSTRPE DSSSSSSSSS SANPSTSIPS NTSSSSSSNS
SNSSSSSSSS SSSKHLEALK AELRLHKQLQ KVLLQGDGFA GINRKIQLKP KRWTREVEPT
AAAAAAAAAA GTAGTAGGAA GAAGAGGVSS PSKQQQQEGE PQQQQQQQQQ QQQQQVELDR
KASAANISSS SVSAGVLRSS SVPLLPSAPV CLLSPAAAAA SFSIADKAFY HAAASPTAQP
TGSAAAAAAA AAAAAAVANW QENTQRAAHS SSSSNSSSSS SNSNSSSPAA KQSPPQGSGS
SVCSNGSAGW GGGSSSSSTS SNSSNSSKRL ESCVVVAKWG GELTAIGRKQ AEDLGQRFRY
QLYPGDSAGL LRLHSTFRHD FKIYTSDEGR CQITSAAFTK GFLALEGELT PILVALVIHN
SKAYALLDEG SQCPSEKRVL KQCLDYLLNL NGEQLGALQA RVMELIQQQK QQQQQQKQLE
AGEPDPSTAT AATAAAAAPA AGSAADAAAA AAGGAGEDKE KGEETTKPPQ QQQPQQQQQP
QQQPPQQQQQ PQQQQQQQQD TVRAAAVSVH PDSREEEVWG AERLLLSAKE GDTCLVPKQL
EALQRLQSPV DRQKEILELL QHFLSLLDPL IEETAGGDTE GLGTPVSSAP LSLKQITATK
LLDMKSRWSK IAADWCKGGI FDSSKISDIL DLVRYELIHH CHLLSREGFY ESRELQSASA
AGVAAAAAAA AVAAGAAAAA AAAALAFLLL LKTTVKTALM VHWSIKEVQE SIAAFAAAHS
SKDKLRLAVP VVSRLIRKIL RDVTFFRNDD SQQKPQAAAC FSCSSAAWGT SLGAAAAAAA
AVSSDEPQGS CASARETQGE EALLLQQGDT AAAAAAAAVS PTGCSTPACG DSSCPTIKED
KDIPPLRASR RGATVGGNGR SSSSSSSSSS SSSSFGRSCS PTCHGASAAN SALRGTGDSL
QSPCSSGGPG AVGPGSGSGS GSGSAAAAVG SPRGRSSLEP RCSPGGGGAT RSSSTQGCSS
SSSSRDCAAA AAGGKGSSCC RSNSRSSGSS SISCSSSMRG RGRCSPAAAA ASSSNPTTEL
VGALRPLSVS CGIGGIVSAD GGETVVINSN DLWAHQQTGS REKKEKAMKL KRQEQVQQLH
IKHMQSELKL LQQQQQQQQQ QQQQQQQQQQ QQQDTPDTTH RLATPLQQQL QQQLQQQLQQ
QLQQQLAGRD SATHSPELQH PQKQPSTPTE LLLLQDTQQH LQLQLQLQQQ QQQQQQQQQR
HPGLSSGQAP STPFESSALP SRQDSEDPQQ LQQQQQLQQQ LQQQLQQQLH QQLQQQHQDP
SQTRDIATAA EDPNAENAEQ QQDAAAGEEE EEHEDDDPHQ HEVAAEIRLK EGEAHLFGIR
SPWRIVRSRF YVTSASHVEA LLNVLLLSHN AVASEGTAAA ASSTEETDNK AEKSEECKGP
TGPMFDSDLR EWLGQCELHY LSHIVFRVWE RRKARVTPAA AAAADPQQQQ QQQQQQQQQD
ERGRYRLEIF FSTGARDGFG ENVYLLERKA RQQQQQQQQQ QQQQQQQQQQ QTAPAPSARS
QLWQEVHQQE EEEAGPHPLQ PEIQVPPYSS RVPPYCEIAP LLPLGRSVDV ADFDALMTEV
LRRYGDGGPQ RNRSDKLKTQ QQQQQQQQQQ QQQQQQQQQQ QQG
//
