ID A0A2K3E856_CHLRE Unreviewed; 2484 AA.
AC A0A2K3E856;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=diphosphoinositol-pentakisphosphate 1-kinase {ECO:0000256|ARBA:ARBA00012893};
DE EC=2.7.4.24 {ECO:0000256|ARBA:ARBA00012893};
GN ORFNames=CHLRE_01g052650v5 {ECO:0000313|EMBL:PNW88970.1};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055 {ECO:0000313|EMBL:PNW88970.1, ECO:0000313|Proteomes:UP000006906};
RN [1] {ECO:0000313|EMBL:PNW88970.1, ECO:0000313|Proteomes:UP000006906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503 {ECO:0000313|Proteomes:UP000006906};
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
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; CM008962; PNW88970.1; -; Genomic_DNA.
DR STRING; 3055.A0A2K3E856; -.
DR EnsemblPlants; PNW88970; PNW88970; CHLRE_01g052650v5.
DR Gramene; PNW88970; PNW88970; CHLRE_01g052650v5.
DR InParanoid; A0A2K3E856; -.
DR OrthoDB; 5476261at2759; -.
DR Proteomes; UP000006906; Chromosome 1.
DR ExpressionAtlas; A0A2K3E856; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0046872; F:metal ion binding; IEA:InterPro.
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; IPR011761; ATP-grasp.
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; 2.
DR Pfam; PF18086; PPIP5K2_N; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000006906};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 328..546
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 22..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1102..1192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1316..1356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1431..1518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1626..1689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1758..1806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1821..1926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1971..2053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2128..2210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2278..2299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2370..2414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..909
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1173..1187
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1335..1356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1431..1472
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1481..1513
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1645..1665
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1821..1835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1971..2018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2131..2145
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2484 AA; 244136 MW; D1D3D7D891C5BBBF CRC64;
MPRARPTEAA AAAAEAAAAV GAAGAAAAGA RQPMQSNGSG SSSGGGGGGG GGRVGAECAD
GRGPTGDFRA AAGSAAAGDA AGGEATASPT PGATASGSAA AGGTAAAAGS GGGGGGRGSF
MRCSSAPVWQ LQPSLQPPAA AASGPAAPAT PGNVAGASAT STGGATPIRD ISGRPSSSGC
SPSSTSGSSS GGAGSSCTRT STCDSGGGSS ITSSSGSGSA FSNSATPGGF AGRLRLGVCA
MARKADSKPM REILRRLNTF NEFELVMFPE EVILGQPASE WPVVDCLMAW HSDGFPLSRA
QEYVALRRPF CVNDLGAQEL LLDRRRVYRL LQDSCIPVPR HVVVSREGLA PGQSPPGFVE
GEDFVEMDGV RIAKPFVEKP ASGEDHNIHI YYPAAMGGGV KRLFRKVANR SGAYDPAHSG
AVRREGSFIY EEFLATGGTD VKVYTVGPRY AHAEARKSPV VDGRVARSAD GKEVRFPVVL
SPQEKEVARM VCLAFGQKIC GFDLLRSERG GSYVCDVNGL SLVKNSTKFY ADAADILRSI
LLQALAPHRL HLMPALPATP TFGLMLESQR TMAAAEAAAD AMAAATAAAV AGGGAAAAAA
AVAAAGDGGS SIPDGGVELI RAPTWLRPGG GGEGSSSSGG GGGVSGGGSS GGGLPGEELR
CVLAVVRHGD RTPKQKVKLE VSHPAFLALY QRHVDPSKPP GPHRQAKLKS ASQLQELLDV
TRQLLQQHPQ LQPQPHPQPQ PHNRPSSGGG GGGSGAASDG GAGATPAPKA GDLPAGQQKA
AAAAAAAAAA AAAPAAAGQQ QQPQQPPLVD ADTLAVLAVV RGVLEAGGRF SGVNRKAQLK
PRGWVTAAAA AAGEAAPPPS PPPATAVATG VGVGHVDERL LQGRQRGDSP AALGWASGSS
SSAAVTPAAS RVGSMTPPPP APPASDSATA TISASDAATA SATASATASG PAAATSPAAA
TAATAVAGGG RPGGGPSSLL LIVKWGGVLT HAGRAQAEML GVRFRCGMYP RAGPAGGGLL
RLHSTYRHDF KVYSSDEGRV QTSAAAFAQG LLSLEGASLT PITASLVNKD ALLLEAYGKG
ASADMAAAKQ ELYARLTWDP EAGVSRCKPP GGSSSGSGSS SPAPPPAATA LASMPSLATS
TTSGSSSSQQ TTPLPSPLRP TPPAASPTAT AAAPATPLPP SQSPPPSRPA AAVAAADAAA
VVQNTAAATA ADTLSTVRPL PDRPLELLQL LRAQLQDLVE AMEGPAVAAM NEAVAAAEGG
GGGGRGGADD DGGAAATAGE EGAIAATAAA AVARAGVTAE VAPAAAAPAA AAATAKPTAQ
EQGGGRGGGG GAAGSSNPGG SSRSSSGSGN GSSSGRGISS GCYYSSLSMS PDEWRAVPGV
PCGGEHWMLV YDRWHKLLDS FYSAKKKQYD ISKIPDIYDA AKHALIHNAF IPLTPPPPPP
TPPPPSASAA TQPPPPPPAQ QPPPPPPPQQ SHHQQRQAPQ QPQPQPQPQP QPQPQPQPQP
QQPQQPQQQP RSPPDGVVPL LLGEVVAPLY LTARALADAV VPHEYGLTPQ AQLHVGSAIC
RELLGKLLCD MGAMREESLA TSYSHTGGGG CSSSGYNSYS SYSSYSAGGS SGAAAPAAAQ
RALAAAAAPA APPRRSHPGF IAQPPAAHTP QPPQPPQPPQ QPQQLPHLRS PFSSAASIGP
APPALAAATA TPLPGRAGAA TAIPAPGTAA AAGAALVLLP PPPPPHSMVS EFGNASLEDE
MLLPTGMAAA RQAAVAAAPS PPASPARSAA AGVGSSSRRG GATAGGPAVA PAAAGARAGG
AGAGSSTVSP PLYTVMEECA AHEQQADDRE EEGAGGEQAA AAAVEGDGSP PLLHPLGVAG
FVGAGEEREQ EGEARAAGAA GAAGGSCGGG GPPEQQQQEG EEQVEGEGDD DGLVGGPPPP
PPLEALHRLC PQYATDINSP LRHVRTRVYF TSESHIHALL NVLRYCHLRQ QQQQQQQQPP
APTAATAATA AAQPSSPAAS ATSLGPSGGS STSAAGVAGS TAAPAAAAAT SVPADDLSPA
QPQPQPQPPE QPATLLGAAG EALLAGVPEY DYMTQIVFRM FENRHVSAAA GGQEEAGGGG
GSGCRFRVEV LFSPGASRAA LEARAQSMLA RGRGRGRRRG RRRRQGAGMA RGEEAAGGEE
GERQRQQRLG GGCSSSDSSS GEGEEEEEEE GGREGGVGVG GGGGGDALEA DRHCLPLEPL
VHLNAGPGAA RALEALEALL APLAAPRKAQ PNTYALQVAL KAPGAATADS ATATATFGGG
QLPAGSSTSG SSTSGSSTSY MRRELAAAVA SRAPSTALRG PAPLAPDMLL PALGAMATAV
ADEAAAATAA ARAAVLGGST AAAAVQPRPP AAAAAEGAPG AGSGGDAATA NTGARGGNGG
AAGTGGLPPG AATARLHPYM QDGLQSAASL PVLPSHRLRA AAALMAAGGG GAAAAAAAAA
ADVAAAAKEA GDGGRAGDPT PAEP
//
