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Database: UniProt
Entry: A0A059LSK6_9CHLO
LinkDB: A0A059LSK6_9CHLO
Original site: A0A059LSK6_9CHLO 
ID   A0A059LSK6_9CHLO        Unreviewed;       588 AA.
AC   A0A059LSK6;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Inositol-1,3,4-trisphosphate 5/6-kinase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=H632_c8p4 {ECO:0000313|EMBL:KDD77151.1};
OS   Helicosporidium sp. ATCC 50920.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Helicosporidium.
OX   NCBI_TaxID=1291522 {ECO:0000313|EMBL:KDD77151.1, ECO:0000313|Proteomes:UP000026042};
RN   [1] {ECO:0000313|EMBL:KDD77151.1, ECO:0000313|Proteomes:UP000026042}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50920 {ECO:0000313|EMBL:KDD77151.1,
RC   ECO:0000313|Proteomes:UP000026042};
RX   PubMed=24809511;
RA   Pombert J.F., Blouin N.A., Lane C., Boucias D., Keeling P.J.;
RT   "A lack of parasitic reduction in the obligate parasitic green alga
RT   helicosporidium.";
RL   PLoS Genet. 10:E1004355-E1004355(2014).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the ITPK1 family.
CC       {ECO:0000256|ARBA:ARBA00009601}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KDD77151.1}.
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DR   EMBL; AYPS01000008; KDD77151.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059LSK6; -.
DR   STRING; 1291522.A0A059LSK6; -.
DR   OrthoDB; 315387at2759; -.
DR   Proteomes; UP000026042; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0047325; F:inositol tetrakisphosphate 1-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052726; F:inositol-1,3,4-trisphosphate 5-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052725; F:inositol-1,3,4-trisphosphate 6-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0032957; P:inositol trisphosphate metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.11370; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR   InterPro; IPR008656; Inositol_tetrakis-P_1-kinase.
DR   InterPro; IPR040464; InsP(3)kin_ATP-grasp.
DR   InterPro; IPR041429; ITPK1_N.
DR   PANTHER; PTHR14217; INOSITOL-TETRAKISPHOSPHATE 1-KINASE; 1.
DR   PANTHER; PTHR14217:SF39; INOSITOL-TETRAKISPHOSPHATE 1-KINASE 3; 1.
DR   Pfam; PF05770; Ins134_P3_kin; 1.
DR   Pfam; PF17927; Ins134_P3_kin_N; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026042};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          31..109
FT                   /note="Inositol-tetrakisphosphate 1-kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17927"
FT   DOMAIN          549..578
FT                   /note="Inositol 1,3,4-trisphosphate 5/6-kinase ATP-grasp"
FT                   /evidence="ECO:0000259|Pfam:PF05770"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          227..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          401..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..309
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..415
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..452
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   588 AA;  62570 MW;  8906D854C090C17D CRC64;
     MKASPRAEEH EGLAPIPGPT APPRRAPRPR VIGYAMRAGK VAKHVTPALT SRAAAAGLAV
     RVLDPRRPLQ EQGRLDAVLH KVVAPDWVDR LEHYMAGHPE VAVPDPPRAT QTLRHRGRML
     SVIPAEGWVV RESEGESSEG CHATFAASLP SSDPAPVSYR CTVPSFTTLE RGESASALAA
     QLKERGLAYP LMIKPMWADG RPGSHSVAIV SSERGLEALL ARQLGDLDSA GGKAPGEQRE
     WATSEWARGK RCPEGGIGLP PTAPRSTPPL VPLPAIPLDE DSESAGDDDL TQAVRVDSTP
     ASSASHSGLA WQPPDPCSDP SSAQPLSSTS ISPPPSRHLP PSPSKNCQTF PTIPQLPVIA
     QEYVPHGDLL IKVYVLGSQT RTVLRGSVCL HCRREGAAAR NGREALEERG VDSESASATR
     ADASPIPLSR SQPSIPPSLA SPSKSTLQAE GLETLRRVSD HRSAPGAAAH GARGREGGQR
     EVPEAVLAGL GQRLRDSLGL DLFNFDVIVP LDQGEGESWR ACEGGCQGAG RDSSVKPSSP
     AAAFSGQPGR LHVIDINHFP GYEKLENYET LMVNYFLEVL DRCRQSSF
//
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