ID A0A176VYV2_MARPO Unreviewed; 500 AA.
AC A0A176VYV2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Inositol-1,3,4-trisphosphate 5/6-kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AXG93_1712s1590 {ECO:0000313|EMBL:OAE25979.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE25979.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE25979.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE25979.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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:OAE25979.1}.
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DR EMBL; LVLJ01002271; OAE25979.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176VYV2; -.
DR OrthoDB; 454531at2759; -.
DR Proteomes; UP000077202; 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; 3.30.470.20; ATP-grasp fold, B domain; 1.
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:SF1; INOSITOL-TETRAKISPHOSPHATE 1-KINASE; 1.
DR Pfam; PF05770; Ins134_P3_kin; 1.
DR Pfam; PF17927; Ins134_P3_kin_N; 1.
DR PIRSF; PIRSF038163; ITPK_uncN; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 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:UP000077202};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 167..266
FT /note="Inositol-tetrakisphosphate 1-kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17927"
FT DOMAIN 290..479
FT /note="Inositol 1,3,4-trisphosphate 5/6-kinase ATP-grasp"
FT /evidence="ECO:0000259|Pfam:PF05770"
SQ SEQUENCE 500 AA; 55046 MW; 730900E8427A4F3A CRC64;
MDMEGVQGVL IDESLLFKSG KVLHFQPDAH QLLSRLQYSR LCLGLLQRED DYDVGSNKEF
LLRDIGVAES LRYVRLLSNS SPTEALMTAG WAVPFTSSVY ITGQHPHRVD GDLSSQGWKV
IRVAAQPFAG LGNGDTDGSL LTVEQLYEIP AALAVLNKRA LKDRIVVVGY TMKWSRELEF
LKRGALPMLR NSYGLSFVAL QLNQPLEKQL LAVDVILHKA TDEIVSVNPG HFGTLASIEF
SQGIQNLQSY LQEHAEICVI DPIERILPLL DRVSTQAILK GLKIPAQQII RPPRSVEVTS
FEEPLLSQAL GSQNVVLPTI VKPRIACGAS ESHSMAIVFD LNGFRGLPVP LPATIQEYVD
HGAFQYKMYV VGSKLLYSRR KSTPNASRLA AGNEGSPVIL FDSLKSLPVE ADMEIPQGQG
APEESSELDN EAVQMAASWL SKKLGLTIIG FDIVVQAGTK DYVIVDVNYF PSFKDVADEE
AIPAFWEALV TAFGQWSRSR
//