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Database: UniProt
Entry: A0A176VYV2_MARPO
LinkDB: A0A176VYV2_MARPO
Original site: A0A176VYV2_MARPO 
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
//
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